data_9EDM
# 
_entry.id   9EDM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EDM         pdb_00009edm 10.2210/pdb9edm/pdb 
WWPDB D_1000289861 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-19 ? 
3 'Structure model' 1 2 2025-04-23 ? 
# 
_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' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EDM 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Holroyd, D.L.' 1 0009-0002-2830-6020 
'Kumar, A.'     2 0000-0001-7540-6177 
'Bruning, J.B.' 3 0000-0002-6919-1824 
'Hansman, G.S.' 4 0000-0001-8735-4618 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Virol. 
_citation.journal_id_ASTM           JOVIAM 
_citation.journal_id_CSD            0825 
_citation.journal_id_ISSN           1098-5514 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            99 
_citation.language                  ? 
_citation.page_first                e0197124 
_citation.page_last                 e0197124 
_citation.title                     'Antigenic structural analysis of bat and human norovirus protruding (P) domains.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/jvi.01971-24 
_citation.pdbx_database_id_PubMed   40062838 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Holroyd, D.L.'    1 0009-0002-2830-6020 
primary 'Kumar, A.'        2 0000-0001-7540-6177 
primary 'Vasquez, E.'      3 ?                   
primary 'Masic, V.'        4 ?                   
primary 'von Itzstein, M.' 5 0000-0001-6302-7524 
primary 'Bruning, J.B.'    6 0000-0002-6919-1824 
primary 'Hansman, G.S.'    7 0000-0001-8735-4618 
# 
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 Capsid         33285.086 2   ? ? 'protruding domain' ? 
2 non-polymer syn 'CHLORIDE ION' 35.453    2   ? ? ?                   ? 
3 water       nat water          18.015    557 ? ? ?                   ? 
# 
_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       
;KAFTIPVLKISEMTNSRFPVPVDQMYTSRSEGIVVQPQNGRATIDGELLGTTLVSPVSVCNFKGNLQAEVPGQHQLYQLQ
LTNLDGSPIDPTDDTPGPLGCPDFTGLLYGVASQRGPGDATRAHEARIDTGSDTFAPKIGQVRFYSTSSDFETNQPTHFT
PIGIYIEGNSSDFNQWQLPRYGGHLANNNHLAPAVSPLFPGEQILFFRSFIPGASGHTNGEMDCLLPQEFVQHFYQEAAT
ARSEVALLRFVNPDTGRALFESKLHKQGFMTIASSGDHPIIMPTNGYFRFEAWVNQFYSLAPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;KAFTIPVLKISEMTNSRFPVPVDQMYTSRSEGIVVQPQNGRATIDGELLGTTLVSPVSVCNFKGNLQAEVPGQHQLYQLQ
LTNLDGSPIDPTDDTPGPLGCPDFTGLLYGVASQRGPGDATRAHEARIDTGSDTFAPKIGQVRFYSTSSDFETNQPTHFT
PIGIYIEGNSSDFNQWQLPRYGGHLANNNHLAPAVSPLFPGEQILFFRSFIPGASGHTNGEMDCLLPQEFVQHFYQEAAT
ARSEVALLRFVNPDTGRALFESKLHKQGFMTIASSGDHPIIMPTNGYFRFEAWVNQFYSLAPV
;
_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 'CHLORIDE ION' CL  
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LYS n 
1 2   ALA n 
1 3   PHE n 
1 4   THR n 
1 5   ILE n 
1 6   PRO n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  ILE n 
1 11  SER n 
1 12  GLU n 
1 13  MET n 
1 14  THR n 
1 15  ASN n 
1 16  SER n 
1 17  ARG n 
1 18  PHE n 
1 19  PRO n 
1 20  VAL n 
1 21  PRO n 
1 22  VAL n 
1 23  ASP n 
1 24  GLN n 
1 25  MET n 
1 26  TYR n 
1 27  THR n 
1 28  SER n 
1 29  ARG n 
1 30  SER n 
1 31  GLU n 
1 32  GLY n 
1 33  ILE n 
1 34  VAL n 
1 35  VAL n 
1 36  GLN n 
1 37  PRO n 
1 38  GLN n 
1 39  ASN n 
1 40  GLY n 
1 41  ARG n 
1 42  ALA n 
1 43  THR n 
1 44  ILE n 
1 45  ASP n 
1 46  GLY n 
1 47  GLU n 
1 48  LEU n 
1 49  LEU n 
1 50  GLY n 
1 51  THR n 
1 52  THR n 
1 53  LEU n 
1 54  VAL n 
1 55  SER n 
1 56  PRO n 
1 57  VAL n 
1 58  SER n 
1 59  VAL n 
1 60  CYS n 
1 61  ASN n 
1 62  PHE n 
1 63  LYS n 
1 64  GLY n 
1 65  ASN n 
1 66  LEU n 
1 67  GLN n 
1 68  ALA n 
1 69  GLU n 
1 70  VAL n 
1 71  PRO n 
1 72  GLY n 
1 73  GLN n 
1 74  HIS n 
1 75  GLN n 
1 76  LEU n 
1 77  TYR n 
1 78  GLN n 
1 79  LEU n 
1 80  GLN n 
1 81  LEU n 
1 82  THR n 
1 83  ASN n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  SER n 
1 88  PRO n 
1 89  ILE n 
1 90  ASP n 
1 91  PRO n 
1 92  THR n 
1 93  ASP n 
1 94  ASP n 
1 95  THR n 
1 96  PRO n 
1 97  GLY n 
1 98  PRO n 
1 99  LEU n 
1 100 GLY n 
1 101 CYS n 
1 102 PRO n 
1 103 ASP n 
1 104 PHE n 
1 105 THR n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 TYR n 
1 110 GLY n 
1 111 VAL n 
1 112 ALA n 
1 113 SER n 
1 114 GLN n 
1 115 ARG n 
1 116 GLY n 
1 117 PRO n 
1 118 GLY n 
1 119 ASP n 
1 120 ALA n 
1 121 THR n 
1 122 ARG n 
1 123 ALA n 
1 124 HIS n 
1 125 GLU n 
1 126 ALA n 
1 127 ARG n 
1 128 ILE n 
1 129 ASP n 
1 130 THR n 
1 131 GLY n 
1 132 SER n 
1 133 ASP n 
1 134 THR n 
1 135 PHE n 
1 136 ALA n 
1 137 PRO n 
1 138 LYS n 
1 139 ILE n 
1 140 GLY n 
1 141 GLN n 
1 142 VAL n 
1 143 ARG n 
1 144 PHE n 
1 145 TYR n 
1 146 SER n 
1 147 THR n 
1 148 SER n 
1 149 SER n 
1 150 ASP n 
1 151 PHE n 
1 152 GLU n 
1 153 THR n 
1 154 ASN n 
1 155 GLN n 
1 156 PRO n 
1 157 THR n 
1 158 HIS n 
1 159 PHE n 
1 160 THR n 
1 161 PRO n 
1 162 ILE n 
1 163 GLY n 
1 164 ILE n 
1 165 TYR n 
1 166 ILE n 
1 167 GLU n 
1 168 GLY n 
1 169 ASN n 
1 170 SER n 
1 171 SER n 
1 172 ASP n 
1 173 PHE n 
1 174 ASN n 
1 175 GLN n 
1 176 TRP n 
1 177 GLN n 
1 178 LEU n 
1 179 PRO n 
1 180 ARG n 
1 181 TYR n 
1 182 GLY n 
1 183 GLY n 
1 184 HIS n 
1 185 LEU n 
1 186 ALA n 
1 187 ASN n 
1 188 ASN n 
1 189 ASN n 
1 190 HIS n 
1 191 LEU n 
1 192 ALA n 
1 193 PRO n 
1 194 ALA n 
1 195 VAL n 
1 196 SER n 
1 197 PRO n 
1 198 LEU n 
1 199 PHE n 
1 200 PRO n 
1 201 GLY n 
1 202 GLU n 
1 203 GLN n 
1 204 ILE n 
1 205 LEU n 
1 206 PHE n 
1 207 PHE n 
1 208 ARG n 
1 209 SER n 
1 210 PHE n 
1 211 ILE n 
1 212 PRO n 
1 213 GLY n 
1 214 ALA n 
1 215 SER n 
1 216 GLY n 
1 217 HIS n 
1 218 THR n 
1 219 ASN n 
1 220 GLY n 
1 221 GLU n 
1 222 MET n 
1 223 ASP n 
1 224 CYS n 
1 225 LEU n 
1 226 LEU n 
1 227 PRO n 
1 228 GLN n 
1 229 GLU n 
1 230 PHE n 
1 231 VAL n 
1 232 GLN n 
1 233 HIS n 
1 234 PHE n 
1 235 TYR n 
1 236 GLN n 
1 237 GLU n 
1 238 ALA n 
1 239 ALA n 
1 240 THR n 
1 241 ALA n 
1 242 ARG n 
1 243 SER n 
1 244 GLU n 
1 245 VAL n 
1 246 ALA n 
1 247 LEU n 
1 248 LEU n 
1 249 ARG n 
1 250 PHE n 
1 251 VAL n 
1 252 ASN n 
1 253 PRO n 
1 254 ASP n 
1 255 THR n 
1 256 GLY n 
1 257 ARG n 
1 258 ALA n 
1 259 LEU n 
1 260 PHE n 
1 261 GLU n 
1 262 SER n 
1 263 LYS n 
1 264 LEU n 
1 265 HIS n 
1 266 LYS n 
1 267 GLN n 
1 268 GLY n 
1 269 PHE n 
1 270 MET n 
1 271 THR n 
1 272 ILE n 
1 273 ALA n 
1 274 SER n 
1 275 SER n 
1 276 GLY n 
1 277 ASP n 
1 278 HIS n 
1 279 PRO n 
1 280 ILE n 
1 281 ILE n 
1 282 MET n 
1 283 PRO n 
1 284 THR n 
1 285 ASN n 
1 286 GLY n 
1 287 TYR n 
1 288 PHE n 
1 289 ARG n 
1 290 PHE n 
1 291 GLU n 
1 292 ALA n 
1 293 TRP n 
1 294 VAL n 
1 295 ASN n 
1 296 GLN n 
1 297 PHE n 
1 298 TYR n 
1 299 SER n 
1 300 LEU n 
1 301 ALA n 
1 302 PRO n 
1 303 VAL 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                   303 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Human calicivirus NLV/VA97207/1997' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     165510 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     511693 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   LYS 1   225 ?   ?   ?   A . n 
A 1 2   ALA 2   226 226 ALA ALA A . n 
A 1 3   PHE 3   227 227 PHE PHE A . n 
A 1 4   THR 4   228 228 THR THR A . n 
A 1 5   ILE 5   229 229 ILE ILE A . n 
A 1 6   PRO 6   230 230 PRO PRO A . n 
A 1 7   VAL 7   231 231 VAL VAL A . n 
A 1 8   LEU 8   232 232 LEU LEU A . n 
A 1 9   LYS 9   233 233 LYS LYS A . n 
A 1 10  ILE 10  234 234 ILE ILE A . n 
A 1 11  SER 11  235 235 SER SER A . n 
A 1 12  GLU 12  236 236 GLU GLU A . n 
A 1 13  MET 13  237 237 MET MET A . n 
A 1 14  THR 14  238 238 THR THR A . n 
A 1 15  ASN 15  239 239 ASN ASN A . n 
A 1 16  SER 16  240 240 SER SER A . n 
A 1 17  ARG 17  241 241 ARG ARG A . n 
A 1 18  PHE 18  242 242 PHE PHE A . n 
A 1 19  PRO 19  243 243 PRO PRO A . n 
A 1 20  VAL 20  244 244 VAL VAL A . n 
A 1 21  PRO 21  245 245 PRO PRO A . n 
A 1 22  VAL 22  246 246 VAL VAL A . n 
A 1 23  ASP 23  247 247 ASP ASP A . n 
A 1 24  GLN 24  248 248 GLN GLN A . n 
A 1 25  MET 25  249 249 MET MET A . n 
A 1 26  TYR 26  250 250 TYR TYR A . n 
A 1 27  THR 27  251 251 THR THR A . n 
A 1 28  SER 28  252 252 SER SER A . n 
A 1 29  ARG 29  253 253 ARG ARG A . n 
A 1 30  SER 30  254 254 SER SER A . n 
A 1 31  GLU 31  255 255 GLU GLU A . n 
A 1 32  GLY 32  256 256 GLY GLY A . n 
A 1 33  ILE 33  257 257 ILE ILE A . n 
A 1 34  VAL 34  258 258 VAL VAL A . n 
A 1 35  VAL 35  259 259 VAL VAL A . n 
A 1 36  GLN 36  260 260 GLN GLN A . n 
A 1 37  PRO 37  261 261 PRO PRO A . n 
A 1 38  GLN 38  262 262 GLN GLN A . n 
A 1 39  ASN 39  263 263 ASN ASN A . n 
A 1 40  GLY 40  264 264 GLY GLY A . n 
A 1 41  ARG 41  265 265 ARG ARG A . n 
A 1 42  ALA 42  266 266 ALA ALA A . n 
A 1 43  THR 43  267 267 THR THR A . n 
A 1 44  ILE 44  268 268 ILE ILE A . n 
A 1 45  ASP 45  269 269 ASP ASP A . n 
A 1 46  GLY 46  270 270 GLY GLY A . n 
A 1 47  GLU 47  271 271 GLU GLU A . n 
A 1 48  LEU 48  272 272 LEU LEU A . n 
A 1 49  LEU 49  273 273 LEU LEU A . n 
A 1 50  GLY 50  274 274 GLY GLY A . n 
A 1 51  THR 51  275 275 THR THR A . n 
A 1 52  THR 52  276 276 THR THR A . n 
A 1 53  LEU 53  277 277 LEU LEU A . n 
A 1 54  VAL 54  278 278 VAL VAL A . n 
A 1 55  SER 55  279 279 SER SER A . n 
A 1 56  PRO 56  280 280 PRO PRO A . n 
A 1 57  VAL 57  281 281 VAL VAL A . n 
A 1 58  SER 58  282 282 SER SER A . n 
A 1 59  VAL 59  283 283 VAL VAL A . n 
A 1 60  CYS 60  284 284 CYS CYS A . n 
A 1 61  ASN 61  285 285 ASN ASN A . n 
A 1 62  PHE 62  286 286 PHE PHE A . n 
A 1 63  LYS 63  287 287 LYS LYS A . n 
A 1 64  GLY 64  288 288 GLY GLY A . n 
A 1 65  ASN 65  289 289 ASN ASN A . n 
A 1 66  LEU 66  290 290 LEU LEU A . n 
A 1 67  GLN 67  291 291 GLN GLN A . n 
A 1 68  ALA 68  292 292 ALA ALA A . n 
A 1 69  GLU 69  293 293 GLU GLU A . n 
A 1 70  VAL 70  294 294 VAL VAL A . n 
A 1 71  PRO 71  295 295 PRO PRO A . n 
A 1 72  GLY 72  296 296 GLY GLY A . n 
A 1 73  GLN 73  297 297 GLN GLN A . n 
A 1 74  HIS 74  298 298 HIS HIS A . n 
A 1 75  GLN 75  299 299 GLN GLN A . n 
A 1 76  LEU 76  300 300 LEU LEU A . n 
A 1 77  TYR 77  301 301 TYR TYR A . n 
A 1 78  GLN 78  302 302 GLN GLN A . n 
A 1 79  LEU 79  303 303 LEU LEU A . n 
A 1 80  GLN 80  304 304 GLN GLN A . n 
A 1 81  LEU 81  305 305 LEU LEU A . n 
A 1 82  THR 82  306 306 THR THR A . n 
A 1 83  ASN 83  307 307 ASN ASN A . n 
A 1 84  LEU 84  308 308 LEU LEU A . n 
A 1 85  ASP 85  309 309 ASP ASP A . n 
A 1 86  GLY 86  310 310 GLY GLY A . n 
A 1 87  SER 87  311 311 SER SER A . n 
A 1 88  PRO 88  312 312 PRO PRO A . n 
A 1 89  ILE 89  313 313 ILE ILE A . n 
A 1 90  ASP 90  314 314 ASP ASP A . n 
A 1 91  PRO 91  315 315 PRO PRO A . n 
A 1 92  THR 92  316 316 THR THR A . n 
A 1 93  ASP 93  317 317 ASP ASP A . n 
A 1 94  ASP 94  318 318 ASP ASP A . n 
A 1 95  THR 95  319 319 THR THR A . n 
A 1 96  PRO 96  320 320 PRO PRO A . n 
A 1 97  GLY 97  321 321 GLY GLY A . n 
A 1 98  PRO 98  322 322 PRO PRO A . n 
A 1 99  LEU 99  323 323 LEU LEU A . n 
A 1 100 GLY 100 324 324 GLY GLY A . n 
A 1 101 CYS 101 325 325 CYS CYS A . n 
A 1 102 PRO 102 326 326 PRO PRO A . n 
A 1 103 ASP 103 327 327 ASP ASP A . n 
A 1 104 PHE 104 328 328 PHE PHE A . n 
A 1 105 THR 105 329 329 THR THR A . n 
A 1 106 GLY 106 330 330 GLY GLY A . n 
A 1 107 LEU 107 331 331 LEU LEU A . n 
A 1 108 LEU 108 332 332 LEU LEU A . n 
A 1 109 TYR 109 333 333 TYR TYR A . n 
A 1 110 GLY 110 334 334 GLY GLY A . n 
A 1 111 VAL 111 335 335 VAL VAL A . n 
A 1 112 ALA 112 336 336 ALA ALA A . n 
A 1 113 SER 113 337 337 SER SER A . n 
A 1 114 GLN 114 338 338 GLN GLN A . n 
A 1 115 ARG 115 339 339 ARG ARG A . n 
A 1 116 GLY 116 340 340 GLY GLY A . n 
A 1 117 PRO 117 341 341 PRO PRO A . n 
A 1 118 GLY 118 342 342 GLY GLY A . n 
A 1 119 ASP 119 343 343 ASP ASP A . n 
A 1 120 ALA 120 344 344 ALA ALA A . n 
A 1 121 THR 121 345 345 THR THR A . n 
A 1 122 ARG 122 346 346 ARG ARG A . n 
A 1 123 ALA 123 347 347 ALA ALA A . n 
A 1 124 HIS 124 348 348 HIS HIS A . n 
A 1 125 GLU 125 349 349 GLU GLU A . n 
A 1 126 ALA 126 350 350 ALA ALA A . n 
A 1 127 ARG 127 351 351 ARG ARG A . n 
A 1 128 ILE 128 352 352 ILE ILE A . n 
A 1 129 ASP 129 353 353 ASP ASP A . n 
A 1 130 THR 130 354 354 THR THR A . n 
A 1 131 GLY 131 355 355 GLY GLY A . n 
A 1 132 SER 132 356 356 SER SER A . n 
A 1 133 ASP 133 357 357 ASP ASP A . n 
A 1 134 THR 134 358 358 THR THR A . n 
A 1 135 PHE 135 359 359 PHE PHE A . n 
A 1 136 ALA 136 360 360 ALA ALA A . n 
A 1 137 PRO 137 361 361 PRO PRO A . n 
A 1 138 LYS 138 362 362 LYS LYS A . n 
A 1 139 ILE 139 363 363 ILE ILE A . n 
A 1 140 GLY 140 364 364 GLY GLY A . n 
A 1 141 GLN 141 365 365 GLN GLN A . n 
A 1 142 VAL 142 366 366 VAL VAL A . n 
A 1 143 ARG 143 367 367 ARG ARG A . n 
A 1 144 PHE 144 368 368 PHE PHE A . n 
A 1 145 TYR 145 369 369 TYR TYR A . n 
A 1 146 SER 146 370 370 SER SER A . n 
A 1 147 THR 147 371 371 THR THR A . n 
A 1 148 SER 148 372 372 SER SER A . n 
A 1 149 SER 149 373 373 SER SER A . n 
A 1 150 ASP 150 374 374 ASP ASP A . n 
A 1 151 PHE 151 375 375 PHE PHE A . n 
A 1 152 GLU 152 376 376 GLU GLU A . n 
A 1 153 THR 153 377 377 THR THR A . n 
A 1 154 ASN 154 378 378 ASN ASN A . n 
A 1 155 GLN 155 379 379 GLN GLN A . n 
A 1 156 PRO 156 380 380 PRO PRO A . n 
A 1 157 THR 157 381 381 THR THR A . n 
A 1 158 HIS 158 382 382 HIS HIS A . n 
A 1 159 PHE 159 383 383 PHE PHE A . n 
A 1 160 THR 160 384 384 THR THR A . n 
A 1 161 PRO 161 385 385 PRO PRO A . n 
A 1 162 ILE 162 386 386 ILE ILE A . n 
A 1 163 GLY 163 387 387 GLY GLY A . n 
A 1 164 ILE 164 388 388 ILE ILE A . n 
A 1 165 TYR 165 389 389 TYR TYR A . n 
A 1 166 ILE 166 390 390 ILE ILE A . n 
A 1 167 GLU 167 391 391 GLU GLU A . n 
A 1 168 GLY 168 392 392 GLY GLY A . n 
A 1 169 ASN 169 393 393 ASN ASN A . n 
A 1 170 SER 170 394 394 SER SER A . n 
A 1 171 SER 171 395 395 SER SER A . n 
A 1 172 ASP 172 396 396 ASP ASP A . n 
A 1 173 PHE 173 397 397 PHE PHE A . n 
A 1 174 ASN 174 398 398 ASN ASN A . n 
A 1 175 GLN 175 399 399 GLN GLN A . n 
A 1 176 TRP 176 400 400 TRP TRP A . n 
A 1 177 GLN 177 401 401 GLN GLN A . n 
A 1 178 LEU 178 402 402 LEU LEU A . n 
A 1 179 PRO 179 403 403 PRO PRO A . n 
A 1 180 ARG 180 404 404 ARG ARG A . n 
A 1 181 TYR 181 405 405 TYR TYR A . n 
A 1 182 GLY 182 406 406 GLY GLY A . n 
A 1 183 GLY 183 407 407 GLY GLY A . n 
A 1 184 HIS 184 408 408 HIS HIS A . n 
A 1 185 LEU 185 409 409 LEU LEU A . n 
A 1 186 ALA 186 410 410 ALA ALA A . n 
A 1 187 ASN 187 411 411 ASN ASN A . n 
A 1 188 ASN 188 412 412 ASN ASN A . n 
A 1 189 ASN 189 413 413 ASN ASN A . n 
A 1 190 HIS 190 414 414 HIS HIS A . n 
A 1 191 LEU 191 415 415 LEU LEU A . n 
A 1 192 ALA 192 416 416 ALA ALA A . n 
A 1 193 PRO 193 417 417 PRO PRO A . n 
A 1 194 ALA 194 418 418 ALA ALA A . n 
A 1 195 VAL 195 419 419 VAL VAL A . n 
A 1 196 SER 196 420 420 SER SER A . n 
A 1 197 PRO 197 421 421 PRO PRO A . n 
A 1 198 LEU 198 422 422 LEU LEU A . n 
A 1 199 PHE 199 423 423 PHE PHE A . n 
A 1 200 PRO 200 424 424 PRO PRO A . n 
A 1 201 GLY 201 425 425 GLY GLY A . n 
A 1 202 GLU 202 426 426 GLU GLU A . n 
A 1 203 GLN 203 427 427 GLN GLN A . n 
A 1 204 ILE 204 428 428 ILE ILE A . n 
A 1 205 LEU 205 429 429 LEU LEU A . n 
A 1 206 PHE 206 430 430 PHE PHE A . n 
A 1 207 PHE 207 431 431 PHE PHE A . n 
A 1 208 ARG 208 432 432 ARG ARG A . n 
A 1 209 SER 209 433 433 SER SER A . n 
A 1 210 PHE 210 434 434 PHE PHE A . n 
A 1 211 ILE 211 435 435 ILE ILE A . n 
A 1 212 PRO 212 436 436 PRO PRO A . n 
A 1 213 GLY 213 437 437 GLY GLY A . n 
A 1 214 ALA 214 438 438 ALA ALA A . n 
A 1 215 SER 215 439 439 SER SER A . n 
A 1 216 GLY 216 440 440 GLY GLY A . n 
A 1 217 HIS 217 441 441 HIS HIS A . n 
A 1 218 THR 218 442 442 THR THR A . n 
A 1 219 ASN 219 443 443 ASN ASN A . n 
A 1 220 GLY 220 444 444 GLY GLY A . n 
A 1 221 GLU 221 445 445 GLU GLU A . n 
A 1 222 MET 222 446 446 MET MET A . n 
A 1 223 ASP 223 447 447 ASP ASP A . n 
A 1 224 CYS 224 448 448 CYS CYS A . n 
A 1 225 LEU 225 449 449 LEU LEU A . n 
A 1 226 LEU 226 450 450 LEU LEU A . n 
A 1 227 PRO 227 451 451 PRO PRO A . n 
A 1 228 GLN 228 452 452 GLN GLN A . n 
A 1 229 GLU 229 453 453 GLU GLU A . n 
A 1 230 PHE 230 454 454 PHE PHE A . n 
A 1 231 VAL 231 455 455 VAL VAL A . n 
A 1 232 GLN 232 456 456 GLN GLN A . n 
A 1 233 HIS 233 457 457 HIS HIS A . n 
A 1 234 PHE 234 458 458 PHE PHE A . n 
A 1 235 TYR 235 459 459 TYR TYR A . n 
A 1 236 GLN 236 460 460 GLN GLN A . n 
A 1 237 GLU 237 461 461 GLU GLU A . n 
A 1 238 ALA 238 462 462 ALA ALA A . n 
A 1 239 ALA 239 463 463 ALA ALA A . n 
A 1 240 THR 240 464 464 THR THR A . n 
A 1 241 ALA 241 465 465 ALA ALA A . n 
A 1 242 ARG 242 466 466 ARG ARG A . n 
A 1 243 SER 243 467 467 SER SER A . n 
A 1 244 GLU 244 468 468 GLU GLU A . n 
A 1 245 VAL 245 469 469 VAL VAL A . n 
A 1 246 ALA 246 470 470 ALA ALA A . n 
A 1 247 LEU 247 471 471 LEU LEU A . n 
A 1 248 LEU 248 472 472 LEU LEU A . n 
A 1 249 ARG 249 473 473 ARG ARG A . n 
A 1 250 PHE 250 474 474 PHE PHE A . n 
A 1 251 VAL 251 475 475 VAL VAL A . n 
A 1 252 ASN 252 476 476 ASN ASN A . n 
A 1 253 PRO 253 477 477 PRO PRO A . n 
A 1 254 ASP 254 478 478 ASP ASP A . n 
A 1 255 THR 255 479 479 THR THR A . n 
A 1 256 GLY 256 480 480 GLY GLY A . n 
A 1 257 ARG 257 481 481 ARG ARG A . n 
A 1 258 ALA 258 482 482 ALA ALA A . n 
A 1 259 LEU 259 483 483 LEU LEU A . n 
A 1 260 PHE 260 484 484 PHE PHE A . n 
A 1 261 GLU 261 485 485 GLU GLU A . n 
A 1 262 SER 262 486 486 SER SER A . n 
A 1 263 LYS 263 487 487 LYS LYS A . n 
A 1 264 LEU 264 488 488 LEU LEU A . n 
A 1 265 HIS 265 489 489 HIS HIS A . n 
A 1 266 LYS 266 490 490 LYS LYS A . n 
A 1 267 GLN 267 491 491 GLN GLN A . n 
A 1 268 GLY 268 492 492 GLY GLY A . n 
A 1 269 PHE 269 493 493 PHE PHE A . n 
A 1 270 MET 270 494 494 MET MET A . n 
A 1 271 THR 271 495 495 THR THR A . n 
A 1 272 ILE 272 496 496 ILE ILE A . n 
A 1 273 ALA 273 497 497 ALA ALA A . n 
A 1 274 SER 274 498 498 SER SER A . n 
A 1 275 SER 275 499 499 SER SER A . n 
A 1 276 GLY 276 500 500 GLY GLY A . n 
A 1 277 ASP 277 501 501 ASP ASP A . n 
A 1 278 HIS 278 502 502 HIS HIS A . n 
A 1 279 PRO 279 503 503 PRO PRO A . n 
A 1 280 ILE 280 504 504 ILE ILE A . n 
A 1 281 ILE 281 505 505 ILE ILE A . n 
A 1 282 MET 282 506 506 MET MET A . n 
A 1 283 PRO 283 507 507 PRO PRO A . n 
A 1 284 THR 284 508 508 THR THR A . n 
A 1 285 ASN 285 509 509 ASN ASN A . n 
A 1 286 GLY 286 510 510 GLY GLY A . n 
A 1 287 TYR 287 511 511 TYR TYR A . n 
A 1 288 PHE 288 512 512 PHE PHE A . n 
A 1 289 ARG 289 513 513 ARG ARG A . n 
A 1 290 PHE 290 514 514 PHE PHE A . n 
A 1 291 GLU 291 515 515 GLU GLU A . n 
A 1 292 ALA 292 516 516 ALA ALA A . n 
A 1 293 TRP 293 517 517 TRP TRP A . n 
A 1 294 VAL 294 518 518 VAL VAL A . n 
A 1 295 ASN 295 519 519 ASN ASN A . n 
A 1 296 GLN 296 520 520 GLN GLN A . n 
A 1 297 PHE 297 521 521 PHE PHE A . n 
A 1 298 TYR 298 522 522 TYR TYR A . n 
A 1 299 SER 299 523 523 SER SER A . n 
A 1 300 LEU 300 524 524 LEU LEU A . n 
A 1 301 ALA 301 525 525 ALA ALA A . n 
A 1 302 PRO 302 526 526 PRO PRO A . n 
A 1 303 VAL 303 527 527 VAL VAL A . n 
B 1 1   LYS 1   225 225 LYS LYS B . n 
B 1 2   ALA 2   226 226 ALA ALA B . n 
B 1 3   PHE 3   227 227 PHE PHE B . n 
B 1 4   THR 4   228 228 THR THR B . n 
B 1 5   ILE 5   229 229 ILE ILE B . n 
B 1 6   PRO 6   230 230 PRO PRO B . n 
B 1 7   VAL 7   231 231 VAL VAL B . n 
B 1 8   LEU 8   232 232 LEU LEU B . n 
B 1 9   LYS 9   233 233 LYS LYS B . n 
B 1 10  ILE 10  234 234 ILE ILE B . n 
B 1 11  SER 11  235 235 SER SER B . n 
B 1 12  GLU 12  236 236 GLU GLU B . n 
B 1 13  MET 13  237 237 MET MET B . n 
B 1 14  THR 14  238 238 THR THR B . n 
B 1 15  ASN 15  239 239 ASN ASN B . n 
B 1 16  SER 16  240 240 SER SER B . n 
B 1 17  ARG 17  241 241 ARG ARG B . n 
B 1 18  PHE 18  242 242 PHE PHE B . n 
B 1 19  PRO 19  243 243 PRO PRO B . n 
B 1 20  VAL 20  244 244 VAL VAL B . n 
B 1 21  PRO 21  245 245 PRO PRO B . n 
B 1 22  VAL 22  246 246 VAL VAL B . n 
B 1 23  ASP 23  247 247 ASP ASP B . n 
B 1 24  GLN 24  248 248 GLN GLN B . n 
B 1 25  MET 25  249 249 MET MET B . n 
B 1 26  TYR 26  250 250 TYR TYR B . n 
B 1 27  THR 27  251 251 THR THR B . n 
B 1 28  SER 28  252 252 SER SER B . n 
B 1 29  ARG 29  253 253 ARG ARG B . n 
B 1 30  SER 30  254 254 SER SER B . n 
B 1 31  GLU 31  255 255 GLU GLU B . n 
B 1 32  GLY 32  256 256 GLY GLY B . n 
B 1 33  ILE 33  257 257 ILE ILE B . n 
B 1 34  VAL 34  258 258 VAL VAL B . n 
B 1 35  VAL 35  259 259 VAL VAL B . n 
B 1 36  GLN 36  260 260 GLN GLN B . n 
B 1 37  PRO 37  261 261 PRO PRO B . n 
B 1 38  GLN 38  262 262 GLN GLN B . n 
B 1 39  ASN 39  263 263 ASN ASN B . n 
B 1 40  GLY 40  264 264 GLY GLY B . n 
B 1 41  ARG 41  265 265 ARG ARG B . n 
B 1 42  ALA 42  266 266 ALA ALA B . n 
B 1 43  THR 43  267 267 THR THR B . n 
B 1 44  ILE 44  268 268 ILE ILE B . n 
B 1 45  ASP 45  269 269 ASP ASP B . n 
B 1 46  GLY 46  270 270 GLY GLY B . n 
B 1 47  GLU 47  271 271 GLU GLU B . n 
B 1 48  LEU 48  272 272 LEU LEU B . n 
B 1 49  LEU 49  273 273 LEU LEU B . n 
B 1 50  GLY 50  274 274 GLY GLY B . n 
B 1 51  THR 51  275 275 THR THR B . n 
B 1 52  THR 52  276 276 THR THR B . n 
B 1 53  LEU 53  277 277 LEU LEU B . n 
B 1 54  VAL 54  278 278 VAL VAL B . n 
B 1 55  SER 55  279 279 SER SER B . n 
B 1 56  PRO 56  280 280 PRO PRO B . n 
B 1 57  VAL 57  281 281 VAL VAL B . n 
B 1 58  SER 58  282 282 SER SER B . n 
B 1 59  VAL 59  283 283 VAL VAL B . n 
B 1 60  CYS 60  284 284 CYS CYS B . n 
B 1 61  ASN 61  285 285 ASN ASN B . n 
B 1 62  PHE 62  286 286 PHE PHE B . n 
B 1 63  LYS 63  287 287 LYS LYS B . n 
B 1 64  GLY 64  288 288 GLY GLY B . n 
B 1 65  ASN 65  289 289 ASN ASN B . n 
B 1 66  LEU 66  290 290 LEU LEU B . n 
B 1 67  GLN 67  291 291 GLN GLN B . n 
B 1 68  ALA 68  292 292 ALA ALA B . n 
B 1 69  GLU 69  293 293 GLU GLU B . n 
B 1 70  VAL 70  294 294 VAL VAL B . n 
B 1 71  PRO 71  295 295 PRO PRO B . n 
B 1 72  GLY 72  296 296 GLY GLY B . n 
B 1 73  GLN 73  297 297 GLN GLN B . n 
B 1 74  HIS 74  298 298 HIS HIS B . n 
B 1 75  GLN 75  299 299 GLN GLN B . n 
B 1 76  LEU 76  300 300 LEU LEU B . n 
B 1 77  TYR 77  301 301 TYR TYR B . n 
B 1 78  GLN 78  302 302 GLN GLN B . n 
B 1 79  LEU 79  303 303 LEU LEU B . n 
B 1 80  GLN 80  304 304 GLN GLN B . n 
B 1 81  LEU 81  305 305 LEU LEU B . n 
B 1 82  THR 82  306 306 THR THR B . n 
B 1 83  ASN 83  307 307 ASN ASN B . n 
B 1 84  LEU 84  308 308 LEU LEU B . n 
B 1 85  ASP 85  309 309 ASP ASP B . n 
B 1 86  GLY 86  310 310 GLY GLY B . n 
B 1 87  SER 87  311 311 SER SER B . n 
B 1 88  PRO 88  312 312 PRO PRO B . n 
B 1 89  ILE 89  313 313 ILE ILE B . n 
B 1 90  ASP 90  314 314 ASP ASP B . n 
B 1 91  PRO 91  315 315 PRO PRO B . n 
B 1 92  THR 92  316 316 THR THR B . n 
B 1 93  ASP 93  317 317 ASP ASP B . n 
B 1 94  ASP 94  318 318 ASP ASP B . n 
B 1 95  THR 95  319 319 THR THR B . n 
B 1 96  PRO 96  320 320 PRO PRO B . n 
B 1 97  GLY 97  321 321 GLY GLY B . n 
B 1 98  PRO 98  322 322 PRO PRO B . n 
B 1 99  LEU 99  323 323 LEU LEU B . n 
B 1 100 GLY 100 324 324 GLY GLY B . n 
B 1 101 CYS 101 325 325 CYS CYS B . n 
B 1 102 PRO 102 326 326 PRO PRO B . n 
B 1 103 ASP 103 327 327 ASP ASP B . n 
B 1 104 PHE 104 328 328 PHE PHE B . n 
B 1 105 THR 105 329 329 THR THR B . n 
B 1 106 GLY 106 330 330 GLY GLY B . n 
B 1 107 LEU 107 331 331 LEU LEU B . n 
B 1 108 LEU 108 332 332 LEU LEU B . n 
B 1 109 TYR 109 333 333 TYR TYR B . n 
B 1 110 GLY 110 334 334 GLY GLY B . n 
B 1 111 VAL 111 335 335 VAL VAL B . n 
B 1 112 ALA 112 336 336 ALA ALA B . n 
B 1 113 SER 113 337 337 SER SER B . n 
B 1 114 GLN 114 338 338 GLN GLN B . n 
B 1 115 ARG 115 339 339 ARG ARG B . n 
B 1 116 GLY 116 340 340 GLY GLY B . n 
B 1 117 PRO 117 341 341 PRO PRO B . n 
B 1 118 GLY 118 342 342 GLY GLY B . n 
B 1 119 ASP 119 343 343 ASP ASP B . n 
B 1 120 ALA 120 344 344 ALA ALA B . n 
B 1 121 THR 121 345 345 THR THR B . n 
B 1 122 ARG 122 346 346 ARG ARG B . n 
B 1 123 ALA 123 347 347 ALA ALA B . n 
B 1 124 HIS 124 348 348 HIS HIS B . n 
B 1 125 GLU 125 349 349 GLU GLU B . n 
B 1 126 ALA 126 350 350 ALA ALA B . n 
B 1 127 ARG 127 351 351 ARG ARG B . n 
B 1 128 ILE 128 352 352 ILE ILE B . n 
B 1 129 ASP 129 353 353 ASP ASP B . n 
B 1 130 THR 130 354 354 THR THR B . n 
B 1 131 GLY 131 355 355 GLY GLY B . n 
B 1 132 SER 132 356 356 SER SER B . n 
B 1 133 ASP 133 357 357 ASP ASP B . n 
B 1 134 THR 134 358 358 THR THR B . n 
B 1 135 PHE 135 359 359 PHE PHE B . n 
B 1 136 ALA 136 360 360 ALA ALA B . n 
B 1 137 PRO 137 361 361 PRO PRO B . n 
B 1 138 LYS 138 362 362 LYS LYS B . n 
B 1 139 ILE 139 363 363 ILE ILE B . n 
B 1 140 GLY 140 364 364 GLY GLY B . n 
B 1 141 GLN 141 365 365 GLN GLN B . n 
B 1 142 VAL 142 366 366 VAL VAL B . n 
B 1 143 ARG 143 367 367 ARG ARG B . n 
B 1 144 PHE 144 368 368 PHE PHE B . n 
B 1 145 TYR 145 369 369 TYR TYR B . n 
B 1 146 SER 146 370 370 SER SER B . n 
B 1 147 THR 147 371 371 THR THR B . n 
B 1 148 SER 148 372 372 SER SER B . n 
B 1 149 SER 149 373 373 SER SER B . n 
B 1 150 ASP 150 374 374 ASP ASP B . n 
B 1 151 PHE 151 375 375 PHE PHE B . n 
B 1 152 GLU 152 376 376 GLU GLU B . n 
B 1 153 THR 153 377 377 THR THR B . n 
B 1 154 ASN 154 378 378 ASN ASN B . n 
B 1 155 GLN 155 379 379 GLN GLN B . n 
B 1 156 PRO 156 380 380 PRO PRO B . n 
B 1 157 THR 157 381 381 THR THR B . n 
B 1 158 HIS 158 382 382 HIS HIS B . n 
B 1 159 PHE 159 383 383 PHE PHE B . n 
B 1 160 THR 160 384 384 THR THR B . n 
B 1 161 PRO 161 385 385 PRO PRO B . n 
B 1 162 ILE 162 386 386 ILE ILE B . n 
B 1 163 GLY 163 387 387 GLY GLY B . n 
B 1 164 ILE 164 388 388 ILE ILE B . n 
B 1 165 TYR 165 389 389 TYR TYR B . n 
B 1 166 ILE 166 390 390 ILE ILE B . n 
B 1 167 GLU 167 391 391 GLU GLU B . n 
B 1 168 GLY 168 392 392 GLY GLY B . n 
B 1 169 ASN 169 393 393 ASN ASN B . n 
B 1 170 SER 170 394 394 SER SER B . n 
B 1 171 SER 171 395 395 SER SER B . n 
B 1 172 ASP 172 396 396 ASP ASP B . n 
B 1 173 PHE 173 397 397 PHE PHE B . n 
B 1 174 ASN 174 398 398 ASN ASN B . n 
B 1 175 GLN 175 399 399 GLN GLN B . n 
B 1 176 TRP 176 400 400 TRP TRP B . n 
B 1 177 GLN 177 401 401 GLN GLN B . n 
B 1 178 LEU 178 402 402 LEU LEU B . n 
B 1 179 PRO 179 403 403 PRO PRO B . n 
B 1 180 ARG 180 404 404 ARG ARG B . n 
B 1 181 TYR 181 405 405 TYR TYR B . n 
B 1 182 GLY 182 406 406 GLY GLY B . n 
B 1 183 GLY 183 407 407 GLY GLY B . n 
B 1 184 HIS 184 408 408 HIS HIS B . n 
B 1 185 LEU 185 409 409 LEU LEU B . n 
B 1 186 ALA 186 410 410 ALA ALA B . n 
B 1 187 ASN 187 411 411 ASN ASN B . n 
B 1 188 ASN 188 412 412 ASN ASN B . n 
B 1 189 ASN 189 413 413 ASN ASN B . n 
B 1 190 HIS 190 414 414 HIS HIS B . n 
B 1 191 LEU 191 415 415 LEU LEU B . n 
B 1 192 ALA 192 416 416 ALA ALA B . n 
B 1 193 PRO 193 417 417 PRO PRO B . n 
B 1 194 ALA 194 418 418 ALA ALA B . n 
B 1 195 VAL 195 419 419 VAL VAL B . n 
B 1 196 SER 196 420 420 SER SER B . n 
B 1 197 PRO 197 421 421 PRO PRO B . n 
B 1 198 LEU 198 422 422 LEU LEU B . n 
B 1 199 PHE 199 423 423 PHE PHE B . n 
B 1 200 PRO 200 424 424 PRO PRO B . n 
B 1 201 GLY 201 425 425 GLY GLY B . n 
B 1 202 GLU 202 426 426 GLU GLU B . n 
B 1 203 GLN 203 427 427 GLN GLN B . n 
B 1 204 ILE 204 428 428 ILE ILE B . n 
B 1 205 LEU 205 429 429 LEU LEU B . n 
B 1 206 PHE 206 430 430 PHE PHE B . n 
B 1 207 PHE 207 431 431 PHE PHE B . n 
B 1 208 ARG 208 432 432 ARG ARG B . n 
B 1 209 SER 209 433 433 SER SER B . n 
B 1 210 PHE 210 434 434 PHE PHE B . n 
B 1 211 ILE 211 435 435 ILE ILE B . n 
B 1 212 PRO 212 436 436 PRO PRO B . n 
B 1 213 GLY 213 437 437 GLY GLY B . n 
B 1 214 ALA 214 438 438 ALA ALA B . n 
B 1 215 SER 215 439 439 SER SER B . n 
B 1 216 GLY 216 440 440 GLY GLY B . n 
B 1 217 HIS 217 441 441 HIS HIS B . n 
B 1 218 THR 218 442 442 THR THR B . n 
B 1 219 ASN 219 443 443 ASN ASN B . n 
B 1 220 GLY 220 444 444 GLY GLY B . n 
B 1 221 GLU 221 445 445 GLU GLU B . n 
B 1 222 MET 222 446 446 MET MET B . n 
B 1 223 ASP 223 447 447 ASP ASP B . n 
B 1 224 CYS 224 448 448 CYS CYS B . n 
B 1 225 LEU 225 449 449 LEU LEU B . n 
B 1 226 LEU 226 450 450 LEU LEU B . n 
B 1 227 PRO 227 451 451 PRO PRO B . n 
B 1 228 GLN 228 452 452 GLN GLN B . n 
B 1 229 GLU 229 453 453 GLU GLU B . n 
B 1 230 PHE 230 454 454 PHE PHE B . n 
B 1 231 VAL 231 455 455 VAL VAL B . n 
B 1 232 GLN 232 456 456 GLN GLN B . n 
B 1 233 HIS 233 457 457 HIS HIS B . n 
B 1 234 PHE 234 458 458 PHE PHE B . n 
B 1 235 TYR 235 459 459 TYR TYR B . n 
B 1 236 GLN 236 460 460 GLN GLN B . n 
B 1 237 GLU 237 461 461 GLU GLU B . n 
B 1 238 ALA 238 462 462 ALA ALA B . n 
B 1 239 ALA 239 463 463 ALA ALA B . n 
B 1 240 THR 240 464 464 THR THR B . n 
B 1 241 ALA 241 465 465 ALA ALA B . n 
B 1 242 ARG 242 466 466 ARG ARG B . n 
B 1 243 SER 243 467 467 SER SER B . n 
B 1 244 GLU 244 468 468 GLU GLU B . n 
B 1 245 VAL 245 469 469 VAL VAL B . n 
B 1 246 ALA 246 470 470 ALA ALA B . n 
B 1 247 LEU 247 471 471 LEU LEU B . n 
B 1 248 LEU 248 472 472 LEU LEU B . n 
B 1 249 ARG 249 473 473 ARG ARG B . n 
B 1 250 PHE 250 474 474 PHE PHE B . n 
B 1 251 VAL 251 475 475 VAL VAL B . n 
B 1 252 ASN 252 476 476 ASN ASN B . n 
B 1 253 PRO 253 477 477 PRO PRO B . n 
B 1 254 ASP 254 478 478 ASP ASP B . n 
B 1 255 THR 255 479 479 THR THR B . n 
B 1 256 GLY 256 480 480 GLY GLY B . n 
B 1 257 ARG 257 481 481 ARG ARG B . n 
B 1 258 ALA 258 482 482 ALA ALA B . n 
B 1 259 LEU 259 483 483 LEU LEU B . n 
B 1 260 PHE 260 484 484 PHE PHE B . n 
B 1 261 GLU 261 485 485 GLU GLU B . n 
B 1 262 SER 262 486 486 SER SER B . n 
B 1 263 LYS 263 487 487 LYS LYS B . n 
B 1 264 LEU 264 488 488 LEU LEU B . n 
B 1 265 HIS 265 489 489 HIS HIS B . n 
B 1 266 LYS 266 490 490 LYS LYS B . n 
B 1 267 GLN 267 491 491 GLN GLN B . n 
B 1 268 GLY 268 492 492 GLY GLY B . n 
B 1 269 PHE 269 493 493 PHE PHE B . n 
B 1 270 MET 270 494 494 MET MET B . n 
B 1 271 THR 271 495 495 THR THR B . n 
B 1 272 ILE 272 496 496 ILE ILE B . n 
B 1 273 ALA 273 497 497 ALA ALA B . n 
B 1 274 SER 274 498 498 SER SER B . n 
B 1 275 SER 275 499 499 SER SER B . n 
B 1 276 GLY 276 500 500 GLY GLY B . n 
B 1 277 ASP 277 501 501 ASP ASP B . n 
B 1 278 HIS 278 502 502 HIS HIS B . n 
B 1 279 PRO 279 503 503 PRO PRO B . n 
B 1 280 ILE 280 504 504 ILE ILE B . n 
B 1 281 ILE 281 505 505 ILE ILE B . n 
B 1 282 MET 282 506 506 MET MET B . n 
B 1 283 PRO 283 507 507 PRO PRO B . n 
B 1 284 THR 284 508 508 THR THR B . n 
B 1 285 ASN 285 509 509 ASN ASN B . n 
B 1 286 GLY 286 510 510 GLY GLY B . n 
B 1 287 TYR 287 511 511 TYR TYR B . n 
B 1 288 PHE 288 512 512 PHE PHE B . n 
B 1 289 ARG 289 513 513 ARG ARG B . n 
B 1 290 PHE 290 514 514 PHE PHE B . n 
B 1 291 GLU 291 515 515 GLU GLU B . n 
B 1 292 ALA 292 516 516 ALA ALA B . n 
B 1 293 TRP 293 517 517 TRP TRP B . n 
B 1 294 VAL 294 518 518 VAL VAL B . n 
B 1 295 ASN 295 519 519 ASN ASN B . n 
B 1 296 GLN 296 520 520 GLN GLN B . n 
B 1 297 PHE 297 521 521 PHE PHE B . n 
B 1 298 TYR 298 522 522 TYR TYR B . n 
B 1 299 SER 299 523 523 SER SER B . n 
B 1 300 LEU 300 524 524 LEU LEU B . n 
B 1 301 ALA 301 525 525 ALA ALA B . n 
B 1 302 PRO 302 526 526 PRO PRO B . n 
B 1 303 VAL 303 527 527 VAL VAL 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 CL  1   601  2   CL  CL  A . 
D 2 CL  1   601  1   CL  CL  B . 
E 3 HOH 1   701  228 HOH HOH A . 
E 3 HOH 2   702  429 HOH HOH A . 
E 3 HOH 3   703  390 HOH HOH A . 
E 3 HOH 4   704  459 HOH HOH A . 
E 3 HOH 5   705  74  HOH HOH A . 
E 3 HOH 6   706  19  HOH HOH A . 
E 3 HOH 7   707  283 HOH HOH A . 
E 3 HOH 8   708  273 HOH HOH A . 
E 3 HOH 9   709  281 HOH HOH A . 
E 3 HOH 10  710  299 HOH HOH A . 
E 3 HOH 11  711  302 HOH HOH A . 
E 3 HOH 12  712  303 HOH HOH A . 
E 3 HOH 13  713  130 HOH HOH A . 
E 3 HOH 14  714  70  HOH HOH A . 
E 3 HOH 15  715  465 HOH HOH A . 
E 3 HOH 16  716  288 HOH HOH A . 
E 3 HOH 17  717  525 HOH HOH A . 
E 3 HOH 18  718  167 HOH HOH A . 
E 3 HOH 19  719  29  HOH HOH A . 
E 3 HOH 20  720  98  HOH HOH A . 
E 3 HOH 21  721  150 HOH HOH A . 
E 3 HOH 22  722  60  HOH HOH A . 
E 3 HOH 23  723  292 HOH HOH A . 
E 3 HOH 24  724  416 HOH HOH A . 
E 3 HOH 25  725  403 HOH HOH A . 
E 3 HOH 26  726  128 HOH HOH A . 
E 3 HOH 27  727  457 HOH HOH A . 
E 3 HOH 28  728  59  HOH HOH A . 
E 3 HOH 29  729  57  HOH HOH A . 
E 3 HOH 30  730  319 HOH HOH A . 
E 3 HOH 31  731  10  HOH HOH A . 
E 3 HOH 32  732  433 HOH HOH A . 
E 3 HOH 33  733  247 HOH HOH A . 
E 3 HOH 34  734  524 HOH HOH A . 
E 3 HOH 35  735  56  HOH HOH A . 
E 3 HOH 36  736  1   HOH HOH A . 
E 3 HOH 37  737  317 HOH HOH A . 
E 3 HOH 38  738  15  HOH HOH A . 
E 3 HOH 39  739  401 HOH HOH A . 
E 3 HOH 40  740  437 HOH HOH A . 
E 3 HOH 41  741  147 HOH HOH A . 
E 3 HOH 42  742  136 HOH HOH A . 
E 3 HOH 43  743  100 HOH HOH A . 
E 3 HOH 44  744  558 HOH HOH A . 
E 3 HOH 45  745  501 HOH HOH A . 
E 3 HOH 46  746  470 HOH HOH A . 
E 3 HOH 47  747  241 HOH HOH A . 
E 3 HOH 48  748  87  HOH HOH A . 
E 3 HOH 49  749  88  HOH HOH A . 
E 3 HOH 50  750  8   HOH HOH A . 
E 3 HOH 51  751  259 HOH HOH A . 
E 3 HOH 52  752  189 HOH HOH A . 
E 3 HOH 53  753  471 HOH HOH A . 
E 3 HOH 54  754  229 HOH HOH A . 
E 3 HOH 55  755  264 HOH HOH A . 
E 3 HOH 56  756  249 HOH HOH A . 
E 3 HOH 57  757  14  HOH HOH A . 
E 3 HOH 58  758  263 HOH HOH A . 
E 3 HOH 59  759  12  HOH HOH A . 
E 3 HOH 60  760  75  HOH HOH A . 
E 3 HOH 61  761  120 HOH HOH A . 
E 3 HOH 62  762  2   HOH HOH A . 
E 3 HOH 63  763  20  HOH HOH A . 
E 3 HOH 64  764  232 HOH HOH A . 
E 3 HOH 65  765  330 HOH HOH A . 
E 3 HOH 66  766  301 HOH HOH A . 
E 3 HOH 67  767  194 HOH HOH A . 
E 3 HOH 68  768  154 HOH HOH A . 
E 3 HOH 69  769  377 HOH HOH A . 
E 3 HOH 70  770  101 HOH HOH A . 
E 3 HOH 71  771  18  HOH HOH A . 
E 3 HOH 72  772  468 HOH HOH A . 
E 3 HOH 73  773  504 HOH HOH A . 
E 3 HOH 74  774  54  HOH HOH A . 
E 3 HOH 75  775  79  HOH HOH A . 
E 3 HOH 76  776  67  HOH HOH A . 
E 3 HOH 77  777  385 HOH HOH A . 
E 3 HOH 78  778  219 HOH HOH A . 
E 3 HOH 79  779  31  HOH HOH A . 
E 3 HOH 80  780  211 HOH HOH A . 
E 3 HOH 81  781  139 HOH HOH A . 
E 3 HOH 82  782  422 HOH HOH A . 
E 3 HOH 83  783  388 HOH HOH A . 
E 3 HOH 84  784  115 HOH HOH A . 
E 3 HOH 85  785  406 HOH HOH A . 
E 3 HOH 86  786  65  HOH HOH A . 
E 3 HOH 87  787  173 HOH HOH A . 
E 3 HOH 88  788  35  HOH HOH A . 
E 3 HOH 89  789  238 HOH HOH A . 
E 3 HOH 90  790  32  HOH HOH A . 
E 3 HOH 91  791  107 HOH HOH A . 
E 3 HOH 92  792  28  HOH HOH A . 
E 3 HOH 93  793  405 HOH HOH A . 
E 3 HOH 94  794  230 HOH HOH A . 
E 3 HOH 95  795  149 HOH HOH A . 
E 3 HOH 96  796  85  HOH HOH A . 
E 3 HOH 97  797  25  HOH HOH A . 
E 3 HOH 98  798  188 HOH HOH A . 
E 3 HOH 99  799  322 HOH HOH A . 
E 3 HOH 100 800  82  HOH HOH A . 
E 3 HOH 101 801  415 HOH HOH A . 
E 3 HOH 102 802  526 HOH HOH A . 
E 3 HOH 103 803  289 HOH HOH A . 
E 3 HOH 104 804  193 HOH HOH A . 
E 3 HOH 105 805  477 HOH HOH A . 
E 3 HOH 106 806  453 HOH HOH A . 
E 3 HOH 107 807  49  HOH HOH A . 
E 3 HOH 108 808  397 HOH HOH A . 
E 3 HOH 109 809  185 HOH HOH A . 
E 3 HOH 110 810  133 HOH HOH A . 
E 3 HOH 111 811  96  HOH HOH A . 
E 3 HOH 112 812  408 HOH HOH A . 
E 3 HOH 113 813  179 HOH HOH A . 
E 3 HOH 114 814  458 HOH HOH A . 
E 3 HOH 115 815  321 HOH HOH A . 
E 3 HOH 116 816  312 HOH HOH A . 
E 3 HOH 117 817  181 HOH HOH A . 
E 3 HOH 118 818  77  HOH HOH A . 
E 3 HOH 119 819  155 HOH HOH A . 
E 3 HOH 120 820  58  HOH HOH A . 
E 3 HOH 121 821  366 HOH HOH A . 
E 3 HOH 122 822  80  HOH HOH A . 
E 3 HOH 123 823  478 HOH HOH A . 
E 3 HOH 124 824  92  HOH HOH A . 
E 3 HOH 125 825  561 HOH HOH A . 
E 3 HOH 126 826  140 HOH HOH A . 
E 3 HOH 127 827  493 HOH HOH A . 
E 3 HOH 128 828  160 HOH HOH A . 
E 3 HOH 129 829  108 HOH HOH A . 
E 3 HOH 130 830  393 HOH HOH A . 
E 3 HOH 131 831  534 HOH HOH A . 
E 3 HOH 132 832  240 HOH HOH A . 
E 3 HOH 133 833  277 HOH HOH A . 
E 3 HOH 134 834  318 HOH HOH A . 
E 3 HOH 135 835  430 HOH HOH A . 
E 3 HOH 136 836  105 HOH HOH A . 
E 3 HOH 137 837  271 HOH HOH A . 
E 3 HOH 138 838  148 HOH HOH A . 
E 3 HOH 139 839  315 HOH HOH A . 
E 3 HOH 140 840  153 HOH HOH A . 
E 3 HOH 141 841  426 HOH HOH A . 
E 3 HOH 142 842  209 HOH HOH A . 
E 3 HOH 143 843  205 HOH HOH A . 
E 3 HOH 144 844  90  HOH HOH A . 
E 3 HOH 145 845  51  HOH HOH A . 
E 3 HOH 146 846  467 HOH HOH A . 
E 3 HOH 147 847  425 HOH HOH A . 
E 3 HOH 148 848  544 HOH HOH A . 
E 3 HOH 149 849  286 HOH HOH A . 
E 3 HOH 150 850  48  HOH HOH A . 
E 3 HOH 151 851  326 HOH HOH A . 
E 3 HOH 152 852  81  HOH HOH A . 
E 3 HOH 153 853  207 HOH HOH A . 
E 3 HOH 154 854  221 HOH HOH A . 
E 3 HOH 155 855  191 HOH HOH A . 
E 3 HOH 156 856  515 HOH HOH A . 
E 3 HOH 157 857  144 HOH HOH A . 
E 3 HOH 158 858  358 HOH HOH A . 
E 3 HOH 159 859  399 HOH HOH A . 
E 3 HOH 160 860  484 HOH HOH A . 
E 3 HOH 161 861  488 HOH HOH A . 
E 3 HOH 162 862  538 HOH HOH A . 
E 3 HOH 163 863  474 HOH HOH A . 
E 3 HOH 164 864  389 HOH HOH A . 
E 3 HOH 165 865  365 HOH HOH A . 
E 3 HOH 166 866  293 HOH HOH A . 
E 3 HOH 167 867  223 HOH HOH A . 
E 3 HOH 168 868  436 HOH HOH A . 
E 3 HOH 169 869  563 HOH HOH A . 
E 3 HOH 170 870  539 HOH HOH A . 
E 3 HOH 171 871  261 HOH HOH A . 
E 3 HOH 172 872  502 HOH HOH A . 
E 3 HOH 173 873  537 HOH HOH A . 
E 3 HOH 174 874  496 HOH HOH A . 
E 3 HOH 175 875  213 HOH HOH A . 
E 3 HOH 176 876  392 HOH HOH A . 
E 3 HOH 177 877  182 HOH HOH A . 
E 3 HOH 178 878  513 HOH HOH A . 
E 3 HOH 179 879  547 HOH HOH A . 
E 3 HOH 180 880  439 HOH HOH A . 
E 3 HOH 181 881  222 HOH HOH A . 
E 3 HOH 182 882  452 HOH HOH A . 
E 3 HOH 183 883  104 HOH HOH A . 
E 3 HOH 184 884  536 HOH HOH A . 
E 3 HOH 185 885  218 HOH HOH A . 
E 3 HOH 186 886  253 HOH HOH A . 
E 3 HOH 187 887  215 HOH HOH A . 
E 3 HOH 188 888  460 HOH HOH A . 
E 3 HOH 189 889  529 HOH HOH A . 
E 3 HOH 190 890  419 HOH HOH A . 
E 3 HOH 191 891  423 HOH HOH A . 
E 3 HOH 192 892  339 HOH HOH A . 
E 3 HOH 193 893  169 HOH HOH A . 
E 3 HOH 194 894  184 HOH HOH A . 
E 3 HOH 195 895  351 HOH HOH A . 
E 3 HOH 196 896  559 HOH HOH A . 
E 3 HOH 197 897  518 HOH HOH A . 
E 3 HOH 198 898  512 HOH HOH A . 
E 3 HOH 199 899  443 HOH HOH A . 
E 3 HOH 200 900  495 HOH HOH A . 
E 3 HOH 201 901  121 HOH HOH A . 
E 3 HOH 202 902  348 HOH HOH A . 
E 3 HOH 203 903  162 HOH HOH A . 
E 3 HOH 204 904  387 HOH HOH A . 
E 3 HOH 205 905  506 HOH HOH A . 
E 3 HOH 206 906  233 HOH HOH A . 
E 3 HOH 207 907  398 HOH HOH A . 
E 3 HOH 208 908  442 HOH HOH A . 
E 3 HOH 209 909  505 HOH HOH A . 
E 3 HOH 210 910  516 HOH HOH A . 
E 3 HOH 211 911  517 HOH HOH A . 
E 3 HOH 212 912  248 HOH HOH A . 
E 3 HOH 213 913  417 HOH HOH A . 
E 3 HOH 214 914  461 HOH HOH A . 
E 3 HOH 215 915  509 HOH HOH A . 
E 3 HOH 216 916  553 HOH HOH A . 
E 3 HOH 217 917  391 HOH HOH A . 
E 3 HOH 218 918  379 HOH HOH A . 
E 3 HOH 219 919  236 HOH HOH A . 
E 3 HOH 220 920  530 HOH HOH A . 
E 3 HOH 221 921  545 HOH HOH A . 
E 3 HOH 222 922  476 HOH HOH A . 
E 3 HOH 223 923  431 HOH HOH A . 
E 3 HOH 224 924  532 HOH HOH A . 
E 3 HOH 225 925  71  HOH HOH A . 
E 3 HOH 226 926  521 HOH HOH A . 
E 3 HOH 227 927  131 HOH HOH A . 
E 3 HOH 228 928  497 HOH HOH A . 
E 3 HOH 229 929  357 HOH HOH A . 
E 3 HOH 230 930  475 HOH HOH A . 
E 3 HOH 231 931  332 HOH HOH A . 
E 3 HOH 232 932  327 HOH HOH A . 
E 3 HOH 233 933  542 HOH HOH A . 
E 3 HOH 234 934  304 HOH HOH A . 
E 3 HOH 235 935  252 HOH HOH A . 
E 3 HOH 236 936  396 HOH HOH A . 
E 3 HOH 237 937  314 HOH HOH A . 
E 3 HOH 238 938  560 HOH HOH A . 
E 3 HOH 239 939  372 HOH HOH A . 
E 3 HOH 240 940  323 HOH HOH A . 
E 3 HOH 241 941  557 HOH HOH A . 
E 3 HOH 242 942  400 HOH HOH A . 
E 3 HOH 243 943  456 HOH HOH A . 
E 3 HOH 244 944  371 HOH HOH A . 
E 3 HOH 245 945  226 HOH HOH A . 
E 3 HOH 246 946  432 HOH HOH A . 
E 3 HOH 247 947  543 HOH HOH A . 
E 3 HOH 248 948  546 HOH HOH A . 
E 3 HOH 249 949  479 HOH HOH A . 
E 3 HOH 250 950  353 HOH HOH A . 
F 3 HOH 1   701  554 HOH HOH B . 
F 3 HOH 2   702  472 HOH HOH B . 
F 3 HOH 3   703  234 HOH HOH B . 
F 3 HOH 4   704  359 HOH HOH B . 
F 3 HOH 5   705  156 HOH HOH B . 
F 3 HOH 6   706  69  HOH HOH B . 
F 3 HOH 7   707  492 HOH HOH B . 
F 3 HOH 8   708  199 HOH HOH B . 
F 3 HOH 9   709  410 HOH HOH B . 
F 3 HOH 10  710  350 HOH HOH B . 
F 3 HOH 11  711  21  HOH HOH B . 
F 3 HOH 12  712  243 HOH HOH B . 
F 3 HOH 13  713  62  HOH HOH B . 
F 3 HOH 14  714  528 HOH HOH B . 
F 3 HOH 15  715  297 HOH HOH B . 
F 3 HOH 16  716  369 HOH HOH B . 
F 3 HOH 17  717  135 HOH HOH B . 
F 3 HOH 18  718  257 HOH HOH B . 
F 3 HOH 19  719  300 HOH HOH B . 
F 3 HOH 20  720  381 HOH HOH B . 
F 3 HOH 21  721  285 HOH HOH B . 
F 3 HOH 22  722  190 HOH HOH B . 
F 3 HOH 23  723  446 HOH HOH B . 
F 3 HOH 24  724  76  HOH HOH B . 
F 3 HOH 25  725  201 HOH HOH B . 
F 3 HOH 26  726  111 HOH HOH B . 
F 3 HOH 27  727  279 HOH HOH B . 
F 3 HOH 28  728  47  HOH HOH B . 
F 3 HOH 29  729  125 HOH HOH B . 
F 3 HOH 30  730  349 HOH HOH B . 
F 3 HOH 31  731  183 HOH HOH B . 
F 3 HOH 32  732  239 HOH HOH B . 
F 3 HOH 33  733  168 HOH HOH B . 
F 3 HOH 34  734  175 HOH HOH B . 
F 3 HOH 35  735  483 HOH HOH B . 
F 3 HOH 36  736  186 HOH HOH B . 
F 3 HOH 37  737  174 HOH HOH B . 
F 3 HOH 38  738  347 HOH HOH B . 
F 3 HOH 39  739  142 HOH HOH B . 
F 3 HOH 40  740  112 HOH HOH B . 
F 3 HOH 41  741  552 HOH HOH B . 
F 3 HOH 42  742  482 HOH HOH B . 
F 3 HOH 43  743  212 HOH HOH B . 
F 3 HOH 44  744  24  HOH HOH B . 
F 3 HOH 45  745  177 HOH HOH B . 
F 3 HOH 46  746  448 HOH HOH B . 
F 3 HOH 47  747  91  HOH HOH B . 
F 3 HOH 48  748  320 HOH HOH B . 
F 3 HOH 49  749  187 HOH HOH B . 
F 3 HOH 50  750  36  HOH HOH B . 
F 3 HOH 51  751  421 HOH HOH B . 
F 3 HOH 52  752  255 HOH HOH B . 
F 3 HOH 53  753  6   HOH HOH B . 
F 3 HOH 54  754  334 HOH HOH B . 
F 3 HOH 55  755  110 HOH HOH B . 
F 3 HOH 56  756  7   HOH HOH B . 
F 3 HOH 57  757  43  HOH HOH B . 
F 3 HOH 58  758  40  HOH HOH B . 
F 3 HOH 59  759  225 HOH HOH B . 
F 3 HOH 60  760  41  HOH HOH B . 
F 3 HOH 61  761  22  HOH HOH B . 
F 3 HOH 62  762  118 HOH HOH B . 
F 3 HOH 63  763  42  HOH HOH B . 
F 3 HOH 64  764  37  HOH HOH B . 
F 3 HOH 65  765  16  HOH HOH B . 
F 3 HOH 66  766  487 HOH HOH B . 
F 3 HOH 67  767  146 HOH HOH B . 
F 3 HOH 68  768  522 HOH HOH B . 
F 3 HOH 69  769  519 HOH HOH B . 
F 3 HOH 70  770  216 HOH HOH B . 
F 3 HOH 71  771  17  HOH HOH B . 
F 3 HOH 72  772  338 HOH HOH B . 
F 3 HOH 73  773  237 HOH HOH B . 
F 3 HOH 74  774  324 HOH HOH B . 
F 3 HOH 75  775  258 HOH HOH B . 
F 3 HOH 76  776  97  HOH HOH B . 
F 3 HOH 77  777  45  HOH HOH B . 
F 3 HOH 78  778  61  HOH HOH B . 
F 3 HOH 79  779  278 HOH HOH B . 
F 3 HOH 80  780  3   HOH HOH B . 
F 3 HOH 81  781  203 HOH HOH B . 
F 3 HOH 82  782  157 HOH HOH B . 
F 3 HOH 83  783  510 HOH HOH B . 
F 3 HOH 84  784  308 HOH HOH B . 
F 3 HOH 85  785  50  HOH HOH B . 
F 3 HOH 86  786  23  HOH HOH B . 
F 3 HOH 87  787  4   HOH HOH B . 
F 3 HOH 88  788  103 HOH HOH B . 
F 3 HOH 89  789  491 HOH HOH B . 
F 3 HOH 90  790  94  HOH HOH B . 
F 3 HOH 91  791  122 HOH HOH B . 
F 3 HOH 92  792  72  HOH HOH B . 
F 3 HOH 93  793  523 HOH HOH B . 
F 3 HOH 94  794  340 HOH HOH B . 
F 3 HOH 95  795  83  HOH HOH B . 
F 3 HOH 96  796  407 HOH HOH B . 
F 3 HOH 97  797  306 HOH HOH B . 
F 3 HOH 98  798  413 HOH HOH B . 
F 3 HOH 99  799  329 HOH HOH B . 
F 3 HOH 100 800  374 HOH HOH B . 
F 3 HOH 101 801  565 HOH HOH B . 
F 3 HOH 102 802  224 HOH HOH B . 
F 3 HOH 103 803  152 HOH HOH B . 
F 3 HOH 104 804  454 HOH HOH B . 
F 3 HOH 105 805  84  HOH HOH B . 
F 3 HOH 106 806  161 HOH HOH B . 
F 3 HOH 107 807  106 HOH HOH B . 
F 3 HOH 108 808  63  HOH HOH B . 
F 3 HOH 109 809  231 HOH HOH B . 
F 3 HOH 110 810  141 HOH HOH B . 
F 3 HOH 111 811  490 HOH HOH B . 
F 3 HOH 112 812  198 HOH HOH B . 
F 3 HOH 113 813  46  HOH HOH B . 
F 3 HOH 114 814  44  HOH HOH B . 
F 3 HOH 115 815  166 HOH HOH B . 
F 3 HOH 116 816  210 HOH HOH B . 
F 3 HOH 117 817  466 HOH HOH B . 
F 3 HOH 118 818  200 HOH HOH B . 
F 3 HOH 119 819  217 HOH HOH B . 
F 3 HOH 120 820  132 HOH HOH B . 
F 3 HOH 121 821  5   HOH HOH B . 
F 3 HOH 122 822  55  HOH HOH B . 
F 3 HOH 123 823  164 HOH HOH B . 
F 3 HOH 124 824  287 HOH HOH B . 
F 3 HOH 125 825  73  HOH HOH B . 
F 3 HOH 126 826  99  HOH HOH B . 
F 3 HOH 127 827  337 HOH HOH B . 
F 3 HOH 128 828  333 HOH HOH B . 
F 3 HOH 129 829  9   HOH HOH B . 
F 3 HOH 130 830  382 HOH HOH B . 
F 3 HOH 131 831  328 HOH HOH B . 
F 3 HOH 132 832  86  HOH HOH B . 
F 3 HOH 133 833  325 HOH HOH B . 
F 3 HOH 134 834  127 HOH HOH B . 
F 3 HOH 135 835  145 HOH HOH B . 
F 3 HOH 136 836  438 HOH HOH B . 
F 3 HOH 137 837  68  HOH HOH B . 
F 3 HOH 138 838  176 HOH HOH B . 
F 3 HOH 139 839  39  HOH HOH B . 
F 3 HOH 140 840  428 HOH HOH B . 
F 3 HOH 141 841  434 HOH HOH B . 
F 3 HOH 142 842  227 HOH HOH B . 
F 3 HOH 143 843  170 HOH HOH B . 
F 3 HOH 144 844  254 HOH HOH B . 
F 3 HOH 145 845  13  HOH HOH B . 
F 3 HOH 146 846  66  HOH HOH B . 
F 3 HOH 147 847  64  HOH HOH B . 
F 3 HOH 148 848  196 HOH HOH B . 
F 3 HOH 149 849  27  HOH HOH B . 
F 3 HOH 150 850  311 HOH HOH B . 
F 3 HOH 151 851  178 HOH HOH B . 
F 3 HOH 152 852  310 HOH HOH B . 
F 3 HOH 153 853  336 HOH HOH B . 
F 3 HOH 154 854  265 HOH HOH B . 
F 3 HOH 155 855  272 HOH HOH B . 
F 3 HOH 156 856  246 HOH HOH B . 
F 3 HOH 157 857  274 HOH HOH B . 
F 3 HOH 158 858  138 HOH HOH B . 
F 3 HOH 159 859  514 HOH HOH B . 
F 3 HOH 160 860  481 HOH HOH B . 
F 3 HOH 161 861  208 HOH HOH B . 
F 3 HOH 162 862  335 HOH HOH B . 
F 3 HOH 163 863  290 HOH HOH B . 
F 3 HOH 164 864  469 HOH HOH B . 
F 3 HOH 165 865  409 HOH HOH B . 
F 3 HOH 166 866  244 HOH HOH B . 
F 3 HOH 167 867  549 HOH HOH B . 
F 3 HOH 168 868  262 HOH HOH B . 
F 3 HOH 169 869  360 HOH HOH B . 
F 3 HOH 170 870  267 HOH HOH B . 
F 3 HOH 171 871  345 HOH HOH B . 
F 3 HOH 172 872  418 HOH HOH B . 
F 3 HOH 173 873  53  HOH HOH B . 
F 3 HOH 174 874  126 HOH HOH B . 
F 3 HOH 175 875  102 HOH HOH B . 
F 3 HOH 176 876  117 HOH HOH B . 
F 3 HOH 177 877  93  HOH HOH B . 
F 3 HOH 178 878  11  HOH HOH B . 
F 3 HOH 179 879  143 HOH HOH B . 
F 3 HOH 180 880  109 HOH HOH B . 
F 3 HOH 181 881  235 HOH HOH B . 
F 3 HOH 182 882  295 HOH HOH B . 
F 3 HOH 183 883  151 HOH HOH B . 
F 3 HOH 184 884  298 HOH HOH B . 
F 3 HOH 185 885  462 HOH HOH B . 
F 3 HOH 186 886  38  HOH HOH B . 
F 3 HOH 187 887  89  HOH HOH B . 
F 3 HOH 188 888  427 HOH HOH B . 
F 3 HOH 189 889  444 HOH HOH B . 
F 3 HOH 190 890  440 HOH HOH B . 
F 3 HOH 191 891  165 HOH HOH B . 
F 3 HOH 192 892  123 HOH HOH B . 
F 3 HOH 193 893  420 HOH HOH B . 
F 3 HOH 194 894  171 HOH HOH B . 
F 3 HOH 195 895  245 HOH HOH B . 
F 3 HOH 196 896  129 HOH HOH B . 
F 3 HOH 197 897  395 HOH HOH B . 
F 3 HOH 198 898  291 HOH HOH B . 
F 3 HOH 199 899  376 HOH HOH B . 
F 3 HOH 200 900  441 HOH HOH B . 
F 3 HOH 201 901  555 HOH HOH B . 
F 3 HOH 202 902  451 HOH HOH B . 
F 3 HOH 203 903  344 HOH HOH B . 
F 3 HOH 204 904  294 HOH HOH B . 
F 3 HOH 205 905  137 HOH HOH B . 
F 3 HOH 206 906  386 HOH HOH B . 
F 3 HOH 207 907  204 HOH HOH B . 
F 3 HOH 208 908  134 HOH HOH B . 
F 3 HOH 209 909  368 HOH HOH B . 
F 3 HOH 210 910  473 HOH HOH B . 
F 3 HOH 211 911  307 HOH HOH B . 
F 3 HOH 212 912  33  HOH HOH B . 
F 3 HOH 213 913  251 HOH HOH B . 
F 3 HOH 214 914  486 HOH HOH B . 
F 3 HOH 215 915  380 HOH HOH B . 
F 3 HOH 216 916  95  HOH HOH B . 
F 3 HOH 217 917  535 HOH HOH B . 
F 3 HOH 218 918  220 HOH HOH B . 
F 3 HOH 219 919  531 HOH HOH B . 
F 3 HOH 220 920  269 HOH HOH B . 
F 3 HOH 221 921  498 HOH HOH B . 
F 3 HOH 222 922  375 HOH HOH B . 
F 3 HOH 223 923  354 HOH HOH B . 
F 3 HOH 224 924  159 HOH HOH B . 
F 3 HOH 225 925  511 HOH HOH B . 
F 3 HOH 226 926  250 HOH HOH B . 
F 3 HOH 227 927  202 HOH HOH B . 
F 3 HOH 228 928  305 HOH HOH B . 
F 3 HOH 229 929  119 HOH HOH B . 
F 3 HOH 230 930  548 HOH HOH B . 
F 3 HOH 231 931  124 HOH HOH B . 
F 3 HOH 232 932  412 HOH HOH B . 
F 3 HOH 233 933  520 HOH HOH B . 
F 3 HOH 234 934  260 HOH HOH B . 
F 3 HOH 235 935  411 HOH HOH B . 
F 3 HOH 236 936  180 HOH HOH B . 
F 3 HOH 237 937  34  HOH HOH B . 
F 3 HOH 238 938  113 HOH HOH B . 
F 3 HOH 239 939  378 HOH HOH B . 
F 3 HOH 240 940  507 HOH HOH B . 
F 3 HOH 241 941  564 HOH HOH B . 
F 3 HOH 242 942  356 HOH HOH B . 
F 3 HOH 243 943  114 HOH HOH B . 
F 3 HOH 244 944  424 HOH HOH B . 
F 3 HOH 245 945  508 HOH HOH B . 
F 3 HOH 246 946  341 HOH HOH B . 
F 3 HOH 247 947  367 HOH HOH B . 
F 3 HOH 248 948  527 HOH HOH B . 
F 3 HOH 249 949  500 HOH HOH B . 
F 3 HOH 250 950  562 HOH HOH B . 
F 3 HOH 251 951  275 HOH HOH B . 
F 3 HOH 252 952  463 HOH HOH B . 
F 3 HOH 253 953  192 HOH HOH B . 
F 3 HOH 254 954  355 HOH HOH B . 
F 3 HOH 255 955  214 HOH HOH B . 
F 3 HOH 256 956  158 HOH HOH B . 
F 3 HOH 257 957  485 HOH HOH B . 
F 3 HOH 258 958  414 HOH HOH B . 
F 3 HOH 259 959  30  HOH HOH B . 
F 3 HOH 260 960  316 HOH HOH B . 
F 3 HOH 261 961  352 HOH HOH B . 
F 3 HOH 262 962  364 HOH HOH B . 
F 3 HOH 263 963  556 HOH HOH B . 
F 3 HOH 264 964  494 HOH HOH B . 
F 3 HOH 265 965  346 HOH HOH B . 
F 3 HOH 266 966  489 HOH HOH B . 
F 3 HOH 267 967  26  HOH HOH B . 
F 3 HOH 268 968  361 HOH HOH B . 
F 3 HOH 269 969  370 HOH HOH B . 
F 3 HOH 270 970  282 HOH HOH B . 
F 3 HOH 271 971  343 HOH HOH B . 
F 3 HOH 272 972  373 HOH HOH B . 
F 3 HOH 273 973  394 HOH HOH B . 
F 3 HOH 274 974  280 HOH HOH B . 
F 3 HOH 275 975  540 HOH HOH B . 
F 3 HOH 276 976  266 HOH HOH B . 
F 3 HOH 277 977  550 HOH HOH B . 
F 3 HOH 278 978  270 HOH HOH B . 
F 3 HOH 279 979  331 HOH HOH B . 
F 3 HOH 280 980  499 HOH HOH B . 
F 3 HOH 281 981  284 HOH HOH B . 
F 3 HOH 282 982  541 HOH HOH B . 
F 3 HOH 283 983  276 HOH HOH B . 
F 3 HOH 284 984  342 HOH HOH B . 
F 3 HOH 285 985  206 HOH HOH B . 
F 3 HOH 286 986  551 HOH HOH B . 
F 3 HOH 287 987  362 HOH HOH B . 
F 3 HOH 288 988  447 HOH HOH B . 
F 3 HOH 289 989  296 HOH HOH B . 
F 3 HOH 290 990  402 HOH HOH B . 
F 3 HOH 291 991  256 HOH HOH B . 
F 3 HOH 292 992  78  HOH HOH B . 
F 3 HOH 293 993  464 HOH HOH B . 
F 3 HOH 294 994  313 HOH HOH B . 
F 3 HOH 295 995  163 HOH HOH B . 
F 3 HOH 296 996  450 HOH HOH B . 
F 3 HOH 297 997  383 HOH HOH B . 
F 3 HOH 298 998  52  HOH HOH B . 
F 3 HOH 299 999  404 HOH HOH B . 
F 3 HOH 300 1000 268 HOH HOH B . 
F 3 HOH 301 1001 363 HOH HOH B . 
F 3 HOH 302 1002 197 HOH HOH B . 
F 3 HOH 303 1003 503 HOH HOH B . 
F 3 HOH 304 1004 195 HOH HOH B . 
F 3 HOH 305 1005 445 HOH HOH B . 
F 3 HOH 306 1006 480 HOH HOH B . 
F 3 HOH 307 1007 455 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.8       2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 9.0.002     4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EDM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     94.190 
_cell.length_a_esd                 ? 
_cell.length_b                     96.890 
_cell.length_b_esd                 ? 
_cell.length_c                     65.790 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EDM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   9EDM 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.61 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES (pH 7.0), 30% v/v Jeffamine ED-2003' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-10-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95372 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95372 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX1 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          25.30 
_reflns.entry_id                                       9EDM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.98 
_reflns.d_resolution_low                               48.44 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     42579 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.57 
_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                                0.241 
_reflns.pdbx_Rpim_I_all                                0.071 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.229 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.98 
_reflns_shell.d_res_low                                     2.02 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           30735 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2810 
_reflns_shell.percent_possible_obs                          94.5 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               10.9 
_reflns_shell.pdbx_chi_squared                              0.54 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.1 
_reflns_shell.pdbx_Rrim_I_all                               1.877 
_reflns_shell.pdbx_Rpim_I_all                               0.554 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.540 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.791 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EDM 
_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                            1.98 
_refine.ls_d_res_low                             47.13 
_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                     42414 
_refine.ls_number_reflns_R_free                  2121 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.37 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1668 
_refine.ls_R_factor_R_free                       0.2095 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1645 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.67 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.98 
_refine_hist.d_res_low                        47.13 
_refine_hist.number_atoms_solvent             557 
_refine_hist.number_atoms_total               5249 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4690 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 4864 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.830  ? 6640 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.051 ? 1769 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 715  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 896  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.98 2.03  . . 137 2592 98.00  . . . . 0.2543 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 2.03 2.08  . . 139 2634 99.00  . . . . 0.2331 . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 2.08 2.13  . . 139 2652 99.00  . . . . 0.2189 . . . . . . . . . . . 0.2625 
'X-RAY DIFFRACTION' 2.13 2.20  . . 140 2647 99.00  . . . . 0.2130 . . . . . . . . . . . 0.2520 
'X-RAY DIFFRACTION' 2.20 2.27  . . 138 2628 99.00  . . . . 0.2083 . . . . . . . . . . . 0.2820 
'X-RAY DIFFRACTION' 2.27 2.35  . . 141 2678 99.00  . . . . 0.1880 . . . . . . . . . . . 0.2230 
'X-RAY DIFFRACTION' 2.35 2.44  . . 139 2651 99.00  . . . . 0.1898 . . . . . . . . . . . 0.2423 
'X-RAY DIFFRACTION' 2.44 2.55  . . 141 2677 99.00  . . . . 0.1798 . . . . . . . . . . . 0.2496 
'X-RAY DIFFRACTION' 2.55 2.69  . . 140 2662 100.00 . . . . 0.1777 . . . . . . . . . . . 0.2488 
'X-RAY DIFFRACTION' 2.69 2.85  . . 142 2687 100.00 . . . . 0.1821 . . . . . . . . . . . 0.2474 
'X-RAY DIFFRACTION' 2.85 3.08  . . 141 2682 100.00 . . . . 0.1707 . . . . . . . . . . . 0.2447 
'X-RAY DIFFRACTION' 3.08 3.38  . . 142 2706 100.00 . . . . 0.1569 . . . . . . . . . . . 0.2281 
'X-RAY DIFFRACTION' 3.38 3.87  . . 145 2745 100.00 . . . . 0.1366 . . . . . . . . . . . 0.1700 
'X-RAY DIFFRACTION' 3.87 4.88  . . 145 2758 100.00 . . . . 0.1175 . . . . . . . . . . . 0.1461 
'X-RAY DIFFRACTION' 4.88 47.13 . . 152 2894 100.00 . . . . 0.1410 . . . . . . . . . . . 0.1608 
# 
_struct.entry_id                     9EDM 
_struct.title                        'GII.9-VA97207 norovirus protruding domain' 
_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        9EDM 
_struct_keywords.text            'norovirus, P domain, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q91H09_9CALI 
_struct_ref.pdbx_db_accession          Q91H09 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KAFTIPVLKISEMTNSRFPVPVDQMYTSRSEGIVVQPQNGRATIDGELLGTTLVSPVSVCNFKGNLQAEVPGQHQLYQLQ
LTNLDGSPIDPTDDTPGPLGCPDFTGLLYGVASQRGPGDATRAHEARIDTGSDTFAPKIGQVRFYSTSSDFETNQPTHFT
PIGIYIEGNSSDFNQWQLPRYGGHLANNNHLAPAVSPLFPGEQILFFRSFIPGASGHTNGEMDCLLPQEFVQHFYQEAAT
ARSEVALLRFVNPDTGRALFESKLHKQGFMTIASSGDHPIIMPTNGYFRFEAWVNQFYSLAPV
;
_struct_ref.pdbx_align_begin           225 
# 
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 9EDM A 1 ? 303 ? Q91H09 225 ? 527 ? 225 527 
2 1 9EDM B 1 ? 303 ? Q91H09 225 ? 527 ? 225 527 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3430  ? 
1 MORE         -26   ? 
1 'SSA (A^2)'  23520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 LYS A 9   ? MET A 13  ? LYS A 233 MET A 237 5 ? 5  
HELX_P HELX_P2 AA2 ALA A 136 ? ILE A 139 ? ALA A 360 ILE A 363 5 ? 4  
HELX_P HELX_P3 AA3 PRO A 227 ? ALA A 238 ? PRO A 451 ALA A 462 1 ? 12 
HELX_P HELX_P4 AA4 LYS B 9   ? MET B 13  ? LYS B 233 MET B 237 5 ? 5  
HELX_P HELX_P5 AA5 ALA B 136 ? ILE B 139 ? ALA B 360 ILE B 363 5 ? 4  
HELX_P HELX_P6 AA6 PRO B 227 ? ALA B 238 ? PRO B 451 ALA B 462 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 116 A . ? GLY 340 A PRO 117 A ? PRO 341 A 1 -4.58 
2 GLY 116 B . ? GLY 340 B PRO 117 B ? PRO 341 B 1 -3.46 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 221 ? CYS A 224 ? GLU A 445 CYS A 448 
AA1 2 GLU A 202 ? PHE A 210 ? GLU A 426 PHE A 434 
AA1 3 GLN A 24  ? SER A 28  ? GLN A 248 SER A 252 
AA1 4 HIS A 278 ? ILE A 280 ? HIS A 502 ILE A 504 
AA2 1 GLU A 221 ? CYS A 224 ? GLU A 445 CYS A 448 
AA2 2 GLU A 202 ? PHE A 210 ? GLU A 426 PHE A 434 
AA2 3 PHE A 269 ? ALA A 273 ? PHE A 493 ALA A 497 
AA2 4 ALA A 258 ? HIS A 265 ? ALA A 482 HIS A 489 
AA2 5 VAL A 245 ? VAL A 251 ? VAL A 469 VAL A 475 
AA2 6 TYR A 287 ? VAL A 294 ? TYR A 511 VAL A 518 
AA3 1 GLY A 213 ? SER A 215 ? GLY A 437 SER A 439 
AA3 2 PRO A 156 ? TYR A 165 ? PRO A 380 TYR A 389 
AA3 3 LEU A 107 ? ARG A 115 ? LEU A 331 ARG A 339 
AA3 4 THR A 121 ? ASP A 129 ? THR A 345 ASP A 353 
AA3 5 GLN A 141 ? TYR A 145 ? GLN A 365 TYR A 369 
AA3 6 LEU A 76  ? THR A 82  ? LEU A 300 THR A 306 
AA3 7 PHE A 62  ? GLU A 69  ? PHE A 286 GLU A 293 
AA3 8 PRO A 156 ? TYR A 165 ? PRO A 380 TYR A 389 
AA4 1 GLU B 221 ? CYS B 224 ? GLU B 445 CYS B 448 
AA4 2 GLU B 202 ? PHE B 210 ? GLU B 426 PHE B 434 
AA4 3 GLN B 24  ? THR B 27  ? GLN B 248 THR B 251 
AA4 4 HIS B 278 ? ILE B 280 ? HIS B 502 ILE B 504 
AA5 1 GLU B 221 ? CYS B 224 ? GLU B 445 CYS B 448 
AA5 2 GLU B 202 ? PHE B 210 ? GLU B 426 PHE B 434 
AA5 3 PHE B 269 ? ALA B 273 ? PHE B 493 ALA B 497 
AA5 4 ALA B 258 ? HIS B 265 ? ALA B 482 HIS B 489 
AA5 5 VAL B 245 ? VAL B 251 ? VAL B 469 VAL B 475 
AA5 6 TYR B 287 ? VAL B 294 ? TYR B 511 VAL B 518 
AA6 1 GLY B 213 ? SER B 215 ? GLY B 437 SER B 439 
AA6 2 PRO B 156 ? TYR B 165 ? PRO B 380 TYR B 389 
AA6 3 LEU B 107 ? ARG B 115 ? LEU B 331 ARG B 339 
AA6 4 THR B 121 ? ASP B 129 ? THR B 345 ASP B 353 
AA6 5 GLN B 141 ? TYR B 145 ? GLN B 365 TYR B 369 
AA6 6 LEU B 76  ? THR B 82  ? LEU B 300 THR B 306 
AA6 7 PHE B 62  ? GLU B 69  ? PHE B 286 GLU B 293 
AA6 8 PRO B 156 ? TYR B 165 ? PRO B 380 TYR B 389 
# 
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 O CYS A 224 ? O CYS A 448 N PHE A 207 ? N PHE A 431 
AA1 2 3 O PHE A 206 ? O PHE A 430 N TYR A 26  ? N TYR A 250 
AA1 3 4 N THR A 27  ? N THR A 251 O HIS A 278 ? O HIS A 502 
AA2 1 2 O CYS A 224 ? O CYS A 448 N PHE A 207 ? N PHE A 431 
AA2 2 3 N GLN A 203 ? N GLN A 427 O ILE A 272 ? O ILE A 496 
AA2 3 4 O PHE A 269 ? O PHE A 493 N HIS A 265 ? N HIS A 489 
AA2 4 5 O LEU A 259 ? O LEU A 483 N PHE A 250 ? N PHE A 474 
AA2 5 6 N LEU A 247 ? N LEU A 471 O ALA A 292 ? O ALA A 516 
AA3 1 2 O ALA A 214 ? O ALA A 438 N ILE A 164 ? N ILE A 388 
AA3 2 3 O GLY A 163 ? O GLY A 387 N TYR A 109 ? N TYR A 333 
AA3 3 4 N GLY A 110 ? N GLY A 334 O ALA A 126 ? O ALA A 350 
AA3 4 5 N ARG A 127 ? N ARG A 351 O TYR A 145 ? O TYR A 369 
AA3 5 6 O VAL A 142 ? O VAL A 366 N LEU A 79  ? N LEU A 303 
AA3 6 7 O GLN A 78  ? O GLN A 302 N ALA A 68  ? N ALA A 292 
AA3 7 8 N PHE A 62  ? N PHE A 286 O PHE A 159 ? O PHE A 383 
AA4 1 2 O CYS B 224 ? O CYS B 448 N PHE B 207 ? N PHE B 431 
AA4 2 3 O PHE B 206 ? O PHE B 430 N TYR B 26  ? N TYR B 250 
AA4 3 4 N THR B 27  ? N THR B 251 O HIS B 278 ? O HIS B 502 
AA5 1 2 O CYS B 224 ? O CYS B 448 N PHE B 207 ? N PHE B 431 
AA5 2 3 N LEU B 205 ? N LEU B 429 O MET B 270 ? O MET B 494 
AA5 3 4 O PHE B 269 ? O PHE B 493 N HIS B 265 ? N HIS B 489 
AA5 4 5 O LEU B 259 ? O LEU B 483 N PHE B 250 ? N PHE B 474 
AA5 5 6 N LEU B 247 ? N LEU B 471 O ALA B 292 ? O ALA B 516 
AA6 1 2 O ALA B 214 ? O ALA B 438 N ILE B 164 ? N ILE B 388 
AA6 2 3 O GLY B 163 ? O GLY B 387 N TYR B 109 ? N TYR B 333 
AA6 3 4 N LEU B 108 ? N LEU B 332 O ILE B 128 ? O ILE B 352 
AA6 4 5 N ARG B 127 ? N ARG B 351 O TYR B 145 ? O TYR B 369 
AA6 5 6 O VAL B 142 ? O VAL B 366 N LEU B 79  ? N LEU B 303 
AA6 6 7 O GLN B 78  ? O GLN B 302 N ALA B 68  ? N ALA B 292 
AA6 7 8 N PHE B 62  ? N PHE B 286 O PHE B 159 ? O PHE B 383 
# 
_pdbx_entry_details.entry_id                   9EDM 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN A 260 ? ? -141.78 55.22  
2 1 ASP A 318 ? ? -86.82  47.07  
3 1 HIS A 408 ? ? -21.73  -59.54 
4 1 GLN B 260 ? ? -143.50 53.34  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -15.9054 
_pdbx_refine_tls.origin_y         25.9249 
_pdbx_refine_tls.origin_z         -15.5366 
_pdbx_refine_tls.T[1][1]          0.1860 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0025 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0072 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1928 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0014 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1743 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.4597 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2058 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0180 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7523 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0947 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.4174 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0396 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0271 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0114 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0859 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0468 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0140 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0282 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0055 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0067 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 1006 ? 6.09 . 
2 1 O ? B HOH 1007 ? 6.15 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     LYS 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      225 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    LYS 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8V95 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EDM 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.010617 
_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]   0.010321 
_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]   0.015200 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A ALA A 1 2   ? -14.241 50.315 -29.861 0.49 57.45 ? 226  ALA A N   1 
ATOM   2    N  N   B ALA A 1 2   ? -14.219 50.306 -29.869 0.51 57.45 ? 226  ALA A N   1 
ATOM   3    C  CA  A ALA A 1 2   ? -14.016 50.476 -28.429 0.49 55.54 ? 226  ALA A CA  1 
ATOM   4    C  CA  B ALA A 1 2   ? -14.010 50.465 -28.433 0.51 55.54 ? 226  ALA A CA  1 
ATOM   5    C  C   A ALA A 1 2   ? -14.739 49.403 -27.618 0.49 57.07 ? 226  ALA A C   1 
ATOM   6    C  C   B ALA A 1 2   ? -14.736 49.388 -27.632 0.51 57.08 ? 226  ALA A C   1 
ATOM   7    O  O   A ALA A 1 2   ? -14.107 48.670 -26.855 0.49 58.01 ? 226  ALA A O   1 
ATOM   8    O  O   B ALA A 1 2   ? -14.102 48.637 -26.887 0.51 58.02 ? 226  ALA A O   1 
ATOM   9    C  CB  A ALA A 1 2   ? -14.452 51.862 -27.975 0.49 55.11 ? 226  ALA A CB  1 
ATOM   10   C  CB  B ALA A 1 2   ? -14.457 51.848 -27.982 0.51 55.11 ? 226  ALA A CB  1 
ATOM   11   N  N   . PHE A 1 3   ? -16.060 49.308 -27.775 1.00 47.48 ? 227  PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -16.862 48.372 -26.994 1.00 40.09 ? 227  PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -17.264 47.168 -27.838 1.00 34.31 ? 227  PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -17.858 47.318 -28.913 1.00 27.63 ? 227  PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -18.108 49.031 -26.398 1.00 30.18 ? 227  PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -18.739 48.209 -25.315 1.00 30.06 ? 227  PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -18.235 48.246 -24.027 1.00 26.74 ? 227  PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -19.790 47.349 -25.595 1.00 27.44 ? 227  PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -18.784 47.461 -23.026 1.00 24.32 ? 227  PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -20.346 46.566 -24.598 1.00 25.99 ? 227  PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -19.833 46.618 -23.310 1.00 22.40 ? 227  PHE A CZ  1 
ATOM   22   N  N   . THR A 1 4   ? -16.951 45.978 -27.340 1.00 28.85 ? 228  THR A N   1 
ATOM   23   C  CA  . THR A 1 4   ? -17.290 44.740 -28.022 1.00 27.01 ? 228  THR A CA  1 
ATOM   24   C  C   . THR A 1 4   ? -17.909 43.753 -27.050 1.00 25.17 ? 228  THR A C   1 
ATOM   25   O  O   . THR A 1 4   ? -17.726 43.838 -25.831 1.00 20.92 ? 228  THR A O   1 
ATOM   26   C  CB  . THR A 1 4   ? -16.073 44.081 -28.667 1.00 32.11 ? 228  THR A CB  1 
ATOM   27   O  OG1 . THR A 1 4   ? -15.052 43.914 -27.674 1.00 31.29 ? 228  THR A OG1 1 
ATOM   28   C  CG2 . THR A 1 4   ? -15.549 44.946 -29.822 1.00 31.74 ? 228  THR A CG2 1 
ATOM   29   N  N   . ILE A 1 5   ? -18.648 42.823 -27.636 1.00 25.74 ? 229  ILE A N   1 
ATOM   30   C  CA  . ILE A 1 5   ? -19.240 41.672 -26.958 1.00 24.86 ? 229  ILE A CA  1 
ATOM   31   C  C   . ILE A 1 5   ? -18.538 40.432 -27.493 1.00 24.07 ? 229  ILE A C   1 
ATOM   32   O  O   . ILE A 1 5   ? -18.378 40.309 -28.709 1.00 23.43 ? 229  ILE A O   1 
ATOM   33   C  CB  . ILE A 1 5   ? -20.760 41.581 -27.222 1.00 21.03 ? 229  ILE A CB  1 
ATOM   34   C  CG1 . ILE A 1 5   ? -21.483 42.815 -26.687 1.00 25.44 ? 229  ILE A CG1 1 
ATOM   35   C  CG2 . ILE A 1 5   ? -21.335 40.326 -26.602 1.00 29.91 ? 229  ILE A CG2 1 
ATOM   36   C  CD1 . ILE A 1 5   ? -21.163 43.119 -25.234 1.00 27.15 ? 229  ILE A CD1 1 
ATOM   37   N  N   . PRO A 1 6   ? -18.106 39.502 -26.648 1.00 24.79 ? 230  PRO A N   1 
ATOM   38   C  CA  . PRO A 1 6   ? -17.557 38.246 -27.174 1.00 24.69 ? 230  PRO A CA  1 
ATOM   39   C  C   . PRO A 1 6   ? -18.591 37.504 -28.017 1.00 21.71 ? 230  PRO A C   1 
ATOM   40   O  O   . PRO A 1 6   ? -19.790 37.525 -27.728 1.00 24.05 ? 230  PRO A O   1 
ATOM   41   C  CB  . PRO A 1 6   ? -17.173 37.467 -25.907 1.00 24.01 ? 230  PRO A CB  1 
ATOM   42   C  CG  . PRO A 1 6   ? -17.964 38.103 -24.806 1.00 25.75 ? 230  PRO A CG  1 
ATOM   43   C  CD  . PRO A 1 6   ? -18.060 39.548 -25.181 1.00 26.60 ? 230  PRO A CD  1 
ATOM   44   N  N   . VAL A 1 7   ? -18.116 36.871 -29.089 1.00 19.14 ? 231  VAL A N   1 
ATOM   45   C  CA  . VAL A 1 7   ? -18.971 36.199 -30.063 1.00 19.78 ? 231  VAL A CA  1 
ATOM   46   C  C   . VAL A 1 7   ? -19.179 34.769 -29.571 1.00 20.92 ? 231  VAL A C   1 
ATOM   47   O  O   . VAL A 1 7   ? -18.281 33.936 -29.673 1.00 19.66 ? 231  VAL A O   1 
ATOM   48   C  CB  . VAL A 1 7   ? -18.356 36.231 -31.465 1.00 27.02 ? 231  VAL A CB  1 
ATOM   49   C  CG1 . VAL A 1 7   ? -19.181 35.362 -32.440 1.00 25.99 ? 231  VAL A CG1 1 
ATOM   50   C  CG2 . VAL A 1 7   ? -18.225 37.686 -31.980 1.00 23.55 ? 231  VAL A CG2 1 
ATOM   51   N  N   . LEU A 1 8   ? -20.368 34.484 -29.035 1.00 19.89 ? 232  LEU A N   1 
ATOM   52   C  CA  . LEU A 1 8   ? -20.635 33.210 -28.366 1.00 21.66 ? 232  LEU A CA  1 
ATOM   53   C  C   . LEU A 1 8   ? -22.058 32.736 -28.619 1.00 23.11 ? 232  LEU A C   1 
ATOM   54   O  O   . LEU A 1 8   ? -23.007 33.498 -28.425 1.00 22.30 ? 232  LEU A O   1 
ATOM   55   C  CB  . LEU A 1 8   ? -20.442 33.333 -26.852 1.00 22.78 ? 232  LEU A CB  1 
ATOM   56   C  CG  . LEU A 1 8   ? -19.038 33.618 -26.355 1.00 24.02 ? 232  LEU A CG  1 
ATOM   57   C  CD1 . LEU A 1 8   ? -19.134 33.954 -24.907 1.00 23.69 ? 232  LEU A CD1 1 
ATOM   58   C  CD2 . LEU A 1 8   ? -18.180 32.375 -26.591 1.00 22.67 ? 232  LEU A CD2 1 
ATOM   59   N  N   . LYS A 1 9   ? -22.212 31.466 -28.988 1.00 23.72 ? 233  LYS A N   1 
ATOM   60   C  CA  . LYS A 1 9   ? -23.543 30.871 -28.992 1.00 22.64 ? 233  LYS A CA  1 
ATOM   61   C  C   . LYS A 1 9   ? -24.045 30.710 -27.562 1.00 21.57 ? 233  LYS A C   1 
ATOM   62   O  O   . LYS A 1 9   ? -23.274 30.731 -26.605 1.00 19.60 ? 233  LYS A O   1 
ATOM   63   C  CB  . LYS A 1 9   ? -23.531 29.514 -29.682 1.00 23.98 ? 233  LYS A CB  1 
ATOM   64   C  CG  . LYS A 1 9   ? -23.061 29.542 -31.118 1.00 27.12 ? 233  LYS A CG  1 
ATOM   65   C  CD  . LYS A 1 9   ? -22.687 28.137 -31.557 1.00 31.95 ? 233  LYS A CD  1 
ATOM   66   C  CE  . LYS A 1 9   ? -21.878 28.149 -32.850 1.00 36.92 ? 233  LYS A CE  1 
ATOM   67   N  NZ  . LYS A 1 9   ? -21.391 26.765 -33.156 1.00 40.34 ? 233  LYS A NZ  1 
ATOM   68   N  N   . ILE A 1 10  ? -25.361 30.538 -27.419 1.00 20.89 ? 234  ILE A N   1 
ATOM   69   C  CA  . ILE A 1 10  ? -25.928 30.332 -26.086 1.00 21.13 ? 234  ILE A CA  1 
ATOM   70   C  C   . ILE A 1 10  ? -25.296 29.111 -25.417 1.00 21.88 ? 234  ILE A C   1 
ATOM   71   O  O   . ILE A 1 10  ? -24.915 29.157 -24.241 1.00 20.15 ? 234  ILE A O   1 
ATOM   72   C  CB  . ILE A 1 10  ? -27.464 30.213 -26.173 1.00 17.89 ? 234  ILE A CB  1 
ATOM   73   C  CG1 . ILE A 1 10  ? -28.085 31.543 -26.640 1.00 21.76 ? 234  ILE A CG1 1 
ATOM   74   C  CG2 . ILE A 1 10  ? -28.049 29.750 -24.845 1.00 25.47 ? 234  ILE A CG2 1 
ATOM   75   C  CD1 . ILE A 1 10  ? -27.779 32.723 -25.754 1.00 23.83 ? 234  ILE A CD1 1 
ATOM   76   N  N   . SER A 1 11  ? -25.123 28.021 -26.170 1.00 21.62 ? 235  SER A N   1 
ATOM   77   C  CA  . SER A 1 11  ? -24.550 26.789 -25.625 1.00 22.55 ? 235  SER A CA  1 
ATOM   78   C  C   . SER A 1 11  ? -23.066 26.900 -25.287 1.00 26.56 ? 235  SER A C   1 
ATOM   79   O  O   . SER A 1 11  ? -22.527 25.980 -24.664 1.00 28.82 ? 235  SER A O   1 
ATOM   80   C  CB  . SER A 1 11  ? -24.738 25.631 -26.612 1.00 23.18 ? 235  SER A CB  1 
ATOM   81   O  OG  . SER A 1 11  ? -24.049 25.889 -27.833 1.00 25.88 ? 235  SER A OG  1 
ATOM   82   N  N   . GLU A 1 12  ? -22.384 27.965 -25.702 1.00 21.17 ? 236  GLU A N   1 
ATOM   83   C  CA  . GLU A 1 12  ? -20.994 28.180 -25.326 1.00 22.46 ? 236  GLU A CA  1 
ATOM   84   C  C   . GLU A 1 12  ? -20.848 29.097 -24.121 1.00 23.19 ? 236  GLU A C   1 
ATOM   85   O  O   . GLU A 1 12  ? -19.723 29.378 -23.706 1.00 22.98 ? 236  GLU A O   1 
ATOM   86   C  CB  . GLU A 1 12  ? -20.213 28.772 -26.503 1.00 22.19 ? 236  GLU A CB  1 
ATOM   87   C  CG  . GLU A 1 12  ? -20.356 27.969 -27.763 1.00 28.13 ? 236  GLU A CG  1 
ATOM   88   C  CD  . GLU A 1 12  ? -19.786 28.669 -28.979 1.00 28.95 ? 236  GLU A CD  1 
ATOM   89   O  OE1 . GLU A 1 12  ? -19.996 29.886 -29.136 1.00 30.68 ? 236  GLU A OE1 1 
ATOM   90   O  OE2 . GLU A 1 12  ? -19.128 27.989 -29.783 1.00 35.37 ? 236  GLU A OE2 1 
ATOM   91   N  N   . MET A 1 13  ? -21.950 29.594 -23.575 1.00 24.66 ? 237  MET A N   1 
ATOM   92   C  CA  . MET A 1 13  ? -21.884 30.512 -22.452 1.00 20.61 ? 237  MET A CA  1 
ATOM   93   C  C   . MET A 1 13  ? -21.924 29.724 -21.158 1.00 19.25 ? 237  MET A C   1 
ATOM   94   O  O   . MET A 1 13  ? -22.501 28.633 -21.090 1.00 17.27 ? 237  MET A O   1 
ATOM   95   C  CB  . MET A 1 13  ? -23.043 31.511 -22.478 1.00 17.24 ? 237  MET A CB  1 
ATOM   96   C  CG  . MET A 1 13  ? -23.118 32.368 -23.712 1.00 19.58 ? 237  MET A CG  1 
ATOM   97   S  SD  . MET A 1 13  ? -24.624 33.384 -23.646 1.00 21.64 ? 237  MET A SD  1 
ATOM   98   C  CE  . MET A 1 13  ? -24.243 34.581 -24.901 1.00 18.21 ? 237  MET A CE  1 
ATOM   99   N  N   . THR A 1 14  ? -21.311 30.298 -20.128 1.00 17.31 ? 238  THR A N   1 
ATOM   100  C  CA  . THR A 1 14  ? -21.258 29.717 -18.800 1.00 19.17 ? 238  THR A CA  1 
ATOM   101  C  C   . THR A 1 14  ? -22.164 30.515 -17.882 1.00 19.32 ? 238  THR A C   1 
ATOM   102  O  O   . THR A 1 14  ? -22.118 31.750 -17.883 1.00 16.61 ? 238  THR A O   1 
ATOM   103  C  CB  . THR A 1 14  ? -19.829 29.737 -18.249 1.00 17.99 ? 238  THR A CB  1 
ATOM   104  O  OG1 . THR A 1 14  ? -18.947 29.154 -19.213 1.00 20.58 ? 238  THR A OG1 1 
ATOM   105  C  CG2 . THR A 1 14  ? -19.740 28.966 -16.959 1.00 18.44 ? 238  THR A CG2 1 
ATOM   106  N  N   . ASN A 1 15  ? -22.966 29.815 -17.092 1.00 19.38 ? 239  ASN A N   1 
ATOM   107  C  CA  . ASN A 1 15  ? -23.729 30.489 -16.060 1.00 20.64 ? 239  ASN A CA  1 
ATOM   108  C  C   . ASN A 1 15  ? -22.779 31.116 -15.045 1.00 22.28 ? 239  ASN A C   1 
ATOM   109  O  O   . ASN A 1 15  ? -21.827 30.477 -14.584 1.00 17.42 ? 239  ASN A O   1 
ATOM   110  C  CB  . ASN A 1 15  ? -24.662 29.510 -15.366 1.00 16.52 ? 239  ASN A CB  1 
ATOM   111  C  CG  . ASN A 1 15  ? -25.807 30.206 -14.682 1.00 16.90 ? 239  ASN A CG  1 
ATOM   112  O  OD1 . ASN A 1 15  ? -25.612 30.962 -13.718 1.00 19.16 ? 239  ASN A OD1 1 
ATOM   113  N  ND2 . ASN A 1 15  ? -27.022 29.965 -15.178 1.00 15.74 ? 239  ASN A ND2 1 
ATOM   114  N  N   . SER A 1 16  ? -23.045 32.370 -14.697 1.00 20.40 ? 240  SER A N   1 
ATOM   115  C  CA  . SER A 1 16  ? -22.195 33.063 -13.744 1.00 17.34 ? 240  SER A CA  1 
ATOM   116  C  C   . SER A 1 16  ? -22.580 32.787 -12.304 1.00 18.60 ? 240  SER A C   1 
ATOM   117  O  O   . SER A 1 16  ? -21.824 33.165 -11.401 1.00 20.44 ? 240  SER A O   1 
ATOM   118  C  CB  . SER A 1 16  ? -22.232 34.568 -14.013 1.00 19.97 ? 240  SER A CB  1 
ATOM   119  O  OG  . SER A 1 16  ? -23.573 35.027 -13.982 1.00 20.03 ? 240  SER A OG  1 
ATOM   120  N  N   . ARG A 1 17  ? -23.722 32.137 -12.061 1.00 15.65 ? 241  ARG A N   1 
ATOM   121  C  CA  . ARG A 1 17  ? -24.134 31.819 -10.700 1.00 18.17 ? 241  ARG A CA  1 
ATOM   122  C  C   . ARG A 1 17  ? -23.939 30.351 -10.332 1.00 18.55 ? 241  ARG A C   1 
ATOM   123  O  O   . ARG A 1 17  ? -24.138 29.989 -9.173  1.00 19.80 ? 241  ARG A O   1 
ATOM   124  C  CB  . ARG A 1 17  ? -25.598 32.231 -10.491 1.00 18.36 ? 241  ARG A CB  1 
ATOM   125  C  CG  . ARG A 1 17  ? -25.795 33.766 -10.690 1.00 17.59 ? 241  ARG A CG  1 
ATOM   126  C  CD  . ARG A 1 17  ? -27.236 34.176 -10.516 1.00 17.46 ? 241  ARG A CD  1 
ATOM   127  N  NE  . ARG A 1 17  ? -27.696 33.827 -9.183  1.00 18.42 ? 241  ARG A NE  1 
ATOM   128  C  CZ  . ARG A 1 17  ? -28.912 33.393 -8.901  1.00 20.11 ? 241  ARG A CZ  1 
ATOM   129  N  NH1 . ARG A 1 17  ? -29.833 33.267 -9.842  1.00 20.76 ? 241  ARG A NH1 1 
ATOM   130  N  NH2 . ARG A 1 17  ? -29.207 33.066 -7.648  1.00 19.31 ? 241  ARG A NH2 1 
ATOM   131  N  N   . PHE A 1 18  ? -23.524 29.506 -11.275 1.00 19.50 ? 242  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 18  ? -23.310 28.094 -10.999 1.00 16.09 ? 242  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 18  ? -22.458 27.560 -12.129 1.00 18.26 ? 242  PHE A C   1 
ATOM   134  O  O   . PHE A 1 18  ? -22.728 27.894 -13.291 1.00 19.12 ? 242  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 18  ? -24.634 27.326 -10.915 1.00 15.96 ? 242  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 18  ? -24.553 26.047 -10.129 1.00 19.84 ? 242  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 18  ? -24.603 26.064 -8.753  1.00 19.33 ? 242  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 18  ? -24.471 24.826 -10.778 1.00 17.73 ? 242  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 18  ? -24.541 24.887 -8.024  1.00 18.35 ? 242  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 18  ? -24.395 23.643 -10.055 1.00 19.35 ? 242  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 18  ? -24.443 23.685 -8.668  1.00 19.10 ? 242  PHE A CZ  1 
ATOM   142  N  N   . PRO A 1 19  ? -21.454 26.732 -11.850 1.00 18.70 ? 243  PRO A N   1 
ATOM   143  C  CA  . PRO A 1 19  ? -20.452 26.429 -12.892 1.00 17.35 ? 243  PRO A CA  1 
ATOM   144  C  C   . PRO A 1 19  ? -20.926 25.375 -13.887 1.00 18.87 ? 243  PRO A C   1 
ATOM   145  O  O   . PRO A 1 19  ? -20.383 24.261 -13.998 1.00 18.55 ? 243  PRO A O   1 
ATOM   146  C  CB  . PRO A 1 19  ? -19.250 25.971 -12.059 1.00 16.27 ? 243  PRO A CB  1 
ATOM   147  C  CG  . PRO A 1 19  ? -19.882 25.322 -10.852 1.00 18.84 ? 243  PRO A CG  1 
ATOM   148  C  CD  . PRO A 1 19  ? -21.109 26.134 -10.550 1.00 15.60 ? 243  PRO A CD  1 
ATOM   149  N  N   . VAL A 1 20  ? -21.958 25.731 -14.647 1.00 15.37 ? 244  VAL A N   1 
ATOM   150  C  CA  . VAL A 1 20  ? -22.493 24.888 -15.714 1.00 17.85 ? 244  VAL A CA  1 
ATOM   151  C  C   . VAL A 1 20  ? -22.786 25.765 -16.922 1.00 19.27 ? 244  VAL A C   1 
ATOM   152  O  O   . VAL A 1 20  ? -22.884 26.996 -16.809 1.00 20.38 ? 244  VAL A O   1 
ATOM   153  C  CB  . VAL A 1 20  ? -23.770 24.136 -15.280 1.00 20.77 ? 244  VAL A CB  1 
ATOM   154  C  CG1 . VAL A 1 20  ? -23.489 23.181 -14.112 1.00 16.02 ? 244  VAL A CG1 1 
ATOM   155  C  CG2 . VAL A 1 20  ? -24.890 25.127 -14.926 1.00 16.30 ? 244  VAL A CG2 1 
ATOM   156  N  N   . PRO A 1 21  ? -22.901 25.163 -18.099 1.00 17.46 ? 245  PRO A N   1 
ATOM   157  C  CA  . PRO A 1 21  ? -23.231 25.950 -19.291 1.00 18.31 ? 245  PRO A CA  1 
ATOM   158  C  C   . PRO A 1 21  ? -24.641 26.515 -19.212 1.00 18.50 ? 245  PRO A C   1 
ATOM   159  O  O   . PRO A 1 21  ? -25.518 25.985 -18.525 1.00 15.61 ? 245  PRO A O   1 
ATOM   160  C  CB  . PRO A 1 21  ? -23.105 24.933 -20.433 1.00 21.46 ? 245  PRO A CB  1 
ATOM   161  C  CG  . PRO A 1 21  ? -22.178 23.865 -19.886 1.00 17.93 ? 245  PRO A CG  1 
ATOM   162  C  CD  . PRO A 1 21  ? -22.590 23.758 -18.446 1.00 17.46 ? 245  PRO A CD  1 
ATOM   163  N  N   . VAL A 1 22  ? -24.850 27.607 -19.947 1.00 15.56 ? 246  VAL A N   1 
ATOM   164  C  CA  . VAL A 1 22  ? -26.180 28.186 -20.092 1.00 17.76 ? 246  VAL A CA  1 
ATOM   165  C  C   . VAL A 1 22  ? -27.024 27.274 -20.960 1.00 17.98 ? 246  VAL A C   1 
ATOM   166  O  O   . VAL A 1 22  ? -26.552 26.757 -21.979 1.00 18.76 ? 246  VAL A O   1 
ATOM   167  C  CB  . VAL A 1 22  ? -26.093 29.597 -20.705 1.00 21.03 ? 246  VAL A CB  1 
ATOM   168  C  CG1 . VAL A 1 22  ? -27.484 30.104 -21.101 1.00 15.58 ? 246  VAL A CG1 1 
ATOM   169  C  CG2 . VAL A 1 22  ? -25.404 30.565 -19.723 1.00 15.19 ? 246  VAL A CG2 1 
ATOM   170  N  N   . ASP A 1 23  ? -28.281 27.068 -20.565 1.00 18.21 ? 247  ASP A N   1 
ATOM   171  C  CA  . ASP A 1 23  ? -29.169 26.245 -21.376 1.00 19.32 ? 247  ASP A CA  1 
ATOM   172  C  C   . ASP A 1 23  ? -30.055 27.063 -22.313 1.00 22.15 ? 247  ASP A C   1 
ATOM   173  O  O   . ASP A 1 23  ? -30.296 26.638 -23.443 1.00 20.91 ? 247  ASP A O   1 
ATOM   174  C  CB  . ASP A 1 23  ? -30.041 25.360 -20.478 1.00 18.92 ? 247  ASP A CB  1 
ATOM   175  C  CG  . ASP A 1 23  ? -29.242 24.210 -19.840 1.00 26.22 ? 247  ASP A CG  1 
ATOM   176  O  OD1 . ASP A 1 23  ? -28.664 23.396 -20.599 1.00 26.85 ? 247  ASP A OD1 1 
ATOM   177  O  OD2 . ASP A 1 23  ? -29.156 24.141 -18.589 1.00 21.32 ? 247  ASP A OD2 1 
ATOM   178  N  N   . GLN A 1 24  ? -30.542 28.229 -21.887 1.00 18.21 ? 248  GLN A N   1 
ATOM   179  C  CA  . GLN A 1 24  ? -31.446 29.003 -22.729 1.00 19.15 ? 248  GLN A CA  1 
ATOM   180  C  C   . GLN A 1 24  ? -31.494 30.434 -22.220 1.00 17.76 ? 248  GLN A C   1 
ATOM   181  O  O   . GLN A 1 24  ? -31.220 30.704 -21.050 1.00 18.60 ? 248  GLN A O   1 
ATOM   182  C  CB  . GLN A 1 24  ? -32.866 28.398 -22.740 1.00 19.43 ? 248  GLN A CB  1 
ATOM   183  C  CG  . GLN A 1 24  ? -33.556 28.490 -21.394 1.00 19.31 ? 248  GLN A CG  1 
ATOM   184  C  CD  . GLN A 1 24  ? -34.973 27.916 -21.378 1.00 23.06 ? 248  GLN A CD  1 
ATOM   185  O  OE1 . GLN A 1 24  ? -35.814 28.364 -20.611 1.00 22.01 ? 248  GLN A OE1 1 
ATOM   186  N  NE2 . GLN A 1 24  ? -35.231 26.920 -22.215 1.00 24.10 ? 248  GLN A NE2 1 
ATOM   187  N  N   . MET A 1 25  ? -31.858 31.346 -23.112 1.00 18.85 ? 249  MET A N   1 
ATOM   188  C  CA  . MET A 1 25  ? -32.323 32.651 -22.676 1.00 19.66 ? 249  MET A CA  1 
ATOM   189  C  C   . MET A 1 25  ? -33.748 32.526 -22.152 1.00 24.09 ? 249  MET A C   1 
ATOM   190  O  O   . MET A 1 25  ? -34.535 31.696 -22.617 1.00 19.38 ? 249  MET A O   1 
ATOM   191  C  CB  . MET A 1 25  ? -32.257 33.662 -23.815 1.00 21.10 ? 249  MET A CB  1 
ATOM   192  C  CG  . MET A 1 25  ? -30.817 34.006 -24.184 1.00 23.72 ? 249  MET A CG  1 
ATOM   193  S  SD  . MET A 1 25  ? -30.673 35.065 -25.624 1.00 24.05 ? 249  MET A SD  1 
ATOM   194  C  CE  . MET A 1 25  ? -31.472 34.058 -26.869 1.00 23.50 ? 249  MET A CE  1 
ATOM   195  N  N   . TYR A 1 26  ? -34.066 33.342 -21.152 1.00 17.44 ? 250  TYR A N   1 
ATOM   196  C  CA  . TYR A 1 26  ? -35.366 33.268 -20.505 1.00 19.72 ? 250  TYR A CA  1 
ATOM   197  C  C   . TYR A 1 26  ? -35.756 34.673 -20.063 1.00 20.25 ? 250  TYR A C   1 
ATOM   198  O  O   . TYR A 1 26  ? -34.898 35.472 -19.688 1.00 21.54 ? 250  TYR A O   1 
ATOM   199  C  CB  . TYR A 1 26  ? -35.330 32.306 -19.308 1.00 21.70 ? 250  TYR A CB  1 
ATOM   200  C  CG  . TYR A 1 26  ? -36.667 32.107 -18.647 1.00 21.74 ? 250  TYR A CG  1 
ATOM   201  C  CD1 . TYR A 1 26  ? -37.610 31.255 -19.198 1.00 24.21 ? 250  TYR A CD1 1 
ATOM   202  C  CD2 . TYR A 1 26  ? -36.988 32.769 -17.476 1.00 23.11 ? 250  TYR A CD2 1 
ATOM   203  C  CE1 . TYR A 1 26  ? -38.840 31.073 -18.601 1.00 27.42 ? 250  TYR A CE1 1 
ATOM   204  C  CE2 . TYR A 1 26  ? -38.207 32.585 -16.866 1.00 20.70 ? 250  TYR A CE2 1 
ATOM   205  C  CZ  . TYR A 1 26  ? -39.129 31.747 -17.438 1.00 25.03 ? 250  TYR A CZ  1 
ATOM   206  O  OH  . TYR A 1 26  ? -40.352 31.569 -16.840 1.00 31.44 ? 250  TYR A OH  1 
ATOM   207  N  N   . THR A 1 27  ? -37.046 34.978 -20.121 1.00 21.72 ? 251  THR A N   1 
ATOM   208  C  CA  . THR A 1 27  ? -37.533 36.255 -19.620 1.00 22.53 ? 251  THR A CA  1 
ATOM   209  C  C   . THR A 1 27  ? -38.744 36.037 -18.720 1.00 24.63 ? 251  THR A C   1 
ATOM   210  O  O   . THR A 1 27  ? -39.500 35.077 -18.886 1.00 24.13 ? 251  THR A O   1 
ATOM   211  C  CB  . THR A 1 27  ? -37.886 37.228 -20.765 1.00 21.82 ? 251  THR A CB  1 
ATOM   212  O  OG1 . THR A 1 27  ? -38.208 38.512 -20.208 1.00 22.86 ? 251  THR A OG1 1 
ATOM   213  C  CG2 . THR A 1 27  ? -39.073 36.716 -21.585 1.00 20.39 ? 251  THR A CG2 1 
ATOM   214  N  N   . SER A 1 28  ? -38.915 36.938 -17.756 1.00 21.14 ? 252  SER A N   1 
ATOM   215  C  CA  . SER A 1 28  ? -40.000 36.811 -16.797 1.00 29.95 ? 252  SER A CA  1 
ATOM   216  C  C   . SER A 1 28  ? -40.428 38.187 -16.300 1.00 31.03 ? 252  SER A C   1 
ATOM   217  O  O   . SER A 1 28  ? -39.665 39.154 -16.340 1.00 27.15 ? 252  SER A O   1 
ATOM   218  C  CB  . SER A 1 28  ? -39.587 35.919 -15.618 1.00 29.89 ? 252  SER A CB  1 
ATOM   219  O  OG  . SER A 1 28  ? -40.476 36.099 -14.537 1.00 34.65 ? 252  SER A OG  1 
ATOM   220  N  N   A ARG A 1 29  ? -41.680 38.265 -15.841 0.86 32.83 ? 253  ARG A N   1 
ATOM   221  C  CA  A ARG A 1 29  ? -42.154 39.479 -15.183 0.86 34.64 ? 253  ARG A CA  1 
ATOM   222  C  C   A ARG A 1 29  ? -41.503 39.664 -13.819 0.86 36.76 ? 253  ARG A C   1 
ATOM   223  O  O   A ARG A 1 29  ? -41.335 40.800 -13.363 0.86 32.77 ? 253  ARG A O   1 
ATOM   224  C  CB  A ARG A 1 29  ? -43.672 39.437 -15.001 0.86 37.99 ? 253  ARG A CB  1 
ATOM   225  C  CG  A ARG A 1 29  ? -44.453 38.874 -16.164 0.86 40.10 ? 253  ARG A CG  1 
ATOM   226  C  CD  A ARG A 1 29  ? -45.938 38.896 -15.843 0.86 43.78 ? 253  ARG A CD  1 
ATOM   227  N  NE  A ARG A 1 29  ? -46.752 38.397 -16.946 0.86 51.18 ? 253  ARG A NE  1 
ATOM   228  C  CZ  A ARG A 1 29  ? -47.191 39.143 -17.953 0.86 47.78 ? 253  ARG A CZ  1 
ATOM   229  N  NH1 A ARG A 1 29  ? -46.889 40.430 -18.044 0.86 44.79 ? 253  ARG A NH1 1 
ATOM   230  N  NH2 A ARG A 1 29  ? -47.949 38.581 -18.896 0.86 43.65 ? 253  ARG A NH2 1 
ATOM   231  N  N   . SER A 1 30  ? -41.169 38.558 -13.147 1.00 34.24 ? 254  SER A N   1 
ATOM   232  C  CA  . SER A 1 30  ? -40.614 38.578 -11.793 1.00 43.51 ? 254  SER A CA  1 
ATOM   233  C  C   . SER A 1 30  ? -41.480 39.400 -10.835 1.00 49.48 ? 254  SER A C   1 
ATOM   234  O  O   . SER A 1 30  ? -40.976 40.209 -10.050 1.00 45.89 ? 254  SER A O   1 
ATOM   235  C  CB  . SER A 1 30  ? -39.178 39.103 -11.799 1.00 40.84 ? 254  SER A CB  1 
ATOM   236  O  OG  . SER A 1 30  ? -38.372 38.416 -12.744 1.00 40.12 ? 254  SER A OG  1 
ATOM   237  N  N   . GLU A 1 31  ? -42.797 39.202 -10.906 1.00 57.39 ? 255  GLU A N   1 
ATOM   238  C  CA  . GLU A 1 31  ? -43.703 39.917 -10.015 1.00 53.95 ? 255  GLU A CA  1 
ATOM   239  C  C   . GLU A 1 31  ? -43.496 39.456 -8.580  1.00 56.33 ? 255  GLU A C   1 
ATOM   240  O  O   . GLU A 1 31  ? -43.335 38.260 -8.311  1.00 55.48 ? 255  GLU A O   1 
ATOM   241  C  CB  . GLU A 1 31  ? -45.161 39.697 -10.425 1.00 58.03 ? 255  GLU A CB  1 
ATOM   242  C  CG  . GLU A 1 31  ? -45.456 40.032 -11.880 1.00 67.19 ? 255  GLU A CG  1 
ATOM   243  C  CD  . GLU A 1 31  ? -46.941 40.249 -12.155 1.00 80.39 ? 255  GLU A CD  1 
ATOM   244  O  OE1 . GLU A 1 31  ? -47.516 41.219 -11.610 1.00 87.37 ? 255  GLU A OE1 1 
ATOM   245  O  OE2 . GLU A 1 31  ? -47.532 39.449 -12.915 1.00 71.12 ? 255  GLU A OE2 1 
ATOM   246  N  N   . GLY A 1 32  ? -43.488 40.416 -7.657  1.00 51.23 ? 256  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 32  ? -43.304 40.094 -6.255  1.00 48.46 ? 256  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 32  ? -41.975 39.462 -5.926  1.00 46.90 ? 256  GLY A C   1 
ATOM   249  O  O   . GLY A 1 32  ? -41.851 38.803 -4.889  1.00 52.01 ? 256  GLY A O   1 
ATOM   250  N  N   . ILE A 1 33  ? -40.972 39.641 -6.780  1.00 38.46 ? 257  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 33  ? -39.649 39.065 -6.587  1.00 39.46 ? 257  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 33  ? -38.633 40.193 -6.607  1.00 32.41 ? 257  ILE A C   1 
ATOM   253  O  O   . ILE A 1 33  ? -38.721 41.101 -7.439  1.00 34.43 ? 257  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 33  ? -39.320 38.022 -7.677  1.00 42.69 ? 257  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 33  ? -40.235 36.803 -7.549  1.00 47.82 ? 257  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 33  ? -37.857 37.607 -7.615  1.00 34.11 ? 257  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 33  ? -39.990 35.752 -8.615  1.00 42.19 ? 257  ILE A CD1 1 
ATOM   258  N  N   . VAL A 1 34  ? -37.669 40.134 -5.700  1.00 30.89 ? 258  VAL A N   1 
ATOM   259  C  CA  . VAL A 1 34  ? -36.534 41.046 -5.713  1.00 29.71 ? 258  VAL A CA  1 
ATOM   260  C  C   . VAL A 1 34  ? -35.372 40.311 -6.369  1.00 23.22 ? 258  VAL A C   1 
ATOM   261  O  O   . VAL A 1 34  ? -34.841 39.349 -5.812  1.00 25.02 ? 258  VAL A O   1 
ATOM   262  C  CB  . VAL A 1 34  ? -36.183 41.536 -4.304  1.00 25.98 ? 258  VAL A CB  1 
ATOM   263  C  CG1 . VAL A 1 34  ? -34.966 42.444 -4.344  1.00 27.48 ? 258  VAL A CG1 1 
ATOM   264  C  CG2 . VAL A 1 34  ? -37.371 42.281 -3.707  1.00 33.50 ? 258  VAL A CG2 1 
ATOM   265  N  N   . VAL A 1 35  ? -34.990 40.751 -7.567  1.00 23.38 ? 259  VAL A N   1 
ATOM   266  C  CA  . VAL A 1 35  ? -33.903 40.138 -8.326  1.00 21.62 ? 259  VAL A CA  1 
ATOM   267  C  C   . VAL A 1 35  ? -32.609 40.813 -7.878  1.00 21.74 ? 259  VAL A C   1 
ATOM   268  O  O   . VAL A 1 35  ? -32.293 41.921 -8.314  1.00 23.77 ? 259  VAL A O   1 
ATOM   269  C  CB  . VAL A 1 35  ? -34.123 40.284 -9.832  1.00 20.97 ? 259  VAL A CB  1 
ATOM   270  C  CG1 . VAL A 1 35  ? -32.961 39.650 -10.611 1.00 19.62 ? 259  VAL A CG1 1 
ATOM   271  C  CG2 . VAL A 1 35  ? -35.486 39.690 -10.235 1.00 23.99 ? 259  VAL A CG2 1 
ATOM   272  N  N   . GLN A 1 36  ? -31.850 40.152 -7.004  1.00 21.02 ? 260  GLN A N   1 
ATOM   273  C  CA  . GLN A 1 36  ? -30.627 40.744 -6.455  1.00 19.70 ? 260  GLN A CA  1 
ATOM   274  C  C   . GLN A 1 36  ? -29.518 39.701 -6.306  1.00 20.59 ? 260  GLN A C   1 
ATOM   275  O  O   . GLN A 1 36  ? -28.942 39.537 -5.225  1.00 18.61 ? 260  GLN A O   1 
ATOM   276  C  CB  . GLN A 1 36  ? -30.938 41.415 -5.119  1.00 21.56 ? 260  GLN A CB  1 
ATOM   277  C  CG  . GLN A 1 36  ? -29.849 42.333 -4.607  1.00 23.35 ? 260  GLN A CG  1 
ATOM   278  C  CD  . GLN A 1 36  ? -30.356 43.246 -3.502  1.00 24.81 ? 260  GLN A CD  1 
ATOM   279  O  OE1 . GLN A 1 36  ? -31.500 43.134 -3.080  1.00 26.65 ? 260  GLN A OE1 1 
ATOM   280  N  NE2 . GLN A 1 36  ? -29.507 44.154 -3.038  1.00 21.31 ? 260  GLN A NE2 1 
ATOM   281  N  N   . PRO A 1 37  ? -29.166 38.997 -7.387  1.00 18.84 ? 261  PRO A N   1 
ATOM   282  C  CA  . PRO A 1 37  ? -28.068 38.031 -7.292  1.00 20.98 ? 261  PRO A CA  1 
ATOM   283  C  C   . PRO A 1 37  ? -26.756 38.755 -7.055  1.00 21.38 ? 261  PRO A C   1 
ATOM   284  O  O   . PRO A 1 37  ? -26.585 39.914 -7.444  1.00 18.04 ? 261  PRO A O   1 
ATOM   285  C  CB  . PRO A 1 37  ? -28.081 37.331 -8.655  1.00 20.66 ? 261  PRO A CB  1 
ATOM   286  C  CG  . PRO A 1 37  ? -28.667 38.365 -9.589  1.00 19.07 ? 261  PRO A CG  1 
ATOM   287  C  CD  . PRO A 1 37  ? -29.695 39.095 -8.763  1.00 19.52 ? 261  PRO A CD  1 
ATOM   288  N  N   . GLN A 1 38  ? -25.838 38.063 -6.375  1.00 19.93 ? 262  GLN A N   1 
ATOM   289  C  CA  . GLN A 1 38  ? -24.558 38.634 -5.986  1.00 20.70 ? 262  GLN A CA  1 
ATOM   290  C  C   . GLN A 1 38  ? -23.395 38.104 -6.804  1.00 20.46 ? 262  GLN A C   1 
ATOM   291  O  O   . GLN A 1 38  ? -22.324 38.726 -6.798  1.00 21.80 ? 262  GLN A O   1 
ATOM   292  C  CB  . GLN A 1 38  ? -24.284 38.376 -4.493  1.00 20.52 ? 262  GLN A CB  1 
ATOM   293  C  CG  . GLN A 1 38  ? -25.293 39.047 -3.571  1.00 19.02 ? 262  GLN A CG  1 
ATOM   294  C  CD  . GLN A 1 38  ? -25.360 40.537 -3.816  1.00 21.42 ? 262  GLN A CD  1 
ATOM   295  O  OE1 . GLN A 1 38  ? -24.339 41.217 -3.794  1.00 20.87 ? 262  GLN A OE1 1 
ATOM   296  N  NE2 . GLN A 1 38  ? -26.558 41.049 -4.067  1.00 22.13 ? 262  GLN A NE2 1 
ATOM   297  N  N   . ASN A 1 39  ? -23.579 36.985 -7.497  1.00 16.89 ? 263  ASN A N   1 
ATOM   298  C  CA  . ASN A 1 39  ? -22.634 36.474 -8.474  1.00 18.40 ? 263  ASN A CA  1 
ATOM   299  C  C   . ASN A 1 39  ? -23.066 36.877 -9.879  1.00 21.01 ? 263  ASN A C   1 
ATOM   300  O  O   . ASN A 1 39  ? -24.238 37.140 -10.136 1.00 19.94 ? 263  ASN A O   1 
ATOM   301  C  CB  . ASN A 1 39  ? -22.524 34.955 -8.356  1.00 17.47 ? 263  ASN A CB  1 
ATOM   302  C  CG  . ASN A 1 39  ? -21.798 34.545 -7.100  1.00 18.89 ? 263  ASN A CG  1 
ATOM   303  O  OD1 . ASN A 1 39  ? -20.749 35.109 -6.782  1.00 18.07 ? 263  ASN A OD1 1 
ATOM   304  N  ND2 . ASN A 1 39  ? -22.360 33.595 -6.355  1.00 18.30 ? 263  ASN A ND2 1 
ATOM   305  N  N   . GLY A 1 40  ? -22.101 36.927 -10.793 1.00 20.64 ? 264  GLY A N   1 
ATOM   306  C  CA  . GLY A 1 40  ? -22.415 37.396 -12.127 1.00 17.93 ? 264  GLY A CA  1 
ATOM   307  C  C   . GLY A 1 40  ? -22.788 38.861 -12.180 1.00 20.87 ? 264  GLY A C   1 
ATOM   308  O  O   . GLY A 1 40  ? -23.627 39.257 -13.001 1.00 20.60 ? 264  GLY A O   1 
ATOM   309  N  N   . ARG A 1 41  ? -22.200 39.676 -11.317 1.00 17.80 ? 265  ARG A N   1 
ATOM   310  C  CA  . ARG A 1 41  ? -22.514 41.099 -11.243 1.00 19.65 ? 265  ARG A CA  1 
ATOM   311  C  C   . ARG A 1 41  ? -21.282 41.886 -11.668 1.00 18.96 ? 265  ARG A C   1 
ATOM   312  O  O   . ARG A 1 41  ? -20.240 41.821 -11.009 1.00 20.07 ? 265  ARG A O   1 
ATOM   313  C  CB  . ARG A 1 41  ? -22.960 41.489 -9.831  1.00 17.98 ? 265  ARG A CB  1 
ATOM   314  C  CG  . ARG A 1 41  ? -24.205 40.758 -9.350  1.00 17.84 ? 265  ARG A CG  1 
ATOM   315  C  CD  . ARG A 1 41  ? -25.407 41.039 -10.275 1.00 19.69 ? 265  ARG A CD  1 
ATOM   316  N  NE  . ARG A 1 41  ? -25.749 42.458 -10.295 1.00 17.34 ? 265  ARG A NE  1 
ATOM   317  C  CZ  . ARG A 1 41  ? -26.663 43.022 -9.516  1.00 19.22 ? 265  ARG A CZ  1 
ATOM   318  N  NH1 . ARG A 1 41  ? -27.381 42.308 -8.662  1.00 21.81 ? 265  ARG A NH1 1 
ATOM   319  N  NH2 . ARG A 1 41  ? -26.872 44.336 -9.603  1.00 20.53 ? 265  ARG A NH2 1 
ATOM   320  N  N   . ALA A 1 42  ? -21.391 42.612 -12.775 1.00 18.74 ? 266  ALA A N   1 
ATOM   321  C  CA  . ALA A 1 42  ? -20.286 43.439 -13.231 1.00 22.10 ? 266  ALA A CA  1 
ATOM   322  C  C   . ALA A 1 42  ? -20.845 44.595 -14.043 1.00 23.03 ? 266  ALA A C   1 
ATOM   323  O  O   . ALA A 1 42  ? -21.822 44.427 -14.776 1.00 22.77 ? 266  ALA A O   1 
ATOM   324  C  CB  . ALA A 1 42  ? -19.290 42.637 -14.073 1.00 18.57 ? 266  ALA A CB  1 
ATOM   325  N  N   . THR A 1 43  ? -20.236 45.763 -13.901 1.00 19.96 ? 267  THR A N   1 
ATOM   326  C  CA  . THR A 1 43  ? -20.578 46.847 -14.802 1.00 25.74 ? 267  THR A CA  1 
ATOM   327  C  C   . THR A 1 43  ? -19.928 46.602 -16.157 1.00 22.12 ? 267  THR A C   1 
ATOM   328  O  O   . THR A 1 43  ? -18.940 45.872 -16.276 1.00 19.49 ? 267  THR A O   1 
ATOM   329  C  CB  . THR A 1 43  ? -20.127 48.192 -14.232 1.00 22.15 ? 267  THR A CB  1 
ATOM   330  O  OG1 . THR A 1 43  ? -18.693 48.272 -14.261 1.00 20.53 ? 267  THR A OG1 1 
ATOM   331  C  CG2 . THR A 1 43  ? -20.624 48.341 -12.800 1.00 22.16 ? 267  THR A CG2 1 
ATOM   332  N  N   . ILE A 1 44  ? -20.475 47.237 -17.196 1.00 21.13 ? 268  ILE A N   1 
ATOM   333  C  CA  . ILE A 1 44  ? -19.898 46.990 -18.515 1.00 22.71 ? 268  ILE A CA  1 
ATOM   334  C  C   . ILE A 1 44  ? -18.531 47.639 -18.683 1.00 25.08 ? 268  ILE A C   1 
ATOM   335  O  O   . ILE A 1 44  ? -17.815 47.309 -19.635 1.00 20.91 ? 268  ILE A O   1 
ATOM   336  C  CB  . ILE A 1 44  ? -20.855 47.418 -19.646 1.00 24.18 ? 268  ILE A CB  1 
ATOM   337  C  CG1 . ILE A 1 44  ? -21.010 48.924 -19.722 1.00 22.60 ? 268  ILE A CG1 1 
ATOM   338  C  CG2 . ILE A 1 44  ? -22.233 46.793 -19.445 1.00 22.17 ? 268  ILE A CG2 1 
ATOM   339  C  CD1 . ILE A 1 44  ? -22.140 49.282 -20.668 1.00 25.46 ? 268  ILE A CD1 1 
ATOM   340  N  N   . ASP A 1 45  ? -18.127 48.527 -17.776 1.00 21.07 ? 269  ASP A N   1 
ATOM   341  C  CA  . ASP A 1 45  ? -16.749 48.997 -17.786 1.00 27.89 ? 269  ASP A CA  1 
ATOM   342  C  C   . ASP A 1 45  ? -15.846 48.169 -16.879 1.00 28.73 ? 269  ASP A C   1 
ATOM   343  O  O   . ASP A 1 45  ? -14.702 48.567 -16.634 1.00 33.47 ? 269  ASP A O   1 
ATOM   344  C  CB  . ASP A 1 45  ? -16.667 50.494 -17.438 1.00 32.53 ? 269  ASP A CB  1 
ATOM   345  C  CG  . ASP A 1 45  ? -17.289 50.849 -16.111 1.00 40.55 ? 269  ASP A CG  1 
ATOM   346  O  OD1 . ASP A 1 45  ? -17.515 49.949 -15.272 1.00 37.12 ? 269  ASP A OD1 1 
ATOM   347  O  OD2 . ASP A 1 45  ? -17.540 52.064 -15.912 1.00 41.46 ? 269  ASP A OD2 1 
ATOM   348  N  N   . GLY A 1 46  ? -16.331 47.028 -16.388 1.00 25.65 ? 270  GLY A N   1 
ATOM   349  C  CA  . GLY A 1 46  ? -15.477 46.018 -15.805 1.00 25.70 ? 270  GLY A CA  1 
ATOM   350  C  C   . GLY A 1 46  ? -15.317 46.034 -14.298 1.00 28.99 ? 270  GLY A C   1 
ATOM   351  O  O   . GLY A 1 46  ? -14.459 45.310 -13.782 1.00 26.93 ? 270  GLY A O   1 
ATOM   352  N  N   . GLU A 1 47  ? -16.100 46.828 -13.575 1.00 22.99 ? 271  GLU A N   1 
ATOM   353  C  CA  . GLU A 1 47  ? -16.067 46.775 -12.122 1.00 23.37 ? 271  GLU A CA  1 
ATOM   354  C  C   . GLU A 1 47  ? -16.908 45.589 -11.649 1.00 25.10 ? 271  GLU A C   1 
ATOM   355  O  O   . GLU A 1 47  ? -18.109 45.523 -11.941 1.00 24.30 ? 271  GLU A O   1 
ATOM   356  C  CB  . GLU A 1 47  ? -16.589 48.087 -11.537 1.00 25.77 ? 271  GLU A CB  1 
ATOM   357  C  CG  . GLU A 1 47  ? -16.683 48.092 -10.018 1.00 27.97 ? 271  GLU A CG  1 
ATOM   358  C  CD  . GLU A 1 47  ? -17.114 49.451 -9.448  1.00 34.62 ? 271  GLU A CD  1 
ATOM   359  O  OE1 . GLU A 1 47  ? -17.869 50.180 -10.125 1.00 30.55 ? 271  GLU A OE1 1 
ATOM   360  O  OE2 . GLU A 1 47  ? -16.693 49.789 -8.320  1.00 40.55 ? 271  GLU A OE2 1 
ATOM   361  N  N   . LEU A 1 48  ? -16.281 44.655 -10.929 1.00 23.77 ? 272  LEU A N   1 
ATOM   362  C  CA  . LEU A 1 48  ? -16.991 43.513 -10.360 1.00 21.15 ? 272  LEU A CA  1 
ATOM   363  C  C   . LEU A 1 48  ? -17.757 43.930 -9.108  1.00 21.81 ? 272  LEU A C   1 
ATOM   364  O  O   . LEU A 1 48  ? -17.252 44.690 -8.280  1.00 26.46 ? 272  LEU A O   1 
ATOM   365  C  CB  . LEU A 1 48  ? -16.001 42.400 -10.013 1.00 21.18 ? 272  LEU A CB  1 
ATOM   366  C  CG  . LEU A 1 48  ? -15.078 41.934 -11.138 1.00 23.36 ? 272  LEU A CG  1 
ATOM   367  C  CD1 . LEU A 1 48  ? -14.048 40.937 -10.603 1.00 22.52 ? 272  LEU A CD1 1 
ATOM   368  C  CD2 . LEU A 1 48  ? -15.888 41.324 -12.258 1.00 21.49 ? 272  LEU A CD2 1 
ATOM   369  N  N   . LEU A 1 49  ? -18.973 43.417 -8.956  1.00 19.73 ? 273  LEU A N   1 
ATOM   370  C  CA  . LEU A 1 49  ? -19.830 43.776 -7.831  1.00 21.34 ? 273  LEU A CA  1 
ATOM   371  C  C   . LEU A 1 49  ? -20.193 42.534 -7.018  1.00 23.70 ? 273  LEU A C   1 
ATOM   372  O  O   . LEU A 1 49  ? -19.965 41.400 -7.438  1.00 20.10 ? 273  LEU A O   1 
ATOM   373  C  CB  . LEU A 1 49  ? -21.105 44.475 -8.318  1.00 21.15 ? 273  LEU A CB  1 
ATOM   374  C  CG  . LEU A 1 49  ? -20.857 45.581 -9.342  1.00 20.72 ? 273  LEU A CG  1 
ATOM   375  C  CD1 . LEU A 1 49  ? -22.176 46.100 -9.886  1.00 24.87 ? 273  LEU A CD1 1 
ATOM   376  C  CD2 . LEU A 1 49  ? -20.048 46.714 -8.699  1.00 22.43 ? 273  LEU A CD2 1 
ATOM   377  N  N   . GLY A 1 50  ? -20.783 42.769 -5.846  1.00 19.34 ? 274  GLY A N   1 
ATOM   378  C  CA  . GLY A 1 50  ? -21.228 41.681 -4.987  1.00 21.36 ? 274  GLY A CA  1 
ATOM   379  C  C   . GLY A 1 50  ? -20.098 40.732 -4.625  1.00 22.62 ? 274  GLY A C   1 
ATOM   380  O  O   . GLY A 1 50  ? -19.055 41.128 -4.076  1.00 23.34 ? 274  GLY A O   1 
ATOM   381  N  N   . THR A 1 51  ? -20.310 39.452 -4.914  1.00 22.68 ? 275  THR A N   1 
ATOM   382  C  CA  . THR A 1 51  ? -19.317 38.412 -4.678  1.00 20.24 ? 275  THR A CA  1 
ATOM   383  C  C   . THR A 1 51  ? -18.713 37.896 -5.980  1.00 18.55 ? 275  THR A C   1 
ATOM   384  O  O   . THR A 1 51  ? -18.225 36.765 -6.023  1.00 17.96 ? 275  THR A O   1 
ATOM   385  C  CB  . THR A 1 51  ? -19.935 37.245 -3.898  1.00 21.30 ? 275  THR A CB  1 
ATOM   386  O  OG1 . THR A 1 51  ? -21.074 36.735 -4.612  1.00 19.36 ? 275  THR A OG1 1 
ATOM   387  C  CG2 . THR A 1 51  ? -20.373 37.681 -2.501  1.00 19.50 ? 275  THR A CG2 1 
ATOM   388  N  N   . THR A 1 52  ? -18.726 38.699 -7.041  1.00 20.51 ? 276  THR A N   1 
ATOM   389  C  CA  . THR A 1 52  ? -18.379 38.190 -8.362  1.00 16.67 ? 276  THR A CA  1 
ATOM   390  C  C   . THR A 1 52  ? -16.869 38.059 -8.528  1.00 21.36 ? 276  THR A C   1 
ATOM   391  O  O   . THR A 1 52  ? -16.112 38.997 -8.248  1.00 21.75 ? 276  THR A O   1 
ATOM   392  C  CB  . THR A 1 52  ? -18.949 39.099 -9.447  1.00 20.00 ? 276  THR A CB  1 
ATOM   393  O  OG1 . THR A 1 52  ? -20.382 39.101 -9.376  1.00 18.19 ? 276  THR A OG1 1 
ATOM   394  C  CG2 . THR A 1 52  ? -18.511 38.621 -10.821 1.00 19.74 ? 276  THR A CG2 1 
ATOM   395  N  N   . LEU A 1 53  ? -16.436 36.895 -8.994  1.00 18.02 ? 277  LEU A N   1 
ATOM   396  C  CA  . LEU A 1 53  ? -15.047 36.652 -9.343  1.00 21.41 ? 277  LEU A CA  1 
ATOM   397  C  C   . LEU A 1 53  ? -14.966 36.326 -10.829 1.00 21.61 ? 277  LEU A C   1 
ATOM   398  O  O   . LEU A 1 53  ? -15.978 36.104 -11.498 1.00 23.35 ? 277  LEU A O   1 
ATOM   399  C  CB  . LEU A 1 53  ? -14.440 35.530 -8.482  1.00 20.51 ? 277  LEU A CB  1 
ATOM   400  C  CG  . LEU A 1 53  ? -15.212 34.240 -8.182  1.00 28.85 ? 277  LEU A CG  1 
ATOM   401  C  CD1 . LEU A 1 53  ? -15.569 33.479 -9.451  1.00 21.95 ? 277  LEU A CD1 1 
ATOM   402  C  CD2 . LEU A 1 53  ? -14.409 33.344 -7.235  1.00 22.16 ? 277  LEU A CD2 1 
ATOM   403  N  N   . VAL A 1 54  ? -13.747 36.312 -11.348 1.00 20.56 ? 278  VAL A N   1 
ATOM   404  C  CA  . VAL A 1 54  ? -13.551 36.168 -12.787 1.00 19.95 ? 278  VAL A CA  1 
ATOM   405  C  C   . VAL A 1 54  ? -13.485 34.699 -13.203 1.00 22.44 ? 278  VAL A C   1 
ATOM   406  O  O   . VAL A 1 54  ? -13.933 34.354 -14.300 1.00 23.10 ? 278  VAL A O   1 
ATOM   407  C  CB  . VAL A 1 54  ? -12.285 36.955 -13.190 1.00 25.30 ? 278  VAL A CB  1 
ATOM   408  C  CG1 . VAL A 1 54  ? -11.884 36.689 -14.624 1.00 30.60 ? 278  VAL A CG1 1 
ATOM   409  C  CG2 . VAL A 1 54  ? -12.532 38.440 -12.993 1.00 27.63 ? 278  VAL A CG2 1 
ATOM   410  N  N   . SER A 1 55  ? -12.984 33.822 -12.326 1.00 25.08 ? 279  SER A N   1 
ATOM   411  C  CA  . SER A 1 55  ? -12.879 32.394 -12.634 1.00 22.77 ? 279  SER A CA  1 
ATOM   412  C  C   . SER A 1 55  ? -14.248 31.785 -12.918 1.00 19.88 ? 279  SER A C   1 
ATOM   413  O  O   . SER A 1 55  ? -15.180 31.960 -12.126 1.00 21.07 ? 279  SER A O   1 
ATOM   414  C  CB  . SER A 1 55  ? -12.218 31.642 -11.481 1.00 20.84 ? 279  SER A CB  1 
ATOM   415  O  OG  . SER A 1 55  ? -12.400 30.236 -11.611 1.00 20.71 ? 279  SER A OG  1 
ATOM   416  N  N   . PRO A 1 56  ? -14.404 31.048 -14.016 1.00 22.14 ? 280  PRO A N   1 
ATOM   417  C  CA  . PRO A 1 56  ? -15.712 30.483 -14.366 1.00 24.57 ? 280  PRO A CA  1 
ATOM   418  C  C   . PRO A 1 56  ? -16.021 29.143 -13.720 1.00 21.63 ? 280  PRO A C   1 
ATOM   419  O  O   . PRO A 1 56  ? -17.136 28.633 -13.895 1.00 24.46 ? 280  PRO A O   1 
ATOM   420  C  CB  . PRO A 1 56  ? -15.603 30.330 -15.891 1.00 22.75 ? 280  PRO A CB  1 
ATOM   421  C  CG  . PRO A 1 56  ? -14.140 30.015 -16.104 1.00 21.72 ? 280  PRO A CG  1 
ATOM   422  C  CD  . PRO A 1 56  ? -13.403 30.854 -15.079 1.00 20.45 ? 280  PRO A CD  1 
ATOM   423  N  N   . VAL A 1 57  ? -15.068 28.546 -13.007 1.00 19.57 ? 281  VAL A N   1 
ATOM   424  C  CA  . VAL A 1 57  ? -15.259 27.248 -12.381 1.00 20.79 ? 281  VAL A CA  1 
ATOM   425  C  C   . VAL A 1 57  ? -15.306 27.342 -10.871 1.00 22.15 ? 281  VAL A C   1 
ATOM   426  O  O   . VAL A 1 57  ? -15.362 26.302 -10.193 1.00 24.91 ? 281  VAL A O   1 
ATOM   427  C  CB  . VAL A 1 57  ? -14.168 26.250 -12.827 1.00 24.09 ? 281  VAL A CB  1 
ATOM   428  C  CG1 . VAL A 1 57  ? -14.259 26.010 -14.320 1.00 19.41 ? 281  VAL A CG1 1 
ATOM   429  C  CG2 . VAL A 1 57  ? -12.781 26.769 -12.463 1.00 18.96 ? 281  VAL A CG2 1 
ATOM   430  N  N   . SER A 1 58  ? -15.295 28.551 -10.314 1.00 17.71 ? 282  SER A N   1 
ATOM   431  C  CA  . SER A 1 58  ? -15.127 28.715 -8.884  1.00 18.56 ? 282  SER A CA  1 
ATOM   432  C  C   . SER A 1 58  ? -16.413 29.036 -8.138  1.00 20.21 ? 282  SER A C   1 
ATOM   433  O  O   . SER A 1 58  ? -16.479 28.784 -6.931  1.00 19.32 ? 282  SER A O   1 
ATOM   434  C  CB  . SER A 1 58  ? -14.098 29.819 -8.605  1.00 20.86 ? 282  SER A CB  1 
ATOM   435  O  OG  . SER A 1 58  ? -12.843 29.490 -9.186  1.00 21.39 ? 282  SER A OG  1 
ATOM   436  N  N   . VAL A 1 59  ? -17.427 29.595 -8.802  1.00 19.93 ? 283  VAL A N   1 
ATOM   437  C  CA  . VAL A 1 59  ? -18.625 29.985 -8.067  1.00 20.05 ? 283  VAL A CA  1 
ATOM   438  C  C   . VAL A 1 59  ? -19.255 28.748 -7.426  1.00 18.47 ? 283  VAL A C   1 
ATOM   439  O  O   . VAL A 1 59  ? -19.277 27.655 -8.009  1.00 21.01 ? 283  VAL A O   1 
ATOM   440  C  CB  . VAL A 1 59  ? -19.604 30.746 -8.981  1.00 22.10 ? 283  VAL A CB  1 
ATOM   441  C  CG1 . VAL A 1 59  ? -20.220 29.826 -10.031 1.00 19.84 ? 283  VAL A CG1 1 
ATOM   442  C  CG2 . VAL A 1 59  ? -20.691 31.457 -8.152  1.00 18.40 ? 283  VAL A CG2 1 
ATOM   443  N  N   . CYS A 1 60  ? -19.700 28.908 -6.179  1.00 20.47 ? 284  CYS A N   1 
ATOM   444  C  CA  . CYS A 1 60  ? -20.296 27.882 -5.325  1.00 19.39 ? 284  CYS A CA  1 
ATOM   445  C  C   . CYS A 1 60  ? -19.290 26.844 -4.850  1.00 20.41 ? 284  CYS A C   1 
ATOM   446  O  O   . CYS A 1 60  ? -19.694 25.801 -4.323  1.00 19.49 ? 284  CYS A O   1 
ATOM   447  C  CB  . CYS A 1 60  ? -21.487 27.186 -5.998  1.00 20.52 ? 284  CYS A CB  1 
ATOM   448  S  SG  . CYS A 1 60  ? -22.924 28.296 -6.212  1.00 23.00 ? 284  CYS A SG  1 
ATOM   449  N  N   . ASN A 1 61  ? -17.994 27.101 -4.997  1.00 19.60 ? 285  ASN A N   1 
ATOM   450  C  CA  . ASN A 1 61  ? -16.977 26.275 -4.365  1.00 17.96 ? 285  ASN A CA  1 
ATOM   451  C  C   . ASN A 1 61  ? -16.588 26.861 -3.013  1.00 19.64 ? 285  ASN A C   1 
ATOM   452  O  O   . ASN A 1 61  ? -16.728 28.062 -2.769  1.00 20.72 ? 285  ASN A O   1 
ATOM   453  C  CB  . ASN A 1 61  ? -15.733 26.159 -5.251  1.00 18.72 ? 285  ASN A CB  1 
ATOM   454  C  CG  . ASN A 1 61  ? -15.974 25.345 -6.506  1.00 19.80 ? 285  ASN A CG  1 
ATOM   455  O  OD1 . ASN A 1 61  ? -16.722 25.747 -7.407  1.00 21.26 ? 285  ASN A OD1 1 
ATOM   456  N  ND2 . ASN A 1 61  ? -15.321 24.208 -6.585  1.00 17.89 ? 285  ASN A ND2 1 
ATOM   457  N  N   . PHE A 1 62  ? -16.111 25.989 -2.127  1.00 18.21 ? 286  PHE A N   1 
ATOM   458  C  CA  . PHE A 1 62  ? -15.610 26.353 -0.811  1.00 22.46 ? 286  PHE A CA  1 
ATOM   459  C  C   . PHE A 1 62  ? -14.311 25.613 -0.563  1.00 21.30 ? 286  PHE A C   1 
ATOM   460  O  O   . PHE A 1 62  ? -14.153 24.478 -1.005  1.00 21.72 ? 286  PHE A O   1 
ATOM   461  C  CB  . PHE A 1 62  ? -16.554 25.955 0.320   1.00 22.13 ? 286  PHE A CB  1 
ATOM   462  C  CG  . PHE A 1 62  ? -17.811 26.737 0.373   1.00 19.70 ? 286  PHE A CG  1 
ATOM   463  C  CD1 . PHE A 1 62  ? -17.798 28.063 0.780   1.00 26.39 ? 286  PHE A CD1 1 
ATOM   464  C  CD2 . PHE A 1 62  ? -19.014 26.141 0.069   1.00 18.64 ? 286  PHE A CD2 1 
ATOM   465  C  CE1 . PHE A 1 62  ? -18.977 28.791 0.837   1.00 25.19 ? 286  PHE A CE1 1 
ATOM   466  C  CE2 . PHE A 1 62  ? -20.195 26.866 0.140   1.00 20.45 ? 286  PHE A CE2 1 
ATOM   467  C  CZ  . PHE A 1 62  ? -20.172 28.174 0.527   1.00 20.32 ? 286  PHE A CZ  1 
ATOM   468  N  N   . LYS A 1 63  ? -13.405 26.227 0.193   1.00 18.64 ? 287  LYS A N   1 
ATOM   469  C  CA  . LYS A 1 63  ? -12.264 25.462 0.669   1.00 23.29 ? 287  LYS A CA  1 
ATOM   470  C  C   . LYS A 1 63  ? -11.768 26.040 1.986   1.00 23.67 ? 287  LYS A C   1 
ATOM   471  O  O   . LYS A 1 63  ? -12.030 27.194 2.328   1.00 24.65 ? 287  LYS A O   1 
ATOM   472  C  CB  . LYS A 1 63  ? -11.139 25.390 -0.369  1.00 22.99 ? 287  LYS A CB  1 
ATOM   473  C  CG  . LYS A 1 63  ? -10.374 26.649 -0.650  1.00 24.44 ? 287  LYS A CG  1 
ATOM   474  C  CD  . LYS A 1 63  ? -9.572  26.423 -1.945  1.00 28.23 ? 287  LYS A CD  1 
ATOM   475  C  CE  . LYS A 1 63  ? -8.296  27.227 -1.970  1.00 33.76 ? 287  LYS A CE  1 
ATOM   476  N  NZ  . LYS A 1 63  ? -7.367  26.780 -0.893  1.00 47.89 ? 287  LYS A NZ  1 
ATOM   477  N  N   . GLY A 1 64  ? -11.074 25.202 2.736   1.00 24.87 ? 288  GLY A N   1 
ATOM   478  C  CA  . GLY A 1 64  ? -10.592 25.591 4.043   1.00 25.12 ? 288  GLY A CA  1 
ATOM   479  C  C   . GLY A 1 64  ? -10.188 24.359 4.824   1.00 25.99 ? 288  GLY A C   1 
ATOM   480  O  O   . GLY A 1 64  ? -10.038 23.271 4.277   1.00 27.72 ? 288  GLY A O   1 
ATOM   481  N  N   . ASN A 1 65  ? -10.025 24.560 6.118   1.00 26.15 ? 289  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 65  ? -9.618  23.484 6.997   1.00 29.74 ? 289  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 65  ? -10.843 22.769 7.548   1.00 32.87 ? 289  ASN A C   1 
ATOM   484  O  O   . ASN A 1 65  ? -11.848 23.407 7.871   1.00 30.21 ? 289  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 65  ? -8.775  24.038 8.141   1.00 31.76 ? 289  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 65  ? -8.176  22.958 8.974   1.00 29.75 ? 289  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 65  ? -7.595  22.007 8.444   1.00 29.85 ? 289  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 65  ? -8.335  23.067 10.286  1.00 29.16 ? 289  ASN A ND2 1 
ATOM   489  N  N   . LEU A 1 66  ? -10.761 21.438 7.630   1.00 26.03 ? 290  LEU A N   1 
ATOM   490  C  CA  . LEU A 1 66  ? -11.748 20.649 8.359   1.00 27.12 ? 290  LEU A CA  1 
ATOM   491  C  C   . LEU A 1 66  ? -11.421 20.805 9.835   1.00 31.72 ? 290  LEU A C   1 
ATOM   492  O  O   . LEU A 1 66  ? -10.587 20.092 10.395  1.00 35.17 ? 290  LEU A O   1 
ATOM   493  C  CB  . LEU A 1 66  ? -11.734 19.190 7.922   1.00 30.05 ? 290  LEU A CB  1 
ATOM   494  C  CG  . LEU A 1 66  ? -12.943 18.357 8.358   1.00 31.57 ? 290  LEU A CG  1 
ATOM   495  C  CD1 . LEU A 1 66  ? -14.111 19.226 8.731   1.00 31.87 ? 290  LEU A CD1 1 
ATOM   496  C  CD2 . LEU A 1 66  ? -13.375 17.421 7.257   1.00 30.98 ? 290  LEU A CD2 1 
ATOM   497  N  N   . GLN A 1 67  ? -12.095 21.768 10.463  1.00 31.02 ? 291  GLN A N   1 
ATOM   498  C  CA  . GLN A 1 67  ? -11.760 22.181 11.823  1.00 33.09 ? 291  GLN A CA  1 
ATOM   499  C  C   . GLN A 1 67  ? -12.072 21.080 12.831  1.00 39.86 ? 291  GLN A C   1 
ATOM   500  O  O   . GLN A 1 67  ? -11.237 20.742 13.682  1.00 37.22 ? 291  GLN A O   1 
ATOM   501  C  CB  . GLN A 1 67  ? -12.530 23.461 12.163  1.00 35.92 ? 291  GLN A CB  1 
ATOM   502  C  CG  . GLN A 1 67  ? -11.956 24.264 13.304  1.00 41.02 ? 291  GLN A CG  1 
ATOM   503  C  CD  . GLN A 1 67  ? -13.027 25.032 14.053  1.00 52.18 ? 291  GLN A CD  1 
ATOM   504  O  OE1 . GLN A 1 67  ? -13.953 24.441 14.611  1.00 52.53 ? 291  GLN A OE1 1 
ATOM   505  N  NE2 . GLN A 1 67  ? -12.910 26.357 14.065  1.00 59.44 ? 291  GLN A NE2 1 
ATOM   506  N  N   . ALA A 1 68  ? -13.263 20.497 12.739  1.00 36.46 ? 292  ALA A N   1 
ATOM   507  C  CA  . ALA A 1 68  ? -13.733 19.521 13.706  1.00 35.40 ? 292  ALA A CA  1 
ATOM   508  C  C   . ALA A 1 68  ? -14.989 18.864 13.155  1.00 38.78 ? 292  ALA A C   1 
ATOM   509  O  O   . ALA A 1 68  ? -15.665 19.423 12.283  1.00 34.27 ? 292  ALA A O   1 
ATOM   510  C  CB  . ALA A 1 68  ? -14.028 20.173 15.064  1.00 35.15 ? 292  ALA A CB  1 
ATOM   511  N  N   . GLU A 1 69  ? -15.269 17.652 13.645  0.92 36.76 ? 293  GLU A N   1 
ATOM   512  C  CA  . GLU A 1 69  ? -16.631 17.136 13.617  0.92 34.65 ? 293  GLU A CA  1 
ATOM   513  C  C   . GLU A 1 69  ? -17.430 17.905 14.652  0.92 39.13 ? 293  GLU A C   1 
ATOM   514  O  O   . GLU A 1 69  ? -16.994 18.043 15.799  0.92 41.89 ? 293  GLU A O   1 
ATOM   515  C  CB  . GLU A 1 69  ? -16.680 15.643 13.935  0.92 36.54 ? 293  GLU A CB  1 
ATOM   516  C  CG  . GLU A 1 69  ? -15.874 14.756 13.009  0.92 43.63 ? 293  GLU A CG  1 
ATOM   517  C  CD  . GLU A 1 69  ? -16.380 13.317 12.990  0.92 48.95 ? 293  GLU A CD  1 
ATOM   518  O  OE1 . GLU A 1 69  ? -17.295 12.989 13.782  0.92 46.55 ? 293  GLU A OE1 1 
ATOM   519  O  OE2 . GLU A 1 69  ? -15.866 12.517 12.171  0.92 53.94 ? 293  GLU A OE2 1 
ATOM   520  N  N   . VAL A 1 70  ? -18.580 18.432 14.253  1.00 40.41 ? 294  VAL A N   1 
ATOM   521  C  CA  . VAL A 1 70  ? -19.326 19.288 15.169  1.00 44.08 ? 294  VAL A CA  1 
ATOM   522  C  C   . VAL A 1 70  ? -19.760 18.437 16.356  1.00 48.79 ? 294  VAL A C   1 
ATOM   523  O  O   . VAL A 1 70  ? -20.386 17.382 16.171  1.00 45.63 ? 294  VAL A O   1 
ATOM   524  C  CB  . VAL A 1 70  ? -20.520 19.967 14.480  1.00 44.30 ? 294  VAL A CB  1 
ATOM   525  C  CG1 . VAL A 1 70  ? -21.172 20.956 15.438  1.00 43.64 ? 294  VAL A CG1 1 
ATOM   526  C  CG2 . VAL A 1 70  ? -20.065 20.684 13.225  1.00 33.59 ? 294  VAL A CG2 1 
ATOM   527  N  N   . PRO A 1 71  ? -19.403 18.832 17.578  1.00 54.39 ? 295  PRO A N   1 
ATOM   528  C  CA  . PRO A 1 71  ? -19.807 18.058 18.756  1.00 59.18 ? 295  PRO A CA  1 
ATOM   529  C  C   . PRO A 1 71  ? -21.319 17.946 18.869  1.00 56.92 ? 295  PRO A C   1 
ATOM   530  O  O   . PRO A 1 71  ? -22.055 18.907 18.639  1.00 54.42 ? 295  PRO A O   1 
ATOM   531  C  CB  . PRO A 1 71  ? -19.213 18.858 19.920  1.00 57.63 ? 295  PRO A CB  1 
ATOM   532  C  CG  . PRO A 1 71  ? -18.013 19.521 19.322  1.00 58.20 ? 295  PRO A CG  1 
ATOM   533  C  CD  . PRO A 1 71  ? -18.433 19.887 17.921  1.00 55.94 ? 295  PRO A CD  1 
ATOM   534  N  N   . GLY A 1 72  ? -21.773 16.758 19.224  1.00 57.93 ? 296  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 72  ? -23.198 16.464 19.321  1.00 58.95 ? 296  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 72  ? -23.817 16.037 18.016  1.00 57.15 ? 296  GLY A C   1 
ATOM   537  O  O   . GLY A 1 72  ? -24.535 15.039 17.960  1.00 59.73 ? 296  GLY A O   1 
ATOM   538  N  N   . GLN A 1 73  ? -23.527 16.766 16.948  1.00 55.86 ? 297  GLN A N   1 
ATOM   539  C  CA  . GLN A 1 73  ? -24.175 16.508 15.677  1.00 54.88 ? 297  GLN A CA  1 
ATOM   540  C  C   . GLN A 1 73  ? -23.705 15.186 15.081  1.00 60.48 ? 297  GLN A C   1 
ATOM   541  O  O   . GLN A 1 73  ? -22.664 14.628 15.446  1.00 60.86 ? 297  GLN A O   1 
ATOM   542  C  CB  . GLN A 1 73  ? -23.900 17.645 14.701  1.00 51.19 ? 297  GLN A CB  1 
ATOM   543  C  CG  . GLN A 1 73  ? -24.093 19.021 15.312  1.00 54.62 ? 297  GLN A CG  1 
ATOM   544  C  CD  . GLN A 1 73  ? -25.553 19.414 15.452  1.00 54.29 ? 297  GLN A CD  1 
ATOM   545  O  OE1 . GLN A 1 73  ? -26.426 18.873 14.764  1.00 49.35 ? 297  GLN A OE1 1 
ATOM   546  N  NE2 . GLN A 1 73  ? -25.823 20.367 16.344  1.00 44.83 ? 297  GLN A NE2 1 
ATOM   547  N  N   . HIS A 1 74  ? -24.502 14.683 14.151  1.00 60.89 ? 298  HIS A N   1 
ATOM   548  C  CA  . HIS A 1 74  ? -24.214 13.437 13.463  1.00 59.45 ? 298  HIS A CA  1 
ATOM   549  C  C   . HIS A 1 74  ? -23.640 13.791 12.099  1.00 51.98 ? 298  HIS A C   1 
ATOM   550  O  O   . HIS A 1 74  ? -24.331 14.391 11.270  1.00 49.82 ? 298  HIS A O   1 
ATOM   551  C  CB  . HIS A 1 74  ? -25.473 12.581 13.339  1.00 56.13 ? 298  HIS A CB  1 
ATOM   552  C  CG  . HIS A 1 74  ? -25.254 11.299 12.602  1.00 65.71 ? 298  HIS A CG  1 
ATOM   553  N  ND1 . HIS A 1 74  ? -25.460 11.177 11.243  1.00 63.69 ? 298  HIS A ND1 1 
ATOM   554  C  CD2 . HIS A 1 74  ? -24.835 10.084 13.031  1.00 66.11 ? 298  HIS A CD2 1 
ATOM   555  C  CE1 . HIS A 1 74  ? -25.182 9.941  10.868  1.00 68.25 ? 298  HIS A CE1 1 
ATOM   556  N  NE2 . HIS A 1 74  ? -24.798 9.258  11.933  1.00 72.32 ? 298  HIS A NE2 1 
ATOM   557  N  N   . GLN A 1 75  ? -22.368 13.443 11.885  1.00 49.08 ? 299  GLN A N   1 
ATOM   558  C  CA  . GLN A 1 75  ? -21.712 13.584 10.581  1.00 42.42 ? 299  GLN A CA  1 
ATOM   559  C  C   . GLN A 1 75  ? -21.868 14.999 10.021  1.00 38.84 ? 299  GLN A C   1 
ATOM   560  O  O   . GLN A 1 75  ? -22.166 15.200 8.841   1.00 33.31 ? 299  GLN A O   1 
ATOM   561  C  CB  . GLN A 1 75  ? -22.236 12.541 9.593   1.00 44.97 ? 299  GLN A CB  1 
ATOM   562  C  CG  . GLN A 1 75  ? -21.198 11.497 9.172   1.00 43.06 ? 299  GLN A CG  1 
ATOM   563  C  CD  . GLN A 1 75  ? -21.429 10.153 9.815   1.00 48.22 ? 299  GLN A CD  1 
ATOM   564  O  OE1 . GLN A 1 75  ? -21.944 10.071 10.929  1.00 60.49 ? 299  GLN A OE1 1 
ATOM   565  N  NE2 . GLN A 1 75  ? -21.057 9.084  9.115   1.00 48.07 ? 299  GLN A NE2 1 
ATOM   566  N  N   . LEU A 1 76  ? -21.694 15.986 10.896  1.00 38.52 ? 300  LEU A N   1 
ATOM   567  C  CA  . LEU A 1 76  ? -21.598 17.389 10.524  1.00 32.73 ? 300  LEU A CA  1 
ATOM   568  C  C   . LEU A 1 76  ? -20.158 17.825 10.714  1.00 32.62 ? 300  LEU A C   1 
ATOM   569  O  O   . LEU A 1 76  ? -19.557 17.540 11.755  1.00 36.52 ? 300  LEU A O   1 
ATOM   570  C  CB  . LEU A 1 76  ? -22.508 18.262 11.387  1.00 38.20 ? 300  LEU A CB  1 
ATOM   571  C  CG  . LEU A 1 76  ? -23.932 18.523 10.929  1.00 42.10 ? 300  LEU A CG  1 
ATOM   572  C  CD1 . LEU A 1 76  ? -24.489 19.717 11.713  1.00 41.66 ? 300  LEU A CD1 1 
ATOM   573  C  CD2 . LEU A 1 76  ? -23.961 18.793 9.445   1.00 33.35 ? 300  LEU A CD2 1 
ATOM   574  N  N   . TYR A 1 77  ? -19.613 18.524 9.727   1.00 28.70 ? 301  TYR A N   1 
ATOM   575  C  CA  . TYR A 1 77  ? -18.211 18.901 9.741   1.00 31.87 ? 301  TYR A CA  1 
ATOM   576  C  C   . TYR A 1 77  ? -18.081 20.410 9.653   1.00 29.54 ? 301  TYR A C   1 
ATOM   577  O  O   . TYR A 1 77  ? -18.760 21.050 8.844   1.00 28.59 ? 301  TYR A O   1 
ATOM   578  C  CB  . TYR A 1 77  ? -17.469 18.207 8.602   1.00 25.97 ? 301  TYR A CB  1 
ATOM   579  C  CG  . TYR A 1 77  ? -17.581 16.714 8.739   1.00 29.26 ? 301  TYR A CG  1 
ATOM   580  C  CD1 . TYR A 1 77  ? -16.720 16.013 9.567   1.00 27.70 ? 301  TYR A CD1 1 
ATOM   581  C  CD2 . TYR A 1 77  ? -18.583 16.011 8.081   1.00 25.02 ? 301  TYR A CD2 1 
ATOM   582  C  CE1 . TYR A 1 77  ? -16.826 14.638 9.707   1.00 34.80 ? 301  TYR A CE1 1 
ATOM   583  C  CE2 . TYR A 1 77  ? -18.690 14.639 8.209   1.00 33.42 ? 301  TYR A CE2 1 
ATOM   584  C  CZ  . TYR A 1 77  ? -17.808 13.961 9.028   1.00 31.54 ? 301  TYR A CZ  1 
ATOM   585  O  OH  . TYR A 1 77  ? -17.910 12.603 9.167   1.00 40.32 ? 301  TYR A OH  1 
ATOM   586  N  N   . GLN A 1 78  ? -17.212 20.964 10.490  1.00 30.37 ? 302  GLN A N   1 
ATOM   587  C  CA  . GLN A 1 78  ? -17.004 22.401 10.565  1.00 27.37 ? 302  GLN A CA  1 
ATOM   588  C  C   . GLN A 1 78  ? -15.840 22.777 9.657   1.00 32.50 ? 302  GLN A C   1 
ATOM   589  O  O   . GLN A 1 78  ? -14.709 22.327 9.870   1.00 30.66 ? 302  GLN A O   1 
ATOM   590  C  CB  . GLN A 1 78  ? -16.726 22.842 12.001  1.00 29.93 ? 302  GLN A CB  1 
ATOM   591  C  CG  . GLN A 1 78  ? -16.602 24.352 12.152  1.00 29.04 ? 302  GLN A CG  1 
ATOM   592  C  CD  . GLN A 1 78  ? -17.908 25.064 11.846  1.00 32.50 ? 302  GLN A CD  1 
ATOM   593  O  OE1 . GLN A 1 78  ? -18.908 24.876 12.546  1.00 31.08 ? 302  GLN A OE1 1 
ATOM   594  N  NE2 . GLN A 1 78  ? -17.913 25.866 10.782  1.00 29.12 ? 302  GLN A NE2 1 
ATOM   595  N  N   . LEU A 1 79  ? -16.125 23.574 8.635   1.00 25.11 ? 303  LEU A N   1 
ATOM   596  C  CA  . LEU A 1 79  ? -15.080 24.151 7.806   1.00 28.46 ? 303  LEU A CA  1 
ATOM   597  C  C   . LEU A 1 79  ? -14.686 25.515 8.350   1.00 34.35 ? 303  LEU A C   1 
ATOM   598  O  O   . LEU A 1 79  ? -15.544 26.300 8.768   1.00 30.09 ? 303  LEU A O   1 
ATOM   599  C  CB  . LEU A 1 79  ? -15.549 24.307 6.363   1.00 26.74 ? 303  LEU A CB  1 
ATOM   600  C  CG  . LEU A 1 79  ? -15.678 23.093 5.447   1.00 26.08 ? 303  LEU A CG  1 
ATOM   601  C  CD1 . LEU A 1 79  ? -16.134 23.576 4.091   1.00 26.26 ? 303  LEU A CD1 1 
ATOM   602  C  CD2 . LEU A 1 79  ? -14.348 22.373 5.341   1.00 24.69 ? 303  LEU A CD2 1 
ATOM   603  N  N   . GLN A 1 80  ? -13.383 25.787 8.349   1.00 31.04 ? 304  GLN A N   1 
ATOM   604  C  CA  . GLN A 1 80  ? -12.848 27.140 8.505   1.00 32.40 ? 304  GLN A CA  1 
ATOM   605  C  C   . GLN A 1 80  ? -12.332 27.580 7.136   1.00 28.30 ? 304  GLN A C   1 
ATOM   606  O  O   . GLN A 1 80  ? -11.255 27.165 6.700   1.00 29.27 ? 304  GLN A O   1 
ATOM   607  C  CB  . GLN A 1 80  ? -11.765 27.191 9.577   1.00 32.47 ? 304  GLN A CB  1 
ATOM   608  C  CG  . GLN A 1 80  ? -12.322 27.404 10.980  1.00 47.87 ? 304  GLN A CG  1 
ATOM   609  C  CD  . GLN A 1 80  ? -13.289 28.590 11.064  1.00 51.87 ? 304  GLN A CD  1 
ATOM   610  O  OE1 . GLN A 1 80  ? -14.448 28.437 11.475  1.00 51.64 ? 304  GLN A OE1 1 
ATOM   611  N  NE2 . GLN A 1 80  ? -12.814 29.778 10.678  1.00 46.36 ? 304  GLN A NE2 1 
ATOM   612  N  N   . LEU A 1 81  ? -13.118 28.411 6.461   1.00 30.25 ? 305  LEU A N   1 
ATOM   613  C  CA  . LEU A 1 81  ? -12.855 28.787 5.083   1.00 26.32 ? 305  LEU A CA  1 
ATOM   614  C  C   . LEU A 1 81  ? -11.584 29.602 4.942   1.00 26.80 ? 305  LEU A C   1 
ATOM   615  O  O   . LEU A 1 81  ? -11.209 30.382 5.819   1.00 27.23 ? 305  LEU A O   1 
ATOM   616  C  CB  . LEU A 1 81  ? -14.006 29.621 4.522   1.00 21.02 ? 305  LEU A CB  1 
ATOM   617  C  CG  . LEU A 1 81  ? -15.336 28.917 4.310   1.00 27.15 ? 305  LEU A CG  1 
ATOM   618  C  CD1 . LEU A 1 81  ? -16.313 29.863 3.624   1.00 23.75 ? 305  LEU A CD1 1 
ATOM   619  C  CD2 . LEU A 1 81  ? -15.134 27.622 3.514   1.00 20.02 ? 305  LEU A CD2 1 
ATOM   620  N  N   . THR A 1 82  ? -10.923 29.412 3.813   1.00 27.44 ? 306  THR A N   1 
ATOM   621  C  CA  . THR A 1 82  ? -10.103 30.452 3.220   1.00 28.39 ? 306  THR A CA  1 
ATOM   622  C  C   . THR A 1 82  ? -10.851 30.989 2.007   1.00 26.48 ? 306  THR A C   1 
ATOM   623  O  O   . THR A 1 82  ? -11.890 30.457 1.604   1.00 24.41 ? 306  THR A O   1 
ATOM   624  C  CB  . THR A 1 82  ? -8.712  29.926 2.821   1.00 27.94 ? 306  THR A CB  1 
ATOM   625  O  OG1 . THR A 1 82  ? -8.839  28.959 1.774   1.00 24.18 ? 306  THR A OG1 1 
ATOM   626  C  CG2 . THR A 1 82  ? -7.980  29.297 4.021   1.00 26.95 ? 306  THR A CG2 1 
ATOM   627  N  N   . ASN A 1 83  ? -10.329 32.068 1.436   1.00 28.73 ? 307  ASN A N   1 
ATOM   628  C  CA  . ASN A 1 83  ? -10.794 32.501 0.126   1.00 26.07 ? 307  ASN A CA  1 
ATOM   629  C  C   . ASN A 1 83  ? -10.367 31.481 -0.918  1.00 26.51 ? 307  ASN A C   1 
ATOM   630  O  O   . ASN A 1 83  ? -9.377  30.773 -0.744  1.00 28.80 ? 307  ASN A O   1 
ATOM   631  C  CB  . ASN A 1 83  ? -10.242 33.889 -0.202  1.00 28.46 ? 307  ASN A CB  1 
ATOM   632  C  CG  . ASN A 1 83  ? -11.047 34.988 0.452   1.00 32.32 ? 307  ASN A CG  1 
ATOM   633  O  OD1 . ASN A 1 83  ? -12.247 35.098 0.215   1.00 32.60 ? 307  ASN A OD1 1 
ATOM   634  N  ND2 . ASN A 1 83  ? -10.406 35.779 1.309   1.00 32.85 ? 307  ASN A ND2 1 
ATOM   635  N  N   . LEU A 1 84  ? -11.138 31.390 -2.003  1.00 28.49 ? 308  LEU A N   1 
ATOM   636  C  CA  . LEU A 1 84  ? -10.863 30.365 -3.006  1.00 28.67 ? 308  LEU A CA  1 
ATOM   637  C  C   . LEU A 1 84  ? -9.464  30.497 -3.605  1.00 30.08 ? 308  LEU A C   1 
ATOM   638  O  O   . LEU A 1 84  ? -8.917  29.499 -4.093  1.00 26.30 ? 308  LEU A O   1 
ATOM   639  C  CB  . LEU A 1 84  ? -11.941 30.402 -4.095  1.00 27.15 ? 308  LEU A CB  1 
ATOM   640  C  CG  . LEU A 1 84  ? -13.346 29.970 -3.622  1.00 24.35 ? 308  LEU A CG  1 
ATOM   641  C  CD1 . LEU A 1 84  ? -14.373 30.118 -4.725  1.00 20.17 ? 308  LEU A CD1 1 
ATOM   642  C  CD2 . LEU A 1 84  ? -13.346 28.532 -3.096  1.00 24.80 ? 308  LEU A CD2 1 
ATOM   643  N  N   . ASP A 1 85  ? -8.852  31.683 -3.537  1.00 28.52 ? 309  ASP A N   1 
ATOM   644  C  CA  . ASP A 1 85  ? -7.460  31.843 -3.947  1.00 33.64 ? 309  ASP A CA  1 
ATOM   645  C  C   . ASP A 1 85  ? -6.462  31.461 -2.851  1.00 35.16 ? 309  ASP A C   1 
ATOM   646  O  O   . ASP A 1 85  ? -5.263  31.702 -3.018  1.00 38.34 ? 309  ASP A O   1 
ATOM   647  C  CB  . ASP A 1 85  ? -7.203  33.285 -4.428  1.00 30.25 ? 309  ASP A CB  1 
ATOM   648  C  CG  . ASP A 1 85  ? -7.332  34.334 -3.321  1.00 36.03 ? 309  ASP A CG  1 
ATOM   649  O  OD1 . ASP A 1 85  ? -7.448  33.992 -2.122  1.00 34.94 ? 309  ASP A OD1 1 
ATOM   650  O  OD2 . ASP A 1 85  ? -7.312  35.536 -3.662  1.00 38.86 ? 309  ASP A OD2 1 
ATOM   651  N  N   . GLY A 1 86  ? -6.920  30.891 -1.736  1.00 34.17 ? 310  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 86  ? -6.049  30.498 -0.653  1.00 34.00 ? 310  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 86  ? -5.825  31.557 0.407   1.00 32.38 ? 310  GLY A C   1 
ATOM   654  O  O   . GLY A 1 86  ? -5.464  31.211 1.537   1.00 30.96 ? 310  GLY A O   1 
ATOM   655  N  N   . SER A 1 87  ? -6.037  32.831 0.080   1.00 33.36 ? 311  SER A N   1 
ATOM   656  C  CA  . SER A 1 87  ? -5.814  33.906 1.031   1.00 34.06 ? 311  SER A CA  1 
ATOM   657  C  C   . SER A 1 87  ? -6.811  33.820 2.186   1.00 35.08 ? 311  SER A C   1 
ATOM   658  O  O   . SER A 1 87  ? -7.885  33.225 2.056   1.00 34.20 ? 311  SER A O   1 
ATOM   659  C  CB  . SER A 1 87  ? -5.923  35.266 0.340   1.00 38.34 ? 311  SER A CB  1 
ATOM   660  O  OG  . SER A 1 87  ? -7.267  35.608 0.030   1.00 34.54 ? 311  SER A OG  1 
ATOM   661  N  N   . PRO A 1 88  ? -6.466  34.390 3.335   1.00 35.56 ? 312  PRO A N   1 
ATOM   662  C  CA  . PRO A 1 88  ? -7.383  34.354 4.477   1.00 34.16 ? 312  PRO A CA  1 
ATOM   663  C  C   . PRO A 1 88  ? -8.639  35.181 4.255   1.00 34.46 ? 312  PRO A C   1 
ATOM   664  O  O   . PRO A 1 88  ? -8.645  36.180 3.529   1.00 34.54 ? 312  PRO A O   1 
ATOM   665  C  CB  . PRO A 1 88  ? -6.544  34.917 5.635   1.00 38.64 ? 312  PRO A CB  1 
ATOM   666  C  CG  . PRO A 1 88  ? -5.336  35.534 5.004   1.00 39.99 ? 312  PRO A CG  1 
ATOM   667  C  CD  . PRO A 1 88  ? -5.107  34.807 3.724   1.00 39.86 ? 312  PRO A CD  1 
ATOM   668  N  N   . ILE A 1 89  ? -9.719  34.727 4.889   1.00 35.44 ? 313  ILE A N   1 
ATOM   669  C  CA  . ILE A 1 89  ? -10.991 35.443 4.891   1.00 36.70 ? 313  ILE A CA  1 
ATOM   670  C  C   . ILE A 1 89  ? -10.826 36.723 5.691   1.00 36.79 ? 313  ILE A C   1 
ATOM   671  O  O   . ILE A 1 89  ? -10.425 36.686 6.858   1.00 35.15 ? 313  ILE A O   1 
ATOM   672  C  CB  . ILE A 1 89  ? -12.110 34.577 5.489   1.00 29.92 ? 313  ILE A CB  1 
ATOM   673  C  CG1 . ILE A 1 89  ? -12.456 33.410 4.562   1.00 33.36 ? 313  ILE A CG1 1 
ATOM   674  C  CG2 . ILE A 1 89  ? -13.344 35.417 5.773   1.00 36.55 ? 313  ILE A CG2 1 
ATOM   675  C  CD1 . ILE A 1 89  ? -12.813 33.842 3.178   1.00 32.87 ? 313  ILE A CD1 1 
ATOM   676  N  N   . ASP A 1 90  ? -11.149 37.860 5.075   1.00 40.58 ? 314  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 90  ? -11.116 39.140 5.775   1.00 39.06 ? 314  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 90  ? -12.536 39.678 5.895   1.00 37.74 ? 314  ASP A C   1 
ATOM   679  O  O   . ASP A 1 90  ? -13.060 40.270 4.938   1.00 39.33 ? 314  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 90  ? -10.215 40.140 5.043   1.00 43.68 ? 314  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 90  ? -10.088 41.475 5.781   1.00 44.00 ? 314  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 90  ? -10.800 41.691 6.784   1.00 42.77 ? 314  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 90  ? -9.262  42.311 5.358   1.00 50.62 ? 314  ASP A OD2 1 
ATOM   684  N  N   . PRO A 1 91  ? -13.197 39.516 7.043   1.00 38.38 ? 315  PRO A N   1 
ATOM   685  C  CA  . PRO A 1 91  ? -14.594 39.969 7.157   1.00 38.59 ? 315  PRO A CA  1 
ATOM   686  C  C   . PRO A 1 91  ? -14.782 41.473 7.028   1.00 38.63 ? 315  PRO A C   1 
ATOM   687  O  O   . PRO A 1 91  ? -15.936 41.918 6.972   1.00 39.10 ? 315  PRO A O   1 
ATOM   688  C  CB  . PRO A 1 91  ? -15.018 39.473 8.549   1.00 36.91 ? 315  PRO A CB  1 
ATOM   689  C  CG  . PRO A 1 91  ? -13.744 39.150 9.264   1.00 40.36 ? 315  PRO A CG  1 
ATOM   690  C  CD  . PRO A 1 91  ? -12.758 38.750 8.220   1.00 41.81 ? 315  PRO A CD  1 
ATOM   691  N  N   . THR A 1 92  ? -13.712 42.268 6.984   1.00 38.52 ? 316  THR A N   1 
ATOM   692  C  CA  . THR A 1 92  ? -13.859 43.707 6.789   1.00 42.05 ? 316  THR A CA  1 
ATOM   693  C  C   . THR A 1 92  ? -13.847 44.104 5.318   1.00 41.72 ? 316  THR A C   1 
ATOM   694  O  O   . THR A 1 92  ? -14.016 45.290 5.013   1.00 38.96 ? 316  THR A O   1 
ATOM   695  C  CB  . THR A 1 92  ? -12.765 44.476 7.542   1.00 38.90 ? 316  THR A CB  1 
ATOM   696  O  OG1 . THR A 1 92  ? -11.482 44.178 6.979   1.00 44.54 ? 316  THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 92  ? -12.778 44.117 9.027   1.00 36.75 ? 316  THR A CG2 1 
ATOM   698  N  N   . ASP A 1 93  ? -13.655 43.145 4.408   1.00 36.60 ? 317  ASP A N   1 
ATOM   699  C  CA  . ASP A 1 93  ? -13.769 43.422 2.982   1.00 35.08 ? 317  ASP A CA  1 
ATOM   700  C  C   . ASP A 1 93  ? -15.142 43.995 2.663   1.00 34.28 ? 317  ASP A C   1 
ATOM   701  O  O   . ASP A 1 93  ? -16.134 43.680 3.320   1.00 34.02 ? 317  ASP A O   1 
ATOM   702  C  CB  . ASP A 1 93  ? -13.556 42.150 2.164   1.00 35.98 ? 317  ASP A CB  1 
ATOM   703  C  CG  . ASP A 1 93  ? -12.104 41.700 2.134   1.00 42.82 ? 317  ASP A CG  1 
ATOM   704  O  OD1 . ASP A 1 93  ? -11.253 42.356 2.775   1.00 45.05 ? 317  ASP A OD1 1 
ATOM   705  O  OD2 . ASP A 1 93  ? -11.819 40.693 1.456   1.00 43.17 ? 317  ASP A OD2 1 
ATOM   706  N  N   . ASP A 1 94  ? -15.198 44.824 1.623   1.00 31.74 ? 318  ASP A N   1 
ATOM   707  C  CA  . ASP A 1 94  ? -16.449 45.475 1.225   1.00 35.58 ? 318  ASP A CA  1 
ATOM   708  C  C   . ASP A 1 94  ? -17.259 44.596 0.279   1.00 32.46 ? 318  ASP A C   1 
ATOM   709  O  O   . ASP A 1 94  ? -17.738 45.039 -0.762  1.00 30.36 ? 318  ASP A O   1 
ATOM   710  C  CB  . ASP A 1 94  ? -16.160 46.829 0.590   1.00 36.98 ? 318  ASP A CB  1 
ATOM   711  C  CG  . ASP A 1 94  ? -15.310 47.715 1.469   1.00 45.72 ? 318  ASP A CG  1 
ATOM   712  O  OD1 . ASP A 1 94  ? -15.499 47.702 2.706   1.00 43.29 ? 318  ASP A OD1 1 
ATOM   713  O  OD2 . ASP A 1 94  ? -14.446 48.433 0.915   1.00 63.49 ? 318  ASP A OD2 1 
ATOM   714  N  N   . THR A 1 95  ? -17.401 43.326 0.636   1.00 33.00 ? 319  THR A N   1 
ATOM   715  C  CA  . THR A 1 95  ? -18.221 42.365 -0.081  1.00 28.55 ? 319  THR A CA  1 
ATOM   716  C  C   . THR A 1 95  ? -19.244 41.790 0.891   1.00 27.18 ? 319  THR A C   1 
ATOM   717  O  O   . THR A 1 95  ? -19.052 41.856 2.108   1.00 28.77 ? 319  THR A O   1 
ATOM   718  C  CB  . THR A 1 95  ? -17.362 41.239 -0.680  1.00 32.58 ? 319  THR A CB  1 
ATOM   719  O  OG1 . THR A 1 95  ? -16.660 40.557 0.363   1.00 30.42 ? 319  THR A OG1 1 
ATOM   720  C  CG2 . THR A 1 95  ? -16.353 41.802 -1.664  1.00 29.05 ? 319  THR A CG2 1 
ATOM   721  N  N   . PRO A 1 96  ? -20.360 41.252 0.399   1.00 26.27 ? 320  PRO A N   1 
ATOM   722  C  CA  . PRO A 1 96  ? -21.307 40.622 1.330   1.00 26.50 ? 320  PRO A CA  1 
ATOM   723  C  C   . PRO A 1 96  ? -20.741 39.356 1.941   1.00 25.73 ? 320  PRO A C   1 
ATOM   724  O  O   . PRO A 1 96  ? -21.122 38.988 3.058   1.00 25.99 ? 320  PRO A O   1 
ATOM   725  C  CB  . PRO A 1 96  ? -22.536 40.324 0.457   1.00 25.30 ? 320  PRO A CB  1 
ATOM   726  C  CG  . PRO A 1 96  ? -22.283 40.990 -0.860  1.00 24.78 ? 320  PRO A CG  1 
ATOM   727  C  CD  . PRO A 1 96  ? -20.818 41.191 -0.996  1.00 26.24 ? 320  PRO A CD  1 
ATOM   728  N  N   . GLY A 1 97  ? -19.838 38.690 1.231   1.00 26.69 ? 321  GLY A N   1 
ATOM   729  C  CA  . GLY A 1 97  ? -19.231 37.457 1.663   1.00 26.89 ? 321  GLY A CA  1 
ATOM   730  C  C   . GLY A 1 97  ? -18.037 37.188 0.773   1.00 27.24 ? 321  GLY A C   1 
ATOM   731  O  O   . GLY A 1 97  ? -17.722 37.988 -0.114  1.00 23.29 ? 321  GLY A O   1 
ATOM   732  N  N   . PRO A 1 98  ? -17.346 36.067 0.981   1.00 25.74 ? 322  PRO A N   1 
ATOM   733  C  CA  . PRO A 1 98  ? -16.167 35.775 0.152   1.00 24.50 ? 322  PRO A CA  1 
ATOM   734  C  C   . PRO A 1 98  ? -16.564 35.566 -1.300  1.00 20.06 ? 322  PRO A C   1 
ATOM   735  O  O   . PRO A 1 98  ? -17.682 35.149 -1.607  1.00 21.71 ? 322  PRO A O   1 
ATOM   736  C  CB  . PRO A 1 98  ? -15.595 34.494 0.778   1.00 26.58 ? 322  PRO A CB  1 
ATOM   737  C  CG  . PRO A 1 98  ? -16.711 33.903 1.558   1.00 24.03 ? 322  PRO A CG  1 
ATOM   738  C  CD  . PRO A 1 98  ? -17.611 35.021 1.983   1.00 22.11 ? 322  PRO A CD  1 
ATOM   739  N  N   . LEU A 1 99  ? -15.655 35.910 -2.209  1.00 21.53 ? 323  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 99  ? -15.991 35.808 -3.622  1.00 23.88 ? 323  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 99  ? -16.352 34.371 -3.973  1.00 23.22 ? 323  LEU A C   1 
ATOM   742  O  O   . LEU A 1 99  ? -15.813 33.418 -3.408  1.00 21.83 ? 323  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 99  ? -14.833 36.287 -4.503  1.00 23.27 ? 323  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 99  ? -14.364 37.727 -4.263  1.00 24.50 ? 323  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 99  ? -13.328 38.129 -5.326  1.00 26.38 ? 323  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 99  ? -15.556 38.684 -4.239  1.00 24.18 ? 323  LEU A CD2 1 
ATOM   747  N  N   . GLY A 1 100 ? -17.295 34.228 -4.902  1.00 21.83 ? 324  GLY A N   1 
ATOM   748  C  CA  . GLY A 1 100 ? -17.775 32.930 -5.335  1.00 21.06 ? 324  GLY A CA  1 
ATOM   749  C  C   . GLY A 1 100 ? -18.785 32.272 -4.420  1.00 21.81 ? 324  GLY A C   1 
ATOM   750  O  O   . GLY A 1 100 ? -19.259 31.174 -4.737  1.00 22.14 ? 324  GLY A O   1 
ATOM   751  N  N   . CYS A 1 101 ? -19.121 32.891 -3.295  1.00 23.04 ? 325  CYS A N   1 
ATOM   752  C  CA  . CYS A 1 101 ? -20.059 32.283 -2.366  1.00 19.45 ? 325  CYS A CA  1 
ATOM   753  C  C   . CYS A 1 101 ? -21.443 32.157 -3.012  1.00 22.05 ? 325  CYS A C   1 
ATOM   754  O  O   . CYS A 1 101 ? -21.863 33.055 -3.753  1.00 21.75 ? 325  CYS A O   1 
ATOM   755  C  CB  . CYS A 1 101 ? -20.126 33.138 -1.097  1.00 24.07 ? 325  CYS A CB  1 
ATOM   756  S  SG  . CYS A 1 101 ? -21.214 32.532 0.183   1.00 24.75 ? 325  CYS A SG  1 
ATOM   757  N  N   . PRO A 1 102 ? -22.171 31.058 -2.774  1.00 23.57 ? 326  PRO A N   1 
ATOM   758  C  CA  . PRO A 1 102 ? -23.533 30.945 -3.317  1.00 21.12 ? 326  PRO A CA  1 
ATOM   759  C  C   . PRO A 1 102 ? -24.387 32.141 -2.916  1.00 19.87 ? 326  PRO A C   1 
ATOM   760  O  O   . PRO A 1 102 ? -24.316 32.631 -1.788  1.00 20.14 ? 326  PRO A O   1 
ATOM   761  C  CB  . PRO A 1 102 ? -24.065 29.644 -2.693  1.00 22.81 ? 326  PRO A CB  1 
ATOM   762  C  CG  . PRO A 1 102 ? -22.877 28.867 -2.313  1.00 23.95 ? 326  PRO A CG  1 
ATOM   763  C  CD  . PRO A 1 102 ? -21.777 29.861 -2.009  1.00 20.35 ? 326  PRO A CD  1 
ATOM   764  N  N   . ASP A 1 103 ? -25.212 32.620 -3.844  1.00 20.32 ? 327  ASP A N   1 
ATOM   765  C  CA  . ASP A 1 103 ? -26.089 33.749 -3.557  1.00 19.14 ? 327  ASP A CA  1 
ATOM   766  C  C   . ASP A 1 103 ? -27.554 33.332 -3.511  1.00 21.36 ? 327  ASP A C   1 
ATOM   767  O  O   . ASP A 1 103 ? -28.436 34.148 -3.770  1.00 21.52 ? 327  ASP A O   1 
ATOM   768  C  CB  . ASP A 1 103 ? -25.892 34.869 -4.579  1.00 19.16 ? 327  ASP A CB  1 
ATOM   769  C  CG  . ASP A 1 103 ? -26.206 34.428 -5.991  1.00 21.21 ? 327  ASP A CG  1 
ATOM   770  O  OD1 . ASP A 1 103 ? -26.490 33.231 -6.181  1.00 21.39 ? 327  ASP A OD1 1 
ATOM   771  O  OD2 . ASP A 1 103 ? -26.163 35.264 -6.922  1.00 22.25 ? 327  ASP A OD2 1 
ATOM   772  N  N   . PHE A 1 104 ? -27.824 32.061 -3.219  1.00 21.23 ? 328  PHE A N   1 
ATOM   773  C  CA  . PHE A 1 104 ? -29.186 31.551 -3.122  1.00 23.10 ? 328  PHE A CA  1 
ATOM   774  C  C   . PHE A 1 104 ? -29.319 30.754 -1.832  1.00 21.73 ? 328  PHE A C   1 
ATOM   775  O  O   . PHE A 1 104 ? -28.326 30.344 -1.233  1.00 23.16 ? 328  PHE A O   1 
ATOM   776  C  CB  . PHE A 1 104 ? -29.541 30.677 -4.335  1.00 22.08 ? 328  PHE A CB  1 
ATOM   777  C  CG  . PHE A 1 104 ? -28.532 29.603 -4.614  1.00 21.55 ? 328  PHE A CG  1 
ATOM   778  C  CD1 . PHE A 1 104 ? -27.453 29.845 -5.460  1.00 21.76 ? 328  PHE A CD1 1 
ATOM   779  C  CD2 . PHE A 1 104 ? -28.646 28.356 -4.012  1.00 22.02 ? 328  PHE A CD2 1 
ATOM   780  C  CE1 . PHE A 1 104 ? -26.517 28.857 -5.709  1.00 21.29 ? 328  PHE A CE1 1 
ATOM   781  C  CE2 . PHE A 1 104 ? -27.714 27.362 -4.260  1.00 23.28 ? 328  PHE A CE2 1 
ATOM   782  C  CZ  . PHE A 1 104 ? -26.650 27.609 -5.107  1.00 22.30 ? 328  PHE A CZ  1 
ATOM   783  N  N   . THR A 1 105 ? -30.546 30.548 -1.381  1.00 23.12 ? 329  THR A N   1 
ATOM   784  C  CA  . THR A 1 105 ? -30.773 29.681 -0.236  1.00 24.67 ? 329  THR A CA  1 
ATOM   785  C  C   . THR A 1 105 ? -31.260 28.332 -0.741  1.00 25.16 ? 329  THR A C   1 
ATOM   786  O  O   . THR A 1 105 ? -32.123 28.263 -1.622  1.00 25.91 ? 329  THR A O   1 
ATOM   787  C  CB  . THR A 1 105 ? -31.773 30.272 0.766   1.00 28.17 ? 329  THR A CB  1 
ATOM   788  O  OG1 . THR A 1 105 ? -33.046 30.427 0.142   1.00 34.31 ? 329  THR A OG1 1 
ATOM   789  C  CG2 . THR A 1 105 ? -31.310 31.630 1.258   1.00 27.32 ? 329  THR A CG2 1 
ATOM   790  N  N   . GLY A 1 106 ? -30.691 27.270 -0.199  1.00 25.00 ? 330  GLY A N   1 
ATOM   791  C  CA  . GLY A 1 106 ? -31.104 25.936 -0.577  1.00 28.40 ? 330  GLY A CA  1 
ATOM   792  C  C   . GLY A 1 106 ? -30.133 24.929 -0.014  1.00 25.47 ? 330  GLY A C   1 
ATOM   793  O  O   . GLY A 1 106 ? -29.166 25.278 0.670   1.00 20.54 ? 330  GLY A O   1 
ATOM   794  N  N   . LEU A 1 107 ? -30.405 23.665 -0.324  1.00 24.72 ? 331  LEU A N   1 
ATOM   795  C  CA  . LEU A 1 107 ? -29.527 22.571 0.089   1.00 22.81 ? 331  LEU A CA  1 
ATOM   796  C  C   . LEU A 1 107 ? -28.576 22.290 -1.066  1.00 24.88 ? 331  LEU A C   1 
ATOM   797  O  O   . LEU A 1 107 ? -28.883 21.541 -1.992  1.00 24.42 ? 331  LEU A O   1 
ATOM   798  C  CB  . LEU A 1 107 ? -30.336 21.345 0.488   1.00 24.96 ? 331  LEU A CB  1 
ATOM   799  C  CG  . LEU A 1 107 ? -29.609 20.261 1.276   1.00 36.58 ? 331  LEU A CG  1 
ATOM   800  C  CD1 . LEU A 1 107 ? -28.961 20.842 2.528   1.00 33.06 ? 331  LEU A CD1 1 
ATOM   801  C  CD2 . LEU A 1 107 ? -30.594 19.149 1.645   1.00 38.82 ? 331  LEU A CD2 1 
ATOM   802  N  N   . LEU A 1 108 ? -27.406 22.917 -1.012  1.00 22.83 ? 332  LEU A N   1 
ATOM   803  C  CA  . LEU A 1 108 ? -26.406 22.794 -2.062  1.00 22.03 ? 332  LEU A CA  1 
ATOM   804  C  C   . LEU A 1 108 ? -25.734 21.428 -1.955  1.00 23.19 ? 332  LEU A C   1 
ATOM   805  O  O   . LEU A 1 108 ? -25.218 21.067 -0.892  1.00 21.26 ? 332  LEU A O   1 
ATOM   806  C  CB  . LEU A 1 108 ? -25.391 23.926 -1.936  1.00 22.12 ? 332  LEU A CB  1 
ATOM   807  C  CG  . LEU A 1 108 ? -24.187 23.972 -2.884  1.00 18.61 ? 332  LEU A CG  1 
ATOM   808  C  CD1 . LEU A 1 108 ? -24.610 24.071 -4.342  1.00 17.83 ? 332  LEU A CD1 1 
ATOM   809  C  CD2 . LEU A 1 108 ? -23.356 25.166 -2.500  1.00 19.58 ? 332  LEU A CD2 1 
ATOM   810  N  N   . TYR A 1 109 ? -25.756 20.665 -3.047  1.00 21.20 ? 333  TYR A N   1 
ATOM   811  C  CA  . TYR A 1 109 ? -25.247 19.301 -3.070  1.00 22.47 ? 333  TYR A CA  1 
ATOM   812  C  C   . TYR A 1 109 ? -23.955 19.230 -3.871  1.00 23.57 ? 333  TYR A C   1 
ATOM   813  O  O   . TYR A 1 109 ? -23.829 19.856 -4.926  1.00 20.68 ? 333  TYR A O   1 
ATOM   814  C  CB  . TYR A 1 109 ? -26.291 18.353 -3.662  1.00 24.73 ? 333  TYR A CB  1 
ATOM   815  C  CG  . TYR A 1 109 ? -25.786 16.986 -4.062  1.00 21.56 ? 333  TYR A CG  1 
ATOM   816  C  CD1 . TYR A 1 109 ? -25.698 15.957 -3.136  1.00 22.63 ? 333  TYR A CD1 1 
ATOM   817  C  CD2 . TYR A 1 109 ? -25.431 16.718 -5.377  1.00 22.24 ? 333  TYR A CD2 1 
ATOM   818  C  CE1 . TYR A 1 109 ? -25.250 14.689 -3.513  1.00 24.91 ? 333  TYR A CE1 1 
ATOM   819  C  CE2 . TYR A 1 109 ? -24.980 15.466 -5.761  1.00 21.15 ? 333  TYR A CE2 1 
ATOM   820  C  CZ  . TYR A 1 109 ? -24.898 14.457 -4.826  1.00 25.13 ? 333  TYR A CZ  1 
ATOM   821  O  OH  . TYR A 1 109 ? -24.463 13.210 -5.216  1.00 30.04 ? 333  TYR A OH  1 
ATOM   822  N  N   . GLY A 1 110 ? -23.005 18.442 -3.374  1.00 23.62 ? 334  GLY A N   1 
ATOM   823  C  CA  . GLY A 1 110 ? -21.735 18.309 -4.048  1.00 20.60 ? 334  GLY A CA  1 
ATOM   824  C  C   . GLY A 1 110 ? -20.836 17.282 -3.401  1.00 20.78 ? 334  GLY A C   1 
ATOM   825  O  O   . GLY A 1 110 ? -21.311 16.353 -2.744  1.00 21.69 ? 334  GLY A O   1 
ATOM   826  N  N   . VAL A 1 111 ? -19.529 17.438 -3.577  1.00 22.46 ? 335  VAL A N   1 
ATOM   827  C  CA  . VAL A 1 111 ? -18.550 16.479 -3.077  1.00 21.82 ? 335  VAL A CA  1 
ATOM   828  C  C   . VAL A 1 111 ? -17.498 17.231 -2.275  1.00 19.12 ? 335  VAL A C   1 
ATOM   829  O  O   . VAL A 1 111 ? -16.874 18.169 -2.787  1.00 20.48 ? 335  VAL A O   1 
ATOM   830  C  CB  . VAL A 1 111 ? -17.896 15.686 -4.219  1.00 23.72 ? 335  VAL A CB  1 
ATOM   831  C  CG1 . VAL A 1 111 ? -16.722 14.883 -3.695  1.00 20.68 ? 335  VAL A CG1 1 
ATOM   832  C  CG2 . VAL A 1 111 ? -18.940 14.770 -4.882  1.00 20.82 ? 335  VAL A CG2 1 
ATOM   833  N  N   . ALA A 1 112 ? -17.307 16.822 -1.026  1.00 21.49 ? 336  ALA A N   1 
ATOM   834  C  CA  . ALA A 1 112 ? -16.211 17.311 -0.202  1.00 22.53 ? 336  ALA A CA  1 
ATOM   835  C  C   . ALA A 1 112 ? -15.032 16.363 -0.355  1.00 22.86 ? 336  ALA A C   1 
ATOM   836  O  O   . ALA A 1 112 ? -15.189 15.146 -0.204  1.00 21.57 ? 336  ALA A O   1 
ATOM   837  C  CB  . ALA A 1 112 ? -16.625 17.406 1.267   1.00 20.44 ? 336  ALA A CB  1 
ATOM   838  N  N   . SER A 1 113 ? -13.861 16.916 -0.672  1.00 19.13 ? 337  SER A N   1 
ATOM   839  C  CA  . SER A 1 113 ? -12.664 16.117 -0.879  1.00 20.72 ? 337  SER A CA  1 
ATOM   840  C  C   . SER A 1 113 ? -11.535 16.667 -0.027  1.00 22.06 ? 337  SER A C   1 
ATOM   841  O  O   . SER A 1 113 ? -11.520 17.850 0.322   1.00 22.29 ? 337  SER A O   1 
ATOM   842  C  CB  . SER A 1 113 ? -12.235 16.092 -2.354  1.00 19.03 ? 337  SER A CB  1 
ATOM   843  O  OG  . SER A 1 113 ? -12.030 17.405 -2.845  1.00 20.86 ? 337  SER A OG  1 
ATOM   844  N  N   . GLN A 1 114 ? -10.595 15.789 0.320   1.00 23.66 ? 338  GLN A N   1 
ATOM   845  C  CA  . GLN A 1 114 ? -9.419  16.172 1.081   1.00 23.87 ? 338  GLN A CA  1 
ATOM   846  C  C   . GLN A 1 114 ? -8.181  15.574 0.438   1.00 24.59 ? 338  GLN A C   1 
ATOM   847  O  O   . GLN A 1 114 ? -8.246  14.553 -0.249  1.00 22.28 ? 338  GLN A O   1 
ATOM   848  C  CB  . GLN A 1 114 ? -9.475  15.696 2.529   1.00 21.99 ? 338  GLN A CB  1 
ATOM   849  C  CG  . GLN A 1 114 ? -10.682 16.132 3.324   1.00 25.27 ? 338  GLN A CG  1 
ATOM   850  C  CD  . GLN A 1 114 ? -10.578 15.651 4.760   1.00 29.93 ? 338  GLN A CD  1 
ATOM   851  O  OE1 . GLN A 1 114 ? -10.341 14.465 5.016   1.00 27.36 ? 338  GLN A OE1 1 
ATOM   852  N  NE2 . GLN A 1 114 ? -10.711 16.569 5.699   1.00 24.23 ? 338  GLN A NE2 1 
ATOM   853  N  N   . ARG A 1 115 ? -7.044  16.220 0.685   1.00 23.01 ? 339  ARG A N   1 
ATOM   854  C  CA  . ARG A 1 115 ? -5.739  15.638 0.396   1.00 25.48 ? 339  ARG A CA  1 
ATOM   855  C  C   . ARG A 1 115 ? -4.865  15.870 1.613   1.00 27.37 ? 339  ARG A C   1 
ATOM   856  O  O   . ARG A 1 115 ? -4.691  17.013 2.046   1.00 23.68 ? 339  ARG A O   1 
ATOM   857  C  CB  . ARG A 1 115 ? -5.104  16.241 -0.862  1.00 27.64 ? 339  ARG A CB  1 
ATOM   858  C  CG  . ARG A 1 115 ? -3.697  15.708 -1.160  1.00 25.61 ? 339  ARG A CG  1 
ATOM   859  C  CD  . ARG A 1 115 ? -3.169  16.205 -2.514  1.00 29.82 ? 339  ARG A CD  1 
ATOM   860  N  NE  . ARG A 1 115 ? -3.678  15.402 -3.623  1.00 30.31 ? 339  ARG A NE  1 
ATOM   861  C  CZ  . ARG A 1 115 ? -4.646  15.766 -4.454  1.00 25.31 ? 339  ARG A CZ  1 
ATOM   862  N  NH1 . ARG A 1 115 ? -5.218  16.956 -4.376  1.00 25.11 ? 339  ARG A NH1 1 
ATOM   863  N  NH2 . ARG A 1 115 ? -5.043  14.917 -5.394  1.00 22.33 ? 339  ARG A NH2 1 
ATOM   864  N  N   . GLY A 1 116 ? -4.322  14.792 2.168   1.00 26.79 ? 340  GLY A N   1 
ATOM   865  C  CA  . GLY A 1 116 ? -3.600  14.873 3.408   1.00 27.34 ? 340  GLY A CA  1 
ATOM   866  C  C   . GLY A 1 116 ? -4.078  13.808 4.369   1.00 32.37 ? 340  GLY A C   1 
ATOM   867  O  O   . GLY A 1 116 ? -5.229  13.366 4.303   1.00 30.38 ? 340  GLY A O   1 
ATOM   868  N  N   . PRO A 1 117 ? -3.183  13.335 5.258   1.00 35.00 ? 341  PRO A N   1 
ATOM   869  C  CA  . PRO A 1 117 ? -1.750  13.675 5.341   1.00 37.98 ? 341  PRO A CA  1 
ATOM   870  C  C   . PRO A 1 117 ? -0.991  13.147 4.125   1.00 36.13 ? 341  PRO A C   1 
ATOM   871  O  O   . PRO A 1 117 ? -1.384  12.136 3.541   1.00 37.80 ? 341  PRO A O   1 
ATOM   872  C  CB  . PRO A 1 117 ? -1.308  13.009 6.656   1.00 37.72 ? 341  PRO A CB  1 
ATOM   873  C  CG  . PRO A 1 117 ? -2.286  11.887 6.866   1.00 34.89 ? 341  PRO A CG  1 
ATOM   874  C  CD  . PRO A 1 117 ? -3.591  12.398 6.319   1.00 35.56 ? 341  PRO A CD  1 
ATOM   875  N  N   . GLY A 1 118 ? 0.078   13.824 3.709   1.00 37.40 ? 342  GLY A N   1 
ATOM   876  C  CA  . GLY A 1 118 ? 0.769   13.428 2.493   1.00 32.80 ? 342  GLY A CA  1 
ATOM   877  C  C   . GLY A 1 118 ? -0.149  13.540 1.296   1.00 30.90 ? 342  GLY A C   1 
ATOM   878  O  O   . GLY A 1 118 ? -0.957  14.470 1.189   1.00 30.83 ? 342  GLY A O   1 
ATOM   879  N  N   . ASP A 1 119 ? -0.057  12.561 0.391   1.00 32.83 ? 343  ASP A N   1 
ATOM   880  C  CA  . ASP A 1 119 ? -0.912  12.512 -0.790  1.00 30.35 ? 343  ASP A CA  1 
ATOM   881  C  C   . ASP A 1 119 ? -2.089  11.543 -0.632  1.00 29.46 ? 343  ASP A C   1 
ATOM   882  O  O   . ASP A 1 119 ? -2.718  11.164 -1.631  1.00 30.85 ? 343  ASP A O   1 
ATOM   883  C  CB  . ASP A 1 119 ? -0.082  12.162 -2.027  1.00 33.07 ? 343  ASP A CB  1 
ATOM   884  C  CG  . ASP A 1 119 ? 0.547   10.778 -1.944  1.00 35.49 ? 343  ASP A CG  1 
ATOM   885  O  OD1 . ASP A 1 119 ? 0.757   10.271 -0.817  1.00 38.63 ? 343  ASP A OD1 1 
ATOM   886  O  OD2 . ASP A 1 119 ? 0.837   10.200 -3.013  1.00 38.90 ? 343  ASP A OD2 1 
ATOM   887  N  N   . ALA A 1 120 ? -2.383  11.122 0.596   1.00 28.24 ? 344  ALA A N   1 
ATOM   888  C  CA  . ALA A 1 120 ? -3.613  10.392 0.879   1.00 30.54 ? 344  ALA A CA  1 
ATOM   889  C  C   . ALA A 1 120 ? -4.828  11.256 0.548   1.00 27.87 ? 344  ALA A C   1 
ATOM   890  O  O   . ALA A 1 120 ? -4.904  12.415 0.966   1.00 24.17 ? 344  ALA A O   1 
ATOM   891  C  CB  . ALA A 1 120 ? -3.638  9.988  2.354   1.00 30.21 ? 344  ALA A CB  1 
ATOM   892  N  N   . THR A 1 121 ? -5.774  10.705 -0.214  1.00 25.28 ? 345  THR A N   1 
ATOM   893  C  CA  . THR A 1 121 ? -6.959  11.457 -0.625  1.00 26.07 ? 345  THR A CA  1 
ATOM   894  C  C   . THR A 1 121 ? -8.238  10.710 -0.258  1.00 27.85 ? 345  THR A C   1 
ATOM   895  O  O   . THR A 1 121 ? -8.233  9.505  0.005   1.00 28.30 ? 345  THR A O   1 
ATOM   896  C  CB  . THR A 1 121 ? -6.966  11.753 -2.141  1.00 27.37 ? 345  THR A CB  1 
ATOM   897  O  OG1 . THR A 1 121 ? -7.159  10.531 -2.873  1.00 26.67 ? 345  THR A OG1 1 
ATOM   898  C  CG2 . THR A 1 121 ? -5.656  12.431 -2.583  1.00 26.19 ? 345  THR A CG2 1 
ATOM   899  N  N   . ARG A 1 122 ? -9.348  11.453 -0.262  1.00 29.05 ? 346  ARG A N   1 
ATOM   900  C  CA  . ARG A 1 122 ? -10.674 10.910 -0.004  1.00 24.68 ? 346  ARG A CA  1 
ATOM   901  C  C   . ARG A 1 122 ? -11.706 11.959 -0.393  1.00 24.38 ? 346  ARG A C   1 
ATOM   902  O  O   . ARG A 1 122 ? -11.476 13.156 -0.222  1.00 25.06 ? 346  ARG A O   1 
ATOM   903  C  CB  . ARG A 1 122 ? -10.835 10.512 1.469   1.00 25.62 ? 346  ARG A CB  1 
ATOM   904  C  CG  . ARG A 1 122 ? -10.779 11.699 2.448   1.00 23.60 ? 346  ARG A CG  1 
ATOM   905  C  CD  . ARG A 1 122 ? -10.473 11.241 3.869   1.00 29.20 ? 346  ARG A CD  1 
ATOM   906  N  NE  . ARG A 1 122 ? -9.132  10.670 3.963   1.00 28.84 ? 346  ARG A NE  1 
ATOM   907  C  CZ  . ARG A 1 122 ? -8.024  11.390 4.058   1.00 30.61 ? 346  ARG A CZ  1 
ATOM   908  N  NH1 . ARG A 1 122 ? -8.062  12.713 4.128   1.00 33.16 ? 346  ARG A NH1 1 
ATOM   909  N  NH2 . ARG A 1 122 ? -6.847  10.770 4.075   1.00 31.62 ? 346  ARG A NH2 1 
ATOM   910  N  N   . ALA A 1 123 ? -12.841 11.501 -0.916  1.00 25.61 ? 347  ALA A N   1 
ATOM   911  C  CA  . ALA A 1 123 ? -13.926 12.393 -1.311  1.00 23.51 ? 347  ALA A CA  1 
ATOM   912  C  C   . ALA A 1 123 ? -15.264 11.691 -1.107  1.00 27.69 ? 347  ALA A C   1 
ATOM   913  O  O   . ALA A 1 123 ? -15.373 10.484 -1.340  1.00 22.66 ? 347  ALA A O   1 
ATOM   914  C  CB  . ALA A 1 123 ? -13.778 12.819 -2.771  1.00 24.22 ? 347  ALA A CB  1 
ATOM   915  N  N   . HIS A 1 124 ? -16.276 12.442 -0.661  1.00 23.21 ? 348  HIS A N   1 
ATOM   916  C  CA  . HIS A 1 124 ? -17.609 11.885 -0.481  1.00 24.72 ? 348  HIS A CA  1 
ATOM   917  C  C   . HIS A 1 124 ? -18.650 12.964 -0.726  1.00 27.11 ? 348  HIS A C   1 
ATOM   918  O  O   . HIS A 1 124 ? -18.394 14.151 -0.508  1.00 22.74 ? 348  HIS A O   1 
ATOM   919  C  CB  . HIS A 1 124 ? -17.803 11.301 0.923   1.00 25.47 ? 348  HIS A CB  1 
ATOM   920  C  CG  . HIS A 1 124 ? -16.700 10.391 1.346   1.00 27.66 ? 348  HIS A CG  1 
ATOM   921  N  ND1 . HIS A 1 124 ? -16.576 9.106  0.865   1.00 27.85 ? 348  HIS A ND1 1 
ATOM   922  C  CD2 . HIS A 1 124 ? -15.640 10.593 2.166   1.00 28.21 ? 348  HIS A CD2 1 
ATOM   923  C  CE1 . HIS A 1 124 ? -15.498 8.548  1.388   1.00 33.14 ? 348  HIS A CE1 1 
ATOM   924  N  NE2 . HIS A 1 124 ? -14.914 9.429  2.182   1.00 28.63 ? 348  HIS A NE2 1 
ATOM   925  N  N   . GLU A 1 125 ? -19.831 12.534 -1.174  1.00 28.37 ? 349  GLU A N   1 
ATOM   926  C  CA  . GLU A 1 125 ? -20.960 13.444 -1.312  1.00 25.01 ? 349  GLU A CA  1 
ATOM   927  C  C   . GLU A 1 125 ? -21.168 14.236 -0.027  1.00 26.97 ? 349  GLU A C   1 
ATOM   928  O  O   . GLU A 1 125 ? -20.928 13.749 1.084   1.00 24.54 ? 349  GLU A O   1 
ATOM   929  C  CB  . GLU A 1 125 ? -22.235 12.678 -1.655  1.00 26.51 ? 349  GLU A CB  1 
ATOM   930  C  CG  . GLU A 1 125 ? -22.369 12.266 -3.110  1.00 32.44 ? 349  GLU A CG  1 
ATOM   931  C  CD  . GLU A 1 125 ? -23.326 11.089 -3.267  1.00 38.26 ? 349  GLU A CD  1 
ATOM   932  O  OE1 . GLU A 1 125 ? -23.239 10.161 -2.440  1.00 40.63 ? 349  GLU A OE1 1 
ATOM   933  O  OE2 . GLU A 1 125 ? -24.170 11.100 -4.194  1.00 33.33 ? 349  GLU A OE2 1 
ATOM   934  N  N   . ALA A 1 126 ? -21.616 15.476 -0.192  1.00 23.59 ? 350  ALA A N   1 
ATOM   935  C  CA  . ALA A 1 126 ? -21.782 16.380 0.929   1.00 25.31 ? 350  ALA A CA  1 
ATOM   936  C  C   . ALA A 1 126 ? -22.866 17.379 0.563   1.00 25.44 ? 350  ALA A C   1 
ATOM   937  O  O   . ALA A 1 126 ? -23.152 17.596 -0.615  1.00 21.80 ? 350  ALA A O   1 
ATOM   938  C  CB  . ALA A 1 126 ? -20.465 17.086 1.264   1.00 23.70 ? 350  ALA A CB  1 
ATOM   939  N  N   . ARG A 1 127 ? -23.499 17.966 1.573   1.00 24.16 ? 351  ARG A N   1 
ATOM   940  C  CA  A ARG A 1 127 ? -24.485 19.008 1.329   0.36 27.11 ? 351  ARG A CA  1 
ATOM   941  C  CA  B ARG A 1 127 ? -24.437 19.036 1.297   0.64 27.51 ? 351  ARG A CA  1 
ATOM   942  C  C   . ARG A 1 127 ? -24.332 20.122 2.356   1.00 24.80 ? 351  ARG A C   1 
ATOM   943  O  O   . ARG A 1 127 ? -24.009 19.868 3.519   1.00 23.95 ? 351  ARG A O   1 
ATOM   944  C  CB  A ARG A 1 127 ? -25.924 18.455 1.337   0.36 29.51 ? 351  ARG A CB  1 
ATOM   945  C  CB  B ARG A 1 127 ? -25.884 18.534 1.168   0.64 29.53 ? 351  ARG A CB  1 
ATOM   946  C  CG  A ARG A 1 127 ? -26.289 17.529 2.482   0.36 33.54 ? 351  ARG A CG  1 
ATOM   947  C  CG  B ARG A 1 127 ? -26.363 17.533 2.171   0.64 33.48 ? 351  ARG A CG  1 
ATOM   948  C  CD  A ARG A 1 127 ? -27.666 16.900 2.219   0.36 38.25 ? 351  ARG A CD  1 
ATOM   949  C  CD  B ARG A 1 127 ? -27.732 17.032 1.703   0.64 38.34 ? 351  ARG A CD  1 
ATOM   950  N  NE  A ARG A 1 127 ? -28.083 15.944 3.240   0.36 41.43 ? 351  ARG A NE  1 
ATOM   951  N  NE  B ARG A 1 127 ? -28.502 16.355 2.740   0.64 42.07 ? 351  ARG A NE  1 
ATOM   952  C  CZ  A ARG A 1 127 ? -29.031 16.168 4.142   0.36 41.03 ? 351  ARG A CZ  1 
ATOM   953  C  CZ  B ARG A 1 127 ? -28.707 15.045 2.783   0.64 40.27 ? 351  ARG A CZ  1 
ATOM   954  N  NH1 A ARG A 1 127 ? -29.679 17.319 4.193   0.36 42.26 ? 351  ARG A NH1 1 
ATOM   955  N  NH1 B ARG A 1 127 ? -28.196 14.237 1.869   0.64 37.36 ? 351  ARG A NH1 1 
ATOM   956  N  NH2 A ARG A 1 127 ? -29.339 15.211 5.012   0.36 43.10 ? 351  ARG A NH2 1 
ATOM   957  N  NH2 B ARG A 1 127 ? -29.447 14.537 3.764   0.64 41.45 ? 351  ARG A NH2 1 
ATOM   958  N  N   . ILE A 1 128 ? -24.583 21.350 1.908   1.00 23.99 ? 352  ILE A N   1 
ATOM   959  C  CA  . ILE A 1 128 ? -24.468 22.558 2.717   1.00 23.56 ? 352  ILE A CA  1 
ATOM   960  C  C   . ILE A 1 128 ? -25.794 23.297 2.635   1.00 24.01 ? 352  ILE A C   1 
ATOM   961  O  O   . ILE A 1 128 ? -26.226 23.672 1.538   1.00 24.54 ? 352  ILE A O   1 
ATOM   962  C  CB  . ILE A 1 128 ? -23.328 23.463 2.225   1.00 25.01 ? 352  ILE A CB  1 
ATOM   963  C  CG1 . ILE A 1 128 ? -21.973 22.781 2.403   1.00 20.94 ? 352  ILE A CG1 1 
ATOM   964  C  CG2 . ILE A 1 128 ? -23.360 24.823 2.926   1.00 21.14 ? 352  ILE A CG2 1 
ATOM   965  C  CD1 . ILE A 1 128 ? -20.918 23.383 1.514   1.00 20.81 ? 352  ILE A CD1 1 
ATOM   966  N  N   . ASP A 1 129 ? -26.428 23.526 3.782   1.00 21.48 ? 353  ASP A N   1 
ATOM   967  C  CA  . ASP A 1 129 ? -27.696 24.254 3.818   1.00 23.92 ? 353  ASP A CA  1 
ATOM   968  C  C   . ASP A 1 129 ? -27.377 25.744 3.889   1.00 22.40 ? 353  ASP A C   1 
ATOM   969  O  O   . ASP A 1 129 ? -26.994 26.261 4.943   1.00 24.11 ? 353  ASP A O   1 
ATOM   970  C  CB  . ASP A 1 129 ? -28.544 23.788 4.996   1.00 26.06 ? 353  ASP A CB  1 
ATOM   971  C  CG  . ASP A 1 129 ? -29.972 24.326 4.941   1.00 32.06 ? 353  ASP A CG  1 
ATOM   972  O  OD1 . ASP A 1 129 ? -30.209 25.357 4.278   1.00 24.23 ? 353  ASP A OD1 1 
ATOM   973  O  OD2 . ASP A 1 129 ? -30.860 23.714 5.566   1.00 33.11 ? 353  ASP A OD2 1 
ATOM   974  N  N   . THR A 1 130 ? -27.516 26.448 2.762   1.00 20.96 ? 354  THR A N   1 
ATOM   975  C  CA  . THR A 1 130 ? -27.135 27.853 2.789   1.00 23.92 ? 354  THR A CA  1 
ATOM   976  C  C   . THR A 1 130 ? -28.153 28.710 3.520   1.00 22.81 ? 354  THR A C   1 
ATOM   977  O  O   . THR A 1 130 ? -27.885 29.894 3.734   1.00 25.02 ? 354  THR A O   1 
ATOM   978  C  CB  . THR A 1 130 ? -26.908 28.411 1.378   1.00 24.75 ? 354  THR A CB  1 
ATOM   979  O  OG1 . THR A 1 130 ? -28.137 28.425 0.651   1.00 21.32 ? 354  THR A OG1 1 
ATOM   980  C  CG2 . THR A 1 130 ? -25.872 27.592 0.630   1.00 19.64 ? 354  THR A CG2 1 
ATOM   981  N  N   . GLY A 1 131 ? -29.283 28.137 3.939   1.00 25.97 ? 355  GLY A N   1 
ATOM   982  C  CA  . GLY A 1 131 ? -30.249 28.822 4.769   1.00 26.88 ? 355  GLY A CA  1 
ATOM   983  C  C   . GLY A 1 131 ? -30.118 28.552 6.250   1.00 30.61 ? 355  GLY A C   1 
ATOM   984  O  O   . GLY A 1 131 ? -30.873 29.129 7.040   1.00 28.64 ? 355  GLY A O   1 
ATOM   985  N  N   . SER A 1 132 ? -29.183 27.692 6.652   1.00 24.72 ? 356  SER A N   1 
ATOM   986  C  CA  . SER A 1 132 ? -28.978 27.379 8.057   1.00 31.40 ? 356  SER A CA  1 
ATOM   987  C  C   . SER A 1 132 ? -28.400 28.570 8.804   1.00 28.96 ? 356  SER A C   1 
ATOM   988  O  O   . SER A 1 132 ? -27.621 29.352 8.258   1.00 25.56 ? 356  SER A O   1 
ATOM   989  C  CB  . SER A 1 132 ? -28.023 26.194 8.208   1.00 31.70 ? 356  SER A CB  1 
ATOM   990  O  OG  . SER A 1 132 ? -27.407 26.226 9.487   1.00 36.88 ? 356  SER A OG  1 
ATOM   991  N  N   . ASP A 1 133 ? -28.749 28.680 10.088  1.00 34.46 ? 357  ASP A N   1 
ATOM   992  C  CA  . ASP A 1 133 ? -28.238 29.814 10.848  1.00 38.98 ? 357  ASP A CA  1 
ATOM   993  C  C   . ASP A 1 133 ? -26.744 29.694 11.134  1.00 38.41 ? 357  ASP A C   1 
ATOM   994  O  O   . ASP A 1 133 ? -26.118 30.705 11.474  1.00 35.87 ? 357  ASP A O   1 
ATOM   995  C  CB  . ASP A 1 133 ? -29.041 30.006 12.144  1.00 41.55 ? 357  ASP A CB  1 
ATOM   996  C  CG  . ASP A 1 133 ? -28.907 28.840 13.107  1.00 47.65 ? 357  ASP A CG  1 
ATOM   997  O  OD1 . ASP A 1 133 ? -28.680 27.693 12.651  1.00 47.44 ? 357  ASP A OD1 1 
ATOM   998  O  OD2 . ASP A 1 133 ? -29.044 29.073 14.329  1.00 47.37 ? 357  ASP A OD2 1 
ATOM   999  N  N   . THR A 1 134 ? -26.156 28.501 10.966  1.00 35.58 ? 358  THR A N   1 
ATOM   1000 C  CA  . THR A 1 134 ? -24.709 28.307 11.063  1.00 33.21 ? 358  THR A CA  1 
ATOM   1001 C  C   . THR A 1 134 ? -23.968 28.716 9.792   1.00 32.32 ? 358  THR A C   1 
ATOM   1002 O  O   . THR A 1 134 ? -22.741 28.852 9.818   1.00 34.09 ? 358  THR A O   1 
ATOM   1003 C  CB  . THR A 1 134 ? -24.385 26.838 11.390  1.00 33.10 ? 358  THR A CB  1 
ATOM   1004 O  OG1 . THR A 1 134 ? -24.685 26.007 10.259  1.00 36.71 ? 358  THR A OG1 1 
ATOM   1005 C  CG2 . THR A 1 134 ? -25.202 26.365 12.576  1.00 37.73 ? 358  THR A CG2 1 
ATOM   1006 N  N   . PHE A 1 135 ? -24.669 28.910 8.684   1.00 28.54 ? 359  PHE A N   1 
ATOM   1007 C  CA  . PHE A 1 135 ? -24.020 29.299 7.437   1.00 28.64 ? 359  PHE A CA  1 
ATOM   1008 C  C   . PHE A 1 135 ? -23.568 30.750 7.566   1.00 29.16 ? 359  PHE A C   1 
ATOM   1009 O  O   . PHE A 1 135 ? -24.379 31.674 7.526   1.00 24.33 ? 359  PHE A O   1 
ATOM   1010 C  CB  . PHE A 1 135 ? -24.975 29.100 6.267   1.00 24.28 ? 359  PHE A CB  1 
ATOM   1011 C  CG  . PHE A 1 135 ? -24.363 29.382 4.930   1.00 25.31 ? 359  PHE A CG  1 
ATOM   1012 C  CD1 . PHE A 1 135 ? -23.441 28.498 4.370   1.00 24.77 ? 359  PHE A CD1 1 
ATOM   1013 C  CD2 . PHE A 1 135 ? -24.721 30.516 4.217   1.00 23.46 ? 359  PHE A CD2 1 
ATOM   1014 C  CE1 . PHE A 1 135 ? -22.880 28.753 3.125   1.00 25.62 ? 359  PHE A CE1 1 
ATOM   1015 C  CE2 . PHE A 1 135 ? -24.163 30.781 2.970   1.00 22.25 ? 359  PHE A CE2 1 
ATOM   1016 C  CZ  . PHE A 1 135 ? -23.245 29.895 2.423   1.00 22.69 ? 359  PHE A CZ  1 
ATOM   1017 N  N   . ALA A 1 136 ? -22.268 30.963 7.765   1.00 30.20 ? 360  ALA A N   1 
ATOM   1018 C  CA  . ALA A 1 136 ? -21.721 32.312 7.941   1.00 26.95 ? 360  ALA A CA  1 
ATOM   1019 C  C   . ALA A 1 136 ? -20.390 32.426 7.216   1.00 22.07 ? 360  ALA A C   1 
ATOM   1020 O  O   . ALA A 1 136 ? -19.344 32.651 7.832   1.00 24.05 ? 360  ALA A O   1 
ATOM   1021 C  CB  . ALA A 1 136 ? -21.572 32.652 9.423   1.00 25.21 ? 360  ALA A CB  1 
ATOM   1022 N  N   . PRO A 1 137 ? -20.398 32.286 5.888   1.00 23.74 ? 361  PRO A N   1 
ATOM   1023 C  CA  . PRO A 1 137 ? -19.132 32.352 5.138   1.00 24.12 ? 361  PRO A CA  1 
ATOM   1024 C  C   . PRO A 1 137 ? -18.420 33.685 5.246   1.00 24.81 ? 361  PRO A C   1 
ATOM   1025 O  O   . PRO A 1 137 ? -17.200 33.722 5.035   1.00 24.03 ? 361  PRO A O   1 
ATOM   1026 C  CB  . PRO A 1 137 ? -19.568 32.075 3.691   1.00 24.88 ? 361  PRO A CB  1 
ATOM   1027 C  CG  . PRO A 1 137 ? -20.996 32.535 3.659   1.00 22.67 ? 361  PRO A CG  1 
ATOM   1028 C  CD  . PRO A 1 137 ? -21.551 32.112 4.985   1.00 24.71 ? 361  PRO A CD  1 
ATOM   1029 N  N   . LYS A 1 138 ? -19.136 34.780 5.538   1.00 23.46 ? 362  LYS A N   1 
ATOM   1030 C  CA  . LYS A 1 138 ? -18.486 36.089 5.630   1.00 25.75 ? 362  LYS A CA  1 
ATOM   1031 C  C   . LYS A 1 138 ? -17.383 36.077 6.682   1.00 25.40 ? 362  LYS A C   1 
ATOM   1032 O  O   . LYS A 1 138 ? -16.343 36.722 6.513   1.00 23.34 ? 362  LYS A O   1 
ATOM   1033 C  CB  . LYS A 1 138 ? -19.523 37.173 5.950   1.00 24.64 ? 362  LYS A CB  1 
ATOM   1034 C  CG  . LYS A 1 138 ? -18.994 38.603 5.970   1.00 26.27 ? 362  LYS A CG  1 
ATOM   1035 C  CD  . LYS A 1 138 ? -20.080 39.561 6.426   1.00 31.38 ? 362  LYS A CD  1 
ATOM   1036 C  CE  . LYS A 1 138 ? -19.702 41.037 6.231   1.00 30.80 ? 362  LYS A CE  1 
ATOM   1037 N  NZ  . LYS A 1 138 ? -19.557 41.419 4.800   1.00 33.46 ? 362  LYS A NZ  1 
ATOM   1038 N  N   . ILE A 1 139 ? -17.591 35.343 7.773   1.00 27.11 ? 363  ILE A N   1 
ATOM   1039 C  CA  . ILE A 1 139 ? -16.563 35.144 8.788   1.00 27.33 ? 363  ILE A CA  1 
ATOM   1040 C  C   . ILE A 1 139 ? -15.923 33.759 8.667   1.00 30.31 ? 363  ILE A C   1 
ATOM   1041 O  O   . ILE A 1 139 ? -15.252 33.304 9.592   1.00 25.61 ? 363  ILE A O   1 
ATOM   1042 C  CB  . ILE A 1 139 ? -17.112 35.384 10.200  1.00 31.23 ? 363  ILE A CB  1 
ATOM   1043 C  CG1 . ILE A 1 139 ? -18.294 34.447 10.477  1.00 27.88 ? 363  ILE A CG1 1 
ATOM   1044 C  CG2 . ILE A 1 139 ? -17.517 36.846 10.365  1.00 30.11 ? 363  ILE A CG2 1 
ATOM   1045 C  CD1 . ILE A 1 139 ? -18.880 34.612 11.867  1.00 33.10 ? 363  ILE A CD1 1 
ATOM   1046 N  N   . GLY A 1 140 ? -16.126 33.080 7.536   1.00 24.66 ? 364  GLY A N   1 
ATOM   1047 C  CA  . GLY A 1 140 ? -15.407 31.848 7.259   1.00 27.32 ? 364  GLY A CA  1 
ATOM   1048 C  C   . GLY A 1 140 ? -15.909 30.605 7.959   1.00 29.57 ? 364  GLY A C   1 
ATOM   1049 O  O   . GLY A 1 140 ? -15.152 29.635 8.086   1.00 31.71 ? 364  GLY A O   1 
ATOM   1050 N  N   . GLN A 1 141 ? -17.166 30.581 8.396   1.00 27.82 ? 365  GLN A N   1 
ATOM   1051 C  CA  . GLN A 1 141 ? -17.734 29.428 9.091   1.00 29.68 ? 365  GLN A CA  1 
ATOM   1052 C  C   . GLN A 1 141 ? -18.845 28.803 8.252   1.00 28.96 ? 365  GLN A C   1 
ATOM   1053 O  O   . GLN A 1 141 ? -19.899 29.418 8.041   1.00 25.08 ? 365  GLN A O   1 
ATOM   1054 C  CB  . GLN A 1 141 ? -18.251 29.841 10.461  1.00 28.27 ? 365  GLN A CB  1 
ATOM   1055 C  CG  . GLN A 1 141 ? -17.149 30.309 11.371  1.00 35.59 ? 365  GLN A CG  1 
ATOM   1056 C  CD  . GLN A 1 141 ? -17.677 30.976 12.627  1.00 45.81 ? 365  GLN A CD  1 
ATOM   1057 O  OE1 . GLN A 1 141 ? -18.872 31.269 12.741  1.00 44.13 ? 365  GLN A OE1 1 
ATOM   1058 N  NE2 . GLN A 1 141 ? -16.785 31.220 13.580  1.00 49.13 ? 365  GLN A NE2 1 
ATOM   1059 N  N   . VAL A 1 142 ? -18.604 27.584 7.768   1.00 28.14 ? 366  VAL A N   1 
ATOM   1060 C  CA  A VAL A 1 142 ? -19.611 26.821 7.041   0.09 26.08 ? 366  VAL A CA  1 
ATOM   1061 C  CA  B VAL A 1 142 ? -19.582 26.814 7.008   0.91 26.85 ? 366  VAL A CA  1 
ATOM   1062 C  C   . VAL A 1 142 ? -19.526 25.369 7.483   1.00 26.54 ? 366  VAL A C   1 
ATOM   1063 O  O   . VAL A 1 142 ? -18.442 24.851 7.771   1.00 26.29 ? 366  VAL A O   1 
ATOM   1064 C  CB  A VAL A 1 142 ? -19.452 26.934 5.508   0.09 25.48 ? 366  VAL A CB  1 
ATOM   1065 C  CB  B VAL A 1 142 ? -19.311 26.895 5.491   0.91 25.46 ? 366  VAL A CB  1 
ATOM   1066 C  CG1 A VAL A 1 142 ? -19.721 28.359 5.032   0.09 25.94 ? 366  VAL A CG1 1 
ATOM   1067 C  CG1 B VAL A 1 142 ? -20.270 26.002 4.727   0.91 22.33 ? 366  VAL A CG1 1 
ATOM   1068 C  CG2 A VAL A 1 142 ? -18.079 26.476 5.078   0.09 25.43 ? 366  VAL A CG2 1 
ATOM   1069 C  CG2 B VAL A 1 142 ? -19.425 28.338 5.002   0.91 26.04 ? 366  VAL A CG2 1 
ATOM   1070 N  N   . ARG A 1 143 ? -20.683 24.719 7.556   1.00 24.41 ? 367  ARG A N   1 
ATOM   1071 C  CA  . ARG A 1 143 ? -20.776 23.307 7.899   1.00 26.33 ? 367  ARG A CA  1 
ATOM   1072 C  C   . ARG A 1 143 ? -21.308 22.512 6.721   1.00 27.57 ? 367  ARG A C   1 
ATOM   1073 O  O   . ARG A 1 143 ? -22.150 22.992 5.952   1.00 27.07 ? 367  ARG A O   1 
ATOM   1074 C  CB  . ARG A 1 143 ? -21.694 23.072 9.095   1.00 24.78 ? 367  ARG A CB  1 
ATOM   1075 C  CG  . ARG A 1 143 ? -21.179 23.655 10.365  1.00 32.12 ? 367  ARG A CG  1 
ATOM   1076 C  CD  . ARG A 1 143 ? -22.240 23.638 11.444  1.00 33.69 ? 367  ARG A CD  1 
ATOM   1077 N  NE  . ARG A 1 143 ? -21.671 24.083 12.705  1.00 32.70 ? 367  ARG A NE  1 
ATOM   1078 C  CZ  . ARG A 1 143 ? -22.270 23.963 13.878  1.00 37.26 ? 367  ARG A CZ  1 
ATOM   1079 N  NH1 . ARG A 1 143 ? -23.500 23.484 13.979  1.00 40.07 ? 367  ARG A NH1 1 
ATOM   1080 N  NH2 . ARG A 1 143 ? -21.613 24.316 14.976  1.00 36.42 ? 367  ARG A NH2 1 
ATOM   1081 N  N   . PHE A 1 144 ? -20.826 21.282 6.588   1.00 23.21 ? 368  PHE A N   1 
ATOM   1082 C  CA  . PHE A 1 144 ? -21.379 20.396 5.586   1.00 24.73 ? 368  PHE A CA  1 
ATOM   1083 C  C   . PHE A 1 144 ? -21.766 19.086 6.250   1.00 27.67 ? 368  PHE A C   1 
ATOM   1084 O  O   . PHE A 1 144 ? -21.203 18.696 7.282   1.00 23.11 ? 368  PHE A O   1 
ATOM   1085 C  CB  . PHE A 1 144 ? -20.416 20.182 4.383   1.00 26.89 ? 368  PHE A CB  1 
ATOM   1086 C  CG  . PHE A 1 144 ? -19.173 19.357 4.685   1.00 26.48 ? 368  PHE A CG  1 
ATOM   1087 C  CD1 . PHE A 1 144 ? -19.220 17.966 4.668   1.00 26.00 ? 368  PHE A CD1 1 
ATOM   1088 C  CD2 . PHE A 1 144 ? -17.941 19.977 4.879   1.00 24.76 ? 368  PHE A CD2 1 
ATOM   1089 C  CE1 . PHE A 1 144 ? -18.075 17.202 4.916   1.00 29.15 ? 368  PHE A CE1 1 
ATOM   1090 C  CE2 . PHE A 1 144 ? -16.793 19.228 5.113   1.00 27.24 ? 368  PHE A CE2 1 
ATOM   1091 C  CZ  . PHE A 1 144 ? -16.861 17.830 5.135   1.00 27.89 ? 368  PHE A CZ  1 
ATOM   1092 N  N   . TYR A 1 145 ? -22.782 18.448 5.679   1.00 28.28 ? 369  TYR A N   1 
ATOM   1093 C  CA  . TYR A 1 145 ? -23.224 17.130 6.104   1.00 29.18 ? 369  TYR A CA  1 
ATOM   1094 C  C   . TYR A 1 145 ? -22.757 16.111 5.076   1.00 25.66 ? 369  TYR A C   1 
ATOM   1095 O  O   . TYR A 1 145 ? -22.729 16.401 3.879   1.00 27.30 ? 369  TYR A O   1 
ATOM   1096 C  CB  . TYR A 1 145 ? -24.750 17.075 6.250   1.00 30.22 ? 369  TYR A CB  1 
ATOM   1097 C  CG  . TYR A 1 145 ? -25.283 15.669 6.445   1.00 33.64 ? 369  TYR A CG  1 
ATOM   1098 C  CD1 . TYR A 1 145 ? -25.287 15.073 7.699   1.00 32.76 ? 369  TYR A CD1 1 
ATOM   1099 C  CD2 . TYR A 1 145 ? -25.768 14.935 5.365   1.00 33.67 ? 369  TYR A CD2 1 
ATOM   1100 C  CE1 . TYR A 1 145 ? -25.768 13.783 7.872   1.00 41.34 ? 369  TYR A CE1 1 
ATOM   1101 C  CE2 . TYR A 1 145 ? -26.250 13.649 5.527   1.00 37.07 ? 369  TYR A CE2 1 
ATOM   1102 C  CZ  . TYR A 1 145 ? -26.245 13.077 6.776   1.00 35.99 ? 369  TYR A CZ  1 
ATOM   1103 O  OH  . TYR A 1 145 ? -26.726 11.800 6.926   1.00 44.36 ? 369  TYR A OH  1 
ATOM   1104 N  N   . SER A 1 146 ? -22.393 14.923 5.545   1.00 29.70 ? 370  SER A N   1 
ATOM   1105 C  CA  . SER A 1 146 ? -22.012 13.836 4.658   1.00 26.69 ? 370  SER A CA  1 
ATOM   1106 C  C   . SER A 1 146 ? -22.465 12.535 5.296   1.00 31.30 ? 370  SER A C   1 
ATOM   1107 O  O   . SER A 1 146 ? -22.354 12.372 6.510   1.00 32.48 ? 370  SER A O   1 
ATOM   1108 C  CB  . SER A 1 146 ? -20.496 13.815 4.404   1.00 29.16 ? 370  SER A CB  1 
ATOM   1109 O  OG  . SER A 1 146 ? -20.111 12.749 3.540   1.00 27.95 ? 370  SER A OG  1 
ATOM   1110 N  N   . THR A 1 147 ? -22.993 11.622 4.477   1.00 29.12 ? 371  THR A N   1 
ATOM   1111 C  CA  . THR A 1 147 ? -23.306 10.286 4.973   1.00 38.30 ? 371  THR A CA  1 
ATOM   1112 C  C   . THR A 1 147 ? -22.051 9.522  5.380   1.00 34.13 ? 371  THR A C   1 
ATOM   1113 O  O   . THR A 1 147 ? -22.146 8.570  6.161   1.00 38.00 ? 371  THR A O   1 
ATOM   1114 C  CB  . THR A 1 147 ? -24.083 9.486  3.922   1.00 36.52 ? 371  THR A CB  1 
ATOM   1115 O  OG1 . THR A 1 147 ? -23.293 9.371  2.738   1.00 39.01 ? 371  THR A OG1 1 
ATOM   1116 C  CG2 . THR A 1 147 ? -25.391 10.186 3.576   1.00 32.09 ? 371  THR A CG2 1 
ATOM   1117 N  N   . SER A 1 148 ? -20.881 9.935  4.901   1.00 34.89 ? 372  SER A N   1 
ATOM   1118 C  CA  . SER A 1 148 ? -19.634 9.272  5.245   1.00 33.91 ? 372  SER A CA  1 
ATOM   1119 C  C   . SER A 1 148 ? -19.017 9.877  6.500   1.00 34.46 ? 372  SER A C   1 
ATOM   1120 O  O   . SER A 1 148 ? -19.120 11.077 6.757   1.00 33.20 ? 372  SER A O   1 
ATOM   1121 C  CB  . SER A 1 148 ? -18.635 9.365  4.094   1.00 29.79 ? 372  SER A CB  1 
ATOM   1122 O  OG  . SER A 1 148 ? -17.357 8.929  4.526   1.00 31.11 ? 372  SER A OG  1 
ATOM   1123 N  N   . SER A 1 149 ? -18.375 9.025  7.291   1.00 35.06 ? 373  SER A N   1 
ATOM   1124 C  CA  . SER A 1 149 ? -17.547 9.474  8.401   1.00 36.05 ? 373  SER A CA  1 
ATOM   1125 C  C   . SER A 1 149 ? -16.077 9.575  8.016   1.00 32.32 ? 373  SER A C   1 
ATOM   1126 O  O   . SER A 1 149 ? -15.246 9.892  8.872   1.00 36.48 ? 373  SER A O   1 
ATOM   1127 C  CB  . SER A 1 149 ? -17.705 8.526  9.598   1.00 37.55 ? 373  SER A CB  1 
ATOM   1128 O  OG  . SER A 1 149 ? -17.458 7.187  9.199   1.00 41.90 ? 373  SER A OG  1 
ATOM   1129 N  N   . ASP A 1 150 ? -15.749 9.333  6.745   1.00 33.65 ? 374  ASP A N   1 
ATOM   1130 C  CA  . ASP A 1 150 ? -14.366 9.223  6.276   1.00 35.44 ? 374  ASP A CA  1 
ATOM   1131 C  C   . ASP A 1 150 ? -13.821 10.612 5.923   1.00 32.54 ? 374  ASP A C   1 
ATOM   1132 O  O   . ASP A 1 150 ? -13.606 10.962 4.761   1.00 32.82 ? 374  ASP A O   1 
ATOM   1133 C  CB  . ASP A 1 150 ? -14.307 8.264  5.089   1.00 33.92 ? 374  ASP A CB  1 
ATOM   1134 C  CG  . ASP A 1 150 ? -12.888 7.947  4.635   1.00 34.12 ? 374  ASP A CG  1 
ATOM   1135 O  OD1 . ASP A 1 150 ? -11.967 7.894  5.478   1.00 38.80 ? 374  ASP A OD1 1 
ATOM   1136 O  OD2 . ASP A 1 150 ? -12.699 7.739  3.418   1.00 33.60 ? 374  ASP A OD2 1 
ATOM   1137 N  N   . PHE A 1 151 ? -13.597 11.413 6.968   1.00 31.18 ? 375  PHE A N   1 
ATOM   1138 C  CA  . PHE A 1 151 ? -13.012 12.743 6.828   1.00 30.45 ? 375  PHE A CA  1 
ATOM   1139 C  C   . PHE A 1 151 ? -12.002 12.959 7.942   1.00 34.77 ? 375  PHE A C   1 
ATOM   1140 O  O   . PHE A 1 151 ? -12.307 12.714 9.111   1.00 34.34 ? 375  PHE A O   1 
ATOM   1141 C  CB  . PHE A 1 151 ? -14.083 13.849 6.872   1.00 29.13 ? 375  PHE A CB  1 
ATOM   1142 C  CG  . PHE A 1 151 ? -14.945 13.906 5.642   1.00 30.14 ? 375  PHE A CG  1 
ATOM   1143 C  CD1 . PHE A 1 151 ? -14.488 14.527 4.491   1.00 24.14 ? 375  PHE A CD1 1 
ATOM   1144 C  CD2 . PHE A 1 151 ? -16.212 13.340 5.639   1.00 27.15 ? 375  PHE A CD2 1 
ATOM   1145 C  CE1 . PHE A 1 151 ? -15.272 14.566 3.341   1.00 28.67 ? 375  PHE A CE1 1 
ATOM   1146 C  CE2 . PHE A 1 151 ? -17.000 13.379 4.505   1.00 26.76 ? 375  PHE A CE2 1 
ATOM   1147 C  CZ  . PHE A 1 151 ? -16.531 13.990 3.350   1.00 25.69 ? 375  PHE A CZ  1 
ATOM   1148 N  N   . GLU A 1 152 ? -10.805 13.416 7.582   1.00 35.32 ? 376  GLU A N   1 
ATOM   1149 C  CA  . GLU A 1 152 ? -9.757  13.682 8.559   1.00 32.77 ? 376  GLU A CA  1 
ATOM   1150 C  C   . GLU A 1 152 ? -9.867  15.115 9.062   1.00 30.07 ? 376  GLU A C   1 
ATOM   1151 O  O   . GLU A 1 152 ? -9.964  16.051 8.266   1.00 30.47 ? 376  GLU A O   1 
ATOM   1152 C  CB  . GLU A 1 152 ? -8.375  13.460 7.947   1.00 30.57 ? 376  GLU A CB  1 
ATOM   1153 C  CG  . GLU A 1 152 ? -8.136  12.063 7.399   1.00 39.25 ? 376  GLU A CG  1 
ATOM   1154 C  CD  . GLU A 1 152 ? -7.792  11.062 8.478   1.00 43.89 ? 376  GLU A CD  1 
ATOM   1155 O  OE1 . GLU A 1 152 ? -7.547  11.497 9.625   1.00 46.25 ? 376  GLU A OE1 1 
ATOM   1156 O  OE2 . GLU A 1 152 ? -7.770  9.844  8.178   1.00 44.55 ? 376  GLU A OE2 1 
ATOM   1157 N  N   . THR A 1 153 ? -9.833  15.282 10.378  1.00 34.48 ? 377  THR A N   1 
ATOM   1158 C  CA  . THR A 1 153 ? -9.745  16.612 10.959  1.00 32.78 ? 377  THR A CA  1 
ATOM   1159 C  C   . THR A 1 153 ? -8.402  17.252 10.613  1.00 33.31 ? 377  THR A C   1 
ATOM   1160 O  O   . THR A 1 153 ? -7.382  16.566 10.506  1.00 30.59 ? 377  THR A O   1 
ATOM   1161 C  CB  . THR A 1 153 ? -9.933  16.517 12.475  1.00 39.56 ? 377  THR A CB  1 
ATOM   1162 O  OG1 . THR A 1 153 ? -11.303 16.206 12.757  1.00 36.58 ? 377  THR A OG1 1 
ATOM   1163 C  CG2 . THR A 1 153 ? -9.575  17.810 13.161  1.00 36.65 ? 377  THR A CG2 1 
ATOM   1164 N  N   . ASN A 1 154 ? -8.417  18.571 10.397  1.00 30.88 ? 378  ASN A N   1 
ATOM   1165 C  CA  . ASN A 1 154 ? -7.211  19.378 10.202  1.00 31.36 ? 378  ASN A CA  1 
ATOM   1166 C  C   . ASN A 1 154 ? -6.478  19.034 8.911   1.00 31.04 ? 378  ASN A C   1 
ATOM   1167 O  O   . ASN A 1 154 ? -5.247  19.082 8.852   1.00 33.36 ? 378  ASN A O   1 
ATOM   1168 C  CB  . ASN A 1 154 ? -6.258  19.264 11.397  1.00 30.12 ? 378  ASN A CB  1 
ATOM   1169 C  CG  . ASN A 1 154 ? -6.684  20.127 12.556  1.00 38.91 ? 378  ASN A CG  1 
ATOM   1170 O  OD1 . ASN A 1 154 ? -7.208  21.226 12.363  1.00 36.60 ? 378  ASN A OD1 1 
ATOM   1171 N  ND2 . ASN A 1 154 ? -6.464  19.639 13.774  1.00 34.72 ? 378  ASN A ND2 1 
ATOM   1172 N  N   . GLN A 1 155 ? -7.222  18.683 7.871   1.00 26.10 ? 379  GLN A N   1 
ATOM   1173 C  CA  . GLN A 1 155 ? -6.659  18.490 6.551   1.00 26.98 ? 379  GLN A CA  1 
ATOM   1174 C  C   . GLN A 1 155 ? -7.343  19.430 5.566   1.00 28.47 ? 379  GLN A C   1 
ATOM   1175 O  O   . GLN A 1 155 ? -8.527  19.742 5.723   1.00 26.38 ? 379  GLN A O   1 
ATOM   1176 C  CB  . GLN A 1 155 ? -6.823  17.036 6.081   1.00 27.17 ? 379  GLN A CB  1 
ATOM   1177 C  CG  . GLN A 1 155 ? -6.058  16.029 6.930   1.00 29.25 ? 379  GLN A CG  1 
ATOM   1178 C  CD  . GLN A 1 155 ? -4.551  16.219 6.845   1.00 31.21 ? 379  GLN A CD  1 
ATOM   1179 O  OE1 . GLN A 1 155 ? -4.049  16.920 5.964   1.00 32.68 ? 379  GLN A OE1 1 
ATOM   1180 N  NE2 . GLN A 1 155 ? -3.821  15.579 7.752   1.00 33.61 ? 379  GLN A NE2 1 
ATOM   1181 N  N   . PRO A 1 156 ? -6.626  19.900 4.548   1.00 29.21 ? 380  PRO A N   1 
ATOM   1182 C  CA  . PRO A 1 156 ? -7.258  20.766 3.546   1.00 27.69 ? 380  PRO A CA  1 
ATOM   1183 C  C   . PRO A 1 156 ? -8.446  20.062 2.907   1.00 25.82 ? 380  PRO A C   1 
ATOM   1184 O  O   . PRO A 1 156 ? -8.364  18.894 2.518   1.00 22.06 ? 380  PRO A O   1 
ATOM   1185 C  CB  . PRO A 1 156 ? -6.137  21.020 2.530   1.00 26.55 ? 380  PRO A CB  1 
ATOM   1186 C  CG  . PRO A 1 156 ? -4.882  20.633 3.212   1.00 27.33 ? 380  PRO A CG  1 
ATOM   1187 C  CD  . PRO A 1 156 ? -5.234  19.574 4.203   1.00 28.51 ? 380  PRO A CD  1 
ATOM   1188 N  N   . THR A 1 157 ? -9.552  20.788 2.798   1.00 23.73 ? 381  THR A N   1 
ATOM   1189 C  CA  . THR A 1 157 ? -10.814 20.238 2.326   1.00 22.46 ? 381  THR A CA  1 
ATOM   1190 C  C   . THR A 1 157 ? -11.408 21.155 1.269   1.00 20.33 ? 381  THR A C   1 
ATOM   1191 O  O   . THR A 1 157 ? -11.337 22.378 1.395   1.00 22.93 ? 381  THR A O   1 
ATOM   1192 C  CB  . THR A 1 157 ? -11.770 20.075 3.504   1.00 24.70 ? 381  THR A CB  1 
ATOM   1193 O  OG1 . THR A 1 157 ? -11.095 19.338 4.525   1.00 21.97 ? 381  THR A OG1 1 
ATOM   1194 C  CG2 . THR A 1 157 ? -13.054 19.356 3.097   1.00 22.93 ? 381  THR A CG2 1 
ATOM   1195 N  N   . HIS A 1 158 ? -11.986 20.566 0.222   1.00 21.46 ? 382  HIS A N   1 
ATOM   1196 C  CA  . HIS A 1 158 ? -12.616 21.336 -0.841  1.00 19.94 ? 382  HIS A CA  1 
ATOM   1197 C  C   . HIS A 1 158 ? -14.042 20.847 -1.077  1.00 20.56 ? 382  HIS A C   1 
ATOM   1198 O  O   . HIS A 1 158 ? -14.294 19.637 -1.118  1.00 19.81 ? 382  HIS A O   1 
ATOM   1199 C  CB  . HIS A 1 158 ? -11.798 21.241 -2.139  1.00 19.43 ? 382  HIS A CB  1 
ATOM   1200 C  CG  . HIS A 1 158 ? -12.256 22.180 -3.209  1.00 20.25 ? 382  HIS A CG  1 
ATOM   1201 N  ND1 . HIS A 1 158 ? -11.642 23.390 -3.449  1.00 24.12 ? 382  HIS A ND1 1 
ATOM   1202 C  CD2 . HIS A 1 158 ? -13.290 22.103 -4.079  1.00 19.21 ? 382  HIS A CD2 1 
ATOM   1203 C  CE1 . HIS A 1 158 ? -12.265 24.009 -4.436  1.00 23.70 ? 382  HIS A CE1 1 
ATOM   1204 N  NE2 . HIS A 1 158 ? -13.273 23.252 -4.832  1.00 22.35 ? 382  HIS A NE2 1 
ATOM   1205 N  N   . PHE A 1 159 ? -14.975 21.794 -1.217  1.00 20.44 ? 383  PHE A N   1 
ATOM   1206 C  CA  . PHE A 1 159 ? -16.348 21.491 -1.609  1.00 21.39 ? 383  PHE A CA  1 
ATOM   1207 C  C   . PHE A 1 159 ? -16.545 21.850 -3.076  1.00 18.35 ? 383  PHE A C   1 
ATOM   1208 O  O   . PHE A 1 159 ? -16.463 23.027 -3.452  1.00 20.17 ? 383  PHE A O   1 
ATOM   1209 C  CB  . PHE A 1 159 ? -17.368 22.237 -0.750  1.00 20.52 ? 383  PHE A CB  1 
ATOM   1210 C  CG  . PHE A 1 159 ? -18.793 21.893 -1.083  1.00 20.41 ? 383  PHE A CG  1 
ATOM   1211 C  CD1 . PHE A 1 159 ? -19.381 20.749 -0.569  1.00 19.89 ? 383  PHE A CD1 1 
ATOM   1212 C  CD2 . PHE A 1 159 ? -19.538 22.701 -1.928  1.00 19.15 ? 383  PHE A CD2 1 
ATOM   1213 C  CE1 . PHE A 1 159 ? -20.701 20.413 -0.889  1.00 23.13 ? 383  PHE A CE1 1 
ATOM   1214 C  CE2 . PHE A 1 159 ? -20.861 22.378 -2.244  1.00 22.00 ? 383  PHE A CE2 1 
ATOM   1215 C  CZ  . PHE A 1 159 ? -21.437 21.230 -1.724  1.00 21.83 ? 383  PHE A CZ  1 
ATOM   1216 N  N   . THR A 1 160 ? -16.822 20.839 -3.893  1.00 18.97 ? 384  THR A N   1 
ATOM   1217 C  CA  . THR A 1 160 ? -17.111 21.035 -5.299  1.00 17.00 ? 384  THR A CA  1 
ATOM   1218 C  C   . THR A 1 160 ? -18.612 20.957 -5.513  1.00 18.00 ? 384  THR A C   1 
ATOM   1219 O  O   . THR A 1 160 ? -19.223 19.928 -5.184  1.00 19.38 ? 384  THR A O   1 
ATOM   1220 C  CB  . THR A 1 160 ? -16.400 19.985 -6.150  1.00 19.12 ? 384  THR A CB  1 
ATOM   1221 O  OG1 . THR A 1 160 ? -14.989 20.048 -5.893  1.00 20.13 ? 384  THR A OG1 1 
ATOM   1222 C  CG2 . THR A 1 160 ? -16.647 20.253 -7.639  1.00 18.74 ? 384  THR A CG2 1 
ATOM   1223 N  N   . PRO A 1 161 ? -19.248 21.995 -6.038  1.00 18.95 ? 385  PRO A N   1 
ATOM   1224 C  CA  . PRO A 1 161 ? -20.704 21.977 -6.159  1.00 19.06 ? 385  PRO A CA  1 
ATOM   1225 C  C   . PRO A 1 161 ? -21.135 21.159 -7.357  1.00 20.33 ? 385  PRO A C   1 
ATOM   1226 O  O   . PRO A 1 161 ? -20.452 21.101 -8.380  1.00 22.05 ? 385  PRO A O   1 
ATOM   1227 C  CB  . PRO A 1 161 ? -21.058 23.451 -6.345  1.00 18.73 ? 385  PRO A CB  1 
ATOM   1228 C  CG  . PRO A 1 161 ? -19.842 24.009 -7.018  1.00 17.83 ? 385  PRO A CG  1 
ATOM   1229 C  CD  . PRO A 1 161 ? -18.669 23.287 -6.437  1.00 16.54 ? 385  PRO A CD  1 
ATOM   1230 N  N   . ILE A 1 162 ? -22.291 20.522 -7.221  1.00 17.91 ? 386  ILE A N   1 
ATOM   1231 C  CA  . ILE A 1 162 ? -22.792 19.694 -8.311  1.00 16.88 ? 386  ILE A CA  1 
ATOM   1232 C  C   . ILE A 1 162 ? -24.234 20.075 -8.600  1.00 17.86 ? 386  ILE A C   1 
ATOM   1233 O  O   . ILE A 1 162 ? -24.618 20.248 -9.759  1.00 18.49 ? 386  ILE A O   1 
ATOM   1234 C  CB  . ILE A 1 162 ? -22.669 18.188 -7.993  1.00 23.34 ? 386  ILE A CB  1 
ATOM   1235 C  CG1 . ILE A 1 162 ? -21.203 17.761 -7.953  1.00 17.03 ? 386  ILE A CG1 1 
ATOM   1236 C  CG2 . ILE A 1 162 ? -23.436 17.340 -9.042  1.00 17.17 ? 386  ILE A CG2 1 
ATOM   1237 C  CD1 . ILE A 1 162 ? -20.993 16.486 -7.257  1.00 27.03 ? 386  ILE A CD1 1 
ATOM   1238 N  N   . GLY A 1 163 ? -25.050 20.196 -7.559  1.00 21.22 ? 387  GLY A N   1 
ATOM   1239 C  CA  . GLY A 1 163 ? -26.421 20.604 -7.799  1.00 22.47 ? 387  GLY A CA  1 
ATOM   1240 C  C   . GLY A 1 163 ? -27.199 20.924 -6.544  1.00 20.81 ? 387  GLY A C   1 
ATOM   1241 O  O   . GLY A 1 163 ? -26.637 21.401 -5.556  1.00 23.56 ? 387  GLY A O   1 
ATOM   1242 N  N   . ILE A 1 164 ? -28.496 20.648 -6.564  1.00 20.44 ? 388  ILE A N   1 
ATOM   1243 C  CA  . ILE A 1 164 ? -29.372 21.006 -5.461  1.00 23.24 ? 388  ILE A CA  1 
ATOM   1244 C  C   . ILE A 1 164 ? -30.118 19.761 -4.998  1.00 25.59 ? 388  ILE A C   1 
ATOM   1245 O  O   . ILE A 1 164 ? -30.389 18.842 -5.779  1.00 25.48 ? 388  ILE A O   1 
ATOM   1246 C  CB  . ILE A 1 164 ? -30.348 22.135 -5.864  1.00 28.02 ? 388  ILE A CB  1 
ATOM   1247 C  CG1 . ILE A 1 164 ? -30.971 22.777 -4.629  1.00 30.47 ? 388  ILE A CG1 1 
ATOM   1248 C  CG2 . ILE A 1 164 ? -31.412 21.624 -6.797  1.00 26.74 ? 388  ILE A CG2 1 
ATOM   1249 C  CD1 . ILE A 1 164 ? -30.066 23.830 -3.997  1.00 32.94 ? 388  ILE A CD1 1 
ATOM   1250 N  N   . TYR A 1 165 ? -30.417 19.725 -3.704  1.00 25.82 ? 389  TYR A N   1 
ATOM   1251 C  CA  . TYR A 1 165 ? -31.013 18.575 -3.038  1.00 27.38 ? 389  TYR A CA  1 
ATOM   1252 C  C   . TYR A 1 165 ? -32.315 19.039 -2.402  1.00 26.64 ? 389  TYR A C   1 
ATOM   1253 O  O   . TYR A 1 165 ? -32.292 19.892 -1.512  1.00 27.35 ? 389  TYR A O   1 
ATOM   1254 C  CB  . TYR A 1 165 ? -30.054 18.021 -1.978  1.00 25.94 ? 389  TYR A CB  1 
ATOM   1255 C  CG  . TYR A 1 165 ? -30.423 16.680 -1.374  1.00 30.52 ? 389  TYR A CG  1 
ATOM   1256 C  CD1 . TYR A 1 165 ? -31.543 16.539 -0.563  1.00 37.68 ? 389  TYR A CD1 1 
ATOM   1257 C  CD2 . TYR A 1 165 ? -29.629 15.562 -1.587  1.00 33.88 ? 389  TYR A CD2 1 
ATOM   1258 C  CE1 . TYR A 1 165 ? -31.876 15.315 -0.001  1.00 41.00 ? 389  TYR A CE1 1 
ATOM   1259 C  CE2 . TYR A 1 165 ? -29.956 14.334 -1.033  1.00 38.15 ? 389  TYR A CE2 1 
ATOM   1260 C  CZ  . TYR A 1 165 ? -31.078 14.220 -0.237  1.00 38.85 ? 389  TYR A CZ  1 
ATOM   1261 O  OH  . TYR A 1 165 ? -31.410 13.007 0.323   1.00 45.95 ? 389  TYR A OH  1 
ATOM   1262 N  N   . ILE A 1 166 ? -33.439 18.470 -2.839  1.00 28.32 ? 390  ILE A N   1 
ATOM   1263 C  CA  . ILE A 1 166 ? -34.765 18.854 -2.353  1.00 30.15 ? 390  ILE A CA  1 
ATOM   1264 C  C   . ILE A 1 166 ? -35.232 17.802 -1.346  1.00 39.69 ? 390  ILE A C   1 
ATOM   1265 O  O   . ILE A 1 166 ? -35.459 16.639 -1.701  1.00 32.86 ? 390  ILE A O   1 
ATOM   1266 C  CB  . ILE A 1 166 ? -35.773 19.001 -3.504  1.00 28.83 ? 390  ILE A CB  1 
ATOM   1267 C  CG1 . ILE A 1 166 ? -35.318 20.061 -4.513  1.00 31.06 ? 390  ILE A CG1 1 
ATOM   1268 C  CG2 . ILE A 1 166 ? -37.151 19.335 -2.957  1.00 35.05 ? 390  ILE A CG2 1 
ATOM   1269 C  CD1 . ILE A 1 166 ? -35.128 21.445 -3.928  1.00 30.32 ? 390  ILE A CD1 1 
ATOM   1270 N  N   . GLU A 1 167 ? -35.370 18.204 -0.084  1.00 40.29 ? 391  GLU A N   1 
ATOM   1271 C  CA  . GLU A 1 167 ? -35.888 17.336 0.966   1.00 47.81 ? 391  GLU A CA  1 
ATOM   1272 C  C   . GLU A 1 167 ? -36.696 18.185 1.932   1.00 57.53 ? 391  GLU A C   1 
ATOM   1273 O  O   . GLU A 1 167 ? -36.472 19.391 2.064   1.00 58.29 ? 391  GLU A O   1 
ATOM   1274 C  CB  . GLU A 1 167 ? -34.775 16.598 1.727   1.00 49.49 ? 391  GLU A CB  1 
ATOM   1275 C  CG  . GLU A 1 167 ? -34.111 17.414 2.837   1.00 52.14 ? 391  GLU A CG  1 
ATOM   1276 C  CD  . GLU A 1 167 ? -33.317 16.550 3.816   1.00 59.47 ? 391  GLU A CD  1 
ATOM   1277 O  OE1 . GLU A 1 167 ? -33.341 15.308 3.665   1.00 66.98 ? 391  GLU A OE1 1 
ATOM   1278 O  OE2 . GLU A 1 167 ? -32.668 17.105 4.736   1.00 54.54 ? 391  GLU A OE2 1 
ATOM   1279 N  N   . GLY A 1 168 ? -37.632 17.538 2.626   1.00 71.12 ? 392  GLY A N   1 
ATOM   1280 C  CA  . GLY A 1 168 ? -38.590 18.287 3.426   1.00 71.75 ? 392  GLY A CA  1 
ATOM   1281 C  C   . GLY A 1 168 ? -37.958 19.054 4.574   1.00 71.96 ? 392  GLY A C   1 
ATOM   1282 O  O   . GLY A 1 168 ? -38.358 20.184 4.871   1.00 71.47 ? 392  GLY A O   1 
ATOM   1283 N  N   . ASN A 1 169 ? -36.959 18.461 5.228   1.00 54.37 ? 393  ASN A N   1 
ATOM   1284 C  CA  . ASN A 1 169 ? -36.393 19.009 6.455   1.00 52.62 ? 393  ASN A CA  1 
ATOM   1285 C  C   . ASN A 1 169 ? -35.213 19.962 6.218   1.00 51.92 ? 393  ASN A C   1 
ATOM   1286 O  O   . ASN A 1 169 ? -34.516 20.320 7.177   1.00 43.75 ? 393  ASN A O   1 
ATOM   1287 C  CB  . ASN A 1 169 ? -35.964 17.870 7.385   1.00 45.82 ? 393  ASN A CB  1 
ATOM   1288 C  CG  . ASN A 1 169 ? -36.048 18.256 8.842   1.00 44.25 ? 393  ASN A CG  1 
ATOM   1289 O  OD1 . ASN A 1 169 ? -36.822 19.139 9.213   1.00 41.35 ? 393  ASN A OD1 1 
ATOM   1290 N  ND2 . ASN A 1 169 ? -35.252 17.598 9.679   1.00 46.10 ? 393  ASN A ND2 1 
ATOM   1291 N  N   . SER A 1 170 ? -34.974 20.380 4.978   1.00 49.02 ? 394  SER A N   1 
ATOM   1292 C  CA  . SER A 1 170 ? -34.009 21.429 4.682   1.00 49.20 ? 394  SER A CA  1 
ATOM   1293 C  C   . SER A 1 170 ? -34.705 22.514 3.868   1.00 47.95 ? 394  SER A C   1 
ATOM   1294 O  O   . SER A 1 170 ? -35.840 22.345 3.409   1.00 45.43 ? 394  SER A O   1 
ATOM   1295 C  CB  . SER A 1 170 ? -32.781 20.877 3.941   1.00 47.15 ? 394  SER A CB  1 
ATOM   1296 O  OG  . SER A 1 170 ? -32.051 19.967 4.756   1.00 47.82 ? 394  SER A OG  1 
ATOM   1297 N  N   . SER A 1 171 ? -34.025 23.648 3.706   1.00 42.40 ? 395  SER A N   1 
ATOM   1298 C  CA  . SER A 1 171 ? -34.629 24.775 3.007   1.00 46.21 ? 395  SER A CA  1 
ATOM   1299 C  C   . SER A 1 171 ? -34.792 24.463 1.526   1.00 43.55 ? 395  SER A C   1 
ATOM   1300 O  O   . SER A 1 171 ? -33.899 23.898 0.890   1.00 39.75 ? 395  SER A O   1 
ATOM   1301 C  CB  . SER A 1 171 ? -33.787 26.043 3.191   1.00 47.35 ? 395  SER A CB  1 
ATOM   1302 O  OG  . SER A 1 171 ? -32.407 25.750 3.280   1.00 38.74 ? 395  SER A OG  1 
ATOM   1303 N  N   . ASP A 1 172 ? -35.948 24.818 0.976   1.00 43.52 ? 396  ASP A N   1 
ATOM   1304 C  CA  . ASP A 1 172 ? -36.136 24.593 -0.447  1.00 49.27 ? 396  ASP A CA  1 
ATOM   1305 C  C   . ASP A 1 172 ? -35.293 25.579 -1.251  1.00 41.89 ? 396  ASP A C   1 
ATOM   1306 O  O   . ASP A 1 172 ? -34.872 26.633 -0.763  1.00 39.40 ? 396  ASP A O   1 
ATOM   1307 C  CB  . ASP A 1 172 ? -37.609 24.713 -0.839  1.00 52.15 ? 396  ASP A CB  1 
ATOM   1308 C  CG  . ASP A 1 172 ? -37.981 23.799 -1.994  1.00 52.31 ? 396  ASP A CG  1 
ATOM   1309 O  OD1 . ASP A 1 172 ? -37.519 24.056 -3.126  1.00 48.00 ? 396  ASP A OD1 1 
ATOM   1310 O  OD2 . ASP A 1 172 ? -38.724 22.814 -1.762  1.00 54.47 ? 396  ASP A OD2 1 
ATOM   1311 N  N   . PHE A 1 173 ? -35.028 25.204 -2.493  1.00 36.08 ? 397  PHE A N   1 
ATOM   1312 C  CA  . PHE A 1 173 ? -34.202 26.006 -3.380  1.00 29.15 ? 397  PHE A CA  1 
ATOM   1313 C  C   . PHE A 1 173 ? -34.989 27.248 -3.787  1.00 25.48 ? 397  PHE A C   1 
ATOM   1314 O  O   . PHE A 1 173 ? -36.038 27.149 -4.430  1.00 24.03 ? 397  PHE A O   1 
ATOM   1315 C  CB  . PHE A 1 173 ? -33.798 25.140 -4.569  1.00 29.69 ? 397  PHE A CB  1 
ATOM   1316 C  CG  . PHE A 1 173 ? -33.109 25.873 -5.667  1.00 26.47 ? 397  PHE A CG  1 
ATOM   1317 C  CD1 . PHE A 1 173 ? -32.090 26.754 -5.398  1.00 24.55 ? 397  PHE A CD1 1 
ATOM   1318 C  CD2 . PHE A 1 173 ? -33.472 25.652 -6.978  1.00 27.25 ? 397  PHE A CD2 1 
ATOM   1319 C  CE1 . PHE A 1 173 ? -31.455 27.425 -6.418  1.00 25.08 ? 397  PHE A CE1 1 
ATOM   1320 C  CE2 . PHE A 1 173 ? -32.844 26.317 -8.006  1.00 27.44 ? 397  PHE A CE2 1 
ATOM   1321 C  CZ  . PHE A 1 173 ? -31.837 27.209 -7.724  1.00 27.04 ? 397  PHE A CZ  1 
ATOM   1322 N  N   . ASN A 1 174 ? -34.522 28.415 -3.346  1.00 23.52 ? 398  ASN A N   1 
ATOM   1323 C  CA  . ASN A 1 174 ? -35.103 29.709 -3.705  1.00 22.93 ? 398  ASN A CA  1 
ATOM   1324 C  C   . ASN A 1 174 ? -33.957 30.538 -4.272  1.00 24.28 ? 398  ASN A C   1 
ATOM   1325 O  O   . ASN A 1 174 ? -33.149 31.086 -3.513  1.00 20.91 ? 398  ASN A O   1 
ATOM   1326 C  CB  . ASN A 1 174 ? -35.760 30.375 -2.492  1.00 23.55 ? 398  ASN A CB  1 
ATOM   1327 C  CG  . ASN A 1 174 ? -36.424 31.718 -2.822  1.00 34.69 ? 398  ASN A CG  1 
ATOM   1328 O  OD1 . ASN A 1 174 ? -36.165 32.337 -3.868  1.00 33.17 ? 398  ASN A OD1 1 
ATOM   1329 N  ND2 . ASN A 1 174 ? -37.278 32.187 -1.905  1.00 39.23 ? 398  ASN A ND2 1 
ATOM   1330 N  N   . GLN A 1 175 ? -33.891 30.632 -5.604  1.00 20.54 ? 399  GLN A N   1 
ATOM   1331 C  CA  . GLN A 1 175 ? -32.723 31.219 -6.250  1.00 23.13 ? 399  GLN A CA  1 
ATOM   1332 C  C   . GLN A 1 175 ? -32.638 32.729 -6.035  1.00 20.48 ? 399  GLN A C   1 
ATOM   1333 O  O   . GLN A 1 175 ? -31.560 33.307 -6.202  1.00 21.89 ? 399  GLN A O   1 
ATOM   1334 C  CB  . GLN A 1 175 ? -32.728 30.901 -7.749  1.00 23.56 ? 399  GLN A CB  1 
ATOM   1335 C  CG  . GLN A 1 175 ? -33.894 31.504 -8.538  1.00 19.88 ? 399  GLN A CG  1 
ATOM   1336 C  CD  . GLN A 1 175 ? -33.564 31.645 -10.015 1.00 22.31 ? 399  GLN A CD  1 
ATOM   1337 O  OE1 . GLN A 1 175 ? -32.399 31.837 -10.386 1.00 19.78 ? 399  GLN A OE1 1 
ATOM   1338 N  NE2 . GLN A 1 175 ? -34.577 31.515 -10.868 1.00 18.39 ? 399  GLN A NE2 1 
ATOM   1339 N  N   . TRP A 1 176 ? -33.733 33.374 -5.652  1.00 20.91 ? 400  TRP A N   1 
ATOM   1340 C  CA  . TRP A 1 176 ? -33.731 34.809 -5.419  1.00 22.25 ? 400  TRP A CA  1 
ATOM   1341 C  C   . TRP A 1 176 ? -33.676 35.186 -3.948  1.00 24.33 ? 400  TRP A C   1 
ATOM   1342 O  O   . TRP A 1 176 ? -33.745 36.376 -3.637  1.00 25.36 ? 400  TRP A O   1 
ATOM   1343 C  CB  . TRP A 1 176 ? -34.962 35.456 -6.067  1.00 22.09 ? 400  TRP A CB  1 
ATOM   1344 C  CG  . TRP A 1 176 ? -35.033 35.232 -7.542  1.00 22.13 ? 400  TRP A CG  1 
ATOM   1345 C  CD1 . TRP A 1 176 ? -36.081 34.713 -8.240  1.00 23.74 ? 400  TRP A CD1 1 
ATOM   1346 C  CD2 . TRP A 1 176 ? -34.009 35.513 -8.502  1.00 21.21 ? 400  TRP A CD2 1 
ATOM   1347 N  NE1 . TRP A 1 176 ? -35.778 34.657 -9.574  1.00 19.98 ? 400  TRP A NE1 1 
ATOM   1348 C  CE2 . TRP A 1 176 ? -34.511 35.141 -9.763  1.00 21.51 ? 400  TRP A CE2 1 
ATOM   1349 C  CE3 . TRP A 1 176 ? -32.719 36.045 -8.419  1.00 20.16 ? 400  TRP A CE3 1 
ATOM   1350 C  CZ2 . TRP A 1 176 ? -33.771 35.282 -10.933 1.00 20.40 ? 400  TRP A CZ2 1 
ATOM   1351 C  CZ3 . TRP A 1 176 ? -31.975 36.170 -9.588  1.00 19.55 ? 400  TRP A CZ3 1 
ATOM   1352 C  CH2 . TRP A 1 176 ? -32.504 35.797 -10.822 1.00 19.65 ? 400  TRP A CH2 1 
ATOM   1353 N  N   . GLN A 1 177 ? -33.560 34.220 -3.033  1.00 23.54 ? 401  GLN A N   1 
ATOM   1354 C  CA  . GLN A 1 177 ? -33.460 34.517 -1.607  1.00 26.30 ? 401  GLN A CA  1 
ATOM   1355 C  C   . GLN A 1 177 ? -31.993 34.477 -1.204  1.00 23.84 ? 401  GLN A C   1 
ATOM   1356 O  O   . GLN A 1 177 ? -31.356 33.418 -1.254  1.00 23.87 ? 401  GLN A O   1 
ATOM   1357 C  CB  . GLN A 1 177 ? -34.283 33.542 -0.772  1.00 22.86 ? 401  GLN A CB  1 
ATOM   1358 C  CG  . GLN A 1 177 ? -34.224 33.862 0.713   1.00 27.60 ? 401  GLN A CG  1 
ATOM   1359 C  CD  . GLN A 1 177 ? -34.940 32.824 1.549   1.00 35.50 ? 401  GLN A CD  1 
ATOM   1360 O  OE1 . GLN A 1 177 ? -35.392 31.799 1.029   1.00 34.39 ? 401  GLN A OE1 1 
ATOM   1361 N  NE2 . GLN A 1 177 ? -35.053 33.081 2.852   1.00 44.80 ? 401  GLN A NE2 1 
ATOM   1362 N  N   . LEU A 1 178 ? -31.453 35.632 -0.823  1.00 22.79 ? 402  LEU A N   1 
ATOM   1363 C  CA  . LEU A 1 178 ? -30.040 35.698 -0.485  1.00 22.59 ? 402  LEU A CA  1 
ATOM   1364 C  C   . LEU A 1 178 ? -29.790 35.002 0.850   1.00 21.85 ? 402  LEU A C   1 
ATOM   1365 O  O   . LEU A 1 178 ? -30.603 35.109 1.771   1.00 24.37 ? 402  LEU A O   1 
ATOM   1366 C  CB  . LEU A 1 178 ? -29.559 37.151 -0.401  1.00 22.50 ? 402  LEU A CB  1 
ATOM   1367 C  CG  . LEU A 1 178 ? -29.481 37.950 -1.703  1.00 23.09 ? 402  LEU A CG  1 
ATOM   1368 C  CD1 . LEU A 1 178 ? -29.160 39.422 -1.424  1.00 23.58 ? 402  LEU A CD1 1 
ATOM   1369 C  CD2 . LEU A 1 178 ? -28.447 37.339 -2.634  1.00 20.76 ? 402  LEU A CD2 1 
ATOM   1370 N  N   . PRO A 1 179 ? -28.683 34.282 0.986   1.00 23.15 ? 403  PRO A N   1 
ATOM   1371 C  CA  . PRO A 1 179 ? -28.296 33.789 2.308   1.00 21.85 ? 403  PRO A CA  1 
ATOM   1372 C  C   . PRO A 1 179 ? -27.935 34.952 3.217   1.00 24.21 ? 403  PRO A C   1 
ATOM   1373 O  O   . PRO A 1 179 ? -27.572 36.037 2.764   1.00 24.10 ? 403  PRO A O   1 
ATOM   1374 C  CB  . PRO A 1 179 ? -27.071 32.909 2.027   1.00 23.18 ? 403  PRO A CB  1 
ATOM   1375 C  CG  . PRO A 1 179 ? -26.562 33.346 0.677   1.00 19.72 ? 403  PRO A CG  1 
ATOM   1376 C  CD  . PRO A 1 179 ? -27.727 33.909 -0.075  1.00 21.73 ? 403  PRO A CD  1 
ATOM   1377 N  N   . ARG A 1 180 ? -28.041 34.709 4.521   1.00 23.46 ? 404  ARG A N   1 
ATOM   1378 C  CA  . ARG A 1 180 ? -27.465 35.616 5.516   1.00 27.57 ? 404  ARG A CA  1 
ATOM   1379 C  C   . ARG A 1 180 ? -25.972 35.321 5.587   1.00 21.92 ? 404  ARG A C   1 
ATOM   1380 O  O   . ARG A 1 180 ? -25.525 34.455 6.338   1.00 25.50 ? 404  ARG A O   1 
ATOM   1381 C  CB  . ARG A 1 180 ? -28.128 35.435 6.876   1.00 27.07 ? 404  ARG A CB  1 
ATOM   1382 C  CG  . ARG A 1 180 ? -29.519 36.021 6.998   1.00 41.08 ? 404  ARG A CG  1 
ATOM   1383 C  CD  . ARG A 1 180 ? -29.964 36.055 8.463   1.00 44.30 ? 404  ARG A CD  1 
ATOM   1384 N  NE  . ARG A 1 180 ? -31.247 36.726 8.641   1.00 50.66 ? 404  ARG A NE  1 
ATOM   1385 C  CZ  . ARG A 1 180 ? -31.389 37.970 9.081   1.00 55.37 ? 404  ARG A CZ  1 
ATOM   1386 N  NH1 . ARG A 1 180 ? -30.341 38.710 9.416   1.00 48.41 ? 404  ARG A NH1 1 
ATOM   1387 N  NH2 . ARG A 1 180 ? -32.612 38.483 9.192   1.00 62.71 ? 404  ARG A NH2 1 
ATOM   1388 N  N   . TYR A 1 181 ? -25.188 36.054 4.793   1.00 25.29 ? 405  TYR A N   1 
ATOM   1389 C  CA  . TYR A 1 181 ? -23.761 35.756 4.650   1.00 23.37 ? 405  TYR A CA  1 
ATOM   1390 C  C   . TYR A 1 181 ? -23.015 35.759 5.980   1.00 23.54 ? 405  TYR A C   1 
ATOM   1391 O  O   . TYR A 1 181 ? -21.971 35.100 6.105   1.00 23.37 ? 405  TYR A O   1 
ATOM   1392 C  CB  . TYR A 1 181 ? -23.110 36.765 3.708   1.00 25.03 ? 405  TYR A CB  1 
ATOM   1393 C  CG  . TYR A 1 181 ? -23.565 36.657 2.275   1.00 22.32 ? 405  TYR A CG  1 
ATOM   1394 C  CD1 . TYR A 1 181 ? -23.057 35.678 1.437   1.00 19.73 ? 405  TYR A CD1 1 
ATOM   1395 C  CD2 . TYR A 1 181 ? -24.492 37.551 1.752   1.00 21.39 ? 405  TYR A CD2 1 
ATOM   1396 C  CE1 . TYR A 1 181 ? -23.472 35.583 0.127   1.00 19.50 ? 405  TYR A CE1 1 
ATOM   1397 C  CE2 . TYR A 1 181 ? -24.900 37.465 0.441   1.00 21.86 ? 405  TYR A CE2 1 
ATOM   1398 C  CZ  . TYR A 1 181 ? -24.394 36.478 -0.366  1.00 20.39 ? 405  TYR A CZ  1 
ATOM   1399 O  OH  . TYR A 1 181 ? -24.811 36.395 -1.680  1.00 19.19 ? 405  TYR A OH  1 
ATOM   1400 N  N   . GLY A 1 182 ? -23.510 36.501 6.970   1.00 25.07 ? 406  GLY A N   1 
ATOM   1401 C  CA  . GLY A 1 182 ? -22.861 36.627 8.252   1.00 25.57 ? 406  GLY A CA  1 
ATOM   1402 C  C   . GLY A 1 182 ? -23.401 35.743 9.352   1.00 31.24 ? 406  GLY A C   1 
ATOM   1403 O  O   . GLY A 1 182 ? -22.956 35.875 10.498  1.00 31.95 ? 406  GLY A O   1 
ATOM   1404 N  N   . GLY A 1 183 ? -24.334 34.842 9.053   1.00 27.35 ? 407  GLY A N   1 
ATOM   1405 C  CA  . GLY A 1 183 ? -24.956 34.032 10.079  1.00 34.99 ? 407  GLY A CA  1 
ATOM   1406 C  C   . GLY A 1 183 ? -26.142 34.729 10.732  1.00 43.52 ? 407  GLY A C   1 
ATOM   1407 O  O   . GLY A 1 183 ? -26.355 35.936 10.598  1.00 43.20 ? 407  GLY A O   1 
ATOM   1408 N  N   . HIS A 1 184 ? -26.915 33.926 11.472  1.00 50.37 ? 408  HIS A N   1 
ATOM   1409 C  CA  . HIS A 1 184 ? -28.225 34.247 12.047  1.00 53.19 ? 408  HIS A CA  1 
ATOM   1410 C  C   . HIS A 1 184 ? -28.537 35.728 12.227  1.00 54.84 ? 408  HIS A C   1 
ATOM   1411 O  O   . HIS A 1 184 ? -29.519 36.235 11.674  1.00 58.18 ? 408  HIS A O   1 
ATOM   1412 C  CB  . HIS A 1 184 ? -28.369 33.552 13.407  1.00 55.99 ? 408  HIS A CB  1 
ATOM   1413 C  CG  . HIS A 1 184 ? -27.076 33.030 13.953  1.00 62.73 ? 408  HIS A CG  1 
ATOM   1414 N  ND1 . HIS A 1 184 ? -26.022 33.852 14.292  1.00 69.61 ? 408  HIS A ND1 1 
ATOM   1415 C  CD2 . HIS A 1 184 ? -26.659 31.765 14.201  1.00 68.55 ? 408  HIS A CD2 1 
ATOM   1416 C  CE1 . HIS A 1 184 ? -25.015 33.117 14.731  1.00 72.38 ? 408  HIS A CE1 1 
ATOM   1417 N  NE2 . HIS A 1 184 ? -25.375 31.847 14.684  1.00 74.72 ? 408  HIS A NE2 1 
ATOM   1418 N  N   . LEU A 1 185 ? -27.724 36.430 13.005  1.00 44.01 ? 409  LEU A N   1 
ATOM   1419 C  CA  . LEU A 1 185 ? -28.122 37.749 13.472  1.00 47.06 ? 409  LEU A CA  1 
ATOM   1420 C  C   . LEU A 1 185 ? -27.640 38.890 12.585  1.00 46.59 ? 409  LEU A C   1 
ATOM   1421 O  O   . LEU A 1 185 ? -28.168 40.005 12.700  1.00 46.37 ? 409  LEU A O   1 
ATOM   1422 C  CB  . LEU A 1 185 ? -27.626 37.963 14.903  1.00 49.91 ? 409  LEU A CB  1 
ATOM   1423 C  CG  . LEU A 1 185 ? -26.668 36.891 15.438  1.00 53.28 ? 409  LEU A CG  1 
ATOM   1424 C  CD1 . LEU A 1 185 ? -25.279 37.064 14.866  1.00 45.95 ? 409  LEU A CD1 1 
ATOM   1425 C  CD2 . LEU A 1 185 ? -26.621 36.893 16.967  1.00 51.71 ? 409  LEU A CD2 1 
ATOM   1426 N  N   . ALA A 1 186 ? -26.676 38.647 11.698  1.00 39.03 ? 410  ALA A N   1 
ATOM   1427 C  CA  . ALA A 1 186 ? -26.089 39.729 10.920  1.00 35.21 ? 410  ALA A CA  1 
ATOM   1428 C  C   . ALA A 1 186 ? -26.944 40.072 9.706   1.00 37.60 ? 410  ALA A C   1 
ATOM   1429 O  O   . ALA A 1 186 ? -27.469 39.190 9.019   1.00 35.91 ? 410  ALA A O   1 
ATOM   1430 C  CB  . ALA A 1 186 ? -24.675 39.363 10.471  1.00 34.57 ? 410  ALA A CB  1 
ATOM   1431 N  N   . ASN A 1 187 ? -27.085 41.369 9.460   1.00 33.62 ? 411  ASN A N   1 
ATOM   1432 C  CA  . ASN A 1 187 ? -27.687 41.868 8.235   1.00 31.81 ? 411  ASN A CA  1 
ATOM   1433 C  C   . ASN A 1 187 ? -26.665 41.827 7.113   1.00 30.55 ? 411  ASN A C   1 
ATOM   1434 O  O   . ASN A 1 187 ? -25.482 42.096 7.331   1.00 31.04 ? 411  ASN A O   1 
ATOM   1435 C  CB  . ASN A 1 187 ? -28.163 43.306 8.427   1.00 36.80 ? 411  ASN A CB  1 
ATOM   1436 C  CG  . ASN A 1 187 ? -29.652 43.406 8.592   1.00 46.94 ? 411  ASN A CG  1 
ATOM   1437 O  OD1 . ASN A 1 187 ? -30.374 43.611 7.615   1.00 54.44 ? 411  ASN A OD1 1 
ATOM   1438 N  ND2 . ASN A 1 187 ? -30.130 43.263 9.830   1.00 46.23 ? 411  ASN A ND2 1 
ATOM   1439 N  N   . ASN A 1 188 ? -27.122 41.503 5.906   1.00 26.12 ? 412  ASN A N   1 
ATOM   1440 C  CA  . ASN A 1 188 ? -26.216 41.538 4.768   1.00 25.23 ? 412  ASN A CA  1 
ATOM   1441 C  C   . ASN A 1 188 ? -25.784 42.974 4.494   1.00 26.34 ? 412  ASN A C   1 
ATOM   1442 O  O   . ASN A 1 188 ? -26.515 43.923 4.775   1.00 24.41 ? 412  ASN A O   1 
ATOM   1443 C  CB  . ASN A 1 188 ? -26.882 40.937 3.534   1.00 22.60 ? 412  ASN A CB  1 
ATOM   1444 C  CG  . ASN A 1 188 ? -26.967 39.428 3.599   1.00 24.49 ? 412  ASN A CG  1 
ATOM   1445 O  OD1 . ASN A 1 188 ? -26.219 38.790 4.341   1.00 24.60 ? 412  ASN A OD1 1 
ATOM   1446 N  ND2 . ASN A 1 188 ? -27.864 38.846 2.812   1.00 22.52 ? 412  ASN A ND2 1 
ATOM   1447 N  N   . ASN A 1 189 ? -24.579 43.133 3.952   1.00 25.45 ? 413  ASN A N   1 
ATOM   1448 C  CA  . ASN A 1 189 ? -24.095 44.467 3.624   1.00 26.51 ? 413  ASN A CA  1 
ATOM   1449 C  C   . ASN A 1 189 ? -23.213 44.398 2.384   1.00 24.19 ? 413  ASN A C   1 
ATOM   1450 O  O   . ASN A 1 189 ? -22.754 43.328 1.974   1.00 26.26 ? 413  ASN A O   1 
ATOM   1451 C  CB  . ASN A 1 189 ? -23.351 45.120 4.805   1.00 28.99 ? 413  ASN A CB  1 
ATOM   1452 C  CG  . ASN A 1 189 ? -22.229 44.241 5.365   1.00 32.06 ? 413  ASN A CG  1 
ATOM   1453 O  OD1 . ASN A 1 189 ? -21.243 43.952 4.678   1.00 32.28 ? 413  ASN A OD1 1 
ATOM   1454 N  ND2 . ASN A 1 189 ? -22.371 43.832 6.627   1.00 30.61 ? 413  ASN A ND2 1 
ATOM   1455 N  N   . HIS A 1 190 ? -23.013 45.566 1.776   1.00 26.01 ? 414  HIS A N   1 
ATOM   1456 C  CA  . HIS A 1 190 ? -22.213 45.726 0.562   1.00 26.75 ? 414  HIS A CA  1 
ATOM   1457 C  C   . HIS A 1 190 ? -22.755 44.882 -0.590  1.00 21.84 ? 414  HIS A C   1 
ATOM   1458 O  O   . HIS A 1 190 ? -21.999 44.411 -1.441  1.00 20.47 ? 414  HIS A O   1 
ATOM   1459 C  CB  . HIS A 1 190 ? -20.735 45.429 0.837   1.00 24.83 ? 414  HIS A CB  1 
ATOM   1460 C  CG  . HIS A 1 190 ? -20.128 46.358 1.841   1.00 33.16 ? 414  HIS A CG  1 
ATOM   1461 N  ND1 . HIS A 1 190 ? -19.923 46.003 3.158   1.00 31.82 ? 414  HIS A ND1 1 
ATOM   1462 C  CD2 . HIS A 1 190 ? -19.731 47.649 1.734   1.00 32.22 ? 414  HIS A CD2 1 
ATOM   1463 C  CE1 . HIS A 1 190 ? -19.404 47.027 3.813   1.00 34.72 ? 414  HIS A CE1 1 
ATOM   1464 N  NE2 . HIS A 1 190 ? -19.283 48.041 2.974   1.00 35.79 ? 414  HIS A NE2 1 
ATOM   1465 N  N   . LEU A 1 191 ? -24.077 44.725 -0.647  1.00 22.38 ? 415  LEU A N   1 
ATOM   1466 C  CA  . LEU A 1 191 ? -24.712 43.922 -1.685  1.00 21.69 ? 415  LEU A CA  1 
ATOM   1467 C  C   . LEU A 1 191 ? -24.734 44.659 -3.019  1.00 25.52 ? 415  LEU A C   1 
ATOM   1468 O  O   . LEU A 1 191 ? -24.996 45.862 -3.072  1.00 19.69 ? 415  LEU A O   1 
ATOM   1469 C  CB  . LEU A 1 191 ? -26.151 43.602 -1.285  1.00 23.88 ? 415  LEU A CB  1 
ATOM   1470 C  CG  . LEU A 1 191 ? -26.385 42.716 -0.063  1.00 26.11 ? 415  LEU A CG  1 
ATOM   1471 C  CD1 . LEU A 1 191 ? -27.827 42.849 0.384   1.00 24.31 ? 415  LEU A CD1 1 
ATOM   1472 C  CD2 . LEU A 1 191 ? -26.049 41.268 -0.394  1.00 19.91 ? 415  LEU A CD2 1 
ATOM   1473 N  N   . ALA A 1 192 ? -24.505 43.934 -4.105  1.00 19.92 ? 416  ALA A N   1 
ATOM   1474 C  CA  . ALA A 1 192 ? -24.874 44.494 -5.400  1.00 23.45 ? 416  ALA A CA  1 
ATOM   1475 C  C   . ALA A 1 192 ? -26.373 44.806 -5.392  1.00 21.58 ? 416  ALA A C   1 
ATOM   1476 O  O   . ALA A 1 192 ? -27.148 44.091 -4.750  1.00 23.89 ? 416  ALA A O   1 
ATOM   1477 C  CB  . ALA A 1 192 ? -24.514 43.525 -6.532  1.00 18.44 ? 416  ALA A CB  1 
ATOM   1478 N  N   . PRO A 1 193 ? -26.816 45.885 -6.037  1.00 22.29 ? 417  PRO A N   1 
ATOM   1479 C  CA  . PRO A 1 193 ? -28.221 46.282 -5.908  1.00 20.86 ? 417  PRO A CA  1 
ATOM   1480 C  C   . PRO A 1 193 ? -29.160 45.385 -6.699  1.00 24.20 ? 417  PRO A C   1 
ATOM   1481 O  O   . PRO A 1 193 ? -28.779 44.703 -7.653  1.00 23.10 ? 417  PRO A O   1 
ATOM   1482 C  CB  . PRO A 1 193 ? -28.240 47.709 -6.467  1.00 23.45 ? 417  PRO A CB  1 
ATOM   1483 C  CG  . PRO A 1 193 ? -27.118 47.708 -7.451  1.00 26.30 ? 417  PRO A CG  1 
ATOM   1484 C  CD  . PRO A 1 193 ? -26.044 46.881 -6.802  1.00 25.30 ? 417  PRO A CD  1 
ATOM   1485 N  N   . ALA A 1 194 ? -30.425 45.433 -6.292  1.00 25.23 ? 418  ALA A N   1 
ATOM   1486 C  CA  . ALA A 1 194 ? -31.504 44.796 -7.030  1.00 27.11 ? 418  ALA A CA  1 
ATOM   1487 C  C   . ALA A 1 194 ? -31.676 45.449 -8.404  1.00 24.89 ? 418  ALA A C   1 
ATOM   1488 O  O   . ALA A 1 194 ? -31.373 46.629 -8.598  1.00 25.64 ? 418  ALA A O   1 
ATOM   1489 C  CB  . ALA A 1 194 ? -32.796 44.887 -6.214  1.00 20.04 ? 418  ALA A CB  1 
ATOM   1490 N  N   . VAL A 1 195 ? -32.161 44.668 -9.370  1.00 23.19 ? 419  VAL A N   1 
ATOM   1491 C  CA  . VAL A 1 195 ? -32.350 45.146 -10.735 1.00 25.82 ? 419  VAL A CA  1 
ATOM   1492 C  C   . VAL A 1 195 ? -33.788 44.902 -11.149 1.00 27.73 ? 419  VAL A C   1 
ATOM   1493 O  O   . VAL A 1 195 ? -34.429 43.948 -10.705 1.00 24.28 ? 419  VAL A O   1 
ATOM   1494 C  CB  . VAL A 1 195 ? -31.399 44.470 -11.741 1.00 23.75 ? 419  VAL A CB  1 
ATOM   1495 C  CG1 . VAL A 1 195 ? -29.950 44.793 -11.398 1.00 26.07 ? 419  VAL A CG1 1 
ATOM   1496 C  CG2 . VAL A 1 195 ? -31.616 42.978 -11.758 1.00 23.25 ? 419  VAL A CG2 1 
ATOM   1497 N  N   . SER A 1 196 ? -34.291 45.772 -12.019 1.00 28.17 ? 420  SER A N   1 
ATOM   1498 C  CA  . SER A 1 196 ? -35.635 45.614 -12.551 1.00 33.29 ? 420  SER A CA  1 
ATOM   1499 C  C   . SER A 1 196 ? -35.745 46.447 -13.816 1.00 32.82 ? 420  SER A C   1 
ATOM   1500 O  O   . SER A 1 196 ? -35.063 47.473 -13.936 1.00 30.41 ? 420  SER A O   1 
ATOM   1501 C  CB  . SER A 1 196 ? -36.691 46.043 -11.520 1.00 33.18 ? 420  SER A CB  1 
ATOM   1502 O  OG  . SER A 1 196 ? -36.399 47.325 -10.999 1.00 35.26 ? 420  SER A OG  1 
ATOM   1503 N  N   . PRO A 1 197 ? -36.578 46.038 -14.773 1.00 29.90 ? 421  PRO A N   1 
ATOM   1504 C  CA  . PRO A 1 197 ? -36.776 46.867 -15.961 1.00 30.93 ? 421  PRO A CA  1 
ATOM   1505 C  C   . PRO A 1 197 ? -37.505 48.140 -15.572 1.00 32.74 ? 421  PRO A C   1 
ATOM   1506 O  O   . PRO A 1 197 ? -38.446 48.119 -14.777 1.00 33.39 ? 421  PRO A O   1 
ATOM   1507 C  CB  . PRO A 1 197 ? -37.631 45.982 -16.871 1.00 24.69 ? 421  PRO A CB  1 
ATOM   1508 C  CG  . PRO A 1 197 ? -38.418 45.152 -15.920 1.00 30.72 ? 421  PRO A CG  1 
ATOM   1509 C  CD  . PRO A 1 197 ? -37.517 44.901 -14.737 1.00 30.36 ? 421  PRO A CD  1 
ATOM   1510 N  N   . LEU A 1 198 ? -37.047 49.259 -16.116 1.00 34.38 ? 422  LEU A N   1 
ATOM   1511 C  CA  . LEU A 1 198 ? -37.669 50.531 -15.794 1.00 40.52 ? 422  LEU A CA  1 
ATOM   1512 C  C   . LEU A 1 198 ? -38.517 51.096 -16.921 1.00 40.17 ? 422  LEU A C   1 
ATOM   1513 O  O   . LEU A 1 198 ? -39.449 51.856 -16.647 1.00 44.82 ? 422  LEU A O   1 
ATOM   1514 C  CB  . LEU A 1 198 ? -36.593 51.545 -15.385 1.00 46.39 ? 422  LEU A CB  1 
ATOM   1515 C  CG  . LEU A 1 198 ? -35.842 51.004 -14.159 1.00 50.74 ? 422  LEU A CG  1 
ATOM   1516 C  CD1 . LEU A 1 198 ? -34.682 51.897 -13.731 1.00 51.57 ? 422  LEU A CD1 1 
ATOM   1517 C  CD2 . LEU A 1 198 ? -36.817 50.765 -12.996 1.00 46.46 ? 422  LEU A CD2 1 
ATOM   1518 N  N   . PHE A 1 199 ? -38.250 50.726 -18.140 1.00 32.69 ? 423  PHE A N   1 
ATOM   1519 C  CA  . PHE A 1 199 ? -38.998 51.253 -19.268 1.00 30.88 ? 423  PHE A CA  1 
ATOM   1520 C  C   . PHE A 1 199 ? -40.228 50.380 -19.527 1.00 29.06 ? 423  PHE A C   1 
ATOM   1521 O  O   . PHE A 1 199 ? -40.111 49.149 -19.530 1.00 25.66 ? 423  PHE A O   1 
ATOM   1522 C  CB  . PHE A 1 199 ? -38.096 51.309 -20.493 1.00 27.46 ? 423  PHE A CB  1 
ATOM   1523 C  CG  . PHE A 1 199 ? -38.645 52.125 -21.607 1.00 29.44 ? 423  PHE A CG  1 
ATOM   1524 C  CD1 . PHE A 1 199 ? -38.769 53.496 -21.475 1.00 32.67 ? 423  PHE A CD1 1 
ATOM   1525 C  CD2 . PHE A 1 199 ? -39.052 51.522 -22.784 1.00 27.26 ? 423  PHE A CD2 1 
ATOM   1526 C  CE1 . PHE A 1 199 ? -39.286 54.252 -22.502 1.00 32.92 ? 423  PHE A CE1 1 
ATOM   1527 C  CE2 . PHE A 1 199 ? -39.568 52.272 -23.818 1.00 29.80 ? 423  PHE A CE2 1 
ATOM   1528 C  CZ  . PHE A 1 199 ? -39.683 53.644 -23.679 1.00 29.82 ? 423  PHE A CZ  1 
ATOM   1529 N  N   . PRO A 1 200 ? -41.415 50.968 -19.708 1.00 31.68 ? 424  PRO A N   1 
ATOM   1530 C  CA  . PRO A 1 200 ? -42.628 50.156 -19.903 1.00 29.99 ? 424  PRO A CA  1 
ATOM   1531 C  C   . PRO A 1 200 ? -42.513 49.189 -21.076 1.00 30.32 ? 424  PRO A C   1 
ATOM   1532 O  O   . PRO A 1 200 ? -41.938 49.508 -22.117 1.00 26.06 ? 424  PRO A O   1 
ATOM   1533 C  CB  . PRO A 1 200 ? -43.721 51.202 -20.159 1.00 28.40 ? 424  PRO A CB  1 
ATOM   1534 C  CG  . PRO A 1 200 ? -43.246 52.416 -19.463 1.00 31.55 ? 424  PRO A CG  1 
ATOM   1535 C  CD  . PRO A 1 200 ? -41.728 52.397 -19.551 1.00 30.70 ? 424  PRO A CD  1 
ATOM   1536 N  N   . GLY A 1 201 ? -43.096 48.001 -20.895 1.00 26.79 ? 425  GLY A N   1 
ATOM   1537 C  CA  . GLY A 1 201 ? -43.074 46.947 -21.878 1.00 24.49 ? 425  GLY A CA  1 
ATOM   1538 C  C   . GLY A 1 201 ? -41.826 46.092 -21.877 1.00 28.09 ? 425  GLY A C   1 
ATOM   1539 O  O   . GLY A 1 201 ? -41.751 45.144 -22.670 1.00 21.70 ? 425  GLY A O   1 
ATOM   1540 N  N   . GLU A 1 202 ? -40.844 46.388 -21.026 1.00 22.64 ? 426  GLU A N   1 
ATOM   1541 C  CA  . GLU A 1 202 ? -39.592 45.643 -21.022 1.00 23.00 ? 426  GLU A CA  1 
ATOM   1542 C  C   . GLU A 1 202 ? -39.528 44.668 -19.849 1.00 21.42 ? 426  GLU A C   1 
ATOM   1543 O  O   . GLU A 1 202 ? -40.132 44.880 -18.796 1.00 20.85 ? 426  GLU A O   1 
ATOM   1544 C  CB  . GLU A 1 202 ? -38.377 46.590 -20.980 1.00 20.76 ? 426  GLU A CB  1 
ATOM   1545 C  CG  . GLU A 1 202 ? -38.120 47.287 -22.309 1.00 24.07 ? 426  GLU A CG  1 
ATOM   1546 C  CD  . GLU A 1 202 ? -36.898 48.204 -22.315 1.00 30.75 ? 426  GLU A CD  1 
ATOM   1547 O  OE1 . GLU A 1 202 ? -36.054 48.141 -21.378 1.00 23.51 ? 426  GLU A OE1 1 
ATOM   1548 O  OE2 . GLU A 1 202 ? -36.792 48.998 -23.283 1.00 26.72 ? 426  GLU A OE2 1 
ATOM   1549 N  N   . GLN A 1 203 ? -38.774 43.589 -20.047 1.00 20.20 ? 427  GLN A N   1 
ATOM   1550 C  CA  . GLN A 1 203 ? -38.498 42.624 -19.002 1.00 22.01 ? 427  GLN A CA  1 
ATOM   1551 C  C   . GLN A 1 203 ? -37.010 42.316 -19.015 1.00 19.94 ? 427  GLN A C   1 
ATOM   1552 O  O   . GLN A 1 203 ? -36.332 42.481 -20.029 1.00 19.67 ? 427  GLN A O   1 
ATOM   1553 C  CB  . GLN A 1 203 ? -39.324 41.336 -19.187 1.00 20.95 ? 427  GLN A CB  1 
ATOM   1554 C  CG  . GLN A 1 203 ? -40.817 41.566 -19.020 1.00 24.94 ? 427  GLN A CG  1 
ATOM   1555 C  CD  . GLN A 1 203 ? -41.644 40.295 -19.142 1.00 28.56 ? 427  GLN A CD  1 
ATOM   1556 O  OE1 . GLN A 1 203 ? -42.796 40.266 -18.713 1.00 24.79 ? 427  GLN A OE1 1 
ATOM   1557 N  NE2 . GLN A 1 203 ? -41.061 39.239 -19.735 1.00 23.36 ? 427  GLN A NE2 1 
ATOM   1558 N  N   . ILE A 1 204 ? -36.494 41.881 -17.872 1.00 20.17 ? 428  ILE A N   1 
ATOM   1559 C  CA  . ILE A 1 204 ? -35.115 41.431 -17.843 1.00 20.70 ? 428  ILE A CA  1 
ATOM   1560 C  C   . ILE A 1 204 ? -34.976 40.185 -18.707 1.00 21.35 ? 428  ILE A C   1 
ATOM   1561 O  O   . ILE A 1 204 ? -35.885 39.348 -18.779 1.00 18.48 ? 428  ILE A O   1 
ATOM   1562 C  CB  . ILE A 1 204 ? -34.663 41.175 -16.399 1.00 19.69 ? 428  ILE A CB  1 
ATOM   1563 C  CG1 . ILE A 1 204 ? -34.544 42.501 -15.658 1.00 24.73 ? 428  ILE A CG1 1 
ATOM   1564 C  CG2 . ILE A 1 204 ? -33.320 40.426 -16.366 1.00 19.10 ? 428  ILE A CG2 1 
ATOM   1565 C  CD1 . ILE A 1 204 ? -34.155 42.346 -14.228 1.00 26.31 ? 428  ILE A CD1 1 
ATOM   1566 N  N   . LEU A 1 205 ? -33.846 40.089 -19.405 1.00 19.88 ? 429  LEU A N   1 
ATOM   1567 C  CA  . LEU A 1 205 ? -33.449 38.899 -20.142 1.00 18.61 ? 429  LEU A CA  1 
ATOM   1568 C  C   . LEU A 1 205 ? -32.467 38.119 -19.280 1.00 20.39 ? 429  LEU A C   1 
ATOM   1569 O  O   . LEU A 1 205 ? -31.405 38.643 -18.923 1.00 20.73 ? 429  LEU A O   1 
ATOM   1570 C  CB  . LEU A 1 205 ? -32.801 39.284 -21.474 1.00 20.92 ? 429  LEU A CB  1 
ATOM   1571 C  CG  . LEU A 1 205 ? -32.295 38.151 -22.374 1.00 22.29 ? 429  LEU A CG  1 
ATOM   1572 C  CD1 . LEU A 1 205 ? -33.468 37.455 -23.017 1.00 21.59 ? 429  LEU A CD1 1 
ATOM   1573 C  CD2 . LEU A 1 205 ? -31.382 38.702 -23.436 1.00 24.02 ? 429  LEU A CD2 1 
ATOM   1574 N  N   . PHE A 1 206 ? -32.819 36.881 -18.942 1.00 18.09 ? 430  PHE A N   1 
ATOM   1575 C  CA  . PHE A 1 206 ? -31.979 36.026 -18.112 1.00 18.57 ? 430  PHE A CA  1 
ATOM   1576 C  C   . PHE A 1 206 ? -31.313 34.950 -18.954 1.00 18.21 ? 430  PHE A C   1 
ATOM   1577 O  O   . PHE A 1 206 ? -31.827 34.535 -19.993 1.00 19.37 ? 430  PHE A O   1 
ATOM   1578 C  CB  . PHE A 1 206 ? -32.775 35.331 -17.004 1.00 19.37 ? 430  PHE A CB  1 
ATOM   1579 C  CG  . PHE A 1 206 ? -33.409 36.274 -16.011 1.00 22.86 ? 430  PHE A CG  1 
ATOM   1580 C  CD1 . PHE A 1 206 ? -32.715 36.696 -14.890 1.00 19.99 ? 430  PHE A CD1 1 
ATOM   1581 C  CD2 . PHE A 1 206 ? -34.712 36.718 -16.192 1.00 23.52 ? 430  PHE A CD2 1 
ATOM   1582 C  CE1 . PHE A 1 206 ? -33.314 37.549 -13.972 1.00 19.31 ? 430  PHE A CE1 1 
ATOM   1583 C  CE2 . PHE A 1 206 ? -35.313 37.578 -15.280 1.00 21.02 ? 430  PHE A CE2 1 
ATOM   1584 C  CZ  . PHE A 1 206 ? -34.616 37.986 -14.170 1.00 22.69 ? 430  PHE A CZ  1 
ATOM   1585 N  N   . PHE A 1 207 ? -30.171 34.493 -18.478 1.00 16.39 ? 431  PHE A N   1 
ATOM   1586 C  CA  . PHE A 1 207 ? -29.471 33.353 -19.051 1.00 16.88 ? 431  PHE A CA  1 
ATOM   1587 C  C   . PHE A 1 207 ? -29.652 32.202 -18.076 1.00 16.17 ? 431  PHE A C   1 
ATOM   1588 O  O   . PHE A 1 207 ? -29.093 32.217 -16.973 1.00 17.70 ? 431  PHE A O   1 
ATOM   1589 C  CB  . PHE A 1 207 ? -28.014 33.713 -19.314 1.00 16.19 ? 431  PHE A CB  1 
ATOM   1590 C  CG  . PHE A 1 207 ? -27.881 34.826 -20.306 1.00 18.80 ? 431  PHE A CG  1 
ATOM   1591 C  CD1 . PHE A 1 207 ? -27.974 36.155 -19.895 1.00 19.16 ? 431  PHE A CD1 1 
ATOM   1592 C  CD2 . PHE A 1 207 ? -27.757 34.552 -21.659 1.00 19.09 ? 431  PHE A CD2 1 
ATOM   1593 C  CE1 . PHE A 1 207 ? -27.895 37.188 -20.817 1.00 16.62 ? 431  PHE A CE1 1 
ATOM   1594 C  CE2 . PHE A 1 207 ? -27.672 35.585 -22.588 1.00 19.50 ? 431  PHE A CE2 1 
ATOM   1595 C  CZ  . PHE A 1 207 ? -27.748 36.896 -22.165 1.00 20.03 ? 431  PHE A CZ  1 
ATOM   1596 N  N   . ARG A 1 208 ? -30.485 31.242 -18.462 1.00 16.34 ? 432  ARG A N   1 
ATOM   1597 C  CA  . ARG A 1 208 ? -30.987 30.226 -17.549 1.00 16.51 ? 432  ARG A CA  1 
ATOM   1598 C  C   . ARG A 1 208 ? -30.247 28.903 -17.737 1.00 17.68 ? 432  ARG A C   1 
ATOM   1599 O  O   . ARG A 1 208 ? -30.011 28.462 -18.867 1.00 18.08 ? 432  ARG A O   1 
ATOM   1600 C  CB  . ARG A 1 208 ? -32.490 30.022 -17.773 1.00 17.94 ? 432  ARG A CB  1 
ATOM   1601 C  CG  . ARG A 1 208 ? -33.099 28.780 -17.146 1.00 19.95 ? 432  ARG A CG  1 
ATOM   1602 C  CD  . ARG A 1 208 ? -34.645 28.859 -17.164 1.00 20.68 ? 432  ARG A CD  1 
ATOM   1603 N  NE  . ARG A 1 208 ? -35.156 29.792 -16.163 1.00 19.75 ? 432  ARG A NE  1 
ATOM   1604 C  CZ  . ARG A 1 208 ? -36.390 29.770 -15.674 1.00 20.21 ? 432  ARG A CZ  1 
ATOM   1605 N  NH1 . ARG A 1 208 ? -37.300 28.919 -16.124 1.00 22.39 ? 432  ARG A NH1 1 
ATOM   1606 N  NH2 . ARG A 1 208 ? -36.709 30.599 -14.687 1.00 19.58 ? 432  ARG A NH2 1 
ATOM   1607 N  N   . SER A 1 209 ? -29.907 28.260 -16.622 1.00 16.81 ? 433  SER A N   1 
ATOM   1608 C  CA  . SER A 1 209 ? -29.398 26.898 -16.644 1.00 17.13 ? 433  SER A CA  1 
ATOM   1609 C  C   . SER A 1 209 ? -30.316 26.012 -15.821 1.00 18.83 ? 433  SER A C   1 
ATOM   1610 O  O   . SER A 1 209 ? -30.994 26.485 -14.912 1.00 17.91 ? 433  SER A O   1 
ATOM   1611 C  CB  . SER A 1 209 ? -27.978 26.815 -16.087 1.00 17.61 ? 433  SER A CB  1 
ATOM   1612 O  OG  . SER A 1 209 ? -27.084 27.563 -16.886 1.00 18.49 ? 433  SER A OG  1 
ATOM   1613 N  N   . PHE A 1 210 ? -30.343 24.722 -16.145 1.00 18.79 ? 434  PHE A N   1 
ATOM   1614 C  CA  . PHE A 1 210 ? -31.099 23.748 -15.362 1.00 20.41 ? 434  PHE A CA  1 
ATOM   1615 C  C   . PHE A 1 210 ? -30.053 22.940 -14.597 1.00 19.70 ? 434  PHE A C   1 
ATOM   1616 O  O   . PHE A 1 210 ? -29.458 22.011 -15.142 1.00 20.76 ? 434  PHE A O   1 
ATOM   1617 C  CB  . PHE A 1 210 ? -31.984 22.882 -16.262 1.00 20.60 ? 434  PHE A CB  1 
ATOM   1618 C  CG  . PHE A 1 210 ? -32.939 23.684 -17.113 1.00 22.52 ? 434  PHE A CG  1 
ATOM   1619 C  CD1 . PHE A 1 210 ? -34.024 24.343 -16.534 1.00 20.05 ? 434  PHE A CD1 1 
ATOM   1620 C  CD2 . PHE A 1 210 ? -32.734 23.814 -18.473 1.00 19.88 ? 434  PHE A CD2 1 
ATOM   1621 C  CE1 . PHE A 1 210 ? -34.897 25.115 -17.311 1.00 22.17 ? 434  PHE A CE1 1 
ATOM   1622 C  CE2 . PHE A 1 210 ? -33.596 24.577 -19.256 1.00 21.78 ? 434  PHE A CE2 1 
ATOM   1623 C  CZ  . PHE A 1 210 ? -34.675 25.227 -18.677 1.00 19.81 ? 434  PHE A CZ  1 
ATOM   1624 N  N   . ILE A 1 211 ? -29.786 23.324 -13.354 1.00 20.01 ? 435  ILE A N   1 
ATOM   1625 C  CA  . ILE A 1 211 ? -28.679 22.698 -12.633 1.00 18.27 ? 435  ILE A CA  1 
ATOM   1626 C  C   . ILE A 1 211 ? -29.150 21.318 -12.198 1.00 19.14 ? 435  ILE A C   1 
ATOM   1627 O  O   . ILE A 1 211 ? -30.366 21.083 -12.136 1.00 18.75 ? 435  ILE A O   1 
ATOM   1628 C  CB  . ILE A 1 211 ? -28.207 23.552 -11.448 1.00 19.04 ? 435  ILE A CB  1 
ATOM   1629 C  CG1 . ILE A 1 211 ? -29.248 23.547 -10.325 1.00 20.50 ? 435  ILE A CG1 1 
ATOM   1630 C  CG2 . ILE A 1 211 ? -27.891 24.996 -11.918 1.00 19.72 ? 435  ILE A CG2 1 
ATOM   1631 C  CD1 . ILE A 1 211 ? -28.710 24.112 -9.009  1.00 21.99 ? 435  ILE A CD1 1 
ATOM   1632 N  N   . PRO A 1 212 ? -28.232 20.380 -11.928 1.00 18.53 ? 436  PRO A N   1 
ATOM   1633 C  CA  . PRO A 1 212 ? -28.636 19.027 -11.536 1.00 18.55 ? 436  PRO A CA  1 
ATOM   1634 C  C   . PRO A 1 212 ? -29.353 18.982 -10.195 1.00 19.38 ? 436  PRO A C   1 
ATOM   1635 O  O   . PRO A 1 212 ? -29.077 19.757 -9.276  1.00 20.12 ? 436  PRO A O   1 
ATOM   1636 C  CB  . PRO A 1 212 ? -27.305 18.269 -11.469 1.00 17.91 ? 436  PRO A CB  1 
ATOM   1637 C  CG  . PRO A 1 212 ? -26.404 19.016 -12.454 1.00 21.36 ? 436  PRO A CG  1 
ATOM   1638 C  CD  . PRO A 1 212 ? -26.789 20.459 -12.234 1.00 19.51 ? 436  PRO A CD  1 
ATOM   1639 N  N   . GLY A 1 213 ? -30.291 18.047 -10.093 1.00 19.65 ? 437  GLY A N   1 
ATOM   1640 C  CA  . GLY A 1 213 ? -30.930 17.727 -8.831  1.00 21.18 ? 437  GLY A CA  1 
ATOM   1641 C  C   . GLY A 1 213 ? -30.369 16.420 -8.298  1.00 21.31 ? 437  GLY A C   1 
ATOM   1642 O  O   . GLY A 1 213 ? -30.093 15.492 -9.060  1.00 24.53 ? 437  GLY A O   1 
ATOM   1643 N  N   . ALA A 1 214 ? -30.181 16.371 -6.986  1.00 22.24 ? 438  ALA A N   1 
ATOM   1644 C  CA  . ALA A 1 214 ? -29.719 15.162 -6.321  1.00 23.45 ? 438  ALA A CA  1 
ATOM   1645 C  C   . ALA A 1 214 ? -30.851 14.350 -5.706  1.00 24.70 ? 438  ALA A C   1 
ATOM   1646 O  O   . ALA A 1 214 ? -30.664 13.163 -5.425  1.00 25.51 ? 438  ALA A O   1 
ATOM   1647 C  CB  . ALA A 1 214 ? -28.705 15.527 -5.233  1.00 28.20 ? 438  ALA A CB  1 
ATOM   1648 N  N   . SER A 1 215 ? -32.015 14.953 -5.504  1.00 26.70 ? 439  SER A N   1 
ATOM   1649 C  CA  . SER A 1 215 ? -33.138 14.271 -4.873  1.00 27.15 ? 439  SER A CA  1 
ATOM   1650 C  C   . SER A 1 215 ? -34.346 15.188 -4.955  1.00 30.38 ? 439  SER A C   1 
ATOM   1651 O  O   . SER A 1 215 ? -34.205 16.407 -5.081  1.00 28.44 ? 439  SER A O   1 
ATOM   1652 C  CB  . SER A 1 215 ? -32.834 13.912 -3.416  1.00 29.91 ? 439  SER A CB  1 
ATOM   1653 O  OG  . SER A 1 215 ? -33.894 13.175 -2.847  1.00 34.67 ? 439  SER A OG  1 
ATOM   1654 N  N   . GLY A 1 216 ? -35.537 14.587 -4.878  1.00 31.83 ? 440  GLY A N   1 
ATOM   1655 C  CA  . GLY A 1 216 ? -36.755 15.370 -4.923  1.00 28.22 ? 440  GLY A CA  1 
ATOM   1656 C  C   . GLY A 1 216 ? -37.062 15.893 -6.322  1.00 27.30 ? 440  GLY A C   1 
ATOM   1657 O  O   . GLY A 1 216 ? -36.391 15.588 -7.306  1.00 28.55 ? 440  GLY A O   1 
ATOM   1658 N  N   . HIS A 1 217 ? -38.099 16.720 -6.385  1.00 23.83 ? 441  HIS A N   1 
ATOM   1659 C  CA  . HIS A 1 217 ? -38.576 17.304 -7.629  1.00 26.31 ? 441  HIS A CA  1 
ATOM   1660 C  C   . HIS A 1 217 ? -38.084 18.736 -7.727  1.00 29.39 ? 441  HIS A C   1 
ATOM   1661 O  O   . HIS A 1 217 ? -38.410 19.561 -6.868  1.00 28.11 ? 441  HIS A O   1 
ATOM   1662 C  CB  . HIS A 1 217 ? -40.100 17.290 -7.688  1.00 29.65 ? 441  HIS A CB  1 
ATOM   1663 C  CG  . HIS A 1 217 ? -40.694 15.926 -7.569  1.00 32.67 ? 441  HIS A CG  1 
ATOM   1664 N  ND1 . HIS A 1 217 ? -41.114 15.203 -8.664  1.00 33.61 ? 441  HIS A ND1 1 
ATOM   1665 C  CD2 . HIS A 1 217 ? -40.938 15.151 -6.487  1.00 34.42 ? 441  HIS A CD2 1 
ATOM   1666 C  CE1 . HIS A 1 217 ? -41.589 14.039 -8.262  1.00 40.55 ? 441  HIS A CE1 1 
ATOM   1667 N  NE2 . HIS A 1 217 ? -41.493 13.983 -6.946  1.00 40.94 ? 441  HIS A NE2 1 
ATOM   1668 N  N   . THR A 1 218 ? -37.324 19.034 -8.775  1.00 29.24 ? 442  THR A N   1 
ATOM   1669 C  CA  . THR A 1 218 ? -36.917 20.406 -9.030  1.00 25.31 ? 442  THR A CA  1 
ATOM   1670 C  C   . THR A 1 218 ? -36.476 20.512 -10.479 1.00 27.68 ? 442  THR A C   1 
ATOM   1671 O  O   . THR A 1 218 ? -35.842 19.599 -11.010 1.00 27.70 ? 442  THR A O   1 
ATOM   1672 C  CB  . THR A 1 218 ? -35.789 20.844 -8.086  1.00 27.97 ? 442  THR A CB  1 
ATOM   1673 O  OG1 . THR A 1 218 ? -35.377 22.179 -8.413  1.00 29.83 ? 442  THR A OG1 1 
ATOM   1674 C  CG2 . THR A 1 218 ? -34.576 19.878 -8.184  1.00 21.53 ? 442  THR A CG2 1 
ATOM   1675 N  N   . ASN A 1 219 ? -36.824 21.619 -11.120 1.00 25.25 ? 443  ASN A N   1 
ATOM   1676 C  CA  . ASN A 1 219 ? -36.267 21.886 -12.433 1.00 26.53 ? 443  ASN A CA  1 
ATOM   1677 C  C   . ASN A 1 219 ? -34.926 22.593 -12.366 1.00 25.25 ? 443  ASN A C   1 
ATOM   1678 O  O   . ASN A 1 219 ? -34.344 22.886 -13.417 1.00 22.35 ? 443  ASN A O   1 
ATOM   1679 C  CB  . ASN A 1 219 ? -37.256 22.687 -13.271 1.00 30.03 ? 443  ASN A CB  1 
ATOM   1680 C  CG  . ASN A 1 219 ? -38.413 21.833 -13.733 1.00 38.67 ? 443  ASN A CG  1 
ATOM   1681 O  OD1 . ASN A 1 219 ? -38.222 20.894 -14.519 1.00 39.45 ? 443  ASN A OD1 1 
ATOM   1682 N  ND2 . ASN A 1 219 ? -39.609 22.120 -13.225 1.00 32.58 ? 443  ASN A ND2 1 
ATOM   1683 N  N   . GLY A 1 220 ? -34.417 22.861 -11.165 1.00 26.49 ? 444  GLY A N   1 
ATOM   1684 C  CA  . GLY A 1 220 ? -33.059 23.371 -11.026 1.00 24.24 ? 444  GLY A CA  1 
ATOM   1685 C  C   . GLY A 1 220 ? -32.821 24.713 -11.682 1.00 20.11 ? 444  GLY A C   1 
ATOM   1686 O  O   . GLY A 1 220 ? -31.693 25.006 -12.085 1.00 20.64 ? 444  GLY A O   1 
ATOM   1687 N  N   . GLU A 1 221 ? -33.854 25.544 -11.797 1.00 20.78 ? 445  GLU A N   1 
ATOM   1688 C  CA  . GLU A 1 221 ? -33.747 26.767 -12.586 1.00 19.90 ? 445  GLU A CA  1 
ATOM   1689 C  C   . GLU A 1 221 ? -32.837 27.782 -11.898 1.00 19.05 ? 445  GLU A C   1 
ATOM   1690 O  O   . GLU A 1 221 ? -33.077 28.175 -10.752 1.00 21.17 ? 445  GLU A O   1 
ATOM   1691 C  CB  . GLU A 1 221 ? -35.141 27.351 -12.840 1.00 22.43 ? 445  GLU A CB  1 
ATOM   1692 C  CG  . GLU A 1 221 ? -35.878 26.643 -13.981 1.00 25.01 ? 445  GLU A CG  1 
ATOM   1693 C  CD  . GLU A 1 221 ? -37.354 26.377 -13.673 1.00 37.42 ? 445  GLU A CD  1 
ATOM   1694 O  OE1 . GLU A 1 221 ? -37.793 26.683 -12.544 1.00 43.64 ? 445  GLU A OE1 1 
ATOM   1695 O  OE2 . GLU A 1 221 ? -38.072 25.858 -14.560 1.00 38.54 ? 445  GLU A OE2 1 
ATOM   1696 N  N   . MET A 1 222 ? -31.791 28.211 -12.605 1.00 19.71 ? 446  MET A N   1 
ATOM   1697 C  CA  . MET A 1 222 ? -30.822 29.169 -12.081 1.00 17.60 ? 446  MET A CA  1 
ATOM   1698 C  C   . MET A 1 222 ? -30.594 30.239 -13.143 1.00 17.73 ? 446  MET A C   1 
ATOM   1699 O  O   . MET A 1 222 ? -29.962 29.969 -14.169 1.00 19.39 ? 446  MET A O   1 
ATOM   1700 C  CB  . MET A 1 222 ? -29.510 28.467 -11.720 1.00 21.06 ? 446  MET A CB  1 
ATOM   1701 C  CG  . MET A 1 222 ? -28.420 29.377 -11.185 1.00 17.47 ? 446  MET A CG  1 
ATOM   1702 S  SD  . MET A 1 222 ? -28.695 29.863 -9.478  1.00 26.43 ? 446  MET A SD  1 
ATOM   1703 C  CE  . MET A 1 222 ? -28.571 28.290 -8.649  1.00 27.72 ? 446  MET A CE  1 
ATOM   1704 N  N   . ASP A 1 223 ? -31.066 31.458 -12.876 1.00 18.66 ? 447  ASP A N   1 
ATOM   1705 C  CA  . ASP A 1 223 ? -31.034 32.557 -13.835 1.00 16.88 ? 447  ASP A CA  1 
ATOM   1706 C  C   . ASP A 1 223 ? -29.927 33.533 -13.468 1.00 20.76 ? 447  ASP A C   1 
ATOM   1707 O  O   . ASP A 1 223 ? -29.914 34.063 -12.351 1.00 18.76 ? 447  ASP A O   1 
ATOM   1708 C  CB  . ASP A 1 223 ? -32.382 33.283 -13.850 1.00 18.44 ? 447  ASP A CB  1 
ATOM   1709 C  CG  . ASP A 1 223 ? -33.494 32.397 -14.326 1.00 21.01 ? 447  ASP A CG  1 
ATOM   1710 O  OD1 . ASP A 1 223 ? -33.265 31.729 -15.352 1.00 22.19 ? 447  ASP A OD1 1 
ATOM   1711 O  OD2 . ASP A 1 223 ? -34.575 32.346 -13.691 1.00 22.76 ? 447  ASP A OD2 1 
ATOM   1712 N  N   . CYS A 1 224 ? -29.019 33.797 -14.403 1.00 17.25 ? 448  CYS A N   1 
ATOM   1713 C  CA  . CYS A 1 224 ? -28.044 34.852 -14.179 1.00 16.79 ? 448  CYS A CA  1 
ATOM   1714 C  C   . CYS A 1 224 ? -28.291 36.018 -15.133 1.00 18.58 ? 448  CYS A C   1 
ATOM   1715 O  O   . CYS A 1 224 ? -28.963 35.887 -16.167 1.00 18.76 ? 448  CYS A O   1 
ATOM   1716 C  CB  . CYS A 1 224 ? -26.610 34.323 -14.303 1.00 17.42 ? 448  CYS A CB  1 
ATOM   1717 S  SG  . CYS A 1 224 ? -26.065 33.882 -15.955 1.00 21.19 ? 448  CYS A SG  1 
ATOM   1718 N  N   . LEU A 1 225 ? -27.751 37.178 -14.748 1.00 16.32 ? 449  LEU A N   1 
ATOM   1719 C  CA  . LEU A 1 225 ? -27.983 38.410 -15.497 1.00 18.23 ? 449  LEU A CA  1 
ATOM   1720 C  C   . LEU A 1 225 ? -27.003 38.581 -16.647 1.00 18.99 ? 449  LEU A C   1 
ATOM   1721 O  O   . LEU A 1 225 ? -27.315 39.279 -17.619 1.00 19.06 ? 449  LEU A O   1 
ATOM   1722 C  CB  . LEU A 1 225 ? -27.877 39.617 -14.571 1.00 16.65 ? 449  LEU A CB  1 
ATOM   1723 C  CG  . LEU A 1 225 ? -28.857 39.665 -13.402 1.00 22.68 ? 449  LEU A CG  1 
ATOM   1724 C  CD1 . LEU A 1 225 ? -28.557 40.855 -12.518 1.00 17.87 ? 449  LEU A CD1 1 
ATOM   1725 C  CD2 . LEU A 1 225 ? -30.296 39.717 -13.909 1.00 21.64 ? 449  LEU A CD2 1 
ATOM   1726 N  N   . LEU A 1 226 ? -25.809 37.987 -16.533 1.00 17.33 ? 450  LEU A N   1 
ATOM   1727 C  CA  . LEU A 1 226 ? -24.747 38.100 -17.521 1.00 16.11 ? 450  LEU A CA  1 
ATOM   1728 C  C   . LEU A 1 226 ? -24.044 36.750 -17.563 1.00 17.34 ? 450  LEU A C   1 
ATOM   1729 O  O   . LEU A 1 226 ? -23.672 36.227 -16.506 1.00 21.41 ? 450  LEU A O   1 
ATOM   1730 C  CB  . LEU A 1 226 ? -23.734 39.191 -17.168 1.00 18.75 ? 450  LEU A CB  1 
ATOM   1731 C  CG  . LEU A 1 226 ? -24.119 40.661 -17.198 1.00 25.38 ? 450  LEU A CG  1 
ATOM   1732 C  CD1 . LEU A 1 226 ? -22.954 41.486 -16.657 1.00 26.65 ? 450  LEU A CD1 1 
ATOM   1733 C  CD2 . LEU A 1 226 ? -24.463 41.078 -18.623 1.00 24.44 ? 450  LEU A CD2 1 
ATOM   1734 N  N   . PRO A 1 227 ? -23.827 36.166 -18.737 1.00 20.25 ? 451  PRO A N   1 
ATOM   1735 C  CA  . PRO A 1 227 ? -22.965 34.978 -18.795 1.00 22.93 ? 451  PRO A CA  1 
ATOM   1736 C  C   . PRO A 1 227 ? -21.576 35.319 -18.274 1.00 21.80 ? 451  PRO A C   1 
ATOM   1737 O  O   . PRO A 1 227 ? -21.118 36.461 -18.369 1.00 16.88 ? 451  PRO A O   1 
ATOM   1738 C  CB  . PRO A 1 227 ? -22.948 34.614 -20.284 1.00 20.99 ? 451  PRO A CB  1 
ATOM   1739 C  CG  . PRO A 1 227 ? -23.384 35.841 -20.995 1.00 21.79 ? 451  PRO A CG  1 
ATOM   1740 C  CD  . PRO A 1 227 ? -24.339 36.540 -20.067 1.00 20.81 ? 451  PRO A CD  1 
ATOM   1741 N  N   . GLN A 1 228 ? -20.908 34.315 -17.694 1.00 21.51 ? 452  GLN A N   1 
ATOM   1742 C  CA  . GLN A 1 228 ? -19.608 34.571 -17.081 1.00 18.32 ? 452  GLN A CA  1 
ATOM   1743 C  C   . GLN A 1 228 ? -18.613 35.136 -18.087 1.00 19.71 ? 452  GLN A C   1 
ATOM   1744 O  O   . GLN A 1 228 ? -17.751 35.945 -17.716 1.00 18.49 ? 452  GLN A O   1 
ATOM   1745 C  CB  . GLN A 1 228 ? -19.071 33.290 -16.437 1.00 20.12 ? 452  GLN A CB  1 
ATOM   1746 C  CG  . GLN A 1 228 ? -17.763 33.464 -15.638 1.00 21.01 ? 452  GLN A CG  1 
ATOM   1747 C  CD  . GLN A 1 228 ? -17.900 34.446 -14.471 1.00 23.87 ? 452  GLN A CD  1 
ATOM   1748 O  OE1 . GLN A 1 228 ? -18.999 34.816 -14.076 1.00 23.57 ? 452  GLN A OE1 1 
ATOM   1749 N  NE2 . GLN A 1 228 ? -16.770 34.875 -13.927 1.00 24.98 ? 452  GLN A NE2 1 
ATOM   1750 N  N   . GLU A 1 229 ? -18.746 34.772 -19.367 1.00 17.42 ? 453  GLU A N   1 
ATOM   1751 C  CA  . GLU A 1 229 ? -17.812 35.277 -20.371 1.00 18.06 ? 453  GLU A CA  1 
ATOM   1752 C  C   . GLU A 1 229 ? -17.975 36.773 -20.600 1.00 17.39 ? 453  GLU A C   1 
ATOM   1753 O  O   . GLU A 1 229 ? -16.993 37.454 -20.910 1.00 17.89 ? 453  GLU A O   1 
ATOM   1754 C  CB  . GLU A 1 229 ? -17.987 34.539 -21.694 1.00 21.90 ? 453  GLU A CB  1 
ATOM   1755 C  CG  . GLU A 1 229 ? -17.486 33.086 -21.701 1.00 21.31 ? 453  GLU A CG  1 
ATOM   1756 C  CD  . GLU A 1 229 ? -18.434 32.108 -21.023 1.00 22.38 ? 453  GLU A CD  1 
ATOM   1757 O  OE1 . GLU A 1 229 ? -19.616 32.476 -20.763 1.00 18.84 ? 453  GLU A OE1 1 
ATOM   1758 O  OE2 . GLU A 1 229 ? -17.991 30.958 -20.750 1.00 21.38 ? 453  GLU A OE2 1 
ATOM   1759 N  N   . PHE A 1 230 ? -19.199 37.301 -20.478 1.00 16.27 ? 454  PHE A N   1 
ATOM   1760 C  CA  . PHE A 1 230 ? -19.365 38.749 -20.533 1.00 19.06 ? 454  PHE A CA  1 
ATOM   1761 C  C   . PHE A 1 230 ? -18.643 39.410 -19.362 1.00 17.30 ? 454  PHE A C   1 
ATOM   1762 O  O   . PHE A 1 230 ? -17.965 40.430 -19.535 1.00 20.71 ? 454  PHE A O   1 
ATOM   1763 C  CB  . PHE A 1 230 ? -20.860 39.126 -20.537 1.00 17.77 ? 454  PHE A CB  1 
ATOM   1764 C  CG  . PHE A 1 230 ? -21.582 38.849 -21.862 1.00 20.81 ? 454  PHE A CG  1 
ATOM   1765 C  CD1 . PHE A 1 230 ? -21.035 38.015 -22.829 1.00 22.87 ? 454  PHE A CD1 1 
ATOM   1766 C  CD2 . PHE A 1 230 ? -22.816 39.440 -22.128 1.00 26.86 ? 454  PHE A CD2 1 
ATOM   1767 C  CE1 . PHE A 1 230 ? -21.701 37.770 -24.035 1.00 22.67 ? 454  PHE A CE1 1 
ATOM   1768 C  CE2 . PHE A 1 230 ? -23.488 39.202 -23.328 1.00 25.36 ? 454  PHE A CE2 1 
ATOM   1769 C  CZ  . PHE A 1 230 ? -22.931 38.365 -24.278 1.00 24.74 ? 454  PHE A CZ  1 
ATOM   1770 N  N   . VAL A 1 231 ? -18.778 38.834 -18.161 1.00 18.51 ? 455  VAL A N   1 
ATOM   1771 C  CA  . VAL A 1 231 ? -18.098 39.361 -16.973 1.00 17.77 ? 455  VAL A CA  1 
ATOM   1772 C  C   . VAL A 1 231 ? -16.590 39.395 -17.188 1.00 19.90 ? 455  VAL A C   1 
ATOM   1773 O  O   . VAL A 1 231 ? -15.918 40.388 -16.878 1.00 18.10 ? 455  VAL A O   1 
ATOM   1774 C  CB  . VAL A 1 231 ? -18.447 38.521 -15.732 1.00 18.92 ? 455  VAL A CB  1 
ATOM   1775 C  CG1 . VAL A 1 231 ? -17.581 38.947 -14.539 1.00 20.46 ? 455  VAL A CG1 1 
ATOM   1776 C  CG2 . VAL A 1 231 ? -19.929 38.623 -15.404 1.00 19.76 ? 455  VAL A CG2 1 
ATOM   1777 N  N   . GLN A 1 232 ? -16.032 38.285 -17.672 1.00 18.57 ? 456  GLN A N   1 
ATOM   1778 C  CA  . GLN A 1 232 ? -14.598 38.226 -17.912 1.00 21.15 ? 456  GLN A CA  1 
ATOM   1779 C  C   . GLN A 1 232 ? -14.173 39.250 -18.952 1.00 20.02 ? 456  GLN A C   1 
ATOM   1780 O  O   . GLN A 1 232 ? -13.136 39.916 -18.797 1.00 22.81 ? 456  GLN A O   1 
ATOM   1781 C  CB  . GLN A 1 232 ? -14.207 36.820 -18.360 1.00 18.55 ? 456  GLN A CB  1 
ATOM   1782 C  CG  . GLN A 1 232 ? -14.566 35.753 -17.384 1.00 20.07 ? 456  GLN A CG  1 
ATOM   1783 C  CD  . GLN A 1 232 ? -14.286 34.357 -17.927 1.00 22.54 ? 456  GLN A CD  1 
ATOM   1784 O  OE1 . GLN A 1 232 ? -14.779 33.971 -18.987 1.00 25.40 ? 456  GLN A OE1 1 
ATOM   1785 N  NE2 . GLN A 1 232 ? -13.484 33.603 -17.202 1.00 26.87 ? 456  GLN A NE2 1 
ATOM   1786 N  N   . HIS A 1 233 ? -14.961 39.380 -20.022 1.00 20.25 ? 457  HIS A N   1 
ATOM   1787 C  CA  . HIS A 1 233 ? -14.618 40.293 -21.108 1.00 20.02 ? 457  HIS A CA  1 
ATOM   1788 C  C   . HIS A 1 233 ? -14.634 41.742 -20.643 1.00 20.53 ? 457  HIS A C   1 
ATOM   1789 O  O   . HIS A 1 233 ? -13.703 42.504 -20.932 1.00 21.59 ? 457  HIS A O   1 
ATOM   1790 C  CB  . HIS A 1 233 ? -15.581 40.102 -22.275 1.00 23.68 ? 457  HIS A CB  1 
ATOM   1791 C  CG  . HIS A 1 233 ? -15.215 40.905 -23.480 1.00 25.18 ? 457  HIS A CG  1 
ATOM   1792 N  ND1 . HIS A 1 233 ? -14.171 40.562 -24.311 1.00 26.08 ? 457  HIS A ND1 1 
ATOM   1793 C  CD2 . HIS A 1 233 ? -15.740 42.047 -23.985 1.00 25.80 ? 457  HIS A CD2 1 
ATOM   1794 C  CE1 . HIS A 1 233 ? -14.081 41.446 -25.288 1.00 32.85 ? 457  HIS A CE1 1 
ATOM   1795 N  NE2 . HIS A 1 233 ? -15.023 42.357 -25.115 1.00 27.10 ? 457  HIS A NE2 1 
ATOM   1796 N  N   . PHE A 1 234 ? -15.687 42.143 -19.917 1.00 21.29 ? 458  PHE A N   1 
ATOM   1797 C  CA  . PHE A 1 234 ? -15.762 43.519 -19.419 1.00 21.00 ? 458  PHE A CA  1 
ATOM   1798 C  C   . PHE A 1 234 ? -14.609 43.813 -18.470 1.00 22.05 ? 458  PHE A C   1 
ATOM   1799 O  O   . PHE A 1 234 ? -14.004 44.892 -18.517 1.00 20.06 ? 458  PHE A O   1 
ATOM   1800 C  CB  . PHE A 1 234 ? -17.094 43.769 -18.709 1.00 19.40 ? 458  PHE A CB  1 
ATOM   1801 C  CG  . PHE A 1 234 ? -18.294 43.566 -19.588 1.00 19.52 ? 458  PHE A CG  1 
ATOM   1802 C  CD1 . PHE A 1 234 ? -18.179 43.648 -20.959 1.00 18.91 ? 458  PHE A CD1 1 
ATOM   1803 C  CD2 . PHE A 1 234 ? -19.529 43.285 -19.039 1.00 21.87 ? 458  PHE A CD2 1 
ATOM   1804 C  CE1 . PHE A 1 234 ? -19.266 43.449 -21.764 1.00 24.64 ? 458  PHE A CE1 1 
ATOM   1805 C  CE2 . PHE A 1 234 ? -20.627 43.084 -19.852 1.00 20.34 ? 458  PHE A CE2 1 
ATOM   1806 C  CZ  . PHE A 1 234 ? -20.490 43.170 -21.208 1.00 19.43 ? 458  PHE A CZ  1 
ATOM   1807 N  N   . TYR A 1 235 ? -14.289 42.853 -17.607 1.00 21.77 ? 459  TYR A N   1 
ATOM   1808 C  CA  . TYR A 1 235 ? -13.131 42.990 -16.731 1.00 22.68 ? 459  TYR A CA  1 
ATOM   1809 C  C   . TYR A 1 235 ? -11.849 43.183 -17.533 1.00 20.68 ? 459  TYR A C   1 
ATOM   1810 O  O   . TYR A 1 235 ? -11.026 44.043 -17.201 1.00 22.30 ? 459  TYR A O   1 
ATOM   1811 C  CB  . TYR A 1 235 ? -13.033 41.759 -15.833 1.00 24.05 ? 459  TYR A CB  1 
ATOM   1812 C  CG  . TYR A 1 235 ? -11.992 41.869 -14.749 1.00 26.04 ? 459  TYR A CG  1 
ATOM   1813 C  CD1 . TYR A 1 235 ? -12.205 42.689 -13.649 1.00 27.26 ? 459  TYR A CD1 1 
ATOM   1814 C  CD2 . TYR A 1 235 ? -10.808 41.136 -14.815 1.00 23.96 ? 459  TYR A CD2 1 
ATOM   1815 C  CE1 . TYR A 1 235 ? -11.275 42.791 -12.647 1.00 30.87 ? 459  TYR A CE1 1 
ATOM   1816 C  CE2 . TYR A 1 235 ? -9.868  41.229 -13.812 1.00 32.37 ? 459  TYR A CE2 1 
ATOM   1817 C  CZ  . TYR A 1 235 ? -10.111 42.062 -12.728 1.00 29.55 ? 459  TYR A CZ  1 
ATOM   1818 O  OH  . TYR A 1 235 ? -9.196  42.172 -11.715 1.00 41.71 ? 459  TYR A OH  1 
ATOM   1819 N  N   . GLN A 1 236 ? -11.664 42.398 -18.600 1.00 20.60 ? 460  GLN A N   1 
ATOM   1820 C  CA  . GLN A 1 236 ? -10.462 42.549 -19.415 1.00 25.10 ? 460  GLN A CA  1 
ATOM   1821 C  C   . GLN A 1 236 ? -10.409 43.923 -20.070 1.00 27.62 ? 460  GLN A C   1 
ATOM   1822 O  O   . GLN A 1 236 ? -9.358  44.572 -20.076 1.00 25.81 ? 460  GLN A O   1 
ATOM   1823 C  CB  . GLN A 1 236 ? -10.394 41.461 -20.488 1.00 24.17 ? 460  GLN A CB  1 
ATOM   1824 C  CG  . GLN A 1 236 ? -9.963  40.088 -19.973 1.00 26.39 ? 460  GLN A CG  1 
ATOM   1825 C  CD  . GLN A 1 236 ? -8.565  40.114 -19.372 1.00 27.47 ? 460  GLN A CD  1 
ATOM   1826 O  OE1 . GLN A 1 236 ? -7.617  40.594 -19.997 1.00 27.03 ? 460  GLN A OE1 1 
ATOM   1827 N  NE2 . GLN A 1 236 ? -8.436  39.618 -18.145 1.00 25.25 ? 460  GLN A NE2 1 
ATOM   1828 N  N   . GLU A 1 237 ? -11.536 44.387 -20.622 1.00 24.59 ? 461  GLU A N   1 
ATOM   1829 C  CA  . GLU A 1 237 ? -11.503 45.558 -21.497 1.00 28.68 ? 461  GLU A CA  1 
ATOM   1830 C  C   . GLU A 1 237 ? -11.432 46.875 -20.728 1.00 28.85 ? 461  GLU A C   1 
ATOM   1831 O  O   . GLU A 1 237 ? -10.755 47.808 -21.172 1.00 29.74 ? 461  GLU A O   1 
ATOM   1832 C  CB  . GLU A 1 237 ? -12.721 45.559 -22.421 1.00 28.49 ? 461  GLU A CB  1 
ATOM   1833 C  CG  . GLU A 1 237 ? -12.652 44.508 -23.511 1.00 29.88 ? 461  GLU A CG  1 
ATOM   1834 C  CD  . GLU A 1 237 ? -11.500 44.767 -24.464 1.00 40.43 ? 461  GLU A CD  1 
ATOM   1835 O  OE1 . GLU A 1 237 ? -11.597 45.715 -25.280 1.00 46.79 ? 461  GLU A OE1 1 
ATOM   1836 O  OE2 . GLU A 1 237 ? -10.492 44.036 -24.383 1.00 39.03 ? 461  GLU A OE2 1 
ATOM   1837 N  N   . ALA A 1 238 ? -12.129 46.977 -19.595 1.00 27.26 ? 462  ALA A N   1 
ATOM   1838 C  CA  . ALA A 1 238 ? -12.245 48.236 -18.853 1.00 29.52 ? 462  ALA A CA  1 
ATOM   1839 C  C   . ALA A 1 238 ? -12.583 49.395 -19.787 1.00 31.53 ? 462  ALA A C   1 
ATOM   1840 O  O   . ALA A 1 238 ? -12.000 50.476 -19.703 1.00 30.17 ? 462  ALA A O   1 
ATOM   1841 C  CB  . ALA A 1 238 ? -10.972 48.533 -18.062 1.00 33.13 ? 462  ALA A CB  1 
ATOM   1842 N  N   . ALA A 1 239 ? -13.518 49.154 -20.703 1.00 27.14 ? 463  ALA A N   1 
ATOM   1843 C  CA  . ALA A 1 239 ? -13.916 50.161 -21.677 1.00 31.77 ? 463  ALA A CA  1 
ATOM   1844 C  C   . ALA A 1 239 ? -14.888 51.136 -21.039 1.00 32.17 ? 463  ALA A C   1 
ATOM   1845 O  O   . ALA A 1 239 ? -15.709 50.752 -20.210 1.00 34.33 ? 463  ALA A O   1 
ATOM   1846 C  CB  . ALA A 1 239 ? -14.571 49.514 -22.897 1.00 30.39 ? 463  ALA A CB  1 
ATOM   1847 N  N   . THR A 1 240 ? -14.804 52.397 -21.432 1.00 29.60 ? 464  THR A N   1 
ATOM   1848 C  CA  . THR A 1 240 ? -15.694 53.399 -20.858 1.00 33.08 ? 464  THR A CA  1 
ATOM   1849 C  C   . THR A 1 240 ? -17.078 53.285 -21.485 1.00 26.18 ? 464  THR A C   1 
ATOM   1850 O  O   . THR A 1 240 ? -17.211 53.174 -22.708 1.00 28.91 ? 464  THR A O   1 
ATOM   1851 C  CB  . THR A 1 240 ? -15.127 54.805 -21.053 1.00 40.15 ? 464  THR A CB  1 
ATOM   1852 O  OG1 . THR A 1 240 ? -14.884 55.042 -22.446 1.00 47.75 ? 464  THR A OG1 1 
ATOM   1853 C  CG2 . THR A 1 240 ? -13.818 54.955 -20.279 1.00 35.27 ? 464  THR A CG2 1 
ATOM   1854 N  N   . ALA A 1 241 ? -18.105 53.262 -20.642 1.00 21.56 ? 465  ALA A N   1 
ATOM   1855 C  CA  . ALA A 1 241 ? -19.481 53.266 -21.123 1.00 28.91 ? 465  ALA A CA  1 
ATOM   1856 C  C   . ALA A 1 241 ? -19.816 54.678 -21.595 1.00 25.94 ? 465  ALA A C   1 
ATOM   1857 O  O   . ALA A 1 241 ? -19.894 55.609 -20.788 1.00 28.62 ? 465  ALA A O   1 
ATOM   1858 C  CB  . ALA A 1 241 ? -20.437 52.791 -20.032 1.00 24.68 ? 465  ALA A CB  1 
ATOM   1859 N  N   . ARG A 1 242 ? -20.008 54.835 -22.908 1.00 24.95 ? 466  ARG A N   1 
ATOM   1860 C  CA  . ARG A 1 242 ? -20.287 56.140 -23.499 1.00 22.75 ? 466  ARG A CA  1 
ATOM   1861 C  C   . ARG A 1 242 ? -21.705 56.622 -23.216 1.00 27.87 ? 466  ARG A C   1 
ATOM   1862 O  O   . ARG A 1 242 ? -21.995 57.809 -23.402 1.00 24.11 ? 466  ARG A O   1 
ATOM   1863 C  CB  . ARG A 1 242 ? -20.037 56.068 -25.001 1.00 24.20 ? 466  ARG A CB  1 
ATOM   1864 C  CG  . ARG A 1 242 ? -18.622 55.599 -25.349 1.00 25.33 ? 466  ARG A CG  1 
ATOM   1865 C  CD  . ARG A 1 242 ? -17.662 56.739 -25.145 1.00 35.19 ? 466  ARG A CD  1 
ATOM   1866 N  NE  . ARG A 1 242 ? -17.962 57.817 -26.077 1.00 33.07 ? 466  ARG A NE  1 
ATOM   1867 C  CZ  . ARG A 1 242 ? -17.627 59.088 -25.902 1.00 34.98 ? 466  ARG A CZ  1 
ATOM   1868 N  NH1 . ARG A 1 242 ? -17.024 59.500 -24.794 1.00 34.57 ? 466  ARG A NH1 1 
ATOM   1869 N  NH2 . ARG A 1 242 ? -17.898 59.966 -26.867 1.00 35.14 ? 466  ARG A NH2 1 
ATOM   1870 N  N   . SER A 1 243 ? -22.596 55.731 -22.793 1.00 26.19 ? 467  SER A N   1 
ATOM   1871 C  CA  . SER A 1 243 ? -23.939 56.107 -22.374 1.00 27.87 ? 467  SER A CA  1 
ATOM   1872 C  C   . SER A 1 243 ? -24.367 55.094 -21.331 1.00 26.08 ? 467  SER A C   1 
ATOM   1873 O  O   . SER A 1 243 ? -23.594 54.214 -20.952 1.00 26.98 ? 467  SER A O   1 
ATOM   1874 C  CB  . SER A 1 243 ? -24.916 56.144 -23.551 1.00 22.73 ? 467  SER A CB  1 
ATOM   1875 O  OG  . SER A 1 243 ? -25.133 54.830 -24.049 1.00 20.20 ? 467  SER A OG  1 
ATOM   1876 N  N   . GLU A 1 244 ? -25.614 55.206 -20.875 1.00 26.95 ? 468  GLU A N   1 
ATOM   1877 C  CA  . GLU A 1 244 ? -26.097 54.310 -19.835 1.00 27.29 ? 468  GLU A CA  1 
ATOM   1878 C  C   . GLU A 1 244 ? -26.527 52.948 -20.369 1.00 24.82 ? 468  GLU A C   1 
ATOM   1879 O  O   . GLU A 1 244 ? -26.741 52.035 -19.567 1.00 23.94 ? 468  GLU A O   1 
ATOM   1880 C  CB  . GLU A 1 244 ? -27.268 54.953 -19.079 1.00 28.34 ? 468  GLU A CB  1 
ATOM   1881 C  CG  . GLU A 1 244 ? -26.852 56.072 -18.119 1.00 34.52 ? 468  GLU A CG  1 
ATOM   1882 C  CD  . GLU A 1 244 ? -25.955 55.571 -16.989 1.00 45.49 ? 468  GLU A CD  1 
ATOM   1883 O  OE1 . GLU A 1 244 ? -26.421 54.730 -16.187 1.00 52.08 ? 468  GLU A OE1 1 
ATOM   1884 O  OE2 . GLU A 1 244 ? -24.779 56.004 -16.910 1.00 50.52 ? 468  GLU A OE2 1 
ATOM   1885 N  N   . VAL A 1 245 ? -26.702 52.801 -21.683 1.00 22.13 ? 469  VAL A N   1 
ATOM   1886 C  CA  . VAL A 1 245 ? -27.191 51.559 -22.275 1.00 19.68 ? 469  VAL A CA  1 
ATOM   1887 C  C   . VAL A 1 245 ? -26.378 51.236 -23.518 1.00 19.37 ? 469  VAL A C   1 
ATOM   1888 O  O   . VAL A 1 245 ? -26.238 52.074 -24.415 1.00 20.50 ? 469  VAL A O   1 
ATOM   1889 C  CB  . VAL A 1 245 ? -28.683 51.634 -22.646 1.00 22.78 ? 469  VAL A CB  1 
ATOM   1890 C  CG1 . VAL A 1 245 ? -29.099 50.352 -23.347 1.00 19.15 ? 469  VAL A CG1 1 
ATOM   1891 C  CG2 . VAL A 1 245 ? -29.529 51.881 -21.408 1.00 20.46 ? 469  VAL A CG2 1 
ATOM   1892 N  N   . ALA A 1 246 ? -25.854 50.020 -23.579 1.00 18.59 ? 470  ALA A N   1 
ATOM   1893 C  CA  . ALA A 1 246 ? -25.285 49.493 -24.808 1.00 18.50 ? 470  ALA A CA  1 
ATOM   1894 C  C   . ALA A 1 246 ? -26.389 48.755 -25.560 1.00 18.51 ? 470  ALA A C   1 
ATOM   1895 O  O   . ALA A 1 246 ? -26.983 47.810 -25.025 1.00 20.85 ? 470  ALA A O   1 
ATOM   1896 C  CB  . ALA A 1 246 ? -24.102 48.567 -24.502 1.00 18.08 ? 470  ALA A CB  1 
ATOM   1897 N  N   . LEU A 1 247 ? -26.691 49.204 -26.775 1.00 18.85 ? 471  LEU A N   1 
ATOM   1898 C  CA  . LEU A 1 247 ? -27.679 48.518 -27.597 1.00 18.93 ? 471  LEU A CA  1 
ATOM   1899 C  C   . LEU A 1 247 ? -27.026 47.308 -28.257 1.00 19.55 ? 471  LEU A C   1 
ATOM   1900 O  O   . LEU A 1 247 ? -25.986 47.435 -28.915 1.00 19.61 ? 471  LEU A O   1 
ATOM   1901 C  CB  . LEU A 1 247 ? -28.254 49.460 -28.655 1.00 19.48 ? 471  LEU A CB  1 
ATOM   1902 C  CG  . LEU A 1 247 ? -29.241 48.846 -29.662 1.00 19.68 ? 471  LEU A CG  1 
ATOM   1903 C  CD1 . LEU A 1 247 ? -30.560 48.536 -29.014 1.00 19.73 ? 471  LEU A CD1 1 
ATOM   1904 C  CD2 . LEU A 1 247 ? -29.456 49.769 -30.840 1.00 20.25 ? 471  LEU A CD2 1 
ATOM   1905 N  N   . LEU A 1 248 ? -27.626 46.139 -28.066 1.00 18.37 ? 472  LEU A N   1 
ATOM   1906 C  CA  . LEU A 1 248 ? -27.134 44.879 -28.608 1.00 18.82 ? 472  LEU A CA  1 
ATOM   1907 C  C   . LEU A 1 248 ? -28.142 44.333 -29.613 1.00 21.75 ? 472  LEU A C   1 
ATOM   1908 O  O   . LEU A 1 248 ? -29.344 44.590 -29.493 1.00 20.79 ? 472  LEU A O   1 
ATOM   1909 C  CB  . LEU A 1 248 ? -26.909 43.842 -27.488 1.00 18.36 ? 472  LEU A CB  1 
ATOM   1910 C  CG  . LEU A 1 248 ? -25.521 43.713 -26.841 1.00 25.33 ? 472  LEU A CG  1 
ATOM   1911 C  CD1 . LEU A 1 248 ? -24.893 45.066 -26.532 1.00 19.65 ? 472  LEU A CD1 1 
ATOM   1912 C  CD2 . LEU A 1 248 ? -25.592 42.851 -25.587 1.00 19.37 ? 472  LEU A CD2 1 
ATOM   1913 N  N   . ARG A 1 249 ? -27.648 43.569 -30.600 1.00 19.20 ? 473  ARG A N   1 
ATOM   1914 C  CA  . ARG A 1 249 ? -28.485 42.929 -31.615 1.00 20.04 ? 473  ARG A CA  1 
ATOM   1915 C  C   . ARG A 1 249 ? -28.155 41.439 -31.691 1.00 22.03 ? 473  ARG A C   1 
ATOM   1916 O  O   . ARG A 1 249 ? -26.985 41.061 -31.800 1.00 19.97 ? 473  ARG A O   1 
ATOM   1917 C  CB  . ARG A 1 249 ? -28.294 43.590 -32.985 1.00 20.52 ? 473  ARG A CB  1 
ATOM   1918 C  CG  . ARG A 1 249 ? -29.246 43.106 -34.086 1.00 23.06 ? 473  ARG A CG  1 
ATOM   1919 C  CD  . ARG A 1 249 ? -29.047 43.901 -35.371 1.00 20.56 ? 473  ARG A CD  1 
ATOM   1920 N  NE  . ARG A 1 249 ? -29.468 45.287 -35.200 1.00 26.13 ? 473  ARG A NE  1 
ATOM   1921 C  CZ  . ARG A 1 249 ? -28.965 46.317 -35.863 1.00 24.54 ? 473  ARG A CZ  1 
ATOM   1922 N  NH1 . ARG A 1 249 ? -28.040 46.158 -36.798 1.00 22.47 ? 473  ARG A NH1 1 
ATOM   1923 N  NH2 . ARG A 1 249 ? -29.379 47.542 -35.559 1.00 25.39 ? 473  ARG A NH2 1 
ATOM   1924 N  N   . PHE A 1 250 ? -29.181 40.592 -31.627 1.00 20.95 ? 474  PHE A N   1 
ATOM   1925 C  CA  . PHE A 1 250 ? -28.995 39.145 -31.721 1.00 21.81 ? 474  PHE A CA  1 
ATOM   1926 C  C   . PHE A 1 250 ? -29.119 38.726 -33.187 1.00 20.84 ? 474  PHE A C   1 
ATOM   1927 O  O   . PHE A 1 250 ? -30.162 38.945 -33.811 1.00 19.67 ? 474  PHE A O   1 
ATOM   1928 C  CB  . PHE A 1 250 ? -30.022 38.424 -30.844 1.00 19.78 ? 474  PHE A CB  1 
ATOM   1929 C  CG  . PHE A 1 250 ? -29.701 36.971 -30.588 1.00 21.04 ? 474  PHE A CG  1 
ATOM   1930 C  CD1 . PHE A 1 250 ? -28.804 36.613 -29.600 1.00 19.87 ? 474  PHE A CD1 1 
ATOM   1931 C  CD2 . PHE A 1 250 ? -30.300 35.965 -31.340 1.00 22.85 ? 474  PHE A CD2 1 
ATOM   1932 C  CE1 . PHE A 1 250 ? -28.505 35.274 -29.363 1.00 22.07 ? 474  PHE A CE1 1 
ATOM   1933 C  CE2 . PHE A 1 250 ? -30.005 34.631 -31.108 1.00 18.89 ? 474  PHE A CE2 1 
ATOM   1934 C  CZ  . PHE A 1 250 ? -29.113 34.287 -30.109 1.00 20.57 ? 474  PHE A CZ  1 
ATOM   1935 N  N   . VAL A 1 251 ? -28.056 38.151 -33.754 1.00 18.43 ? 475  VAL A N   1 
ATOM   1936 C  CA  . VAL A 1 251 ? -28.052 37.864 -35.184 1.00 19.39 ? 475  VAL A CA  1 
ATOM   1937 C  C   . VAL A 1 251 ? -27.687 36.410 -35.439 1.00 21.11 ? 475  VAL A C   1 
ATOM   1938 O  O   . VAL A 1 251 ? -26.939 35.786 -34.678 1.00 18.59 ? 475  VAL A O   1 
ATOM   1939 C  CB  . VAL A 1 251 ? -27.101 38.801 -35.970 1.00 24.04 ? 475  VAL A CB  1 
ATOM   1940 C  CG1 . VAL A 1 251 ? -27.393 40.271 -35.645 1.00 26.59 ? 475  VAL A CG1 1 
ATOM   1941 C  CG2 . VAL A 1 251 ? -25.652 38.463 -35.687 1.00 24.88 ? 475  VAL A CG2 1 
ATOM   1942 N  N   . ASN A 1 252 ? -28.236 35.874 -36.532 1.00 20.97 ? 476  ASN A N   1 
ATOM   1943 C  CA  . ASN A 1 252 ? -27.954 34.514 -36.966 1.00 25.78 ? 476  ASN A CA  1 
ATOM   1944 C  C   . ASN A 1 252 ? -26.911 34.572 -38.068 1.00 23.65 ? 476  ASN A C   1 
ATOM   1945 O  O   . ASN A 1 252 ? -27.224 35.025 -39.176 1.00 20.98 ? 476  ASN A O   1 
ATOM   1946 C  CB  . ASN A 1 252 ? -29.226 33.833 -37.470 1.00 29.46 ? 476  ASN A CB  1 
ATOM   1947 C  CG  . ASN A 1 252 ? -28.993 32.385 -37.888 1.00 30.14 ? 476  ASN A CG  1 
ATOM   1948 O  OD1 . ASN A 1 252 ? -27.888 31.871 -37.783 1.00 30.10 ? 476  ASN A OD1 1 
ATOM   1949 N  ND2 . ASN A 1 252 ? -30.044 31.726 -38.351 1.00 30.56 ? 476  ASN A ND2 1 
ATOM   1950 N  N   . PRO A 1 253 ? -25.676 34.131 -37.823 1.00 29.45 ? 477  PRO A N   1 
ATOM   1951 C  CA  . PRO A 1 253 ? -24.635 34.256 -38.854 1.00 26.00 ? 477  PRO A CA  1 
ATOM   1952 C  C   . PRO A 1 253 ? -24.860 33.362 -40.057 1.00 30.96 ? 477  PRO A C   1 
ATOM   1953 O  O   . PRO A 1 253 ? -24.322 33.666 -41.129 1.00 34.52 ? 477  PRO A O   1 
ATOM   1954 C  CB  . PRO A 1 253 ? -23.352 33.865 -38.109 1.00 24.69 ? 477  PRO A CB  1 
ATOM   1955 C  CG  . PRO A 1 253 ? -23.824 32.930 -37.041 1.00 31.67 ? 477  PRO A CG  1 
ATOM   1956 C  CD  . PRO A 1 253 ? -25.175 33.474 -36.606 1.00 29.33 ? 477  PRO A CD  1 
ATOM   1957 N  N   . ASP A 1 254 ? -25.629 32.281 -39.924 1.00 29.11 ? 478  ASP A N   1 
ATOM   1958 C  CA  . ASP A 1 254 ? -25.872 31.409 -41.072 1.00 34.52 ? 478  ASP A CA  1 
ATOM   1959 C  C   . ASP A 1 254 ? -26.577 32.158 -42.190 1.00 36.22 ? 478  ASP A C   1 
ATOM   1960 O  O   . ASP A 1 254 ? -26.291 31.941 -43.373 1.00 36.61 ? 478  ASP A O   1 
ATOM   1961 C  CB  . ASP A 1 254 ? -26.716 30.200 -40.670 1.00 35.90 ? 478  ASP A CB  1 
ATOM   1962 C  CG  . ASP A 1 254 ? -26.102 29.402 -39.541 1.00 39.78 ? 478  ASP A CG  1 
ATOM   1963 O  OD1 . ASP A 1 254 ? -24.878 29.525 -39.313 1.00 40.23 ? 478  ASP A OD1 1 
ATOM   1964 O  OD2 . ASP A 1 254 ? -26.857 28.636 -38.891 1.00 46.99 ? 478  ASP A OD2 1 
ATOM   1965 N  N   . THR A 1 255 ? -27.509 33.038 -41.833 1.00 33.39 ? 479  THR A N   1 
ATOM   1966 C  CA  . THR A 1 255 ? -28.345 33.721 -42.802 1.00 37.07 ? 479  THR A CA  1 
ATOM   1967 C  C   . THR A 1 255 ? -28.219 35.236 -42.762 1.00 32.93 ? 479  THR A C   1 
ATOM   1968 O  O   . THR A 1 255 ? -28.819 35.903 -43.606 1.00 30.90 ? 479  THR A O   1 
ATOM   1969 C  CB  . THR A 1 255 ? -29.821 33.350 -42.585 1.00 36.99 ? 479  THR A CB  1 
ATOM   1970 O  OG1 . THR A 1 255 ? -30.247 33.832 -41.304 1.00 35.36 ? 479  THR A OG1 1 
ATOM   1971 C  CG2 . THR A 1 255 ? -30.008 31.835 -42.632 1.00 41.43 ? 479  THR A CG2 1 
ATOM   1972 N  N   . GLY A 1 256 ? -27.477 35.800 -41.810 1.00 32.75 ? 480  GLY A N   1 
ATOM   1973 C  CA  . GLY A 1 256 ? -27.403 37.244 -41.683 1.00 35.32 ? 480  GLY A CA  1 
ATOM   1974 C  C   . GLY A 1 256 ? -28.669 37.900 -41.177 1.00 25.27 ? 480  GLY A C   1 
ATOM   1975 O  O   . GLY A 1 256 ? -28.721 39.131 -41.095 1.00 35.85 ? 480  GLY A O   1 
ATOM   1976 N  N   . ARG A 1 257 ? -29.688 37.117 -40.850 1.00 26.27 ? 481  ARG A N   1 
ATOM   1977 C  CA  . ARG A 1 257 ? -30.915 37.644 -40.279 1.00 31.33 ? 481  ARG A CA  1 
ATOM   1978 C  C   . ARG A 1 257 ? -30.665 38.131 -38.855 1.00 29.61 ? 481  ARG A C   1 
ATOM   1979 O  O   . ARG A 1 257 ? -30.056 37.429 -38.040 1.00 26.71 ? 481  ARG A O   1 
ATOM   1980 C  CB  . ARG A 1 257 ? -31.993 36.559 -40.285 1.00 35.19 ? 481  ARG A CB  1 
ATOM   1981 C  CG  . ARG A 1 257 ? -33.412 37.063 -40.088 1.00 35.29 ? 481  ARG A CG  1 
ATOM   1982 C  CD  . ARG A 1 257 ? -34.366 35.895 -39.862 1.00 38.32 ? 481  ARG A CD  1 
ATOM   1983 N  NE  . ARG A 1 257 ? -35.744 36.349 -39.750 1.00 43.02 ? 481  ARG A NE  1 
ATOM   1984 C  CZ  . ARG A 1 257 ? -36.609 36.404 -40.756 1.00 43.04 ? 481  ARG A CZ  1 
ATOM   1985 N  NH1 . ARG A 1 257 ? -36.296 35.968 -41.968 1.00 40.57 ? 481  ARG A NH1 1 
ATOM   1986 N  NH2 . ARG A 1 257 ? -37.819 36.913 -40.540 1.00 39.86 ? 481  ARG A NH2 1 
ATOM   1987 N  N   . ALA A 1 258 ? -31.125 39.337 -38.559 1.00 23.43 ? 482  ALA A N   1 
ATOM   1988 C  CA  . ALA A 1 258 ? -31.090 39.856 -37.203 1.00 24.67 ? 482  ALA A CA  1 
ATOM   1989 C  C   . ALA A 1 258 ? -32.438 39.576 -36.552 1.00 23.03 ? 482  ALA A C   1 
ATOM   1990 O  O   . ALA A 1 258 ? -33.485 39.798 -37.164 1.00 24.56 ? 482  ALA A O   1 
ATOM   1991 C  CB  . ALA A 1 258 ? -30.778 41.350 -37.205 1.00 25.22 ? 482  ALA A CB  1 
ATOM   1992 N  N   . LEU A 1 259 ? -32.413 39.082 -35.321 1.00 21.23 ? 483  LEU A N   1 
ATOM   1993 C  CA  . LEU A 1 259 ? -33.617 38.504 -34.737 1.00 21.26 ? 483  LEU A CA  1 
ATOM   1994 C  C   . LEU A 1 259 ? -34.307 39.414 -33.731 1.00 25.21 ? 483  LEU A C   1 
ATOM   1995 O  O   . LEU A 1 259 ? -35.533 39.524 -33.759 1.00 21.03 ? 483  LEU A O   1 
ATOM   1996 C  CB  . LEU A 1 259 ? -33.270 37.166 -34.088 1.00 24.01 ? 483  LEU A CB  1 
ATOM   1997 C  CG  . LEU A 1 259 ? -32.767 36.190 -35.151 1.00 27.38 ? 483  LEU A CG  1 
ATOM   1998 C  CD1 . LEU A 1 259 ? -31.733 35.258 -34.576 1.00 25.99 ? 483  LEU A CD1 1 
ATOM   1999 C  CD2 . LEU A 1 259 ? -33.936 35.416 -35.718 1.00 32.76 ? 483  LEU A CD2 1 
ATOM   2000 N  N   . PHE A 1 260 ? -33.557 40.033 -32.819 1.00 19.54 ? 484  PHE A N   1 
ATOM   2001 C  CA  . PHE A 1 260 ? -34.126 41.020 -31.908 1.00 20.12 ? 484  PHE A CA  1 
ATOM   2002 C  C   . PHE A 1 260 ? -32.996 41.867 -31.356 1.00 19.32 ? 484  PHE A C   1 
ATOM   2003 O  O   . PHE A 1 260 ? -31.813 41.549 -31.524 1.00 19.17 ? 484  PHE A O   1 
ATOM   2004 C  CB  . PHE A 1 260 ? -34.919 40.379 -30.761 1.00 22.26 ? 484  PHE A CB  1 
ATOM   2005 C  CG  . PHE A 1 260 ? -34.084 39.527 -29.836 1.00 20.39 ? 484  PHE A CG  1 
ATOM   2006 C  CD1 . PHE A 1 260 ? -33.764 38.228 -30.176 1.00 18.75 ? 484  PHE A CD1 1 
ATOM   2007 C  CD2 . PHE A 1 260 ? -33.647 40.023 -28.619 1.00 19.54 ? 484  PHE A CD2 1 
ATOM   2008 C  CE1 . PHE A 1 260 ? -33.012 37.436 -29.331 1.00 21.60 ? 484  PHE A CE1 1 
ATOM   2009 C  CE2 . PHE A 1 260 ? -32.890 39.242 -27.765 1.00 19.21 ? 484  PHE A CE2 1 
ATOM   2010 C  CZ  . PHE A 1 260 ? -32.567 37.943 -28.123 1.00 20.64 ? 484  PHE A CZ  1 
ATOM   2011 N  N   . GLU A 1 261 ? -33.376 42.945 -30.681 1.00 19.47 ? 485  GLU A N   1 
ATOM   2012 C  CA  . GLU A 1 261 ? -32.424 43.803 -30.008 1.00 19.24 ? 485  GLU A CA  1 
ATOM   2013 C  C   . GLU A 1 261 ? -32.718 43.814 -28.516 1.00 19.03 ? 485  GLU A C   1 
ATOM   2014 O  O   . GLU A 1 261 ? -33.835 43.530 -28.071 1.00 19.20 ? 485  GLU A O   1 
ATOM   2015 C  CB  . GLU A 1 261 ? -32.441 45.235 -30.594 1.00 22.64 ? 485  GLU A CB  1 
ATOM   2016 C  CG  . GLU A 1 261 ? -31.733 45.298 -31.938 1.00 20.96 ? 485  GLU A CG  1 
ATOM   2017 C  CD  . GLU A 1 261 ? -31.859 46.642 -32.652 1.00 26.42 ? 485  GLU A CD  1 
ATOM   2018 O  OE1 . GLU A 1 261 ? -32.438 47.590 -32.074 1.00 26.12 ? 485  GLU A OE1 1 
ATOM   2019 O  OE2 . GLU A 1 261 ? -31.376 46.741 -33.805 1.00 21.45 ? 485  GLU A OE2 1 
ATOM   2020 N  N   . SER A 1 262 ? -31.681 44.128 -27.750 1.00 18.69 ? 486  SER A N   1 
ATOM   2021 C  CA  . SER A 1 262 ? -31.717 44.105 -26.299 1.00 18.48 ? 486  SER A CA  1 
ATOM   2022 C  C   . SER A 1 262 ? -30.915 45.287 -25.772 1.00 18.47 ? 486  SER A C   1 
ATOM   2023 O  O   . SER A 1 262 ? -29.993 45.769 -26.435 1.00 18.47 ? 486  SER A O   1 
ATOM   2024 C  CB  . SER A 1 262 ? -31.138 42.790 -25.761 1.00 18.01 ? 486  SER A CB  1 
ATOM   2025 O  OG  . SER A 1 262 ? -31.040 42.818 -24.350 1.00 24.35 ? 486  SER A OG  1 
ATOM   2026 N  N   . LYS A 1 263 ? -31.253 45.739 -24.568 1.00 18.51 ? 487  LYS A N   1 
ATOM   2027 C  CA  . LYS A 1 263 ? -30.583 46.884 -23.957 1.00 20.95 ? 487  LYS A CA  1 
ATOM   2028 C  C   . LYS A 1 263 ? -29.709 46.395 -22.806 1.00 19.60 ? 487  LYS A C   1 
ATOM   2029 O  O   . LYS A 1 263 ? -30.214 45.918 -21.787 1.00 19.98 ? 487  LYS A O   1 
ATOM   2030 C  CB  . LYS A 1 263 ? -31.601 47.929 -23.504 1.00 19.01 ? 487  LYS A CB  1 
ATOM   2031 C  CG  . LYS A 1 263 ? -32.248 48.664 -24.681 1.00 20.21 ? 487  LYS A CG  1 
ATOM   2032 C  CD  . LYS A 1 263 ? -33.652 49.170 -24.330 1.00 22.76 ? 487  LYS A CD  1 
ATOM   2033 C  CE  . LYS A 1 263 ? -33.614 50.237 -23.264 1.00 24.82 ? 487  LYS A CE  1 
ATOM   2034 N  NZ  . LYS A 1 263 ? -34.955 50.833 -23.040 1.00 20.83 ? 487  LYS A NZ  1 
ATOM   2035 N  N   . LEU A 1 264 ? -28.398 46.511 -22.978 1.00 17.96 ? 488  LEU A N   1 
ATOM   2036 C  CA  . LEU A 1 264 ? -27.439 46.092 -21.957 1.00 17.63 ? 488  LEU A CA  1 
ATOM   2037 C  C   . LEU A 1 264 ? -27.135 47.313 -21.099 1.00 19.75 ? 488  LEU A C   1 
ATOM   2038 O  O   . LEU A 1 264 ? -26.429 48.239 -21.524 1.00 18.01 ? 488  LEU A O   1 
ATOM   2039 C  CB  . LEU A 1 264 ? -26.189 45.502 -22.606 1.00 18.49 ? 488  LEU A CB  1 
ATOM   2040 C  CG  . LEU A 1 264 ? -25.002 45.257 -21.674 1.00 18.48 ? 488  LEU A CG  1 
ATOM   2041 C  CD1 . LEU A 1 264 ? -25.409 44.339 -20.563 1.00 17.07 ? 488  LEU A CD1 1 
ATOM   2042 C  CD2 . LEU A 1 264 ? -23.778 44.686 -22.421 1.00 17.83 ? 488  LEU A CD2 1 
ATOM   2043 N  N   . HIS A 1 265 ? -27.714 47.339 -19.905 1.00 18.81 ? 489  HIS A N   1 
ATOM   2044 C  CA  . HIS A 1 265 ? -27.569 48.497 -19.039 1.00 19.92 ? 489  HIS A CA  1 
ATOM   2045 C  C   . HIS A 1 265 ? -26.171 48.525 -18.444 1.00 20.18 ? 489  HIS A C   1 
ATOM   2046 O  O   . HIS A 1 265 ? -25.554 47.488 -18.213 1.00 21.21 ? 489  HIS A O   1 
ATOM   2047 C  CB  . HIS A 1 265 ? -28.634 48.481 -17.942 1.00 18.78 ? 489  HIS A CB  1 
ATOM   2048 C  CG  . HIS A 1 265 ? -30.029 48.518 -18.478 1.00 20.62 ? 489  HIS A CG  1 
ATOM   2049 N  ND1 . HIS A 1 265 ? -30.749 49.686 -18.599 1.00 26.22 ? 489  HIS A ND1 1 
ATOM   2050 C  CD2 . HIS A 1 265 ? -30.820 47.536 -18.972 1.00 23.66 ? 489  HIS A CD2 1 
ATOM   2051 C  CE1 . HIS A 1 265 ? -31.934 49.418 -19.117 1.00 27.17 ? 489  HIS A CE1 1 
ATOM   2052 N  NE2 . HIS A 1 265 ? -32.001 48.120 -19.354 1.00 25.35 ? 489  HIS A NE2 1 
ATOM   2053 N  N   . LYS A 1 266 ? -25.673 49.741 -18.223 1.00 19.22 ? 490  LYS A N   1 
ATOM   2054 C  CA  . LYS A 1 266 ? -24.299 49.948 -17.782 1.00 22.89 ? 490  LYS A CA  1 
ATOM   2055 C  C   . LYS A 1 266 ? -23.993 49.183 -16.506 1.00 20.58 ? 490  LYS A C   1 
ATOM   2056 O  O   . LYS A 1 266 ? -22.875 48.692 -16.332 1.00 22.81 ? 490  LYS A O   1 
ATOM   2057 C  CB  . LYS A 1 266 ? -24.060 51.460 -17.590 1.00 28.04 ? 490  LYS A CB  1 
ATOM   2058 C  CG  . LYS A 1 266 ? -22.705 51.871 -17.030 1.00 33.18 ? 490  LYS A CG  1 
ATOM   2059 C  CD  . LYS A 1 266 ? -22.688 53.393 -16.805 1.00 35.90 ? 490  LYS A CD  1 
ATOM   2060 C  CE  . LYS A 1 266 ? -21.387 53.859 -16.164 1.00 40.53 ? 490  LYS A CE  1 
ATOM   2061 N  NZ  . LYS A 1 266 ? -21.432 55.330 -15.906 1.00 51.47 ? 490  LYS A NZ  1 
ATOM   2062 N  N   . GLN A 1 267 ? -24.962 49.063 -15.608 1.00 21.57 ? 491  GLN A N   1 
ATOM   2063 C  CA  . GLN A 1 267 ? -24.709 48.441 -14.317 1.00 23.51 ? 491  GLN A CA  1 
ATOM   2064 C  C   . GLN A 1 267 ? -24.813 46.921 -14.367 1.00 26.64 ? 491  GLN A C   1 
ATOM   2065 O  O   . GLN A 1 267 ? -24.648 46.267 -13.329 1.00 23.72 ? 491  GLN A O   1 
ATOM   2066 C  CB  . GLN A 1 267 ? -25.654 49.017 -13.252 1.00 31.67 ? 491  GLN A CB  1 
ATOM   2067 C  CG  . GLN A 1 267 ? -25.304 50.484 -12.856 1.00 34.65 ? 491  GLN A CG  1 
ATOM   2068 C  CD  . GLN A 1 267 ? -23.833 50.671 -12.447 1.00 38.31 ? 491  GLN A CD  1 
ATOM   2069 O  OE1 . GLN A 1 267 ? -23.394 50.176 -11.395 1.00 39.34 ? 491  GLN A OE1 1 
ATOM   2070 N  NE2 . GLN A 1 267 ? -23.061 51.383 -13.285 1.00 26.11 ? 491  GLN A NE2 1 
ATOM   2071 N  N   . GLY A 1 268 ? -25.067 46.348 -15.543 1.00 19.90 ? 492  GLY A N   1 
ATOM   2072 C  CA  . GLY A 1 268 ? -24.771 44.944 -15.771 1.00 20.94 ? 492  GLY A CA  1 
ATOM   2073 C  C   . GLY A 1 268 ? -25.962 44.013 -15.899 1.00 21.22 ? 492  GLY A C   1 
ATOM   2074 O  O   . GLY A 1 268 ? -25.984 42.951 -15.271 1.00 22.68 ? 492  GLY A O   1 
ATOM   2075 N  N   . PHE A 1 269 ? -26.947 44.376 -16.713 1.00 20.95 ? 493  PHE A N   1 
ATOM   2076 C  CA  . PHE A 1 269 ? -28.035 43.452 -17.002 1.00 19.91 ? 493  PHE A CA  1 
ATOM   2077 C  C   . PHE A 1 269 ? -28.709 43.890 -18.294 1.00 19.27 ? 493  PHE A C   1 
ATOM   2078 O  O   . PHE A 1 269 ? -28.539 45.022 -18.752 1.00 22.92 ? 493  PHE A O   1 
ATOM   2079 C  CB  . PHE A 1 269 ? -29.036 43.368 -15.834 1.00 17.67 ? 493  PHE A CB  1 
ATOM   2080 C  CG  . PHE A 1 269 ? -29.835 44.622 -15.609 1.00 22.28 ? 493  PHE A CG  1 
ATOM   2081 C  CD1 . PHE A 1 269 ? -29.313 45.674 -14.874 1.00 24.73 ? 493  PHE A CD1 1 
ATOM   2082 C  CD2 . PHE A 1 269 ? -31.128 44.733 -16.106 1.00 23.37 ? 493  PHE A CD2 1 
ATOM   2083 C  CE1 . PHE A 1 269 ? -30.067 46.834 -14.656 1.00 32.11 ? 493  PHE A CE1 1 
ATOM   2084 C  CE2 . PHE A 1 269 ? -31.882 45.869 -15.887 1.00 25.62 ? 493  PHE A CE2 1 
ATOM   2085 C  CZ  . PHE A 1 269 ? -31.348 46.928 -15.167 1.00 26.88 ? 493  PHE A CZ  1 
ATOM   2086 N  N   . MET A 1 270 ? -29.476 42.979 -18.879 1.00 17.80 ? 494  MET A N   1 
ATOM   2087 C  CA  . MET A 1 270 ? -30.090 43.195 -20.180 1.00 20.94 ? 494  MET A CA  1 
ATOM   2088 C  C   . MET A 1 270 ? -31.602 43.169 -20.052 1.00 18.04 ? 494  MET A C   1 
ATOM   2089 O  O   . MET A 1 270 ? -32.147 42.414 -19.241 1.00 18.94 ? 494  MET A O   1 
ATOM   2090 C  CB  . MET A 1 270 ? -29.624 42.126 -21.176 1.00 18.68 ? 494  MET A CB  1 
ATOM   2091 C  CG  . MET A 1 270 ? -28.115 42.146 -21.362 1.00 25.08 ? 494  MET A CG  1 
ATOM   2092 S  SD  . MET A 1 270 ? -27.444 40.779 -22.334 1.00 29.00 ? 494  MET A SD  1 
ATOM   2093 C  CE  . MET A 1 270 ? -28.475 40.935 -23.786 1.00 22.25 ? 494  MET A CE  1 
ATOM   2094 N  N   . THR A 1 271 ? -32.271 44.010 -20.844 1.00 18.14 ? 495  THR A N   1 
ATOM   2095 C  CA  . THR A 1 271 ? -33.715 43.980 -20.987 1.00 18.52 ? 495  THR A CA  1 
ATOM   2096 C  C   . THR A 1 271 ? -34.083 43.837 -22.456 1.00 19.35 ? 495  THR A C   1 
ATOM   2097 O  O   . THR A 1 271 ? -33.314 44.187 -23.361 1.00 18.59 ? 495  THR A O   1 
ATOM   2098 C  CB  . THR A 1 271 ? -34.391 45.239 -20.403 1.00 19.88 ? 495  THR A CB  1 
ATOM   2099 O  OG1 . THR A 1 271 ? -33.916 46.425 -21.076 1.00 21.44 ? 495  THR A OG1 1 
ATOM   2100 C  CG2 . THR A 1 271 ? -34.104 45.334 -18.911 1.00 18.87 ? 495  THR A CG2 1 
ATOM   2101 N  N   . ILE A 1 272 ? -35.278 43.300 -22.669 1.00 18.96 ? 496  ILE A N   1 
ATOM   2102 C  CA  . ILE A 1 272 ? -35.889 43.156 -23.977 1.00 19.23 ? 496  ILE A CA  1 
ATOM   2103 C  C   . ILE A 1 272 ? -37.339 43.589 -23.849 1.00 19.79 ? 496  ILE A C   1 
ATOM   2104 O  O   . ILE A 1 272 ? -37.891 43.660 -22.751 1.00 21.50 ? 496  ILE A O   1 
ATOM   2105 C  CB  . ILE A 1 272 ? -35.815 41.708 -24.486 1.00 19.34 ? 496  ILE A CB  1 
ATOM   2106 C  CG1 . ILE A 1 272 ? -36.438 40.796 -23.427 1.00 19.00 ? 496  ILE A CG1 1 
ATOM   2107 C  CG2 . ILE A 1 272 ? -34.371 41.348 -24.803 1.00 18.53 ? 496  ILE A CG2 1 
ATOM   2108 C  CD1 . ILE A 1 272 ? -36.785 39.405 -23.888 1.00 19.63 ? 496  ILE A CD1 1 
ATOM   2109 N  N   . ALA A 1 273 ? -37.951 43.896 -24.987 1.00 20.18 ? 497  ALA A N   1 
ATOM   2110 C  CA  . ALA A 1 273 ? -39.386 44.161 -25.025 1.00 22.47 ? 497  ALA A CA  1 
ATOM   2111 C  C   . ALA A 1 273 ? -40.097 42.812 -25.093 1.00 23.87 ? 497  ALA A C   1 
ATOM   2112 O  O   . ALA A 1 273 ? -40.053 42.134 -26.122 1.00 21.88 ? 497  ALA A O   1 
ATOM   2113 C  CB  . ALA A 1 273 ? -39.744 45.039 -26.217 1.00 21.73 ? 497  ALA A CB  1 
ATOM   2114 N  N   . SER A 1 274 ? -40.723 42.404 -23.996 1.00 23.21 ? 498  SER A N   1 
ATOM   2115 C  CA  . SER A 1 274 ? -41.416 41.123 -23.980 1.00 25.65 ? 498  SER A CA  1 
ATOM   2116 C  C   . SER A 1 274 ? -42.412 41.133 -22.837 1.00 26.67 ? 498  SER A C   1 
ATOM   2117 O  O   . SER A 1 274 ? -42.367 41.988 -21.952 1.00 28.35 ? 498  SER A O   1 
ATOM   2118 C  CB  . SER A 1 274 ? -40.437 39.949 -23.849 1.00 26.98 ? 498  SER A CB  1 
ATOM   2119 O  OG  . SER A 1 274 ? -41.015 38.746 -24.343 1.00 29.44 ? 498  SER A OG  1 
ATOM   2120 N  N   . SER A 1 275 ? -43.323 40.169 -22.873 1.00 26.79 ? 499  SER A N   1 
ATOM   2121 C  CA  . SER A 1 275 ? -44.354 40.050 -21.859 1.00 29.44 ? 499  SER A CA  1 
ATOM   2122 C  C   . SER A 1 275 ? -44.523 38.586 -21.487 1.00 31.19 ? 499  SER A C   1 
ATOM   2123 O  O   . SER A 1 275 ? -44.635 37.727 -22.366 1.00 33.71 ? 499  SER A O   1 
ATOM   2124 C  CB  . SER A 1 275 ? -45.682 40.624 -22.364 1.00 31.66 ? 499  SER A CB  1 
ATOM   2125 O  OG  . SER A 1 275 ? -46.660 40.580 -21.342 1.00 42.16 ? 499  SER A OG  1 
ATOM   2126 N  N   . GLY A 1 276 ? -44.552 38.304 -20.194 1.00 30.33 ? 500  GLY A N   1 
ATOM   2127 C  CA  . GLY A 1 276 ? -44.786 36.958 -19.721 1.00 29.17 ? 500  GLY A CA  1 
ATOM   2128 C  C   . GLY A 1 276 ? -43.504 36.241 -19.342 1.00 31.01 ? 500  GLY A C   1 
ATOM   2129 O  O   . GLY A 1 276 ? -42.385 36.715 -19.560 1.00 29.31 ? 500  GLY A O   1 
ATOM   2130 N  N   . ASP A 1 277 ? -43.689 35.069 -18.748 1.00 30.41 ? 501  ASP A N   1 
ATOM   2131 C  CA  . ASP A 1 277 ? -42.593 34.206 -18.332 1.00 26.74 ? 501  ASP A CA  1 
ATOM   2132 C  C   . ASP A 1 277 ? -42.464 33.106 -19.377 1.00 30.08 ? 501  ASP A C   1 
ATOM   2133 O  O   . ASP A 1 277 ? -43.332 32.236 -19.478 1.00 27.54 ? 501  ASP A O   1 
ATOM   2134 C  CB  . ASP A 1 277 ? -42.850 33.623 -16.943 1.00 30.64 ? 501  ASP A CB  1 
ATOM   2135 C  CG  . ASP A 1 277 ? -43.168 34.693 -15.899 1.00 35.73 ? 501  ASP A CG  1 
ATOM   2136 O  OD1 . ASP A 1 277 ? -42.975 35.892 -16.170 1.00 34.68 ? 501  ASP A OD1 1 
ATOM   2137 O  OD2 . ASP A 1 277 ? -43.631 34.333 -14.800 1.00 43.62 ? 501  ASP A OD2 1 
ATOM   2138 N  N   . HIS A 1 278 ? -41.392 33.148 -20.165 1.00 25.16 ? 502  HIS A N   1 
ATOM   2139 C  CA  . HIS A 1 278 ? -41.229 32.159 -21.218 1.00 26.22 ? 502  HIS A CA  1 
ATOM   2140 C  C   . HIS A 1 278 ? -39.786 32.171 -21.670 1.00 25.45 ? 502  HIS A C   1 
ATOM   2141 O  O   . HIS A 1 278 ? -39.111 33.195 -21.536 1.00 23.52 ? 502  HIS A O   1 
ATOM   2142 C  CB  . HIS A 1 278 ? -42.166 32.443 -22.402 1.00 26.29 ? 502  HIS A CB  1 
ATOM   2143 C  CG  . HIS A 1 278 ? -42.101 33.847 -22.906 1.00 26.12 ? 502  HIS A CG  1 
ATOM   2144 N  ND1 . HIS A 1 278 ? -41.169 34.262 -23.835 1.00 31.41 ? 502  HIS A ND1 1 
ATOM   2145 C  CD2 . HIS A 1 278 ? -42.851 34.936 -22.610 1.00 28.42 ? 502  HIS A CD2 1 
ATOM   2146 C  CE1 . HIS A 1 278 ? -41.348 35.548 -24.089 1.00 26.96 ? 502  HIS A CE1 1 
ATOM   2147 N  NE2 . HIS A 1 278 ? -42.362 35.979 -23.361 1.00 31.65 ? 502  HIS A NE2 1 
ATOM   2148 N  N   . PRO A 1 279 ? -39.281 31.061 -22.196 1.00 25.58 ? 503  PRO A N   1 
ATOM   2149 C  CA  . PRO A 1 279 ? -37.952 31.083 -22.812 1.00 24.43 ? 503  PRO A CA  1 
ATOM   2150 C  C   . PRO A 1 279 ? -37.957 31.894 -24.100 1.00 25.37 ? 503  PRO A C   1 
ATOM   2151 O  O   . PRO A 1 279 ? -38.989 32.100 -24.746 1.00 23.94 ? 503  PRO A O   1 
ATOM   2152 C  CB  . PRO A 1 279 ? -37.663 29.602 -23.084 1.00 25.00 ? 503  PRO A CB  1 
ATOM   2153 C  CG  . PRO A 1 279 ? -39.004 28.966 -23.186 1.00 26.43 ? 503  PRO A CG  1 
ATOM   2154 C  CD  . PRO A 1 279 ? -39.928 29.738 -22.297 1.00 25.36 ? 503  PRO A CD  1 
ATOM   2155 N  N   . ILE A 1 280 ? -36.772 32.370 -24.462 1.00 24.57 ? 504  ILE A N   1 
ATOM   2156 C  CA  . ILE A 1 280 ? -36.550 33.072 -25.720 1.00 23.28 ? 504  ILE A CA  1 
ATOM   2157 C  C   . ILE A 1 280 ? -35.775 32.108 -26.607 1.00 24.15 ? 504  ILE A C   1 
ATOM   2158 O  O   . ILE A 1 280 ? -34.553 31.977 -26.484 1.00 25.51 ? 504  ILE A O   1 
ATOM   2159 C  CB  . ILE A 1 280 ? -35.796 34.393 -25.523 1.00 22.65 ? 504  ILE A CB  1 
ATOM   2160 C  CG1 . ILE A 1 280 ? -36.567 35.338 -24.580 1.00 22.30 ? 504  ILE A CG1 1 
ATOM   2161 C  CG2 . ILE A 1 280 ? -35.518 35.058 -26.872 1.00 24.07 ? 504  ILE A CG2 1 
ATOM   2162 C  CD1 . ILE A 1 280 ? -37.944 35.738 -25.050 1.00 25.48 ? 504  ILE A CD1 1 
ATOM   2163 N  N   . ILE A 1 281 ? -36.471 31.411 -27.487 1.00 24.09 ? 505  ILE A N   1 
ATOM   2164 C  CA  . ILE A 1 281 ? -35.845 30.374 -28.298 1.00 30.17 ? 505  ILE A CA  1 
ATOM   2165 C  C   . ILE A 1 281 ? -35.427 30.985 -29.622 1.00 26.71 ? 505  ILE A C   1 
ATOM   2166 O  O   . ILE A 1 281 ? -36.232 31.641 -30.292 1.00 26.81 ? 505  ILE A O   1 
ATOM   2167 C  CB  . ILE A 1 281 ? -36.795 29.182 -28.507 1.00 32.07 ? 505  ILE A CB  1 
ATOM   2168 C  CG1 . ILE A 1 281 ? -37.294 28.667 -27.158 1.00 33.07 ? 505  ILE A CG1 1 
ATOM   2169 C  CG2 . ILE A 1 281 ? -36.079 28.058 -29.233 1.00 33.10 ? 505  ILE A CG2 1 
ATOM   2170 C  CD1 . ILE A 1 281 ? -38.805 28.746 -27.013 1.00 36.84 ? 505  ILE A CD1 1 
ATOM   2171 N  N   . MET A 1 282 ? -34.169 30.776 -29.991 1.00 25.52 ? 506  MET A N   1 
ATOM   2172 C  CA  . MET A 1 282 ? -33.558 31.405 -31.150 1.00 27.33 ? 506  MET A CA  1 
ATOM   2173 C  C   . MET A 1 282 ? -32.739 30.378 -31.915 1.00 24.99 ? 506  MET A C   1 
ATOM   2174 O  O   . MET A 1 282 ? -32.412 29.313 -31.376 1.00 23.23 ? 506  MET A O   1 
ATOM   2175 C  CB  . MET A 1 282 ? -32.663 32.572 -30.714 1.00 24.72 ? 506  MET A CB  1 
ATOM   2176 C  CG  . MET A 1 282 ? -33.444 33.721 -30.103 1.00 22.96 ? 506  MET A CG  1 
ATOM   2177 S  SD  . MET A 1 282 ? -34.324 34.580 -31.404 1.00 27.49 ? 506  MET A SD  1 
ATOM   2178 C  CE  . MET A 1 282 ? -35.801 35.177 -30.578 1.00 22.63 ? 506  MET A CE  1 
ATOM   2179 N  N   . PRO A 1 283 ? -32.401 30.663 -33.178 1.00 27.43 ? 507  PRO A N   1 
ATOM   2180 C  CA  . PRO A 1 283 ? -31.485 29.787 -33.926 1.00 27.84 ? 507  PRO A CA  1 
ATOM   2181 C  C   . PRO A 1 283 ? -30.236 29.470 -33.119 1.00 25.78 ? 507  PRO A C   1 
ATOM   2182 O  O   . PRO A 1 283 ? -29.689 30.329 -32.426 1.00 22.51 ? 507  PRO A O   1 
ATOM   2183 C  CB  . PRO A 1 283 ? -31.156 30.604 -35.177 1.00 23.81 ? 507  PRO A CB  1 
ATOM   2184 C  CG  . PRO A 1 283 ? -32.395 31.433 -35.401 1.00 29.86 ? 507  PRO A CG  1 
ATOM   2185 C  CD  . PRO A 1 283 ? -32.988 31.711 -34.035 1.00 23.62 ? 507  PRO A CD  1 
ATOM   2186 N  N   . THR A 1 284 ? -29.780 28.219 -33.239 1.00 25.24 ? 508  THR A N   1 
ATOM   2187 C  CA  A THR A 1 284 ? -28.732 27.753 -32.339 0.47 24.37 ? 508  THR A CA  1 
ATOM   2188 C  CA  B THR A 1 284 ? -28.703 27.697 -32.396 0.53 24.44 ? 508  THR A CA  1 
ATOM   2189 C  C   . THR A 1 284 ? -27.424 28.516 -32.526 1.00 21.49 ? 508  THR A C   1 
ATOM   2190 O  O   . THR A 1 284 ? -26.670 28.673 -31.563 1.00 22.55 ? 508  THR A O   1 
ATOM   2191 C  CB  A THR A 1 284 ? -28.507 26.251 -32.518 0.47 25.68 ? 508  THR A CB  1 
ATOM   2192 C  CB  B THR A 1 284 ? -28.422 26.241 -32.779 0.53 25.65 ? 508  THR A CB  1 
ATOM   2193 O  OG1 A THR A 1 284 ? -28.057 25.990 -33.849 0.47 25.27 ? 508  THR A OG1 1 
ATOM   2194 O  OG1 B THR A 1 284 ? -29.660 25.542 -32.940 0.53 26.66 ? 508  THR A OG1 1 
ATOM   2195 C  CG2 A THR A 1 284 ? -29.798 25.496 -32.270 0.47 27.50 ? 508  THR A CG2 1 
ATOM   2196 C  CG2 B THR A 1 284 ? -27.570 25.553 -31.721 0.53 27.61 ? 508  THR A CG2 1 
ATOM   2197 N  N   . ASN A 1 285 ? -27.136 29.007 -33.723 1.00 20.18 ? 509  ASN A N   1 
ATOM   2198 C  CA  . ASN A 1 285 ? -25.868 29.690 -33.953 1.00 27.34 ? 509  ASN A CA  1 
ATOM   2199 C  C   . ASN A 1 285 ? -25.932 31.207 -33.720 1.00 26.07 ? 509  ASN A C   1 
ATOM   2200 O  O   . ASN A 1 285 ? -24.938 31.901 -33.970 1.00 23.30 ? 509  ASN A O   1 
ATOM   2201 C  CB  . ASN A 1 285 ? -25.364 29.390 -35.369 1.00 27.89 ? 509  ASN A CB  1 
ATOM   2202 C  CG  . ASN A 1 285 ? -24.848 27.963 -35.512 1.00 28.88 ? 509  ASN A CG  1 
ATOM   2203 O  OD1 . ASN A 1 285 ? -24.638 27.271 -34.518 1.00 27.47 ? 509  ASN A OD1 1 
ATOM   2204 N  ND2 . ASN A 1 285 ? -24.650 27.520 -36.749 1.00 29.96 ? 509  ASN A ND2 1 
ATOM   2205 N  N   . GLY A 1 286 ? -27.051 31.728 -33.226 1.00 22.76 ? 510  GLY A N   1 
ATOM   2206 C  CA  . GLY A 1 286 ? -27.170 33.163 -33.040 1.00 21.47 ? 510  GLY A CA  1 
ATOM   2207 C  C   . GLY A 1 286 ? -26.323 33.690 -31.893 1.00 18.57 ? 510  GLY A C   1 
ATOM   2208 O  O   . GLY A 1 286 ? -26.008 32.989 -30.931 1.00 18.50 ? 510  GLY A O   1 
ATOM   2209 N  N   . TYR A 1 287 ? -25.952 34.966 -31.993 1.00 20.20 ? 511  TYR A N   1 
ATOM   2210 C  CA  . TYR A 1 287 ? -25.169 35.595 -30.940 1.00 19.14 ? 511  TYR A CA  1 
ATOM   2211 C  C   . TYR A 1 287 ? -25.455 37.092 -30.920 1.00 19.83 ? 511  TYR A C   1 
ATOM   2212 O  O   . TYR A 1 287 ? -25.948 37.666 -31.897 1.00 18.34 ? 511  TYR A O   1 
ATOM   2213 C  CB  . TYR A 1 287 ? -23.670 35.339 -31.126 1.00 18.84 ? 511  TYR A CB  1 
ATOM   2214 C  CG  . TYR A 1 287 ? -23.105 35.958 -32.385 1.00 20.52 ? 511  TYR A CG  1 
ATOM   2215 C  CD1 . TYR A 1 287 ? -22.610 37.255 -32.380 1.00 20.32 ? 511  TYR A CD1 1 
ATOM   2216 C  CD2 . TYR A 1 287 ? -23.067 35.249 -33.579 1.00 23.67 ? 511  TYR A CD2 1 
ATOM   2217 C  CE1 . TYR A 1 287 ? -22.105 37.839 -33.528 1.00 24.23 ? 511  TYR A CE1 1 
ATOM   2218 C  CE2 . TYR A 1 287 ? -22.550 35.826 -34.739 1.00 30.25 ? 511  TYR A CE2 1 
ATOM   2219 C  CZ  . TYR A 1 287 ? -22.076 37.121 -34.705 1.00 31.23 ? 511  TYR A CZ  1 
ATOM   2220 O  OH  . TYR A 1 287 ? -21.563 37.710 -35.841 1.00 40.52 ? 511  TYR A OH  1 
ATOM   2221 N  N   . PHE A 1 288 ? -25.125 37.712 -29.786 1.00 19.34 ? 512  PHE A N   1 
ATOM   2222 C  CA  . PHE A 1 288 ? -25.267 39.148 -29.590 1.00 19.45 ? 512  PHE A CA  1 
ATOM   2223 C  C   . PHE A 1 288 ? -24.073 39.922 -30.129 1.00 19.79 ? 512  PHE A C   1 
ATOM   2224 O  O   . PHE A 1 288 ? -22.922 39.482 -30.057 1.00 20.17 ? 512  PHE A O   1 
ATOM   2225 C  CB  . PHE A 1 288 ? -25.416 39.488 -28.109 1.00 18.81 ? 512  PHE A CB  1 
ATOM   2226 C  CG  . PHE A 1 288 ? -26.772 39.184 -27.555 1.00 20.54 ? 512  PHE A CG  1 
ATOM   2227 C  CD1 . PHE A 1 288 ? -27.852 39.979 -27.864 1.00 19.16 ? 512  PHE A CD1 1 
ATOM   2228 C  CD2 . PHE A 1 288 ? -26.958 38.101 -26.710 1.00 22.60 ? 512  PHE A CD2 1 
ATOM   2229 C  CE1 . PHE A 1 288 ? -29.110 39.700 -27.339 1.00 22.55 ? 512  PHE A CE1 1 
ATOM   2230 C  CE2 . PHE A 1 288 ? -28.210 37.821 -26.187 1.00 21.87 ? 512  PHE A CE2 1 
ATOM   2231 C  CZ  . PHE A 1 288 ? -29.279 38.619 -26.506 1.00 19.02 ? 512  PHE A CZ  1 
ATOM   2232 N  N   . ARG A 1 289 ? -24.355 41.132 -30.592 1.00 21.42 ? 513  ARG A N   1 
ATOM   2233 C  CA  . ARG A 1 289 ? -23.348 42.006 -31.165 1.00 22.66 ? 513  ARG A CA  1 
ATOM   2234 C  C   . ARG A 1 289 ? -23.676 43.435 -30.746 1.00 20.82 ? 513  ARG A C   1 
ATOM   2235 O  O   . ARG A 1 289 ? -24.845 43.833 -30.754 1.00 20.15 ? 513  ARG A O   1 
ATOM   2236 C  CB  . ARG A 1 289 ? -23.334 41.838 -32.694 1.00 27.83 ? 513  ARG A CB  1 
ATOM   2237 C  CG  . ARG A 1 289 ? -22.294 42.621 -33.478 1.00 35.82 ? 513  ARG A CG  1 
ATOM   2238 C  CD  . ARG A 1 289 ? -22.397 42.258 -34.980 1.00 37.45 ? 513  ARG A CD  1 
ATOM   2239 N  NE  . ARG A 1 289 ? -23.514 42.924 -35.640 1.00 44.94 ? 513  ARG A NE  1 
ATOM   2240 C  CZ  . ARG A 1 289 ? -24.021 42.576 -36.819 1.00 49.05 ? 513  ARG A CZ  1 
ATOM   2241 N  NH1 . ARG A 1 289 ? -23.570 41.521 -37.484 1.00 46.47 ? 513  ARG A NH1 1 
ATOM   2242 N  NH2 . ARG A 1 289 ? -25.009 43.304 -37.344 1.00 41.89 ? 513  ARG A NH2 1 
ATOM   2243 N  N   . PHE A 1 290 ? -22.651 44.186 -30.336 1.00 17.96 ? 514  PHE A N   1 
ATOM   2244 C  CA  . PHE A 1 290 ? -22.839 45.586 -29.970 1.00 19.71 ? 514  PHE A CA  1 
ATOM   2245 C  C   . PHE A 1 290 ? -23.169 46.418 -31.200 1.00 18.53 ? 514  PHE A C   1 
ATOM   2246 O  O   . PHE A 1 290 ? -22.506 46.297 -32.231 1.00 19.55 ? 514  PHE A O   1 
ATOM   2247 C  CB  . PHE A 1 290 ? -21.579 46.138 -29.304 1.00 22.27 ? 514  PHE A CB  1 
ATOM   2248 C  CG  . PHE A 1 290 ? -21.609 47.624 -29.098 1.00 24.00 ? 514  PHE A CG  1 
ATOM   2249 C  CD1 . PHE A 1 290 ? -22.392 48.181 -28.098 1.00 19.98 ? 514  PHE A CD1 1 
ATOM   2250 C  CD2 . PHE A 1 290 ? -20.865 48.466 -29.909 1.00 22.09 ? 514  PHE A CD2 1 
ATOM   2251 C  CE1 . PHE A 1 290 ? -22.418 49.548 -27.904 1.00 22.00 ? 514  PHE A CE1 1 
ATOM   2252 C  CE2 . PHE A 1 290 ? -20.895 49.832 -29.724 1.00 25.07 ? 514  PHE A CE2 1 
ATOM   2253 C  CZ  . PHE A 1 290 ? -21.677 50.378 -28.726 1.00 19.11 ? 514  PHE A CZ  1 
ATOM   2254 N  N   . GLU A 1 291 ? -24.169 47.284 -31.083 1.00 18.84 ? 515  GLU A N   1 
ATOM   2255 C  CA  . GLU A 1 291 ? -24.558 48.148 -32.188 1.00 19.39 ? 515  GLU A CA  1 
ATOM   2256 C  C   . GLU A 1 291 ? -24.394 49.633 -31.904 1.00 20.93 ? 515  GLU A C   1 
ATOM   2257 O  O   . GLU A 1 291 ? -23.937 50.359 -32.787 1.00 24.43 ? 515  GLU A O   1 
ATOM   2258 C  CB  . GLU A 1 291 ? -26.017 47.880 -32.605 1.00 19.85 ? 515  GLU A CB  1 
ATOM   2259 C  CG  . GLU A 1 291 ? -26.281 46.456 -33.133 1.00 23.19 ? 515  GLU A CG  1 
ATOM   2260 C  CD  . GLU A 1 291 ? -25.473 46.106 -34.379 1.00 24.77 ? 515  GLU A CD  1 
ATOM   2261 O  OE1 . GLU A 1 291 ? -25.113 47.014 -35.153 1.00 25.36 ? 515  GLU A OE1 1 
ATOM   2262 O  OE2 . GLU A 1 291 ? -25.206 44.904 -34.594 1.00 29.47 ? 515  GLU A OE2 1 
ATOM   2263 N  N   . ALA A 1 292 ? -24.751 50.118 -30.713 1.00 19.77 ? 516  ALA A N   1 
ATOM   2264 C  CA  . ALA A 1 292 ? -24.769 51.564 -30.497 1.00 20.79 ? 516  ALA A CA  1 
ATOM   2265 C  C   . ALA A 1 292 ? -24.936 51.885 -29.019 1.00 20.08 ? 516  ALA A C   1 
ATOM   2266 O  O   . ALA A 1 292 ? -25.395 51.058 -28.225 1.00 19.51 ? 516  ALA A O   1 
ATOM   2267 C  CB  . ALA A 1 292 ? -25.889 52.237 -31.303 1.00 20.62 ? 516  ALA A CB  1 
ATOM   2268 N  N   . TRP A 1 293 ? -24.560 53.112 -28.666 1.00 20.22 ? 517  TRP A N   1 
ATOM   2269 C  CA  . TRP A 1 293 ? -24.750 53.643 -27.321 1.00 21.23 ? 517  TRP A CA  1 
ATOM   2270 C  C   . TRP A 1 293 ? -26.076 54.390 -27.277 1.00 21.05 ? 517  TRP A C   1 
ATOM   2271 O  O   . TRP A 1 293 ? -26.216 55.430 -27.925 1.00 21.82 ? 517  TRP A O   1 
ATOM   2272 C  CB  . TRP A 1 293 ? -23.601 54.578 -26.958 1.00 23.37 ? 517  TRP A CB  1 
ATOM   2273 C  CG  . TRP A 1 293 ? -22.308 53.868 -26.754 1.00 23.57 ? 517  TRP A CG  1 
ATOM   2274 C  CD1 . TRP A 1 293 ? -21.198 53.918 -27.557 1.00 22.94 ? 517  TRP A CD1 1 
ATOM   2275 C  CD2 . TRP A 1 293 ? -21.975 53.002 -25.662 1.00 20.17 ? 517  TRP A CD2 1 
ATOM   2276 N  NE1 . TRP A 1 293 ? -20.205 53.131 -27.030 1.00 19.74 ? 517  TRP A NE1 1 
ATOM   2277 C  CE2 . TRP A 1 293 ? -20.650 52.572 -25.860 1.00 19.37 ? 517  TRP A CE2 1 
ATOM   2278 C  CE3 . TRP A 1 293 ? -22.667 52.559 -24.529 1.00 19.63 ? 517  TRP A CE3 1 
ATOM   2279 C  CZ2 . TRP A 1 293 ? -20.009 51.701 -24.979 1.00 23.62 ? 517  TRP A CZ2 1 
ATOM   2280 C  CZ3 . TRP A 1 293 ? -22.030 51.710 -23.656 1.00 21.13 ? 517  TRP A CZ3 1 
ATOM   2281 C  CH2 . TRP A 1 293 ? -20.710 51.281 -23.890 1.00 20.19 ? 517  TRP A CH2 1 
ATOM   2282 N  N   . VAL A 1 294 ? -27.046 53.881 -26.506 1.00 20.38 ? 518  VAL A N   1 
ATOM   2283 C  CA  . VAL A 1 294 ? -28.351 54.551 -26.424 1.00 20.79 ? 518  VAL A CA  1 
ATOM   2284 C  C   . VAL A 1 294 ? -28.676 54.891 -24.973 1.00 20.76 ? 518  VAL A C   1 
ATOM   2285 O  O   . VAL A 1 294 ? -27.842 54.735 -24.084 1.00 21.99 ? 518  VAL A O   1 
ATOM   2286 C  CB  . VAL A 1 294 ? -29.464 53.692 -27.060 1.00 21.96 ? 518  VAL A CB  1 
ATOM   2287 C  CG1 . VAL A 1 294 ? -29.138 53.361 -28.527 1.00 21.38 ? 518  VAL A CG1 1 
ATOM   2288 C  CG2 . VAL A 1 294 ? -29.696 52.421 -26.265 1.00 20.25 ? 518  VAL A CG2 1 
ATOM   2289 N  N   . ASN A 1 295 ? -29.871 55.375 -24.706 1.00 23.52 ? 519  ASN A N   1 
ATOM   2290 C  CA  . ASN A 1 295 ? -30.218 55.636 -23.320 1.00 25.96 ? 519  ASN A CA  1 
ATOM   2291 C  C   . ASN A 1 295 ? -31.320 54.685 -22.883 1.00 27.79 ? 519  ASN A C   1 
ATOM   2292 O  O   . ASN A 1 295 ? -31.820 53.868 -23.663 1.00 25.25 ? 519  ASN A O   1 
ATOM   2293 C  CB  . ASN A 1 295 ? -30.603 57.101 -23.104 1.00 25.34 ? 519  ASN A CB  1 
ATOM   2294 C  CG  . ASN A 1 295 ? -31.826 57.512 -23.880 1.00 28.11 ? 519  ASN A CG  1 
ATOM   2295 O  OD1 . ASN A 1 295 ? -32.766 56.749 -24.038 1.00 29.08 ? 519  ASN A OD1 1 
ATOM   2296 N  ND2 . ASN A 1 295 ? -31.820 58.739 -24.369 1.00 36.14 ? 519  ASN A ND2 1 
ATOM   2297 N  N   . GLN A 1 296 ? -31.700 54.813 -21.613 1.00 26.93 ? 520  GLN A N   1 
ATOM   2298 C  CA  . GLN A 1 296 ? -32.660 53.911 -20.998 1.00 31.15 ? 520  GLN A CA  1 
ATOM   2299 C  C   . GLN A 1 296 ? -34.053 53.999 -21.623 1.00 30.96 ? 520  GLN A C   1 
ATOM   2300 O  O   . GLN A 1 296 ? -34.872 53.107 -21.374 1.00 29.14 ? 520  GLN A O   1 
ATOM   2301 C  CB  . GLN A 1 296 ? -32.698 54.185 -19.486 1.00 36.64 ? 520  GLN A CB  1 
ATOM   2302 C  CG  . GLN A 1 296 ? -32.976 55.639 -19.083 1.00 40.21 ? 520  GLN A CG  1 
ATOM   2303 C  CD  . GLN A 1 296 ? -31.737 56.582 -19.079 1.00 50.37 ? 520  GLN A CD  1 
ATOM   2304 O  OE1 . GLN A 1 296 ? -30.605 56.191 -19.398 1.00 39.10 ? 520  GLN A OE1 1 
ATOM   2305 N  NE2 . GLN A 1 296 ? -31.976 57.842 -18.709 1.00 56.84 ? 520  GLN A NE2 1 
ATOM   2306 N  N   . PHE A 1 297 ? -34.327 55.011 -22.459 1.00 28.30 ? 521  PHE A N   1 
ATOM   2307 C  CA  . PHE A 1 297 ? -35.631 55.203 -23.097 1.00 30.38 ? 521  PHE A CA  1 
ATOM   2308 C  C   . PHE A 1 297 ? -35.693 54.723 -24.544 1.00 27.05 ? 521  PHE A C   1 
ATOM   2309 O  O   . PHE A 1 297 ? -36.719 54.925 -25.202 1.00 28.71 ? 521  PHE A O   1 
ATOM   2310 C  CB  . PHE A 1 297 ? -36.029 56.681 -23.043 1.00 36.65 ? 521  PHE A CB  1 
ATOM   2311 C  CG  . PHE A 1 297 ? -35.933 57.264 -21.674 1.00 40.10 ? 521  PHE A CG  1 
ATOM   2312 C  CD1 . PHE A 1 297 ? -36.829 56.890 -20.690 1.00 41.75 ? 521  PHE A CD1 1 
ATOM   2313 C  CD2 . PHE A 1 297 ? -34.931 58.163 -21.359 1.00 44.52 ? 521  PHE A CD2 1 
ATOM   2314 C  CE1 . PHE A 1 297 ? -36.735 57.412 -19.417 1.00 52.48 ? 521  PHE A CE1 1 
ATOM   2315 C  CE2 . PHE A 1 297 ? -34.831 58.693 -20.086 1.00 47.84 ? 521  PHE A CE2 1 
ATOM   2316 C  CZ  . PHE A 1 297 ? -35.734 58.317 -19.115 1.00 50.18 ? 521  PHE A CZ  1 
ATOM   2317 N  N   . TYR A 1 298 ? -34.629 54.097 -25.050 1.00 24.54 ? 522  TYR A N   1 
ATOM   2318 C  CA  . TYR A 1 298 ? -34.646 53.504 -26.382 1.00 25.81 ? 522  TYR A CA  1 
ATOM   2319 C  C   . TYR A 1 298 ? -35.697 52.407 -26.455 1.00 23.05 ? 522  TYR A C   1 
ATOM   2320 O  O   . TYR A 1 298 ? -35.697 51.482 -25.638 1.00 23.08 ? 522  TYR A O   1 
ATOM   2321 C  CB  . TYR A 1 298 ? -33.273 52.919 -26.705 1.00 21.25 ? 522  TYR A CB  1 
ATOM   2322 C  CG  . TYR A 1 298 ? -33.038 52.690 -28.168 1.00 21.37 ? 522  TYR A CG  1 
ATOM   2323 C  CD1 . TYR A 1 298 ? -32.726 53.755 -29.008 1.00 21.82 ? 522  TYR A CD1 1 
ATOM   2324 C  CD2 . TYR A 1 298 ? -33.118 51.412 -28.716 1.00 21.09 ? 522  TYR A CD2 1 
ATOM   2325 C  CE1 . TYR A 1 298 ? -32.496 53.562 -30.360 1.00 23.75 ? 522  TYR A CE1 1 
ATOM   2326 C  CE2 . TYR A 1 298 ? -32.887 51.204 -30.072 1.00 21.27 ? 522  TYR A CE2 1 
ATOM   2327 C  CZ  . TYR A 1 298 ? -32.585 52.288 -30.889 1.00 24.19 ? 522  TYR A CZ  1 
ATOM   2328 O  OH  . TYR A 1 298 ? -32.353 52.110 -32.235 1.00 25.22 ? 522  TYR A OH  1 
ATOM   2329 N  N   . SER A 1 299 ? -36.561 52.480 -27.460 1.00 22.16 ? 523  SER A N   1 
ATOM   2330 C  CA  . SER A 1 299 ? -37.748 51.635 -27.527 1.00 22.75 ? 523  SER A CA  1 
ATOM   2331 C  C   . SER A 1 299 ? -37.520 50.462 -28.479 1.00 22.17 ? 523  SER A C   1 
ATOM   2332 O  O   . SER A 1 299 ? -37.301 50.671 -29.676 1.00 22.29 ? 523  SER A O   1 
ATOM   2333 C  CB  . SER A 1 299 ? -38.957 52.463 -27.964 1.00 23.04 ? 523  SER A CB  1 
ATOM   2334 O  OG  . SER A 1 299 ? -40.111 51.649 -27.979 1.00 30.49 ? 523  SER A OG  1 
ATOM   2335 N  N   . LEU A 1 300 ? -37.615 49.234 -27.954 1.00 24.41 ? 524  LEU A N   1 
ATOM   2336 C  CA  . LEU A 1 300 ? -37.318 48.015 -28.703 1.00 22.15 ? 524  LEU A CA  1 
ATOM   2337 C  C   . LEU A 1 300 ? -38.580 47.376 -29.284 1.00 28.19 ? 524  LEU A C   1 
ATOM   2338 O  O   . LEU A 1 300 ? -39.665 47.442 -28.699 1.00 24.91 ? 524  LEU A O   1 
ATOM   2339 C  CB  . LEU A 1 300 ? -36.605 46.988 -27.815 1.00 20.75 ? 524  LEU A CB  1 
ATOM   2340 C  CG  . LEU A 1 300 ? -35.344 47.406 -27.034 1.00 26.39 ? 524  LEU A CG  1 
ATOM   2341 C  CD1 . LEU A 1 300 ? -34.859 46.267 -26.113 1.00 19.77 ? 524  LEU A CD1 1 
ATOM   2342 C  CD2 . LEU A 1 300 ? -34.229 47.873 -27.962 1.00 20.55 ? 524  LEU A CD2 1 
ATOM   2343 N  N   . ALA A 1 301 ? -38.424 46.731 -30.441 1.00 23.65 ? 525  ALA A N   1 
ATOM   2344 C  CA  . ALA A 1 301 ? -39.515 45.938 -30.984 1.00 28.44 ? 525  ALA A CA  1 
ATOM   2345 C  C   . ALA A 1 301 ? -39.662 44.652 -30.176 1.00 24.80 ? 525  ALA A C   1 
ATOM   2346 O  O   . ALA A 1 301 ? -38.662 44.048 -29.784 1.00 23.97 ? 525  ALA A O   1 
ATOM   2347 C  CB  . ALA A 1 301 ? -39.281 45.601 -32.456 1.00 24.81 ? 525  ALA A CB  1 
ATOM   2348 N  N   . PRO A 1 302 ? -40.889 44.215 -29.911 1.00 22.43 ? 526  PRO A N   1 
ATOM   2349 C  CA  . PRO A 1 302 ? -41.091 43.038 -29.058 1.00 26.52 ? 526  PRO A CA  1 
ATOM   2350 C  C   . PRO A 1 302 ? -40.479 41.771 -29.640 1.00 28.60 ? 526  PRO A C   1 
ATOM   2351 O  O   . PRO A 1 302 ? -40.338 41.617 -30.856 1.00 24.29 ? 526  PRO A O   1 
ATOM   2352 C  CB  . PRO A 1 302 ? -42.620 42.923 -28.976 1.00 25.90 ? 526  PRO A CB  1 
ATOM   2353 C  CG  . PRO A 1 302 ? -43.097 44.321 -29.163 1.00 28.68 ? 526  PRO A CG  1 
ATOM   2354 C  CD  . PRO A 1 302 ? -42.142 44.953 -30.149 1.00 30.96 ? 526  PRO A CD  1 
ATOM   2355 N  N   . VAL A 1 303 ? -40.130 40.855 -28.741 1.00 29.46 ? 527  VAL A N   1 
ATOM   2356 C  CA  . VAL A 1 303 ? -39.692 39.520 -29.104 1.00 25.49 ? 527  VAL A CA  1 
ATOM   2357 C  C   . VAL A 1 303 ? -40.460 38.485 -28.286 1.00 36.16 ? 527  VAL A C   1 
ATOM   2358 O  O   . VAL A 1 303 ? -41.075 38.818 -27.266 1.00 36.20 ? 527  VAL A O   1 
ATOM   2359 C  CB  . VAL A 1 303 ? -38.190 39.353 -28.905 1.00 25.82 ? 527  VAL A CB  1 
ATOM   2360 C  CG1 . VAL A 1 303 ? -37.798 39.648 -27.464 1.00 27.24 ? 527  VAL A CG1 1 
ATOM   2361 C  CG2 . VAL A 1 303 ? -37.775 37.934 -29.291 1.00 27.46 ? 527  VAL A CG2 1 
ATOM   2362 N  N   . LYS B 1 1   ? -5.460  43.135 -37.388 1.00 58.65 ? 225  LYS B N   1 
ATOM   2363 C  CA  . LYS B 1 1   ? -5.696  42.952 -35.955 1.00 57.61 ? 225  LYS B CA  1 
ATOM   2364 C  C   . LYS B 1 1   ? -4.454  42.421 -35.234 1.00 55.06 ? 225  LYS B C   1 
ATOM   2365 O  O   . LYS B 1 1   ? -3.917  41.366 -35.585 1.00 52.25 ? 225  LYS B O   1 
ATOM   2366 C  CB  . LYS B 1 1   ? -6.875  42.004 -35.717 1.00 59.54 ? 225  LYS B CB  1 
ATOM   2367 C  CG  . LYS B 1 1   ? -7.035  41.571 -34.261 1.00 54.14 ? 225  LYS B CG  1 
ATOM   2368 C  CD  . LYS B 1 1   ? -8.206  40.607 -34.072 1.00 46.07 ? 225  LYS B CD  1 
ATOM   2369 C  CE  . LYS B 1 1   ? -9.534  41.333 -34.192 1.00 52.97 ? 225  LYS B CE  1 
ATOM   2370 N  NZ  . LYS B 1 1   ? -10.695 40.405 -34.091 1.00 55.62 ? 225  LYS B NZ  1 
ATOM   2371 N  N   . ALA B 1 2   ? -4.024  43.161 -34.214 1.00 48.89 ? 226  ALA B N   1 
ATOM   2372 C  CA  . ALA B 1 2   ? -2.814  42.839 -33.471 1.00 41.01 ? 226  ALA B CA  1 
ATOM   2373 C  C   . ALA B 1 2   ? -3.042  41.680 -32.511 1.00 34.88 ? 226  ALA B C   1 
ATOM   2374 O  O   . ALA B 1 2   ? -4.078  41.598 -31.844 1.00 32.29 ? 226  ALA B O   1 
ATOM   2375 C  CB  . ALA B 1 2   ? -2.331  44.059 -32.688 1.00 41.21 ? 226  ALA B CB  1 
ATOM   2376 N  N   . PHE B 1 3   ? -2.054  40.793 -32.434 1.00 32.03 ? 227  PHE B N   1 
ATOM   2377 C  CA  . PHE B 1 3   ? -2.102  39.681 -31.494 1.00 28.57 ? 227  PHE B CA  1 
ATOM   2378 C  C   . PHE B 1 3   ? -2.029  40.192 -30.056 1.00 23.44 ? 227  PHE B C   1 
ATOM   2379 O  O   . PHE B 1 3   ? -1.267  41.106 -29.744 1.00 24.90 ? 227  PHE B O   1 
ATOM   2380 C  CB  . PHE B 1 3   ? -0.949  38.714 -31.791 1.00 28.86 ? 227  PHE B CB  1 
ATOM   2381 C  CG  . PHE B 1 3   ? -0.840  37.575 -30.825 1.00 26.83 ? 227  PHE B CG  1 
ATOM   2382 C  CD1 . PHE B 1 3   ? -1.735  36.512 -30.878 1.00 23.66 ? 227  PHE B CD1 1 
ATOM   2383 C  CD2 . PHE B 1 3   ? 0.175   37.547 -29.883 1.00 25.33 ? 227  PHE B CD2 1 
ATOM   2384 C  CE1 . PHE B 1 3   ? -1.637  35.457 -29.994 1.00 22.39 ? 227  PHE B CE1 1 
ATOM   2385 C  CE2 . PHE B 1 3   ? 0.281   36.497 -28.991 1.00 22.53 ? 227  PHE B CE2 1 
ATOM   2386 C  CZ  . PHE B 1 3   ? -0.634  35.443 -29.049 1.00 25.48 ? 227  PHE B CZ  1 
ATOM   2387 N  N   . THR B 1 4   ? -2.839  39.607 -29.174 1.00 26.58 ? 228  THR B N   1 
ATOM   2388 C  CA  . THR B 1 4   ? -2.854  39.989 -27.767 1.00 27.08 ? 228  THR B CA  1 
ATOM   2389 C  C   . THR B 1 4   ? -3.065  38.759 -26.895 1.00 23.75 ? 228  THR B C   1 
ATOM   2390 O  O   . THR B 1 4   ? -3.572  37.731 -27.342 1.00 26.13 ? 228  THR B O   1 
ATOM   2391 C  CB  . THR B 1 4   ? -3.964  40.996 -27.429 1.00 23.88 ? 228  THR B CB  1 
ATOM   2392 O  OG1 . THR B 1 4   ? -5.233  40.416 -27.745 1.00 25.14 ? 228  THR B OG1 1 
ATOM   2393 C  CG2 . THR B 1 4   ? -3.797  42.308 -28.197 1.00 26.19 ? 228  THR B CG2 1 
ATOM   2394 N  N   . ILE B 1 5   ? -2.690  38.907 -25.630 1.00 25.80 ? 229  ILE B N   1 
ATOM   2395 C  CA  . ILE B 1 5   ? -2.866  37.930 -24.557 1.00 27.61 ? 229  ILE B CA  1 
ATOM   2396 C  C   . ILE B 1 5   ? -3.824  38.561 -23.552 1.00 26.45 ? 229  ILE B C   1 
ATOM   2397 O  O   . ILE B 1 5   ? -3.713  39.764 -23.285 1.00 25.47 ? 229  ILE B O   1 
ATOM   2398 C  CB  . ILE B 1 5   ? -1.522  37.599 -23.882 1.00 28.02 ? 229  ILE B CB  1 
ATOM   2399 C  CG1 . ILE B 1 5   ? -0.513  37.055 -24.885 1.00 33.71 ? 229  ILE B CG1 1 
ATOM   2400 C  CG2 . ILE B 1 5   ? -1.702  36.600 -22.754 1.00 31.46 ? 229  ILE B CG2 1 
ATOM   2401 C  CD1 . ILE B 1 5   ? -0.933  35.739 -25.490 1.00 27.94 ? 229  ILE B CD1 1 
ATOM   2402 N  N   . PRO B 1 6   ? -4.759  37.823 -22.964 1.00 27.49 ? 230  PRO B N   1 
ATOM   2403 C  CA  . PRO B 1 6   ? -5.528  38.393 -21.850 1.00 25.19 ? 230  PRO B CA  1 
ATOM   2404 C  C   . PRO B 1 6   ? -4.659  38.542 -20.606 1.00 29.86 ? 230  PRO B C   1 
ATOM   2405 O  O   . PRO B 1 6   ? -3.737  37.753 -20.373 1.00 25.20 ? 230  PRO B O   1 
ATOM   2406 C  CB  . PRO B 1 6   ? -6.652  37.372 -21.632 1.00 26.78 ? 230  PRO B CB  1 
ATOM   2407 C  CG  . PRO B 1 6   ? -6.108  36.089 -22.154 1.00 24.29 ? 230  PRO B CG  1 
ATOM   2408 C  CD  . PRO B 1 6   ? -5.216  36.466 -23.322 1.00 24.73 ? 230  PRO B CD  1 
ATOM   2409 N  N   . VAL B 1 7   ? -4.968  39.569 -19.808 1.00 25.14 ? 231  VAL B N   1 
ATOM   2410 C  CA  . VAL B 1 7   ? -4.209  39.915 -18.605 1.00 24.32 ? 231  VAL B CA  1 
ATOM   2411 C  C   . VAL B 1 7   ? -4.768  39.135 -17.418 1.00 25.12 ? 231  VAL B C   1 
ATOM   2412 O  O   . VAL B 1 7   ? -5.851  39.443 -16.917 1.00 26.64 ? 231  VAL B O   1 
ATOM   2413 C  CB  . VAL B 1 7   ? -4.251  41.425 -18.330 1.00 28.33 ? 231  VAL B CB  1 
ATOM   2414 C  CG1 . VAL B 1 7   ? -3.474  41.758 -17.064 1.00 29.29 ? 231  VAL B CG1 1 
ATOM   2415 C  CG2 . VAL B 1 7   ? -3.698  42.208 -19.507 1.00 30.37 ? 231  VAL B CG2 1 
ATOM   2416 N  N   . LEU B 1 8   ? -4.016  38.144 -16.939 1.00 25.05 ? 232  LEU B N   1 
ATOM   2417 C  CA  . LEU B 1 8   ? -4.503  37.247 -15.897 1.00 23.50 ? 232  LEU B CA  1 
ATOM   2418 C  C   . LEU B 1 8   ? -3.378  36.836 -14.959 1.00 22.50 ? 232  LEU B C   1 
ATOM   2419 O  O   . LEU B 1 8   ? -2.293  36.463 -15.419 1.00 20.99 ? 232  LEU B O   1 
ATOM   2420 C  CB  . LEU B 1 8   ? -5.101  35.984 -16.519 1.00 24.64 ? 232  LEU B CB  1 
ATOM   2421 C  CG  . LEU B 1 8   ? -6.216  36.102 -17.537 1.00 23.63 ? 232  LEU B CG  1 
ATOM   2422 C  CD1 . LEU B 1 8   ? -6.305  34.778 -18.254 1.00 28.49 ? 232  LEU B CD1 1 
ATOM   2423 C  CD2 . LEU B 1 8   ? -7.515  36.393 -16.832 1.00 28.18 ? 232  LEU B CD2 1 
ATOM   2424 N  N   . LYS B 1 9   ? -3.652  36.861 -13.656 1.00 24.04 ? 233  LYS B N   1 
ATOM   2425 C  CA  . LYS B 1 9   ? -2.783  36.203 -12.694 1.00 24.20 ? 233  LYS B CA  1 
ATOM   2426 C  C   . LYS B 1 9   ? -2.888  34.690 -12.861 1.00 22.91 ? 233  LYS B C   1 
ATOM   2427 O  O   . LYS B 1 9   ? -3.847  34.177 -13.441 1.00 23.28 ? 233  LYS B O   1 
ATOM   2428 C  CB  . LYS B 1 9   ? -3.160  36.593 -11.262 1.00 23.92 ? 233  LYS B CB  1 
ATOM   2429 C  CG  . LYS B 1 9   ? -3.038  38.080 -10.967 1.00 34.67 ? 233  LYS B CG  1 
ATOM   2430 C  CD  . LYS B 1 9   ? -3.384  38.406 -9.518  1.00 37.95 ? 233  LYS B CD  1 
ATOM   2431 C  CE  . LYS B 1 9   ? -4.883  38.498 -9.305  1.00 42.93 ? 233  LYS B CE  1 
ATOM   2432 N  NZ  . LYS B 1 9   ? -5.204  39.408 -8.164  1.00 47.49 ? 233  LYS B NZ  1 
ATOM   2433 N  N   . ILE B 1 10  ? -1.887  33.970 -12.352 1.00 22.39 ? 234  ILE B N   1 
ATOM   2434 C  CA  . ILE B 1 10  ? -1.967  32.509 -12.396 1.00 29.24 ? 234  ILE B CA  1 
ATOM   2435 C  C   . ILE B 1 10  ? -3.234  32.035 -11.695 1.00 27.07 ? 234  ILE B C   1 
ATOM   2436 O  O   . ILE B 1 10  ? -3.934  31.132 -12.175 1.00 25.07 ? 234  ILE B O   1 
ATOM   2437 C  CB  . ILE B 1 10  ? -0.709  31.871 -11.776 1.00 27.66 ? 234  ILE B CB  1 
ATOM   2438 C  CG1 . ILE B 1 10  ? 0.555   32.284 -12.544 1.00 24.23 ? 234  ILE B CG1 1 
ATOM   2439 C  CG2 . ILE B 1 10  ? -0.841  30.340 -11.755 1.00 31.52 ? 234  ILE B CG2 1 
ATOM   2440 C  CD1 . ILE B 1 10  ? 0.533   31.925 -14.016 1.00 28.89 ? 234  ILE B CD1 1 
ATOM   2441 N  N   . SER B 1 11  ? -3.572  32.669 -10.570 1.00 27.89 ? 235  SER B N   1 
ATOM   2442 C  CA  . SER B 1 11  ? -4.715  32.259 -9.766  1.00 29.73 ? 235  SER B CA  1 
ATOM   2443 C  C   . SER B 1 11  ? -6.053  32.598 -10.412 1.00 30.20 ? 235  SER B C   1 
ATOM   2444 O  O   . SER B 1 11  ? -7.098  32.227 -9.864  1.00 36.60 ? 235  SER B O   1 
ATOM   2445 C  CB  . SER B 1 11  ? -4.633  32.909 -8.381  1.00 31.12 ? 235  SER B CB  1 
ATOM   2446 O  OG  . SER B 1 11  ? -4.836  34.314 -8.456  1.00 29.46 ? 235  SER B OG  1 
ATOM   2447 N  N   . GLU B 1 12  ? -6.057  33.310 -11.531 1.00 27.03 ? 236  GLU B N   1 
ATOM   2448 C  CA  . GLU B 1 12  ? -7.283  33.566 -12.271 1.00 30.10 ? 236  GLU B CA  1 
ATOM   2449 C  C   . GLU B 1 12  ? -7.441  32.644 -13.474 1.00 25.50 ? 236  GLU B C   1 
ATOM   2450 O  O   . GLU B 1 12  ? -8.463  32.711 -14.162 1.00 26.65 ? 236  GLU B O   1 
ATOM   2451 C  CB  . GLU B 1 12  ? -7.332  35.032 -12.712 1.00 25.04 ? 236  GLU B CB  1 
ATOM   2452 C  CG  . GLU B 1 12  ? -7.422  35.988 -11.536 1.00 30.22 ? 236  GLU B CG  1 
ATOM   2453 C  CD  . GLU B 1 12  ? -7.142  37.425 -11.916 1.00 32.59 ? 236  GLU B CD  1 
ATOM   2454 O  OE1 . GLU B 1 12  ? -6.383  37.654 -12.880 1.00 30.26 ? 236  GLU B OE1 1 
ATOM   2455 O  OE2 . GLU B 1 12  ? -7.679  38.332 -11.242 1.00 38.32 ? 236  GLU B OE2 1 
ATOM   2456 N  N   . MET B 1 13  ? -6.468  31.779 -13.729 1.00 21.64 ? 237  MET B N   1 
ATOM   2457 C  CA  . MET B 1 13  ? -6.489  30.915 -14.893 1.00 21.40 ? 237  MET B CA  1 
ATOM   2458 C  C   . MET B 1 13  ? -7.208  29.602 -14.613 1.00 20.73 ? 237  MET B C   1 
ATOM   2459 O  O   . MET B 1 13  ? -7.181  29.078 -13.494 1.00 21.65 ? 237  MET B O   1 
ATOM   2460 C  CB  . MET B 1 13  ? -5.060  30.614 -15.353 1.00 23.23 ? 237  MET B CB  1 
ATOM   2461 C  CG  . MET B 1 13  ? -4.306  31.814 -15.863 1.00 23.25 ? 237  MET B CG  1 
ATOM   2462 S  SD  . MET B 1 13  ? -2.637  31.318 -16.348 1.00 26.39 ? 237  MET B SD  1 
ATOM   2463 C  CE  . MET B 1 13  ? -2.033  32.863 -17.044 1.00 26.82 ? 237  MET B CE  1 
ATOM   2464 N  N   . THR B 1 14  ? -7.813  29.056 -15.667 1.00 17.78 ? 238  THR B N   1 
ATOM   2465 C  CA  . THR B 1 14  ? -8.565  27.811 -15.622 1.00 20.32 ? 238  THR B CA  1 
ATOM   2466 C  C   . THR B 1 14  ? -7.804  26.726 -16.373 1.00 17.94 ? 238  THR B C   1 
ATOM   2467 O  O   . THR B 1 14  ? -7.337  26.952 -17.494 1.00 18.50 ? 238  THR B O   1 
ATOM   2468 C  CB  . THR B 1 14  ? -9.943  27.991 -16.259 1.00 19.74 ? 238  THR B CB  1 
ATOM   2469 O  OG1 . THR B 1 14  ? -10.650 29.041 -15.584 1.00 19.35 ? 238  THR B OG1 1 
ATOM   2470 C  CG2 . THR B 1 14  ? -10.731 26.707 -16.182 1.00 18.54 ? 238  THR B CG2 1 
ATOM   2471 N  N   . ASN B 1 15  ? -7.696  25.551 -15.769 1.00 18.76 ? 239  ASN B N   1 
ATOM   2472 C  CA  . ASN B 1 15  ? -7.093  24.436 -16.472 1.00 16.45 ? 239  ASN B CA  1 
ATOM   2473 C  C   . ASN B 1 15  ? -7.973  24.055 -17.652 1.00 19.18 ? 239  ASN B C   1 
ATOM   2474 O  O   . ASN B 1 15  ? -9.201  24.003 -17.545 1.00 18.26 ? 239  ASN B O   1 
ATOM   2475 C  CB  . ASN B 1 15  ? -6.901  23.249 -15.538 1.00 15.90 ? 239  ASN B CB  1 
ATOM   2476 C  CG  . ASN B 1 15  ? -5.830  22.284 -16.042 1.00 19.58 ? 239  ASN B CG  1 
ATOM   2477 O  OD1 . ASN B 1 15  ? -5.981  21.652 -17.090 1.00 18.20 ? 239  ASN B OD1 1 
ATOM   2478 N  ND2 . ASN B 1 15  ? -4.749  22.168 -15.290 1.00 17.36 ? 239  ASN B ND2 1 
ATOM   2479 N  N   . SER B 1 16  ? -7.340  23.829 -18.796 1.00 18.43 ? 240  SER B N   1 
ATOM   2480 C  CA  . SER B 1 16  ? -8.060  23.421 -19.989 1.00 17.26 ? 240  SER B CA  1 
ATOM   2481 C  C   . SER B 1 16  ? -8.239  21.906 -20.099 1.00 18.07 ? 240  SER B C   1 
ATOM   2482 O  O   . SER B 1 16  ? -8.937  21.454 -21.005 1.00 17.25 ? 240  SER B O   1 
ATOM   2483 C  CB  . SER B 1 16  ? -7.338  23.943 -21.227 1.00 18.43 ? 240  SER B CB  1 
ATOM   2484 O  OG  . SER B 1 16  ? -5.992  23.497 -21.241 1.00 18.80 ? 240  SER B OG  1 
ATOM   2485 N  N   . ARG B 1 17  ? -7.653  21.111 -19.200 1.00 15.89 ? 241  ARG B N   1 
ATOM   2486 C  CA  . ARG B 1 17  ? -7.851  19.665 -19.244 1.00 19.52 ? 241  ARG B CA  1 
ATOM   2487 C  C   . ARG B 1 17  ? -8.725  19.127 -18.118 1.00 20.65 ? 241  ARG B C   1 
ATOM   2488 O  O   . ARG B 1 17  ? -9.075  17.940 -18.142 1.00 16.70 ? 241  ARG B O   1 
ATOM   2489 C  CB  . ARG B 1 17  ? -6.493  18.948 -19.246 1.00 18.53 ? 241  ARG B CB  1 
ATOM   2490 C  CG  . ARG B 1 17  ? -5.651  19.334 -20.459 1.00 15.82 ? 241  ARG B CG  1 
ATOM   2491 C  CD  . ARG B 1 17  ? -4.310  18.642 -20.413 1.00 17.48 ? 241  ARG B CD  1 
ATOM   2492 N  NE  . ARG B 1 17  ? -4.496  17.200 -20.524 1.00 17.82 ? 241  ARG B NE  1 
ATOM   2493 C  CZ  . ARG B 1 17  ? -3.739  16.308 -19.902 1.00 18.31 ? 241  ARG B CZ  1 
ATOM   2494 N  NH1 . ARG B 1 17  ? -2.681  16.675 -19.192 1.00 17.85 ? 241  ARG B NH1 1 
ATOM   2495 N  NH2 . ARG B 1 17  ? -4.071  15.022 -19.966 1.00 17.99 ? 241  ARG B NH2 1 
ATOM   2496 N  N   . PHE B 1 18  ? -9.119  19.967 -17.156 1.00 21.02 ? 242  PHE B N   1 
ATOM   2497 C  CA  . PHE B 1 18  ? -9.992  19.542 -16.067 1.00 17.27 ? 242  PHE B CA  1 
ATOM   2498 C  C   . PHE B 1 18  ? -10.607 20.803 -15.490 1.00 19.84 ? 242  PHE B C   1 
ATOM   2499 O  O   . PHE B 1 18  ? -9.897  21.810 -15.358 1.00 18.66 ? 242  PHE B O   1 
ATOM   2500 C  CB  . PHE B 1 18  ? -9.220  18.765 -14.996 1.00 16.85 ? 242  PHE B CB  1 
ATOM   2501 C  CG  . PHE B 1 18  ? -10.082 17.870 -14.154 1.00 17.99 ? 242  PHE B CG  1 
ATOM   2502 C  CD1 . PHE B 1 18  ? -10.479 16.618 -14.629 1.00 16.86 ? 242  PHE B CD1 1 
ATOM   2503 C  CD2 . PHE B 1 18  ? -10.497 18.269 -12.891 1.00 15.80 ? 242  PHE B CD2 1 
ATOM   2504 C  CE1 . PHE B 1 18  ? -11.276 15.784 -13.856 1.00 20.69 ? 242  PHE B CE1 1 
ATOM   2505 C  CE2 . PHE B 1 18  ? -11.285 17.437 -12.116 1.00 18.47 ? 242  PHE B CE2 1 
ATOM   2506 C  CZ  . PHE B 1 18  ? -11.676 16.188 -12.594 1.00 16.29 ? 242  PHE B CZ  1 
ATOM   2507 N  N   . PRO B 1 19  ? -11.902 20.815 -15.176 1.00 21.65 ? 243  PRO B N   1 
ATOM   2508 C  CA  . PRO B 1 19  ? -12.546 22.132 -14.909 1.00 17.75 ? 243  PRO B CA  1 
ATOM   2509 C  C   . PRO B 1 19  ? -12.284 22.639 -13.497 1.00 19.10 ? 243  PRO B C   1 
ATOM   2510 O  O   . PRO B 1 19  ? -13.169 22.688 -12.637 1.00 20.65 ? 243  PRO B O   1 
ATOM   2511 C  CB  . PRO B 1 19  ? -14.026 21.831 -15.167 1.00 18.75 ? 243  PRO B CB  1 
ATOM   2512 C  CG  . PRO B 1 19  ? -14.170 20.376 -14.778 1.00 20.67 ? 243  PRO B CG  1 
ATOM   2513 C  CD  . PRO B 1 19  ? -12.874 19.708 -15.206 1.00 15.73 ? 243  PRO B CD  1 
ATOM   2514 N  N   . VAL B 1 20  ? -11.032 23.019 -13.250 1.00 16.17 ? 244  VAL B N   1 
ATOM   2515 C  CA  . VAL B 1 20  ? -10.587 23.567 -11.968 1.00 19.93 ? 244  VAL B CA  1 
ATOM   2516 C  C   . VAL B 1 20  ? -9.563  24.659 -12.240 1.00 18.17 ? 244  VAL B C   1 
ATOM   2517 O  O   . VAL B 1 20  ? -8.970  24.714 -13.327 1.00 18.24 ? 244  VAL B O   1 
ATOM   2518 C  CB  . VAL B 1 20  ? -9.978  22.480 -11.055 1.00 17.88 ? 244  VAL B CB  1 
ATOM   2519 C  CG1 . VAL B 1 20  ? -11.042 21.489 -10.619 1.00 17.68 ? 244  VAL B CG1 1 
ATOM   2520 C  CG2 . VAL B 1 20  ? -8.815  21.763 -11.762 1.00 19.53 ? 244  VAL B CG2 1 
ATOM   2521 N  N   . PRO B 1 21  ? -9.342  25.555 -11.277 1.00 19.67 ? 245  PRO B N   1 
ATOM   2522 C  CA  . PRO B 1 21  ? -8.346  26.613 -11.488 1.00 19.84 ? 245  PRO B CA  1 
ATOM   2523 C  C   . PRO B 1 21  ? -6.942  26.044 -11.625 1.00 18.70 ? 245  PRO B C   1 
ATOM   2524 O  O   . PRO B 1 21  ? -6.630  24.967 -11.120 1.00 18.29 ? 245  PRO B O   1 
ATOM   2525 C  CB  . PRO B 1 21  ? -8.462  27.480 -10.229 1.00 21.83 ? 245  PRO B CB  1 
ATOM   2526 C  CG  . PRO B 1 21  ? -9.809  27.135 -9.644  1.00 21.89 ? 245  PRO B CG  1 
ATOM   2527 C  CD  . PRO B 1 21  ? -10.005 25.690 -9.966  1.00 21.02 ? 245  PRO B CD  1 
ATOM   2528 N  N   . VAL B 1 22  ? -6.092  26.791 -12.333 1.00 17.72 ? 246  VAL B N   1 
ATOM   2529 C  CA  . VAL B 1 22  ? -4.663  26.504 -12.344 1.00 19.55 ? 246  VAL B CA  1 
ATOM   2530 C  C   . VAL B 1 22  ? -4.075  26.787 -10.963 1.00 19.95 ? 246  VAL B C   1 
ATOM   2531 O  O   . VAL B 1 22  ? -4.382  27.807 -10.335 1.00 20.50 ? 246  VAL B O   1 
ATOM   2532 C  CB  . VAL B 1 22  ? -3.964  27.352 -13.424 1.00 20.19 ? 246  VAL B CB  1 
ATOM   2533 C  CG1 . VAL B 1 22  ? -2.452  27.237 -13.306 1.00 18.97 ? 246  VAL B CG1 1 
ATOM   2534 C  CG2 . VAL B 1 22  ? -4.434  26.964 -14.824 1.00 16.40 ? 246  VAL B CG2 1 
ATOM   2535 N  N   . ASP B 1 23  ? -3.215  25.887 -10.484 1.00 20.27 ? 247  ASP B N   1 
ATOM   2536 C  CA  . ASP B 1 23  ? -2.521  26.079 -9.213  1.00 20.91 ? 247  ASP B CA  1 
ATOM   2537 C  C   . ASP B 1 23  ? -1.129  26.684 -9.382  1.00 22.11 ? 247  ASP B C   1 
ATOM   2538 O  O   . ASP B 1 23  ? -0.747  27.571 -8.618  1.00 23.56 ? 247  ASP B O   1 
ATOM   2539 C  CB  . ASP B 1 23  ? -2.417  24.745 -8.452  1.00 21.52 ? 247  ASP B CB  1 
ATOM   2540 C  CG  . ASP B 1 23  ? -3.778  24.246 -7.929  1.00 30.46 ? 247  ASP B CG  1 
ATOM   2541 O  OD1 . ASP B 1 23  ? -4.384  24.931 -7.063  1.00 29.21 ? 247  ASP B OD1 1 
ATOM   2542 O  OD2 . ASP B 1 23  ? -4.253  23.171 -8.383  1.00 21.94 ? 247  ASP B OD2 1 
ATOM   2543 N  N   . GLN B 1 24  ? -0.356  26.238 -10.364 1.00 20.14 ? 248  GLN B N   1 
ATOM   2544 C  CA  . GLN B 1 24  ? 1.005   26.733 -10.513 1.00 20.29 ? 248  GLN B CA  1 
ATOM   2545 C  C   . GLN B 1 24  ? 1.455   26.511 -11.948 1.00 21.79 ? 248  GLN B C   1 
ATOM   2546 O  O   . GLN B 1 24  ? 0.949   25.632 -12.647 1.00 20.07 ? 248  GLN B O   1 
ATOM   2547 C  CB  . GLN B 1 24  ? 1.966   26.026 -9.548  1.00 21.85 ? 248  GLN B CB  1 
ATOM   2548 C  CG  . GLN B 1 24  ? 2.202   24.578 -9.933  1.00 21.31 ? 248  GLN B CG  1 
ATOM   2549 C  CD  . GLN B 1 24  ? 3.068   23.807 -8.956  1.00 23.12 ? 248  GLN B CD  1 
ATOM   2550 O  OE1 . GLN B 1 24  ? 3.705   22.821 -9.329  1.00 24.60 ? 248  GLN B OE1 1 
ATOM   2551 N  NE2 . GLN B 1 24  ? 3.084   24.235 -7.702  1.00 23.11 ? 248  GLN B NE2 1 
ATOM   2552 N  N   . MET B 1 25  ? 2.414   27.318 -12.377 1.00 21.88 ? 249  MET B N   1 
ATOM   2553 C  CA  . MET B 1 25  ? 3.189   26.993 -13.563 1.00 23.22 ? 249  MET B CA  1 
ATOM   2554 C  C   . MET B 1 25  ? 4.205   25.912 -13.220 1.00 20.77 ? 249  MET B C   1 
ATOM   2555 O  O   . MET B 1 25  ? 4.636   25.778 -12.072 1.00 20.81 ? 249  MET B O   1 
ATOM   2556 C  CB  . MET B 1 25  ? 3.899   28.239 -14.098 1.00 23.20 ? 249  MET B CB  1 
ATOM   2557 C  CG  . MET B 1 25  ? 2.949   29.297 -14.616 1.00 22.46 ? 249  MET B CG  1 
ATOM   2558 S  SD  . MET B 1 25  ? 3.797   30.749 -15.247 1.00 26.91 ? 249  MET B SD  1 
ATOM   2559 C  CE  . MET B 1 25  ? 4.482   31.470 -13.749 1.00 26.06 ? 249  MET B CE  1 
ATOM   2560 N  N   . TYR B 1 26  ? 4.571   25.117 -14.217 1.00 21.86 ? 250  TYR B N   1 
ATOM   2561 C  CA  . TYR B 1 26  ? 5.403   23.955 -13.941 1.00 22.33 ? 250  TYR B CA  1 
ATOM   2562 C  C   . TYR B 1 26  ? 6.216   23.633 -15.181 1.00 21.49 ? 250  TYR B C   1 
ATOM   2563 O  O   . TYR B 1 26  ? 5.735   23.795 -16.303 1.00 22.94 ? 250  TYR B O   1 
ATOM   2564 C  CB  . TYR B 1 26  ? 4.537   22.753 -13.529 1.00 21.38 ? 250  TYR B CB  1 
ATOM   2565 C  CG  . TYR B 1 26  ? 5.335   21.543 -13.091 1.00 22.76 ? 250  TYR B CG  1 
ATOM   2566 C  CD1 . TYR B 1 26  ? 5.879   21.472 -11.819 1.00 24.77 ? 250  TYR B CD1 1 
ATOM   2567 C  CD2 . TYR B 1 26  ? 5.548   20.472 -13.955 1.00 26.77 ? 250  TYR B CD2 1 
ATOM   2568 C  CE1 . TYR B 1 26  ? 6.622   20.375 -11.414 1.00 26.72 ? 250  TYR B CE1 1 
ATOM   2569 C  CE2 . TYR B 1 26  ? 6.284   19.364 -13.553 1.00 25.96 ? 250  TYR B CE2 1 
ATOM   2570 C  CZ  . TYR B 1 26  ? 6.823   19.328 -12.287 1.00 29.03 ? 250  TYR B CZ  1 
ATOM   2571 O  OH  . TYR B 1 26  ? 7.559   18.234 -11.887 1.00 37.10 ? 250  TYR B OH  1 
ATOM   2572 N  N   . THR B 1 27  ? 7.450   23.196 -14.987 1.00 22.13 ? 251  THR B N   1 
ATOM   2573 C  CA  . THR B 1 27  ? 8.237   22.741 -16.118 1.00 22.01 ? 251  THR B CA  1 
ATOM   2574 C  C   . THR B 1 27  ? 8.754   21.342 -15.836 1.00 23.07 ? 251  THR B C   1 
ATOM   2575 O  O   . THR B 1 27  ? 8.912   20.938 -14.682 1.00 23.99 ? 251  THR B O   1 
ATOM   2576 C  CB  . THR B 1 27  ? 9.389   23.694 -16.458 1.00 21.71 ? 251  THR B CB  1 
ATOM   2577 O  OG1 . THR B 1 27  ? 9.908   23.343 -17.739 1.00 21.15 ? 251  THR B OG1 1 
ATOM   2578 C  CG2 . THR B 1 27  ? 10.514  23.618 -15.423 1.00 23.94 ? 251  THR B CG2 1 
ATOM   2579 N  N   . SER B 1 28  ? 8.981   20.597 -16.911 1.00 21.81 ? 252  SER B N   1 
ATOM   2580 C  CA  . SER B 1 28  ? 9.371   19.204 -16.808 1.00 23.70 ? 252  SER B CA  1 
ATOM   2581 C  C   . SER B 1 28  ? 10.238  18.833 -17.998 1.00 25.53 ? 252  SER B C   1 
ATOM   2582 O  O   . SER B 1 28  ? 10.109  19.405 -19.083 1.00 23.68 ? 252  SER B O   1 
ATOM   2583 C  CB  . SER B 1 28  ? 8.148   18.282 -16.754 1.00 28.16 ? 252  SER B CB  1 
ATOM   2584 O  OG  . SER B 1 28  ? 8.526   16.932 -16.980 1.00 30.61 ? 252  SER B OG  1 
ATOM   2585 N  N   . ARG B 1 29  ? 11.126  17.863 -17.772 1.00 23.75 ? 253  ARG B N   1 
ATOM   2586 C  CA  . ARG B 1 29  ? 11.897  17.243 -18.835 1.00 27.32 ? 253  ARG B CA  1 
ATOM   2587 C  C   . ARG B 1 29  ? 11.070  16.242 -19.644 1.00 29.58 ? 253  ARG B C   1 
ATOM   2588 O  O   . ARG B 1 29  ? 11.444  15.909 -20.776 1.00 28.56 ? 253  ARG B O   1 
ATOM   2589 C  CB  . ARG B 1 29  ? 13.124  16.558 -18.217 1.00 32.55 ? 253  ARG B CB  1 
ATOM   2590 C  CG  . ARG B 1 29  ? 14.197  16.164 -19.190 1.00 41.98 ? 253  ARG B CG  1 
ATOM   2591 C  CD  . ARG B 1 29  ? 15.343  15.468 -18.467 1.00 40.97 ? 253  ARG B CD  1 
ATOM   2592 N  NE  . ARG B 1 29  ? 15.675  16.132 -17.212 1.00 46.55 ? 253  ARG B NE  1 
ATOM   2593 C  CZ  . ARG B 1 29  ? 16.540  17.131 -17.099 1.00 46.84 ? 253  ARG B CZ  1 
ATOM   2594 N  NH1 . ARG B 1 29  ? 17.152  17.640 -18.160 1.00 47.71 ? 253  ARG B NH1 1 
ATOM   2595 N  NH2 . ARG B 1 29  ? 16.808  17.623 -15.891 1.00 40.80 ? 253  ARG B NH2 1 
ATOM   2596 N  N   . SER B 1 30  ? 9.960   15.754 -19.089 1.00 25.65 ? 254  SER B N   1 
ATOM   2597 C  CA  . SER B 1 30  ? 9.092   14.791 -19.772 1.00 27.71 ? 254  SER B CA  1 
ATOM   2598 C  C   . SER B 1 30  ? 9.846   13.528 -20.187 1.00 29.22 ? 254  SER B C   1 
ATOM   2599 O  O   . SER B 1 30  ? 9.613   12.980 -21.266 1.00 28.64 ? 254  SER B O   1 
ATOM   2600 C  CB  . SER B 1 30  ? 8.413   15.433 -20.982 1.00 28.67 ? 254  SER B CB  1 
ATOM   2601 O  OG  . SER B 1 30  ? 7.676   16.590 -20.586 1.00 26.19 ? 254  SER B OG  1 
ATOM   2602 N  N   . GLU B 1 31  ? 10.750  13.063 -19.325 1.00 29.39 ? 255  GLU B N   1 
ATOM   2603 C  CA  . GLU B 1 31  ? 11.486  11.829 -19.584 1.00 33.03 ? 255  GLU B CA  1 
ATOM   2604 C  C   . GLU B 1 31  ? 10.533  10.652 -19.767 1.00 36.82 ? 255  GLU B C   1 
ATOM   2605 O  O   . GLU B 1 31  ? 9.672   10.396 -18.918 1.00 30.41 ? 255  GLU B O   1 
ATOM   2606 C  CB  . GLU B 1 31  ? 12.455  11.533 -18.440 1.00 36.51 ? 255  GLU B CB  1 
ATOM   2607 C  CG  . GLU B 1 31  ? 13.787  12.259 -18.559 1.00 44.39 ? 255  GLU B CG  1 
ATOM   2608 C  CD  . GLU B 1 31  ? 14.419  12.097 -19.937 1.00 53.27 ? 255  GLU B CD  1 
ATOM   2609 O  OE1 . GLU B 1 31  ? 14.810  10.958 -20.290 1.00 59.05 ? 255  GLU B OE1 1 
ATOM   2610 O  OE2 . GLU B 1 31  ? 14.506  13.107 -20.675 1.00 51.75 ? 255  GLU B OE2 1 
ATOM   2611 N  N   . GLY B 1 32  ? 10.698  9.936  -20.881 1.00 33.75 ? 256  GLY B N   1 
ATOM   2612 C  CA  . GLY B 1 32  ? 9.871   8.779  -21.166 1.00 36.83 ? 256  GLY B CA  1 
ATOM   2613 C  C   . GLY B 1 32  ? 8.404   9.079  -21.380 1.00 35.05 ? 256  GLY B C   1 
ATOM   2614 O  O   . GLY B 1 32  ? 7.567   8.186  -21.204 1.00 30.83 ? 256  GLY B O   1 
ATOM   2615 N  N   . ILE B 1 33  ? 8.068   10.308 -21.780 1.00 29.09 ? 257  ILE B N   1 
ATOM   2616 C  CA  . ILE B 1 33  ? 6.684   10.771 -21.853 1.00 29.22 ? 257  ILE B CA  1 
ATOM   2617 C  C   . ILE B 1 33  ? 6.448   11.455 -23.194 1.00 31.66 ? 257  ILE B C   1 
ATOM   2618 O  O   . ILE B 1 33  ? 7.276   12.249 -23.654 1.00 26.36 ? 257  ILE B O   1 
ATOM   2619 C  CB  . ILE B 1 33  ? 6.368   11.732 -20.684 1.00 29.71 ? 257  ILE B CB  1 
ATOM   2620 C  CG1 . ILE B 1 33  ? 6.086   10.940 -19.404 1.00 31.02 ? 257  ILE B CG1 1 
ATOM   2621 C  CG2 . ILE B 1 33  ? 5.258   12.714 -21.047 1.00 29.63 ? 257  ILE B CG2 1 
ATOM   2622 C  CD1 . ILE B 1 33  ? 6.092   11.784 -18.162 1.00 36.19 ? 257  ILE B CD1 1 
ATOM   2623 N  N   . VAL B 1 34  ? 5.323   11.135 -23.825 1.00 28.87 ? 258  VAL B N   1 
ATOM   2624 C  CA  . VAL B 1 34  ? 4.881   11.801 -25.041 1.00 23.61 ? 258  VAL B CA  1 
ATOM   2625 C  C   . VAL B 1 34  ? 3.763   12.754 -24.648 1.00 24.63 ? 258  VAL B C   1 
ATOM   2626 O  O   . VAL B 1 34  ? 2.728   12.329 -24.121 1.00 22.09 ? 258  VAL B O   1 
ATOM   2627 C  CB  . VAL B 1 34  ? 4.418   10.789 -26.101 1.00 24.11 ? 258  VAL B CB  1 
ATOM   2628 C  CG1 . VAL B 1 34  ? 3.900   11.496 -27.355 1.00 21.71 ? 258  VAL B CG1 1 
ATOM   2629 C  CG2 . VAL B 1 34  ? 5.571   9.861  -26.452 1.00 28.57 ? 258  VAL B CG2 1 
ATOM   2630 N  N   . VAL B 1 35  ? 3.990   14.044 -24.863 1.00 19.23 ? 259  VAL B N   1 
ATOM   2631 C  CA  . VAL B 1 35  ? 3.037   15.076 -24.488 1.00 22.46 ? 259  VAL B CA  1 
ATOM   2632 C  C   . VAL B 1 35  ? 2.102   15.273 -25.674 1.00 21.86 ? 259  VAL B C   1 
ATOM   2633 O  O   . VAL B 1 35  ? 2.464   15.903 -26.671 1.00 19.87 ? 259  VAL B O   1 
ATOM   2634 C  CB  . VAL B 1 35  ? 3.741   16.372 -24.091 1.00 22.60 ? 259  VAL B CB  1 
ATOM   2635 C  CG1 . VAL B 1 35  ? 2.710   17.416 -23.670 1.00 20.52 ? 259  VAL B CG1 1 
ATOM   2636 C  CG2 . VAL B 1 35  ? 4.723   16.090 -22.970 1.00 23.28 ? 259  VAL B CG2 1 
ATOM   2637 N  N   . GLN B 1 36  ? 0.890   14.726 -25.571 1.00 17.57 ? 260  GLN B N   1 
ATOM   2638 C  CA  . GLN B 1 36  ? -0.039  14.872 -26.685 1.00 19.77 ? 260  GLN B CA  1 
ATOM   2639 C  C   . GLN B 1 36  ? -1.466  15.046 -26.169 1.00 21.03 ? 260  GLN B C   1 
ATOM   2640 O  O   . GLN B 1 36  ? -2.374  14.319 -26.594 1.00 20.56 ? 260  GLN B O   1 
ATOM   2641 C  CB  . GLN B 1 36  ? 0.066   13.662 -27.624 1.00 17.31 ? 260  GLN B CB  1 
ATOM   2642 C  CG  . GLN B 1 36  ? -0.625  13.839 -28.984 1.00 18.15 ? 260  GLN B CG  1 
ATOM   2643 C  CD  . GLN B 1 36  ? -0.285  12.735 -29.957 1.00 17.97 ? 260  GLN B CD  1 
ATOM   2644 O  OE1 . GLN B 1 36  ? 0.398   11.784 -29.602 1.00 19.67 ? 260  GLN B OE1 1 
ATOM   2645 N  NE2 . GLN B 1 36  ? -0.762  12.849 -31.182 1.00 18.61 ? 260  GLN B NE2 1 
ATOM   2646 N  N   . PRO B 1 37  ? -1.718  16.004 -25.273 1.00 21.24 ? 261  PRO B N   1 
ATOM   2647 C  CA  . PRO B 1 37  ? -3.084  16.191 -24.796 1.00 17.05 ? 261  PRO B CA  1 
ATOM   2648 C  C   . PRO B 1 37  ? -3.974  16.614 -25.948 1.00 18.48 ? 261  PRO B C   1 
ATOM   2649 O  O   . PRO B 1 37  ? -3.511  17.157 -26.954 1.00 18.50 ? 261  PRO B O   1 
ATOM   2650 C  CB  . PRO B 1 37  ? -2.947  17.302 -23.753 1.00 17.54 ? 261  PRO B CB  1 
ATOM   2651 C  CG  . PRO B 1 37  ? -1.856  18.139 -24.317 1.00 17.43 ? 261  PRO B CG  1 
ATOM   2652 C  CD  . PRO B 1 37  ? -0.853  17.125 -24.848 1.00 16.52 ? 261  PRO B CD  1 
ATOM   2653 N  N   . GLN B 1 38  ? -5.261  16.316 -25.804 1.00 17.02 ? 262  GLN B N   1 
ATOM   2654 C  CA  . GLN B 1 38  ? -6.253  16.653 -26.811 1.00 18.26 ? 262  GLN B CA  1 
ATOM   2655 C  C   . GLN B 1 38  ? -7.175  17.786 -26.387 1.00 17.09 ? 262  GLN B C   1 
ATOM   2656 O  O   . GLN B 1 38  ? -7.791  18.414 -27.254 1.00 17.73 ? 262  GLN B O   1 
ATOM   2657 C  CB  . GLN B 1 38  ? -7.082  15.405 -27.159 1.00 15.74 ? 262  GLN B CB  1 
ATOM   2658 C  CG  . GLN B 1 38  ? -6.209  14.290 -27.740 1.00 16.05 ? 262  GLN B CG  1 
ATOM   2659 C  CD  . GLN B 1 38  ? -5.485  14.726 -29.011 1.00 16.46 ? 262  GLN B CD  1 
ATOM   2660 O  OE1 . GLN B 1 38  ? -6.118  15.128 -29.993 1.00 16.27 ? 262  GLN B OE1 1 
ATOM   2661 N  NE2 . GLN B 1 38  ? -4.147  14.648 -28.998 1.00 18.83 ? 262  GLN B NE2 1 
ATOM   2662 N  N   . ASN B 1 39  ? -7.278  18.064 -25.094 1.00 18.11 ? 263  ASN B N   1 
ATOM   2663 C  CA  . ASN B 1 39  ? -7.965  19.251 -24.606 1.00 18.55 ? 263  ASN B CA  1 
ATOM   2664 C  C   . ASN B 1 39  ? -6.965  20.371 -24.360 1.00 20.99 ? 263  ASN B C   1 
ATOM   2665 O  O   . ASN B 1 39  ? -5.771  20.136 -24.152 1.00 16.81 ? 263  ASN B O   1 
ATOM   2666 C  CB  . ASN B 1 39  ? -8.743  18.942 -23.332 1.00 15.05 ? 263  ASN B CB  1 
ATOM   2667 C  CG  . ASN B 1 39  ? -9.871  17.951 -23.584 1.00 18.20 ? 263  ASN B CG  1 
ATOM   2668 O  OD1 . ASN B 1 39  ? -10.682 18.161 -24.468 1.00 18.90 ? 263  ASN B OD1 1 
ATOM   2669 N  ND2 . ASN B 1 39  ? -9.904  16.864 -22.826 1.00 15.79 ? 263  ASN B ND2 1 
ATOM   2670 N  N   . GLY B 1 40  ? -7.466  21.603 -24.388 1.00 17.72 ? 264  GLY B N   1 
ATOM   2671 C  CA  . GLY B 1 40  ? -6.551  22.735 -24.309 1.00 19.06 ? 264  GLY B CA  1 
ATOM   2672 C  C   . GLY B 1 40  ? -5.603  22.835 -25.485 1.00 17.82 ? 264  GLY B C   1 
ATOM   2673 O  O   . GLY B 1 40  ? -4.431  23.197 -25.306 1.00 19.52 ? 264  GLY B O   1 
ATOM   2674 N  N   . ARG B 1 41  ? -6.084  22.525 -26.687 1.00 15.73 ? 265  ARG B N   1 
ATOM   2675 C  CA  . ARG B 1 41  ? -5.282  22.547 -27.908 1.00 15.65 ? 265  ARG B CA  1 
ATOM   2676 C  C   . ARG B 1 41  ? -5.871  23.581 -28.861 1.00 19.31 ? 265  ARG B C   1 
ATOM   2677 O  O   . ARG B 1 41  ? -6.977  23.400 -29.375 1.00 18.64 ? 265  ARG B O   1 
ATOM   2678 C  CB  . ARG B 1 41  ? -5.239  21.161 -28.561 1.00 16.97 ? 265  ARG B CB  1 
ATOM   2679 C  CG  . ARG B 1 41  ? -4.594  20.081 -27.691 1.00 16.97 ? 265  ARG B CG  1 
ATOM   2680 C  CD  . ARG B 1 41  ? -3.139  20.442 -27.360 1.00 18.08 ? 265  ARG B CD  1 
ATOM   2681 N  NE  . ARG B 1 41  ? -2.296  20.569 -28.548 1.00 18.76 ? 265  ARG B NE  1 
ATOM   2682 C  CZ  . ARG B 1 41  ? -1.564  19.580 -29.055 1.00 20.48 ? 265  ARG B CZ  1 
ATOM   2683 N  NH1 . ARG B 1 41  ? -1.561  18.370 -28.515 1.00 17.31 ? 265  ARG B NH1 1 
ATOM   2684 N  NH2 . ARG B 1 41  ? -0.818  19.809 -30.129 1.00 18.73 ? 265  ARG B NH2 1 
ATOM   2685 N  N   . ALA B 1 42  ? -5.137  24.670 -29.083 1.00 20.57 ? 266  ALA B N   1 
ATOM   2686 C  CA  . ALA B 1 42  ? -5.581  25.744 -29.959 1.00 22.01 ? 266  ALA B CA  1 
ATOM   2687 C  C   . ALA B 1 42  ? -4.359  26.475 -30.492 1.00 18.55 ? 266  ALA B C   1 
ATOM   2688 O  O   . ALA B 1 42  ? -3.442  26.780 -29.731 1.00 17.08 ? 266  ALA B O   1 
ATOM   2689 C  CB  . ALA B 1 42  ? -6.500  26.737 -29.221 1.00 18.44 ? 266  ALA B CB  1 
ATOM   2690 N  N   . THR B 1 43  ? -4.360  26.773 -31.786 1.00 18.13 ? 267  THR B N   1 
ATOM   2691 C  CA  . THR B 1 43  ? -3.304  27.605 -32.336 1.00 22.64 ? 267  THR B CA  1 
ATOM   2692 C  C   . THR B 1 43  ? -3.502  29.050 -31.890 1.00 23.65 ? 267  THR B C   1 
ATOM   2693 O  O   . THR B 1 43  ? -4.603  29.470 -31.513 1.00 23.18 ? 267  THR B O   1 
ATOM   2694 C  CB  . THR B 1 43  ? -3.279  27.538 -33.866 1.00 20.70 ? 267  THR B CB  1 
ATOM   2695 O  OG1 . THR B 1 43  ? -4.442  28.191 -34.387 1.00 22.82 ? 267  THR B OG1 1 
ATOM   2696 C  CG2 . THR B 1 43  ? -3.239  26.093 -34.352 1.00 22.23 ? 267  THR B CG2 1 
ATOM   2697 N  N   . ILE B 1 44  ? -2.415  29.830 -31.942 1.00 22.21 ? 268  ILE B N   1 
ATOM   2698 C  CA  . ILE B 1 44  ? -2.517  31.214 -31.484 1.00 22.89 ? 268  ILE B CA  1 
ATOM   2699 C  C   . ILE B 1 44  ? -3.251  32.093 -32.477 1.00 21.74 ? 268  ILE B C   1 
ATOM   2700 O  O   . ILE B 1 44  ? -3.620  33.221 -32.126 1.00 19.49 ? 268  ILE B O   1 
ATOM   2701 C  CB  . ILE B 1 44  ? -1.152  31.862 -31.187 1.00 22.37 ? 268  ILE B CB  1 
ATOM   2702 C  CG1 . ILE B 1 44  ? -0.353  32.049 -32.467 1.00 21.97 ? 268  ILE B CG1 1 
ATOM   2703 C  CG2 . ILE B 1 44  ? -0.374  31.024 -30.166 1.00 19.49 ? 268  ILE B CG2 1 
ATOM   2704 C  CD1 . ILE B 1 44  ? 0.997   32.729 -32.230 1.00 21.07 ? 268  ILE B CD1 1 
ATOM   2705 N  N   . ASP B 1 45  ? -3.493  31.618 -33.700 1.00 19.47 ? 269  ASP B N   1 
ATOM   2706 C  CA  . ASP B 1 45  ? -4.364  32.354 -34.603 1.00 24.78 ? 269  ASP B CA  1 
ATOM   2707 C  C   . ASP B 1 45  ? -5.773  31.774 -34.649 1.00 26.51 ? 269  ASP B C   1 
ATOM   2708 O  O   . ASP B 1 45  ? -6.511  32.037 -35.603 1.00 29.19 ? 269  ASP B O   1 
ATOM   2709 C  CB  . ASP B 1 45  ? -3.762  32.464 -36.010 1.00 24.99 ? 269  ASP B CB  1 
ATOM   2710 C  CG  . ASP B 1 45  ? -3.444  31.132 -36.641 1.00 30.18 ? 269  ASP B CG  1 
ATOM   2711 O  OD1 . ASP B 1 45  ? -3.537  30.083 -35.967 1.00 30.40 ? 269  ASP B OD1 1 
ATOM   2712 O  OD2 . ASP B 1 45  ? -3.090  31.145 -37.839 1.00 35.48 ? 269  ASP B OD2 1 
ATOM   2713 N  N   . GLY B 1 46  ? -6.161  31.004 -33.632 1.00 24.17 ? 270  GLY B N   1 
ATOM   2714 C  CA  . GLY B 1 46  ? -7.556  30.758 -33.342 1.00 19.54 ? 270  GLY B CA  1 
ATOM   2715 C  C   . GLY B 1 46  ? -8.155  29.437 -33.787 1.00 25.03 ? 270  GLY B C   1 
ATOM   2716 O  O   . GLY B 1 46  ? -9.385  29.299 -33.759 1.00 19.38 ? 270  GLY B O   1 
ATOM   2717 N  N   . GLU B 1 47  ? -7.349  28.459 -34.172 1.00 23.07 ? 271  GLU B N   1 
ATOM   2718 C  CA  . GLU B 1 47  ? -7.893  27.180 -34.597 1.00 22.95 ? 271  GLU B CA  1 
ATOM   2719 C  C   . GLU B 1 47  ? -7.899  26.213 -33.420 1.00 19.45 ? 271  GLU B C   1 
ATOM   2720 O  O   . GLU B 1 47  ? -6.862  25.995 -32.790 1.00 18.58 ? 271  GLU B O   1 
ATOM   2721 C  CB  . GLU B 1 47  ? -7.080  26.616 -35.761 1.00 26.92 ? 271  GLU B CB  1 
ATOM   2722 C  CG  . GLU B 1 47  ? -7.589  25.280 -36.267 1.00 29.05 ? 271  GLU B CG  1 
ATOM   2723 C  CD  . GLU B 1 47  ? -6.718  24.709 -37.373 1.00 41.45 ? 271  GLU B CD  1 
ATOM   2724 O  OE1 . GLU B 1 47  ? -5.619  25.273 -37.613 1.00 41.34 ? 271  GLU B OE1 1 
ATOM   2725 O  OE2 . GLU B 1 47  ? -7.131  23.697 -37.996 1.00 46.67 ? 271  GLU B OE2 1 
ATOM   2726 N  N   . LEU B 1 48  ? -9.066  25.646 -33.122 1.00 18.69 ? 272  LEU B N   1 
ATOM   2727 C  CA  . LEU B 1 48  ? -9.177  24.649 -32.063 1.00 19.49 ? 272  LEU B CA  1 
ATOM   2728 C  C   . LEU B 1 48  ? -8.802  23.269 -32.590 1.00 20.19 ? 272  LEU B C   1 
ATOM   2729 O  O   . LEU B 1 48  ? -9.186  22.882 -33.696 1.00 18.17 ? 272  LEU B O   1 
ATOM   2730 C  CB  . LEU B 1 48  ? -10.598 24.599 -31.498 1.00 22.22 ? 272  LEU B CB  1 
ATOM   2731 C  CG  . LEU B 1 48  ? -11.270 25.888 -31.022 1.00 27.59 ? 272  LEU B CG  1 
ATOM   2732 C  CD1 . LEU B 1 48  ? -12.696 25.584 -30.537 1.00 24.26 ? 272  LEU B CD1 1 
ATOM   2733 C  CD2 . LEU B 1 48  ? -10.464 26.533 -29.929 1.00 19.98 ? 272  LEU B CD2 1 
ATOM   2734 N  N   . LEU B 1 49  ? -8.079  22.512 -31.777 1.00 17.13 ? 273  LEU B N   1 
ATOM   2735 C  CA  . LEU B 1 49  ? -7.578  21.210 -32.188 1.00 19.29 ? 273  LEU B CA  1 
ATOM   2736 C  C   . LEU B 1 49  ? -8.032  20.126 -31.215 1.00 19.44 ? 273  LEU B C   1 
ATOM   2737 O  O   . LEU B 1 49  ? -8.530  20.397 -30.118 1.00 15.57 ? 273  LEU B O   1 
ATOM   2738 C  CB  . LEU B 1 49  ? -6.043  21.219 -32.285 1.00 19.52 ? 273  LEU B CB  1 
ATOM   2739 C  CG  . LEU B 1 49  ? -5.440  22.396 -33.056 1.00 22.70 ? 273  LEU B CG  1 
ATOM   2740 C  CD1 . LEU B 1 49  ? -3.921  22.471 -32.852 1.00 22.17 ? 273  LEU B CD1 1 
ATOM   2741 C  CD2 . LEU B 1 49  ? -5.789  22.267 -34.545 1.00 25.21 ? 273  LEU B CD2 1 
ATOM   2742 N  N   . GLY B 1 50  ? -7.840  18.879 -31.640 1.00 20.20 ? 274  GLY B N   1 
ATOM   2743 C  CA  . GLY B 1 50  ? -8.168  17.743 -30.790 1.00 17.13 ? 274  GLY B CA  1 
ATOM   2744 C  C   . GLY B 1 50  ? -9.636  17.710 -30.400 1.00 19.63 ? 274  GLY B C   1 
ATOM   2745 O  O   . GLY B 1 50  ? -10.537 17.743 -31.250 1.00 17.87 ? 274  GLY B O   1 
ATOM   2746 N  N   . THR B 1 51  ? -9.889  17.616 -29.092 1.00 16.08 ? 275  THR B N   1 
ATOM   2747 C  CA  . THR B 1 51  ? -11.249 17.616 -28.566 1.00 16.95 ? 275  THR B CA  1 
ATOM   2748 C  C   . THR B 1 51  ? -11.577 18.920 -27.855 1.00 17.23 ? 275  THR B C   1 
ATOM   2749 O  O   . THR B 1 51  ? -12.470 18.959 -27.001 1.00 19.27 ? 275  THR B O   1 
ATOM   2750 C  CB  . THR B 1 51  ? -11.461 16.431 -27.624 1.00 18.57 ? 275  THR B CB  1 
ATOM   2751 O  OG1 . THR B 1 51  ? -10.482 16.467 -26.577 1.00 20.66 ? 275  THR B OG1 1 
ATOM   2752 C  CG2 . THR B 1 51  ? -11.324 15.103 -28.381 1.00 19.80 ? 275  THR B CG2 1 
ATOM   2753 N  N   . THR B 1 52  ? -10.876 19.988 -28.197 1.00 16.96 ? 276  THR B N   1 
ATOM   2754 C  CA  . THR B 1 52  ? -10.939 21.213 -27.425 1.00 18.61 ? 276  THR B CA  1 
ATOM   2755 C  C   . THR B 1 52  ? -12.226 21.970 -27.719 1.00 18.58 ? 276  THR B C   1 
ATOM   2756 O  O   . THR B 1 52  ? -12.548 22.230 -28.881 1.00 16.29 ? 276  THR B O   1 
ATOM   2757 C  CB  . THR B 1 52  ? -9.723  22.081 -27.751 1.00 16.68 ? 276  THR B CB  1 
ATOM   2758 O  OG1 . THR B 1 52  ? -8.533  21.390 -27.339 1.00 15.58 ? 276  THR B OG1 1 
ATOM   2759 C  CG2 . THR B 1 52  ? -9.818  23.417 -27.048 1.00 16.03 ? 276  THR B CG2 1 
ATOM   2760 N  N   . LEU B 1 53  ? -12.950 22.340 -26.666 1.00 15.74 ? 277  LEU B N   1 
ATOM   2761 C  CA  . LEU B 1 53  ? -14.094 23.228 -26.791 1.00 17.91 ? 277  LEU B CA  1 
ATOM   2762 C  C   . LEU B 1 53  ? -13.789 24.531 -26.056 1.00 17.44 ? 277  LEU B C   1 
ATOM   2763 O  O   . LEU B 1 53  ? -12.811 24.639 -25.316 1.00 19.70 ? 277  LEU B O   1 
ATOM   2764 C  CB  . LEU B 1 53  ? -15.372 22.555 -26.263 1.00 18.01 ? 277  LEU B CB  1 
ATOM   2765 C  CG  . LEU B 1 53  ? -15.270 21.675 -25.007 1.00 20.39 ? 277  LEU B CG  1 
ATOM   2766 C  CD1 . LEU B 1 53  ? -14.829 22.461 -23.764 1.00 16.62 ? 277  LEU B CD1 1 
ATOM   2767 C  CD2 . LEU B 1 53  ? -16.586 20.958 -24.748 1.00 18.66 ? 277  LEU B CD2 1 
ATOM   2768 N  N   . VAL B 1 54  ? -14.626 25.545 -26.250 1.00 17.76 ? 278  VAL B N   1 
ATOM   2769 C  CA  . VAL B 1 54  ? -14.322 26.815 -25.603 1.00 18.93 ? 278  VAL B CA  1 
ATOM   2770 C  C   . VAL B 1 54  ? -14.954 26.924 -24.224 1.00 18.77 ? 278  VAL B C   1 
ATOM   2771 O  O   . VAL B 1 54  ? -14.451 27.680 -23.386 1.00 23.78 ? 278  VAL B O   1 
ATOM   2772 C  CB  . VAL B 1 54  ? -14.742 28.029 -26.456 1.00 23.15 ? 278  VAL B CB  1 
ATOM   2773 C  CG1 . VAL B 1 54  ? -13.936 28.066 -27.759 1.00 26.93 ? 278  VAL B CG1 1 
ATOM   2774 C  CG2 . VAL B 1 54  ? -16.241 28.028 -26.718 1.00 24.65 ? 278  VAL B CG2 1 
ATOM   2775 N  N   . SER B 1 55  ? -16.016 26.187 -23.957 1.00 17.84 ? 279  SER B N   1 
ATOM   2776 C  CA  . SER B 1 55  ? -16.658 26.276 -22.653 1.00 18.45 ? 279  SER B CA  1 
ATOM   2777 C  C   . SER B 1 55  ? -15.703 25.815 -21.560 1.00 22.04 ? 279  SER B C   1 
ATOM   2778 O  O   . SER B 1 55  ? -15.146 24.712 -21.657 1.00 20.45 ? 279  SER B O   1 
ATOM   2779 C  CB  . SER B 1 55  ? -17.917 25.423 -22.615 1.00 18.45 ? 279  SER B CB  1 
ATOM   2780 O  OG  . SER B 1 55  ? -18.210 25.097 -21.276 1.00 20.46 ? 279  SER B OG  1 
ATOM   2781 N  N   . PRO B 1 56  ? -15.517 26.597 -20.491 1.00 21.05 ? 280  PRO B N   1 
ATOM   2782 C  CA  . PRO B 1 56  ? -14.522 26.233 -19.475 1.00 18.55 ? 280  PRO B CA  1 
ATOM   2783 C  C   . PRO B 1 56  ? -15.029 25.288 -18.400 1.00 22.22 ? 280  PRO B C   1 
ATOM   2784 O  O   . PRO B 1 56  ? -14.218 24.833 -17.583 1.00 21.64 ? 280  PRO B O   1 
ATOM   2785 C  CB  . PRO B 1 56  ? -14.152 27.590 -18.866 1.00 18.37 ? 280  PRO B CB  1 
ATOM   2786 C  CG  . PRO B 1 56  ? -15.484 28.360 -18.944 1.00 19.88 ? 280  PRO B CG  1 
ATOM   2787 C  CD  . PRO B 1 56  ? -16.105 27.933 -20.253 1.00 18.28 ? 280  PRO B CD  1 
ATOM   2788 N  N   . VAL B 1 57  ? -16.326 24.992 -18.356 1.00 17.25 ? 281  VAL B N   1 
ATOM   2789 C  CA  . VAL B 1 57  ? -16.897 24.119 -17.344 1.00 15.15 ? 281  VAL B CA  1 
ATOM   2790 C  C   . VAL B 1 57  ? -17.258 22.756 -17.910 1.00 18.51 ? 281  VAL B C   1 
ATOM   2791 O  O   . VAL B 1 57  ? -17.935 21.972 -17.241 1.00 24.63 ? 281  VAL B O   1 
ATOM   2792 C  CB  . VAL B 1 57  ? -18.124 24.767 -16.685 1.00 18.93 ? 281  VAL B CB  1 
ATOM   2793 C  CG1 . VAL B 1 57  ? -17.708 25.926 -15.780 1.00 22.35 ? 281  VAL B CG1 1 
ATOM   2794 C  CG2 . VAL B 1 57  ? -19.090 25.240 -17.752 1.00 16.38 ? 281  VAL B CG2 1 
ATOM   2795 N  N   . SER B 1 58  ? -16.832 22.447 -19.131 1.00 19.83 ? 282  SER B N   1 
ATOM   2796 C  CA  . SER B 1 58  ? -17.362 21.286 -19.828 1.00 18.87 ? 282  SER B CA  1 
ATOM   2797 C  C   . SER B 1 58  ? -16.383 20.130 -19.967 1.00 20.56 ? 282  SER B C   1 
ATOM   2798 O  O   . SER B 1 58  ? -16.829 18.996 -20.151 1.00 20.22 ? 282  SER B O   1 
ATOM   2799 C  CB  . SER B 1 58  ? -17.851 21.690 -21.225 1.00 19.39 ? 282  SER B CB  1 
ATOM   2800 O  OG  . SER B 1 58  ? -19.019 22.501 -21.149 1.00 23.70 ? 282  SER B OG  1 
ATOM   2801 N  N   . VAL B 1 59  ? -15.072 20.380 -19.900 1.00 15.59 ? 283  VAL B N   1 
ATOM   2802 C  CA  . VAL B 1 59  ? -14.119 19.304 -20.127 1.00 18.34 ? 283  VAL B CA  1 
ATOM   2803 C  C   . VAL B 1 59  ? -14.318 18.208 -19.074 1.00 18.52 ? 283  VAL B C   1 
ATOM   2804 O  O   . VAL B 1 59  ? -14.559 18.483 -17.888 1.00 19.24 ? 283  VAL B O   1 
ATOM   2805 C  CB  . VAL B 1 59  ? -12.682 19.863 -20.142 1.00 19.03 ? 283  VAL B CB  1 
ATOM   2806 C  CG1 . VAL B 1 59  ? -12.260 20.385 -18.760 1.00 19.76 ? 283  VAL B CG1 1 
ATOM   2807 C  CG2 . VAL B 1 59  ? -11.713 18.816 -20.646 1.00 19.78 ? 283  VAL B CG2 1 
ATOM   2808 N  N   . CYS B 1 60  ? -14.286 16.954 -19.529 1.00 17.04 ? 284  CYS B N   1 
ATOM   2809 C  CA  . CYS B 1 60  ? -14.472 15.742 -18.730 1.00 17.40 ? 284  CYS B CA  1 
ATOM   2810 C  C   . CYS B 1 60  ? -15.909 15.539 -18.250 1.00 17.59 ? 284  CYS B C   1 
ATOM   2811 O  O   . CYS B 1 60  ? -16.147 14.658 -17.411 1.00 19.86 ? 284  CYS B O   1 
ATOM   2812 C  CB  . CYS B 1 60  ? -13.527 15.698 -17.523 1.00 16.94 ? 284  CYS B CB  1 
ATOM   2813 S  SG  . CYS B 1 60  ? -11.809 15.502 -17.988 1.00 21.31 ? 284  CYS B SG  1 
ATOM   2814 N  N   . ASN B 1 61  ? -16.871 16.311 -18.745 1.00 15.12 ? 285  ASN B N   1 
ATOM   2815 C  CA  . ASN B 1 61  ? -18.279 16.009 -18.516 1.00 16.28 ? 285  ASN B CA  1 
ATOM   2816 C  C   . ASN B 1 61  ? -18.790 15.048 -19.584 1.00 18.47 ? 285  ASN B C   1 
ATOM   2817 O  O   . ASN B 1 61  ? -18.261 14.991 -20.695 1.00 18.85 ? 285  ASN B O   1 
ATOM   2818 C  CB  . ASN B 1 61  ? -19.145 17.274 -18.537 1.00 17.54 ? 285  ASN B CB  1 
ATOM   2819 C  CG  . ASN B 1 61  ? -18.986 18.110 -17.287 1.00 19.02 ? 285  ASN B CG  1 
ATOM   2820 O  OD1 . ASN B 1 61  ? -19.880 18.158 -16.442 1.00 18.12 ? 285  ASN B OD1 1 
ATOM   2821 N  ND2 . ASN B 1 61  ? -17.830 18.754 -17.150 1.00 15.49 ? 285  ASN B ND2 1 
ATOM   2822 N  N   . PHE B 1 62  ? -19.844 14.302 -19.240 1.00 18.44 ? 286  PHE B N   1 
ATOM   2823 C  CA  . PHE B 1 62  ? -20.560 13.471 -20.202 1.00 17.75 ? 286  PHE B CA  1 
ATOM   2824 C  C   . PHE B 1 62  ? -22.060 13.695 -20.071 1.00 20.65 ? 286  PHE B C   1 
ATOM   2825 O  O   . PHE B 1 62  ? -22.563 13.982 -18.979 1.00 23.19 ? 286  PHE B O   1 
ATOM   2826 C  CB  . PHE B 1 62  ? -20.293 11.971 -19.998 1.00 16.56 ? 286  PHE B CB  1 
ATOM   2827 C  CG  . PHE B 1 62  ? -18.879 11.528 -20.318 1.00 19.11 ? 286  PHE B CG  1 
ATOM   2828 C  CD1 . PHE B 1 62  ? -18.504 11.243 -21.622 1.00 18.27 ? 286  PHE B CD1 1 
ATOM   2829 C  CD2 . PHE B 1 62  ? -17.951 11.346 -19.307 1.00 18.06 ? 286  PHE B CD2 1 
ATOM   2830 C  CE1 . PHE B 1 62  ? -17.226 10.801 -21.910 1.00 22.85 ? 286  PHE B CE1 1 
ATOM   2831 C  CE2 . PHE B 1 62  ? -16.665 10.909 -19.593 1.00 20.06 ? 286  PHE B CE2 1 
ATOM   2832 C  CZ  . PHE B 1 62  ? -16.309 10.631 -20.886 1.00 21.24 ? 286  PHE B CZ  1 
ATOM   2833 N  N   . LYS B 1 63  ? -22.770 13.522 -21.193 1.00 17.19 ? 287  LYS B N   1 
ATOM   2834 C  CA  A LYS B 1 63  ? -24.221 13.585 -21.217 0.60 23.40 ? 287  LYS B CA  1 
ATOM   2835 C  CA  B LYS B 1 63  ? -24.222 13.641 -21.284 0.40 23.05 ? 287  LYS B CA  1 
ATOM   2836 C  C   . LYS B 1 63  ? -24.746 12.509 -22.146 1.00 17.98 ? 287  LYS B C   1 
ATOM   2837 O  O   . LYS B 1 63  ? -24.153 12.208 -23.182 1.00 20.00 ? 287  LYS B O   1 
ATOM   2838 C  CB  A LYS B 1 63  ? -24.750 14.949 -21.682 0.60 21.27 ? 287  LYS B CB  1 
ATOM   2839 C  CB  B LYS B 1 63  ? -24.672 14.957 -21.943 0.40 21.38 ? 287  LYS B CB  1 
ATOM   2840 C  CG  A LYS B 1 63  ? -25.521 15.691 -20.608 0.60 25.53 ? 287  LYS B CG  1 
ATOM   2841 C  CG  B LYS B 1 63  ? -24.679 16.187 -21.075 0.40 25.47 ? 287  LYS B CG  1 
ATOM   2842 C  CD  A LYS B 1 63  ? -26.152 16.976 -21.138 0.60 26.01 ? 287  LYS B CD  1 
ATOM   2843 C  CD  B LYS B 1 63  ? -25.355 17.335 -21.810 0.40 23.64 ? 287  LYS B CD  1 
ATOM   2844 C  CE  A LYS B 1 63  ? -26.369 18.017 -20.018 0.60 27.52 ? 287  LYS B CE  1 
ATOM   2845 C  CE  B LYS B 1 63  ? -25.584 18.521 -20.884 0.40 26.57 ? 287  LYS B CE  1 
ATOM   2846 N  NZ  A LYS B 1 63  ? -27.134 17.521 -18.830 0.60 21.62 ? 287  LYS B NZ  1 
ATOM   2847 N  NZ  B LYS B 1 63  ? -26.646 19.436 -21.389 0.40 26.59 ? 287  LYS B NZ  1 
ATOM   2848 N  N   . GLY B 1 64  ? -25.870 11.932 -21.770 1.00 20.98 ? 288  GLY B N   1 
ATOM   2849 C  CA  . GLY B 1 64  ? -26.437 10.924 -22.638 1.00 20.85 ? 288  GLY B CA  1 
ATOM   2850 C  C   . GLY B 1 64  ? -27.650 10.285 -22.010 1.00 24.27 ? 288  GLY B C   1 
ATOM   2851 O  O   . GLY B 1 64  ? -28.108 10.668 -20.926 1.00 24.45 ? 288  GLY B O   1 
ATOM   2852 N  N   . ASN B 1 65  ? -28.174 9.309  -22.737 1.00 21.49 ? 289  ASN B N   1 
ATOM   2853 C  CA  . ASN B 1 65  ? -29.266 8.491  -22.255 1.00 22.92 ? 289  ASN B CA  1 
ATOM   2854 C  C   . ASN B 1 65  ? -28.712 7.333  -21.438 1.00 23.80 ? 289  ASN B C   1 
ATOM   2855 O  O   . ASN B 1 65  ? -27.688 6.746  -21.796 1.00 25.61 ? 289  ASN B O   1 
ATOM   2856 C  CB  . ASN B 1 65  ? -30.078 7.957  -23.431 1.00 24.67 ? 289  ASN B CB  1 
ATOM   2857 C  CG  . ASN B 1 65  ? -31.259 7.159  -22.987 1.00 25.58 ? 289  ASN B CG  1 
ATOM   2858 O  OD1 . ASN B 1 65  ? -32.129 7.673  -22.287 1.00 22.88 ? 289  ASN B OD1 1 
ATOM   2859 N  ND2 . ASN B 1 65  ? -31.296 5.890  -23.371 1.00 25.25 ? 289  ASN B ND2 1 
ATOM   2860 N  N   . LEU B 1 66  ? -29.375 7.005  -20.332 1.00 24.69 ? 290  LEU B N   1 
ATOM   2861 C  CA  . LEU B 1 66  ? -29.026 5.758  -19.649 1.00 25.42 ? 290  LEU B CA  1 
ATOM   2862 C  C   . LEU B 1 66  ? -29.741 4.637  -20.385 1.00 25.69 ? 290  LEU B C   1 
ATOM   2863 O  O   . LEU B 1 66  ? -30.945 4.437  -20.236 1.00 27.65 ? 290  LEU B O   1 
ATOM   2864 C  CB  . LEU B 1 66  ? -29.382 5.799  -18.166 1.00 29.59 ? 290  LEU B CB  1 
ATOM   2865 C  CG  . LEU B 1 66  ? -28.527 4.816  -17.342 1.00 25.59 ? 290  LEU B CG  1 
ATOM   2866 C  CD1 . LEU B 1 66  ? -28.558 5.184  -15.878 1.00 25.96 ? 290  LEU B CD1 1 
ATOM   2867 C  CD2 . LEU B 1 66  ? -28.982 3.372  -17.521 1.00 24.06 ? 290  LEU B CD2 1 
ATOM   2868 N  N   . GLN B 1 67  ? -28.992 3.900  -21.198 1.00 25.77 ? 291  GLN B N   1 
ATOM   2869 C  CA  . GLN B 1 67  ? -29.609 2.899  -22.049 1.00 24.34 ? 291  GLN B CA  1 
ATOM   2870 C  C   . GLN B 1 67  ? -30.079 1.698  -21.237 1.00 32.00 ? 291  GLN B C   1 
ATOM   2871 O  O   . GLN B 1 67  ? -31.236 1.274  -21.344 1.00 25.06 ? 291  GLN B O   1 
ATOM   2872 C  CB  . GLN B 1 67  ? -28.626 2.468  -23.131 1.00 29.37 ? 291  GLN B CB  1 
ATOM   2873 C  CG  . GLN B 1 67  ? -29.019 1.165  -23.783 1.00 35.47 ? 291  GLN B CG  1 
ATOM   2874 C  CD  . GLN B 1 67  ? -28.322 0.952  -25.102 1.00 43.75 ? 291  GLN B CD  1 
ATOM   2875 O  OE1 . GLN B 1 67  ? -27.152 1.309  -25.268 1.00 42.89 ? 291  GLN B OE1 1 
ATOM   2876 N  NE2 . GLN B 1 67  ? -29.040 0.371  -26.061 1.00 50.18 ? 291  GLN B NE2 1 
ATOM   2877 N  N   . ALA B 1 68  ? -29.196 1.134  -20.423 1.00 27.99 ? 292  ALA B N   1 
ATOM   2878 C  CA  . ALA B 1 68  ? -29.533 -0.054 -19.658 1.00 28.56 ? 292  ALA B CA  1 
ATOM   2879 C  C   . ALA B 1 68  ? -28.442 -0.300 -18.633 1.00 23.91 ? 292  ALA B C   1 
ATOM   2880 O  O   . ALA B 1 68  ? -27.322 0.200  -18.760 1.00 24.04 ? 292  ALA B O   1 
ATOM   2881 C  CB  . ALA B 1 68  ? -29.679 -1.284 -20.560 1.00 32.83 ? 292  ALA B CB  1 
ATOM   2882 N  N   . GLU B 1 69  ? -28.782 -1.089 -17.623 1.00 26.61 ? 293  GLU B N   1 
ATOM   2883 C  CA  . GLU B 1 69  ? -27.752 -1.717 -16.812 1.00 29.81 ? 293  GLU B CA  1 
ATOM   2884 C  C   . GLU B 1 69  ? -27.052 -2.764 -17.662 1.00 27.22 ? 293  GLU B C   1 
ATOM   2885 O  O   . GLU B 1 69  ? -27.694 -3.490 -18.420 1.00 30.48 ? 293  GLU B O   1 
ATOM   2886 C  CB  . GLU B 1 69  ? -28.365 -2.355 -15.568 1.00 28.57 ? 293  GLU B CB  1 
ATOM   2887 C  CG  . GLU B 1 69  ? -27.406 -2.530 -14.418 1.00 31.28 ? 293  GLU B CG  1 
ATOM   2888 C  CD  . GLU B 1 69  ? -28.052 -3.238 -13.242 1.00 38.03 ? 293  GLU B CD  1 
ATOM   2889 O  OE1 . GLU B 1 69  ? -28.616 -4.338 -13.442 1.00 49.69 ? 293  GLU B OE1 1 
ATOM   2890 O  OE2 . GLU B 1 69  ? -28.006 -2.697 -12.120 1.00 38.06 ? 293  GLU B OE2 1 
ATOM   2891 N  N   . VAL B 1 70  ? -25.729 -2.822 -17.569 1.00 30.04 ? 294  VAL B N   1 
ATOM   2892 C  CA  . VAL B 1 70  ? -25.016 -3.847 -18.342 1.00 25.47 ? 294  VAL B CA  1 
ATOM   2893 C  C   . VAL B 1 70  ? -25.444 -5.230 -17.853 1.00 33.83 ? 294  VAL B C   1 
ATOM   2894 O  O   . VAL B 1 70  ? -25.376 -5.504 -16.640 1.00 34.42 ? 294  VAL B O   1 
ATOM   2895 C  CB  . VAL B 1 70  ? -23.494 -3.655 -18.213 1.00 29.34 ? 294  VAL B CB  1 
ATOM   2896 C  CG1 . VAL B 1 70  ? -22.754 -4.837 -18.805 1.00 31.84 ? 294  VAL B CG1 1 
ATOM   2897 C  CG2 . VAL B 1 70  ? -23.067 -2.359 -18.893 1.00 26.45 ? 294  VAL B CG2 1 
ATOM   2898 N  N   . PRO B 1 71  ? -25.897 -6.131 -18.730 1.00 35.24 ? 295  PRO B N   1 
ATOM   2899 C  CA  . PRO B 1 71  ? -26.470 -7.401 -18.258 1.00 38.72 ? 295  PRO B CA  1 
ATOM   2900 C  C   . PRO B 1 71  ? -25.469 -8.222 -17.452 1.00 33.91 ? 295  PRO B C   1 
ATOM   2901 O  O   . PRO B 1 71  ? -24.322 -8.418 -17.862 1.00 34.63 ? 295  PRO B O   1 
ATOM   2902 C  CB  . PRO B 1 71  ? -26.873 -8.106 -19.559 1.00 38.39 ? 295  PRO B CB  1 
ATOM   2903 C  CG  . PRO B 1 71  ? -27.065 -6.978 -20.545 1.00 35.43 ? 295  PRO B CG  1 
ATOM   2904 C  CD  . PRO B 1 71  ? -25.991 -5.998 -20.196 1.00 32.76 ? 295  PRO B CD  1 
ATOM   2905 N  N   . GLY B 1 72  ? -25.910 -8.687 -16.279 1.00 35.12 ? 296  GLY B N   1 
ATOM   2906 C  CA  . GLY B 1 72  ? -25.066 -9.449 -15.385 1.00 31.25 ? 296  GLY B CA  1 
ATOM   2907 C  C   . GLY B 1 72  ? -24.115 -8.644 -14.522 1.00 34.94 ? 296  GLY B C   1 
ATOM   2908 O  O   . GLY B 1 72  ? -23.523 -9.208 -13.596 1.00 38.67 ? 296  GLY B O   1 
ATOM   2909 N  N   . GLN B 1 73  ? -23.939 -7.349 -14.778 1.00 32.74 ? 297  GLN B N   1 
ATOM   2910 C  CA  . GLN B 1 73  ? -22.996 -6.529 -14.016 1.00 34.54 ? 297  GLN B CA  1 
ATOM   2911 C  C   . GLN B 1 73  ? -23.780 -5.444 -13.288 1.00 33.20 ? 297  GLN B C   1 
ATOM   2912 O  O   . GLN B 1 73  ? -23.894 -4.317 -13.777 1.00 30.84 ? 297  GLN B O   1 
ATOM   2913 C  CB  . GLN B 1 73  ? -21.927 -5.947 -14.934 1.00 33.86 ? 297  GLN B CB  1 
ATOM   2914 C  CG  . GLN B 1 73  ? -21.309 -7.013 -15.836 1.00 35.40 ? 297  GLN B CG  1 
ATOM   2915 C  CD  . GLN B 1 73  ? -20.011 -6.578 -16.472 1.00 36.43 ? 297  GLN B CD  1 
ATOM   2916 O  OE1 . GLN B 1 73  ? -19.098 -6.109 -15.792 1.00 39.10 ? 297  GLN B OE1 1 
ATOM   2917 N  NE2 . GLN B 1 73  ? -19.917 -6.736 -17.784 1.00 34.21 ? 297  GLN B NE2 1 
ATOM   2918 N  N   . HIS B 1 74  ? -24.305 -5.790 -12.112 1.00 34.22 ? 298  HIS B N   1 
ATOM   2919 C  CA  . HIS B 1 74  ? -25.184 -4.886 -11.381 1.00 30.16 ? 298  HIS B CA  1 
ATOM   2920 C  C   . HIS B 1 74  ? -24.497 -3.559 -11.109 1.00 28.40 ? 298  HIS B C   1 
ATOM   2921 O  O   . HIS B 1 74  ? -23.319 -3.516 -10.740 1.00 26.87 ? 298  HIS B O   1 
ATOM   2922 C  CB  . HIS B 1 74  ? -25.630 -5.517 -10.062 1.00 28.56 ? 298  HIS B CB  1 
ATOM   2923 C  CG  . HIS B 1 74  ? -26.134 -6.916 -10.210 1.00 34.54 ? 298  HIS B CG  1 
ATOM   2924 N  ND1 . HIS B 1 74  ? -27.289 -7.218 -10.901 1.00 43.64 ? 298  HIS B ND1 1 
ATOM   2925 C  CD2 . HIS B 1 74  ? -25.639 -8.097 -9.767  1.00 28.69 ? 298  HIS B CD2 1 
ATOM   2926 C  CE1 . HIS B 1 74  ? -27.484 -8.526 -10.875 1.00 35.89 ? 298  HIS B CE1 1 
ATOM   2927 N  NE2 . HIS B 1 74  ? -26.498 -9.081 -10.192 1.00 36.50 ? 298  HIS B NE2 1 
ATOM   2928 N  N   . GLN B 1 75  ? -25.250 -2.475 -11.322 1.00 24.22 ? 299  GLN B N   1 
ATOM   2929 C  CA  . GLN B 1 75  ? -24.841 -1.096 -11.060 1.00 24.68 ? 299  GLN B CA  1 
ATOM   2930 C  C   . GLN B 1 75  ? -23.707 -0.625 -11.960 1.00 22.42 ? 299  GLN B C   1 
ATOM   2931 O  O   . GLN B 1 75  ? -23.026 0.370  -11.650 1.00 22.56 ? 299  GLN B O   1 
ATOM   2932 C  CB  . GLN B 1 75  ? -24.501 -0.902 -9.576  1.00 24.07 ? 299  GLN B CB  1 
ATOM   2933 C  CG  . GLN B 1 75  ? -25.777 -0.962 -8.740  1.00 30.22 ? 299  GLN B CG  1 
ATOM   2934 C  CD  . GLN B 1 75  ? -25.559 -0.999 -7.238  1.00 29.71 ? 299  GLN B CD  1 
ATOM   2935 O  OE1 . GLN B 1 75  ? -26.367 -1.567 -6.512  1.00 27.42 ? 299  GLN B OE1 1 
ATOM   2936 N  NE2 . GLN B 1 75  ? -24.498 -0.365 -6.766  1.00 28.64 ? 299  GLN B NE2 1 
ATOM   2937 N  N   . LEU B 1 76  ? -23.503 -1.304 -13.085 1.00 21.88 ? 300  LEU B N   1 
ATOM   2938 C  CA  . LEU B 1 76  ? -22.711 -0.797 -14.196 1.00 21.29 ? 300  LEU B CA  1 
ATOM   2939 C  C   . LEU B 1 76  ? -23.695 -0.411 -15.290 1.00 21.18 ? 300  LEU B C   1 
ATOM   2940 O  O   . LEU B 1 76  ? -24.491 -1.246 -15.733 1.00 24.43 ? 300  LEU B O   1 
ATOM   2941 C  CB  . LEU B 1 76  ? -21.710 -1.839 -14.696 1.00 23.82 ? 300  LEU B CB  1 
ATOM   2942 C  CG  . LEU B 1 76  ? -20.799 -1.360 -15.826 1.00 25.19 ? 300  LEU B CG  1 
ATOM   2943 C  CD1 . LEU B 1 76  ? -19.753 -0.376 -15.302 1.00 23.38 ? 300  LEU B CD1 1 
ATOM   2944 C  CD2 . LEU B 1 76  ? -20.137 -2.540 -16.518 1.00 21.87 ? 300  LEU B CD2 1 
ATOM   2945 N  N   . TYR B 1 77  ? -23.657 0.856  -15.698 1.00 22.20 ? 301  TYR B N   1 
ATOM   2946 C  CA  . TYR B 1 77  ? -24.705 1.458  -16.501 1.00 20.54 ? 301  TYR B CA  1 
ATOM   2947 C  C   . TYR B 1 77  ? -24.144 1.893  -17.842 1.00 21.57 ? 301  TYR B C   1 
ATOM   2948 O  O   . TYR B 1 77  ? -23.092 2.541  -17.904 1.00 24.88 ? 301  TYR B O   1 
ATOM   2949 C  CB  . TYR B 1 77  ? -25.336 2.653  -15.771 1.00 21.91 ? 301  TYR B CB  1 
ATOM   2950 C  CG  . TYR B 1 77  ? -26.020 2.255  -14.476 1.00 24.94 ? 301  TYR B CG  1 
ATOM   2951 C  CD1 . TYR B 1 77  ? -27.289 1.684  -14.483 1.00 26.13 ? 301  TYR B CD1 1 
ATOM   2952 C  CD2 . TYR B 1 77  ? -25.388 2.425  -13.253 1.00 21.21 ? 301  TYR B CD2 1 
ATOM   2953 C  CE1 . TYR B 1 77  ? -27.912 1.308  -13.302 1.00 27.18 ? 301  TYR B CE1 1 
ATOM   2954 C  CE2 . TYR B 1 77  ? -26.004 2.056  -12.070 1.00 23.01 ? 301  TYR B CE2 1 
ATOM   2955 C  CZ  . TYR B 1 77  ? -27.265 1.508  -12.103 1.00 23.58 ? 301  TYR B CZ  1 
ATOM   2956 O  OH  . TYR B 1 77  ? -27.879 1.136  -10.931 1.00 31.49 ? 301  TYR B OH  1 
ATOM   2957 N  N   . GLN B 1 78  ? -24.864 1.554  -18.905 1.00 22.33 ? 302  GLN B N   1 
ATOM   2958 C  CA  . GLN B 1 78  ? -24.469 1.899  -20.260 1.00 22.01 ? 302  GLN B CA  1 
ATOM   2959 C  C   . GLN B 1 78  ? -25.106 3.228  -20.649 1.00 26.16 ? 302  GLN B C   1 
ATOM   2960 O  O   . GLN B 1 78  ? -26.337 3.351  -20.662 1.00 22.31 ? 302  GLN B O   1 
ATOM   2961 C  CB  . GLN B 1 78  ? -24.895 0.801  -21.232 1.00 24.79 ? 302  GLN B CB  1 
ATOM   2962 C  CG  . GLN B 1 78  ? -24.479 1.077  -22.657 1.00 24.21 ? 302  GLN B CG  1 
ATOM   2963 C  CD  . GLN B 1 78  ? -22.975 0.972  -22.824 1.00 24.06 ? 302  GLN B CD  1 
ATOM   2964 O  OE1 . GLN B 1 78  ? -22.405 -0.114 -22.688 1.00 20.52 ? 302  GLN B OE1 1 
ATOM   2965 N  NE2 . GLN B 1 78  ? -22.323 2.102  -23.102 1.00 23.45 ? 302  GLN B NE2 1 
ATOM   2966 N  N   . LEU B 1 79  ? -24.273 4.218  -20.972 1.00 22.22 ? 303  LEU B N   1 
ATOM   2967 C  CA  . LEU B 1 79  ? -24.759 5.458  -21.555 1.00 20.50 ? 303  LEU B CA  1 
ATOM   2968 C  C   . LEU B 1 79  ? -24.707 5.382  -23.078 1.00 26.29 ? 303  LEU B C   1 
ATOM   2969 O  O   . LEU B 1 79  ? -23.790 4.780  -23.650 1.00 22.84 ? 303  LEU B O   1 
ATOM   2970 C  CB  . LEU B 1 79  ? -23.921 6.652  -21.087 1.00 23.25 ? 303  LEU B CB  1 
ATOM   2971 C  CG  . LEU B 1 79  ? -23.901 7.075  -19.619 1.00 24.61 ? 303  LEU B CG  1 
ATOM   2972 C  CD1 . LEU B 1 79  ? -22.791 8.094  -19.412 1.00 21.59 ? 303  LEU B CD1 1 
ATOM   2973 C  CD2 . LEU B 1 79  ? -25.233 7.681  -19.223 1.00 23.62 ? 303  LEU B CD2 1 
ATOM   2974 N  N   . GLN B 1 80  ? -25.701 6.006  -23.727 1.00 24.11 ? 304  GLN B N   1 
ATOM   2975 C  CA  . GLN B 1 80  ? -25.631 6.410  -25.136 1.00 25.57 ? 304  GLN B CA  1 
ATOM   2976 C  C   . GLN B 1 80  ? -25.366 7.916  -25.154 1.00 22.95 ? 304  GLN B C   1 
ATOM   2977 O  O   . GLN B 1 80  ? -26.278 8.715  -24.926 1.00 20.08 ? 304  GLN B O   1 
ATOM   2978 C  CB  . GLN B 1 80  ? -26.926 6.077  -25.877 1.00 28.25 ? 304  GLN B CB  1 
ATOM   2979 C  CG  . GLN B 1 80  ? -27.253 4.587  -25.961 1.00 33.01 ? 304  GLN B CG  1 
ATOM   2980 C  CD  . GLN B 1 80  ? -28.730 4.313  -26.273 1.00 42.43 ? 304  GLN B CD  1 
ATOM   2981 O  OE1 . GLN B 1 80  ? -29.628 4.947  -25.713 1.00 32.49 ? 304  GLN B OE1 1 
ATOM   2982 N  NE2 . GLN B 1 80  ? -28.979 3.354  -27.164 1.00 45.08 ? 304  GLN B NE2 1 
ATOM   2983 N  N   . LEU B 1 81  ? -24.121 8.308  -25.420 1.00 21.24 ? 305  LEU B N   1 
ATOM   2984 C  CA  . LEU B 1 81  ? -23.754 9.714  -25.313 1.00 20.69 ? 305  LEU B CA  1 
ATOM   2985 C  C   . LEU B 1 81  ? -24.457 10.574 -26.363 1.00 20.59 ? 305  LEU B C   1 
ATOM   2986 O  O   . LEU B 1 81  ? -24.763 10.130 -27.471 1.00 22.51 ? 305  LEU B O   1 
ATOM   2987 C  CB  . LEU B 1 81  ? -22.241 9.901  -25.470 1.00 18.78 ? 305  LEU B CB  1 
ATOM   2988 C  CG  . LEU B 1 81  ? -21.240 9.338  -24.451 1.00 19.40 ? 305  LEU B CG  1 
ATOM   2989 C  CD1 . LEU B 1 81  ? -19.825 9.759  -24.824 1.00 19.55 ? 305  LEU B CD1 1 
ATOM   2990 C  CD2 . LEU B 1 81  ? -21.580 9.804  -23.036 1.00 18.87 ? 305  LEU B CD2 1 
ATOM   2991 N  N   . THR B 1 82  ? -24.726 11.818 -25.988 1.00 19.82 ? 306  THR B N   1 
ATOM   2992 C  CA  . THR B 1 82  ? -24.811 12.936 -26.917 1.00 21.68 ? 306  THR B CA  1 
ATOM   2993 C  C   . THR B 1 82  ? -23.583 13.818 -26.710 1.00 22.22 ? 306  THR B C   1 
ATOM   2994 O  O   . THR B 1 82  ? -22.818 13.632 -25.763 1.00 17.57 ? 306  THR B O   1 
ATOM   2995 C  CB  . THR B 1 82  ? -26.090 13.764 -26.696 1.00 26.02 ? 306  THR B CB  1 
ATOM   2996 O  OG1 . THR B 1 82  ? -26.025 14.427 -25.422 1.00 22.30 ? 306  THR B OG1 1 
ATOM   2997 C  CG2 . THR B 1 82  ? -27.336 12.880 -26.743 1.00 23.44 ? 306  THR B CG2 1 
ATOM   2998 N  N   . ASN B 1 83  ? -23.399 14.788 -27.601 1.00 21.96 ? 307  ASN B N   1 
ATOM   2999 C  CA  . ASN B 1 83  ? -22.444 15.854 -27.337 1.00 22.68 ? 307  ASN B CA  1 
ATOM   3000 C  C   . ASN B 1 83  ? -22.920 16.714 -26.172 1.00 21.93 ? 307  ASN B C   1 
ATOM   3001 O  O   . ASN B 1 83  ? -24.107 16.756 -25.837 1.00 22.44 ? 307  ASN B O   1 
ATOM   3002 C  CB  . ASN B 1 83  ? -22.259 16.730 -28.573 1.00 24.99 ? 307  ASN B CB  1 
ATOM   3003 C  CG  . ASN B 1 83  ? -21.331 16.111 -29.572 1.00 26.53 ? 307  ASN B CG  1 
ATOM   3004 O  OD1 . ASN B 1 83  ? -20.195 15.770 -29.242 1.00 28.86 ? 307  ASN B OD1 1 
ATOM   3005 N  ND2 . ASN B 1 83  ? -21.808 15.933 -30.798 1.00 23.93 ? 307  ASN B ND2 1 
ATOM   3006 N  N   . LEU B 1 84  ? -21.974 17.417 -25.557 1.00 21.66 ? 308  LEU B N   1 
ATOM   3007 C  CA  . LEU B 1 84  ? -22.308 18.189 -24.365 1.00 27.34 ? 308  LEU B CA  1 
ATOM   3008 C  C   . LEU B 1 84  ? -23.309 19.308 -24.652 1.00 26.37 ? 308  LEU B C   1 
ATOM   3009 O  O   . LEU B 1 84  ? -24.021 19.729 -23.734 1.00 26.73 ? 308  LEU B O   1 
ATOM   3010 C  CB  . LEU B 1 84  ? -21.026 18.746 -23.733 1.00 19.11 ? 308  LEU B CB  1 
ATOM   3011 C  CG  . LEU B 1 84  ? -20.248 17.633 -23.025 1.00 21.43 ? 308  LEU B CG  1 
ATOM   3012 C  CD1 . LEU B 1 84  ? -18.854 18.113 -22.567 1.00 17.06 ? 308  LEU B CD1 1 
ATOM   3013 C  CD2 . LEU B 1 84  ? -21.060 17.109 -21.832 1.00 19.46 ? 308  LEU B CD2 1 
ATOM   3014 N  N   . ASP B 1 85  ? -23.410 19.776 -25.899 1.00 25.08 ? 309  ASP B N   1 
ATOM   3015 C  CA  . ASP B 1 85  ? -24.389 20.803 -26.250 1.00 27.28 ? 309  ASP B CA  1 
ATOM   3016 C  C   . ASP B 1 85  ? -25.737 20.219 -26.654 1.00 29.42 ? 309  ASP B C   1 
ATOM   3017 O  O   . ASP B 1 85  ? -26.641 20.974 -27.020 1.00 26.48 ? 309  ASP B O   1 
ATOM   3018 C  CB  . ASP B 1 85  ? -23.852 21.714 -27.376 1.00 26.08 ? 309  ASP B CB  1 
ATOM   3019 C  CG  . ASP B 1 85  ? -23.576 20.965 -28.693 1.00 31.84 ? 309  ASP B CG  1 
ATOM   3020 O  OD1 . ASP B 1 85  ? -23.891 19.766 -28.819 1.00 27.80 ? 309  ASP B OD1 1 
ATOM   3021 O  OD2 . ASP B 1 85  ? -23.029 21.591 -29.622 1.00 33.52 ? 309  ASP B OD2 1 
ATOM   3022 N  N   . GLY B 1 86  ? -25.899 18.897 -26.607 1.00 24.81 ? 310  GLY B N   1 
ATOM   3023 C  CA  . GLY B 1 86  ? -27.150 18.267 -26.941 1.00 27.07 ? 310  GLY B CA  1 
ATOM   3024 C  C   . GLY B 1 86  ? -27.224 17.667 -28.332 1.00 24.70 ? 310  GLY B C   1 
ATOM   3025 O  O   . GLY B 1 86  ? -28.104 16.838 -28.578 1.00 23.23 ? 310  GLY B O   1 
ATOM   3026 N  N   . SER B 1 87  ? -26.343 18.063 -29.246 1.00 21.87 ? 311  SER B N   1 
ATOM   3027 C  CA  . SER B 1 87  ? -26.379 17.491 -30.583 1.00 26.39 ? 311  SER B CA  1 
ATOM   3028 C  C   . SER B 1 87  ? -25.929 16.028 -30.547 1.00 24.17 ? 311  SER B C   1 
ATOM   3029 O  O   . SER B 1 87  ? -25.172 15.626 -29.657 1.00 22.19 ? 311  SER B O   1 
ATOM   3030 C  CB  . SER B 1 87  ? -25.491 18.290 -31.527 1.00 24.86 ? 311  SER B CB  1 
ATOM   3031 O  OG  . SER B 1 87  ? -24.168 18.337 -31.033 1.00 29.93 ? 311  SER B OG  1 
ATOM   3032 N  N   . PRO B 1 88  ? -26.396 15.205 -31.489 1.00 23.56 ? 312  PRO B N   1 
ATOM   3033 C  CA  . PRO B 1 88  ? -26.059 13.779 -31.439 1.00 21.39 ? 312  PRO B CA  1 
ATOM   3034 C  C   . PRO B 1 88  ? -24.578 13.566 -31.684 1.00 29.18 ? 312  PRO B C   1 
ATOM   3035 O  O   . PRO B 1 88  ? -23.913 14.375 -32.332 1.00 27.83 ? 312  PRO B O   1 
ATOM   3036 C  CB  . PRO B 1 88  ? -26.902 13.166 -32.564 1.00 26.32 ? 312  PRO B CB  1 
ATOM   3037 C  CG  . PRO B 1 88  ? -27.147 14.291 -33.505 1.00 30.84 ? 312  PRO B CG  1 
ATOM   3038 C  CD  . PRO B 1 88  ? -27.242 15.530 -32.653 1.00 27.31 ? 312  PRO B CD  1 
ATOM   3039 N  N   . ILE B 1 89  ? -24.048 12.479 -31.121 1.00 27.59 ? 313  ILE B N   1 
ATOM   3040 C  CA  . ILE B 1 89  ? -22.676 12.108 -31.436 1.00 25.77 ? 313  ILE B CA  1 
ATOM   3041 C  C   . ILE B 1 89  ? -22.608 11.780 -32.918 1.00 26.45 ? 313  ILE B C   1 
ATOM   3042 O  O   . ILE B 1 89  ? -23.414 10.996 -33.436 1.00 29.08 ? 313  ILE B O   1 
ATOM   3043 C  CB  . ILE B 1 89  ? -22.211 10.918 -30.579 1.00 25.71 ? 313  ILE B CB  1 
ATOM   3044 C  CG1 . ILE B 1 89  ? -22.101 11.302 -29.099 1.00 26.01 ? 313  ILE B CG1 1 
ATOM   3045 C  CG2 . ILE B 1 89  ? -20.882 10.405 -31.086 1.00 22.44 ? 313  ILE B CG2 1 
ATOM   3046 C  CD1 . ILE B 1 89  ? -20.931 12.207 -28.761 1.00 29.19 ? 313  ILE B CD1 1 
ATOM   3047 N  N   . ASP B 1 90  ? -21.655 12.384 -33.615 1.00 26.31 ? 314  ASP B N   1 
ATOM   3048 C  CA  . ASP B 1 90  ? -21.418 12.056 -35.021 1.00 26.86 ? 314  ASP B CA  1 
ATOM   3049 C  C   . ASP B 1 90  ? -20.005 11.509 -35.169 1.00 28.05 ? 314  ASP B C   1 
ATOM   3050 O  O   . ASP B 1 90  ? -19.038 12.289 -35.247 1.00 24.88 ? 314  ASP B O   1 
ATOM   3051 C  CB  . ASP B 1 90  ? -21.630 13.279 -35.910 1.00 27.03 ? 314  ASP B CB  1 
ATOM   3052 C  CG  . ASP B 1 90  ? -21.626 12.931 -37.382 1.00 29.57 ? 314  ASP B CG  1 
ATOM   3053 O  OD1 . ASP B 1 90  ? -21.202 11.808 -37.730 1.00 31.00 ? 314  ASP B OD1 1 
ATOM   3054 O  OD2 . ASP B 1 90  ? -22.053 13.773 -38.201 1.00 26.25 ? 314  ASP B OD2 1 
ATOM   3055 N  N   . PRO B 1 91  ? -19.833 10.180 -35.217 1.00 27.46 ? 315  PRO B N   1 
ATOM   3056 C  CA  . PRO B 1 91  ? -18.481 9.615  -35.331 1.00 23.13 ? 315  PRO B CA  1 
ATOM   3057 C  C   . PRO B 1 91  ? -17.795 9.915  -36.655 1.00 26.33 ? 315  PRO B C   1 
ATOM   3058 O  O   . PRO B 1 91  ? -16.620 9.552  -36.806 1.00 26.31 ? 315  PRO B O   1 
ATOM   3059 C  CB  . PRO B 1 91  ? -18.716 8.103  -35.159 1.00 23.88 ? 315  PRO B CB  1 
ATOM   3060 C  CG  . PRO B 1 91  ? -20.079 7.987  -34.510 1.00 22.56 ? 315  PRO B CG  1 
ATOM   3061 C  CD  . PRO B 1 91  ? -20.854 9.125  -35.073 1.00 25.85 ? 315  PRO B CD  1 
ATOM   3062 N  N   . THR B 1 92  ? -18.481 10.536 -37.624 1.00 27.15 ? 316  THR B N   1 
ATOM   3063 C  CA  . THR B 1 92  ? -17.810 10.997 -38.834 1.00 26.00 ? 316  THR B CA  1 
ATOM   3064 C  C   . THR B 1 92  ? -17.068 12.312 -38.627 1.00 28.33 ? 316  THR B C   1 
ATOM   3065 O  O   . THR B 1 92  ? -16.338 12.734 -39.528 1.00 30.30 ? 316  THR B O   1 
ATOM   3066 C  CB  . THR B 1 92  ? -18.804 11.169 -39.996 1.00 27.52 ? 316  THR B CB  1 
ATOM   3067 O  OG1 . THR B 1 92  ? -19.741 12.205 -39.685 1.00 24.43 ? 316  THR B OG1 1 
ATOM   3068 C  CG2 . THR B 1 92  ? -19.569 9.857  -40.291 1.00 22.92 ? 316  THR B CG2 1 
ATOM   3069 N  N   . ASP B 1 93  ? -17.237 12.965 -37.479 1.00 24.31 ? 317  ASP B N   1 
ATOM   3070 C  CA  . ASP B 1 93  ? -16.537 14.216 -37.211 1.00 28.17 ? 317  ASP B CA  1 
ATOM   3071 C  C   . ASP B 1 93  ? -15.025 14.023 -37.289 1.00 29.78 ? 317  ASP B C   1 
ATOM   3072 O  O   . ASP B 1 93  ? -14.495 12.958 -36.978 1.00 25.10 ? 317  ASP B O   1 
ATOM   3073 C  CB  . ASP B 1 93  ? -16.903 14.745 -35.829 1.00 27.47 ? 317  ASP B CB  1 
ATOM   3074 C  CG  . ASP B 1 93  ? -18.297 15.369 -35.779 1.00 29.61 ? 317  ASP B CG  1 
ATOM   3075 O  OD1 . ASP B 1 93  ? -18.857 15.721 -36.846 1.00 25.57 ? 317  ASP B OD1 1 
ATOM   3076 O  OD2 . ASP B 1 93  ? -18.819 15.517 -34.651 1.00 29.71 ? 317  ASP B OD2 1 
ATOM   3077 N  N   . ASP B 1 94  ? -14.323 15.079 -37.690 1.00 28.21 ? 318  ASP B N   1 
ATOM   3078 C  CA  . ASP B 1 94  ? -12.871 14.998 -37.801 1.00 32.92 ? 318  ASP B CA  1 
ATOM   3079 C  C   . ASP B 1 94  ? -12.183 15.263 -36.466 1.00 29.25 ? 318  ASP B C   1 
ATOM   3080 O  O   . ASP B 1 94  ? -11.267 16.090 -36.394 1.00 26.72 ? 318  ASP B O   1 
ATOM   3081 C  CB  . ASP B 1 94  ? -12.360 15.985 -38.852 1.00 38.20 ? 318  ASP B CB  1 
ATOM   3082 C  CG  . ASP B 1 94  ? -12.755 15.590 -40.265 1.00 45.68 ? 318  ASP B CG  1 
ATOM   3083 O  OD1 . ASP B 1 94  ? -12.941 14.375 -40.526 1.00 43.42 ? 318  ASP B OD1 1 
ATOM   3084 O  OD2 . ASP B 1 94  ? -12.878 16.500 -41.116 1.00 55.95 ? 318  ASP B OD2 1 
ATOM   3085 N  N   . THR B 1 95  ? -12.603 14.569 -35.413 1.00 25.92 ? 319  THR B N   1 
ATOM   3086 C  CA  . THR B 1 95  ? -12.041 14.713 -34.077 1.00 22.52 ? 319  THR B CA  1 
ATOM   3087 C  C   . THR B 1 95  ? -11.702 13.336 -33.524 1.00 23.03 ? 319  THR B C   1 
ATOM   3088 O  O   . THR B 1 95  ? -12.315 12.346 -33.930 1.00 23.08 ? 319  THR B O   1 
ATOM   3089 C  CB  . THR B 1 95  ? -13.030 15.414 -33.128 1.00 26.39 ? 319  THR B CB  1 
ATOM   3090 O  OG1 . THR B 1 95  ? -14.275 14.695 -33.107 1.00 23.19 ? 319  THR B OG1 1 
ATOM   3091 C  CG2 . THR B 1 95  ? -13.284 16.872 -33.556 1.00 25.09 ? 319  THR B CG2 1 
ATOM   3092 N  N   . PRO B 1 96  ? -10.740 13.239 -32.598 1.00 20.50 ? 320  PRO B N   1 
ATOM   3093 C  CA  . PRO B 1 96  ? -10.495 11.935 -31.950 1.00 21.84 ? 320  PRO B CA  1 
ATOM   3094 C  C   . PRO B 1 96  ? -11.732 11.380 -31.264 1.00 21.41 ? 320  PRO B C   1 
ATOM   3095 O  O   . PRO B 1 96  ? -11.979 10.169 -31.302 1.00 21.44 ? 320  PRO B O   1 
ATOM   3096 C  CB  . PRO B 1 96  ? -9.390  12.245 -30.929 1.00 20.20 ? 320  PRO B CB  1 
ATOM   3097 C  CG  . PRO B 1 96  ? -8.812  13.548 -31.337 1.00 21.08 ? 320  PRO B CG  1 
ATOM   3098 C  CD  . PRO B 1 96  ? -9.865  14.305 -32.069 1.00 21.31 ? 320  PRO B CD  1 
ATOM   3099 N  N   . GLY B 1 97  ? -12.521 12.259 -30.650 1.00 20.08 ? 321  GLY B N   1 
ATOM   3100 C  CA  . GLY B 1 97  ? -13.696 11.894 -29.897 1.00 19.06 ? 321  GLY B CA  1 
ATOM   3101 C  C   . GLY B 1 97  ? -14.558 13.118 -29.667 1.00 22.30 ? 321  GLY B C   1 
ATOM   3102 O  O   . GLY B 1 97  ? -14.306 14.189 -30.237 1.00 19.07 ? 321  GLY B O   1 
ATOM   3103 N  N   . PRO B 1 98  ? -15.595 12.993 -28.841 1.00 20.88 ? 322  PRO B N   1 
ATOM   3104 C  CA  . PRO B 1 98  ? -16.474 14.144 -28.607 1.00 17.93 ? 322  PRO B CA  1 
ATOM   3105 C  C   . PRO B 1 98  ? -15.736 15.253 -27.883 1.00 18.85 ? 322  PRO B C   1 
ATOM   3106 O  O   . PRO B 1 98  ? -14.848 15.011 -27.064 1.00 19.70 ? 322  PRO B O   1 
ATOM   3107 C  CB  . PRO B 1 98  ? -17.614 13.569 -27.750 1.00 21.67 ? 322  PRO B CB  1 
ATOM   3108 C  CG  . PRO B 1 98  ? -17.152 12.255 -27.264 1.00 21.10 ? 322  PRO B CG  1 
ATOM   3109 C  CD  . PRO B 1 98  ? -16.105 11.757 -28.225 1.00 19.74 ? 322  PRO B CD  1 
ATOM   3110 N  N   . LEU B 1 99  ? -16.097 16.489 -28.213 1.00 18.92 ? 323  LEU B N   1 
ATOM   3111 C  CA  . LEU B 1 99  ? -15.463 17.636 -27.572 1.00 18.96 ? 323  LEU B CA  1 
ATOM   3112 C  C   . LEU B 1 99  ? -15.617 17.550 -26.056 1.00 18.42 ? 323  LEU B C   1 
ATOM   3113 O  O   . LEU B 1 99  ? -16.664 17.146 -25.542 1.00 19.70 ? 323  LEU B O   1 
ATOM   3114 C  CB  . LEU B 1 99  ? -16.063 18.940 -28.095 1.00 20.69 ? 323  LEU B CB  1 
ATOM   3115 C  CG  . LEU B 1 99  ? -15.878 19.187 -29.592 1.00 20.66 ? 323  LEU B CG  1 
ATOM   3116 C  CD1 . LEU B 1 99  ? -16.353 20.604 -29.928 1.00 25.67 ? 323  LEU B CD1 1 
ATOM   3117 C  CD2 . LEU B 1 99  ? -14.426 18.980 -30.027 1.00 18.36 ? 323  LEU B CD2 1 
ATOM   3118 N  N   . GLY B 1 100 ? -14.549 17.908 -25.343 1.00 17.00 ? 324  GLY B N   1 
ATOM   3119 C  CA  . GLY B 1 100 ? -14.520 17.808 -23.902 1.00 16.09 ? 324  GLY B CA  1 
ATOM   3120 C  C   . GLY B 1 100 ? -14.223 16.429 -23.345 1.00 16.30 ? 324  GLY B C   1 
ATOM   3121 O  O   . GLY B 1 100 ? -14.069 16.298 -22.123 1.00 20.37 ? 324  GLY B O   1 
ATOM   3122 N  N   . CYS B 1 101 ? -14.146 15.398 -24.186 1.00 18.38 ? 325  CYS B N   1 
ATOM   3123 C  CA  . CYS B 1 101 ? -13.859 14.049 -23.703 1.00 19.35 ? 325  CYS B CA  1 
ATOM   3124 C  C   . CYS B 1 101 ? -12.515 14.014 -22.975 1.00 20.14 ? 325  CYS B C   1 
ATOM   3125 O  O   . CYS B 1 101 ? -11.554 14.662 -23.415 1.00 17.49 ? 325  CYS B O   1 
ATOM   3126 C  CB  . CYS B 1 101 ? -13.849 13.061 -24.871 1.00 19.35 ? 325  CYS B CB  1 
ATOM   3127 S  SG  . CYS B 1 101 ? -13.457 11.320 -24.450 1.00 23.69 ? 325  CYS B SG  1 
ATOM   3128 N  N   . PRO B 1 102 ? -12.412 13.283 -21.859 1.00 20.63 ? 326  PRO B N   1 
ATOM   3129 C  CA  . PRO B 1 102 ? -11.114 13.137 -21.177 1.00 18.39 ? 326  PRO B CA  1 
ATOM   3130 C  C   . PRO B 1 102 ? -10.024 12.708 -22.150 1.00 21.13 ? 326  PRO B C   1 
ATOM   3131 O  O   . PRO B 1 102 ? -10.271 11.926 -23.071 1.00 20.50 ? 326  PRO B O   1 
ATOM   3132 C  CB  . PRO B 1 102 ? -11.376 12.049 -20.129 1.00 20.63 ? 326  PRO B CB  1 
ATOM   3133 C  CG  . PRO B 1 102 ? -12.851 12.044 -19.910 1.00 22.33 ? 326  PRO B CG  1 
ATOM   3134 C  CD  . PRO B 1 102 ? -13.517 12.628 -21.135 1.00 16.22 ? 326  PRO B CD  1 
ATOM   3135 N  N   . ASP B 1 103 ? -8.808  13.238 -21.949 1.00 16.62 ? 327  ASP B N   1 
ATOM   3136 C  CA  . ASP B 1 103 ? -7.669  12.878 -22.787 1.00 18.70 ? 327  ASP B CA  1 
ATOM   3137 C  C   . ASP B 1 103 ? -6.612  12.092 -22.010 1.00 20.08 ? 327  ASP B C   1 
ATOM   3138 O  O   . ASP B 1 103 ? -5.425  12.130 -22.342 1.00 21.68 ? 327  ASP B O   1 
ATOM   3139 C  CB  . ASP B 1 103 ? -7.054  14.116 -23.451 1.00 15.93 ? 327  ASP B CB  1 
ATOM   3140 C  CG  . ASP B 1 103 ? -6.496  15.118 -22.462 1.00 19.42 ? 327  ASP B CG  1 
ATOM   3141 O  OD1 . ASP B 1 103 ? -6.540  14.880 -21.227 1.00 19.29 ? 327  ASP B OD1 1 
ATOM   3142 O  OD2 . ASP B 1 103 ? -5.993  16.162 -22.937 1.00 18.09 ? 327  ASP B OD2 1 
ATOM   3143 N  N   . PHE B 1 104 ? -7.040  11.349 -20.993 1.00 19.90 ? 328  PHE B N   1 
ATOM   3144 C  CA  . PHE B 1 104 ? -6.143  10.582 -20.140 1.00 19.74 ? 328  PHE B CA  1 
ATOM   3145 C  C   . PHE B 1 104 ? -6.850  9.296  -19.749 1.00 20.45 ? 328  PHE B C   1 
ATOM   3146 O  O   . PHE B 1 104 ? -8.076  9.198  -19.830 1.00 21.89 ? 328  PHE B O   1 
ATOM   3147 C  CB  . PHE B 1 104 ? -5.762  11.367 -18.878 1.00 19.39 ? 328  PHE B CB  1 
ATOM   3148 C  CG  . PHE B 1 104 ? -6.957  11.855 -18.091 1.00 22.81 ? 328  PHE B CG  1 
ATOM   3149 C  CD1 . PHE B 1 104 ? -7.561  11.044 -17.141 1.00 22.67 ? 328  PHE B CD1 1 
ATOM   3150 C  CD2 . PHE B 1 104 ? -7.485  13.119 -18.319 1.00 20.26 ? 328  PHE B CD2 1 
ATOM   3151 C  CE1 . PHE B 1 104 ? -8.648  11.487 -16.434 1.00 21.46 ? 328  PHE B CE1 1 
ATOM   3152 C  CE2 . PHE B 1 104 ? -8.581  13.563 -17.611 1.00 20.48 ? 328  PHE B CE2 1 
ATOM   3153 C  CZ  . PHE B 1 104 ? -9.156  12.752 -16.661 1.00 23.52 ? 328  PHE B CZ  1 
ATOM   3154 N  N   . THR B 1 105 ? -6.075  8.314  -19.307 1.00 19.66 ? 329  THR B N   1 
ATOM   3155 C  CA  . THR B 1 105 ? -6.630  7.061  -18.815 1.00 22.29 ? 329  THR B CA  1 
ATOM   3156 C  C   . THR B 1 105 ? -6.601  7.067  -17.289 1.00 23.63 ? 329  THR B C   1 
ATOM   3157 O  O   . THR B 1 105 ? -5.622  7.505  -16.678 1.00 23.17 ? 329  THR B O   1 
ATOM   3158 C  CB  . THR B 1 105 ? -5.852  5.852  -19.355 1.00 23.18 ? 329  THR B CB  1 
ATOM   3159 O  OG1 . THR B 1 105 ? -4.516  5.906  -18.875 1.00 29.30 ? 329  THR B OG1 1 
ATOM   3160 C  CG2 . THR B 1 105 ? -5.797  5.859  -20.871 1.00 20.07 ? 329  THR B CG2 1 
ATOM   3161 N  N   . GLY B 1 106 ? -7.686  6.605  -16.678 1.00 21.51 ? 330  GLY B N   1 
ATOM   3162 C  CA  . GLY B 1 106 ? -7.742  6.503  -15.233 1.00 22.17 ? 330  GLY B CA  1 
ATOM   3163 C  C   . GLY B 1 106 ? -9.168  6.278  -14.781 1.00 22.56 ? 330  GLY B C   1 
ATOM   3164 O  O   . GLY B 1 106 ? -10.088 6.185  -15.592 1.00 20.96 ? 330  GLY B O   1 
ATOM   3165 N  N   . LEU B 1 107 ? -9.339  6.209  -13.461 1.00 21.14 ? 331  LEU B N   1 
ATOM   3166 C  CA  . LEU B 1 107 ? -10.667 6.071  -12.865 1.00 20.01 ? 331  LEU B CA  1 
ATOM   3167 C  C   . LEU B 1 107 ? -11.203 7.470  -12.585 1.00 21.13 ? 331  LEU B C   1 
ATOM   3168 O  O   . LEU B 1 107 ? -10.909 8.072  -11.549 1.00 20.19 ? 331  LEU B O   1 
ATOM   3169 C  CB  . LEU B 1 107 ? -10.616 5.225  -11.600 1.00 20.83 ? 331  LEU B CB  1 
ATOM   3170 C  CG  . LEU B 1 107 ? -10.093 3.799  -11.780 1.00 32.09 ? 331  LEU B CG  1 
ATOM   3171 C  CD1 . LEU B 1 107 ? -10.275 3.018  -10.494 1.00 29.09 ? 331  LEU B CD1 1 
ATOM   3172 C  CD2 . LEU B 1 107 ? -10.805 3.125  -12.941 1.00 28.39 ? 331  LEU B CD2 1 
ATOM   3173 N  N   . LEU B 1 108 ? -11.975 7.995  -13.519 1.00 21.07 ? 332  LEU B N   1 
ATOM   3174 C  CA  . LEU B 1 108 ? -12.545 9.325  -13.366 1.00 19.56 ? 332  LEU B CA  1 
ATOM   3175 C  C   . LEU B 1 108 ? -13.685 9.265  -12.354 1.00 20.67 ? 332  LEU B C   1 
ATOM   3176 O  O   . LEU B 1 108 ? -14.638 8.505  -12.534 1.00 18.06 ? 332  LEU B O   1 
ATOM   3177 C  CB  . LEU B 1 108 ? -13.032 9.823  -14.717 1.00 18.52 ? 332  LEU B CB  1 
ATOM   3178 C  CG  . LEU B 1 108 ? -13.696 11.196 -14.805 1.00 22.01 ? 332  LEU B CG  1 
ATOM   3179 C  CD1 . LEU B 1 108 ? -12.786 12.295 -14.279 1.00 20.10 ? 332  LEU B CD1 1 
ATOM   3180 C  CD2 . LEU B 1 108 ? -14.064 11.463 -16.244 1.00 19.57 ? 332  LEU B CD2 1 
ATOM   3181 N  N   . TYR B 1 109 ? -13.580 10.045 -11.285 1.00 21.23 ? 333  TYR B N   1 
ATOM   3182 C  CA  . TYR B 1 109 ? -14.573 10.067 -10.220 1.00 21.18 ? 333  TYR B CA  1 
ATOM   3183 C  C   . TYR B 1 109 ? -15.472 11.285 -10.379 1.00 19.50 ? 333  TYR B C   1 
ATOM   3184 O  O   . TYR B 1 109 ? -15.003 12.372 -10.728 1.00 16.84 ? 333  TYR B O   1 
ATOM   3185 C  CB  . TYR B 1 109 ? -13.889 10.102 -8.855  1.00 23.90 ? 333  TYR B CB  1 
ATOM   3186 C  CG  . TYR B 1 109 ? -14.794 10.377 -7.682  1.00 25.90 ? 333  TYR B CG  1 
ATOM   3187 C  CD1 . TYR B 1 109 ? -15.535 9.357  -7.095  1.00 25.63 ? 333  TYR B CD1 1 
ATOM   3188 C  CD2 . TYR B 1 109 ? -14.871 11.651 -7.128  1.00 23.88 ? 333  TYR B CD2 1 
ATOM   3189 C  CE1 . TYR B 1 109 ? -16.350 9.602  -6.001  1.00 29.59 ? 333  TYR B CE1 1 
ATOM   3190 C  CE2 . TYR B 1 109 ? -15.682 11.907 -6.027  1.00 28.83 ? 333  TYR B CE2 1 
ATOM   3191 C  CZ  . TYR B 1 109 ? -16.417 10.880 -5.471  1.00 30.51 ? 333  TYR B CZ  1 
ATOM   3192 O  OH  . TYR B 1 109 ? -17.226 11.135 -4.378  1.00 44.08 ? 333  TYR B OH  1 
ATOM   3193 N  N   . GLY B 1 110 ? -16.767 11.093 -10.135 1.00 17.89 ? 334  GLY B N   1 
ATOM   3194 C  CA  . GLY B 1 110 ? -17.704 12.193 -10.238 1.00 17.46 ? 334  GLY B CA  1 
ATOM   3195 C  C   . GLY B 1 110 ? -19.088 11.828 -9.756  1.00 19.38 ? 334  GLY B C   1 
ATOM   3196 O  O   . GLY B 1 110 ? -19.249 10.928 -8.922  1.00 21.03 ? 334  GLY B O   1 
ATOM   3197 N  N   . VAL B 1 111 ? -20.102 12.519 -10.266 1.00 17.33 ? 335  VAL B N   1 
ATOM   3198 C  CA  . VAL B 1 111 ? -21.481 12.255 -9.886  1.00 18.12 ? 335  VAL B CA  1 
ATOM   3199 C  C   . VAL B 1 111 ? -22.321 12.148 -11.149 1.00 21.49 ? 335  VAL B C   1 
ATOM   3200 O  O   . VAL B 1 111 ? -22.240 13.010 -12.031 1.00 19.21 ? 335  VAL B O   1 
ATOM   3201 C  CB  . VAL B 1 111 ? -22.024 13.337 -8.936  1.00 18.08 ? 335  VAL B CB  1 
ATOM   3202 C  CG1 . VAL B 1 111 ? -23.557 13.336 -8.912  1.00 18.02 ? 335  VAL B CG1 1 
ATOM   3203 C  CG2 . VAL B 1 111 ? -21.478 13.093 -7.547  1.00 18.08 ? 335  VAL B CG2 1 
ATOM   3204 N  N   . ALA B 1 112 ? -23.094 11.066 -11.246 1.00 19.11 ? 336  ALA B N   1 
ATOM   3205 C  CA  . ALA B 1 112 ? -24.063 10.870 -12.309 1.00 18.06 ? 336  ALA B CA  1 
ATOM   3206 C  C   . ALA B 1 112 ? -25.421 11.331 -11.794 1.00 20.75 ? 336  ALA B C   1 
ATOM   3207 O  O   . ALA B 1 112 ? -25.899 10.849 -10.757 1.00 19.16 ? 336  ALA B O   1 
ATOM   3208 C  CB  . ALA B 1 112 ? -24.103 9.404  -12.743 1.00 21.34 ? 336  ALA B CB  1 
ATOM   3209 N  N   . SER B 1 113 ? -26.018 12.291 -12.489 1.00 18.03 ? 337  SER B N   1 
ATOM   3210 C  CA  . SER B 1 113 ? -27.327 12.799 -12.126 1.00 19.18 ? 337  SER B CA  1 
ATOM   3211 C  C   . SER B 1 113 ? -28.309 12.581 -13.267 1.00 21.93 ? 337  SER B C   1 
ATOM   3212 O  O   . SER B 1 113 ? -27.930 12.495 -14.440 1.00 19.64 ? 337  SER B O   1 
ATOM   3213 C  CB  . SER B 1 113 ? -27.271 14.291 -11.777 1.00 18.01 ? 337  SER B CB  1 
ATOM   3214 O  OG  . SER B 1 113 ? -26.719 15.028 -12.856 1.00 18.75 ? 337  SER B OG  1 
ATOM   3215 N  N   . GLN B 1 114 ? -29.588 12.516 -12.893 1.00 20.73 ? 338  GLN B N   1 
ATOM   3216 C  CA  . GLN B 1 114 ? -30.694 12.382 -13.821 1.00 22.05 ? 338  GLN B CA  1 
ATOM   3217 C  C   . GLN B 1 114 ? -31.788 13.374 -13.463 1.00 22.42 ? 338  GLN B C   1 
ATOM   3218 O  O   . GLN B 1 114 ? -31.982 13.718 -12.294 1.00 22.76 ? 338  GLN B O   1 
ATOM   3219 C  CB  . GLN B 1 114 ? -31.297 10.964 -13.799 1.00 19.71 ? 338  GLN B CB  1 
ATOM   3220 C  CG  . GLN B 1 114 ? -30.357 9.862  -14.257 1.00 21.16 ? 338  GLN B CG  1 
ATOM   3221 C  CD  . GLN B 1 114 ? -31.066 8.528  -14.369 1.00 22.23 ? 338  GLN B CD  1 
ATOM   3222 O  OE1 . GLN B 1 114 ? -31.894 8.189  -13.526 1.00 26.75 ? 338  GLN B OE1 1 
ATOM   3223 N  NE2 . GLN B 1 114 ? -30.757 7.769  -15.423 1.00 22.57 ? 338  GLN B NE2 1 
ATOM   3224 N  N   . ARG B 1 115 ? -32.513 13.818 -14.483 1.00 21.23 ? 339  ARG B N   1 
ATOM   3225 C  CA  . ARG B 1 115 ? -33.777 14.521 -14.291 1.00 26.88 ? 339  ARG B CA  1 
ATOM   3226 C  C   . ARG B 1 115 ? -34.813 13.846 -15.175 1.00 23.32 ? 339  ARG B C   1 
ATOM   3227 O  O   . ARG B 1 115 ? -34.638 13.782 -16.395 1.00 25.27 ? 339  ARG B O   1 
ATOM   3228 C  CB  . ARG B 1 115 ? -33.664 16.013 -14.629 1.00 21.15 ? 339  ARG B CB  1 
ATOM   3229 C  CG  . ARG B 1 115 ? -35.011 16.754 -14.549 1.00 25.25 ? 339  ARG B CG  1 
ATOM   3230 C  CD  . ARG B 1 115 ? -34.862 18.284 -14.595 1.00 25.70 ? 339  ARG B CD  1 
ATOM   3231 N  NE  . ARG B 1 115 ? -34.417 18.844 -13.321 1.00 24.24 ? 339  ARG B NE  1 
ATOM   3232 C  CZ  . ARG B 1 115 ? -33.212 19.362 -13.105 1.00 23.77 ? 339  ARG B CZ  1 
ATOM   3233 N  NH1 . ARG B 1 115 ? -32.306 19.438 -14.068 1.00 22.88 ? 339  ARG B NH1 1 
ATOM   3234 N  NH2 . ARG B 1 115 ? -32.917 19.836 -11.900 1.00 23.00 ? 339  ARG B NH2 1 
ATOM   3235 N  N   . GLY B 1 116 ? -35.879 13.342 -14.566 1.00 25.91 ? 340  GLY B N   1 
ATOM   3236 C  CA  . GLY B 1 116 ? -36.907 12.634 -15.291 1.00 26.20 ? 340  GLY B CA  1 
ATOM   3237 C  C   . GLY B 1 116 ? -37.258 11.313 -14.637 1.00 27.05 ? 340  GLY B C   1 
ATOM   3238 O  O   . GLY B 1 116 ? -36.448 10.721 -13.920 1.00 27.49 ? 340  GLY B O   1 
ATOM   3239 N  N   . PRO B 1 117 ? -38.490 10.828 -14.846 1.00 30.14 ? 341  PRO B N   1 
ATOM   3240 C  CA  . PRO B 1 117 ? -39.602 11.447 -15.586 1.00 31.26 ? 341  PRO B CA  1 
ATOM   3241 C  C   . PRO B 1 117 ? -40.090 12.744 -14.930 1.00 33.36 ? 341  PRO B C   1 
ATOM   3242 O  O   . PRO B 1 117 ? -40.041 12.899 -13.706 1.00 30.22 ? 341  PRO B O   1 
ATOM   3243 C  CB  . PRO B 1 117 ? -40.679 10.345 -15.571 1.00 32.80 ? 341  PRO B CB  1 
ATOM   3244 C  CG  . PRO B 1 117 ? -40.379 9.547  -14.339 1.00 31.95 ? 341  PRO B CG  1 
ATOM   3245 C  CD  . PRO B 1 117 ? -38.876 9.529  -14.264 1.00 26.61 ? 341  PRO B CD  1 
ATOM   3246 N  N   . GLY B 1 118 ? -40.548 13.701 -15.736 1.00 33.29 ? 342  GLY B N   1 
ATOM   3247 C  CA  . GLY B 1 118 ? -40.954 14.978 -15.188 1.00 33.31 ? 342  GLY B CA  1 
ATOM   3248 C  C   . GLY B 1 118 ? -39.771 15.682 -14.560 1.00 31.48 ? 342  GLY B C   1 
ATOM   3249 O  O   . GLY B 1 118 ? -38.665 15.691 -15.106 1.00 29.58 ? 342  GLY B O   1 
ATOM   3250 N  N   . ASP B 1 119 ? -39.992 16.247 -13.374 1.00 27.51 ? 343  ASP B N   1 
ATOM   3251 C  CA  . ASP B 1 119 ? -38.949 16.943 -12.634 1.00 28.34 ? 343  ASP B CA  1 
ATOM   3252 C  C   . ASP B 1 119 ? -38.370 16.107 -11.493 1.00 29.57 ? 343  ASP B C   1 
ATOM   3253 O  O   . ASP B 1 119 ? -37.698 16.654 -10.612 1.00 26.86 ? 343  ASP B O   1 
ATOM   3254 C  CB  . ASP B 1 119 ? -39.486 18.268 -12.097 1.00 29.97 ? 343  ASP B CB  1 
ATOM   3255 C  CG  . ASP B 1 119 ? -40.643 18.083 -11.138 1.00 35.81 ? 343  ASP B CG  1 
ATOM   3256 O  OD1 . ASP B 1 119 ? -41.241 16.983 -11.116 1.00 38.97 ? 343  ASP B OD1 1 
ATOM   3257 O  OD2 . ASP B 1 119 ? -40.965 19.047 -10.410 1.00 40.99 ? 343  ASP B OD2 1 
ATOM   3258 N  N   . ALA B 1 120 ? -38.613 14.800 -11.482 1.00 27.41 ? 344  ALA B N   1 
ATOM   3259 C  CA  . ALA B 1 120 ? -37.964 13.941 -10.497 1.00 25.86 ? 344  ALA B CA  1 
ATOM   3260 C  C   . ALA B 1 120 ? -36.470 13.895 -10.780 1.00 25.51 ? 344  ALA B C   1 
ATOM   3261 O  O   . ALA B 1 120 ? -36.053 13.759 -11.934 1.00 24.68 ? 344  ALA B O   1 
ATOM   3262 C  CB  . ALA B 1 120 ? -38.557 12.535 -10.533 1.00 25.25 ? 344  ALA B CB  1 
ATOM   3263 N  N   . THR B 1 121 ? -35.657 14.041 -9.737  1.00 22.20 ? 345  THR B N   1 
ATOM   3264 C  CA  . THR B 1 121 ? -34.213 14.050 -9.914  1.00 24.00 ? 345  THR B CA  1 
ATOM   3265 C  C   . THR B 1 121 ? -33.567 13.057 -8.959  1.00 25.95 ? 345  THR B C   1 
ATOM   3266 O  O   . THR B 1 121 ? -34.164 12.629 -7.969  1.00 28.86 ? 345  THR B O   1 
ATOM   3267 C  CB  . THR B 1 121 ? -33.596 15.461 -9.713  1.00 22.45 ? 345  THR B CB  1 
ATOM   3268 O  OG1 . THR B 1 121 ? -33.651 15.855 -8.334  1.00 23.55 ? 345  THR B OG1 1 
ATOM   3269 C  CG2 . THR B 1 121 ? -34.302 16.494 -10.554 1.00 23.29 ? 345  THR B CG2 1 
ATOM   3270 N  N   . ARG B 1 122 ? -32.332 12.682 -9.284  1.00 21.16 ? 346  ARG B N   1 
ATOM   3271 C  CA  . ARG B 1 122 ? -31.541 11.804 -8.436  1.00 23.22 ? 346  ARG B CA  1 
ATOM   3272 C  C   . ARG B 1 122 ? -30.091 11.934 -8.869  1.00 20.88 ? 346  ARG B C   1 
ATOM   3273 O  O   . ARG B 1 122 ? -29.805 12.215 -10.040 1.00 22.20 ? 346  ARG B O   1 
ATOM   3274 C  CB  . ARG B 1 122 ? -32.009 10.345 -8.525  1.00 23.24 ? 346  ARG B CB  1 
ATOM   3275 C  CG  . ARG B 1 122 ? -31.793 9.702  -9.886  1.00 22.01 ? 346  ARG B CG  1 
ATOM   3276 C  CD  . ARG B 1 122 ? -32.727 8.502  -10.071 1.00 23.85 ? 346  ARG B CD  1 
ATOM   3277 N  NE  . ARG B 1 122 ? -34.120 8.926  -10.007 1.00 27.27 ? 346  ARG B NE  1 
ATOM   3278 C  CZ  . ARG B 1 122 ? -34.786 9.430  -11.038 1.00 29.07 ? 346  ARG B CZ  1 
ATOM   3279 N  NH1 . ARG B 1 122 ? -34.237 9.515  -12.245 1.00 22.84 ? 346  ARG B NH1 1 
ATOM   3280 N  NH2 . ARG B 1 122 ? -36.029 9.862  -10.857 1.00 25.17 ? 346  ARG B NH2 1 
ATOM   3281 N  N   . ALA B 1 123 ? -29.180 11.761 -7.916  1.00 20.05 ? 347  ALA B N   1 
ATOM   3282 C  CA  . ALA B 1 123 ? -27.766 11.880 -8.242  1.00 19.53 ? 347  ALA B CA  1 
ATOM   3283 C  C   . ALA B 1 123 ? -26.944 11.071 -7.251  1.00 21.00 ? 347  ALA B C   1 
ATOM   3284 O  O   . ALA B 1 123 ? -27.260 11.035 -6.060  1.00 20.24 ? 347  ALA B O   1 
ATOM   3285 C  CB  . ALA B 1 123 ? -27.310 13.339 -8.253  1.00 20.74 ? 347  ALA B CB  1 
ATOM   3286 N  N   . HIS B 1 124 ? -25.889 10.428 -7.755  1.00 19.61 ? 348  HIS B N   1 
ATOM   3287 C  CA  . HIS B 1 124 ? -25.062 9.552  -6.935  1.00 23.86 ? 348  HIS B CA  1 
ATOM   3288 C  C   . HIS B 1 124 ? -23.654 9.517  -7.500  1.00 23.30 ? 348  HIS B C   1 
ATOM   3289 O  O   . HIS B 1 124 ? -23.446 9.717  -8.699  1.00 20.53 ? 348  HIS B O   1 
ATOM   3290 C  CB  . HIS B 1 124 ? -25.626 8.130  -6.876  1.00 20.45 ? 348  HIS B CB  1 
ATOM   3291 C  CG  . HIS B 1 124 ? -27.041 8.072  -6.409  1.00 22.20 ? 348  HIS B CG  1 
ATOM   3292 N  ND1 . HIS B 1 124 ? -27.390 8.221  -5.084  1.00 27.52 ? 348  HIS B ND1 1 
ATOM   3293 C  CD2 . HIS B 1 124 ? -28.202 7.938  -7.092  1.00 22.12 ? 348  HIS B CD2 1 
ATOM   3294 C  CE1 . HIS B 1 124 ? -28.704 8.160  -4.968  1.00 23.99 ? 348  HIS B CE1 1 
ATOM   3295 N  NE2 . HIS B 1 124 ? -29.221 7.983  -6.170  1.00 24.60 ? 348  HIS B NE2 1 
ATOM   3296 N  N   . GLU B 1 125 ? -22.692 9.242  -6.625  1.00 24.81 ? 349  GLU B N   1 
ATOM   3297 C  CA  . GLU B 1 125 ? -21.307 9.180  -7.058  1.00 25.31 ? 349  GLU B CA  1 
ATOM   3298 C  C   . GLU B 1 125 ? -21.120 8.049  -8.065  1.00 24.00 ? 349  GLU B C   1 
ATOM   3299 O  O   . GLU B 1 125 ? -21.794 7.014  -8.012  1.00 25.38 ? 349  GLU B O   1 
ATOM   3300 C  CB  . GLU B 1 125 ? -20.380 9.006  -5.853  1.00 26.91 ? 349  GLU B CB  1 
ATOM   3301 C  CG  . GLU B 1 125 ? -20.559 7.712  -5.108  1.00 38.24 ? 349  GLU B CG  1 
ATOM   3302 C  CD  . GLU B 1 125 ? -19.578 7.573  -3.959  1.00 48.07 ? 349  GLU B CD  1 
ATOM   3303 O  OE1 . GLU B 1 125 ? -19.114 8.630  -3.440  1.00 46.13 ? 349  GLU B OE1 1 
ATOM   3304 O  OE2 . GLU B 1 125 ? -19.276 6.406  -3.592  1.00 42.87 ? 349  GLU B OE2 1 
ATOM   3305 N  N   . ALA B 1 126 ? -20.218 8.274  -9.014  1.00 19.78 ? 350  ALA B N   1 
ATOM   3306 C  CA  . ALA B 1 126 ? -20.030 7.356  -10.128 1.00 23.33 ? 350  ALA B CA  1 
ATOM   3307 C  C   . ALA B 1 126 ? -18.569 7.382  -10.551 1.00 24.35 ? 350  ALA B C   1 
ATOM   3308 O  O   . ALA B 1 126 ? -17.836 8.342  -10.274 1.00 19.94 ? 350  ALA B O   1 
ATOM   3309 C  CB  . ALA B 1 126 ? -20.933 7.712  -11.319 1.00 21.29 ? 350  ALA B CB  1 
ATOM   3310 N  N   . ARG B 1 127 ? -18.156 6.315  -11.237 1.00 21.11 ? 351  ARG B N   1 
ATOM   3311 C  CA  A ARG B 1 127 ? -16.788 6.176  -11.720 0.47 21.63 ? 351  ARG B CA  1 
ATOM   3312 C  CA  B ARG B 1 127 ? -16.793 6.185  -11.720 0.53 22.30 ? 351  ARG B CA  1 
ATOM   3313 C  C   . ARG B 1 127 ? -16.803 5.717  -13.172 1.00 22.04 ? 351  ARG B C   1 
ATOM   3314 O  O   . ARG B 1 127 ? -17.535 4.789  -13.534 1.00 21.45 ? 351  ARG B O   1 
ATOM   3315 C  CB  A ARG B 1 127 ? -15.984 5.192  -10.854 0.47 24.61 ? 351  ARG B CB  1 
ATOM   3316 C  CB  B ARG B 1 127 ? -16.018 5.232  -10.799 0.53 24.62 ? 351  ARG B CB  1 
ATOM   3317 C  CG  A ARG B 1 127 ? -16.568 3.792  -10.807 0.47 25.38 ? 351  ARG B CG  1 
ATOM   3318 C  CG  B ARG B 1 127 ? -15.040 4.296  -11.450 0.53 25.15 ? 351  ARG B CG  1 
ATOM   3319 C  CD  A ARG B 1 127 ? -15.802 2.845  -9.870  0.47 28.18 ? 351  ARG B CD  1 
ATOM   3320 C  CD  B ARG B 1 127 ? -14.064 3.761  -10.401 0.53 27.55 ? 351  ARG B CD  1 
ATOM   3321 N  NE  A ARG B 1 127 ? -14.496 2.430  -10.374 0.47 27.45 ? 351  ARG B NE  1 
ATOM   3322 N  NE  B ARG B 1 127 ? -14.625 3.804  -9.053  0.53 29.67 ? 351  ARG B NE  1 
ATOM   3323 C  CZ  A ARG B 1 127 ? -14.307 1.596  -11.388 0.47 26.38 ? 351  ARG B CZ  1 
ATOM   3324 C  CZ  B ARG B 1 127 ? -14.984 2.735  -8.354  0.53 30.59 ? 351  ARG B CZ  1 
ATOM   3325 N  NH1 A ARG B 1 127 ? -15.315 1.167  -12.128 0.47 28.71 ? 351  ARG B NH1 1 
ATOM   3326 N  NH1 B ARG B 1 127 ? -14.839 1.512  -8.838  0.53 31.55 ? 351  ARG B NH1 1 
ATOM   3327 N  NH2 A ARG B 1 127 ? -13.078 1.177  -11.664 0.47 27.44 ? 351  ARG B NH2 1 
ATOM   3328 N  NH2 B ARG B 1 127 ? -15.499 2.899  -7.137  0.53 32.18 ? 351  ARG B NH2 1 
ATOM   3329 N  N   . ILE B 1 128 ? -16.002 6.372  -14.005 1.00 20.60 ? 352  ILE B N   1 
ATOM   3330 C  CA  . ILE B 1 128 ? -15.858 6.015  -15.414 1.00 17.70 ? 352  ILE B CA  1 
ATOM   3331 C  C   . ILE B 1 128 ? -14.400 5.653  -15.644 1.00 21.33 ? 352  ILE B C   1 
ATOM   3332 O  O   . ILE B 1 128 ? -13.497 6.436  -15.318 1.00 17.58 ? 352  ILE B O   1 
ATOM   3333 C  CB  . ILE B 1 128 ? -16.298 7.154  -16.344 1.00 18.68 ? 352  ILE B CB  1 
ATOM   3334 C  CG1 . ILE B 1 128 ? -17.796 7.438  -16.186 1.00 18.73 ? 352  ILE B CG1 1 
ATOM   3335 C  CG2 . ILE B 1 128 ? -15.951 6.822  -17.795 1.00 18.13 ? 352  ILE B CG2 1 
ATOM   3336 C  CD1 . ILE B 1 128 ? -18.276 8.666  -17.005 1.00 18.14 ? 352  ILE B CD1 1 
ATOM   3337 N  N   . ASP B 1 129 ? -14.169 4.458  -16.177 1.00 19.43 ? 353  ASP B N   1 
ATOM   3338 C  CA  . ASP B 1 129 ? -12.817 3.946  -16.405 1.00 19.67 ? 353  ASP B CA  1 
ATOM   3339 C  C   . ASP B 1 129 ? -12.431 4.287  -17.833 1.00 22.00 ? 353  ASP B C   1 
ATOM   3340 O  O   . ASP B 1 129 ? -12.740 3.543  -18.768 1.00 20.31 ? 353  ASP B O   1 
ATOM   3341 C  CB  . ASP B 1 129 ? -12.766 2.439  -16.173 1.00 22.55 ? 353  ASP B CB  1 
ATOM   3342 C  CG  . ASP B 1 129 ? -11.361 1.868  -16.322 1.00 27.15 ? 353  ASP B CG  1 
ATOM   3343 O  OD1 . ASP B 1 129 ? -10.414 2.623  -16.677 1.00 27.09 ? 353  ASP B OD1 1 
ATOM   3344 O  OD2 . ASP B 1 129 ? -11.203 0.660  -16.050 1.00 25.08 ? 353  ASP B OD2 1 
ATOM   3345 N  N   . THR B 1 130 ? -11.728 5.411  -18.011 1.00 17.41 ? 354  THR B N   1 
ATOM   3346 C  CA  . THR B 1 130 ? -11.380 5.790  -19.370 1.00 18.45 ? 354  THR B CA  1 
ATOM   3347 C  C   . THR B 1 130 ? -10.301 4.902  -19.965 1.00 20.03 ? 354  THR B C   1 
ATOM   3348 O  O   . THR B 1 130 ? -9.929  5.116  -21.124 1.00 19.43 ? 354  THR B O   1 
ATOM   3349 C  CB  . THR B 1 130 ? -10.933 7.244  -19.429 1.00 16.90 ? 354  THR B CB  1 
ATOM   3350 O  OG1 . THR B 1 130 ? -9.720  7.402  -18.678 1.00 18.53 ? 354  THR B OG1 1 
ATOM   3351 C  CG2 . THR B 1 130 ? -12.042 8.155  -18.847 1.00 17.73 ? 354  THR B CG2 1 
ATOM   3352 N  N   . GLY B 1 131 ? -9.798  3.925  -19.210 1.00 19.24 ? 355  GLY B N   1 
ATOM   3353 C  CA  . GLY B 1 131 ? -8.877  2.935  -19.718 1.00 20.17 ? 355  GLY B CA  1 
ATOM   3354 C  C   . GLY B 1 131 ? -9.508  1.607  -20.079 1.00 25.82 ? 355  GLY B C   1 
ATOM   3355 O  O   . GLY B 1 131 ? -8.812  0.733  -20.603 1.00 21.70 ? 355  GLY B O   1 
ATOM   3356 N  N   . SER B 1 132 ? -10.803 1.423  -19.827 1.00 23.38 ? 356  SER B N   1 
ATOM   3357 C  CA  . SER B 1 132 ? -11.414 0.111  -20.007 1.00 21.44 ? 356  SER B CA  1 
ATOM   3358 C  C   . SER B 1 132 ? -11.637 -0.198 -21.481 1.00 22.55 ? 356  SER B C   1 
ATOM   3359 O  O   . SER B 1 132 ? -11.784 0.703  -22.317 1.00 21.65 ? 356  SER B O   1 
ATOM   3360 C  CB  . SER B 1 132 ? -12.740 0.018  -19.259 1.00 19.86 ? 356  SER B CB  1 
ATOM   3361 O  OG  . SER B 1 132 ? -13.568 1.098  -19.611 1.00 22.54 ? 356  SER B OG  1 
ATOM   3362 N  N   . ASP B 1 133 ? -11.688 -1.501 -21.783 1.00 22.31 ? 357  ASP B N   1 
ATOM   3363 C  CA  . ASP B 1 133 ? -11.826 -1.963 -23.161 1.00 21.63 ? 357  ASP B CA  1 
ATOM   3364 C  C   . ASP B 1 133 ? -13.027 -1.347 -23.863 1.00 20.36 ? 357  ASP B C   1 
ATOM   3365 O  O   . ASP B 1 133 ? -12.949 -1.008 -25.046 1.00 19.90 ? 357  ASP B O   1 
ATOM   3366 C  CB  . ASP B 1 133 ? -11.928 -3.491 -23.188 1.00 23.52 ? 357  ASP B CB  1 
ATOM   3367 C  CG  . ASP B 1 133 ? -10.584 -4.149 -23.067 1.00 26.92 ? 357  ASP B CG  1 
ATOM   3368 O  OD1 . ASP B 1 133 ? -9.570  -3.420 -23.179 1.00 28.54 ? 357  ASP B OD1 1 
ATOM   3369 O  OD2 . ASP B 1 133 ? -10.538 -5.380 -22.862 1.00 33.94 ? 357  ASP B OD2 1 
ATOM   3370 N  N   . THR B 1 134 ? -14.144 -1.186 -23.153 1.00 21.58 ? 358  THR B N   1 
ATOM   3371 C  CA  . THR B 1 134 ? -15.377 -0.734 -23.784 1.00 19.50 ? 358  THR B CA  1 
ATOM   3372 C  C   . THR B 1 134 ? -15.583 0.772  -23.698 1.00 20.58 ? 358  THR B C   1 
ATOM   3373 O  O   . THR B 1 134 ? -16.607 1.267  -24.181 1.00 18.79 ? 358  THR B O   1 
ATOM   3374 C  CB  . THR B 1 134 ? -16.587 -1.434 -23.167 1.00 21.14 ? 358  THR B CB  1 
ATOM   3375 O  OG1 . THR B 1 134 ? -16.650 -1.132 -21.767 1.00 21.83 ? 358  THR B OG1 1 
ATOM   3376 C  CG2 . THR B 1 134 ? -16.512 -2.954 -23.382 1.00 23.31 ? 358  THR B CG2 1 
ATOM   3377 N  N   . PHE B 1 135 ? -14.661 1.512  -23.092 1.00 18.52 ? 359  PHE B N   1 
ATOM   3378 C  CA  . PHE B 1 135 ? -14.754 2.969  -23.123 1.00 20.41 ? 359  PHE B CA  1 
ATOM   3379 C  C   . PHE B 1 135 ? -14.540 3.431  -24.563 1.00 17.91 ? 359  PHE B C   1 
ATOM   3380 O  O   . PHE B 1 135 ? -13.430 3.324  -25.096 1.00 18.03 ? 359  PHE B O   1 
ATOM   3381 C  CB  . PHE B 1 135 ? -13.731 3.589  -22.174 1.00 17.79 ? 359  PHE B CB  1 
ATOM   3382 C  CG  . PHE B 1 135 ? -13.734 5.100  -22.190 1.00 17.94 ? 359  PHE B CG  1 
ATOM   3383 C  CD1 . PHE B 1 135 ? -14.747 5.814  -21.547 1.00 18.39 ? 359  PHE B CD1 1 
ATOM   3384 C  CD2 . PHE B 1 135 ? -12.740 5.800  -22.849 1.00 17.11 ? 359  PHE B CD2 1 
ATOM   3385 C  CE1 . PHE B 1 135 ? -14.769 7.210  -21.560 1.00 17.39 ? 359  PHE B CE1 1 
ATOM   3386 C  CE2 . PHE B 1 135 ? -12.739 7.183  -22.865 1.00 16.74 ? 359  PHE B CE2 1 
ATOM   3387 C  CZ  . PHE B 1 135 ? -13.754 7.900  -22.225 1.00 17.10 ? 359  PHE B CZ  1 
ATOM   3388 N  N   . ALA B 1 136 ? -15.606 3.895  -25.216 1.00 17.87 ? 360  ALA B N   1 
ATOM   3389 C  CA  . ALA B 1 136 ? -15.568 4.208  -26.649 1.00 17.86 ? 360  ALA B CA  1 
ATOM   3390 C  C   . ALA B 1 136 ? -16.394 5.457  -26.926 1.00 17.58 ? 360  ALA B C   1 
ATOM   3391 O  O   . ALA B 1 136 ? -17.392 5.421  -27.659 1.00 17.76 ? 360  ALA B O   1 
ATOM   3392 C  CB  . ALA B 1 136 ? -16.064 3.025  -27.484 1.00 18.34 ? 360  ALA B CB  1 
ATOM   3393 N  N   . PRO B 1 137 ? -15.977 6.597  -26.374 1.00 17.19 ? 361  PRO B N   1 
ATOM   3394 C  CA  . PRO B 1 137 ? -16.772 7.819  -26.531 1.00 17.94 ? 361  PRO B CA  1 
ATOM   3395 C  C   . PRO B 1 137 ? -16.890 8.300  -27.972 1.00 19.50 ? 361  PRO B C   1 
ATOM   3396 O  O   . PRO B 1 137 ? -17.847 9.022  -28.278 1.00 18.64 ? 361  PRO B O   1 
ATOM   3397 C  CB  . PRO B 1 137 ? -16.023 8.838  -25.653 1.00 16.56 ? 361  PRO B CB  1 
ATOM   3398 C  CG  . PRO B 1 137 ? -14.602 8.342  -25.615 1.00 16.60 ? 361  PRO B CG  1 
ATOM   3399 C  CD  . PRO B 1 137 ? -14.743 6.828  -25.599 1.00 16.99 ? 361  PRO B CD  1 
ATOM   3400 N  N   . LYS B 1 138 ? -15.950 7.943  -28.856 1.00 19.88 ? 362  LYS B N   1 
ATOM   3401 C  CA  . LYS B 1 138 ? -16.044 8.376  -30.250 1.00 18.30 ? 362  LYS B CA  1 
ATOM   3402 C  C   . LYS B 1 138 ? -17.341 7.923  -30.892 1.00 19.06 ? 362  LYS B C   1 
ATOM   3403 O  O   . LYS B 1 138 ? -17.892 8.627  -31.747 1.00 19.67 ? 362  LYS B O   1 
ATOM   3404 C  CB  . LYS B 1 138 ? -14.868 7.857  -31.078 1.00 17.38 ? 362  LYS B CB  1 
ATOM   3405 C  CG  . LYS B 1 138 ? -14.920 8.396  -32.510 1.00 20.92 ? 362  LYS B CG  1 
ATOM   3406 C  CD  . LYS B 1 138 ? -13.800 7.914  -33.409 1.00 28.61 ? 362  LYS B CD  1 
ATOM   3407 C  CE  . LYS B 1 138 ? -13.412 9.020  -34.419 1.00 32.83 ? 362  LYS B CE  1 
ATOM   3408 N  NZ  . LYS B 1 138 ? -14.495 10.060 -34.656 1.00 30.62 ? 362  LYS B NZ  1 
ATOM   3409 N  N   . ILE B 1 139 ? -17.837 6.755  -30.506 1.00 18.51 ? 363  ILE B N   1 
ATOM   3410 C  CA  . ILE B 1 139 ? -19.092 6.240  -31.025 1.00 20.06 ? 363  ILE B CA  1 
ATOM   3411 C  C   . ILE B 1 139 ? -20.187 6.289  -29.963 1.00 23.68 ? 363  ILE B C   1 
ATOM   3412 O  O   . ILE B 1 139 ? -21.218 5.629  -30.102 1.00 22.46 ? 363  ILE B O   1 
ATOM   3413 C  CB  . ILE B 1 139 ? -18.913 4.825  -31.589 1.00 18.78 ? 363  ILE B CB  1 
ATOM   3414 C  CG1 . ILE B 1 139 ? -18.244 3.915  -30.543 1.00 18.68 ? 363  ILE B CG1 1 
ATOM   3415 C  CG2 . ILE B 1 139 ? -18.113 4.876  -32.882 1.00 18.79 ? 363  ILE B CG2 1 
ATOM   3416 C  CD1 . ILE B 1 139 ? -18.249 2.409  -30.921 1.00 19.22 ? 363  ILE B CD1 1 
ATOM   3417 N  N   . GLY B 1 140 ? -19.970 7.057  -28.894 1.00 21.16 ? 364  GLY B N   1 
ATOM   3418 C  CA  . GLY B 1 140 ? -21.012 7.312  -27.919 1.00 20.06 ? 364  GLY B CA  1 
ATOM   3419 C  C   . GLY B 1 140 ? -21.218 6.244  -26.869 1.00 22.95 ? 364  GLY B C   1 
ATOM   3420 O  O   . GLY B 1 140 ? -22.223 6.304  -26.147 1.00 22.31 ? 364  GLY B O   1 
ATOM   3421 N  N   . GLN B 1 141 ? -20.308 5.270  -26.753 1.00 20.17 ? 365  GLN B N   1 
ATOM   3422 C  CA  . GLN B 1 141 ? -20.458 4.152  -25.818 1.00 20.79 ? 365  GLN B CA  1 
ATOM   3423 C  C   . GLN B 1 141 ? -19.545 4.384  -24.615 1.00 22.22 ? 365  GLN B C   1 
ATOM   3424 O  O   . GLN B 1 141 ? -18.323 4.230  -24.708 1.00 21.04 ? 365  GLN B O   1 
ATOM   3425 C  CB  . GLN B 1 141 ? -20.160 2.826  -26.515 1.00 18.85 ? 365  GLN B CB  1 
ATOM   3426 C  CG  . GLN B 1 141 ? -21.037 2.622  -27.725 1.00 22.51 ? 365  GLN B CG  1 
ATOM   3427 C  CD  . GLN B 1 141 ? -20.731 1.353  -28.479 1.00 22.62 ? 365  GLN B CD  1 
ATOM   3428 O  OE1 . GLN B 1 141 ? -19.746 0.682  -28.207 1.00 20.67 ? 365  GLN B OE1 1 
ATOM   3429 N  NE2 . GLN B 1 141 ? -21.580 1.021  -29.439 1.00 22.54 ? 365  GLN B NE2 1 
ATOM   3430 N  N   . VAL B 1 142 ? -20.146 4.777  -23.487 1.00 18.07 ? 366  VAL B N   1 
ATOM   3431 C  CA  . VAL B 1 142 ? -19.439 4.957  -22.221 1.00 18.64 ? 366  VAL B CA  1 
ATOM   3432 C  C   . VAL B 1 142 ? -20.264 4.314  -21.109 1.00 23.40 ? 366  VAL B C   1 
ATOM   3433 O  O   . VAL B 1 142 ? -21.496 4.421  -21.091 1.00 18.43 ? 366  VAL B O   1 
ATOM   3434 C  CB  . VAL B 1 142 ? -19.174 6.459  -21.936 1.00 21.30 ? 366  VAL B CB  1 
ATOM   3435 C  CG1 . VAL B 1 142 ? -18.669 6.688  -20.509 1.00 18.49 ? 366  VAL B CG1 1 
ATOM   3436 C  CG2 . VAL B 1 142 ? -18.170 7.011  -22.944 1.00 17.13 ? 366  VAL B CG2 1 
ATOM   3437 N  N   . ARG B 1 143 ? -19.580 3.641  -20.182 1.00 21.36 ? 367  ARG B N   1 
ATOM   3438 C  CA  . ARG B 1 143 ? -20.207 3.044  -19.011 1.00 22.20 ? 367  ARG B CA  1 
ATOM   3439 C  C   . ARG B 1 143 ? -19.732 3.726  -17.737 1.00 22.45 ? 367  ARG B C   1 
ATOM   3440 O  O   . ARG B 1 143 ? -18.577 4.143  -17.637 1.00 20.46 ? 367  ARG B O   1 
ATOM   3441 C  CB  . ARG B 1 143 ? -19.880 1.558  -18.912 1.00 22.53 ? 367  ARG B CB  1 
ATOM   3442 C  CG  . ARG B 1 143 ? -20.395 0.742  -20.050 1.00 19.57 ? 367  ARG B CG  1 
ATOM   3443 C  CD  . ARG B 1 143 ? -19.728 -0.619 -20.037 1.00 25.01 ? 367  ARG B CD  1 
ATOM   3444 N  NE  . ARG B 1 143 ? -20.349 -1.506 -21.009 1.00 21.10 ? 367  ARG B NE  1 
ATOM   3445 C  CZ  . ARG B 1 143 ? -20.070 -2.796 -21.126 1.00 28.45 ? 367  ARG B CZ  1 
ATOM   3446 N  NH1 . ARG B 1 143 ? -19.181 -3.387 -20.340 1.00 24.31 ? 367  ARG B NH1 1 
ATOM   3447 N  NH2 . ARG B 1 143 ? -20.699 -3.512 -22.052 1.00 28.29 ? 367  ARG B NH2 1 
ATOM   3448 N  N   . PHE B 1 144 ? -20.623 3.811  -16.748 1.00 20.59 ? 368  PHE B N   1 
ATOM   3449 C  CA  . PHE B 1 144 ? -20.233 4.252  -15.419 1.00 20.45 ? 368  PHE B CA  1 
ATOM   3450 C  C   . PHE B 1 144 ? -20.728 3.256  -14.383 1.00 21.04 ? 368  PHE B C   1 
ATOM   3451 O  O   . PHE B 1 144 ? -21.776 2.629  -14.545 1.00 21.31 ? 368  PHE B O   1 
ATOM   3452 C  CB  . PHE B 1 144 ? -20.754 5.684  -15.093 1.00 18.94 ? 368  PHE B CB  1 
ATOM   3453 C  CG  . PHE B 1 144 ? -22.251 5.789  -14.924 1.00 18.65 ? 368  PHE B CG  1 
ATOM   3454 C  CD1 . PHE B 1 144 ? -23.063 6.062  -16.001 1.00 19.11 ? 368  PHE B CD1 1 
ATOM   3455 C  CD2 . PHE B 1 144 ? -22.840 5.671  -13.670 1.00 19.37 ? 368  PHE B CD2 1 
ATOM   3456 C  CE1 . PHE B 1 144 ? -24.449 6.194  -15.835 1.00 20.26 ? 368  PHE B CE1 1 
ATOM   3457 C  CE2 . PHE B 1 144 ? -24.206 5.798  -13.505 1.00 19.29 ? 368  PHE B CE2 1 
ATOM   3458 C  CZ  . PHE B 1 144 ? -25.009 6.064  -14.590 1.00 21.21 ? 368  PHE B CZ  1 
ATOM   3459 N  N   . TYR B 1 145 ? -19.940 3.099  -13.332 1.00 21.58 ? 369  TYR B N   1 
ATOM   3460 C  CA  . TYR B 1 145 ? -20.306 2.298  -12.182 1.00 21.58 ? 369  TYR B CA  1 
ATOM   3461 C  C   . TYR B 1 145 ? -20.701 3.215  -11.037 1.00 21.28 ? 369  TYR B C   1 
ATOM   3462 O  O   . TYR B 1 145 ? -20.149 4.304  -10.882 1.00 22.19 ? 369  TYR B O   1 
ATOM   3463 C  CB  . TYR B 1 145 ? -19.148 1.398  -11.740 1.00 22.03 ? 369  TYR B CB  1 
ATOM   3464 C  CG  . TYR B 1 145 ? -19.525 0.528  -10.570 1.00 24.49 ? 369  TYR B CG  1 
ATOM   3465 C  CD1 . TYR B 1 145 ? -20.255 -0.636 -10.764 1.00 28.25 ? 369  TYR B CD1 1 
ATOM   3466 C  CD2 . TYR B 1 145 ? -19.173 0.878  -9.267  1.00 27.04 ? 369  TYR B CD2 1 
ATOM   3467 C  CE1 . TYR B 1 145 ? -20.626 -1.436 -9.698  1.00 24.82 ? 369  TYR B CE1 1 
ATOM   3468 C  CE2 . TYR B 1 145 ? -19.540 0.085  -8.195  1.00 24.84 ? 369  TYR B CE2 1 
ATOM   3469 C  CZ  . TYR B 1 145 ? -20.262 -1.074 -8.420  1.00 26.04 ? 369  TYR B CZ  1 
ATOM   3470 O  OH  . TYR B 1 145 ? -20.627 -1.882 -7.368  1.00 30.18 ? 369  TYR B OH  1 
ATOM   3471 N  N   . SER B 1 146 ? -21.652 2.755  -10.227 1.00 24.11 ? 370  SER B N   1 
ATOM   3472 C  CA  . SER B 1 146 ? -22.085 3.498  -9.058  1.00 24.20 ? 370  SER B CA  1 
ATOM   3473 C  C   . SER B 1 146 ? -22.379 2.529  -7.930  1.00 23.19 ? 370  SER B C   1 
ATOM   3474 O  O   . SER B 1 146 ? -22.879 1.425  -8.164  1.00 24.73 ? 370  SER B O   1 
ATOM   3475 C  CB  . SER B 1 146 ? -23.323 4.360  -9.370  1.00 23.40 ? 370  SER B CB  1 
ATOM   3476 O  OG  . SER B 1 146 ? -23.841 4.971  -8.206  1.00 20.67 ? 370  SER B OG  1 
ATOM   3477 N  N   . THR B 1 147 ? -22.061 2.946  -6.701  1.00 24.15 ? 371  THR B N   1 
ATOM   3478 C  CA  . THR B 1 147 ? -22.485 2.212  -5.511  1.00 28.20 ? 371  THR B CA  1 
ATOM   3479 C  C   . THR B 1 147 ? -23.991 2.294  -5.278  1.00 24.51 ? 371  THR B C   1 
ATOM   3480 O  O   . THR B 1 147 ? -24.509 1.570  -4.420  1.00 28.40 ? 371  THR B O   1 
ATOM   3481 C  CB  . THR B 1 147 ? -21.763 2.739  -4.272  1.00 29.38 ? 371  THR B CB  1 
ATOM   3482 O  OG1 . THR B 1 147 ? -22.018 4.148  -4.143  1.00 26.85 ? 371  THR B OG1 1 
ATOM   3483 C  CG2 . THR B 1 147 ? -20.256 2.473  -4.375  1.00 24.24 ? 371  THR B CG2 1 
ATOM   3484 N  N   . SER B 1 148 ? -24.698 3.139  -6.020  1.00 22.98 ? 372  SER B N   1 
ATOM   3485 C  CA  . SER B 1 148 ? -26.145 3.250  -5.909  1.00 27.36 ? 372  SER B CA  1 
ATOM   3486 C  C   . SER B 1 148 ? -26.819 2.515  -7.059  1.00 24.86 ? 372  SER B C   1 
ATOM   3487 O  O   . SER B 1 148 ? -26.299 2.484  -8.174  1.00 28.14 ? 372  SER B O   1 
ATOM   3488 C  CB  . SER B 1 148 ? -26.582 4.712  -5.915  1.00 24.51 ? 372  SER B CB  1 
ATOM   3489 O  OG  . SER B 1 148 ? -27.998 4.809  -5.961  1.00 27.75 ? 372  SER B OG  1 
ATOM   3490 N  N   . SER B 1 149 ? -27.972 1.911  -6.778  1.00 24.68 ? 373  SER B N   1 
ATOM   3491 C  CA  . SER B 1 149 ? -28.819 1.342  -7.815  1.00 24.84 ? 373  SER B CA  1 
ATOM   3492 C  C   . SER B 1 149 ? -29.986 2.261  -8.163  1.00 29.22 ? 373  SER B C   1 
ATOM   3493 O  O   . SER B 1 149 ? -30.864 1.877  -8.943  1.00 24.67 ? 373  SER B O   1 
ATOM   3494 C  CB  . SER B 1 149 ? -29.333 -0.032 -7.382  1.00 31.29 ? 373  SER B CB  1 
ATOM   3495 O  OG  . SER B 1 149 ? -30.262 0.090  -6.318  1.00 30.68 ? 373  SER B OG  1 
ATOM   3496 N  N   . ASP B 1 150 ? -30.006 3.471  -7.610  1.00 27.85 ? 374  ASP B N   1 
ATOM   3497 C  CA  . ASP B 1 150 ? -31.118 4.400  -7.808  1.00 28.14 ? 374  ASP B CA  1 
ATOM   3498 C  C   . ASP B 1 150 ? -30.860 5.236  -9.061  1.00 22.60 ? 374  ASP B C   1 
ATOM   3499 O  O   . ASP B 1 150 ? -30.595 6.438  -9.021  1.00 24.75 ? 374  ASP B O   1 
ATOM   3500 C  CB  . ASP B 1 150 ? -31.316 5.258  -6.559  1.00 23.77 ? 374  ASP B CB  1 
ATOM   3501 C  CG  . ASP B 1 150 ? -32.317 6.378  -6.765  1.00 28.87 ? 374  ASP B CG  1 
ATOM   3502 O  OD1 . ASP B 1 150 ? -33.388 6.119  -7.351  1.00 28.60 ? 374  ASP B OD1 1 
ATOM   3503 O  OD2 . ASP B 1 150 ? -32.034 7.522  -6.336  1.00 30.68 ? 374  ASP B OD2 1 
ATOM   3504 N  N   . PHE B 1 151 ? -30.949 4.559  -10.202 1.00 26.12 ? 375  PHE B N   1 
ATOM   3505 C  CA  . PHE B 1 151 ? -30.927 5.183  -11.520 1.00 22.48 ? 375  PHE B CA  1 
ATOM   3506 C  C   . PHE B 1 151 ? -32.047 4.587  -12.352 1.00 24.07 ? 375  PHE B C   1 
ATOM   3507 O  O   . PHE B 1 151 ? -32.312 3.389  -12.258 1.00 24.67 ? 375  PHE B O   1 
ATOM   3508 C  CB  . PHE B 1 151 ? -29.597 4.959  -12.245 1.00 25.60 ? 375  PHE B CB  1 
ATOM   3509 C  CG  . PHE B 1 151 ? -28.470 5.752  -11.682 1.00 20.79 ? 375  PHE B CG  1 
ATOM   3510 C  CD1 . PHE B 1 151 ? -28.228 7.027  -12.124 1.00 20.39 ? 375  PHE B CD1 1 
ATOM   3511 C  CD2 . PHE B 1 151 ? -27.658 5.222  -10.690 1.00 25.60 ? 375  PHE B CD2 1 
ATOM   3512 C  CE1 . PHE B 1 151 ? -27.191 7.767  -11.589 1.00 24.84 ? 375  PHE B CE1 1 
ATOM   3513 C  CE2 . PHE B 1 151 ? -26.614 5.957  -10.158 1.00 21.16 ? 375  PHE B CE2 1 
ATOM   3514 C  CZ  . PHE B 1 151 ? -26.390 7.230  -10.598 1.00 23.55 ? 375  PHE B CZ  1 
ATOM   3515 N  N   . GLU B 1 152 ? -32.687 5.410  -13.177 1.00 23.49 ? 376  GLU B N   1 
ATOM   3516 C  CA  . GLU B 1 152 ? -33.762 4.962  -14.052 1.00 25.66 ? 376  GLU B CA  1 
ATOM   3517 C  C   . GLU B 1 152 ? -33.264 4.859  -15.489 1.00 28.62 ? 376  GLU B C   1 
ATOM   3518 O  O   . GLU B 1 152 ? -32.535 5.735  -15.968 1.00 23.83 ? 376  GLU B O   1 
ATOM   3519 C  CB  . GLU B 1 152 ? -34.950 5.920  -14.008 1.00 28.32 ? 376  GLU B CB  1 
ATOM   3520 C  CG  . GLU B 1 152 ? -35.450 6.238  -12.634 1.00 30.89 ? 376  GLU B CG  1 
ATOM   3521 C  CD  . GLU B 1 152 ? -36.908 5.867  -12.477 1.00 47.68 ? 376  GLU B CD  1 
ATOM   3522 O  OE1 . GLU B 1 152 ? -37.348 4.937  -13.189 1.00 53.11 ? 376  GLU B OE1 1 
ATOM   3523 O  OE2 . GLU B 1 152 ? -37.612 6.502  -11.659 1.00 50.54 ? 376  GLU B OE2 1 
ATOM   3524 N  N   . THR B 1 153 ? -33.672 3.797  -16.180 1.00 27.76 ? 377  THR B N   1 
ATOM   3525 C  CA  . THR B 1 153 ? -33.338 3.660  -17.589 1.00 29.13 ? 377  THR B CA  1 
ATOM   3526 C  C   . THR B 1 153 ? -34.156 4.639  -18.430 1.00 29.88 ? 377  THR B C   1 
ATOM   3527 O  O   . THR B 1 153 ? -35.270 5.026  -18.064 1.00 25.58 ? 377  THR B O   1 
ATOM   3528 C  CB  . THR B 1 153 ? -33.592 2.231  -18.063 1.00 27.91 ? 377  THR B CB  1 
ATOM   3529 O  OG1 . THR B 1 153 ? -34.973 1.918  -17.878 1.00 38.97 ? 377  THR B OG1 1 
ATOM   3530 C  CG2 . THR B 1 153 ? -32.759 1.247  -17.255 1.00 31.43 ? 377  THR B CG2 1 
ATOM   3531 N  N   . ASN B 1 154 ? -33.564 5.054  -19.557 1.00 25.36 ? 378  ASN B N   1 
ATOM   3532 C  CA  . ASN B 1 154 ? -34.192 5.931  -20.551 1.00 27.77 ? 378  ASN B CA  1 
ATOM   3533 C  C   . ASN B 1 154 ? -34.555 7.298  -19.976 1.00 28.23 ? 378  ASN B C   1 
ATOM   3534 O  O   . ASN B 1 154 ? -35.576 7.889  -20.323 1.00 28.58 ? 378  ASN B O   1 
ATOM   3535 C  CB  . ASN B 1 154 ? -35.405 5.264  -21.194 1.00 26.61 ? 378  ASN B CB  1 
ATOM   3536 C  CG  . ASN B 1 154 ? -35.003 4.100  -22.065 1.00 33.94 ? 378  ASN B CG  1 
ATOM   3537 O  OD1 . ASN B 1 154 ? -33.962 4.153  -22.724 1.00 30.61 ? 378  ASN B OD1 1 
ATOM   3538 N  ND2 . ASN B 1 154 ? -35.797 3.026  -22.051 1.00 31.67 ? 378  ASN B ND2 1 
ATOM   3539 N  N   . GLN B 1 155 ? -33.691 7.816  -19.119 1.00 25.42 ? 379  GLN B N   1 
ATOM   3540 C  CA  . GLN B 1 155 ? -33.807 9.177  -18.632 1.00 24.65 ? 379  GLN B CA  1 
ATOM   3541 C  C   . GLN B 1 155 ? -32.504 9.914  -18.898 1.00 23.98 ? 379  GLN B C   1 
ATOM   3542 O  O   . GLN B 1 155 ? -31.426 9.302  -18.909 1.00 22.76 ? 379  GLN B O   1 
ATOM   3543 C  CB  . GLN B 1 155 ? -34.138 9.216  -17.131 1.00 24.66 ? 379  GLN B CB  1 
ATOM   3544 C  CG  . GLN B 1 155 ? -35.494 8.610  -16.777 1.00 24.94 ? 379  GLN B CG  1 
ATOM   3545 C  CD  . GLN B 1 155 ? -36.653 9.305  -17.477 1.00 29.64 ? 379  GLN B CD  1 
ATOM   3546 O  OE1 . GLN B 1 155 ? -36.522 10.434 -17.953 1.00 27.97 ? 379  GLN B OE1 1 
ATOM   3547 N  NE2 . GLN B 1 155 ? -37.792 8.631  -17.542 1.00 28.32 ? 379  GLN B NE2 1 
ATOM   3548 N  N   . PRO B 1 156 ? -32.570 11.222 -19.141 1.00 23.99 ? 380  PRO B N   1 
ATOM   3549 C  CA  . PRO B 1 156 ? -31.340 11.965 -19.430 1.00 20.71 ? 380  PRO B CA  1 
ATOM   3550 C  C   . PRO B 1 156 ? -30.408 11.977 -18.229 1.00 22.84 ? 380  PRO B C   1 
ATOM   3551 O  O   . PRO B 1 156 ? -30.822 12.189 -17.089 1.00 23.93 ? 380  PRO B O   1 
ATOM   3552 C  CB  . PRO B 1 156 ? -31.843 13.368 -19.784 1.00 22.56 ? 380  PRO B CB  1 
ATOM   3553 C  CG  . PRO B 1 156 ? -33.222 13.441 -19.231 1.00 25.06 ? 380  PRO B CG  1 
ATOM   3554 C  CD  . PRO B 1 156 ? -33.773 12.064 -19.268 1.00 23.20 ? 380  PRO B CD  1 
ATOM   3555 N  N   . THR B 1 157 ? -29.134 11.749 -18.500 1.00 18.74 ? 381  THR B N   1 
ATOM   3556 C  CA  . THR B 1 157 ? -28.146 11.511 -17.469 1.00 18.12 ? 381  THR B CA  1 
ATOM   3557 C  C   . THR B 1 157 ? -26.926 12.373 -17.751 1.00 17.64 ? 381  THR B C   1 
ATOM   3558 O  O   . THR B 1 157 ? -26.491 12.479 -18.897 1.00 19.45 ? 381  THR B O   1 
ATOM   3559 C  CB  . THR B 1 157 ? -27.766 10.025 -17.441 1.00 22.06 ? 381  THR B CB  1 
ATOM   3560 O  OG1 . THR B 1 157 ? -28.964 9.231  -17.347 1.00 21.47 ? 381  THR B OG1 1 
ATOM   3561 C  CG2 . THR B 1 157 ? -26.841 9.735  -16.281 1.00 18.35 ? 381  THR B CG2 1 
ATOM   3562 N  N   . HIS B 1 158 ? -26.380 12.994 -16.716 1.00 17.36 ? 382  HIS B N   1 
ATOM   3563 C  CA  . HIS B 1 158 ? -25.193 13.830 -16.869 1.00 16.90 ? 382  HIS B CA  1 
ATOM   3564 C  C   . HIS B 1 158 ? -24.142 13.361 -15.875 1.00 19.72 ? 382  HIS B C   1 
ATOM   3565 O  O   . HIS B 1 158 ? -24.470 12.991 -14.741 1.00 19.14 ? 382  HIS B O   1 
ATOM   3566 C  CB  . HIS B 1 158 ? -25.507 15.332 -16.654 1.00 19.31 ? 382  HIS B CB  1 
ATOM   3567 C  CG  . HIS B 1 158 ? -24.334 16.234 -16.898 1.00 19.85 ? 382  HIS B CG  1 
ATOM   3568 N  ND1 . HIS B 1 158 ? -24.178 16.959 -18.062 1.00 22.70 ? 382  HIS B ND1 1 
ATOM   3569 C  CD2 . HIS B 1 158 ? -23.243 16.502 -16.144 1.00 19.60 ? 382  HIS B CD2 1 
ATOM   3570 C  CE1 . HIS B 1 158 ? -23.054 17.651 -18.005 1.00 21.55 ? 382  HIS B CE1 1 
ATOM   3571 N  NE2 . HIS B 1 158 ? -22.470 17.398 -16.847 1.00 21.28 ? 382  HIS B NE2 1 
ATOM   3572 N  N   . PHE B 1 159 ? -22.888 13.341 -16.312 1.00 17.82 ? 383  PHE B N   1 
ATOM   3573 C  CA  . PHE B 1 159 ? -21.773 12.978 -15.450 1.00 20.06 ? 383  PHE B CA  1 
ATOM   3574 C  C   . PHE B 1 159 ? -20.932 14.217 -15.203 1.00 19.24 ? 383  PHE B C   1 
ATOM   3575 O  O   . PHE B 1 159 ? -20.342 14.765 -16.142 1.00 15.95 ? 383  PHE B O   1 
ATOM   3576 C  CB  . PHE B 1 159 ? -20.905 11.879 -16.058 1.00 17.61 ? 383  PHE B CB  1 
ATOM   3577 C  CG  . PHE B 1 159 ? -19.696 11.551 -15.218 1.00 17.42 ? 383  PHE B CG  1 
ATOM   3578 C  CD1 . PHE B 1 159 ? -19.778 10.607 -14.200 1.00 21.51 ? 383  PHE B CD1 1 
ATOM   3579 C  CD2 . PHE B 1 159 ? -18.484 12.192 -15.438 1.00 16.31 ? 383  PHE B CD2 1 
ATOM   3580 C  CE1 . PHE B 1 159 ? -18.668 10.293 -13.418 1.00 18.62 ? 383  PHE B CE1 1 
ATOM   3581 C  CE2 . PHE B 1 159 ? -17.372 11.898 -14.654 1.00 21.03 ? 383  PHE B CE2 1 
ATOM   3582 C  CZ  . PHE B 1 159 ? -17.467 10.947 -13.637 1.00 19.63 ? 383  PHE B CZ  1 
ATOM   3583 N  N   . THR B 1 160 ? -20.885 14.651 -13.939 1.00 19.35 ? 384  THR B N   1 
ATOM   3584 C  CA  . THR B 1 160 ? -20.107 15.814 -13.539 1.00 18.52 ? 384  THR B CA  1 
ATOM   3585 C  C   . THR B 1 160 ? -18.787 15.329 -12.970 1.00 17.79 ? 384  THR B C   1 
ATOM   3586 O  O   . THR B 1 160 ? -18.796 14.587 -11.979 1.00 18.02 ? 384  THR B O   1 
ATOM   3587 C  CB  . THR B 1 160 ? -20.857 16.639 -12.494 1.00 19.70 ? 384  THR B CB  1 
ATOM   3588 O  OG1 . THR B 1 160 ? -22.162 16.969 -12.976 1.00 16.84 ? 384  THR B OG1 1 
ATOM   3589 C  CG2 . THR B 1 160 ? -20.122 17.934 -12.201 1.00 20.57 ? 384  THR B CG2 1 
ATOM   3590 N  N   . PRO B 1 161 ? -17.649 15.697 -13.546 1.00 15.83 ? 385  PRO B N   1 
ATOM   3591 C  CA  . PRO B 1 161 ? -16.372 15.191 -13.038 1.00 17.82 ? 385  PRO B CA  1 
ATOM   3592 C  C   . PRO B 1 161 ? -15.970 15.911 -11.759 1.00 18.42 ? 385  PRO B C   1 
ATOM   3593 O  O   . PRO B 1 161 ? -16.210 17.113 -11.588 1.00 17.69 ? 385  PRO B O   1 
ATOM   3594 C  CB  . PRO B 1 161 ? -15.404 15.504 -14.184 1.00 19.47 ? 385  PRO B CB  1 
ATOM   3595 C  CG  . PRO B 1 161 ? -15.950 16.811 -14.741 1.00 17.26 ? 385  PRO B CG  1 
ATOM   3596 C  CD  . PRO B 1 161 ? -17.463 16.698 -14.618 1.00 17.19 ? 385  PRO B CD  1 
ATOM   3597 N  N   . ILE B 1 162 ? -15.374 15.155 -10.840 1.00 17.69 ? 386  ILE B N   1 
ATOM   3598 C  CA  . ILE B 1 162 ? -14.874 15.691 -9.580  1.00 18.07 ? 386  ILE B CA  1 
ATOM   3599 C  C   . ILE B 1 162 ? -13.369 15.489 -9.451  1.00 19.42 ? 386  ILE B C   1 
ATOM   3600 O  O   . ILE B 1 162 ? -12.626 16.429 -9.150  1.00 18.87 ? 386  ILE B O   1 
ATOM   3601 C  CB  . ILE B 1 162 ? -15.611 15.074 -8.372  1.00 19.11 ? 386  ILE B CB  1 
ATOM   3602 C  CG1 . ILE B 1 162 ? -17.113 15.362 -8.436  1.00 19.13 ? 386  ILE B CG1 1 
ATOM   3603 C  CG2 . ILE B 1 162 ? -15.056 15.631 -7.071  1.00 20.72 ? 386  ILE B CG2 1 
ATOM   3604 C  CD1 . ILE B 1 162 ? -17.451 16.811 -8.308  1.00 20.28 ? 386  ILE B CD1 1 
ATOM   3605 N  N   . GLY B 1 163 ? -12.902 14.268 -9.672  1.00 19.12 ? 387  GLY B N   1 
ATOM   3606 C  CA  . GLY B 1 163 ? -11.487 13.982 -9.560  1.00 19.77 ? 387  GLY B CA  1 
ATOM   3607 C  C   . GLY B 1 163 ? -11.153 12.584 -10.024 1.00 20.65 ? 387  GLY B C   1 
ATOM   3608 O  O   . GLY B 1 163 ? -11.812 12.071 -10.934 1.00 17.49 ? 387  GLY B O   1 
ATOM   3609 N  N   . ILE B 1 164 ? -10.154 11.953 -9.397  1.00 21.14 ? 388  ILE B N   1 
ATOM   3610 C  CA  . ILE B 1 164 ? -9.706  10.621 -9.788  1.00 25.08 ? 388  ILE B CA  1 
ATOM   3611 C  C   . ILE B 1 164 ? -9.719  9.680  -8.590  1.00 23.45 ? 388  ILE B C   1 
ATOM   3612 O  O   . ILE B 1 164 ? -9.490  10.071 -7.442  1.00 22.96 ? 388  ILE B O   1 
ATOM   3613 C  CB  . ILE B 1 164 ? -8.303  10.626 -10.439 1.00 24.16 ? 388  ILE B CB  1 
ATOM   3614 C  CG1 . ILE B 1 164 ? -7.313  11.370 -9.552  1.00 24.95 ? 388  ILE B CG1 1 
ATOM   3615 C  CG2 . ILE B 1 164 ? -8.366  11.233 -11.837 1.00 23.75 ? 388  ILE B CG2 1 
ATOM   3616 C  CD1 . ILE B 1 164 ? -5.882  10.999 -9.830  1.00 30.18 ? 388  ILE B CD1 1 
ATOM   3617 N  N   . TYR B 1 165 ? -10.003 8.426  -8.881  1.00 23.84 ? 389  TYR B N   1 
ATOM   3618 C  CA  . TYR B 1 165 ? -10.040 7.348  -7.911  1.00 23.94 ? 389  TYR B CA  1 
ATOM   3619 C  C   . TYR B 1 165 ? -8.797  6.500  -8.142  1.00 25.87 ? 389  TYR B C   1 
ATOM   3620 O  O   . TYR B 1 165 ? -8.537  6.085  -9.274  1.00 27.63 ? 389  TYR B O   1 
ATOM   3621 C  CB  . TYR B 1 165 ? -11.327 6.544  -8.112  1.00 23.51 ? 389  TYR B CB  1 
ATOM   3622 C  CG  . TYR B 1 165 ? -11.733 5.637  -6.983  1.00 32.83 ? 389  TYR B CG  1 
ATOM   3623 C  CD1 . TYR B 1 165 ? -11.103 4.410  -6.797  1.00 35.11 ? 389  TYR B CD1 1 
ATOM   3624 C  CD2 . TYR B 1 165 ? -12.775 5.986  -6.122  1.00 33.80 ? 389  TYR B CD2 1 
ATOM   3625 C  CE1 . TYR B 1 165 ? -11.476 3.552  -5.770  1.00 39.05 ? 389  TYR B CE1 1 
ATOM   3626 C  CE2 . TYR B 1 165 ? -13.159 5.135  -5.086  1.00 36.03 ? 389  TYR B CE2 1 
ATOM   3627 C  CZ  . TYR B 1 165 ? -12.498 3.921  -4.916  1.00 39.22 ? 389  TYR B CZ  1 
ATOM   3628 O  OH  . TYR B 1 165 ? -12.865 3.073  -3.901  1.00 44.26 ? 389  TYR B OH  1 
ATOM   3629 N  N   . ILE B 1 166 ? -8.004  6.289  -7.096  1.00 29.25 ? 390  ILE B N   1 
ATOM   3630 C  CA  . ILE B 1 166 ? -6.805  5.454  -7.164  1.00 25.11 ? 390  ILE B CA  1 
ATOM   3631 C  C   . ILE B 1 166 ? -7.117  4.146  -6.451  1.00 33.19 ? 390  ILE B C   1 
ATOM   3632 O  O   . ILE B 1 166 ? -7.315  4.128  -5.231  1.00 32.38 ? 390  ILE B O   1 
ATOM   3633 C  CB  . ILE B 1 166 ? -5.587  6.134  -6.532  1.00 26.61 ? 390  ILE B CB  1 
ATOM   3634 C  CG1 . ILE B 1 166 ? -5.286  7.470  -7.223  1.00 31.26 ? 390  ILE B CG1 1 
ATOM   3635 C  CG2 . ILE B 1 166 ? -4.381  5.203  -6.545  1.00 30.95 ? 390  ILE B CG2 1 
ATOM   3636 C  CD1 . ILE B 1 166 ? -4.839  7.351  -8.656  1.00 29.55 ? 390  ILE B CD1 1 
ATOM   3637 N  N   . GLU B 1 167 ? -7.169  3.052  -7.209  1.00 36.09 ? 391  GLU B N   1 
ATOM   3638 C  CA  . GLU B 1 167 ? -7.288  1.722  -6.627  1.00 39.55 ? 391  GLU B CA  1 
ATOM   3639 C  C   . GLU B 1 167 ? -5.943  1.083  -6.313  1.00 41.83 ? 391  GLU B C   1 
ATOM   3640 O  O   . GLU B 1 167 ? -5.884  0.201  -5.448  1.00 39.83 ? 391  GLU B O   1 
ATOM   3641 C  CB  . GLU B 1 167 ? -8.072  0.800  -7.562  1.00 37.62 ? 391  GLU B CB  1 
ATOM   3642 C  CG  . GLU B 1 167 ? -9.562  1.039  -7.509  1.00 43.95 ? 391  GLU B CG  1 
ATOM   3643 C  CD  . GLU B 1 167 ? -10.340 0.106  -8.418  1.00 51.71 ? 391  GLU B CD  1 
ATOM   3644 O  OE1 . GLU B 1 167 ? -9.744  -0.873 -8.926  1.00 53.51 ? 391  GLU B OE1 1 
ATOM   3645 O  OE2 . GLU B 1 167 ? -11.549 0.356  -8.626  1.00 49.71 ? 391  GLU B OE2 1 
ATOM   3646 N  N   . GLY B 1 168 ? -4.868  1.516  -6.973  1.00 43.94 ? 392  GLY B N   1 
ATOM   3647 C  CA  . GLY B 1 168 ? -3.551  0.948  -6.749  1.00 42.89 ? 392  GLY B CA  1 
ATOM   3648 C  C   . GLY B 1 168 ? -3.179  -0.169 -7.701  1.00 54.28 ? 392  GLY B C   1 
ATOM   3649 O  O   . GLY B 1 168 ? -2.453  -1.094 -7.306  1.00 54.26 ? 392  GLY B O   1 
ATOM   3650 N  N   . ASN B 1 169 ? -3.652  -0.118 -8.942  1.00 52.22 ? 393  ASN B N   1 
ATOM   3651 C  CA  . ASN B 1 169 ? -3.478  -1.205 -9.903  1.00 51.38 ? 393  ASN B CA  1 
ATOM   3652 C  C   . ASN B 1 169 ? -3.362  -0.610 -11.307 1.00 51.27 ? 393  ASN B C   1 
ATOM   3653 O  O   . ASN B 1 169 ? -3.121  0.592  -11.474 1.00 45.52 ? 393  ASN B O   1 
ATOM   3654 C  CB  . ASN B 1 169 ? -4.631  -2.223 -9.779  1.00 50.05 ? 393  ASN B CB  1 
ATOM   3655 C  CG  . ASN B 1 169 ? -6.017  -1.592 -9.996  1.00 52.32 ? 393  ASN B CG  1 
ATOM   3656 O  OD1 . ASN B 1 169 ? -6.152  -0.512 -10.582 1.00 46.74 ? 393  ASN B OD1 1 
ATOM   3657 N  ND2 . ASN B 1 169 ? -7.054  -2.280 -9.521  1.00 52.40 ? 393  ASN B ND2 1 
ATOM   3658 N  N   . SER B 1 170 ? -3.566  -1.458 -12.319 1.00 54.18 ? 394  SER B N   1 
ATOM   3659 C  CA  . SER B 1 170 ? -3.294  -1.077 -13.702 1.00 56.56 ? 394  SER B CA  1 
ATOM   3660 C  C   . SER B 1 170 ? -4.149  0.103  -14.157 1.00 50.08 ? 394  SER B C   1 
ATOM   3661 O  O   . SER B 1 170 ? -3.751  0.849  -15.058 1.00 47.70 ? 394  SER B O   1 
ATOM   3662 C  CB  . SER B 1 170 ? -3.520  -2.286 -14.615 1.00 60.12 ? 394  SER B CB  1 
ATOM   3663 O  OG  . SER B 1 170 ? -3.053  -2.038 -15.933 1.00 70.79 ? 394  SER B OG  1 
ATOM   3664 N  N   . SER B 1 171 ? -5.314  0.295  -13.551 1.00 45.73 ? 395  SER B N   1 
ATOM   3665 C  CA  . SER B 1 171 ? -6.200  1.377  -13.944 1.00 45.02 ? 395  SER B CA  1 
ATOM   3666 C  C   . SER B 1 171 ? -5.732  2.750  -13.452 1.00 42.39 ? 395  SER B C   1 
ATOM   3667 O  O   . SER B 1 171 ? -6.450  3.730  -13.671 1.00 40.91 ? 395  SER B O   1 
ATOM   3668 C  CB  . SER B 1 171 ? -7.626  1.096  -13.441 1.00 42.57 ? 395  SER B CB  1 
ATOM   3669 O  OG  . SER B 1 171 ? -7.702  1.104  -12.023 1.00 36.92 ? 395  SER B OG  1 
ATOM   3670 N  N   . ASP B 1 172 ? -4.557  2.858  -12.827 1.00 41.35 ? 396  ASP B N   1 
ATOM   3671 C  CA  . ASP B 1 172 ? -4.182  4.106  -12.172 1.00 38.72 ? 396  ASP B CA  1 
ATOM   3672 C  C   . ASP B 1 172 ? -4.019  5.247  -13.173 1.00 33.18 ? 396  ASP B C   1 
ATOM   3673 O  O   . ASP B 1 172 ? -3.665  5.052  -14.338 1.00 29.95 ? 396  ASP B O   1 
ATOM   3674 C  CB  . ASP B 1 172 ? -2.899  3.934  -11.357 1.00 34.34 ? 396  ASP B CB  1 
ATOM   3675 C  CG  . ASP B 1 172 ? -3.152  3.256  -10.009 1.00 49.16 ? 396  ASP B CG  1 
ATOM   3676 O  OD1 . ASP B 1 172 ? -4.255  2.674  -9.832  1.00 44.59 ? 396  ASP B OD1 1 
ATOM   3677 O  OD2 . ASP B 1 172 ? -2.257  3.308  -9.130  1.00 44.79 ? 396  ASP B OD2 1 
ATOM   3678 N  N   . PHE B 1 173 ? -4.300  6.447  -12.684 1.00 34.02 ? 397  PHE B N   1 
ATOM   3679 C  CA  . PHE B 1 173 ? -4.266  7.694  -13.438 1.00 24.74 ? 397  PHE B CA  1 
ATOM   3680 C  C   . PHE B 1 173 ? -2.934  7.912  -14.156 1.00 26.46 ? 397  PHE B C   1 
ATOM   3681 O  O   . PHE B 1 173 ? -1.886  8.011  -13.515 1.00 23.22 ? 397  PHE B O   1 
ATOM   3682 C  CB  . PHE B 1 173 ? -4.532  8.824  -12.438 1.00 23.65 ? 397  PHE B CB  1 
ATOM   3683 C  CG  . PHE B 1 173 ? -4.481  10.195 -13.024 1.00 26.32 ? 397  PHE B CG  1 
ATOM   3684 C  CD1 . PHE B 1 173 ? -5.234  10.519 -14.138 1.00 27.03 ? 397  PHE B CD1 1 
ATOM   3685 C  CD2 . PHE B 1 173 ? -3.704  11.180 -12.436 1.00 27.78 ? 397  PHE B CD2 1 
ATOM   3686 C  CE1 . PHE B 1 173 ? -5.193  11.807 -14.672 1.00 25.60 ? 397  PHE B CE1 1 
ATOM   3687 C  CE2 . PHE B 1 173 ? -3.668  12.462 -12.961 1.00 24.55 ? 397  PHE B CE2 1 
ATOM   3688 C  CZ  . PHE B 1 173 ? -4.411  12.771 -14.075 1.00 21.68 ? 397  PHE B CZ  1 
ATOM   3689 N  N   . ASN B 1 174 ? -2.977  8.016  -15.487 1.00 19.29 ? 398  ASN B N   1 
ATOM   3690 C  CA  . ASN B 1 174 ? -1.809  8.401  -16.287 1.00 20.77 ? 398  ASN B CA  1 
ATOM   3691 C  C   . ASN B 1 174 ? -2.223  9.577  -17.167 1.00 20.27 ? 398  ASN B C   1 
ATOM   3692 O  O   . ASN B 1 174 ? -2.843  9.377  -18.212 1.00 19.36 ? 398  ASN B O   1 
ATOM   3693 C  CB  . ASN B 1 174 ? -1.291  7.227  -17.127 1.00 22.87 ? 398  ASN B CB  1 
ATOM   3694 C  CG  . ASN B 1 174 ? 0.044   7.526  -17.800 1.00 27.94 ? 398  ASN B CG  1 
ATOM   3695 O  OD1 . ASN B 1 174 ? 0.403   8.690  -18.042 1.00 21.80 ? 398  ASN B OD1 1 
ATOM   3696 N  ND2 . ASN B 1 174 ? 0.790   6.468  -18.111 1.00 28.49 ? 398  ASN B ND2 1 
ATOM   3697 N  N   . GLN B 1 175 ? -1.876  10.802 -16.758 1.00 21.82 ? 399  GLN B N   1 
ATOM   3698 C  CA  . GLN B 1 175 ? -2.362  11.984 -17.470 1.00 20.61 ? 399  GLN B CA  1 
ATOM   3699 C  C   . GLN B 1 175 ? -1.810  12.099 -18.883 1.00 18.95 ? 399  GLN B C   1 
ATOM   3700 O  O   . GLN B 1 175 ? -2.328  12.900 -19.666 1.00 19.64 ? 399  GLN B O   1 
ATOM   3701 C  CB  . GLN B 1 175 ? -2.027  13.264 -16.695 1.00 20.09 ? 399  GLN B CB  1 
ATOM   3702 C  CG  . GLN B 1 175 ? -0.532  13.633 -16.654 1.00 20.59 ? 399  GLN B CG  1 
ATOM   3703 C  CD  . GLN B 1 175 ? -0.317  15.106 -16.384 1.00 21.23 ? 399  GLN B CD  1 
ATOM   3704 O  OE1 . GLN B 1 175 ? -1.061  15.950 -16.882 1.00 19.14 ? 399  GLN B OE1 1 
ATOM   3705 N  NE2 . GLN B 1 175 ? 0.699   15.425 -15.597 1.00 20.14 ? 399  GLN B NE2 1 
ATOM   3706 N  N   . TRP B 1 176 ? -0.775  11.341 -19.228 1.00 19.58 ? 400  TRP B N   1 
ATOM   3707 C  CA  . TRP B 1 176 ? -0.188  11.412 -20.556 1.00 21.59 ? 400  TRP B CA  1 
ATOM   3708 C  C   . TRP B 1 176 ? -0.493  10.198 -21.422 1.00 24.39 ? 400  TRP B C   1 
ATOM   3709 O  O   . TRP B 1 176 ? -0.007  10.129 -22.555 1.00 27.95 ? 400  TRP B O   1 
ATOM   3710 C  CB  . TRP B 1 176 ? 1.327   11.607 -20.458 1.00 24.41 ? 400  TRP B CB  1 
ATOM   3711 C  CG  . TRP B 1 176 ? 1.705   12.886 -19.792 1.00 20.78 ? 400  TRP B CG  1 
ATOM   3712 C  CD1 . TRP B 1 176 ? 2.513   13.035 -18.706 1.00 20.49 ? 400  TRP B CD1 1 
ATOM   3713 C  CD2 . TRP B 1 176 ? 1.272   14.202 -20.155 1.00 22.54 ? 400  TRP B CD2 1 
ATOM   3714 N  NE1 . TRP B 1 176 ? 2.623   14.360 -18.376 1.00 22.87 ? 400  TRP B NE1 1 
ATOM   3715 C  CE2 . TRP B 1 176 ? 1.870   15.100 -19.249 1.00 20.73 ? 400  TRP B CE2 1 
ATOM   3716 C  CE3 . TRP B 1 176 ? 0.443   14.708 -21.156 1.00 19.12 ? 400  TRP B CE3 1 
ATOM   3717 C  CZ2 . TRP B 1 176 ? 1.668   16.474 -19.316 1.00 22.92 ? 400  TRP B CZ2 1 
ATOM   3718 C  CZ3 . TRP B 1 176 ? 0.241   16.085 -21.218 1.00 22.26 ? 400  TRP B CZ3 1 
ATOM   3719 C  CH2 . TRP B 1 176 ? 0.849   16.943 -20.305 1.00 24.10 ? 400  TRP B CH2 1 
ATOM   3720 N  N   . GLN B 1 177 ? -1.295  9.254  -20.945 1.00 19.49 ? 401  GLN B N   1 
ATOM   3721 C  CA  . GLN B 1 177 ? -1.744  8.143  -21.774 1.00 20.49 ? 401  GLN B CA  1 
ATOM   3722 C  C   . GLN B 1 177 ? -3.110  8.481  -22.357 1.00 20.73 ? 401  GLN B C   1 
ATOM   3723 O  O   . GLN B 1 177 ? -4.098  8.575  -21.623 1.00 20.51 ? 401  GLN B O   1 
ATOM   3724 C  CB  . GLN B 1 177 ? -1.805  6.853  -20.963 1.00 23.45 ? 401  GLN B CB  1 
ATOM   3725 C  CG  . GLN B 1 177 ? -2.085  5.633  -21.807 1.00 26.63 ? 401  GLN B CG  1 
ATOM   3726 C  CD  . GLN B 1 177 ? -2.030  4.358  -21.003 1.00 32.37 ? 401  GLN B CD  1 
ATOM   3727 O  OE1 . GLN B 1 177 ? -1.971  4.384  -19.772 1.00 37.73 ? 401  GLN B OE1 1 
ATOM   3728 N  NE2 . GLN B 1 177 ? -2.040  3.233  -21.691 1.00 36.52 ? 401  GLN B NE2 1 
ATOM   3729 N  N   . LEU B 1 178 ? -3.168  8.652  -23.670 1.00 20.07 ? 402  LEU B N   1 
ATOM   3730 C  CA  . LEU B 1 178 ? -4.439  8.914  -24.313 1.00 20.51 ? 402  LEU B CA  1 
ATOM   3731 C  C   . LEU B 1 178 ? -5.345  7.690  -24.200 1.00 21.40 ? 402  LEU B C   1 
ATOM   3732 O  O   . LEU B 1 178 ? -4.866  6.554  -24.261 1.00 19.18 ? 402  LEU B O   1 
ATOM   3733 C  CB  . LEU B 1 178 ? -4.236  9.267  -25.782 1.00 20.85 ? 402  LEU B CB  1 
ATOM   3734 C  CG  . LEU B 1 178 ? -3.550  10.608 -26.041 1.00 23.04 ? 402  LEU B CG  1 
ATOM   3735 C  CD1 . LEU B 1 178 ? -3.270  10.782 -27.523 1.00 20.02 ? 402  LEU B CD1 1 
ATOM   3736 C  CD2 . LEU B 1 178 ? -4.420  11.721 -25.508 1.00 21.12 ? 402  LEU B CD2 1 
ATOM   3737 N  N   . PRO B 1 179 ? -6.650  7.883  -24.039 1.00 19.75 ? 403  PRO B N   1 
ATOM   3738 C  CA  . PRO B 1 179 ? -7.572  6.747  -24.146 1.00 21.20 ? 403  PRO B CA  1 
ATOM   3739 C  C   . PRO B 1 179 ? -7.661  6.259  -25.583 1.00 22.20 ? 403  PRO B C   1 
ATOM   3740 O  O   . PRO B 1 179 ? -7.266  6.947  -26.532 1.00 20.27 ? 403  PRO B O   1 
ATOM   3741 C  CB  . PRO B 1 179 ? -8.912  7.327  -23.675 1.00 19.79 ? 403  PRO B CB  1 
ATOM   3742 C  CG  . PRO B 1 179 ? -8.812  8.792  -23.963 1.00 21.52 ? 403  PRO B CG  1 
ATOM   3743 C  CD  . PRO B 1 179 ? -7.350  9.163  -23.827 1.00 18.61 ? 403  PRO B CD  1 
ATOM   3744 N  N   . ARG B 1 180 ? -8.190  5.045  -25.737 1.00 17.52 ? 404  ARG B N   1 
ATOM   3745 C  CA  . ARG B 1 180 ? -8.666  4.585  -27.037 1.00 19.59 ? 404  ARG B CA  1 
ATOM   3746 C  C   . ARG B 1 180 ? -10.072 5.139  -27.226 1.00 20.95 ? 404  ARG B C   1 
ATOM   3747 O  O   . ARG B 1 180 ? -11.050 4.575  -26.725 1.00 21.81 ? 404  ARG B O   1 
ATOM   3748 C  CB  . ARG B 1 180 ? -8.672  3.064  -27.127 1.00 21.82 ? 404  ARG B CB  1 
ATOM   3749 C  CG  . ARG B 1 180 ? -7.317  2.440  -27.312 1.00 28.09 ? 404  ARG B CG  1 
ATOM   3750 C  CD  . ARG B 1 180 ? -7.429  0.928  -27.360 1.00 30.27 ? 404  ARG B CD  1 
ATOM   3751 N  NE  . ARG B 1 180 ? -7.423  0.394  -28.715 1.00 28.47 ? 404  ARG B NE  1 
ATOM   3752 C  CZ  . ARG B 1 180 ? -6.321  0.182  -29.423 1.00 33.28 ? 404  ARG B CZ  1 
ATOM   3753 N  NH1 . ARG B 1 180 ? -5.132  0.569  -28.985 1.00 38.02 ? 404  ARG B NH1 1 
ATOM   3754 N  NH2 . ARG B 1 180 ? -6.410  -0.441 -30.594 1.00 30.16 ? 404  ARG B NH2 1 
ATOM   3755 N  N   . TYR B 1 181 ? -10.183 6.235  -27.971 1.00 17.96 ? 405  TYR B N   1 
ATOM   3756 C  CA  . TYR B 1 181 ? -11.473 6.912  -28.096 1.00 18.57 ? 405  TYR B CA  1 
ATOM   3757 C  C   . TYR B 1 181 ? -12.539 6.020  -28.717 1.00 18.81 ? 405  TYR B C   1 
ATOM   3758 O  O   . TYR B 1 181 ? -13.734 6.222  -28.473 1.00 19.55 ? 405  TYR B O   1 
ATOM   3759 C  CB  . TYR B 1 181 ? -11.311 8.186  -28.914 1.00 16.91 ? 405  TYR B CB  1 
ATOM   3760 C  CG  . TYR B 1 181 ? -10.499 9.230  -28.194 1.00 17.58 ? 405  TYR B CG  1 
ATOM   3761 C  CD1 . TYR B 1 181 ? -11.096 10.106 -27.295 1.00 19.03 ? 405  TYR B CD1 1 
ATOM   3762 C  CD2 . TYR B 1 181 ? -9.124  9.328  -28.395 1.00 19.92 ? 405  TYR B CD2 1 
ATOM   3763 C  CE1 . TYR B 1 181 ? -10.331 11.079 -26.615 1.00 19.65 ? 405  TYR B CE1 1 
ATOM   3764 C  CE2 . TYR B 1 181 ? -8.365  10.285 -27.725 1.00 20.15 ? 405  TYR B CE2 1 
ATOM   3765 C  CZ  . TYR B 1 181 ? -8.971  11.160 -26.830 1.00 19.15 ? 405  TYR B CZ  1 
ATOM   3766 O  OH  . TYR B 1 181 ? -8.202  12.129 -26.165 1.00 17.72 ? 405  TYR B OH  1 
ATOM   3767 N  N   . GLY B 1 182 ? -12.142 5.040  -29.517 1.00 22.77 ? 406  GLY B N   1 
ATOM   3768 C  CA  . GLY B 1 182 ? -13.079 4.111  -30.113 1.00 18.77 ? 406  GLY B CA  1 
ATOM   3769 C  C   . GLY B 1 182 ? -13.146 2.760  -29.442 1.00 18.63 ? 406  GLY B C   1 
ATOM   3770 O  O   . GLY B 1 182 ? -13.706 1.823  -30.029 1.00 19.49 ? 406  GLY B O   1 
ATOM   3771 N  N   . GLY B 1 183 ? -12.595 2.623  -28.237 1.00 18.35 ? 407  GLY B N   1 
ATOM   3772 C  CA  . GLY B 1 183 ? -12.569 1.344  -27.562 1.00 18.73 ? 407  GLY B CA  1 
ATOM   3773 C  C   . GLY B 1 183 ? -11.475 0.440  -28.095 1.00 21.27 ? 407  GLY B C   1 
ATOM   3774 O  O   . GLY B 1 183 ? -10.716 0.783  -29.000 1.00 23.20 ? 407  GLY B O   1 
ATOM   3775 N  N   . HIS B 1 184 ? -11.428 -0.768 -27.537 1.00 21.40 ? 408  HIS B N   1 
ATOM   3776 C  CA  . HIS B 1 184 ? -10.281 -1.645 -27.722 1.00 19.72 ? 408  HIS B CA  1 
ATOM   3777 C  C   . HIS B 1 184 ? -10.170 -2.215 -29.129 1.00 22.75 ? 408  HIS B C   1 
ATOM   3778 O  O   . HIS B 1 184 ? -9.127  -2.786 -29.458 1.00 21.19 ? 408  HIS B O   1 
ATOM   3779 C  CB  . HIS B 1 184 ? -10.303 -2.777 -26.680 1.00 20.23 ? 408  HIS B CB  1 
ATOM   3780 C  CG  . HIS B 1 184 ? -11.351 -3.833 -26.906 1.00 25.15 ? 408  HIS B CG  1 
ATOM   3781 N  ND1 . HIS B 1 184 ? -12.703 -3.559 -26.920 1.00 26.65 ? 408  HIS B ND1 1 
ATOM   3782 C  CD2 . HIS B 1 184 ? -11.240 -5.177 -27.052 1.00 21.06 ? 408  HIS B CD2 1 
ATOM   3783 C  CE1 . HIS B 1 184 ? -13.377 -4.683 -27.106 1.00 22.03 ? 408  HIS B CE1 1 
ATOM   3784 N  NE2 . HIS B 1 184 ? -12.512 -5.679 -27.188 1.00 28.29 ? 408  HIS B NE2 1 
ATOM   3785 N  N   . LEU B 1 185 ? -11.176 -2.047 -29.982 1.00 20.67 ? 409  LEU B N   1 
ATOM   3786 C  CA  . LEU B 1 185 ? -11.132 -2.620 -31.321 1.00 21.86 ? 409  LEU B CA  1 
ATOM   3787 C  C   . LEU B 1 185 ? -10.926 -1.569 -32.406 1.00 23.93 ? 409  LEU B C   1 
ATOM   3788 O  O   . LEU B 1 185 ? -11.049 -1.887 -33.595 1.00 20.67 ? 409  LEU B O   1 
ATOM   3789 C  CB  . LEU B 1 185 ? -12.405 -3.430 -31.596 1.00 20.93 ? 409  LEU B CB  1 
ATOM   3790 C  CG  . LEU B 1 185 ? -12.678 -4.596 -30.643 1.00 21.26 ? 409  LEU B CG  1 
ATOM   3791 C  CD1 . LEU B 1 185 ? -13.945 -5.321 -31.073 1.00 21.71 ? 409  LEU B CD1 1 
ATOM   3792 C  CD2 . LEU B 1 185 ? -11.522 -5.582 -30.624 1.00 21.62 ? 409  LEU B CD2 1 
ATOM   3793 N  N   . ALA B 1 186 ? -10.586 -0.335 -32.035 1.00 21.51 ? 410  ALA B N   1 
ATOM   3794 C  CA  . ALA B 1 186 ? -10.379 0.733  -33.004 1.00 21.73 ? 410  ALA B CA  1 
ATOM   3795 C  C   . ALA B 1 186 ? -9.171  1.562  -32.585 1.00 21.49 ? 410  ALA B C   1 
ATOM   3796 O  O   . ALA B 1 186 ? -8.847  1.648  -31.399 1.00 20.05 ? 410  ALA B O   1 
ATOM   3797 C  CB  . ALA B 1 186 ? -11.627 1.622  -33.131 1.00 20.60 ? 410  ALA B CB  1 
ATOM   3798 N  N   . ASN B 1 187 ? -8.502  2.173  -33.567 1.00 21.67 ? 411  ASN B N   1 
ATOM   3799 C  CA  . ASN B 1 187 ? -7.338  3.017  -33.317 1.00 21.09 ? 411  ASN B CA  1 
ATOM   3800 C  C   . ASN B 1 187 ? -7.698  4.493  -33.409 1.00 19.89 ? 411  ASN B C   1 
ATOM   3801 O  O   . ASN B 1 187 ? -8.555  4.894  -34.202 1.00 21.14 ? 411  ASN B O   1 
ATOM   3802 C  CB  . ASN B 1 187 ? -6.217  2.713  -34.315 1.00 23.42 ? 411  ASN B CB  1 
ATOM   3803 C  CG  . ASN B 1 187 ? -5.801  1.265  -34.291 1.00 25.84 ? 411  ASN B CG  1 
ATOM   3804 O  OD1 . ASN B 1 187 ? -5.764  0.635  -33.237 1.00 27.00 ? 411  ASN B OD1 1 
ATOM   3805 N  ND2 . ASN B 1 187 ? -5.496  0.726  -35.457 1.00 28.12 ? 411  ASN B ND2 1 
ATOM   3806 N  N   . ASN B 1 188 ? -7.007  5.305  -32.606 1.00 18.72 ? 412  ASN B N   1 
ATOM   3807 C  CA  . ASN B 1 188 ? -7.259  6.742  -32.579 1.00 18.87 ? 412  ASN B CA  1 
ATOM   3808 C  C   . ASN B 1 188 ? -6.914  7.389  -33.918 1.00 20.65 ? 412  ASN B C   1 
ATOM   3809 O  O   . ASN B 1 188 ? -5.951  6.998  -34.581 1.00 23.37 ? 412  ASN B O   1 
ATOM   3810 C  CB  . ASN B 1 188 ? -6.438  7.402  -31.468 1.00 21.76 ? 412  ASN B CB  1 
ATOM   3811 C  CG  . ASN B 1 188 ? -6.884  6.983  -30.072 1.00 21.32 ? 412  ASN B CG  1 
ATOM   3812 O  OD1 . ASN B 1 188 ? -7.993  6.464  -29.879 1.00 21.12 ? 412  ASN B OD1 1 
ATOM   3813 N  ND2 . ASN B 1 188 ? -6.022  7.227  -29.085 1.00 19.47 ? 412  ASN B ND2 1 
ATOM   3814 N  N   . ASN B 1 189 ? -7.707  8.381  -34.327 1.00 21.89 ? 413  ASN B N   1 
ATOM   3815 C  CA  . ASN B 1 189 ? -7.344  9.185  -35.485 1.00 26.21 ? 413  ASN B CA  1 
ATOM   3816 C  C   . ASN B 1 189 ? -7.676  10.645 -35.218 1.00 21.40 ? 413  ASN B C   1 
ATOM   3817 O  O   . ASN B 1 189 ? -8.305  10.986 -34.215 1.00 22.86 ? 413  ASN B O   1 
ATOM   3818 C  CB  . ASN B 1 189 ? -8.017  8.690  -36.778 1.00 32.61 ? 413  ASN B CB  1 
ATOM   3819 C  CG  . ASN B 1 189 ? -9.542  8.674  -36.700 1.00 35.28 ? 413  ASN B CG  1 
ATOM   3820 O  OD1 . ASN B 1 189 ? -10.160 9.426  -35.939 1.00 34.90 ? 413  ASN B OD1 1 
ATOM   3821 N  ND2 . ASN B 1 189 ? -10.159 7.806  -37.508 1.00 38.33 ? 413  ASN B ND2 1 
ATOM   3822 N  N   . HIS B 1 190 ? -7.205  11.513 -36.121 1.00 26.57 ? 414  HIS B N   1 
ATOM   3823 C  CA  . HIS B 1 190 ? -7.425  12.962 -36.045 1.00 26.37 ? 414  HIS B CA  1 
ATOM   3824 C  C   . HIS B 1 190 ? -6.852  13.579 -34.768 1.00 21.57 ? 414  HIS B C   1 
ATOM   3825 O  O   . HIS B 1 190 ? -7.335  14.610 -34.305 1.00 22.06 ? 414  HIS B O   1 
ATOM   3826 C  CB  . HIS B 1 190 ? -8.914  13.312 -36.165 1.00 27.01 ? 414  HIS B CB  1 
ATOM   3827 C  CG  . HIS B 1 190 ? -9.500  12.991 -37.504 1.00 33.07 ? 414  HIS B CG  1 
ATOM   3828 N  ND1 . HIS B 1 190 ? -10.295 11.885 -37.723 1.00 32.51 ? 414  HIS B ND1 1 
ATOM   3829 C  CD2 . HIS B 1 190 ? -9.388  13.618 -38.700 1.00 31.48 ? 414  HIS B CD2 1 
ATOM   3830 C  CE1 . HIS B 1 190 ? -10.651 11.847 -38.995 1.00 34.15 ? 414  HIS B CE1 1 
ATOM   3831 N  NE2 . HIS B 1 190 ? -10.118 12.889 -39.608 1.00 40.48 ? 414  HIS B NE2 1 
ATOM   3832 N  N   . LEU B 1 191 ? -5.822  12.972 -34.185 1.00 18.32 ? 415  LEU B N   1 
ATOM   3833 C  CA  . LEU B 1 191 ? -5.251  13.510 -32.955 1.00 19.24 ? 415  LEU B CA  1 
ATOM   3834 C  C   . LEU B 1 191 ? -4.519  14.827 -33.200 1.00 20.19 ? 415  LEU B C   1 
ATOM   3835 O  O   . LEU B 1 191 ? -3.862  15.011 -34.227 1.00 23.74 ? 415  LEU B O   1 
ATOM   3836 C  CB  . LEU B 1 191 ? -4.290  12.504 -32.328 1.00 20.62 ? 415  LEU B CB  1 
ATOM   3837 C  CG  . LEU B 1 191 ? -4.874  11.227 -31.722 1.00 18.33 ? 415  LEU B CG  1 
ATOM   3838 C  CD1 . LEU B 1 191 ? -3.751  10.238 -31.463 1.00 19.47 ? 415  LEU B CD1 1 
ATOM   3839 C  CD2 . LEU B 1 191 ? -5.603  11.533 -30.437 1.00 18.71 ? 415  LEU B CD2 1 
ATOM   3840 N  N   . ALA B 1 192 ? -4.640  15.752 -32.252 1.00 16.83 ? 416  ALA B N   1 
ATOM   3841 C  CA  . ALA B 1 192 ? -3.705  16.869 -32.212 1.00 21.68 ? 416  ALA B CA  1 
ATOM   3842 C  C   . ALA B 1 192 ? -2.297  16.309 -32.026 1.00 19.70 ? 416  ALA B C   1 
ATOM   3843 O  O   . ALA B 1 192 ? -2.131  15.294 -31.339 1.00 21.17 ? 416  ALA B O   1 
ATOM   3844 C  CB  . ALA B 1 192 ? -4.049  17.833 -31.077 1.00 17.42 ? 416  ALA B CB  1 
ATOM   3845 N  N   . PRO B 1 193 ? -1.276  16.888 -32.661 1.00 17.51 ? 417  PRO B N   1 
ATOM   3846 C  CA  . PRO B 1 193 ? 0.047   16.250 -32.640 1.00 19.62 ? 417  PRO B CA  1 
ATOM   3847 C  C   . PRO B 1 193 ? 0.733   16.411 -31.296 1.00 21.09 ? 417  PRO B C   1 
ATOM   3848 O  O   . PRO B 1 193 ? 0.429   17.318 -30.519 1.00 17.94 ? 417  PRO B O   1 
ATOM   3849 C  CB  . PRO B 1 193 ? 0.821   16.988 -33.733 1.00 19.18 ? 417  PRO B CB  1 
ATOM   3850 C  CG  . PRO B 1 193 ? 0.204   18.326 -33.757 1.00 20.96 ? 417  PRO B CG  1 
ATOM   3851 C  CD  . PRO B 1 193 ? -1.276  18.077 -33.525 1.00 23.36 ? 417  PRO B CD  1 
ATOM   3852 N  N   . ALA B 1 194 ? 1.685   15.506 -31.035 1.00 18.52 ? 418  ALA B N   1 
ATOM   3853 C  CA  . ALA B 1 194 ? 2.525   15.646 -29.859 1.00 18.47 ? 418  ALA B CA  1 
ATOM   3854 C  C   . ALA B 1 194 ? 3.358   16.918 -29.979 1.00 21.06 ? 418  ALA B C   1 
ATOM   3855 O  O   . ALA B 1 194 ? 3.616   17.413 -31.076 1.00 18.64 ? 418  ALA B O   1 
ATOM   3856 C  CB  . ALA B 1 194 ? 3.437   14.426 -29.699 1.00 21.05 ? 418  ALA B CB  1 
ATOM   3857 N  N   . VAL B 1 195 ? 3.767   17.456 -28.838 1.00 22.83 ? 419  VAL B N   1 
ATOM   3858 C  CA  . VAL B 1 195 ? 4.585   18.661 -28.799 1.00 25.27 ? 419  VAL B CA  1 
ATOM   3859 C  C   . VAL B 1 195 ? 5.823   18.369 -27.976 1.00 23.02 ? 419  VAL B C   1 
ATOM   3860 O  O   . VAL B 1 195 ? 5.800   17.547 -27.053 1.00 25.27 ? 419  VAL B O   1 
ATOM   3861 C  CB  . VAL B 1 195 ? 3.824   19.862 -28.213 1.00 22.94 ? 419  VAL B CB  1 
ATOM   3862 C  CG1 . VAL B 1 195 ? 2.656   20.222 -29.120 1.00 22.54 ? 419  VAL B CG1 1 
ATOM   3863 C  CG2 . VAL B 1 195 ? 3.350   19.525 -26.804 1.00 17.76 ? 419  VAL B CG2 1 
ATOM   3864 N  N   . SER B 1 196 ? 6.919   19.037 -28.322 1.00 23.60 ? 420  SER B N   1 
ATOM   3865 C  CA  . SER B 1 196 ? 8.154   18.853 -27.572 1.00 28.10 ? 420  SER B CA  1 
ATOM   3866 C  C   . SER B 1 196 ? 9.022   20.085 -27.764 1.00 26.42 ? 420  SER B C   1 
ATOM   3867 O  O   . SER B 1 196 ? 8.875   20.793 -28.768 1.00 26.71 ? 420  SER B O   1 
ATOM   3868 C  CB  . SER B 1 196 ? 8.902   17.585 -28.018 1.00 28.81 ? 420  SER B CB  1 
ATOM   3869 O  OG  . SER B 1 196 ? 9.338   17.677 -29.363 1.00 32.47 ? 420  SER B OG  1 
ATOM   3870 N  N   . PRO B 1 197 ? 9.912   20.383 -26.821 1.00 23.10 ? 421  PRO B N   1 
ATOM   3871 C  CA  . PRO B 1 197 ? 10.859  21.484 -27.037 1.00 31.64 ? 421  PRO B CA  1 
ATOM   3872 C  C   . PRO B 1 197 ? 11.935  21.029 -28.013 1.00 27.54 ? 421  PRO B C   1 
ATOM   3873 O  O   . PRO B 1 197 ? 12.547  19.974 -27.831 1.00 27.86 ? 421  PRO B O   1 
ATOM   3874 C  CB  . PRO B 1 197 ? 11.434  21.738 -25.639 1.00 26.04 ? 421  PRO B CB  1 
ATOM   3875 C  CG  . PRO B 1 197 ? 11.392  20.384 -24.987 1.00 27.89 ? 421  PRO B CG  1 
ATOM   3876 C  CD  . PRO B 1 197 ? 10.159  19.684 -25.548 1.00 24.00 ? 421  PRO B CD  1 
ATOM   3877 N  N   . LEU B 1 198 ? 12.142  21.807 -29.069 1.00 26.32 ? 422  LEU B N   1 
ATOM   3878 C  CA  . LEU B 1 198 ? 13.136  21.443 -30.072 1.00 28.03 ? 422  LEU B CA  1 
ATOM   3879 C  C   . LEU B 1 198 ? 14.465  22.166 -29.900 1.00 28.73 ? 422  LEU B C   1 
ATOM   3880 O  O   . LEU B 1 198 ? 15.478  21.699 -30.431 1.00 27.92 ? 422  LEU B O   1 
ATOM   3881 C  CB  . LEU B 1 198 ? 12.590  21.726 -31.476 1.00 28.99 ? 422  LEU B CB  1 
ATOM   3882 C  CG  . LEU B 1 198 ? 11.231  21.062 -31.702 1.00 33.55 ? 422  LEU B CG  1 
ATOM   3883 C  CD1 . LEU B 1 198 ? 10.611  21.516 -33.028 1.00 37.25 ? 422  LEU B CD1 1 
ATOM   3884 C  CD2 . LEU B 1 198 ? 11.383  19.547 -31.643 1.00 29.59 ? 422  LEU B CD2 1 
ATOM   3885 N  N   . PHE B 1 199 ? 14.486  23.286 -29.174 1.00 24.43 ? 423  PHE B N   1 
ATOM   3886 C  CA  . PHE B 1 199 ? 15.660  24.145 -29.076 1.00 30.40 ? 423  PHE B CA  1 
ATOM   3887 C  C   . PHE B 1 199 ? 16.489  23.804 -27.839 1.00 27.26 ? 423  PHE B C   1 
ATOM   3888 O  O   . PHE B 1 199 ? 15.929  23.584 -26.760 1.00 26.94 ? 423  PHE B O   1 
ATOM   3889 C  CB  . PHE B 1 199 ? 15.227  25.614 -29.028 1.00 31.83 ? 423  PHE B CB  1 
ATOM   3890 C  CG  . PHE B 1 199 ? 16.330  26.570 -29.347 1.00 32.24 ? 423  PHE B CG  1 
ATOM   3891 C  CD1 . PHE B 1 199 ? 16.940  26.546 -30.589 1.00 36.73 ? 423  PHE B CD1 1 
ATOM   3892 C  CD2 . PHE B 1 199 ? 16.760  27.489 -28.406 1.00 34.53 ? 423  PHE B CD2 1 
ATOM   3893 C  CE1 . PHE B 1 199 ? 17.970  27.420 -30.885 1.00 39.12 ? 423  PHE B CE1 1 
ATOM   3894 C  CE2 . PHE B 1 199 ? 17.781  28.374 -28.695 1.00 32.45 ? 423  PHE B CE2 1 
ATOM   3895 C  CZ  . PHE B 1 199 ? 18.387  28.338 -29.934 1.00 38.09 ? 423  PHE B CZ  1 
ATOM   3896 N  N   . PRO B 1 200 ? 17.816  23.725 -27.953 1.00 29.12 ? 424  PRO B N   1 
ATOM   3897 C  CA  . PRO B 1 200 ? 18.635  23.312 -26.804 1.00 30.67 ? 424  PRO B CA  1 
ATOM   3898 C  C   . PRO B 1 200 ? 18.377  24.166 -25.568 1.00 31.52 ? 424  PRO B C   1 
ATOM   3899 O  O   . PRO B 1 200 ? 18.252  25.391 -25.649 1.00 30.97 ? 424  PRO B O   1 
ATOM   3900 C  CB  . PRO B 1 200 ? 20.070  23.483 -27.312 1.00 30.86 ? 424  PRO B CB  1 
ATOM   3901 C  CG  . PRO B 1 200 ? 19.964  23.327 -28.794 1.00 31.16 ? 424  PRO B CG  1 
ATOM   3902 C  CD  . PRO B 1 200 ? 18.627  23.923 -29.167 1.00 30.67 ? 424  PRO B CD  1 
ATOM   3903 N  N   . GLY B 1 201 ? 18.283  23.496 -24.418 1.00 29.78 ? 425  GLY B N   1 
ATOM   3904 C  CA  . GLY B 1 201 ? 18.080  24.145 -23.140 1.00 29.36 ? 425  GLY B CA  1 
ATOM   3905 C  C   . GLY B 1 201 ? 16.661  24.583 -22.848 1.00 28.26 ? 425  GLY B C   1 
ATOM   3906 O  O   . GLY B 1 201 ? 16.431  25.258 -21.837 1.00 29.35 ? 425  GLY B O   1 
ATOM   3907 N  N   . GLU B 1 202 ? 15.706  24.246 -23.697 1.00 24.20 ? 426  GLU B N   1 
ATOM   3908 C  CA  . GLU B 1 202 ? 14.332  24.671 -23.509 1.00 26.85 ? 426  GLU B CA  1 
ATOM   3909 C  C   . GLU B 1 202 ? 13.481  23.494 -23.056 1.00 27.00 ? 426  GLU B C   1 
ATOM   3910 O  O   . GLU B 1 202 ? 13.747  22.338 -23.403 1.00 22.66 ? 426  GLU B O   1 
ATOM   3911 C  CB  . GLU B 1 202 ? 13.765  25.285 -24.798 1.00 27.99 ? 426  GLU B CB  1 
ATOM   3912 C  CG  . GLU B 1 202 ? 14.383  26.654 -25.149 1.00 25.89 ? 426  GLU B CG  1 
ATOM   3913 C  CD  . GLU B 1 202 ? 13.617  27.419 -26.245 1.00 27.34 ? 426  GLU B CD  1 
ATOM   3914 O  OE1 . GLU B 1 202 ? 12.517  26.977 -26.659 1.00 29.67 ? 426  GLU B OE1 1 
ATOM   3915 O  OE2 . GLU B 1 202 ? 14.124  28.466 -26.702 1.00 27.86 ? 426  GLU B OE2 1 
ATOM   3916 N  N   . GLN B 1 203 ? 12.457  23.800 -22.263 1.00 27.49 ? 427  GLN B N   1 
ATOM   3917 C  CA  . GLN B 1 203 ? 11.472  22.814 -21.845 1.00 20.86 ? 427  GLN B CA  1 
ATOM   3918 C  C   . GLN B 1 203 ? 10.089  23.418 -22.001 1.00 21.89 ? 427  GLN B C   1 
ATOM   3919 O  O   . GLN B 1 203 ? 9.923   24.637 -21.989 1.00 20.21 ? 427  GLN B O   1 
ATOM   3920 C  CB  . GLN B 1 203 ? 11.692  22.364 -20.391 1.00 21.09 ? 427  GLN B CB  1 
ATOM   3921 C  CG  . GLN B 1 203 ? 13.004  21.603 -20.179 1.00 22.98 ? 427  GLN B CG  1 
ATOM   3922 C  CD  . GLN B 1 203 ? 13.150  21.054 -18.775 1.00 25.96 ? 427  GLN B CD  1 
ATOM   3923 O  OE1 . GLN B 1 203 ? 13.940  20.142 -18.532 1.00 26.42 ? 427  GLN B OE1 1 
ATOM   3924 N  NE2 . GLN B 1 203 ? 12.379  21.599 -17.846 1.00 23.93 ? 427  GLN B NE2 1 
ATOM   3925 N  N   . ILE B 1 204 ? 9.090   22.558 -22.139 1.00 19.80 ? 428  ILE B N   1 
ATOM   3926 C  CA  . ILE B 1 204 ? 7.718   23.045 -22.158 1.00 19.15 ? 428  ILE B CA  1 
ATOM   3927 C  C   . ILE B 1 204 ? 7.357   23.616 -20.789 1.00 20.38 ? 428  ILE B C   1 
ATOM   3928 O  O   . ILE B 1 204 ? 7.753   23.087 -19.742 1.00 19.19 ? 428  ILE B O   1 
ATOM   3929 C  CB  . ILE B 1 204 ? 6.755   21.922 -22.583 1.00 22.16 ? 428  ILE B CB  1 
ATOM   3930 C  CG1 . ILE B 1 204 ? 6.971   21.578 -24.066 1.00 22.44 ? 428  ILE B CG1 1 
ATOM   3931 C  CG2 . ILE B 1 204 ? 5.309   22.345 -22.357 1.00 18.17 ? 428  ILE B CG2 1 
ATOM   3932 C  CD1 . ILE B 1 204 ? 6.185   20.359 -24.562 1.00 18.58 ? 428  ILE B CD1 1 
ATOM   3933 N  N   . LEU B 1 205 ? 6.652   24.746 -20.797 1.00 18.96 ? 429  LEU B N   1 
ATOM   3934 C  CA  . LEU B 1 205 ? 6.073   25.340 -19.601 1.00 18.60 ? 429  LEU B CA  1 
ATOM   3935 C  C   . LEU B 1 205 ? 4.622   24.887 -19.512 1.00 19.16 ? 429  LEU B C   1 
ATOM   3936 O  O   . LEU B 1 205 ? 3.848   25.127 -20.439 1.00 19.84 ? 429  LEU B O   1 
ATOM   3937 C  CB  . LEU B 1 205 ? 6.153   26.867 -19.663 1.00 21.88 ? 429  LEU B CB  1 
ATOM   3938 C  CG  . LEU B 1 205 ? 5.481   27.614 -18.507 1.00 23.43 ? 429  LEU B CG  1 
ATOM   3939 C  CD1 . LEU B 1 205 ? 6.206   27.250 -17.236 1.00 24.62 ? 429  LEU B CD1 1 
ATOM   3940 C  CD2 . LEU B 1 205 ? 5.522   29.118 -18.711 1.00 26.27 ? 429  LEU B CD2 1 
ATOM   3941 N  N   . PHE B 1 206 ? 4.265   24.208 -18.425 1.00 17.91 ? 430  PHE B N   1 
ATOM   3942 C  CA  . PHE B 1 206 ? 2.902   23.734 -18.224 1.00 20.94 ? 430  PHE B CA  1 
ATOM   3943 C  C   . PHE B 1 206 ? 2.159   24.580 -17.202 1.00 19.56 ? 430  PHE B C   1 
ATOM   3944 O  O   . PHE B 1 206 ? 2.753   25.239 -16.346 1.00 22.49 ? 430  PHE B O   1 
ATOM   3945 C  CB  . PHE B 1 206 ? 2.873   22.287 -17.734 1.00 20.79 ? 430  PHE B CB  1 
ATOM   3946 C  CG  . PHE B 1 206 ? 3.540   21.319 -18.655 1.00 22.42 ? 430  PHE B CG  1 
ATOM   3947 C  CD1 . PHE B 1 206 ? 4.916   21.114 -18.590 1.00 21.67 ? 430  PHE B CD1 1 
ATOM   3948 C  CD2 . PHE B 1 206 ? 2.794   20.604 -19.566 1.00 19.63 ? 430  PHE B CD2 1 
ATOM   3949 C  CE1 . PHE B 1 206 ? 5.534   20.214 -19.437 1.00 23.21 ? 430  PHE B CE1 1 
ATOM   3950 C  CE2 . PHE B 1 206 ? 3.405   19.687 -20.414 1.00 21.70 ? 430  PHE B CE2 1 
ATOM   3951 C  CZ  . PHE B 1 206 ? 4.767   19.494 -20.349 1.00 20.51 ? 430  PHE B CZ  1 
ATOM   3952 N  N   . PHE B 1 207 ? 0.837   24.510 -17.273 1.00 20.06 ? 431  PHE B N   1 
ATOM   3953 C  CA  . PHE B 1 207 ? -0.030  25.091 -16.259 1.00 18.57 ? 431  PHE B CA  1 
ATOM   3954 C  C   . PHE B 1 207 ? -0.658  23.933 -15.495 1.00 19.69 ? 431  PHE B C   1 
ATOM   3955 O  O   . PHE B 1 207 ? -1.495  23.196 -16.031 1.00 20.00 ? 431  PHE B O   1 
ATOM   3956 C  CB  . PHE B 1 207 ? -1.054  26.018 -16.898 1.00 16.39 ? 431  PHE B CB  1 
ATOM   3957 C  CG  . PHE B 1 207 ? -0.418  27.168 -17.634 1.00 20.31 ? 431  PHE B CG  1 
ATOM   3958 C  CD1 . PHE B 1 207 ? 0.034   27.005 -18.935 1.00 19.64 ? 431  PHE B CD1 1 
ATOM   3959 C  CD2 . PHE B 1 207 ? -0.216  28.389 -17.000 1.00 21.74 ? 431  PHE B CD2 1 
ATOM   3960 C  CE1 . PHE B 1 207 ? 0.645   28.044 -19.605 1.00 22.50 ? 431  PHE B CE1 1 
ATOM   3961 C  CE2 . PHE B 1 207 ? 0.388   29.448 -17.664 1.00 22.02 ? 431  PHE B CE2 1 
ATOM   3962 C  CZ  . PHE B 1 207 ? 0.825   29.270 -18.972 1.00 25.33 ? 431  PHE B CZ  1 
ATOM   3963 N  N   . ARG B 1 208 ? -0.247  23.778 -14.248 1.00 19.65 ? 432  ARG B N   1 
ATOM   3964 C  CA  . ARG B 1 208 ? -0.525  22.587 -13.471 1.00 17.75 ? 432  ARG B CA  1 
ATOM   3965 C  C   . ARG B 1 208 ? -1.637  22.852 -12.470 1.00 19.36 ? 432  ARG B C   1 
ATOM   3966 O  O   . ARG B 1 208 ? -1.675  23.910 -11.836 1.00 19.05 ? 432  ARG B O   1 
ATOM   3967 C  CB  . ARG B 1 208 ? 0.743   22.130 -12.752 1.00 20.85 ? 432  ARG B CB  1 
ATOM   3968 C  CG  . ARG B 1 208 ? 0.505   21.198 -11.587 1.00 21.36 ? 432  ARG B CG  1 
ATOM   3969 C  CD  . ARG B 1 208 ? 1.809   20.542 -11.157 1.00 23.34 ? 432  ARG B CD  1 
ATOM   3970 N  NE  . ARG B 1 208 ? 2.259   19.595 -12.166 1.00 21.49 ? 432  ARG B NE  1 
ATOM   3971 C  CZ  . ARG B 1 208 ? 3.170   18.654 -11.960 1.00 25.88 ? 432  ARG B CZ  1 
ATOM   3972 N  NH1 . ARG B 1 208 ? 3.789   18.534 -10.794 1.00 21.95 ? 432  ARG B NH1 1 
ATOM   3973 N  NH2 . ARG B 1 208 ? 3.444   17.793 -12.938 1.00 25.56 ? 432  ARG B NH2 1 
ATOM   3974 N  N   . SER B 1 209 ? -2.539  21.882 -12.345 1.00 18.13 ? 433  SER B N   1 
ATOM   3975 C  CA  . SER B 1 209 ? -3.553  21.830 -11.302 1.00 18.77 ? 433  SER B CA  1 
ATOM   3976 C  C   . SER B 1 209 ? -3.410  20.530 -10.529 1.00 20.30 ? 433  SER B C   1 
ATOM   3977 O  O   . SER B 1 209 ? -3.068  19.491 -11.094 1.00 18.48 ? 433  SER B O   1 
ATOM   3978 C  CB  . SER B 1 209 ? -4.984  21.887 -11.874 1.00 20.11 ? 433  SER B CB  1 
ATOM   3979 O  OG  . SER B 1 209 ? -5.211  23.071 -12.593 1.00 19.44 ? 433  SER B OG  1 
ATOM   3980 N  N   . PHE B 1 210 ? -3.712  20.584 -9.240  1.00 22.63 ? 434  PHE B N   1 
ATOM   3981 C  CA  . PHE B 1 210 ? -3.802  19.387 -8.410  1.00 19.96 ? 434  PHE B CA  1 
ATOM   3982 C  C   . PHE B 1 210 ? -5.285  19.068 -8.259  1.00 18.43 ? 434  PHE B C   1 
ATOM   3983 O  O   . PHE B 1 210 ? -5.987  19.704 -7.468  1.00 19.08 ? 434  PHE B O   1 
ATOM   3984 C  CB  . PHE B 1 210 ? -3.112  19.622 -7.073  1.00 23.41 ? 434  PHE B CB  1 
ATOM   3985 C  CG  . PHE B 1 210 ? -1.714  20.156 -7.216  1.00 21.90 ? 434  PHE B CG  1 
ATOM   3986 C  CD1 . PHE B 1 210 ? -0.680  19.326 -7.618  1.00 21.04 ? 434  PHE B CD1 1 
ATOM   3987 C  CD2 . PHE B 1 210 ? -1.441  21.489 -6.978  1.00 25.97 ? 434  PHE B CD2 1 
ATOM   3988 C  CE1 . PHE B 1 210 ? 0.623   19.813 -7.759  1.00 25.06 ? 434  PHE B CE1 1 
ATOM   3989 C  CE2 . PHE B 1 210 ? -0.140  21.987 -7.109  1.00 25.97 ? 434  PHE B CE2 1 
ATOM   3990 C  CZ  . PHE B 1 210 ? 0.890   21.148 -7.501  1.00 26.49 ? 434  PHE B CZ  1 
ATOM   3991 N  N   . ILE B 1 211 ? -5.773  18.101 -9.034  1.00 20.52 ? 435  ILE B N   1 
ATOM   3992 C  CA  . ILE B 1 211 ? -7.214  17.827 -9.053  1.00 18.18 ? 435  ILE B CA  1 
ATOM   3993 C  C   . ILE B 1 211 ? -7.555  16.949 -7.854  1.00 19.70 ? 435  ILE B C   1 
ATOM   3994 O  O   . ILE B 1 211 ? -6.666  16.296 -7.294  1.00 17.45 ? 435  ILE B O   1 
ATOM   3995 C  CB  . ILE B 1 211 ? -7.664  17.188 -10.387 1.00 19.84 ? 435  ILE B CB  1 
ATOM   3996 C  CG1 . ILE B 1 211 ? -7.232  15.723 -10.490 1.00 20.66 ? 435  ILE B CG1 1 
ATOM   3997 C  CG2 . ILE B 1 211 ? -7.127  17.982 -11.586 1.00 18.90 ? 435  ILE B CG2 1 
ATOM   3998 C  CD1 . ILE B 1 211 ? -7.634  15.068 -11.814 1.00 20.37 ? 435  ILE B CD1 1 
ATOM   3999 N  N   . PRO B 1 212 ? -8.812  16.920 -7.411  1.00 18.40 ? 436  PRO B N   1 
ATOM   4000 C  CA  . PRO B 1 212 ? -9.166  16.116 -6.233  1.00 19.48 ? 436  PRO B CA  1 
ATOM   4001 C  C   . PRO B 1 212 ? -8.966  14.623 -6.453  1.00 20.83 ? 436  PRO B C   1 
ATOM   4002 O  O   . PRO B 1 212 ? -9.122  14.106 -7.565  1.00 22.53 ? 436  PRO B O   1 
ATOM   4003 C  CB  . PRO B 1 212 ? -10.651 16.444 -6.015  1.00 17.85 ? 436  PRO B CB  1 
ATOM   4004 C  CG  . PRO B 1 212 ? -10.799 17.832 -6.592  1.00 20.52 ? 436  PRO B CG  1 
ATOM   4005 C  CD  . PRO B 1 212 ? -9.892  17.841 -7.804  1.00 18.39 ? 436  PRO B CD  1 
ATOM   4006 N  N   . GLY B 1 213 ? -8.641  13.931 -5.365  1.00 22.26 ? 437  GLY B N   1 
ATOM   4007 C  CA  . GLY B 1 213 ? -8.582  12.471 -5.335  1.00 20.67 ? 437  GLY B CA  1 
ATOM   4008 C  C   . GLY B 1 213 ? -9.703  11.941 -4.458  1.00 24.05 ? 437  GLY B C   1 
ATOM   4009 O  O   . GLY B 1 213 ? -10.043 12.548 -3.439  1.00 26.92 ? 437  GLY B O   1 
ATOM   4010 N  N   . ALA B 1 214 ? -10.289 10.817 -4.870  1.00 24.49 ? 438  ALA B N   1 
ATOM   4011 C  CA  . ALA B 1 214 ? -11.452 10.276 -4.182  1.00 24.64 ? 438  ALA B CA  1 
ATOM   4012 C  C   . ALA B 1 214 ? -11.128 9.092  -3.287  1.00 27.79 ? 438  ALA B C   1 
ATOM   4013 O  O   . ALA B 1 214 ? -11.953 8.746  -2.435  1.00 29.98 ? 438  ALA B O   1 
ATOM   4014 C  CB  . ALA B 1 214 ? -12.529 9.868  -5.195  1.00 26.16 ? 438  ALA B CB  1 
ATOM   4015 N  N   . SER B 1 215 ? -9.961  8.472  -3.466  1.00 23.53 ? 439  SER B N   1 
ATOM   4016 C  CA  . SER B 1 215 ? -9.431  7.459  -2.562  1.00 30.46 ? 439  SER B CA  1 
ATOM   4017 C  C   . SER B 1 215 ? -8.001  7.179  -2.994  1.00 30.71 ? 439  SER B C   1 
ATOM   4018 O  O   . SER B 1 215 ? -7.578  7.575  -4.081  1.00 27.76 ? 439  SER B O   1 
ATOM   4019 C  CB  . SER B 1 215 ? -10.248 6.167  -2.576  1.00 32.27 ? 439  SER B CB  1 
ATOM   4020 O  OG  . SER B 1 215 ? -10.042 5.500  -3.800  1.00 40.72 ? 439  SER B OG  1 
ATOM   4021 N  N   . GLY B 1 216 ? -7.264  6.482  -2.132  1.00 29.98 ? 440  GLY B N   1 
ATOM   4022 C  CA  . GLY B 1 216 ? -5.907  6.128  -2.474  1.00 26.59 ? 440  GLY B CA  1 
ATOM   4023 C  C   . GLY B 1 216 ? -4.979  7.334  -2.440  1.00 33.23 ? 440  GLY B C   1 
ATOM   4024 O  O   . GLY B 1 216 ? -5.310  8.408  -1.928  1.00 34.64 ? 440  GLY B O   1 
ATOM   4025 N  N   . HIS B 1 217 ? -3.804  7.151  -3.031  1.00 27.89 ? 441  HIS B N   1 
ATOM   4026 C  CA  . HIS B 1 217 ? -2.730  8.132  -2.962  1.00 29.46 ? 441  HIS B CA  1 
ATOM   4027 C  C   . HIS B 1 217 ? -2.475  8.719  -4.341  1.00 30.06 ? 441  HIS B C   1 
ATOM   4028 O  O   . HIS B 1 217 ? -2.180  7.981  -5.288  1.00 31.74 ? 441  HIS B O   1 
ATOM   4029 C  CB  . HIS B 1 217 ? -1.458  7.494  -2.407  1.00 34.98 ? 441  HIS B CB  1 
ATOM   4030 C  CG  . HIS B 1 217 ? -1.558  7.120  -0.962  1.00 33.94 ? 441  HIS B CG  1 
ATOM   4031 N  ND1 . HIS B 1 217 ? -0.910  7.819  0.033   1.00 35.57 ? 441  HIS B ND1 1 
ATOM   4032 C  CD2 . HIS B 1 217 ? -2.245  6.133  -0.342  1.00 36.95 ? 441  HIS B CD2 1 
ATOM   4033 C  CE1 . HIS B 1 217 ? -1.187  7.273  1.203   1.00 38.51 ? 441  HIS B CE1 1 
ATOM   4034 N  NE2 . HIS B 1 217 ? -1.995  6.248  1.003   1.00 40.44 ? 441  HIS B NE2 1 
ATOM   4035 N  N   . THR B 1 218 ? -2.595  10.041 -4.450  1.00 30.03 ? 442  THR B N   1 
ATOM   4036 C  CA  . THR B 1 218 ? -2.257  10.734 -5.685  1.00 28.50 ? 442  THR B CA  1 
ATOM   4037 C  C   . THR B 1 218 ? -2.134  12.226 -5.412  1.00 31.08 ? 442  THR B C   1 
ATOM   4038 O  O   . THR B 1 218 ? -2.879  12.784 -4.601  1.00 24.93 ? 442  THR B O   1 
ATOM   4039 C  CB  . THR B 1 218 ? -3.298  10.488 -6.789  1.00 26.47 ? 442  THR B CB  1 
ATOM   4040 O  OG1 . THR B 1 218 ? -2.935  11.239 -7.955  1.00 28.48 ? 442  THR B OG1 1 
ATOM   4041 C  CG2 . THR B 1 218 ? -4.690  10.906 -6.332  1.00 27.26 ? 442  THR B CG2 1 
ATOM   4042 N  N   . ASN B 1 219 ? -1.191  12.865 -6.097  1.00 27.86 ? 443  ASN B N   1 
ATOM   4043 C  CA  . ASN B 1 219 ? -1.155  14.320 -6.096  1.00 29.24 ? 443  ASN B CA  1 
ATOM   4044 C  C   . ASN B 1 219 ? -2.083  14.941 -7.137  1.00 23.34 ? 443  ASN B C   1 
ATOM   4045 O  O   . ASN B 1 219 ? -2.195  16.167 -7.187  1.00 25.69 ? 443  ASN B O   1 
ATOM   4046 C  CB  . ASN B 1 219 ? 0.280   14.794 -6.296  1.00 30.63 ? 443  ASN B CB  1 
ATOM   4047 C  CG  . ASN B 1 219 ? 1.063   14.761 -5.010  1.00 39.96 ? 443  ASN B CG  1 
ATOM   4048 O  OD1 . ASN B 1 219 ? 0.664   15.381 -4.016  1.00 39.88 ? 443  ASN B OD1 1 
ATOM   4049 N  ND2 . ASN B 1 219 ? 2.159   14.014 -4.998  1.00 37.61 ? 443  ASN B ND2 1 
ATOM   4050 N  N   . GLY B 1 220 ? -2.755  14.136 -7.954  1.00 24.46 ? 444  GLY B N   1 
ATOM   4051 C  CA  . GLY B 1 220 ? -3.725  14.671 -8.899  1.00 22.24 ? 444  GLY B CA  1 
ATOM   4052 C  C   . GLY B 1 220 ? -3.159  15.673 -9.885  1.00 22.51 ? 444  GLY B C   1 
ATOM   4053 O  O   . GLY B 1 220 ? -3.873  16.590 -10.299 1.00 21.82 ? 444  GLY B O   1 
ATOM   4054 N  N   . GLU B 1 221 ? -1.897  15.519 -10.281 1.00 20.61 ? 445  GLU B N   1 
ATOM   4055 C  CA  . GLU B 1 221 ? -1.281  16.475 -11.196 1.00 22.57 ? 445  GLU B CA  1 
ATOM   4056 C  C   . GLU B 1 221 ? -1.891  16.366 -12.594 1.00 23.67 ? 445  GLU B C   1 
ATOM   4057 O  O   . GLU B 1 221 ? -1.942  15.285 -13.189 1.00 23.58 ? 445  GLU B O   1 
ATOM   4058 C  CB  . GLU B 1 221 ? 0.228   16.257 -11.250 1.00 24.73 ? 445  GLU B CB  1 
ATOM   4059 C  CG  . GLU B 1 221 ? 0.922   16.587 -9.950  1.00 24.15 ? 445  GLU B CG  1 
ATOM   4060 C  CD  . GLU B 1 221 ? 2.109   15.678 -9.671  1.00 36.12 ? 445  GLU B CD  1 
ATOM   4061 O  OE1 . GLU B 1 221 ? 2.647   15.069 -10.621 1.00 42.09 ? 445  GLU B OE1 1 
ATOM   4062 O  OE2 . GLU B 1 221 ? 2.501   15.562 -8.496  1.00 35.92 ? 445  GLU B OE2 1 
ATOM   4063 N  N   . MET B 1 222 ? -2.363  17.499 -13.105 1.00 19.73 ? 446  MET B N   1 
ATOM   4064 C  CA  . MET B 1 222 ? -2.945  17.609 -14.438 1.00 20.39 ? 446  MET B CA  1 
ATOM   4065 C  C   . MET B 1 222 ? -2.337  18.848 -15.080 1.00 21.17 ? 446  MET B C   1 
ATOM   4066 O  O   . MET B 1 222 ? -2.610  19.972 -14.644 1.00 19.64 ? 446  MET B O   1 
ATOM   4067 C  CB  . MET B 1 222 ? -4.474  17.719 -14.362 1.00 20.57 ? 446  MET B CB  1 
ATOM   4068 C  CG  . MET B 1 222 ? -5.164  17.910 -15.712 1.00 18.12 ? 446  MET B CG  1 
ATOM   4069 S  SD  . MET B 1 222 ? -5.250  16.339 -16.592 1.00 24.88 ? 446  MET B SD  1 
ATOM   4070 C  CE  . MET B 1 222 ? -6.463  15.483 -15.595 1.00 22.74 ? 446  MET B CE  1 
ATOM   4071 N  N   . ASP B 1 223 ? -1.526  18.650 -16.111 1.00 20.79 ? 447  ASP B N   1 
ATOM   4072 C  CA  . ASP B 1 223 ? -0.749  19.715 -16.733 1.00 20.19 ? 447  ASP B CA  1 
ATOM   4073 C  C   . ASP B 1 223 ? -1.346  20.046 -18.092 1.00 19.37 ? 447  ASP B C   1 
ATOM   4074 O  O   . ASP B 1 223 ? -1.420  19.176 -18.965 1.00 18.67 ? 447  ASP B O   1 
ATOM   4075 C  CB  . ASP B 1 223 ? 0.703   19.282 -16.911 1.00 21.24 ? 447  ASP B CB  1 
ATOM   4076 C  CG  . ASP B 1 223 ? 1.375   18.975 -15.609 1.00 24.67 ? 447  ASP B CG  1 
ATOM   4077 O  OD1 . ASP B 1 223 ? 1.213   19.799 -14.684 1.00 24.21 ? 447  ASP B OD1 1 
ATOM   4078 O  OD2 . ASP B 1 223 ? 2.063   17.925 -15.510 1.00 21.51 ? 447  ASP B OD2 1 
ATOM   4079 N  N   . CYS B 1 224 ? -1.735  21.297 -18.293 1.00 19.66 ? 448  CYS B N   1 
ATOM   4080 C  CA  . CYS B 1 224 ? -2.212  21.695 -19.607 1.00 16.73 ? 448  CYS B CA  1 
ATOM   4081 C  C   . CYS B 1 224 ? -1.208  22.625 -20.285 1.00 18.15 ? 448  CYS B C   1 
ATOM   4082 O  O   . CYS B 1 224 ? -0.314  23.189 -19.651 1.00 17.10 ? 448  CYS B O   1 
ATOM   4083 C  CB  . CYS B 1 224 ? -3.609  22.337 -19.523 1.00 17.24 ? 448  CYS B CB  1 
ATOM   4084 S  SG  . CYS B 1 224 ? -3.743  23.947 -18.742 1.00 21.71 ? 448  CYS B SG  1 
ATOM   4085 N  N   . LEU B 1 225 ? -1.357  22.753 -21.607 1.00 17.90 ? 449  LEU B N   1 
ATOM   4086 C  CA  . LEU B 1 225 ? -0.431  23.547 -22.408 1.00 19.18 ? 449  LEU B CA  1 
ATOM   4087 C  C   . LEU B 1 225 ? -0.787  25.027 -22.414 1.00 17.53 ? 449  LEU B C   1 
ATOM   4088 O  O   . LEU B 1 225 ? 0.105   25.877 -22.535 1.00 20.74 ? 449  LEU B O   1 
ATOM   4089 C  CB  . LEU B 1 225 ? -0.416  23.012 -23.836 1.00 16.38 ? 449  LEU B CB  1 
ATOM   4090 C  CG  . LEU B 1 225 ? 0.066   21.575 -24.008 1.00 17.37 ? 449  LEU B CG  1 
ATOM   4091 C  CD1 . LEU B 1 225 ? 0.074   21.212 -25.484 1.00 18.62 ? 449  LEU B CD1 1 
ATOM   4092 C  CD2 . LEU B 1 225 ? 1.465   21.401 -23.406 1.00 17.62 ? 449  LEU B CD2 1 
ATOM   4093 N  N   . LEU B 1 226 ? -2.075  25.349 -22.311 1.00 17.48 ? 450  LEU B N   1 
ATOM   4094 C  CA  . LEU B 1 226 ? -2.612  26.705 -22.307 1.00 19.16 ? 450  LEU B CA  1 
ATOM   4095 C  C   . LEU B 1 226 ? -3.737  26.747 -21.288 1.00 18.07 ? 450  LEU B C   1 
ATOM   4096 O  O   . LEU B 1 226 ? -4.536  25.804 -21.215 1.00 21.08 ? 450  LEU B O   1 
ATOM   4097 C  CB  . LEU B 1 226 ? -3.177  27.116 -23.673 1.00 20.93 ? 450  LEU B CB  1 
ATOM   4098 C  CG  . LEU B 1 226 ? -2.264  27.203 -24.881 1.00 25.85 ? 450  LEU B CG  1 
ATOM   4099 C  CD1 . LEU B 1 226 ? -3.094  27.434 -26.147 1.00 21.36 ? 450  LEU B CD1 1 
ATOM   4100 C  CD2 . LEU B 1 226 ? -1.268  28.331 -24.648 1.00 22.07 ? 450  LEU B CD2 1 
ATOM   4101 N  N   . PRO B 1 227 ? -3.851  27.813 -20.507 1.00 20.55 ? 451  PRO B N   1 
ATOM   4102 C  CA  . PRO B 1 227 ? -5.061  27.969 -19.701 1.00 18.23 ? 451  PRO B CA  1 
ATOM   4103 C  C   . PRO B 1 227 ? -6.254  28.136 -20.627 1.00 17.70 ? 451  PRO B C   1 
ATOM   4104 O  O   . PRO B 1 227 ? -6.124  28.604 -21.760 1.00 15.27 ? 451  PRO B O   1 
ATOM   4105 C  CB  . PRO B 1 227 ? -4.783  29.228 -18.871 1.00 16.53 ? 451  PRO B CB  1 
ATOM   4106 C  CG  . PRO B 1 227 ? -3.765  29.976 -19.651 1.00 22.17 ? 451  PRO B CG  1 
ATOM   4107 C  CD  . PRO B 1 227 ? -2.937  28.959 -20.366 1.00 21.24 ? 451  PRO B CD  1 
ATOM   4108 N  N   . GLN B 1 228 ? -7.426  27.730 -20.142 1.00 15.40 ? 452  GLN B N   1 
ATOM   4109 C  CA  . GLN B 1 228 ? -8.610  27.798 -20.986 1.00 18.11 ? 452  GLN B CA  1 
ATOM   4110 C  C   . GLN B 1 228 ? -8.895  29.223 -21.454 1.00 17.84 ? 452  GLN B C   1 
ATOM   4111 O  O   . GLN B 1 228 ? -9.470  29.414 -22.531 1.00 18.20 ? 452  GLN B O   1 
ATOM   4112 C  CB  . GLN B 1 228 ? -9.818  27.212 -20.245 1.00 20.59 ? 452  GLN B CB  1 
ATOM   4113 C  CG  . GLN B 1 228 ? -11.090 27.075 -21.101 1.00 16.91 ? 452  GLN B CG  1 
ATOM   4114 C  CD  . GLN B 1 228 ? -10.920 26.114 -22.281 1.00 21.02 ? 452  GLN B CD  1 
ATOM   4115 O  OE1 . GLN B 1 228 ? -9.975  25.333 -22.322 1.00 20.91 ? 452  GLN B OE1 1 
ATOM   4116 N  NE2 . GLN B 1 228 ? -11.847 26.172 -23.246 1.00 15.92 ? 452  GLN B NE2 1 
ATOM   4117 N  N   . GLU B 1 229 ? -8.484  30.234 -20.677 1.00 21.01 ? 453  GLU B N   1 
ATOM   4118 C  CA  . GLU B 1 229 ? -8.711  31.621 -21.082 1.00 17.39 ? 453  GLU B CA  1 
ATOM   4119 C  C   . GLU B 1 229 ? -7.892  31.993 -22.313 1.00 20.53 ? 453  GLU B C   1 
ATOM   4120 O  O   . GLU B 1 229 ? -8.332  32.825 -23.117 1.00 18.60 ? 453  GLU B O   1 
ATOM   4121 C  CB  . GLU B 1 229 ? -8.386  32.579 -19.930 1.00 18.45 ? 453  GLU B CB  1 
ATOM   4122 C  CG  . GLU B 1 229 ? -9.387  32.573 -18.757 1.00 22.77 ? 453  GLU B CG  1 
ATOM   4123 C  CD  . GLU B 1 229 ? -9.246  31.363 -17.819 1.00 21.53 ? 453  GLU B CD  1 
ATOM   4124 O  OE1 . GLU B 1 229 ? -8.229  30.636 -17.889 1.00 19.23 ? 453  GLU B OE1 1 
ATOM   4125 O  OE2 . GLU B 1 229 ? -10.172 31.136 -17.011 1.00 23.35 ? 453  GLU B OE2 1 
ATOM   4126 N  N   . PHE B 1 230 ? -6.704  31.397 -22.487 1.00 17.03 ? 454  PHE B N   1 
ATOM   4127 C  CA  . PHE B 1 230 ? -5.951  31.652 -23.711 1.00 22.15 ? 454  PHE B CA  1 
ATOM   4128 C  C   . PHE B 1 230 ? -6.625  31.005 -24.917 1.00 16.73 ? 454  PHE B C   1 
ATOM   4129 O  O   . PHE B 1 230 ? -6.713  31.612 -25.988 1.00 16.85 ? 454  PHE B O   1 
ATOM   4130 C  CB  . PHE B 1 230 ? -4.513  31.147 -23.586 1.00 15.83 ? 454  PHE B CB  1 
ATOM   4131 C  CG  . PHE B 1 230 ? -3.623  32.017 -22.740 1.00 20.60 ? 454  PHE B CG  1 
ATOM   4132 C  CD1 . PHE B 1 230 ? -4.145  32.980 -21.896 1.00 24.21 ? 454  PHE B CD1 1 
ATOM   4133 C  CD2 . PHE B 1 230 ? -2.254  31.855 -22.787 1.00 27.04 ? 454  PHE B CD2 1 
ATOM   4134 C  CE1 . PHE B 1 230 ? -3.319  33.766 -21.115 1.00 24.45 ? 454  PHE B CE1 1 
ATOM   4135 C  CE2 . PHE B 1 230 ? -1.417  32.641 -22.007 1.00 28.50 ? 454  PHE B CE2 1 
ATOM   4136 C  CZ  . PHE B 1 230 ? -1.948  33.593 -21.174 1.00 22.67 ? 454  PHE B CZ  1 
ATOM   4137 N  N   . VAL B 1 231 ? -7.083  29.763 -24.764 1.00 15.28 ? 455  VAL B N   1 
ATOM   4138 C  CA  . VAL B 1 231 ? -7.870  29.112 -25.815 1.00 17.66 ? 455  VAL B CA  1 
ATOM   4139 C  C   . VAL B 1 231 ? -9.043  29.990 -26.222 1.00 16.76 ? 455  VAL B C   1 
ATOM   4140 O  O   . VAL B 1 231 ? -9.241  30.300 -27.405 1.00 17.54 ? 455  VAL B O   1 
ATOM   4141 C  CB  . VAL B 1 231 ? -8.365  27.738 -25.336 1.00 16.62 ? 455  VAL B CB  1 
ATOM   4142 C  CG1 . VAL B 1 231 ? -9.321  27.153 -26.348 1.00 16.81 ? 455  VAL B CG1 1 
ATOM   4143 C  CG2 . VAL B 1 231 ? -7.175  26.815 -25.064 1.00 21.05 ? 455  VAL B CG2 1 
ATOM   4144 N  N   . GLN B 1 232 ? -9.851  30.387 -25.242 1.00 15.11 ? 456  GLN B N   1 
ATOM   4145 C  CA  . GLN B 1 232 ? -11.012 31.216 -25.540 1.00 16.37 ? 456  GLN B CA  1 
ATOM   4146 C  C   . GLN B 1 232 ? -10.601 32.504 -26.246 1.00 18.99 ? 456  GLN B C   1 
ATOM   4147 O  O   . GLN B 1 232 ? -11.275 32.958 -27.179 1.00 19.36 ? 456  GLN B O   1 
ATOM   4148 C  CB  . GLN B 1 232 ? -11.759 31.529 -24.248 1.00 18.46 ? 456  GLN B CB  1 
ATOM   4149 C  CG  . GLN B 1 232 ? -12.418 30.313 -23.595 1.00 18.41 ? 456  GLN B CG  1 
ATOM   4150 C  CD  . GLN B 1 232 ? -12.888 30.608 -22.178 1.00 20.56 ? 456  GLN B CD  1 
ATOM   4151 O  OE1 . GLN B 1 232 ? -12.171 31.227 -21.388 1.00 22.64 ? 456  GLN B OE1 1 
ATOM   4152 N  NE2 . GLN B 1 232 ? -14.091 30.168 -21.853 1.00 23.78 ? 456  GLN B NE2 1 
ATOM   4153 N  N   . HIS B 1 233 ? -9.477  33.090 -25.832 1.00 16.64 ? 457  HIS B N   1 
ATOM   4154 C  CA  . HIS B 1 233 ? -9.095  34.386 -26.372 1.00 20.87 ? 457  HIS B CA  1 
ATOM   4155 C  C   . HIS B 1 233 ? -8.632  34.268 -27.819 1.00 20.74 ? 457  HIS B C   1 
ATOM   4156 O  O   . HIS B 1 233 ? -9.017  35.081 -28.670 1.00 24.47 ? 457  HIS B O   1 
ATOM   4157 C  CB  . HIS B 1 233 ? -8.009  35.016 -25.502 1.00 19.81 ? 457  HIS B CB  1 
ATOM   4158 C  CG  . HIS B 1 233 ? -7.659  36.412 -25.902 1.00 24.41 ? 457  HIS B CG  1 
ATOM   4159 N  ND1 . HIS B 1 233 ? -8.400  37.507 -25.510 1.00 27.96 ? 457  HIS B ND1 1 
ATOM   4160 C  CD2 . HIS B 1 233 ? -6.650  36.893 -26.665 1.00 23.99 ? 457  HIS B CD2 1 
ATOM   4161 C  CE1 . HIS B 1 233 ? -7.858  38.604 -26.011 1.00 30.60 ? 457  HIS B CE1 1 
ATOM   4162 N  NE2 . HIS B 1 233 ? -6.788  38.260 -26.705 1.00 27.39 ? 457  HIS B NE2 1 
ATOM   4163 N  N   . PHE B 1 234 ? -7.792  33.271 -28.118 1.00 18.91 ? 458  PHE B N   1 
ATOM   4164 C  CA  . PHE B 1 234 ? -7.358  33.075 -29.500 1.00 20.31 ? 458  PHE B CA  1 
ATOM   4165 C  C   . PHE B 1 234 ? -8.539  32.714 -30.387 1.00 18.72 ? 458  PHE B C   1 
ATOM   4166 O  O   . PHE B 1 234 ? -8.600  33.111 -31.558 1.00 19.17 ? 458  PHE B O   1 
ATOM   4167 C  CB  . PHE B 1 234 ? -6.281  31.981 -29.584 1.00 16.26 ? 458  PHE B CB  1 
ATOM   4168 C  CG  . PHE B 1 234 ? -5.080  32.236 -28.705 1.00 19.38 ? 458  PHE B CG  1 
ATOM   4169 C  CD1 . PHE B 1 234 ? -4.686  33.530 -28.394 1.00 19.61 ? 458  PHE B CD1 1 
ATOM   4170 C  CD2 . PHE B 1 234 ? -4.347  31.179 -28.199 1.00 19.64 ? 458  PHE B CD2 1 
ATOM   4171 C  CE1 . PHE B 1 234 ? -3.581  33.760 -27.594 1.00 18.98 ? 458  PHE B CE1 1 
ATOM   4172 C  CE2 . PHE B 1 234 ? -3.250  31.402 -27.400 1.00 20.61 ? 458  PHE B CE2 1 
ATOM   4173 C  CZ  . PHE B 1 234 ? -2.872  32.700 -27.089 1.00 21.31 ? 458  PHE B CZ  1 
ATOM   4174 N  N   . TYR B 1 235 ? -9.474  31.933 -29.855 1.00 18.68 ? 459  TYR B N   1 
ATOM   4175 C  CA  . TYR B 1 235 ? -10.661 31.603 -30.629 1.00 17.48 ? 459  TYR B CA  1 
ATOM   4176 C  C   . TYR B 1 235 ? -11.431 32.862 -30.989 1.00 18.51 ? 459  TYR B C   1 
ATOM   4177 O  O   . TYR B 1 235 ? -11.870 33.025 -32.132 1.00 17.32 ? 459  TYR B O   1 
ATOM   4178 C  CB  . TYR B 1 235 ? -11.543 30.637 -29.845 1.00 18.13 ? 459  TYR B CB  1 
ATOM   4179 C  CG  . TYR B 1 235 ? -12.724 30.161 -30.633 1.00 21.37 ? 459  TYR B CG  1 
ATOM   4180 C  CD1 . TYR B 1 235 ? -12.558 29.252 -31.670 1.00 22.27 ? 459  TYR B CD1 1 
ATOM   4181 C  CD2 . TYR B 1 235 ? -14.008 30.613 -30.349 1.00 25.14 ? 459  TYR B CD2 1 
ATOM   4182 C  CE1 . TYR B 1 235 ? -13.630 28.796 -32.398 1.00 26.05 ? 459  TYR B CE1 1 
ATOM   4183 C  CE2 . TYR B 1 235 ? -15.099 30.158 -31.080 1.00 28.13 ? 459  TYR B CE2 1 
ATOM   4184 C  CZ  . TYR B 1 235 ? -14.898 29.249 -32.102 1.00 31.59 ? 459  TYR B CZ  1 
ATOM   4185 O  OH  . TYR B 1 235 ? -15.967 28.786 -32.844 1.00 46.58 ? 459  TYR B OH  1 
ATOM   4186 N  N   . GLN B 1 236 ? -11.591 33.767 -30.021 1.00 19.52 ? 460  GLN B N   1 
ATOM   4187 C  CA  . GLN B 1 236 ? -12.276 35.034 -30.263 1.00 22.77 ? 460  GLN B CA  1 
ATOM   4188 C  C   . GLN B 1 236 ? -11.518 35.903 -31.259 1.00 25.19 ? 460  GLN B C   1 
ATOM   4189 O  O   . GLN B 1 236 ? -12.115 36.483 -32.174 1.00 21.06 ? 460  GLN B O   1 
ATOM   4190 C  CB  . GLN B 1 236 ? -12.452 35.792 -28.944 1.00 21.99 ? 460  GLN B CB  1 
ATOM   4191 C  CG  . GLN B 1 236 ? -13.574 35.270 -28.062 1.00 23.30 ? 460  GLN B CG  1 
ATOM   4192 C  CD  . GLN B 1 236 ? -14.903 35.277 -28.778 1.00 24.97 ? 460  GLN B CD  1 
ATOM   4193 O  OE1 . GLN B 1 236 ? -15.268 36.265 -29.419 1.00 24.79 ? 460  GLN B OE1 1 
ATOM   4194 N  NE2 . GLN B 1 236 ? -15.636 34.166 -28.683 1.00 21.52 ? 460  GLN B NE2 1 
ATOM   4195 N  N   . GLU B 1 237 ? -10.199 36.019 -31.088 1.00 20.13 ? 461  GLU B N   1 
ATOM   4196 C  CA  . GLU B 1 237 ? -9.452  37.039 -31.816 1.00 22.94 ? 461  GLU B CA  1 
ATOM   4197 C  C   . GLU B 1 237 ? -9.062  36.579 -33.210 1.00 24.70 ? 461  GLU B C   1 
ATOM   4198 O  O   . GLU B 1 237 ? -9.125  37.367 -34.159 1.00 24.71 ? 461  GLU B O   1 
ATOM   4199 C  CB  . GLU B 1 237 ? -8.207  37.446 -31.026 1.00 26.67 ? 461  GLU B CB  1 
ATOM   4200 C  CG  . GLU B 1 237 ? -8.533  38.192 -29.752 1.00 27.24 ? 461  GLU B CG  1 
ATOM   4201 C  CD  . GLU B 1 237 ? -9.119  39.567 -30.032 1.00 33.48 ? 461  GLU B CD  1 
ATOM   4202 O  OE1 . GLU B 1 237 ? -8.497  40.327 -30.810 1.00 35.77 ? 461  GLU B OE1 1 
ATOM   4203 O  OE2 . GLU B 1 237 ? -10.198 39.888 -29.488 1.00 36.64 ? 461  GLU B OE2 1 
ATOM   4204 N  N   . ALA B 1 238 ? -8.654  35.317 -33.347 1.00 20.69 ? 462  ALA B N   1 
ATOM   4205 C  CA  . ALA B 1 238 ? -8.122  34.780 -34.598 1.00 26.64 ? 462  ALA B CA  1 
ATOM   4206 C  C   . ALA B 1 238 ? -7.148  35.761 -35.246 1.00 24.98 ? 462  ALA B C   1 
ATOM   4207 O  O   . ALA B 1 238 ? -7.242  36.080 -36.431 1.00 29.54 ? 462  ALA B O   1 
ATOM   4208 C  CB  . ALA B 1 238 ? -9.248  34.410 -35.560 1.00 24.27 ? 462  ALA B CB  1 
ATOM   4209 N  N   . ALA B 1 239 ? -6.215  36.270 -34.444 1.00 28.59 ? 463  ALA B N   1 
ATOM   4210 C  CA  . ALA B 1 239 ? -5.251  37.240 -34.951 1.00 27.87 ? 463  ALA B CA  1 
ATOM   4211 C  C   . ALA B 1 239 ? -4.207  36.548 -35.814 1.00 28.14 ? 463  ALA B C   1 
ATOM   4212 O  O   . ALA B 1 239 ? -3.823  35.411 -35.558 1.00 26.82 ? 463  ALA B O   1 
ATOM   4213 C  CB  . ALA B 1 239 ? -4.560  37.983 -33.809 1.00 29.35 ? 463  ALA B CB  1 
ATOM   4214 N  N   . THR B 1 240 ? -3.743  37.252 -36.842 1.00 27.87 ? 464  THR B N   1 
ATOM   4215 C  CA  . THR B 1 240 ? -2.724  36.706 -37.726 1.00 31.63 ? 464  THR B CA  1 
ATOM   4216 C  C   . THR B 1 240 ? -1.419  36.507 -36.970 1.00 30.29 ? 464  THR B C   1 
ATOM   4217 O  O   . THR B 1 240 ? -0.946  37.416 -36.283 1.00 25.67 ? 464  THR B O   1 
ATOM   4218 C  CB  . THR B 1 240 ? -2.494  37.642 -38.911 1.00 36.25 ? 464  THR B CB  1 
ATOM   4219 O  OG1 . THR B 1 240 ? -3.755  37.982 -39.497 1.00 41.61 ? 464  THR B OG1 1 
ATOM   4220 C  CG2 . THR B 1 240 ? -1.602  36.977 -39.955 1.00 36.06 ? 464  THR B CG2 1 
ATOM   4221 N  N   . ALA B 1 241 ? -0.846  35.310 -37.085 1.00 23.85 ? 465  ALA B N   1 
ATOM   4222 C  CA  . ALA B 1 241 ? 0.456   35.030 -36.494 1.00 26.40 ? 465  ALA B CA  1 
ATOM   4223 C  C   . ALA B 1 241 ? 1.522   35.539 -37.450 1.00 26.95 ? 465  ALA B C   1 
ATOM   4224 O  O   . ALA B 1 241 ? 1.672   35.014 -38.558 1.00 30.02 ? 465  ALA B O   1 
ATOM   4225 C  CB  . ALA B 1 241 ? 0.621   33.537 -36.225 1.00 27.43 ? 465  ALA B CB  1 
ATOM   4226 N  N   . ARG B 1 242 ? 2.257   36.569 -37.034 1.00 25.45 ? 466  ARG B N   1 
ATOM   4227 C  CA  . ARG B 1 242 ? 3.232   37.189 -37.922 1.00 24.67 ? 466  ARG B CA  1 
ATOM   4228 C  C   . ARG B 1 242 ? 4.537   36.406 -37.997 1.00 27.78 ? 466  ARG B C   1 
ATOM   4229 O  O   . ARG B 1 242 ? 5.317   36.620 -38.930 1.00 23.34 ? 466  ARG B O   1 
ATOM   4230 C  CB  . ARG B 1 242 ? 3.511   38.627 -37.478 1.00 23.25 ? 466  ARG B CB  1 
ATOM   4231 C  CG  . ARG B 1 242 ? 2.270   39.509 -37.399 1.00 32.92 ? 466  ARG B CG  1 
ATOM   4232 C  CD  . ARG B 1 242 ? 1.665   39.763 -38.770 1.00 36.54 ? 466  ARG B CD  1 
ATOM   4233 N  NE  . ARG B 1 242 ? 0.487   40.621 -38.679 1.00 53.90 ? 466  ARG B NE  1 
ATOM   4234 C  CZ  . ARG B 1 242 ? -0.387  40.809 -39.661 1.00 52.53 ? 466  ARG B CZ  1 
ATOM   4235 N  NH1 . ARG B 1 242 ? -0.229  40.240 -40.848 1.00 52.12 ? 466  ARG B NH1 1 
ATOM   4236 N  NH2 . ARG B 1 242 ? -1.454  41.576 -39.442 1.00 50.97 ? 466  ARG B NH2 1 
ATOM   4237 N  N   . SER B 1 243 ? 4.800   35.536 -37.025 1.00 27.23 ? 467  SER B N   1 
ATOM   4238 C  CA  . SER B 1 243 ? 5.943   34.638 -37.046 1.00 23.09 ? 467  SER B CA  1 
ATOM   4239 C  C   . SER B 1 243 ? 5.501   33.336 -36.410 1.00 24.22 ? 467  SER B C   1 
ATOM   4240 O  O   . SER B 1 243 ? 4.362   33.211 -35.957 1.00 25.27 ? 467  SER B O   1 
ATOM   4241 C  CB  . SER B 1 243 ? 7.139   35.206 -36.286 1.00 24.60 ? 467  SER B CB  1 
ATOM   4242 O  OG  . SER B 1 243 ? 6.996   34.967 -34.890 1.00 24.96 ? 467  SER B OG  1 
ATOM   4243 N  N   . GLU B 1 244 ? 6.426   32.373 -36.348 1.00 26.45 ? 468  GLU B N   1 
ATOM   4244 C  CA  . GLU B 1 244 ? 6.131   31.085 -35.729 1.00 26.58 ? 468  GLU B CA  1 
ATOM   4245 C  C   . GLU B 1 244 ? 6.152   31.136 -34.207 1.00 24.86 ? 468  GLU B C   1 
ATOM   4246 O  O   . GLU B 1 244 ? 5.740   30.163 -33.571 1.00 22.41 ? 468  GLU B O   1 
ATOM   4247 C  CB  . GLU B 1 244 ? 7.122   30.016 -36.205 1.00 32.84 ? 468  GLU B CB  1 
ATOM   4248 C  CG  . GLU B 1 244 ? 6.925   29.568 -37.644 1.00 35.57 ? 468  GLU B CG  1 
ATOM   4249 C  CD  . GLU B 1 244 ? 5.522   29.036 -37.902 1.00 43.22 ? 468  GLU B CD  1 
ATOM   4250 O  OE1 . GLU B 1 244 ? 5.010   28.258 -37.058 1.00 44.00 ? 468  GLU B OE1 1 
ATOM   4251 O  OE2 . GLU B 1 244 ? 4.931   29.400 -38.947 1.00 43.38 ? 468  GLU B OE2 1 
ATOM   4252 N  N   . VAL B 1 245 ? 6.630   32.228 -33.604 1.00 25.63 ? 469  VAL B N   1 
ATOM   4253 C  CA  . VAL B 1 245 ? 6.838   32.293 -32.159 1.00 20.91 ? 469  VAL B CA  1 
ATOM   4254 C  C   . VAL B 1 245 ? 6.469   33.690 -31.671 1.00 24.20 ? 469  VAL B C   1 
ATOM   4255 O  O   . VAL B 1 245 ? 6.968   34.690 -32.194 1.00 23.08 ? 469  VAL B O   1 
ATOM   4256 C  CB  . VAL B 1 245 ? 8.294   31.948 -31.763 1.00 27.10 ? 469  VAL B CB  1 
ATOM   4257 C  CG1 . VAL B 1 245 ? 8.458   31.976 -30.262 1.00 21.90 ? 469  VAL B CG1 1 
ATOM   4258 C  CG2 . VAL B 1 245 ? 8.709   30.584 -32.280 1.00 23.91 ? 469  VAL B CG2 1 
ATOM   4259 N  N   . ALA B 1 246 ? 5.587   33.758 -30.681 1.00 21.94 ? 470  ALA B N   1 
ATOM   4260 C  CA  . ALA B 1 246 ? 5.275   35.004 -29.994 1.00 24.08 ? 470  ALA B CA  1 
ATOM   4261 C  C   . ALA B 1 246 ? 6.080   35.062 -28.707 1.00 26.71 ? 470  ALA B C   1 
ATOM   4262 O  O   . ALA B 1 246 ? 5.906   34.213 -27.819 1.00 26.26 ? 470  ALA B O   1 
ATOM   4263 C  CB  . ALA B 1 246 ? 3.779   35.110 -29.700 1.00 22.01 ? 470  ALA B CB  1 
ATOM   4264 N  N   . LEU B 1 247 ? 6.963   36.055 -28.610 1.00 25.77 ? 471  LEU B N   1 
ATOM   4265 C  CA  . LEU B 1 247 ? 7.740   36.252 -27.393 1.00 24.29 ? 471  LEU B CA  1 
ATOM   4266 C  C   . LEU B 1 247 ? 6.868   36.879 -26.310 1.00 25.11 ? 471  LEU B C   1 
ATOM   4267 O  O   . LEU B 1 247 ? 6.315   37.972 -26.494 1.00 24.55 ? 471  LEU B O   1 
ATOM   4268 C  CB  . LEU B 1 247 ? 8.955   37.133 -27.664 1.00 25.24 ? 471  LEU B CB  1 
ATOM   4269 C  CG  . LEU B 1 247 ? 9.792   37.362 -26.408 1.00 26.01 ? 471  LEU B CG  1 
ATOM   4270 C  CD1 . LEU B 1 247 ? 10.479  36.069 -25.990 1.00 23.13 ? 471  LEU B CD1 1 
ATOM   4271 C  CD2 . LEU B 1 247 ? 10.803  38.495 -26.595 1.00 24.68 ? 471  LEU B CD2 1 
ATOM   4272 N  N   . LEU B 1 248 ? 6.763   36.195 -25.179 1.00 23.39 ? 472  LEU B N   1 
ATOM   4273 C  CA  . LEU B 1 248 ? 5.992   36.654 -24.037 1.00 23.89 ? 472  LEU B CA  1 
ATOM   4274 C  C   . LEU B 1 248 ? 6.947   37.094 -22.934 1.00 26.94 ? 472  LEU B C   1 
ATOM   4275 O  O   . LEU B 1 248 ? 8.061   36.577 -22.809 1.00 30.07 ? 472  LEU B O   1 
ATOM   4276 C  CB  . LEU B 1 248 ? 5.053   35.546 -23.519 1.00 22.74 ? 472  LEU B CB  1 
ATOM   4277 C  CG  . LEU B 1 248 ? 3.602   35.474 -24.012 1.00 30.11 ? 472  LEU B CG  1 
ATOM   4278 C  CD1 . LEU B 1 248 ? 3.481   35.711 -25.503 1.00 24.94 ? 472  LEU B CD1 1 
ATOM   4279 C  CD2 . LEU B 1 248 ? 2.936   34.155 -23.621 1.00 22.43 ? 472  LEU B CD2 1 
ATOM   4280 N  N   . ARG B 1 249 ? 6.525   38.084 -22.161 1.00 25.27 ? 473  ARG B N   1 
ATOM   4281 C  CA  . ARG B 1 249 ? 7.249   38.501 -20.973 1.00 25.10 ? 473  ARG B CA  1 
ATOM   4282 C  C   . ARG B 1 249 ? 6.320   38.303 -19.791 1.00 23.97 ? 473  ARG B C   1 
ATOM   4283 O  O   . ARG B 1 249 ? 5.152   38.693 -19.857 1.00 25.55 ? 473  ARG B O   1 
ATOM   4284 C  CB  . ARG B 1 249 ? 7.720   39.963 -21.075 1.00 23.80 ? 473  ARG B CB  1 
ATOM   4285 C  CG  . ARG B 1 249 ? 8.266   40.527 -19.772 1.00 32.40 ? 473  ARG B CG  1 
ATOM   4286 C  CD  . ARG B 1 249 ? 8.551   42.051 -19.826 1.00 35.58 ? 473  ARG B CD  1 
ATOM   4287 N  NE  . ARG B 1 249 ? 9.705   42.403 -20.648 1.00 38.15 ? 473  ARG B NE  1 
ATOM   4288 C  CZ  . ARG B 1 249 ? 10.263  43.609 -20.670 1.00 36.02 ? 473  ARG B CZ  1 
ATOM   4289 N  NH1 . ARG B 1 249 ? 9.829   44.587 -19.888 1.00 38.76 ? 473  ARG B NH1 1 
ATOM   4290 N  NH2 . ARG B 1 249 ? 11.289  43.837 -21.485 1.00 36.95 ? 473  ARG B NH2 1 
ATOM   4291 N  N   . PHE B 1 250 ? 6.818   37.658 -18.737 1.00 26.87 ? 474  PHE B N   1 
ATOM   4292 C  CA  . PHE B 1 250 ? 6.075   37.552 -17.485 1.00 25.57 ? 474  PHE B CA  1 
ATOM   4293 C  C   . PHE B 1 250 ? 6.453   38.756 -16.628 1.00 28.65 ? 474  PHE B C   1 
ATOM   4294 O  O   . PHE B 1 250 ? 7.574   38.837 -16.106 1.00 23.00 ? 474  PHE B O   1 
ATOM   4295 C  CB  . PHE B 1 250 ? 6.359   36.240 -16.763 1.00 25.70 ? 474  PHE B CB  1 
ATOM   4296 C  CG  . PHE B 1 250 ? 5.295   35.870 -15.755 1.00 22.02 ? 474  PHE B CG  1 
ATOM   4297 C  CD1 . PHE B 1 250 ? 4.070   35.377 -16.176 1.00 22.04 ? 474  PHE B CD1 1 
ATOM   4298 C  CD2 . PHE B 1 250 ? 5.524   36.017 -14.399 1.00 23.53 ? 474  PHE B CD2 1 
ATOM   4299 C  CE1 . PHE B 1 250 ? 3.076   35.031 -15.254 1.00 23.51 ? 474  PHE B CE1 1 
ATOM   4300 C  CE2 . PHE B 1 250 ? 4.553   35.674 -13.467 1.00 24.83 ? 474  PHE B CE2 1 
ATOM   4301 C  CZ  . PHE B 1 250 ? 3.321   35.188 -13.894 1.00 24.69 ? 474  PHE B CZ  1 
ATOM   4302 N  N   . VAL B 1 251 ? 5.507   39.686 -16.497 1.00 29.12 ? 475  VAL B N   1 
ATOM   4303 C  CA  . VAL B 1 251 ? 5.733   41.034 -15.983 1.00 30.25 ? 475  VAL B CA  1 
ATOM   4304 C  C   . VAL B 1 251 ? 5.404   41.066 -14.496 1.00 29.93 ? 475  VAL B C   1 
ATOM   4305 O  O   . VAL B 1 251 ? 4.337   40.596 -14.079 1.00 30.05 ? 475  VAL B O   1 
ATOM   4306 C  CB  . VAL B 1 251 ? 4.861   42.051 -16.746 1.00 30.16 ? 475  VAL B CB  1 
ATOM   4307 C  CG1 . VAL B 1 251 ? 4.806   43.383 -16.014 1.00 32.90 ? 475  VAL B CG1 1 
ATOM   4308 C  CG2 . VAL B 1 251 ? 5.360   42.227 -18.168 1.00 30.45 ? 475  VAL B CG2 1 
ATOM   4309 N  N   . ASN B 1 252 ? 6.302   41.635 -13.697 1.00 30.21 ? 476  ASN B N   1 
ATOM   4310 C  CA  . ASN B 1 252 ? 5.963   42.011 -12.331 1.00 33.97 ? 476  ASN B CA  1 
ATOM   4311 C  C   . ASN B 1 252 ? 5.360   43.408 -12.365 1.00 34.96 ? 476  ASN B C   1 
ATOM   4312 O  O   . ASN B 1 252 ? 6.091   44.374 -12.616 1.00 37.70 ? 476  ASN B O   1 
ATOM   4313 C  CB  . ASN B 1 252 ? 7.201   41.985 -11.444 1.00 38.95 ? 476  ASN B CB  1 
ATOM   4314 C  CG  . ASN B 1 252 ? 6.901   42.363 -10.001 1.00 42.27 ? 476  ASN B CG  1 
ATOM   4315 O  OD1 . ASN B 1 252 ? 5.742   42.375 -9.566  1.00 45.12 ? 476  ASN B OD1 1 
ATOM   4316 N  ND2 . ASN B 1 252 ? 7.952   42.664 -9.246  1.00 44.12 ? 476  ASN B ND2 1 
ATOM   4317 N  N   . PRO B 1 253 ? 4.054   43.575 -12.136 1.00 34.51 ? 477  PRO B N   1 
ATOM   4318 C  CA  . PRO B 1 253 ? 3.469   44.923 -12.219 1.00 37.59 ? 477  PRO B CA  1 
ATOM   4319 C  C   . PRO B 1 253 ? 3.960   45.871 -11.131 1.00 46.51 ? 477  PRO B C   1 
ATOM   4320 O  O   . PRO B 1 253 ? 3.773   47.087 -11.262 1.00 42.58 ? 477  PRO B O   1 
ATOM   4321 C  CB  . PRO B 1 253 ? 1.967   44.662 -12.094 1.00 35.28 ? 477  PRO B CB  1 
ATOM   4322 C  CG  . PRO B 1 253 ? 1.885   43.418 -11.292 1.00 38.81 ? 477  PRO B CG  1 
ATOM   4323 C  CD  . PRO B 1 253 ? 3.066   42.575 -11.703 1.00 36.55 ? 477  PRO B CD  1 
ATOM   4324 N  N   A ASP B 1 254 ? 4.591   45.362 -10.072 0.94 46.04 ? 478  ASP B N   1 
ATOM   4325 C  CA  A ASP B 1 254 ? 5.126   46.245 -9.043  0.94 44.56 ? 478  ASP B CA  1 
ATOM   4326 C  C   A ASP B 1 254 ? 6.346   47.015 -9.532  0.94 50.25 ? 478  ASP B C   1 
ATOM   4327 O  O   A ASP B 1 254 ? 6.578   48.146 -9.094  0.94 63.72 ? 478  ASP B O   1 
ATOM   4328 C  CB  A ASP B 1 254 ? 5.462   45.429 -7.800  0.94 52.34 ? 478  ASP B CB  1 
ATOM   4329 C  CG  A ASP B 1 254 ? 4.300   44.563 -7.360  0.94 61.07 ? 478  ASP B CG  1 
ATOM   4330 O  OD1 A ASP B 1 254 ? 3.153   45.037 -7.484  0.94 57.31 ? 478  ASP B OD1 1 
ATOM   4331 O  OD2 A ASP B 1 254 ? 4.512   43.407 -6.922  0.94 65.47 ? 478  ASP B OD2 1 
ATOM   4332 N  N   . THR B 1 255 ? 7.124   46.436 -10.442 1.00 44.35 ? 479  THR B N   1 
ATOM   4333 C  CA  . THR B 1 255 ? 8.322   47.073 -10.963 1.00 45.60 ? 479  THR B CA  1 
ATOM   4334 C  C   . THR B 1 255 ? 8.252   47.381 -12.451 1.00 43.39 ? 479  THR B C   1 
ATOM   4335 O  O   . THR B 1 255 ? 9.103   48.128 -12.946 1.00 45.19 ? 479  THR B O   1 
ATOM   4336 C  CB  . THR B 1 255 ? 9.556   46.185 -10.716 1.00 47.13 ? 479  THR B CB  1 
ATOM   4337 O  OG1 . THR B 1 255 ? 9.597   45.146 -11.706 1.00 43.35 ? 479  THR B OG1 1 
ATOM   4338 C  CG2 . THR B 1 255 ? 9.492   45.546 -9.334  1.00 49.16 ? 479  THR B CG2 1 
ATOM   4339 N  N   . GLY B 1 256 ? 7.288   46.821 -13.181 1.00 39.08 ? 480  GLY B N   1 
ATOM   4340 C  CA  . GLY B 1 256 ? 7.241   46.960 -14.621 1.00 39.42 ? 480  GLY B CA  1 
ATOM   4341 C  C   . GLY B 1 256 ? 8.220   46.097 -15.389 1.00 43.31 ? 480  GLY B C   1 
ATOM   4342 O  O   . GLY B 1 256 ? 8.109   46.005 -16.622 1.00 42.61 ? 480  GLY B O   1 
ATOM   4343 N  N   . ARG B 1 257 ? 9.163   45.446 -14.714 1.00 37.88 ? 481  ARG B N   1 
ATOM   4344 C  CA  . ARG B 1 257 ? 10.222  44.713 -15.388 1.00 36.51 ? 481  ARG B CA  1 
ATOM   4345 C  C   . ARG B 1 257 ? 9.882   43.232 -15.515 1.00 36.99 ? 481  ARG B C   1 
ATOM   4346 O  O   . ARG B 1 257 ? 8.951   42.708 -14.892 1.00 32.13 ? 481  ARG B O   1 
ATOM   4347 C  CB  . ARG B 1 257 ? 11.556  44.905 -14.658 1.00 34.80 ? 481  ARG B CB  1 
ATOM   4348 C  CG  . ARG B 1 257 ? 12.034  46.341 -14.698 1.00 40.11 ? 481  ARG B CG  1 
ATOM   4349 C  CD  . ARG B 1 257 ? 13.443  46.473 -14.161 1.00 37.04 ? 481  ARG B CD  1 
ATOM   4350 N  NE  . ARG B 1 257 ? 13.530  46.038 -12.773 1.00 38.48 ? 481  ARG B NE  1 
ATOM   4351 C  CZ  . ARG B 1 257 ? 13.286  46.818 -11.728 1.00 40.10 ? 481  ARG B CZ  1 
ATOM   4352 N  NH1 . ARG B 1 257 ? 12.888  48.071 -11.879 1.00 41.73 ? 481  ARG B NH1 1 
ATOM   4353 N  NH2 . ARG B 1 257 ? 13.448  46.330 -10.502 1.00 38.65 ? 481  ARG B NH2 1 
ATOM   4354 N  N   . ALA B 1 258 ? 10.654  42.566 -16.365 1.00 30.50 ? 482  ALA B N   1 
ATOM   4355 C  CA  . ALA B 1 258 ? 10.429  41.165 -16.672 1.00 33.78 ? 482  ALA B CA  1 
ATOM   4356 C  C   . ALA B 1 258 ? 10.858  40.281 -15.505 1.00 33.26 ? 482  ALA B C   1 
ATOM   4357 O  O   . ALA B 1 258 ? 11.941  40.465 -14.939 1.00 33.49 ? 482  ALA B O   1 
ATOM   4358 C  CB  . ALA B 1 258 ? 11.211  40.786 -17.933 1.00 30.77 ? 482  ALA B CB  1 
ATOM   4359 N  N   . LEU B 1 259 ? 10.003  39.319 -15.144 1.00 29.08 ? 483  LEU B N   1 
ATOM   4360 C  CA  . LEU B 1 259 ? 10.427  38.237 -14.259 1.00 30.29 ? 483  LEU B CA  1 
ATOM   4361 C  C   . LEU B 1 259 ? 11.089  37.110 -15.050 1.00 26.75 ? 483  LEU B C   1 
ATOM   4362 O  O   . LEU B 1 259 ? 12.117  36.568 -14.633 1.00 31.39 ? 483  LEU B O   1 
ATOM   4363 C  CB  . LEU B 1 259 ? 9.230   37.711 -13.469 1.00 31.44 ? 483  LEU B CB  1 
ATOM   4364 C  CG  . LEU B 1 259 ? 8.556   38.718 -12.538 1.00 27.42 ? 483  LEU B CG  1 
ATOM   4365 C  CD1 . LEU B 1 259 ? 7.133   38.280 -12.232 1.00 30.47 ? 483  LEU B CD1 1 
ATOM   4366 C  CD2 . LEU B 1 259 ? 9.329   38.893 -11.247 1.00 32.95 ? 483  LEU B CD2 1 
ATOM   4367 N  N   . PHE B 1 260 ? 10.515  36.749 -16.191 1.00 24.36 ? 484  PHE B N   1 
ATOM   4368 C  CA  . PHE B 1 260 ? 11.162  35.864 -17.149 1.00 27.14 ? 484  PHE B CA  1 
ATOM   4369 C  C   . PHE B 1 260 ? 10.450  36.052 -18.480 1.00 25.70 ? 484  PHE B C   1 
ATOM   4370 O  O   . PHE B 1 260 ? 9.430   36.737 -18.559 1.00 25.53 ? 484  PHE B O   1 
ATOM   4371 C  CB  . PHE B 1 260 ? 11.140  34.395 -16.688 1.00 23.72 ? 484  PHE B CB  1 
ATOM   4372 C  CG  . PHE B 1 260 ? 9.757   33.796 -16.562 1.00 27.93 ? 484  PHE B CG  1 
ATOM   4373 C  CD1 . PHE B 1 260 ? 9.003   33.979 -15.407 1.00 25.83 ? 484  PHE B CD1 1 
ATOM   4374 C  CD2 . PHE B 1 260 ? 9.230   33.014 -17.582 1.00 24.07 ? 484  PHE B CD2 1 
ATOM   4375 C  CE1 . PHE B 1 260 ? 7.734   33.411 -15.283 1.00 27.03 ? 484  PHE B CE1 1 
ATOM   4376 C  CE2 . PHE B 1 260 ? 7.970   32.446 -17.471 1.00 23.56 ? 484  PHE B CE2 1 
ATOM   4377 C  CZ  . PHE B 1 260 ? 7.215   32.641 -16.321 1.00 24.79 ? 484  PHE B CZ  1 
ATOM   4378 N  N   . GLU B 1 261 ? 11.009  35.448 -19.528 1.00 28.22 ? 485  GLU B N   1 
ATOM   4379 C  CA  . GLU B 1 261 ? 10.421  35.449 -20.861 1.00 24.18 ? 485  GLU B CA  1 
ATOM   4380 C  C   . GLU B 1 261 ? 10.149  34.019 -21.309 1.00 27.04 ? 485  GLU B C   1 
ATOM   4381 O  O   . GLU B 1 261 ? 10.845  33.079 -20.909 1.00 24.02 ? 485  GLU B O   1 
ATOM   4382 C  CB  . GLU B 1 261 ? 11.330  36.134 -21.886 1.00 26.98 ? 485  GLU B CB  1 
ATOM   4383 C  CG  . GLU B 1 261 ? 11.349  37.649 -21.806 1.00 30.81 ? 485  GLU B CG  1 
ATOM   4384 C  CD  . GLU B 1 261 ? 12.384  38.267 -22.735 1.00 45.75 ? 485  GLU B CD  1 
ATOM   4385 O  OE1 . GLU B 1 261 ? 13.140  37.489 -23.377 1.00 36.08 ? 485  GLU B OE1 1 
ATOM   4386 O  OE2 . GLU B 1 261 ? 12.446  39.526 -22.810 1.00 41.13 ? 485  GLU B OE2 1 
ATOM   4387 N  N   . SER B 1 262 ? 9.129   33.868 -22.152 1.00 23.79 ? 486  SER B N   1 
ATOM   4388 C  CA  . SER B 1 262 ? 8.683   32.572 -22.630 1.00 21.69 ? 486  SER B CA  1 
ATOM   4389 C  C   . SER B 1 262 ? 8.402   32.665 -24.122 1.00 24.11 ? 486  SER B C   1 
ATOM   4390 O  O   . SER B 1 262 ? 8.046   33.729 -24.632 1.00 26.94 ? 486  SER B O   1 
ATOM   4391 C  CB  . SER B 1 262 ? 7.424   32.124 -21.881 1.00 24.58 ? 486  SER B CB  1 
ATOM   4392 O  OG  . SER B 1 262 ? 7.005   30.841 -22.319 1.00 32.25 ? 486  SER B OG  1 
ATOM   4393 N  N   . LYS B 1 263 ? 8.551   31.544 -24.823 1.00 21.66 ? 487  LYS B N   1 
ATOM   4394 C  CA  . LYS B 1 263 ? 8.237   31.471 -26.247 1.00 22.61 ? 487  LYS B CA  1 
ATOM   4395 C  C   . LYS B 1 263 ? 6.894   30.780 -26.408 1.00 25.08 ? 487  LYS B C   1 
ATOM   4396 O  O   . LYS B 1 263 ? 6.762   29.605 -26.050 1.00 24.37 ? 487  LYS B O   1 
ATOM   4397 C  CB  . LYS B 1 263 ? 9.317   30.712 -27.022 1.00 21.08 ? 487  LYS B CB  1 
ATOM   4398 C  CG  . LYS B 1 263 ? 10.562  31.530 -27.325 1.00 28.16 ? 487  LYS B CG  1 
ATOM   4399 C  CD  . LYS B 1 263 ? 11.812  30.640 -27.454 1.00 30.62 ? 487  LYS B CD  1 
ATOM   4400 C  CE  . LYS B 1 263 ? 12.186  30.366 -28.900 1.00 29.53 ? 487  LYS B CE  1 
ATOM   4401 N  NZ  . LYS B 1 263 ? 13.519  29.702 -28.996 1.00 28.74 ? 487  LYS B NZ  1 
ATOM   4402 N  N   . LEU B 1 264 ? 5.896   31.514 -26.921 1.00 22.45 ? 488  LEU B N   1 
ATOM   4403 C  CA  . LEU B 1 264 ? 4.578   30.953 -27.219 1.00 20.83 ? 488  LEU B CA  1 
ATOM   4404 C  C   . LEU B 1 264 ? 4.566   30.519 -28.683 1.00 22.49 ? 488  LEU B C   1 
ATOM   4405 O  O   . LEU B 1 264 ? 4.561   31.353 -29.593 1.00 20.29 ? 488  LEU B O   1 
ATOM   4406 C  CB  . LEU B 1 264 ? 3.469   31.960 -26.921 1.00 20.70 ? 488  LEU B CB  1 
ATOM   4407 C  CG  . LEU B 1 264 ? 2.038   31.577 -27.328 1.00 21.14 ? 488  LEU B CG  1 
ATOM   4408 C  CD1 . LEU B 1 264 ? 1.666   30.187 -26.825 1.00 18.50 ? 488  LEU B CD1 1 
ATOM   4409 C  CD2 . LEU B 1 264 ? 1.037   32.604 -26.817 1.00 21.16 ? 488  LEU B CD2 1 
ATOM   4410 N  N   . HIS B 1 265 ? 4.591   29.214 -28.915 1.00 20.79 ? 489  HIS B N   1 
ATOM   4411 C  CA  . HIS B 1 265 ? 4.671   28.708 -30.273 1.00 21.44 ? 489  HIS B CA  1 
ATOM   4412 C  C   . HIS B 1 265 ? 3.304   28.750 -30.936 1.00 18.80 ? 489  HIS B C   1 
ATOM   4413 O  O   . HIS B 1 265 ? 2.274   28.520 -30.295 1.00 19.76 ? 489  HIS B O   1 
ATOM   4414 C  CB  . HIS B 1 265 ? 5.239   27.291 -30.280 1.00 21.69 ? 489  HIS B CB  1 
ATOM   4415 C  CG  . HIS B 1 265 ? 6.620   27.220 -29.725 1.00 21.36 ? 489  HIS B CG  1 
ATOM   4416 N  ND1 . HIS B 1 265 ? 7.742   27.272 -30.521 1.00 24.63 ? 489  HIS B ND1 1 
ATOM   4417 C  CD2 . HIS B 1 265 ? 7.063   27.144 -28.451 1.00 22.62 ? 489  HIS B CD2 1 
ATOM   4418 C  CE1 . HIS B 1 265 ? 8.820   27.210 -29.760 1.00 26.01 ? 489  HIS B CE1 1 
ATOM   4419 N  NE2 . HIS B 1 265 ? 8.435   27.145 -28.499 1.00 26.61 ? 489  HIS B NE2 1 
ATOM   4420 N  N   . LYS B 1 266 ? 3.310   29.057 -32.234 1.00 19.30 ? 490  LYS B N   1 
ATOM   4421 C  CA  . LYS B 1 266 ? 2.067   29.267 -32.970 1.00 21.73 ? 490  LYS B CA  1 
ATOM   4422 C  C   . LYS B 1 266 ? 1.108   28.088 -32.835 1.00 22.16 ? 490  LYS B C   1 
ATOM   4423 O  O   . LYS B 1 266 ? -0.114  28.277 -32.769 1.00 19.68 ? 490  LYS B O   1 
ATOM   4424 C  CB  . LYS B 1 266 ? 2.396   29.541 -34.436 1.00 24.90 ? 490  LYS B CB  1 
ATOM   4425 C  CG  . LYS B 1 266 ? 1.186   29.704 -35.353 1.00 29.20 ? 490  LYS B CG  1 
ATOM   4426 C  CD  . LYS B 1 266 ? 1.639   29.919 -36.792 1.00 28.99 ? 490  LYS B CD  1 
ATOM   4427 C  CE  . LYS B 1 266 ? 0.470   29.897 -37.758 1.00 34.62 ? 490  LYS B CE  1 
ATOM   4428 N  NZ  . LYS B 1 266 ? 0.947   29.952 -39.170 1.00 36.68 ? 490  LYS B NZ  1 
ATOM   4429 N  N   . GLN B 1 267 ? 1.625   26.870 -32.764 1.00 21.94 ? 491  GLN B N   1 
ATOM   4430 C  CA  . GLN B 1 267 ? 0.709   25.740 -32.658 1.00 22.66 ? 491  GLN B CA  1 
ATOM   4431 C  C   . GLN B 1 267 ? 0.117   25.572 -31.260 1.00 20.69 ? 491  GLN B C   1 
ATOM   4432 O  O   . GLN B 1 267 ? -0.698  24.664 -31.050 1.00 22.82 ? 491  GLN B O   1 
ATOM   4433 C  CB  . GLN B 1 267 ? 1.416   24.467 -33.118 1.00 29.52 ? 491  GLN B CB  1 
ATOM   4434 C  CG  . GLN B 1 267 ? 1.646   24.456 -34.630 1.00 30.75 ? 491  GLN B CG  1 
ATOM   4435 C  CD  . GLN B 1 267 ? 0.378   24.795 -35.431 1.00 35.99 ? 491  GLN B CD  1 
ATOM   4436 O  OE1 . GLN B 1 267 ? 0.198   25.929 -35.898 1.00 35.76 ? 491  GLN B OE1 1 
ATOM   4437 N  NE2 . GLN B 1 267 ? -0.497  23.812 -35.598 1.00 34.96 ? 491  GLN B NE2 1 
ATOM   4438 N  N   . GLY B 1 268 ? 0.495   26.414 -30.306 1.00 20.63 ? 492  GLY B N   1 
ATOM   4439 C  CA  . GLY B 1 268 ? -0.240  26.528 -29.063 1.00 17.83 ? 492  GLY B CA  1 
ATOM   4440 C  C   . GLY B 1 268 ? 0.394   25.897 -27.840 1.00 22.06 ? 492  GLY B C   1 
ATOM   4441 O  O   . GLY B 1 268 ? -0.279  25.183 -27.095 1.00 21.14 ? 492  GLY B O   1 
ATOM   4442 N  N   . PHE B 1 269 ? 1.683   26.143 -27.620 1.00 20.89 ? 493  PHE B N   1 
ATOM   4443 C  CA  . PHE B 1 269 ? 2.333   25.740 -26.383 1.00 21.19 ? 493  PHE B CA  1 
ATOM   4444 C  C   . PHE B 1 269 ? 3.503   26.676 -26.133 1.00 21.33 ? 493  PHE B C   1 
ATOM   4445 O  O   . PHE B 1 269 ? 3.951   27.396 -27.030 1.00 19.20 ? 493  PHE B O   1 
ATOM   4446 C  CB  . PHE B 1 269 ? 2.801   24.273 -26.414 1.00 19.21 ? 493  PHE B CB  1 
ATOM   4447 C  CG  . PHE B 1 269 ? 3.875   23.988 -27.425 1.00 19.66 ? 493  PHE B CG  1 
ATOM   4448 C  CD1 . PHE B 1 269 ? 3.562   23.865 -28.761 1.00 21.70 ? 493  PHE B CD1 1 
ATOM   4449 C  CD2 . PHE B 1 269 ? 5.198   23.802 -27.026 1.00 20.90 ? 493  PHE B CD2 1 
ATOM   4450 C  CE1 . PHE B 1 269 ? 4.546   23.589 -29.692 1.00 22.61 ? 493  PHE B CE1 1 
ATOM   4451 C  CE2 . PHE B 1 269 ? 6.183   23.523 -27.942 1.00 21.51 ? 493  PHE B CE2 1 
ATOM   4452 C  CZ  . PHE B 1 269 ? 5.864   23.423 -29.279 1.00 23.08 ? 493  PHE B CZ  1 
ATOM   4453 N  N   . MET B 1 270 ? 3.988   26.659 -24.897 1.00 21.15 ? 494  MET B N   1 
ATOM   4454 C  CA  . MET B 1 270 ? 5.004   27.595 -24.444 1.00 22.15 ? 494  MET B CA  1 
ATOM   4455 C  C   . MET B 1 270 ? 6.254   26.851 -24.008 1.00 20.23 ? 494  MET B C   1 
ATOM   4456 O  O   . MET B 1 270 ? 6.166   25.799 -23.369 1.00 24.23 ? 494  MET B O   1 
ATOM   4457 C  CB  . MET B 1 270 ? 4.472   28.451 -23.289 1.00 19.71 ? 494  MET B CB  1 
ATOM   4458 C  CG  . MET B 1 270 ? 3.412   29.435 -23.721 1.00 24.92 ? 494  MET B CG  1 
ATOM   4459 S  SD  . MET B 1 270 ? 2.598   30.277 -22.350 1.00 35.27 ? 494  MET B SD  1 
ATOM   4460 C  CE  . MET B 1 270 ? 4.016   30.804 -21.451 1.00 20.11 ? 494  MET B CE  1 
ATOM   4461 N  N   . THR B 1 271 ? 7.415   27.391 -24.356 1.00 20.31 ? 495  THR B N   1 
ATOM   4462 C  CA  . THR B 1 271 ? 8.675   26.874 -23.841 1.00 22.96 ? 495  THR B CA  1 
ATOM   4463 C  C   . THR B 1 271 ? 9.402   27.965 -23.072 1.00 21.71 ? 495  THR B C   1 
ATOM   4464 O  O   . THR B 1 271 ? 9.184   29.157 -23.286 1.00 23.34 ? 495  THR B O   1 
ATOM   4465 C  CB  . THR B 1 271 ? 9.601   26.336 -24.953 1.00 23.66 ? 495  THR B CB  1 
ATOM   4466 O  OG1 . THR B 1 271 ? 9.882   27.361 -25.917 1.00 25.09 ? 495  THR B OG1 1 
ATOM   4467 C  CG2 . THR B 1 271 ? 8.982   25.121 -25.637 1.00 25.67 ? 495  THR B CG2 1 
ATOM   4468 N  N   . ILE B 1 272 ? 10.273  27.532 -22.166 1.00 20.89 ? 496  ILE B N   1 
ATOM   4469 C  CA  . ILE B 1 272 ? 11.131  28.416 -21.390 1.00 24.29 ? 496  ILE B CA  1 
ATOM   4470 C  C   . ILE B 1 272 ? 12.520  27.796 -21.367 1.00 25.54 ? 496  ILE B C   1 
ATOM   4471 O  O   . ILE B 1 272 ? 12.702  26.616 -21.664 1.00 23.31 ? 496  ILE B O   1 
ATOM   4472 C  CB  . ILE B 1 272 ? 10.618  28.625 -19.948 1.00 24.22 ? 496  ILE B CB  1 
ATOM   4473 C  CG1 . ILE B 1 272 ? 10.275  27.261 -19.331 1.00 26.38 ? 496  ILE B CG1 1 
ATOM   4474 C  CG2 . ILE B 1 272 ? 9.418   29.569 -19.930 1.00 24.59 ? 496  ILE B CG2 1 
ATOM   4475 C  CD1 . ILE B 1 272 ? 10.240  27.232 -17.830 1.00 21.38 ? 496  ILE B CD1 1 
ATOM   4476 N  N   . ALA B 1 273 ? 13.508  28.608 -21.015 1.00 23.61 ? 497  ALA B N   1 
ATOM   4477 C  CA  . ALA B 1 273 ? 14.855  28.094 -20.796 1.00 24.72 ? 497  ALA B CA  1 
ATOM   4478 C  C   . ALA B 1 273 ? 14.938  27.579 -19.362 1.00 26.56 ? 497  ALA B C   1 
ATOM   4479 O  O   . ALA B 1 273 ? 15.006  28.357 -18.411 1.00 29.26 ? 497  ALA B O   1 
ATOM   4480 C  CB  . ALA B 1 273 ? 15.894  29.172 -21.075 1.00 31.04 ? 497  ALA B CB  1 
ATOM   4481 N  N   . SER B 1 274 ? 14.918  26.259 -19.193 1.00 28.42 ? 498  SER B N   1 
ATOM   4482 C  CA  . SER B 1 274 ? 14.960  25.682 -17.855 1.00 26.67 ? 498  SER B CA  1 
ATOM   4483 C  C   . SER B 1 274 ? 15.331  24.212 -17.972 1.00 30.73 ? 498  SER B C   1 
ATOM   4484 O  O   . SER B 1 274 ? 15.297  23.623 -19.056 1.00 30.99 ? 498  SER B O   1 
ATOM   4485 C  CB  . SER B 1 274 ? 13.620  25.864 -17.127 1.00 29.10 ? 498  SER B CB  1 
ATOM   4486 O  OG  . SER B 1 274 ? 13.768  25.672 -15.727 1.00 32.59 ? 498  SER B OG  1 
ATOM   4487 N  N   . SER B 1 275 ? 15.682  23.620 -16.836 1.00 32.32 ? 499  SER B N   1 
ATOM   4488 C  CA  . SER B 1 275 ? 16.113  22.230 -16.816 1.00 33.87 ? 499  SER B CA  1 
ATOM   4489 C  C   . SER B 1 275 ? 15.583  21.547 -15.567 1.00 32.89 ? 499  SER B C   1 
ATOM   4490 O  O   . SER B 1 275 ? 15.760  22.056 -14.457 1.00 36.04 ? 499  SER B O   1 
ATOM   4491 C  CB  . SER B 1 275 ? 17.640  22.134 -16.864 1.00 31.30 ? 499  SER B CB  1 
ATOM   4492 O  OG  . SER B 1 275 ? 18.054  20.787 -16.932 1.00 40.02 ? 499  SER B OG  1 
ATOM   4493 N  N   . GLY B 1 276 ? 14.949  20.399 -15.747 1.00 31.55 ? 500  GLY B N   1 
ATOM   4494 C  CA  . GLY B 1 276 ? 14.454  19.621 -14.629 1.00 31.85 ? 500  GLY B CA  1 
ATOM   4495 C  C   . GLY B 1 276 ? 12.957  19.761 -14.436 1.00 32.21 ? 500  GLY B C   1 
ATOM   4496 O  O   . GLY B 1 276 ? 12.243  20.421 -15.200 1.00 24.32 ? 500  GLY B O   1 
ATOM   4497 N  N   . ASP B 1 277 ? 12.485  19.111 -13.377 1.00 28.61 ? 501  ASP B N   1 
ATOM   4498 C  CA  . ASP B 1 277 ? 11.066  19.037 -13.047 1.00 30.18 ? 501  ASP B CA  1 
ATOM   4499 C  C   . ASP B 1 277 ? 10.834  19.825 -11.771 1.00 31.27 ? 501  ASP B C   1 
ATOM   4500 O  O   . ASP B 1 277 ? 11.268  19.408 -10.695 1.00 29.24 ? 501  ASP B O   1 
ATOM   4501 C  CB  . ASP B 1 277 ? 10.623  17.587 -12.875 1.00 28.63 ? 501  ASP B CB  1 
ATOM   4502 C  CG  . ASP B 1 277 ? 10.506  16.859 -14.188 1.00 32.83 ? 501  ASP B CG  1 
ATOM   4503 O  OD1 . ASP B 1 277 ? 11.501  16.848 -14.949 1.00 31.00 ? 501  ASP B OD1 1 
ATOM   4504 O  OD2 . ASP B 1 277 ? 9.414   16.306 -14.459 1.00 41.09 ? 501  ASP B OD2 1 
ATOM   4505 N  N   . HIS B 1 278 ? 10.136  20.945 -11.880 1.00 26.70 ? 502  HIS B N   1 
ATOM   4506 C  CA  . HIS B 1 278 ? 9.959   21.821 -10.735 1.00 27.91 ? 502  HIS B CA  1 
ATOM   4507 C  C   . HIS B 1 278 ? 8.933   22.888 -11.094 1.00 30.54 ? 502  HIS B C   1 
ATOM   4508 O  O   . HIS B 1 278 ? 8.748   23.206 -12.272 1.00 20.63 ? 502  HIS B O   1 
ATOM   4509 C  CB  . HIS B 1 278 ? 11.287  22.470 -10.324 1.00 28.69 ? 502  HIS B CB  1 
ATOM   4510 C  CG  . HIS B 1 278 ? 11.979  23.187 -11.440 1.00 33.40 ? 502  HIS B CG  1 
ATOM   4511 N  ND1 . HIS B 1 278 ? 11.652  24.473 -11.815 1.00 33.22 ? 502  HIS B ND1 1 
ATOM   4512 C  CD2 . HIS B 1 278 ? 12.985  22.800 -12.261 1.00 31.74 ? 502  HIS B CD2 1 
ATOM   4513 C  CE1 . HIS B 1 278 ? 12.426  24.848 -12.818 1.00 33.90 ? 502  HIS B CE1 1 
ATOM   4514 N  NE2 . HIS B 1 278 ? 13.243  23.851 -13.109 1.00 31.98 ? 502  HIS B NE2 1 
ATOM   4515 N  N   . PRO B 1 279 ? 8.244   23.428 -10.099 1.00 26.87 ? 503  PRO B N   1 
ATOM   4516 C  CA  . PRO B 1 279 ? 7.325   24.531 -10.367 1.00 25.20 ? 503  PRO B CA  1 
ATOM   4517 C  C   . PRO B 1 279 ? 8.096   25.785 -10.740 1.00 25.70 ? 503  PRO B C   1 
ATOM   4518 O  O   . PRO B 1 279 ? 9.300   25.901 -10.510 1.00 25.18 ? 503  PRO B O   1 
ATOM   4519 C  CB  . PRO B 1 279 ? 6.567   24.713 -9.047  1.00 21.98 ? 503  PRO B CB  1 
ATOM   4520 C  CG  . PRO B 1 279 ? 7.318   23.940 -8.032  1.00 28.72 ? 503  PRO B CG  1 
ATOM   4521 C  CD  . PRO B 1 279 ? 8.162   22.932 -8.714  1.00 27.85 ? 503  PRO B CD  1 
ATOM   4522 N  N   . ILE B 1 280 ? 7.379   26.706 -11.364 1.00 25.09 ? 504  ILE B N   1 
ATOM   4523 C  CA  . ILE B 1 280 ? 7.831   28.064 -11.629 1.00 26.18 ? 504  ILE B CA  1 
ATOM   4524 C  C   . ILE B 1 280 ? 6.958   28.956 -10.756 1.00 29.94 ? 504  ILE B C   1 
ATOM   4525 O  O   . ILE B 1 280 ? 5.823   29.281 -11.126 1.00 29.51 ? 504  ILE B O   1 
ATOM   4526 C  CB  . ILE B 1 280 ? 7.698   28.428 -13.114 1.00 26.88 ? 504  ILE B CB  1 
ATOM   4527 C  CG1 . ILE B 1 280 ? 8.274   27.314 -14.007 1.00 27.18 ? 504  ILE B CG1 1 
ATOM   4528 C  CG2 . ILE B 1 280 ? 8.332   29.789 -13.422 1.00 23.36 ? 504  ILE B CG2 1 
ATOM   4529 C  CD1 . ILE B 1 280 ? 9.755   27.365 -14.166 1.00 30.78 ? 504  ILE B CD1 1 
ATOM   4530 N  N   . ILE B 1 281 ? 7.454   29.339 -9.582  1.00 30.50 ? 505  ILE B N   1 
ATOM   4531 C  CA  . ILE B 1 281 ? 6.679   30.160 -8.655  1.00 37.74 ? 505  ILE B CA  1 
ATOM   4532 C  C   . ILE B 1 281 ? 7.149   31.604 -8.762  1.00 32.97 ? 505  ILE B C   1 
ATOM   4533 O  O   . ILE B 1 281 ? 8.354   31.883 -8.729  1.00 34.37 ? 505  ILE B O   1 
ATOM   4534 C  CB  . ILE B 1 281 ? 6.790   29.643 -7.210  1.00 45.59 ? 505  ILE B CB  1 
ATOM   4535 C  CG1 . ILE B 1 281 ? 6.291   28.200 -7.124  1.00 39.18 ? 505  ILE B CG1 1 
ATOM   4536 C  CG2 . ILE B 1 281 ? 5.959   30.515 -6.278  1.00 42.31 ? 505  ILE B CG2 1 
ATOM   4537 C  CD1 . ILE B 1 281 ? 4.823   28.042 -7.526  1.00 37.81 ? 505  ILE B CD1 1 
ATOM   4538 N  N   . MET B 1 282 ? 6.200   32.514 -8.894  1.00 34.68 ? 506  MET B N   1 
ATOM   4539 C  CA  . MET B 1 282 ? 6.444   33.923 -9.143  1.00 34.18 ? 506  MET B CA  1 
ATOM   4540 C  C   . MET B 1 282 ? 5.623   34.756 -8.178  1.00 34.26 ? 506  MET B C   1 
ATOM   4541 O  O   . MET B 1 282 ? 4.693   34.243 -7.544  1.00 35.25 ? 506  MET B O   1 
ATOM   4542 C  CB  . MET B 1 282 ? 6.065   34.279 -10.588 1.00 30.25 ? 506  MET B CB  1 
ATOM   4543 C  CG  . MET B 1 282 ? 7.006   33.680 -11.598 1.00 34.74 ? 506  MET B CG  1 
ATOM   4544 S  SD  . MET B 1 282 ? 8.614   34.459 -11.461 1.00 34.38 ? 506  MET B SD  1 
ATOM   4545 C  CE  . MET B 1 282 ? 9.683   33.080 -11.857 1.00 34.90 ? 506  MET B CE  1 
ATOM   4546 N  N   . PRO B 1 283 ? 5.951   36.043 -8.028  1.00 32.54 ? 507  PRO B N   1 
ATOM   4547 C  CA  . PRO B 1 283 ? 5.030   36.963 -7.348  1.00 33.16 ? 507  PRO B CA  1 
ATOM   4548 C  C   . PRO B 1 283 ? 3.620   36.799 -7.895  1.00 31.38 ? 507  PRO B C   1 
ATOM   4549 O  O   . PRO B 1 283 ? 3.419   36.635 -9.099  1.00 30.08 ? 507  PRO B O   1 
ATOM   4550 C  CB  . PRO B 1 283 ? 5.610   38.344 -7.665  1.00 28.99 ? 507  PRO B CB  1 
ATOM   4551 C  CG  . PRO B 1 283 ? 7.076   38.099 -7.809  1.00 31.26 ? 507  PRO B CG  1 
ATOM   4552 C  CD  . PRO B 1 283 ? 7.215   36.701 -8.405  1.00 31.47 ? 507  PRO B CD  1 
ATOM   4553 N  N   . THR B 1 284 ? 2.636   36.816 -6.994  1.00 29.09 ? 508  THR B N   1 
ATOM   4554 C  CA  . THR B 1 284 ? 1.306   36.360 -7.376  1.00 34.15 ? 508  THR B CA  1 
ATOM   4555 C  C   . THR B 1 284 ? 0.610   37.293 -8.350  1.00 29.09 ? 508  THR B C   1 
ATOM   4556 O  O   . THR B 1 284 ? -0.364  36.875 -8.978  1.00 26.89 ? 508  THR B O   1 
ATOM   4557 C  CB  . THR B 1 284 ? 0.418   36.172 -6.147  1.00 33.85 ? 508  THR B CB  1 
ATOM   4558 O  OG1 . THR B 1 284 ? 0.307   37.414 -5.449  1.00 36.54 ? 508  THR B OG1 1 
ATOM   4559 C  CG2 . THR B 1 284 ? 0.996   35.098 -5.224  1.00 32.51 ? 508  THR B CG2 1 
ATOM   4560 N  N   . ASN B 1 285 ? 1.067   38.534 -8.488  1.00 30.02 ? 509  ASN B N   1 
ATOM   4561 C  CA  . ASN B 1 285 ? 0.436   39.470 -9.409  1.00 28.06 ? 509  ASN B CA  1 
ATOM   4562 C  C   . ASN B 1 285 ? 1.065   39.452 -10.790 1.00 28.32 ? 509  ASN B C   1 
ATOM   4563 O  O   . ASN B 1 285 ? 0.636   40.220 -11.653 1.00 28.69 ? 509  ASN B O   1 
ATOM   4564 C  CB  . ASN B 1 285 ? 0.487   40.897 -8.860  1.00 32.48 ? 509  ASN B CB  1 
ATOM   4565 C  CG  . ASN B 1 285 ? -0.442  41.104 -7.680  1.00 42.13 ? 509  ASN B CG  1 
ATOM   4566 O  OD1 . ASN B 1 285 ? -1.422  40.375 -7.505  1.00 46.56 ? 509  ASN B OD1 1 
ATOM   4567 N  ND2 . ASN B 1 285 ? -0.139  42.109 -6.862  1.00 50.89 ? 509  ASN B ND2 1 
ATOM   4568 N  N   . GLY B 1 286 ? 2.068   38.607 -11.018 1.00 25.85 ? 510  GLY B N   1 
ATOM   4569 C  CA  . GLY B 1 286 ? 2.673   38.538 -12.333 1.00 26.22 ? 510  GLY B CA  1 
ATOM   4570 C  C   . GLY B 1 286 ? 1.687   38.076 -13.389 1.00 26.33 ? 510  GLY B C   1 
ATOM   4571 O  O   . GLY B 1 286 ? 0.734   37.346 -13.111 1.00 23.85 ? 510  GLY B O   1 
ATOM   4572 N  N   . TYR B 1 287 ? 1.915   38.531 -14.616 1.00 23.53 ? 511  TYR B N   1 
ATOM   4573 C  CA  . TYR B 1 287 ? 1.080   38.140 -15.740 1.00 25.67 ? 511  TYR B CA  1 
ATOM   4574 C  C   . TYR B 1 287 ? 1.927   38.145 -17.001 1.00 24.21 ? 511  TYR B C   1 
ATOM   4575 O  O   . TYR B 1 287 ? 2.920   38.870 -17.094 1.00 23.94 ? 511  TYR B O   1 
ATOM   4576 C  CB  . TYR B 1 287 ? -0.125  39.079 -15.917 1.00 26.34 ? 511  TYR B CB  1 
ATOM   4577 C  CG  . TYR B 1 287 ? 0.256   40.520 -16.215 1.00 26.55 ? 511  TYR B CG  1 
ATOM   4578 C  CD1 . TYR B 1 287 ? 0.653   41.382 -15.200 1.00 29.22 ? 511  TYR B CD1 1 
ATOM   4579 C  CD2 . TYR B 1 287 ? 0.224   41.013 -17.512 1.00 27.50 ? 511  TYR B CD2 1 
ATOM   4580 C  CE1 . TYR B 1 287 ? 1.014   42.696 -15.471 1.00 35.32 ? 511  TYR B CE1 1 
ATOM   4581 C  CE2 . TYR B 1 287 ? 0.576   42.327 -17.794 1.00 30.38 ? 511  TYR B CE2 1 
ATOM   4582 C  CZ  . TYR B 1 287 ? 0.969   43.164 -16.774 1.00 36.94 ? 511  TYR B CZ  1 
ATOM   4583 O  OH  . TYR B 1 287 ? 1.318   44.468 -17.062 1.00 38.95 ? 511  TYR B OH  1 
ATOM   4584 N  N   . PHE B 1 288 ? 1.524   37.330 -17.969 1.00 26.50 ? 512  PHE B N   1 
ATOM   4585 C  CA  . PHE B 1 288 ? 2.165   37.337 -19.276 1.00 22.50 ? 512  PHE B CA  1 
ATOM   4586 C  C   . PHE B 1 288 ? 1.667   38.509 -20.098 1.00 26.54 ? 512  PHE B C   1 
ATOM   4587 O  O   . PHE B 1 288 ? 0.486   38.880 -20.034 1.00 24.63 ? 512  PHE B O   1 
ATOM   4588 C  CB  . PHE B 1 288 ? 1.887   36.047 -20.046 1.00 21.47 ? 512  PHE B CB  1 
ATOM   4589 C  CG  . PHE B 1 288 ? 2.649   34.858 -19.541 1.00 20.86 ? 512  PHE B CG  1 
ATOM   4590 C  CD1 . PHE B 1 288 ? 3.997   34.704 -19.831 1.00 23.68 ? 512  PHE B CD1 1 
ATOM   4591 C  CD2 . PHE B 1 288 ? 2.013   33.879 -18.796 1.00 21.58 ? 512  PHE B CD2 1 
ATOM   4592 C  CE1 . PHE B 1 288 ? 4.691   33.604 -19.380 1.00 20.16 ? 512  PHE B CE1 1 
ATOM   4593 C  CE2 . PHE B 1 288 ? 2.703   32.774 -18.345 1.00 22.64 ? 512  PHE B CE2 1 
ATOM   4594 C  CZ  . PHE B 1 288 ? 4.046   32.638 -18.628 1.00 21.18 ? 512  PHE B CZ  1 
ATOM   4595 N  N   . ARG B 1 289 ? 2.585   39.078 -20.879 1.00 22.98 ? 513  ARG B N   1 
ATOM   4596 C  CA  . ARG B 1 289 ? 2.308   40.154 -21.814 1.00 26.07 ? 513  ARG B CA  1 
ATOM   4597 C  C   . ARG B 1 289 ? 3.007   39.836 -23.126 1.00 24.73 ? 513  ARG B C   1 
ATOM   4598 O  O   . ARG B 1 289 ? 4.170   39.431 -23.119 1.00 27.87 ? 513  ARG B O   1 
ATOM   4599 C  CB  . ARG B 1 289 ? 2.803   41.482 -21.244 1.00 24.70 ? 513  ARG B CB  1 
ATOM   4600 C  CG  . ARG B 1 289 ? 2.815   42.632 -22.195 1.00 30.21 ? 513  ARG B CG  1 
ATOM   4601 C  CD  . ARG B 1 289 ? 3.334   43.888 -21.490 1.00 38.32 ? 513  ARG B CD  1 
ATOM   4602 N  NE  . ARG B 1 289 ? 4.782   44.046 -21.593 1.00 39.09 ? 513  ARG B NE  1 
ATOM   4603 C  CZ  . ARG B 1 289 ? 5.476   44.955 -20.920 1.00 44.01 ? 513  ARG B CZ  1 
ATOM   4604 N  NH1 . ARG B 1 289 ? 4.888   45.779 -20.067 1.00 41.92 ? 513  ARG B NH1 1 
ATOM   4605 N  NH2 . ARG B 1 289 ? 6.792   45.036 -21.103 1.00 40.67 ? 513  ARG B NH2 1 
ATOM   4606 N  N   . PHE B 1 290 ? 2.312   40.023 -24.245 1.00 22.75 ? 514  PHE B N   1 
ATOM   4607 C  CA  . PHE B 1 290 ? 2.948   39.856 -25.546 1.00 22.39 ? 514  PHE B CA  1 
ATOM   4608 C  C   . PHE B 1 290 ? 4.021   40.918 -25.773 1.00 29.86 ? 514  PHE B C   1 
ATOM   4609 O  O   . PHE B 1 290 ? 3.777   42.116 -25.603 1.00 23.42 ? 514  PHE B O   1 
ATOM   4610 C  CB  . PHE B 1 290 ? 1.917   39.933 -26.656 1.00 23.87 ? 514  PHE B CB  1 
ATOM   4611 C  CG  . PHE B 1 290 ? 2.514   39.913 -28.024 1.00 25.64 ? 514  PHE B CG  1 
ATOM   4612 C  CD1 . PHE B 1 290 ? 3.276   38.838 -28.442 1.00 25.15 ? 514  PHE B CD1 1 
ATOM   4613 C  CD2 . PHE B 1 290 ? 2.325   40.975 -28.891 1.00 28.04 ? 514  PHE B CD2 1 
ATOM   4614 C  CE1 . PHE B 1 290 ? 3.832   38.816 -29.708 1.00 26.00 ? 514  PHE B CE1 1 
ATOM   4615 C  CE2 . PHE B 1 290 ? 2.886   40.965 -30.155 1.00 28.19 ? 514  PHE B CE2 1 
ATOM   4616 C  CZ  . PHE B 1 290 ? 3.637   39.887 -30.566 1.00 28.32 ? 514  PHE B CZ  1 
ATOM   4617 N  N   . GLU B 1 291 ? 5.208   40.477 -26.181 1.00 24.94 ? 515  GLU B N   1 
ATOM   4618 C  CA  . GLU B 1 291 ? 6.342   41.364 -26.403 1.00 26.01 ? 515  GLU B CA  1 
ATOM   4619 C  C   . GLU B 1 291 ? 6.628   41.601 -27.879 1.00 27.55 ? 515  GLU B C   1 
ATOM   4620 O  O   . GLU B 1 291 ? 6.678   42.753 -28.319 1.00 24.51 ? 515  GLU B O   1 
ATOM   4621 C  CB  . GLU B 1 291 ? 7.593   40.788 -25.716 1.00 24.44 ? 515  GLU B CB  1 
ATOM   4622 C  CG  . GLU B 1 291 ? 8.595   41.818 -25.255 1.00 35.64 ? 515  GLU B CG  1 
ATOM   4623 C  CD  . GLU B 1 291 ? 7.994   42.764 -24.223 1.00 43.52 ? 515  GLU B CD  1 
ATOM   4624 O  OE1 . GLU B 1 291 ? 7.034   42.348 -23.525 1.00 42.41 ? 515  GLU B OE1 1 
ATOM   4625 O  OE2 . GLU B 1 291 ? 8.468   43.918 -24.128 1.00 43.24 ? 515  GLU B OE2 1 
ATOM   4626 N  N   . ALA B 1 292 ? 6.803   40.539 -28.665 1.00 27.85 ? 516  ALA B N   1 
ATOM   4627 C  CA  . ALA B 1 292 ? 7.251   40.679 -30.045 1.00 25.57 ? 516  ALA B CA  1 
ATOM   4628 C  C   . ALA B 1 292 ? 7.117   39.347 -30.768 1.00 25.24 ? 516  ALA B C   1 
ATOM   4629 O  O   . ALA B 1 292 ? 7.070   38.288 -30.142 1.00 25.86 ? 516  ALA B O   1 
ATOM   4630 C  CB  . ALA B 1 292 ? 8.707   41.143 -30.111 1.00 25.41 ? 516  ALA B CB  1 
ATOM   4631 N  N   . TRP B 1 293 ? 7.114   39.421 -32.100 1.00 24.14 ? 517  TRP B N   1 
ATOM   4632 C  CA  . TRP B 1 293 ? 7.270   38.245 -32.947 1.00 26.12 ? 517  TRP B CA  1 
ATOM   4633 C  C   . TRP B 1 293 ? 8.747   37.906 -33.112 1.00 27.56 ? 517  TRP B C   1 
ATOM   4634 O  O   . TRP B 1 293 ? 9.549   38.770 -33.476 1.00 23.96 ? 517  TRP B O   1 
ATOM   4635 C  CB  . TRP B 1 293 ? 6.638   38.491 -34.315 1.00 24.03 ? 517  TRP B CB  1 
ATOM   4636 C  CG  . TRP B 1 293 ? 5.186   38.698 -34.212 1.00 25.92 ? 517  TRP B CG  1 
ATOM   4637 C  CD1 . TRP B 1 293 ? 4.509   39.881 -34.317 1.00 27.86 ? 517  TRP B CD1 1 
ATOM   4638 C  CD2 . TRP B 1 293 ? 4.208   37.692 -33.951 1.00 24.83 ? 517  TRP B CD2 1 
ATOM   4639 N  NE1 . TRP B 1 293 ? 3.162   39.667 -34.140 1.00 25.08 ? 517  TRP B NE1 1 
ATOM   4640 C  CE2 . TRP B 1 293 ? 2.953   38.331 -33.909 1.00 26.49 ? 517  TRP B CE2 1 
ATOM   4641 C  CE3 . TRP B 1 293 ? 4.274   36.311 -33.726 1.00 24.63 ? 517  TRP B CE3 1 
ATOM   4642 C  CZ2 . TRP B 1 293 ? 1.773   37.637 -33.672 1.00 25.24 ? 517  TRP B CZ2 1 
ATOM   4643 C  CZ3 . TRP B 1 293 ? 3.095   35.621 -33.496 1.00 24.83 ? 517  TRP B CZ3 1 
ATOM   4644 C  CH2 . TRP B 1 293 ? 1.862   36.285 -33.468 1.00 26.76 ? 517  TRP B CH2 1 
ATOM   4645 N  N   . VAL B 1 294 ? 9.105   36.649 -32.855 1.00 23.34 ? 518  VAL B N   1 
ATOM   4646 C  CA  . VAL B 1 294 ? 10.484  36.200 -33.029 1.00 23.66 ? 518  VAL B CA  1 
ATOM   4647 C  C   . VAL B 1 294 ? 10.466  34.879 -33.782 1.00 28.25 ? 518  VAL B C   1 
ATOM   4648 O  O   . VAL B 1 294 ? 9.421   34.463 -34.298 1.00 28.00 ? 518  VAL B O   1 
ATOM   4649 C  CB  . VAL B 1 294 ? 11.215  36.062 -31.678 1.00 24.68 ? 518  VAL B CB  1 
ATOM   4650 C  CG1 . VAL B 1 294 ? 11.250  37.400 -30.960 1.00 28.54 ? 518  VAL B CG1 1 
ATOM   4651 C  CG2 . VAL B 1 294 ? 10.559  35.006 -30.809 1.00 24.29 ? 518  VAL B CG2 1 
ATOM   4652 N  N   . ASN B 1 295 ? 11.608  34.209 -33.861 1.00 28.87 ? 519  ASN B N   1 
ATOM   4653 C  CA  . ASN B 1 295 ? 11.652  32.907 -34.516 1.00 26.60 ? 519  ASN B CA  1 
ATOM   4654 C  C   . ASN B 1 295 ? 12.033  31.826 -33.505 1.00 29.35 ? 519  ASN B C   1 
ATOM   4655 O  O   . ASN B 1 295 ? 12.189  32.077 -32.304 1.00 25.50 ? 519  ASN B O   1 
ATOM   4656 C  CB  . ASN B 1 295 ? 12.585  32.931 -35.743 1.00 26.46 ? 519  ASN B CB  1 
ATOM   4657 C  CG  . ASN B 1 295 ? 14.051  33.168 -35.396 1.00 28.50 ? 519  ASN B CG  1 
ATOM   4658 O  OD1 . ASN B 1 295 ? 14.506  32.877 -34.297 1.00 30.79 ? 519  ASN B OD1 1 
ATOM   4659 N  ND2 . ASN B 1 295 ? 14.800  33.686 -36.359 1.00 33.06 ? 519  ASN B ND2 1 
ATOM   4660 N  N   . GLN B 1 296 ? 12.154  30.599 -34.005 1.00 25.91 ? 520  GLN B N   1 
ATOM   4661 C  CA  . GLN B 1 296 ? 12.413  29.466 -33.136 1.00 26.43 ? 520  GLN B CA  1 
ATOM   4662 C  C   . GLN B 1 296 ? 13.817  29.477 -32.558 1.00 27.84 ? 520  GLN B C   1 
ATOM   4663 O  O   . GLN B 1 296 ? 14.084  28.727 -31.614 1.00 29.63 ? 520  GLN B O   1 
ATOM   4664 C  CB  . GLN B 1 296 ? 12.153  28.171 -33.905 1.00 29.37 ? 520  GLN B CB  1 
ATOM   4665 C  CG  . GLN B 1 296 ? 10.660  27.797 -33.879 1.00 39.01 ? 520  GLN B CG  1 
ATOM   4666 C  CD  . GLN B 1 296 ? 10.229  26.918 -35.039 1.00 46.40 ? 520  GLN B CD  1 
ATOM   4667 O  OE1 . GLN B 1 296 ? 11.046  26.511 -35.871 1.00 50.10 ? 520  GLN B OE1 1 
ATOM   4668 N  NE2 . GLN B 1 296 ? 8.930   26.627 -35.103 1.00 42.83 ? 520  GLN B NE2 1 
ATOM   4669 N  N   . PHE B 1 297 ? 14.709  30.310 -33.085 1.00 27.67 ? 521  PHE B N   1 
ATOM   4670 C  CA  . PHE B 1 297 ? 16.085  30.364 -32.618 1.00 28.14 ? 521  PHE B CA  1 
ATOM   4671 C  C   . PHE B 1 297 ? 16.292  31.350 -31.484 1.00 31.48 ? 521  PHE B C   1 
ATOM   4672 O  O   . PHE B 1 297 ? 17.420  31.456 -30.989 1.00 29.58 ? 521  PHE B O   1 
ATOM   4673 C  CB  . PHE B 1 297 ? 17.021  30.730 -33.768 1.00 26.47 ? 521  PHE B CB  1 
ATOM   4674 C  CG  . PHE B 1 297 ? 17.016  29.739 -34.886 1.00 30.31 ? 521  PHE B CG  1 
ATOM   4675 C  CD1 . PHE B 1 297 ? 17.799  28.594 -34.817 1.00 36.23 ? 521  PHE B CD1 1 
ATOM   4676 C  CD2 . PHE B 1 297 ? 16.233  29.946 -36.009 1.00 31.55 ? 521  PHE B CD2 1 
ATOM   4677 C  CE1 . PHE B 1 297 ? 17.801  27.676 -35.848 1.00 34.64 ? 521  PHE B CE1 1 
ATOM   4678 C  CE2 . PHE B 1 297 ? 16.230  29.026 -37.046 1.00 36.85 ? 521  PHE B CE2 1 
ATOM   4679 C  CZ  . PHE B 1 297 ? 17.013  27.892 -36.962 1.00 34.22 ? 521  PHE B CZ  1 
ATOM   4680 N  N   . TYR B 1 298 ? 15.245  32.078 -31.075 1.00 28.58 ? 522  TYR B N   1 
ATOM   4681 C  CA  . TYR B 1 298 ? 15.415  33.149 -30.098 1.00 27.52 ? 522  TYR B CA  1 
ATOM   4682 C  C   . TYR B 1 298 ? 15.903  32.580 -28.775 1.00 27.45 ? 522  TYR B C   1 
ATOM   4683 O  O   . TYR B 1 298 ? 15.356  31.597 -28.274 1.00 26.52 ? 522  TYR B O   1 
ATOM   4684 C  CB  . TYR B 1 298 ? 14.100  33.905 -29.892 1.00 29.46 ? 522  TYR B CB  1 
ATOM   4685 C  CG  . TYR B 1 298 ? 14.221  35.159 -29.039 1.00 29.25 ? 522  TYR B CG  1 
ATOM   4686 C  CD1 . TYR B 1 298 ? 14.066  35.106 -27.654 1.00 27.25 ? 522  TYR B CD1 1 
ATOM   4687 C  CD2 . TYR B 1 298 ? 14.491  36.398 -29.623 1.00 34.13 ? 522  TYR B CD2 1 
ATOM   4688 C  CE1 . TYR B 1 298 ? 14.172  36.254 -26.871 1.00 32.09 ? 522  TYR B CE1 1 
ATOM   4689 C  CE2 . TYR B 1 298 ? 14.602  37.554 -28.849 1.00 33.85 ? 522  TYR B CE2 1 
ATOM   4690 C  CZ  . TYR B 1 298 ? 14.441  37.474 -27.474 1.00 35.03 ? 522  TYR B CZ  1 
ATOM   4691 O  OH  . TYR B 1 298 ? 14.553  38.615 -26.708 1.00 36.90 ? 522  TYR B OH  1 
ATOM   4692 N  N   . SER B 1 299 ? 16.933  33.203 -28.209 1.00 25.73 ? 523  SER B N   1 
ATOM   4693 C  CA  . SER B 1 299 ? 17.557  32.703 -26.992 1.00 30.46 ? 523  SER B CA  1 
ATOM   4694 C  C   . SER B 1 299 ? 16.884  33.323 -25.771 1.00 30.22 ? 523  SER B C   1 
ATOM   4695 O  O   . SER B 1 299 ? 16.859  34.549 -25.623 1.00 32.12 ? 523  SER B O   1 
ATOM   4696 C  CB  . SER B 1 299 ? 19.055  33.009 -26.997 1.00 32.61 ? 523  SER B CB  1 
ATOM   4697 O  OG  . SER B 1 299 ? 19.708  32.343 -25.928 1.00 34.09 ? 523  SER B OG  1 
ATOM   4698 N  N   . LEU B 1 300 ? 16.363  32.480 -24.888 1.00 26.37 ? 524  LEU B N   1 
ATOM   4699 C  CA  . LEU B 1 300 ? 15.697  32.938 -23.679 1.00 26.95 ? 524  LEU B CA  1 
ATOM   4700 C  C   . LEU B 1 300 ? 16.660  32.932 -22.502 1.00 30.42 ? 524  LEU B C   1 
ATOM   4701 O  O   . LEU B 1 300 ? 17.497  32.033 -22.378 1.00 30.14 ? 524  LEU B O   1 
ATOM   4702 C  CB  . LEU B 1 300 ? 14.500  32.051 -23.352 1.00 26.78 ? 524  LEU B CB  1 
ATOM   4703 C  CG  . LEU B 1 300 ? 13.304  32.141 -24.290 1.00 28.07 ? 524  LEU B CG  1 
ATOM   4704 C  CD1 . LEU B 1 300 ? 12.266  31.075 -23.936 1.00 24.99 ? 524  LEU B CD1 1 
ATOM   4705 C  CD2 . LEU B 1 300 ? 12.717  33.533 -24.207 1.00 27.95 ? 524  LEU B CD2 1 
ATOM   4706 N  N   . ALA B 1 301 ? 16.531  33.933 -21.634 1.00 32.29 ? 525  ALA B N   1 
ATOM   4707 C  CA  . ALA B 1 301 ? 17.206  33.880 -20.351 1.00 28.42 ? 525  ALA B CA  1 
ATOM   4708 C  C   . ALA B 1 301 ? 16.584  32.784 -19.491 1.00 28.46 ? 525  ALA B C   1 
ATOM   4709 O  O   . ALA B 1 301 ? 15.356  32.639 -19.453 1.00 25.94 ? 525  ALA B O   1 
ATOM   4710 C  CB  . ALA B 1 301 ? 17.118  35.219 -19.623 1.00 33.23 ? 525  ALA B CB  1 
ATOM   4711 N  N   . PRO B 1 302 ? 17.398  31.989 -18.804 1.00 25.29 ? 526  PRO B N   1 
ATOM   4712 C  CA  . PRO B 1 302 ? 16.841  30.906 -17.990 1.00 33.98 ? 526  PRO B CA  1 
ATOM   4713 C  C   . PRO B 1 302 ? 16.044  31.415 -16.793 1.00 38.46 ? 526  PRO B C   1 
ATOM   4714 O  O   . PRO B 1 302 ? 16.327  32.467 -16.215 1.00 35.20 ? 526  PRO B O   1 
ATOM   4715 C  CB  . PRO B 1 302 ? 18.079  30.113 -17.547 1.00 34.60 ? 526  PRO B CB  1 
ATOM   4716 C  CG  . PRO B 1 302 ? 19.249  30.972 -17.849 1.00 37.81 ? 526  PRO B CG  1 
ATOM   4717 C  CD  . PRO B 1 302 ? 18.854  31.869 -18.974 1.00 34.38 ? 526  PRO B CD  1 
ATOM   4718 N  N   . VAL B 1 303 ? 15.019  30.645 -16.444 1.00 35.32 ? 527  VAL B N   1 
ATOM   4719 C  CA  . VAL B 1 303 ? 14.236  30.855 -15.237 1.00 35.61 ? 527  VAL B CA  1 
ATOM   4720 C  C   . VAL B 1 303 ? 14.203  29.536 -14.451 1.00 48.60 ? 527  VAL B C   1 
ATOM   4721 O  O   . VAL B 1 303 ? 13.897  29.458 -13.251 1.00 50.89 ? 527  VAL B O   1 
ATOM   4722 C  CB  . VAL B 1 303 ? 12.831  31.333 -15.579 1.00 36.88 ? 527  VAL B CB  1 
ATOM   4723 C  CG1 . VAL B 1 303 ? 12.139  30.305 -16.456 1.00 30.91 ? 527  VAL B CG1 1 
ATOM   4724 C  CG2 . VAL B 1 303 ? 12.025  31.600 -14.317 1.00 37.96 ? 527  VAL B CG2 1 
ATOM   4725 O  OXT . VAL B 1 303 ? 14.497  28.479 -15.019 1.00 47.13 ? 527  VAL B OXT 1 
HETATM 4726 CL CL  . CL  C 2 .   ? -7.513  44.077 -15.519 1.00 66.65 ? 601  CL  A CL  1 
HETATM 4727 CL CL  . CL  D 2 .   ? -15.152 33.669 -33.590 1.00 66.84 ? 601  CL  B CL  1 
HETATM 4728 O  O   . HOH E 3 .   ? -6.913  27.017 1.301   1.00 35.99 ? 701  HOH A O   1 
HETATM 4729 O  O   . HOH E 3 .   ? -12.258 46.710 5.488   1.00 45.66 ? 702  HOH A O   1 
HETATM 4730 O  O   . HOH E 3 .   ? -21.852 37.147 12.137  1.00 33.65 ? 703  HOH A O   1 
HETATM 4731 O  O   . HOH E 3 .   ? -25.435 22.389 13.152  1.00 48.31 ? 704  HOH A O   1 
HETATM 4732 O  O   . HOH E 3 .   ? -24.497 48.869 -9.695  1.00 27.98 ? 705  HOH A O   1 
HETATM 4733 O  O   . HOH E 3 .   ? -32.099 50.008 -33.397 1.00 26.37 ? 706  HOH A O   1 
HETATM 4734 O  O   . HOH E 3 .   ? -24.589 10.545 -0.419  1.00 41.85 ? 707  HOH A O   1 
HETATM 4735 O  O   . HOH E 3 .   ? -38.741 42.493 -9.492  1.00 35.06 ? 708  HOH A O   1 
HETATM 4736 O  O   . HOH E 3 .   ? -18.014 57.847 -28.563 1.00 39.60 ? 709  HOH A O   1 
HETATM 4737 O  O   . HOH E 3 .   ? -22.153 37.074 -28.426 1.00 24.02 ? 710  HOH A O   1 
HETATM 4738 O  O   . HOH E 3 .   ? -29.694 30.702 -29.949 1.00 24.74 ? 711  HOH A O   1 
HETATM 4739 O  O   . HOH E 3 .   ? -13.752 16.263 15.077  1.00 40.80 ? 712  HOH A O   1 
HETATM 4740 O  O   . HOH E 3 .   ? -37.040 40.432 -13.413 1.00 30.84 ? 713  HOH A O   1 
HETATM 4741 O  O   . HOH E 3 .   ? -38.316 48.831 -25.268 1.00 26.86 ? 714  HOH A O   1 
HETATM 4742 O  O   . HOH E 3 .   ? -31.245 13.042 4.683   1.00 52.98 ? 715  HOH A O   1 
HETATM 4743 O  O   . HOH E 3 .   ? -40.586 42.988 -14.366 1.00 32.31 ? 716  HOH A O   1 
HETATM 4744 O  O   . HOH E 3 .   ? -36.495 25.459 -10.761 1.00 30.70 ? 717  HOH A O   1 
HETATM 4745 O  O   . HOH E 3 .   ? -35.340 28.138 -9.611  1.00 24.00 ? 718  HOH A O   1 
HETATM 4746 O  O   . HOH E 3 .   ? -24.506 31.847 -6.973  1.00 20.47 ? 719  HOH A O   1 
HETATM 4747 O  O   . HOH E 3 .   ? -17.289 30.776 -11.322 1.00 24.98 ? 720  HOH A O   1 
HETATM 4748 O  O   . HOH E 3 .   ? -40.913 30.713 -25.693 1.00 40.03 ? 721  HOH A O   1 
HETATM 4749 O  O   . HOH E 3 .   ? -35.908 43.313 -8.714  1.00 26.42 ? 722  HOH A O   1 
HETATM 4750 O  O   . HOH E 3 .   ? -7.052  43.478 -19.869 1.00 34.92 ? 723  HOH A O   1 
HETATM 4751 O  O   . HOH E 3 .   ? -20.247 39.905 -35.690 1.00 39.70 ? 724  HOH A O   1 
HETATM 4752 O  O   . HOH E 3 .   ? -9.025  22.263 13.846  1.00 38.31 ? 725  HOH A O   1 
HETATM 4753 O  O   . HOH E 3 .   ? -32.587 30.382 -26.074 1.00 21.72 ? 726  HOH A O   1 
HETATM 4754 O  O   . HOH E 3 .   ? -35.852 14.051 -1.430  1.00 36.55 ? 727  HOH A O   1 
HETATM 4755 O  O   . HOH E 3 .   ? -36.091 48.898 -18.917 1.00 30.90 ? 728  HOH A O   1 
HETATM 4756 O  O   . HOH E 3 .   ? -15.593 31.592 -19.568 1.00 23.08 ? 729  HOH A O   1 
HETATM 4757 O  O   B HOH E 3 .   ? -24.132 42.049 -13.715 0.46 20.56 ? 730  HOH A O   1 
HETATM 4758 O  O   . HOH E 3 .   ? -26.325 23.572 -18.039 1.00 18.99 ? 731  HOH A O   1 
HETATM 4759 O  O   . HOH E 3 .   ? -33.447 59.847 -26.057 1.00 39.14 ? 732  HOH A O   1 
HETATM 4760 O  O   . HOH E 3 .   ? -4.841  19.345 -3.431  1.00 32.57 ? 733  HOH A O   1 
HETATM 4761 O  O   . HOH E 3 .   ? -37.076 23.697 -7.152  1.00 33.63 ? 734  HOH A O   1 
HETATM 4762 O  O   . HOH E 3 .   ? -15.328 46.865 -20.311 1.00 23.25 ? 735  HOH A O   1 
HETATM 4763 O  O   . HOH E 3 .   ? -26.987 30.788 -29.908 1.00 18.11 ? 736  HOH A O   1 
HETATM 4764 O  O   . HOH E 3 .   ? -20.546 52.021 -13.652 1.00 36.22 ? 737  HOH A O   1 
HETATM 4765 O  O   . HOH E 3 .   ? -22.891 35.437 -3.188  1.00 21.42 ? 738  HOH A O   1 
HETATM 4766 O  O   . HOH E 3 .   ? -26.030 14.152 0.388   1.00 38.22 ? 739  HOH A O   1 
HETATM 4767 O  O   . HOH E 3 .   ? -15.714 37.558 4.102   1.00 32.39 ? 740  HOH A O   1 
HETATM 4768 O  O   . HOH E 3 .   ? -25.705 46.626 -10.942 1.00 27.91 ? 741  HOH A O   1 
HETATM 4769 O  O   . HOH E 3 .   ? -13.378 37.262 -0.779  1.00 27.85 ? 742  HOH A O   1 
HETATM 4770 O  O   . HOH E 3 .   ? -23.019 20.650 -11.835 1.00 21.30 ? 743  HOH A O   1 
HETATM 4771 O  O   . HOH E 3 .   ? -18.155 46.728 -31.485 1.00 27.46 ? 744  HOH A O   1 
HETATM 4772 O  O   . HOH E 3 .   ? -30.194 21.320 6.507   1.00 38.56 ? 745  HOH A O   1 
HETATM 4773 O  O   . HOH E 3 .   ? -48.403 42.542 -20.894 1.00 35.65 ? 746  HOH A O   1 
HETATM 4774 O  O   . HOH E 3 .   ? -37.896 35.872 -12.109 1.00 33.56 ? 747  HOH A O   1 
HETATM 4775 O  O   . HOH E 3 .   ? -9.472  18.155 -2.733  1.00 20.75 ? 748  HOH A O   1 
HETATM 4776 O  O   . HOH E 3 .   ? -38.380 41.408 -15.716 1.00 24.64 ? 749  HOH A O   1 
HETATM 4777 O  O   . HOH E 3 .   ? -29.742 40.393 -17.653 1.00 18.47 ? 750  HOH A O   1 
HETATM 4778 O  O   . HOH E 3 .   ? -12.615 43.113 -28.424 1.00 42.02 ? 751  HOH A O   1 
HETATM 4779 O  O   . HOH E 3 .   ? -5.951  22.427 6.370   1.00 27.44 ? 752  HOH A O   1 
HETATM 4780 O  O   . HOH E 3 .   ? -14.587 48.762 -1.741  1.00 46.69 ? 753  HOH A O   1 
HETATM 4781 O  O   . HOH E 3 .   ? -13.051 33.893 -21.039 1.00 32.20 ? 754  HOH A O   1 
HETATM 4782 O  O   . HOH E 3 .   ? -32.781 32.939 -41.368 1.00 39.30 ? 755  HOH A O   1 
HETATM 4783 O  O   . HOH E 3 .   ? -41.698 42.652 -32.932 1.00 36.88 ? 756  HOH A O   1 
HETATM 4784 O  O   . HOH E 3 .   ? -14.421 18.263 -3.956  1.00 20.81 ? 757  HOH A O   1 
HETATM 4785 O  O   . HOH E 3 .   ? -23.112 23.410 -24.100 1.00 32.59 ? 758  HOH A O   1 
HETATM 4786 O  O   . HOH E 3 .   ? -12.780 20.860 -7.226  1.00 23.43 ? 759  HOH A O   1 
HETATM 4787 O  O   . HOH E 3 .   ? -28.623 31.963 5.317   1.00 22.21 ? 760  HOH A O   1 
HETATM 4788 O  O   . HOH E 3 .   ? -38.927 56.209 -26.101 1.00 30.08 ? 761  HOH A O   1 
HETATM 4789 O  O   . HOH E 3 .   ? -37.534 27.514 -18.695 1.00 23.25 ? 762  HOH A O   1 
HETATM 4790 O  O   . HOH E 3 .   ? -19.155 30.445 -13.841 1.00 22.42 ? 763  HOH A O   1 
HETATM 4791 O  O   . HOH E 3 .   ? -9.031  22.980 -2.833  1.00 26.86 ? 764  HOH A O   1 
HETATM 4792 O  O   . HOH E 3 .   ? -12.343 46.652 -14.825 1.00 39.17 ? 765  HOH A O   1 
HETATM 4793 O  O   . HOH E 3 .   ? -29.513 20.095 -17.069 1.00 29.26 ? 766  HOH A O   1 
HETATM 4794 O  O   . HOH E 3 .   ? -17.417 6.309  3.802   1.00 33.39 ? 767  HOH A O   1 
HETATM 4795 O  O   . HOH E 3 .   ? -43.359 44.606 -24.796 1.00 29.78 ? 768  HOH A O   1 
HETATM 4796 O  O   . HOH E 3 .   ? -43.991 42.594 -17.968 1.00 33.49 ? 769  HOH A O   1 
HETATM 4797 O  O   . HOH E 3 .   ? -22.347 31.254 -34.497 1.00 30.59 ? 770  HOH A O   1 
HETATM 4798 O  O   . HOH E 3 .   ? -25.626 38.520 7.127   1.00 26.89 ? 771  HOH A O   1 
HETATM 4799 O  O   . HOH E 3 .   ? -14.658 46.365 -25.483 1.00 37.93 ? 772  HOH A O   1 
HETATM 4800 O  O   A HOH E 3 .   ? -14.204 22.906 -8.709  0.91 26.22 ? 773  HOH A O   1 
HETATM 4801 O  O   . HOH E 3 .   ? -24.366 36.218 -27.625 1.00 22.11 ? 774  HOH A O   1 
HETATM 4802 O  O   . HOH E 3 .   ? -20.250 40.134 -30.695 1.00 24.70 ? 775  HOH A O   1 
HETATM 4803 O  O   A HOH E 3 .   ? -24.481 43.637 -12.412 0.89 18.89 ? 776  HOH A O   1 
HETATM 4804 O  O   . HOH E 3 .   ? -28.758 51.837 -17.727 1.00 29.39 ? 777  HOH A O   1 
HETATM 4805 O  O   . HOH E 3 .   ? -9.235  32.258 6.128   1.00 33.78 ? 778  HOH A O   1 
HETATM 4806 O  O   . HOH E 3 .   ? -26.413 27.677 -29.010 1.00 23.33 ? 779  HOH A O   1 
HETATM 4807 O  O   . HOH E 3 .   ? -9.609  7.775  4.063   1.00 34.65 ? 780  HOH A O   1 
HETATM 4808 O  O   . HOH E 3 .   ? -29.720 40.679 5.498   1.00 32.22 ? 781  HOH A O   1 
HETATM 4809 O  O   . HOH E 3 .   ? -13.057 52.394 -18.011 1.00 42.05 ? 782  HOH A O   1 
HETATM 4810 O  O   . HOH E 3 .   ? -16.102 40.563 -30.267 1.00 29.94 ? 783  HOH A O   1 
HETATM 4811 O  O   . HOH E 3 .   ? -13.316 33.402 -2.209  1.00 25.89 ? 784  HOH A O   1 
HETATM 4812 O  O   . HOH E 3 .   ? -40.306 21.753 0.257   1.00 53.60 ? 785  HOH A O   1 
HETATM 4813 O  O   . HOH E 3 .   ? -8.208  15.551 -2.839  1.00 25.19 ? 786  HOH A O   1 
HETATM 4814 O  O   . HOH E 3 .   ? -14.153 39.386 0.100   1.00 36.27 ? 787  HOH A O   1 
HETATM 4815 O  O   . HOH E 3 .   ? -18.625 21.492 -10.438 1.00 24.64 ? 788  HOH A O   1 
HETATM 4816 O  O   . HOH E 3 .   ? -36.610 34.197 -13.278 1.00 32.60 ? 789  HOH A O   1 
HETATM 4817 O  O   . HOH E 3 .   ? -22.856 40.734 4.379   1.00 24.97 ? 790  HOH A O   1 
HETATM 4818 O  O   . HOH E 3 .   ? -26.696 22.153 -15.563 1.00 21.34 ? 791  HOH A O   1 
HETATM 4819 O  O   . HOH E 3 .   ? -13.977 29.055 0.374   1.00 24.80 ? 792  HOH A O   1 
HETATM 4820 O  O   . HOH E 3 .   ? -20.963 45.288 -4.634  1.00 28.32 ? 793  HOH A O   1 
HETATM 4821 O  O   . HOH E 3 .   ? -35.344 47.106 -8.413  1.00 35.76 ? 794  HOH A O   1 
HETATM 4822 O  O   . HOH E 3 .   ? -19.892 35.206 -10.990 1.00 26.59 ? 795  HOH A O   1 
HETATM 4823 O  O   . HOH E 3 .   ? -27.137 32.118 7.810   1.00 29.21 ? 796  HOH A O   1 
HETATM 4824 O  O   . HOH E 3 .   ? -31.768 37.816 -5.447  1.00 23.48 ? 797  HOH A O   1 
HETATM 4825 O  O   . HOH E 3 .   ? -20.476 27.028 10.737  1.00 31.22 ? 798  HOH A O   1 
HETATM 4826 O  O   . HOH E 3 .   ? -33.261 45.246 -2.479  1.00 35.61 ? 799  HOH A O   1 
HETATM 4827 O  O   . HOH E 3 .   ? -18.066 50.375 3.979   1.00 31.95 ? 800  HOH A O   1 
HETATM 4828 O  O   . HOH E 3 .   ? -20.576 14.261 19.772  1.00 50.36 ? 801  HOH A O   1 
HETATM 4829 O  O   . HOH E 3 .   ? -38.427 23.753 -10.181 1.00 34.98 ? 802  HOH A O   1 
HETATM 4830 O  O   . HOH E 3 .   ? -6.708  7.957  4.356   1.00 38.42 ? 803  HOH A O   1 
HETATM 4831 O  O   . HOH E 3 .   ? -32.981 38.001 -0.555  1.00 28.81 ? 804  HOH A O   1 
HETATM 4832 O  O   . HOH E 3 .   ? -10.601 9.560  7.318   1.00 47.30 ? 805  HOH A O   1 
HETATM 4833 O  O   . HOH E 3 .   ? 2.276   10.338 1.581   1.00 44.65 ? 806  HOH A O   1 
HETATM 4834 O  O   . HOH E 3 .   ? -30.009 35.637 -5.682  1.00 21.73 ? 807  HOH A O   1 
HETATM 4835 O  O   . HOH E 3 .   ? -24.197 23.326 16.736  1.00 46.90 ? 808  HOH A O   1 
HETATM 4836 O  O   . HOH E 3 .   ? -24.970 23.100 6.337   1.00 30.75 ? 809  HOH A O   1 
HETATM 4837 O  O   . HOH E 3 .   ? -16.963 29.900 -23.230 1.00 21.85 ? 810  HOH A O   1 
HETATM 4838 O  O   . HOH E 3 .   ? -30.604 16.313 -12.338 1.00 24.87 ? 811  HOH A O   1 
HETATM 4839 O  O   . HOH E 3 .   ? -37.075 32.337 -32.934 1.00 34.00 ? 812  HOH A O   1 
HETATM 4840 O  O   . HOH E 3 .   ? -11.059 38.403 -17.529 1.00 24.30 ? 813  HOH A O   1 
HETATM 4841 O  O   . HOH E 3 .   ? -17.436 54.092 -17.981 1.00 39.35 ? 814  HOH A O   1 
HETATM 4842 O  O   . HOH E 3 .   ? -46.397 34.186 -18.383 1.00 32.14 ? 815  HOH A O   1 
HETATM 4843 O  O   . HOH E 3 .   ? -18.281 6.284  6.433   1.00 41.83 ? 816  HOH A O   1 
HETATM 4844 O  O   . HOH E 3 .   ? -8.484  27.641 7.299   1.00 32.84 ? 817  HOH A O   1 
HETATM 4845 O  O   . HOH E 3 .   ? -36.636 43.211 -27.491 1.00 22.51 ? 818  HOH A O   1 
HETATM 4846 O  O   . HOH E 3 .   ? -30.234 48.748 -10.182 1.00 33.21 ? 819  HOH A O   1 
HETATM 4847 O  O   . HOH E 3 .   ? -25.856 37.497 -12.519 1.00 21.96 ? 820  HOH A O   1 
HETATM 4848 O  O   . HOH E 3 .   ? -23.109 40.464 7.180   1.00 28.90 ? 821  HOH A O   1 
HETATM 4849 O  O   . HOH E 3 .   ? -23.358 54.850 -30.633 1.00 24.83 ? 822  HOH A O   1 
HETATM 4850 O  O   . HOH E 3 .   ? -43.332 36.181 -12.602 1.00 45.75 ? 823  HOH A O   1 
HETATM 4851 O  O   A HOH E 3 .   ? -23.196 26.133 7.406   1.00 27.56 ? 824  HOH A O   1 
HETATM 4852 O  O   . HOH E 3 .   ? -24.062 24.820 -33.104 1.00 35.46 ? 825  HOH A O   1 
HETATM 4853 O  O   . HOH E 3 .   ? -17.668 52.438 -28.224 1.00 29.98 ? 826  HOH A O   1 
HETATM 4854 O  O   . HOH E 3 .   ? -23.389 24.942 -37.083 1.00 41.40 ? 827  HOH A O   1 
HETATM 4855 O  O   . HOH E 3 .   ? -35.815 28.944 -6.950  1.00 27.17 ? 828  HOH A O   1 
HETATM 4856 O  O   . HOH E 3 .   ? -31.212 47.321 -4.240  1.00 30.16 ? 829  HOH A O   1 
HETATM 4857 O  O   . HOH E 3 .   ? -32.264 37.395 2.423   1.00 36.60 ? 830  HOH A O   1 
HETATM 4858 O  O   B HOH E 3 .   ? -13.302 24.655 -8.972  0.61 22.79 ? 831  HOH A O   1 
HETATM 4859 O  O   . HOH E 3 .   ? -20.431 24.178 -25.570 1.00 40.22 ? 832  HOH A O   1 
HETATM 4860 O  O   A HOH E 3 .   ? -39.123 32.429 -28.127 1.00 33.21 ? 833  HOH A O   1 
HETATM 4861 O  O   . HOH E 3 .   ? -10.259 40.404 -9.657  1.00 49.97 ? 834  HOH A O   1 
HETATM 4862 O  O   . HOH E 3 .   ? -15.289 7.959  -2.795  1.00 35.79 ? 835  HOH A O   1 
HETATM 4863 O  O   . HOH E 3 .   ? -32.684 32.936 -38.660 1.00 32.00 ? 836  HOH A O   1 
HETATM 4864 O  O   . HOH E 3 .   ? -20.567 21.717 -12.566 1.00 27.24 ? 837  HOH A O   1 
HETATM 4865 O  O   . HOH E 3 .   ? -16.079 41.443 -6.643  1.00 28.64 ? 838  HOH A O   1 
HETATM 4866 O  O   . HOH E 3 .   ? -43.992 43.878 -20.419 1.00 36.69 ? 839  HOH A O   1 
HETATM 4867 O  O   . HOH E 3 .   ? -26.078 43.411 11.304  1.00 31.52 ? 840  HOH A O   1 
HETATM 4868 O  O   . HOH E 3 .   ? -9.251  7.174  1.472   1.00 45.15 ? 841  HOH A O   1 
HETATM 4869 O  O   . HOH E 3 .   ? -11.172 34.490 -10.111 1.00 29.86 ? 842  HOH A O   1 
HETATM 4870 O  O   . HOH E 3 .   ? -16.749 46.369 5.073   1.00 37.65 ? 843  HOH A O   1 
HETATM 4871 O  O   . HOH E 3 .   ? -18.567 34.870 -8.741  1.00 20.48 ? 844  HOH A O   1 
HETATM 4872 O  O   . HOH E 3 .   ? -32.854 22.932 -1.786  1.00 28.18 ? 845  HOH A O   1 
HETATM 4873 O  O   . HOH E 3 .   ? -19.215 55.948 -17.750 1.00 40.37 ? 846  HOH A O   1 
HETATM 4874 O  O   . HOH E 3 .   ? -13.256 35.231 10.624  1.00 40.45 ? 847  HOH A O   1 
HETATM 4875 O  O   A HOH E 3 .   ? -30.922 31.284 9.086   1.00 39.49 ? 848  HOH A O   1 
HETATM 4876 O  O   . HOH E 3 .   ? -39.561 16.487 -3.801  1.00 34.89 ? 849  HOH A O   1 
HETATM 4877 O  O   . HOH E 3 .   ? -19.853 43.149 -30.461 1.00 22.72 ? 850  HOH A O   1 
HETATM 4878 O  O   . HOH E 3 .   ? -17.696 22.944 -13.857 1.00 27.53 ? 851  HOH A O   1 
HETATM 4879 O  O   . HOH E 3 .   ? -27.460 50.728 -15.463 1.00 26.16 ? 852  HOH A O   1 
HETATM 4880 O  O   . HOH E 3 .   ? -17.149 43.170 -5.201  1.00 31.77 ? 853  HOH A O   1 
HETATM 4881 O  O   . HOH E 3 .   ? -20.423 32.719 14.878  1.00 45.07 ? 854  HOH A O   1 
HETATM 4882 O  O   . HOH E 3 .   ? -35.477 21.367 -15.760 1.00 30.36 ? 855  HOH A O   1 
HETATM 4883 O  O   . HOH E 3 .   ? -27.225 57.707 -21.368 1.00 27.96 ? 856  HOH A O   1 
HETATM 4884 O  O   . HOH E 3 .   ? -18.528 61.367 -29.469 1.00 27.08 ? 857  HOH A O   1 
HETATM 4885 O  O   . HOH E 3 .   ? -28.743 20.689 -19.256 1.00 38.47 ? 858  HOH A O   1 
HETATM 4886 O  O   . HOH E 3 .   ? -37.460 31.513 -9.955  1.00 30.78 ? 859  HOH A O   1 
HETATM 4887 O  O   . HOH E 3 .   ? -33.035 30.906 5.888   1.00 40.56 ? 860  HOH A O   1 
HETATM 4888 O  O   . HOH E 3 .   ? -20.077 59.929 -22.364 1.00 41.37 ? 861  HOH A O   1 
HETATM 4889 O  O   B HOH E 3 .   ? -24.980 25.411 7.073   0.56 27.90 ? 862  HOH A O   1 
HETATM 4890 O  O   . HOH E 3 .   ? -32.194 41.258 -40.677 1.00 37.04 ? 863  HOH A O   1 
HETATM 4891 O  O   . HOH E 3 .   ? -37.104 42.697 -11.516 1.00 33.92 ? 864  HOH A O   1 
HETATM 4892 O  O   . HOH E 3 .   ? -37.772 25.355 -21.523 1.00 30.19 ? 865  HOH A O   1 
HETATM 4893 O  O   . HOH E 3 .   ? -9.696  41.143 -23.751 1.00 39.53 ? 866  HOH A O   1 
HETATM 4894 O  O   . HOH E 3 .   ? -36.338 11.618 -4.822  1.00 34.83 ? 867  HOH A O   1 
HETATM 4895 O  O   . HOH E 3 .   ? -23.808 12.756 1.513   1.00 37.16 ? 868  HOH A O   1 
HETATM 4896 O  O   . HOH E 3 .   ? -29.391 46.527 -1.081  1.00 38.11 ? 869  HOH A O   1 
HETATM 4897 O  O   B HOH E 3 .   ? -29.217 19.009 5.482   1.00 50.10 ? 870  HOH A O   1 
HETATM 4898 O  O   . HOH E 3 .   ? -18.659 31.475 -31.495 1.00 30.33 ? 871  HOH A O   1 
HETATM 4899 O  O   . HOH E 3 .   ? -36.703 36.673 -33.924 1.00 45.90 ? 872  HOH A O   1 
HETATM 4900 O  O   . HOH E 3 .   ? -37.339 26.638 3.050   1.00 49.50 ? 873  HOH A O   1 
HETATM 4901 O  O   . HOH E 3 .   ? -36.719 37.224 -3.624  1.00 40.87 ? 874  HOH A O   1 
HETATM 4902 O  O   . HOH E 3 .   ? -8.535  22.584 0.102   1.00 31.95 ? 875  HOH A O   1 
HETATM 4903 O  O   . HOH E 3 .   ? -16.073 23.863 -11.957 1.00 35.15 ? 876  HOH A O   1 
HETATM 4904 O  O   . HOH E 3 .   ? -7.893  19.475 -0.489  1.00 27.82 ? 877  HOH A O   1 
HETATM 4905 O  O   . HOH E 3 .   ? -16.519 30.690 -1.135  1.00 33.33 ? 878  HOH A O   1 
HETATM 4906 O  O   . HOH E 3 .   ? -44.328 47.304 -18.123 1.00 35.39 ? 879  HOH A O   1 
HETATM 4907 O  O   . HOH E 3 .   ? -43.077 51.483 -24.242 1.00 41.12 ? 880  HOH A O   1 
HETATM 4908 O  O   . HOH E 3 .   ? -30.265 40.779 2.330   1.00 31.11 ? 881  HOH A O   1 
HETATM 4909 O  O   . HOH E 3 .   ? -37.417 29.307 -10.888 1.00 35.20 ? 882  HOH A O   1 
HETATM 4910 O  O   . HOH E 3 .   ? -26.203 46.210 1.112   1.00 27.60 ? 883  HOH A O   1 
HETATM 4911 O  O   . HOH E 3 .   ? -38.907 24.104 1.808   1.00 62.07 ? 884  HOH A O   1 
HETATM 4912 O  O   . HOH E 3 .   ? -11.379 37.260 -9.486  1.00 39.84 ? 885  HOH A O   1 
HETATM 4913 O  O   . HOH E 3 .   ? -21.368 24.345 -28.468 1.00 35.04 ? 886  HOH A O   1 
HETATM 4914 O  O   . HOH E 3 .   ? -6.233  7.256  0.985   1.00 41.57 ? 887  HOH A O   1 
HETATM 4915 O  O   . HOH E 3 .   ? -18.239 58.304 -20.614 1.00 37.31 ? 888  HOH A O   1 
HETATM 4916 O  O   A HOH E 3 .   ? -10.200 30.794 -8.019  1.00 34.03 ? 889  HOH A O   1 
HETATM 4917 O  O   . HOH E 3 .   ? -32.748 48.540 -11.822 1.00 33.51 ? 890  HOH A O   1 
HETATM 4918 O  O   . HOH E 3 .   ? -7.488  41.175 -23.154 1.00 32.95 ? 891  HOH A O   1 
HETATM 4919 O  O   . HOH E 3 .   ? -7.538  46.963 -21.272 1.00 47.60 ? 892  HOH A O   1 
HETATM 4920 O  O   . HOH E 3 .   ? -7.863  23.999 1.992   1.00 28.75 ? 893  HOH A O   1 
HETATM 4921 O  O   . HOH E 3 .   ? -31.495 29.766 -28.285 1.00 30.94 ? 894  HOH A O   1 
HETATM 4922 O  O   . HOH E 3 .   ? -34.463 36.225 3.577   1.00 46.24 ? 895  HOH A O   1 
HETATM 4923 O  O   . HOH E 3 .   ? -12.567 49.401 -32.561 1.00 47.07 ? 896  HOH A O   1 
HETATM 4924 O  O   . HOH E 3 .   ? -9.719  25.731 11.641  1.00 36.17 ? 897  HOH A O   1 
HETATM 4925 O  O   . HOH E 3 .   ? -32.431 25.816 7.581   1.00 40.24 ? 898  HOH A O   1 
HETATM 4926 O  O   . HOH E 3 .   ? -15.955 45.538 -23.592 1.00 29.74 ? 899  HOH A O   1 
HETATM 4927 O  O   . HOH E 3 .   ? -40.230 43.374 -11.566 1.00 53.32 ? 900  HOH A O   1 
HETATM 4928 O  O   . HOH E 3 .   ? -16.906 23.371 -9.821  1.00 23.38 ? 901  HOH A O   1 
HETATM 4929 O  O   . HOH E 3 .   ? -34.182 57.137 -27.039 1.00 31.91 ? 902  HOH A O   1 
HETATM 4930 O  O   . HOH E 3 .   ? -10.985 35.816 -17.627 1.00 27.10 ? 903  HOH A O   1 
HETATM 4931 O  O   B HOH E 3 .   ? -39.158 33.300 -30.023 1.00 40.58 ? 904  HOH A O   1 
HETATM 4932 O  O   . HOH E 3 .   ? -10.698 34.490 -4.004  1.00 33.89 ? 905  HOH A O   1 
HETATM 4933 O  O   . HOH E 3 .   ? -32.997 40.286 -1.992  1.00 38.57 ? 906  HOH A O   1 
HETATM 4934 O  O   . HOH E 3 .   ? -11.720 46.616 -12.238 1.00 44.92 ? 907  HOH A O   1 
HETATM 4935 O  O   . HOH E 3 .   ? -39.697 19.662 -0.878  1.00 53.22 ? 908  HOH A O   1 
HETATM 4936 O  O   . HOH E 3 .   ? -12.424 26.867 -7.017  1.00 29.55 ? 909  HOH A O   1 
HETATM 4937 O  O   . HOH E 3 .   ? -30.800 44.335 -38.232 1.00 26.55 ? 910  HOH A O   1 
HETATM 4938 O  O   . HOH E 3 .   ? -28.338 43.603 -39.108 1.00 28.47 ? 911  HOH A O   1 
HETATM 4939 O  O   . HOH E 3 .   ? -40.703 48.725 -25.627 1.00 32.66 ? 912  HOH A O   1 
HETATM 4940 O  O   . HOH E 3 .   ? -26.186 20.480 6.194   1.00 35.51 ? 913  HOH A O   1 
HETATM 4941 O  O   . HOH E 3 .   ? -21.878 29.728 -36.311 1.00 38.31 ? 914  HOH A O   1 
HETATM 4942 O  O   . HOH E 3 .   ? -19.650 34.983 -37.317 1.00 43.91 ? 915  HOH A O   1 
HETATM 4943 O  O   . HOH E 3 .   ? -23.047 57.733 -19.781 1.00 46.33 ? 916  HOH A O   1 
HETATM 4944 O  O   . HOH E 3 .   ? -44.183 42.459 -25.610 1.00 32.75 ? 917  HOH A O   1 
HETATM 4945 O  O   . HOH E 3 .   ? -6.900  26.482 5.658   1.00 33.34 ? 918  HOH A O   1 
HETATM 4946 O  O   . HOH E 3 .   ? -6.384  24.067 4.506   1.00 30.51 ? 919  HOH A O   1 
HETATM 4947 O  O   B HOH E 3 .   ? -10.397 32.247 -6.932  0.85 33.31 ? 920  HOH A O   1 
HETATM 4948 O  O   B HOH E 3 .   ? -29.924 32.874 9.439   1.00 53.44 ? 921  HOH A O   1 
HETATM 4949 O  O   . HOH E 3 .   ? -22.262 47.173 -5.363  1.00 31.09 ? 922  HOH A O   1 
HETATM 4950 O  O   . HOH E 3 .   ? -10.604 37.224 -2.522  1.00 39.09 ? 923  HOH A O   1 
HETATM 4951 O  O   B HOH E 3 .   ? -14.540 36.227 -23.620 1.00 39.11 ? 924  HOH A O   1 
HETATM 4952 O  O   . HOH E 3 .   ? -10.253 21.478 -6.593  1.00 19.19 ? 925  HOH A O   1 
HETATM 4953 O  O   . HOH E 3 .   ? -39.672 26.132 0.780   1.00 44.46 ? 926  HOH A O   1 
HETATM 4954 O  O   . HOH E 3 .   ? -8.906  20.546 -4.183  1.00 23.96 ? 927  HOH A O   1 
HETATM 4955 O  O   . HOH E 3 .   ? -46.599 44.612 -21.849 1.00 41.47 ? 928  HOH A O   1 
HETATM 4956 O  O   . HOH E 3 .   ? -25.299 48.900 1.105   1.00 35.51 ? 929  HOH A O   1 
HETATM 4957 O  O   . HOH E 3 .   ? -45.080 48.924 -24.703 1.00 44.23 ? 930  HOH A O   1 
HETATM 4958 O  O   . HOH E 3 .   ? -26.308 22.357 8.293   1.00 38.44 ? 931  HOH A O   1 
HETATM 4959 O  O   . HOH E 3 .   ? -40.192 27.784 -19.111 1.00 38.03 ? 932  HOH A O   1 
HETATM 4960 O  O   B HOH E 3 .   ? -47.253 36.509 -16.297 1.00 48.46 ? 933  HOH A O   1 
HETATM 4961 O  O   . HOH E 3 .   ? -28.179 48.217 -11.067 1.00 34.43 ? 934  HOH A O   1 
HETATM 4962 O  O   . HOH E 3 .   ? -5.132  45.566 -20.554 1.00 42.71 ? 935  HOH A O   1 
HETATM 4963 O  O   . HOH E 3 .   ? -23.215 48.962 -7.175  1.00 31.61 ? 936  HOH A O   1 
HETATM 4964 O  O   . HOH E 3 .   ? -1.898  19.696 -3.359  1.00 34.48 ? 937  HOH A O   1 
HETATM 4965 O  O   . HOH E 3 .   ? -20.125 31.372 -33.323 1.00 39.30 ? 938  HOH A O   1 
HETATM 4966 O  O   . HOH E 3 .   ? -19.260 40.717 -33.049 1.00 28.10 ? 939  HOH A O   1 
HETATM 4967 O  O   . HOH E 3 .   ? -29.068 26.802 -27.864 1.00 31.95 ? 940  HOH A O   1 
HETATM 4968 O  O   . HOH E 3 .   ? -5.759  31.276 6.554   1.00 44.43 ? 941  HOH A O   1 
HETATM 4969 O  O   . HOH E 3 .   ? -10.809 35.753 -20.347 1.00 30.58 ? 942  HOH A O   1 
HETATM 4970 O  O   . HOH E 3 .   ? -28.698 50.396 -8.931  1.00 38.02 ? 943  HOH A O   1 
HETATM 4971 O  O   . HOH E 3 .   ? -22.259 57.197 -29.586 1.00 31.53 ? 944  HOH A O   1 
HETATM 4972 O  O   . HOH E 3 .   ? -5.558  20.374 -1.218  1.00 29.92 ? 945  HOH A O   1 
HETATM 4973 O  O   . HOH E 3 .   ? -36.650 45.216 -6.694  1.00 34.23 ? 946  HOH A O   1 
HETATM 4974 O  O   C HOH E 3 .   ? -48.680 36.150 -18.655 0.94 47.61 ? 947  HOH A O   1 
HETATM 4975 O  O   . HOH E 3 .   ? -40.410 56.045 -19.083 1.00 42.97 ? 948  HOH A O   1 
HETATM 4976 O  O   . HOH E 3 .   ? -29.746 51.070 -6.612  1.00 39.16 ? 949  HOH A O   1 
HETATM 4977 O  O   . HOH E 3 .   ? -29.185 50.252 -12.892 1.00 34.76 ? 950  HOH A O   1 
HETATM 4978 O  O   . HOH F 3 .   ? -23.573 5.681  -3.835  1.00 37.57 ? 701  HOH B O   1 
HETATM 4979 O  O   . HOH F 3 .   ? -28.150 -6.267 -14.424 1.00 48.83 ? 702  HOH B O   1 
HETATM 4980 O  O   . HOH F 3 .   ? 13.445  18.161 -26.686 1.00 38.89 ? 703  HOH B O   1 
HETATM 4981 O  O   . HOH F 3 .   ? 2.068   42.842 -6.999  1.00 48.77 ? 704  HOH B O   1 
HETATM 4982 O  O   . HOH F 3 .   ? 7.517   18.147 -22.329 1.00 25.70 ? 705  HOH B O   1 
HETATM 4983 O  O   . HOH F 3 .   ? -0.808  21.703 -34.558 1.00 24.41 ? 706  HOH B O   1 
HETATM 4984 O  O   . HOH F 3 .   ? -8.665  30.705 -10.879 1.00 31.15 ? 707  HOH B O   1 
HETATM 4985 O  O   . HOH F 3 .   ? 3.945   19.355 -32.529 1.00 31.61 ? 708  HOH B O   1 
HETATM 4986 O  O   . HOH F 3 .   ? 2.750   9.283  -17.680 1.00 30.98 ? 709  HOH B O   1 
HETATM 4987 O  O   . HOH F 3 .   ? -28.162 15.092 -24.395 1.00 38.09 ? 710  HOH B O   1 
HETATM 4988 O  O   . HOH F 3 .   ? 0.341   35.553 -11.457 1.00 25.27 ? 711  HOH B O   1 
HETATM 4989 O  O   . HOH F 3 .   ? -43.133 15.735 -12.101 1.00 38.90 ? 712  HOH B O   1 
HETATM 4990 O  O   . HOH F 3 .   ? -18.209 16.825 -30.279 1.00 24.13 ? 713  HOH B O   1 
HETATM 4991 O  O   . HOH F 3 .   ? -15.410 11.994 -33.406 1.00 30.38 ? 714  HOH B O   1 
HETATM 4992 O  O   . HOH F 3 .   ? 15.346  19.239 -20.370 1.00 33.67 ? 715  HOH B O   1 
HETATM 4993 O  O   . HOH F 3 .   ? -16.298 0.769  -20.206 1.00 29.08 ? 716  HOH B O   1 
HETATM 4994 O  O   . HOH F 3 .   ? -23.334 15.920 -38.283 1.00 33.54 ? 717  HOH B O   1 
HETATM 4995 O  O   . HOH F 3 .   ? -24.956 1.030  -26.466 1.00 37.72 ? 718  HOH B O   1 
HETATM 4996 O  O   . HOH F 3 .   ? -4.980  4.077  -23.811 1.00 32.18 ? 719  HOH B O   1 
HETATM 4997 O  O   . HOH F 3 .   ? -20.967 -1.187 -4.955  1.00 31.00 ? 720  HOH B O   1 
HETATM 4998 O  O   . HOH F 3 .   ? -6.286  20.878 -5.237  1.00 35.28 ? 721  HOH B O   1 
HETATM 4999 O  O   . HOH F 3 .   ? -9.010  -0.502 -16.602 1.00 34.52 ? 722  HOH B O   1 
HETATM 5000 O  O   . HOH F 3 .   ? -3.599  4.478  -16.817 1.00 32.59 ? 723  HOH B O   1 
HETATM 5001 O  O   . HOH F 3 .   ? 3.365   29.319 -10.444 1.00 29.25 ? 724  HOH B O   1 
HETATM 5002 O  O   . HOH F 3 .   ? -32.567 10.187 -22.237 1.00 26.36 ? 725  HOH B O   1 
HETATM 5003 O  O   . HOH F 3 .   ? 1.044   10.567 -24.885 1.00 26.86 ? 726  HOH B O   1 
HETATM 5004 O  O   . HOH F 3 .   ? -33.036 1.944  -23.631 1.00 34.68 ? 727  HOH B O   1 
HETATM 5005 O  O   . HOH F 3 .   ? -23.976 15.208 -12.519 1.00 18.34 ? 728  HOH B O   1 
HETATM 5006 O  O   . HOH F 3 .   ? -28.555 4.921  -3.452  1.00 32.25 ? 729  HOH B O   1 
HETATM 5007 O  O   . HOH F 3 .   ? 19.845  31.093 -30.210 1.00 36.32 ? 730  HOH B O   1 
HETATM 5008 O  O   . HOH F 3 .   ? -1.646  37.422 -18.903 1.00 25.81 ? 731  HOH B O   1 
HETATM 5009 O  O   . HOH F 3 .   ? -0.417  43.372 -28.853 1.00 33.79 ? 732  HOH B O   1 
HETATM 5010 O  O   . HOH F 3 .   ? -23.560 16.262 -34.058 1.00 27.03 ? 733  HOH B O   1 
HETATM 5011 O  O   . HOH F 3 .   ? -2.739  24.394 -27.047 1.00 30.33 ? 734  HOH B O   1 
HETATM 5012 O  O   . HOH F 3 .   ? -18.047 7.971  -1.175  1.00 48.32 ? 735  HOH B O   1 
HETATM 5013 O  O   . HOH F 3 .   ? -8.332  -1.280 -22.397 1.00 30.31 ? 736  HOH B O   1 
HETATM 5014 O  O   . HOH F 3 .   ? -7.208  6.304  -11.494 1.00 30.07 ? 737  HOH B O   1 
HETATM 5015 O  O   . HOH F 3 .   ? -6.943  40.772 -11.745 1.00 40.45 ? 738  HOH B O   1 
HETATM 5016 O  O   . HOH F 3 .   ? -19.134 15.148 -39.377 1.00 31.56 ? 739  HOH B O   1 
HETATM 5017 O  O   . HOH F 3 .   ? 14.888  36.099 -22.016 1.00 35.16 ? 740  HOH B O   1 
HETATM 5018 O  O   . HOH F 3 .   ? 12.906  14.039 -22.528 1.00 38.43 ? 741  HOH B O   1 
HETATM 5019 O  O   . HOH F 3 .   ? 5.835   16.173 -18.769 1.00 31.53 ? 742  HOH B O   1 
HETATM 5020 O  O   . HOH F 3 .   ? -5.749  40.071 -30.524 1.00 30.52 ? 743  HOH B O   1 
HETATM 5021 O  O   . HOH F 3 .   ? -0.340  13.229 -12.904 1.00 22.09 ? 744  HOH B O   1 
HETATM 5022 O  O   . HOH F 3 .   ? -20.482 21.426 -16.920 1.00 25.13 ? 745  HOH B O   1 
HETATM 5023 O  O   . HOH F 3 .   ? -1.408  39.975 -35.880 1.00 36.22 ? 746  HOH B O   1 
HETATM 5024 O  O   . HOH F 3 .   ? -25.865 10.866 -29.751 1.00 25.41 ? 747  HOH B O   1 
HETATM 5025 O  O   . HOH F 3 .   ? 18.205  20.858 -24.324 1.00 37.48 ? 748  HOH B O   1 
HETATM 5026 O  O   . HOH F 3 .   ? -29.943 16.035 -26.859 1.00 31.85 ? 749  HOH B O   1 
HETATM 5027 O  O   . HOH F 3 .   ? -13.060 19.037 -9.192  1.00 19.07 ? 750  HOH B O   1 
HETATM 5028 O  O   . HOH F 3 .   ? -22.441 13.487 -40.807 1.00 39.32 ? 751  HOH B O   1 
HETATM 5029 O  O   . HOH F 3 .   ? -5.248  23.696 -4.878  1.00 31.43 ? 752  HOH B O   1 
HETATM 5030 O  O   . HOH F 3 .   ? -9.866  14.157 -25.423 1.00 16.41 ? 753  HOH B O   1 
HETATM 5031 O  O   . HOH F 3 .   ? -2.412  23.708 -37.443 1.00 37.90 ? 754  HOH B O   1 
HETATM 5032 O  O   . HOH F 3 .   ? 4.034   20.260 -8.678  1.00 26.65 ? 755  HOH B O   1 
HETATM 5033 O  O   . HOH F 3 .   ? -13.832 23.069 -20.018 1.00 24.05 ? 756  HOH B O   1 
HETATM 5034 O  O   . HOH F 3 .   ? -17.913 0.005  -26.391 1.00 20.16 ? 757  HOH B O   1 
HETATM 5035 O  O   . HOH F 3 .   ? -22.466 -3.679 -8.082  1.00 27.88 ? 758  HOH B O   1 
HETATM 5036 O  O   . HOH F 3 .   ? -16.453 2.744  -16.815 1.00 25.84 ? 759  HOH B O   1 
HETATM 5037 O  O   . HOH F 3 .   ? -35.044 8.249  -7.588  1.00 28.19 ? 760  HOH B O   1 
HETATM 5038 O  O   . HOH F 3 .   ? -10.953 2.185  -24.387 1.00 20.39 ? 761  HOH B O   1 
HETATM 5039 O  O   . HOH F 3 .   ? -11.302 31.553 -34.300 1.00 25.83 ? 762  HOH B O   1 
HETATM 5040 O  O   . HOH F 3 .   ? -17.110 19.629 -11.815 1.00 22.25 ? 763  HOH B O   1 
HETATM 5041 O  O   . HOH F 3 .   ? -10.198 29.345 -12.956 1.00 23.37 ? 764  HOH B O   1 
HETATM 5042 O  O   . HOH F 3 .   ? -10.718 33.415 -15.699 1.00 21.67 ? 765  HOH B O   1 
HETATM 5043 O  O   A HOH F 3 .   ? -12.428 40.079 -32.064 1.00 40.15 ? 766  HOH B O   1 
HETATM 5044 O  O   . HOH F 3 .   ? -10.972 -3.194 -19.820 1.00 32.96 ? 767  HOH B O   1 
HETATM 5045 O  O   . HOH F 3 .   ? -6.239  11.157 -38.608 1.00 33.68 ? 768  HOH B O   1 
HETATM 5046 O  O   A HOH F 3 .   ? 16.135  29.696 -25.402 0.91 29.14 ? 769  HOH B O   1 
HETATM 5047 O  O   . HOH F 3 .   ? 13.699  34.703 -18.960 1.00 29.77 ? 770  HOH B O   1 
HETATM 5048 O  O   . HOH F 3 .   ? 2.759   24.994 -23.159 1.00 17.36 ? 771  HOH B O   1 
HETATM 5049 O  O   . HOH F 3 .   ? -21.231 17.011 -36.746 1.00 36.58 ? 772  HOH B O   1 
HETATM 5050 O  O   . HOH F 3 .   ? -20.554 9.653  -1.390  1.00 33.97 ? 773  HOH B O   1 
HETATM 5051 O  O   . HOH F 3 .   ? 2.194   13.551 -12.815 1.00 32.57 ? 774  HOH B O   1 
HETATM 5052 O  O   . HOH F 3 .   ? -6.872  3.358  -9.946  1.00 42.39 ? 775  HOH B O   1 
HETATM 5053 O  O   . HOH F 3 .   ? 6.168   14.919 -26.511 1.00 27.28 ? 776  HOH B O   1 
HETATM 5054 O  O   . HOH F 3 .   ? -12.517 31.034 -18.702 1.00 22.35 ? 777  HOH B O   1 
HETATM 5055 O  O   . HOH F 3 .   ? -20.015 26.987 -20.534 1.00 21.08 ? 778  HOH B O   1 
HETATM 5056 O  O   . HOH F 3 .   ? -1.425  9.544  -9.454  1.00 34.36 ? 779  HOH B O   1 
HETATM 5057 O  O   . HOH F 3 .   ? -8.888  16.252 -20.377 1.00 20.27 ? 780  HOH B O   1 
HETATM 5058 O  O   . HOH F 3 .   ? 10.984  43.030 -10.702 1.00 40.26 ? 781  HOH B O   1 
HETATM 5059 O  O   . HOH F 3 .   ? -1.565  34.432 -9.041  1.00 31.25 ? 782  HOH B O   1 
HETATM 5060 O  O   A HOH F 3 .   ? -12.496 21.545 -31.520 1.00 25.44 ? 783  HOH B O   1 
HETATM 5061 O  O   . HOH F 3 .   ? -0.506  4.667  -7.530  1.00 45.78 ? 784  HOH B O   1 
HETATM 5062 O  O   . HOH F 3 .   ? -11.769 24.141 -18.582 1.00 17.83 ? 785  HOH B O   1 
HETATM 5063 O  O   . HOH F 3 .   ? -7.089  23.696 -8.743  1.00 18.52 ? 786  HOH B O   1 
HETATM 5064 O  O   . HOH F 3 .   ? -2.178  23.213 -29.241 1.00 18.32 ? 787  HOH B O   1 
HETATM 5065 O  O   . HOH F 3 .   ? -10.354 8.411  -32.629 1.00 24.41 ? 788  HOH B O   1 
HETATM 5066 O  O   . HOH F 3 .   ? -1.552  41.855 -11.847 1.00 37.14 ? 789  HOH B O   1 
HETATM 5067 O  O   . HOH F 3 .   ? 9.859   19.692 -21.796 1.00 21.16 ? 790  HOH B O   1 
HETATM 5068 O  O   . HOH F 3 .   ? 4.244   16.885 -16.805 1.00 27.72 ? 791  HOH B O   1 
HETATM 5069 O  O   . HOH F 3 .   ? -5.563  35.130 -31.801 1.00 21.93 ? 792  HOH B O   1 
HETATM 5070 O  O   B HOH F 3 .   ? -8.537  17.034 -34.760 0.59 25.17 ? 793  HOH B O   1 
HETATM 5071 O  O   . HOH F 3 .   ? -28.264 9.414  -26.690 1.00 26.65 ? 794  HOH B O   1 
HETATM 5072 O  O   . HOH F 3 .   ? -3.320  7.314  -29.594 1.00 19.98 ? 795  HOH B O   1 
HETATM 5073 O  O   . HOH F 3 .   ? -25.351 10.791 -35.381 1.00 34.85 ? 796  HOH B O   1 
HETATM 5074 O  O   . HOH F 3 .   ? -23.590 -2.600 -22.726 1.00 31.30 ? 797  HOH B O   1 
HETATM 5075 O  O   . HOH F 3 .   ? -32.078 0.806  -13.192 1.00 39.23 ? 798  HOH B O   1 
HETATM 5076 O  O   . HOH F 3 .   ? -19.557 13.714 -32.418 1.00 29.50 ? 799  HOH B O   1 
HETATM 5077 O  O   . HOH F 3 .   ? -34.543 10.679 -6.056  1.00 36.37 ? 800  HOH B O   1 
HETATM 5078 O  O   . HOH F 3 .   ? 1.482   29.078 -8.010  1.00 35.39 ? 801  HOH B O   1 
HETATM 5079 O  O   . HOH F 3 .   ? -32.706 1.343  -6.031  1.00 37.26 ? 802  HOH B O   1 
HETATM 5080 O  O   A HOH F 3 .   ? -6.954  17.929 -34.082 0.99 28.89 ? 803  HOH B O   1 
HETATM 5081 O  O   . HOH F 3 .   ? -22.874 9.665  -38.245 1.00 31.61 ? 804  HOH B O   1 
HETATM 5082 O  O   . HOH F 3 .   ? -0.662  35.587 -17.475 1.00 23.71 ? 805  HOH B O   1 
HETATM 5083 O  O   . HOH F 3 .   ? -23.146 -0.350 -2.967  1.00 30.94 ? 806  HOH B O   1 
HETATM 5084 O  O   . HOH F 3 .   ? -11.065 -4.384 -34.793 1.00 24.42 ? 807  HOH B O   1 
HETATM 5085 O  O   . HOH F 3 .   ? -2.871  13.387 -22.340 1.00 20.64 ? 808  HOH B O   1 
HETATM 5086 O  O   . HOH F 3 .   ? -2.181  33.571 -38.836 1.00 33.06 ? 809  HOH B O   1 
HETATM 5087 O  O   . HOH F 3 .   ? 2.576   34.379 -10.480 1.00 25.85 ? 810  HOH B O   1 
HETATM 5088 O  O   . HOH F 3 .   ? 14.187  43.739 -9.832  1.00 47.79 ? 811  HOH B O   1 
HETATM 5089 O  O   . HOH F 3 .   ? -29.358 14.685 -29.811 1.00 30.63 ? 812  HOH B O   1 
HETATM 5090 O  O   . HOH F 3 .   ? -15.471 7.849  -38.683 1.00 27.99 ? 813  HOH B O   1 
HETATM 5091 O  O   . HOH F 3 .   ? -0.429  11.010 -14.388 1.00 23.10 ? 814  HOH B O   1 
HETATM 5092 O  O   . HOH F 3 .   ? 6.905   27.613 -33.161 1.00 25.76 ? 815  HOH B O   1 
HETATM 5093 O  O   . HOH F 3 .   ? 6.842   47.432 -18.669 1.00 42.25 ? 816  HOH B O   1 
HETATM 5094 O  O   . HOH F 3 .   ? -6.993  -3.864 -24.177 1.00 39.82 ? 817  HOH B O   1 
HETATM 5095 O  O   . HOH F 3 .   ? -16.813 3.220  -20.224 1.00 25.53 ? 818  HOH B O   1 
HETATM 5096 O  O   . HOH F 3 .   ? -8.763  3.145  -2.988  1.00 30.24 ? 819  HOH B O   1 
HETATM 5097 O  O   . HOH F 3 .   ? -0.852  8.082  -25.153 1.00 25.83 ? 820  HOH B O   1 
HETATM 5098 O  O   . HOH F 3 .   ? -0.634  12.899 -24.078 1.00 17.58 ? 821  HOH B O   1 
HETATM 5099 O  O   . HOH F 3 .   ? -11.944 20.667 -24.308 1.00 20.89 ? 822  HOH B O   1 
HETATM 5100 O  O   . HOH F 3 .   ? -7.661  3.010  -16.261 1.00 31.52 ? 823  HOH B O   1 
HETATM 5101 O  O   A HOH F 3 .   ? -19.882 -6.204 -21.977 1.00 41.22 ? 824  HOH B O   1 
HETATM 5102 O  O   . HOH F 3 .   ? 12.908  31.178 -20.032 1.00 22.59 ? 825  HOH B O   1 
HETATM 5103 O  O   . HOH F 3 .   ? -8.254  21.263 -8.088  1.00 19.98 ? 826  HOH B O   1 
HETATM 5104 O  O   . HOH F 3 .   ? -14.912 36.867 -32.220 1.00 32.16 ? 827  HOH B O   1 
HETATM 5105 O  O   . HOH F 3 .   ? 10.778  30.017 -36.411 1.00 33.64 ? 828  HOH B O   1 
HETATM 5106 O  O   . HOH F 3 .   ? -9.625  4.267  -30.623 1.00 19.33 ? 829  HOH B O   1 
HETATM 5107 O  O   . HOH F 3 .   ? 16.897  21.937 -20.685 1.00 34.50 ? 830  HOH B O   1 
HETATM 5108 O  O   . HOH F 3 .   ? -15.868 29.422 -35.609 1.00 53.07 ? 831  HOH B O   1 
HETATM 5109 O  O   . HOH F 3 .   ? -21.095 13.328 -23.481 1.00 20.45 ? 832  HOH B O   1 
HETATM 5110 O  O   . HOH F 3 .   ? -1.288  13.992 -34.874 1.00 38.70 ? 833  HOH B O   1 
HETATM 5111 O  O   . HOH F 3 .   ? -14.352 20.717 -10.963 1.00 25.40 ? 834  HOH B O   1 
HETATM 5112 O  O   . HOH F 3 .   ? -10.131 22.663 -23.299 1.00 23.62 ? 835  HOH B O   1 
HETATM 5113 O  O   . HOH F 3 .   ? -36.718 11.621 -7.201  1.00 36.04 ? 836  HOH B O   1 
HETATM 5114 O  O   . HOH F 3 .   ? -19.349 17.154 -26.639 1.00 24.31 ? 837  HOH B O   1 
HETATM 5115 O  O   . HOH F 3 .   ? -23.927 3.274  -26.070 1.00 30.19 ? 838  HOH B O   1 
HETATM 5116 O  O   . HOH F 3 .   ? -8.953  3.597  -23.338 1.00 19.15 ? 839  HOH B O   1 
HETATM 5117 O  O   B HOH F 3 .   ? -12.269 41.722 -30.209 0.91 40.26 ? 840  HOH B O   1 
HETATM 5118 O  O   . HOH F 3 .   ? -1.733  29.894 -40.165 1.00 42.57 ? 841  HOH B O   1 
HETATM 5119 O  O   . HOH F 3 .   ? -30.194 -4.860 -18.663 1.00 37.23 ? 842  HOH B O   1 
HETATM 5120 O  O   . HOH F 3 .   ? -0.429  21.964 -31.978 1.00 24.02 ? 843  HOH B O   1 
HETATM 5121 O  O   . HOH F 3 .   ? -35.631 2.312  -14.702 1.00 36.23 ? 844  HOH B O   1 
HETATM 5122 O  O   . HOH F 3 .   ? -14.054 -1.020 -29.842 1.00 19.97 ? 845  HOH B O   1 
HETATM 5123 O  O   . HOH F 3 .   ? -3.467  21.538 -23.135 1.00 20.10 ? 846  HOH B O   1 
HETATM 5124 O  O   . HOH F 3 .   ? -28.682 16.222 -14.589 1.00 22.61 ? 847  HOH B O   1 
HETATM 5125 O  O   . HOH F 3 .   ? 1.642   26.135 -6.090  1.00 31.16 ? 848  HOH B O   1 
HETATM 5126 O  O   . HOH F 3 .   ? -11.226 4.858  -35.283 1.00 26.59 ? 849  HOH B O   1 
HETATM 5127 O  O   . HOH F 3 .   ? 10.021  23.732 -29.423 1.00 30.47 ? 850  HOH B O   1 
HETATM 5128 O  O   . HOH F 3 .   ? -5.105  3.944  -30.903 1.00 23.51 ? 851  HOH B O   1 
HETATM 5129 O  O   . HOH F 3 .   ? 11.868  17.761 -22.958 1.00 34.99 ? 852  HOH B O   1 
HETATM 5130 O  O   . HOH F 3 .   ? -7.769  5.510  0.553   1.00 37.61 ? 853  HOH B O   1 
HETATM 5131 O  O   . HOH F 3 .   ? -14.706 39.006 -28.641 1.00 30.96 ? 854  HOH B O   1 
HETATM 5132 O  O   . HOH F 3 .   ? 11.336  15.587 -29.061 1.00 36.47 ? 855  HOH B O   1 
HETATM 5133 O  O   . HOH F 3 .   ? -31.451 -2.214 -17.366 1.00 33.42 ? 856  HOH B O   1 
HETATM 5134 O  O   . HOH F 3 .   ? 12.072  27.318 -29.820 1.00 32.21 ? 857  HOH B O   1 
HETATM 5135 O  O   . HOH F 3 .   ? -32.021 18.953 -16.922 1.00 26.73 ? 858  HOH B O   1 
HETATM 5136 O  O   A HOH F 3 .   ? -26.858 20.300 -23.401 0.82 30.29 ? 859  HOH B O   1 
HETATM 5137 O  O   . HOH F 3 .   ? -4.384  15.687 -37.015 1.00 35.49 ? 860  HOH B O   1 
HETATM 5138 O  O   . HOH F 3 .   ? -14.052 32.090 -26.962 1.00 24.45 ? 861  HOH B O   1 
HETATM 5139 O  O   . HOH F 3 .   ? 16.766  34.578 -33.581 1.00 40.03 ? 862  HOH B O   1 
HETATM 5140 O  O   . HOH F 3 .   ? -30.747 -0.108 -11.081 1.00 30.92 ? 863  HOH B O   1 
HETATM 5141 O  O   . HOH F 3 .   ? 15.097  20.997 -25.682 1.00 38.45 ? 864  HOH B O   1 
HETATM 5142 O  O   B HOH F 3 .   ? 8.191   14.779 -24.820 0.77 33.32 ? 865  HOH B O   1 
HETATM 5143 O  O   . HOH F 3 .   ? -11.375 26.159 -34.861 1.00 29.68 ? 866  HOH B O   1 
HETATM 5144 O  O   A HOH F 3 .   ? 18.741  29.908 -23.980 0.91 33.89 ? 867  HOH B O   1 
HETATM 5145 O  O   . HOH F 3 .   ? -1.077  40.815 -21.598 1.00 27.73 ? 868  HOH B O   1 
HETATM 5146 O  O   . HOH F 3 .   ? -1.047  17.673 -4.700  1.00 35.85 ? 869  HOH B O   1 
HETATM 5147 O  O   . HOH F 3 .   ? 3.460   9.184  -22.637 1.00 30.84 ? 870  HOH B O   1 
HETATM 5148 O  O   . HOH F 3 .   ? -29.906 -5.917 -11.286 1.00 45.06 ? 871  HOH B O   1 
HETATM 5149 O  O   . HOH F 3 .   ? 1.100   12.072 -7.777  1.00 38.27 ? 872  HOH B O   1 
HETATM 5150 O  O   . HOH F 3 .   ? -14.669 -2.883 -20.450 1.00 20.23 ? 873  HOH B O   1 
HETATM 5151 O  O   . HOH F 3 .   ? 2.268   13.583 -33.211 1.00 25.37 ? 874  HOH B O   1 
HETATM 5152 O  O   . HOH F 3 .   ? -4.834  37.277 -29.988 1.00 25.71 ? 875  HOH B O   1 
HETATM 5153 O  O   . HOH F 3 .   ? -4.213  10.885 -35.549 1.00 26.75 ? 876  HOH B O   1 
HETATM 5154 O  O   . HOH F 3 .   ? -3.333  4.250  -3.461  1.00 30.08 ? 877  HOH B O   1 
HETATM 5155 O  O   . HOH F 3 .   ? -19.444 1.385  -23.246 1.00 20.90 ? 878  HOH B O   1 
HETATM 5156 O  O   . HOH F 3 .   ? -27.634 18.184 -15.977 1.00 22.99 ? 879  HOH B O   1 
HETATM 5157 O  O   . HOH F 3 .   ? -20.774 20.450 -14.764 1.00 24.76 ? 880  HOH B O   1 
HETATM 5158 O  O   . HOH F 3 .   ? -10.943 23.704 -35.959 1.00 39.70 ? 881  HOH B O   1 
HETATM 5159 O  O   . HOH F 3 .   ? 9.227   32.221 -37.372 1.00 32.97 ? 882  HOH B O   1 
HETATM 5160 O  O   . HOH F 3 .   ? -29.828 14.980 -16.712 1.00 26.37 ? 883  HOH B O   1 
HETATM 5161 O  O   . HOH F 3 .   ? 13.566  20.024 -8.887  1.00 39.55 ? 884  HOH B O   1 
HETATM 5162 O  O   . HOH F 3 .   ? -17.293 11.551 -31.532 1.00 26.70 ? 885  HOH B O   1 
HETATM 5163 O  O   . HOH F 3 .   ? -18.057 25.080 -25.850 1.00 20.66 ? 886  HOH B O   1 
HETATM 5164 O  O   . HOH F 3 .   ? 0.727   41.403 -33.905 1.00 27.26 ? 887  HOH B O   1 
HETATM 5165 O  O   . HOH F 3 .   ? -15.467 17.573 -38.911 1.00 38.01 ? 888  HOH B O   1 
HETATM 5166 O  O   B HOH F 3 .   ? -17.750 -6.034 -20.439 1.00 39.21 ? 889  HOH B O   1 
HETATM 5167 O  O   . HOH F 3 .   ? -40.262 9.547  -19.002 1.00 37.81 ? 890  HOH B O   1 
HETATM 5168 O  O   . HOH F 3 .   ? -16.829 16.234 -32.504 1.00 28.59 ? 891  HOH B O   1 
HETATM 5169 O  O   . HOH F 3 .   ? -16.834 -2.351 -18.757 1.00 28.89 ? 892  HOH B O   1 
HETATM 5170 O  O   . HOH F 3 .   ? 8.280   17.887 -32.181 1.00 39.20 ? 893  HOH B O   1 
HETATM 5171 O  O   . HOH F 3 .   ? -20.762 22.499 -23.641 1.00 30.88 ? 894  HOH B O   1 
HETATM 5172 O  O   . HOH F 3 .   ? 3.286   31.862 -9.486  1.00 33.46 ? 895  HOH B O   1 
HETATM 5173 O  O   . HOH F 3 .   ? -27.825 -4.038 -7.555  1.00 31.69 ? 896  HOH B O   1 
HETATM 5174 O  O   . HOH F 3 .   ? 2.873   13.351 -15.053 1.00 31.45 ? 897  HOH B O   1 
HETATM 5175 O  O   . HOH F 3 .   ? 7.288   42.128 -33.523 1.00 31.92 ? 898  HOH B O   1 
HETATM 5176 O  O   . HOH F 3 .   ? -0.476  10.611 -33.261 1.00 29.94 ? 899  HOH B O   1 
HETATM 5177 O  O   . HOH F 3 .   ? 4.406   33.955 -4.503  1.00 45.86 ? 900  HOH B O   1 
HETATM 5178 O  O   . HOH F 3 .   ? -20.513 4.975  -1.165  1.00 38.59 ? 901  HOH B O   1 
HETATM 5179 O  O   . HOH F 3 .   ? -16.515 2.993  -4.232  1.00 44.95 ? 902  HOH B O   1 
HETATM 5180 O  O   . HOH F 3 .   ? -19.049 -4.813 -12.999 1.00 40.40 ? 903  HOH B O   1 
HETATM 5181 O  O   . HOH F 3 .   ? 14.233  16.580 -13.201 1.00 42.43 ? 904  HOH B O   1 
HETATM 5182 O  O   . HOH F 3 .   ? 13.036  44.306 -23.980 1.00 35.49 ? 905  HOH B O   1 
HETATM 5183 O  O   . HOH F 3 .   ? -18.210 14.375 -23.717 1.00 28.36 ? 906  HOH B O   1 
HETATM 5184 O  O   . HOH F 3 .   ? -2.054  27.639 -37.134 1.00 32.31 ? 907  HOH B O   1 
HETATM 5185 O  O   . HOH F 3 .   ? 0.915   9.782  -27.311 1.00 25.57 ? 908  HOH B O   1 
HETATM 5186 O  O   . HOH F 3 .   ? 10.874  14.180 -16.371 1.00 32.05 ? 909  HOH B O   1 
HETATM 5187 O  O   . HOH F 3 .   ? 4.334   22.362 -5.587  1.00 43.79 ? 910  HOH B O   1 
HETATM 5188 O  O   . HOH F 3 .   ? -29.223 -3.859 -9.527  1.00 49.36 ? 911  HOH B O   1 
HETATM 5189 O  O   . HOH F 3 .   ? 4.557   26.114 -33.451 1.00 23.44 ? 912  HOH B O   1 
HETATM 5190 O  O   . HOH F 3 .   ? 8.693   24.427 -31.341 1.00 31.11 ? 913  HOH B O   1 
HETATM 5191 O  O   . HOH F 3 .   ? -0.107  12.999 -9.889  1.00 34.45 ? 914  HOH B O   1 
HETATM 5192 O  O   . HOH F 3 .   ? -5.697  40.489 -13.986 1.00 42.23 ? 915  HOH B O   1 
HETATM 5193 O  O   . HOH F 3 .   ? -0.583  41.166 -24.419 1.00 29.20 ? 916  HOH B O   1 
HETATM 5194 O  O   . HOH F 3 .   ? -16.898 5.691  -7.009  1.00 43.57 ? 917  HOH B O   1 
HETATM 5195 O  O   . HOH F 3 .   ? -24.664 8.571  -31.891 1.00 42.60 ? 918  HOH B O   1 
HETATM 5196 O  O   C HOH F 3 .   ? -9.860  33.227 -8.751  0.93 48.09 ? 919  HOH B O   1 
HETATM 5197 O  O   . HOH F 3 .   ? 2.776   11.134 -31.551 1.00 28.52 ? 920  HOH B O   1 
HETATM 5198 O  O   . HOH F 3 .   ? 3.999   12.237 -10.789 1.00 50.21 ? 921  HOH B O   1 
HETATM 5199 O  O   . HOH F 3 .   ? -20.864 20.589 -19.470 1.00 25.39 ? 922  HOH B O   1 
HETATM 5200 O  O   . HOH F 3 .   ? -37.968 2.747  -19.791 1.00 39.06 ? 923  HOH B O   1 
HETATM 5201 O  O   . HOH F 3 .   ? -11.223 5.649  -32.693 1.00 24.06 ? 924  HOH B O   1 
HETATM 5202 O  O   B HOH F 3 .   ? -11.413 20.387 -32.736 1.00 29.76 ? 925  HOH B O   1 
HETATM 5203 O  O   . HOH F 3 .   ? -25.941 2.425  -1.734  1.00 35.44 ? 926  HOH B O   1 
HETATM 5204 O  O   . HOH F 3 .   ? -5.680  1.048  -20.246 1.00 34.60 ? 927  HOH B O   1 
HETATM 5205 O  O   . HOH F 3 .   ? -28.451 14.851 -19.917 1.00 38.17 ? 928  HOH B O   1 
HETATM 5206 O  O   . HOH F 3 .   ? -16.734 25.145 -28.600 1.00 26.95 ? 929  HOH B O   1 
HETATM 5207 O  O   B HOH F 3 .   ? 17.788  28.355 -24.586 0.90 33.89 ? 930  HOH B O   1 
HETATM 5208 O  O   . HOH F 3 .   ? -23.214 19.543 -14.545 1.00 25.64 ? 931  HOH B O   1 
HETATM 5209 O  O   . HOH F 3 .   ? -21.592 16.508 -39.785 1.00 39.25 ? 932  HOH B O   1 
HETATM 5210 O  O   . HOH F 3 .   ? -24.210 5.098  -28.353 1.00 31.02 ? 933  HOH B O   1 
HETATM 5211 O  O   . HOH F 3 .   ? -10.467 18.569 -34.348 1.00 42.13 ? 934  HOH B O   1 
HETATM 5212 O  O   . HOH F 3 .   ? -22.973 20.288 -20.723 1.00 29.36 ? 935  HOH B O   1 
HETATM 5213 O  O   . HOH F 3 .   ? -15.108 31.850 -24.428 1.00 27.02 ? 936  HOH B O   1 
HETATM 5214 O  O   . HOH F 3 .   ? -17.682 20.376 -14.341 1.00 20.71 ? 937  HOH B O   1 
HETATM 5215 O  O   . HOH F 3 .   ? 6.988   20.139 -31.377 1.00 29.58 ? 938  HOH B O   1 
HETATM 5216 O  O   A HOH F 3 .   ? 8.015   16.967 -24.746 0.69 27.67 ? 939  HOH B O   1 
HETATM 5217 O  O   . HOH F 3 .   ? -7.756  36.844 -8.317  1.00 41.13 ? 940  HOH B O   1 
HETATM 5218 O  O   . HOH F 3 .   ? 0.851   6.320  -14.227 1.00 34.44 ? 941  HOH B O   1 
HETATM 5219 O  O   . HOH F 3 .   ? -22.994 6.702  -32.681 1.00 36.47 ? 942  HOH B O   1 
HETATM 5220 O  O   . HOH F 3 .   ? -20.584 19.900 -27.646 1.00 29.33 ? 943  HOH B O   1 
HETATM 5221 O  O   . HOH F 3 .   ? -10.155 35.579 -22.685 1.00 31.79 ? 944  HOH B O   1 
HETATM 5222 O  O   . HOH F 3 .   ? -6.557  33.628 -38.593 1.00 37.67 ? 945  HOH B O   1 
HETATM 5223 O  O   . HOH F 3 .   ? -25.025 21.005 -18.920 1.00 31.32 ? 946  HOH B O   1 
HETATM 5224 O  O   . HOH F 3 .   ? -32.031 2.311  -26.212 1.00 41.37 ? 947  HOH B O   1 
HETATM 5225 O  O   . HOH F 3 .   ? -19.242 4.986  -7.078  1.00 32.07 ? 948  HOH B O   1 
HETATM 5226 O  O   B HOH F 3 .   ? -22.492 -1.829 -27.842 1.00 39.83 ? 949  HOH B O   1 
HETATM 5227 O  O   . HOH F 3 .   ? -26.876 23.540 -29.264 1.00 36.88 ? 950  HOH B O   1 
HETATM 5228 O  O   A HOH F 3 .   ? -22.629 -0.354 -26.091 0.68 28.84 ? 951  HOH B O   1 
HETATM 5229 O  O   . HOH F 3 .   ? 3.262   7.904  -20.001 1.00 41.91 ? 952  HOH B O   1 
HETATM 5230 O  O   . HOH F 3 .   ? -19.994 -1.021 -24.968 1.00 28.69 ? 953  HOH B O   1 
HETATM 5231 O  O   . HOH F 3 .   ? -16.210 0.224  -17.586 1.00 30.70 ? 954  HOH B O   1 
HETATM 5232 O  O   . HOH F 3 .   ? -30.605 11.675 -23.350 1.00 28.83 ? 955  HOH B O   1 
HETATM 5233 O  O   B HOH F 3 .   ? -15.971 1.667  -13.750 0.71 26.67 ? 956  HOH B O   1 
HETATM 5234 O  O   . HOH F 3 .   ? -4.431  21.447 -38.135 1.00 44.18 ? 957  HOH B O   1 
HETATM 5235 O  O   . HOH F 3 .   ? -31.743 1.797  -3.606  1.00 45.06 ? 958  HOH B O   1 
HETATM 5236 O  O   . HOH F 3 .   ? -15.619 -1.582 -27.425 1.00 20.62 ? 959  HOH B O   1 
HETATM 5237 O  O   . HOH F 3 .   ? 1.929   31.875 -7.401  1.00 38.62 ? 960  HOH B O   1 
HETATM 5238 O  O   . HOH F 3 .   ? -1.025  25.081 -5.628  1.00 44.73 ? 961  HOH B O   1 
HETATM 5239 O  O   . HOH F 3 .   ? -9.046  0.091  -24.691 1.00 29.01 ? 962  HOH B O   1 
HETATM 5240 O  O   . HOH F 3 .   ? -17.079 0.174  -5.228  1.00 40.92 ? 963  HOH B O   1 
HETATM 5241 O  O   . HOH F 3 .   ? -29.563 7.462  -28.440 1.00 43.97 ? 964  HOH B O   1 
HETATM 5242 O  O   . HOH F 3 .   ? -17.268 16.125 -40.752 1.00 36.92 ? 965  HOH B O   1 
HETATM 5243 O  O   . HOH F 3 .   ? 15.729  21.253 -10.818 1.00 39.49 ? 966  HOH B O   1 
HETATM 5244 O  O   . HOH F 3 .   ? -25.307 19.713 -15.805 1.00 19.93 ? 967  HOH B O   1 
HETATM 5245 O  O   . HOH F 3 .   ? -19.588 18.908 -31.231 1.00 31.78 ? 968  HOH B O   1 
HETATM 5246 O  O   . HOH F 3 .   ? -6.267  2.343  -22.854 1.00 25.20 ? 969  HOH B O   1 
HETATM 5247 O  O   . HOH F 3 .   ? 8.352   32.902 -39.535 1.00 35.57 ? 970  HOH B O   1 
HETATM 5248 O  O   . HOH F 3 .   ? 3.045   32.178 -4.843  1.00 45.22 ? 971  HOH B O   1 
HETATM 5249 O  O   . HOH F 3 .   ? -30.028 11.090 -25.506 1.00 33.12 ? 972  HOH B O   1 
HETATM 5250 O  O   . HOH F 3 .   ? -4.516  18.609 -35.226 1.00 30.73 ? 973  HOH B O   1 
HETATM 5251 O  O   . HOH F 3 .   ? -24.993 15.290 -36.315 1.00 33.87 ? 974  HOH B O   1 
HETATM 5252 O  O   . HOH F 3 .   ? -10.346 28.145 -37.268 1.00 41.34 ? 975  HOH B O   1 
HETATM 5253 O  O   . HOH F 3 .   ? -4.347  3.532  -37.789 1.00 55.65 ? 976  HOH B O   1 
HETATM 5254 O  O   . HOH F 3 .   ? 21.630  26.259 -23.998 1.00 43.32 ? 977  HOH B O   1 
HETATM 5255 O  O   . HOH F 3 .   ? -25.701 0.898  -28.830 1.00 40.23 ? 978  HOH B O   1 
HETATM 5256 O  O   . HOH F 3 .   ? -25.486 12.424 -39.378 1.00 35.72 ? 979  HOH B O   1 
HETATM 5257 O  O   . HOH F 3 .   ? -43.862 17.247 -14.000 1.00 48.56 ? 980  HOH B O   1 
HETATM 5258 O  O   . HOH F 3 .   ? -26.382 -2.480 -21.996 1.00 35.72 ? 981  HOH B O   1 
HETATM 5259 O  O   . HOH F 3 .   ? -12.889 19.682 -36.434 1.00 48.77 ? 982  HOH B O   1 
HETATM 5260 O  O   . HOH F 3 .   ? -2.599  20.393 -35.943 1.00 32.89 ? 983  HOH B O   1 
HETATM 5261 O  O   . HOH F 3 .   ? -0.604  32.192 -7.708  1.00 35.36 ? 984  HOH B O   1 
HETATM 5262 O  O   . HOH F 3 .   ? -34.130 20.265 -17.814 1.00 27.37 ? 985  HOH B O   1 
HETATM 5263 O  O   . HOH F 3 .   ? 16.873  19.440 -26.785 1.00 39.03 ? 986  HOH B O   1 
HETATM 5264 O  O   . HOH F 3 .   ? -25.881 12.982 -36.524 1.00 33.75 ? 987  HOH B O   1 
HETATM 5265 O  O   . HOH F 3 .   ? 2.656   10.736 -15.069 1.00 39.88 ? 988  HOH B O   1 
HETATM 5266 O  O   . HOH F 3 .   ? 1.287   43.467 -34.965 1.00 45.10 ? 989  HOH B O   1 
HETATM 5267 O  O   . HOH F 3 .   ? -31.803 16.657 -17.925 1.00 32.08 ? 990  HOH B O   1 
HETATM 5268 O  O   . HOH F 3 .   ? 10.828  15.928 -25.065 1.00 34.66 ? 991  HOH B O   1 
HETATM 5269 O  O   A HOH F 3 .   ? -14.573 34.210 -23.447 1.00 27.45 ? 992  HOH B O   1 
HETATM 5270 O  O   . HOH F 3 .   ? -14.608 22.689 -32.761 1.00 35.15 ? 993  HOH B O   1 
HETATM 5271 O  O   . HOH F 3 .   ? 6.807   19.608 -7.734  1.00 34.80 ? 994  HOH B O   1 
HETATM 5272 O  O   . HOH F 3 .   ? -28.811 11.868 -29.689 1.00 31.04 ? 995  HOH B O   1 
HETATM 5273 O  O   . HOH F 3 .   ? 2.121   19.599 -4.632  1.00 46.56 ? 996  HOH B O   1 
HETATM 5274 O  O   . HOH F 3 .   ? -4.031  41.543 -12.716 1.00 37.74 ? 997  HOH B O   1 
HETATM 5275 O  O   . HOH F 3 .   ? 4.343   23.219 -33.415 1.00 29.13 ? 998  HOH B O   1 
HETATM 5276 O  O   . HOH F 3 .   ? 7.162   22.368 -32.744 1.00 39.23 ? 999  HOH B O   1 
HETATM 5277 O  O   . HOH F 3 .   ? 2.878   21.667 -32.711 1.00 36.89 ? 1000 HOH B O   1 
HETATM 5278 O  O   . HOH F 3 .   ? 17.396  36.593 -31.357 1.00 37.09 ? 1001 HOH B O   1 
HETATM 5279 O  O   . HOH F 3 .   ? 6.943   13.280 -28.739 1.00 29.56 ? 1002 HOH B O   1 
HETATM 5280 O  O   . HOH F 3 .   ? 7.532   22.071 -35.637 1.00 44.25 ? 1003 HOH B O   1 
HETATM 5281 O  O   . HOH F 3 .   ? 5.461   11.334 -30.644 1.00 31.73 ? 1004 HOH B O   1 
HETATM 5282 O  O   . HOH F 3 .   ? 9.244   11.761 -28.798 1.00 40.70 ? 1005 HOH B O   1 
HETATM 5283 O  O   . HOH F 3 .   ? -32.293 8.492  -29.883 1.00 49.33 ? 1006 HOH B O   1 
HETATM 5284 O  O   . HOH F 3 .   ? 16.029  40.766 -10.013 1.00 48.85 ? 1007 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   A ALA A 2   ? 0.7419 0.6885 0.7523 -0.0117 0.0048  0.0385  226  ALA A N   
2    N  N   B ALA A 2   ? 0.7419 0.6886 0.7524 -0.0118 0.0049  0.0385  226  ALA A N   
3    C  CA  A ALA A 2   ? 0.7147 0.6629 0.7327 -0.0128 0.0030  0.0333  226  ALA A CA  
4    C  CA  B ALA A 2   ? 0.7146 0.6630 0.7327 -0.0128 0.0030  0.0333  226  ALA A CA  
5    C  C   A ALA A 2   ? 0.7318 0.6873 0.7493 -0.0106 -0.0004 0.0292  226  ALA A C   
6    C  C   B ALA A 2   ? 0.7319 0.6875 0.7493 -0.0106 -0.0004 0.0293  226  ALA A C   
7    O  O   A ALA A 2   ? 0.7406 0.7015 0.7618 -0.0122 -0.0007 0.0254  226  ALA A O   
8    O  O   B ALA A 2   ? 0.7408 0.7018 0.7618 -0.0122 -0.0007 0.0255  226  ALA A O   
9    C  CB  A ALA A 2   ? 0.7110 0.6513 0.7316 -0.0119 0.0020  0.0335  226  ALA A CB  
10   C  CB  B ALA A 2   ? 0.7110 0.6513 0.7315 -0.0119 0.0020  0.0335  226  ALA A CB  
11   N  N   . PHE A 3   ? 0.6117 0.5673 0.6249 -0.0068 -0.0028 0.0301  227  PHE A N   
12   C  CA  . PHE A 3   ? 0.5160 0.4779 0.5293 -0.0047 -0.0055 0.0266  227  PHE A CA  
13   C  C   . PHE A 3   ? 0.4428 0.4100 0.4509 -0.0037 -0.0060 0.0279  227  PHE A C   
14   O  O   . PHE A 3   ? 0.3606 0.3257 0.3636 -0.0018 -0.0064 0.0315  227  PHE A O   
15   C  CB  . PHE A 3   ? 0.3910 0.3505 0.4050 -0.0013 -0.0079 0.0257  227  PHE A CB  
16   C  CG  . PHE A 3   ? 0.3870 0.3524 0.4027 0.0002  -0.0097 0.0216  227  PHE A CG  
17   C  CD1 . PHE A 3   ? 0.3435 0.3094 0.3629 -0.0009 -0.0098 0.0174  227  PHE A CD1 
18   C  CD2 . PHE A 3   ? 0.3530 0.3234 0.3663 0.0026  -0.0113 0.0219  227  PHE A CD2 
19   C  CE1 . PHE A 3   ? 0.3111 0.2819 0.3310 0.0006  -0.0110 0.0140  227  PHE A CE1 
20   C  CE2 . PHE A 3   ? 0.3323 0.3078 0.3474 0.0036  -0.0123 0.0184  227  PHE A CE2 
21   C  CZ  . PHE A 3   ? 0.2859 0.2615 0.3038 0.0027  -0.0118 0.0147  227  PHE A CZ  
22   N  N   . THR A 4   ? 0.3711 0.3448 0.3803 -0.0047 -0.0063 0.0249  228  THR A N   
23   C  CA  . THR A 4   ? 0.3475 0.3262 0.3524 -0.0039 -0.0069 0.0254  228  THR A CA  
24   C  C   . THR A 4   ? 0.3217 0.3060 0.3285 -0.0029 -0.0088 0.0217  228  THR A C   
25   O  O   . THR A 4   ? 0.2663 0.2513 0.2771 -0.0033 -0.0091 0.0186  228  THR A O   
26   C  CB  . THR A 4   ? 0.4120 0.3926 0.4155 -0.0066 -0.0043 0.0261  228  THR A CB  
27   O  OG1 . THR A 4   ? 0.3991 0.3818 0.4082 -0.0089 -0.0034 0.0228  228  THR A OG1 
28   C  CG2 . THR A 4   ? 0.4102 0.3852 0.4106 -0.0074 -0.0016 0.0304  228  THR A CG2 
29   N  N   . ILE A 5   ? 0.3289 0.3168 0.3324 -0.0016 -0.0102 0.0222  229  ILE A N   
30   C  CA  . ILE A 5   ? 0.3155 0.3089 0.3203 -0.0009 -0.0115 0.0193  229  ILE A CA  
31   C  C   . ILE A 5   ? 0.3052 0.3020 0.3074 -0.0025 -0.0107 0.0189  229  ILE A C   
32   O  O   . ILE A 5   ? 0.2988 0.2948 0.2967 -0.0026 -0.0103 0.0213  229  ILE A O   
33   C  CB  . ILE A 5   ? 0.2665 0.2615 0.2711 0.0018  -0.0140 0.0199  229  ILE A CB  
34   C  CG1 . ILE A 5   ? 0.3224 0.3141 0.3299 0.0039  -0.0147 0.0202  229  ILE A CG1 
35   C  CG2 . ILE A 5   ? 0.3765 0.3771 0.3829 0.0020  -0.0148 0.0172  229  ILE A CG2 
36   C  CD1 . ILE A 5   ? 0.3431 0.3342 0.3544 0.0034  -0.0136 0.0172  229  ILE A CD1 
37   N  N   . PRO A 6   ? 0.3125 0.3128 0.3167 -0.0036 -0.0103 0.0161  230  PRO A N   
38   C  CA  . PRO A 6   ? 0.3110 0.3144 0.3128 -0.0046 -0.0097 0.0156  230  PRO A CA  
39   C  C   . PRO A 6   ? 0.2737 0.2790 0.2722 -0.0033 -0.0116 0.0162  230  PRO A C   
40   O  O   . PRO A 6   ? 0.3024 0.3088 0.3025 -0.0017 -0.0135 0.0159  230  PRO A O   
41   C  CB  . PRO A 6   ? 0.3005 0.3067 0.3052 -0.0052 -0.0096 0.0124  230  PRO A CB  
42   C  CG  . PRO A 6   ? 0.3219 0.3270 0.3293 -0.0039 -0.0105 0.0113  230  PRO A CG  
43   C  CD  . PRO A 6   ? 0.3340 0.3349 0.3420 -0.0035 -0.0104 0.0132  230  PRO A CD  
44   N  N   . VAL A 7   ? 0.2424 0.2482 0.2365 -0.0038 -0.0110 0.0171  231  VAL A N   
45   C  CA  . VAL A 7   ? 0.2514 0.2584 0.2416 -0.0026 -0.0132 0.0175  231  VAL A CA  
46   C  C   . VAL A 7   ? 0.2641 0.2750 0.2558 -0.0031 -0.0139 0.0147  231  VAL A C   
47   O  O   . VAL A 7   ? 0.2483 0.2601 0.2386 -0.0042 -0.0124 0.0136  231  VAL A O   
48   C  CB  . VAL A 7   ? 0.3461 0.3509 0.3296 -0.0026 -0.0121 0.0197  231  VAL A CB  
49   C  CG1 . VAL A 7   ? 0.3342 0.3404 0.3129 -0.0012 -0.0149 0.0193  231  VAL A CG1 
50   C  CG2 . VAL A 7   ? 0.3044 0.3044 0.2859 -0.0020 -0.0111 0.0232  231  VAL A CG2 
51   N  N   . LEU A 8   ? 0.2492 0.2623 0.2443 -0.0022 -0.0159 0.0135  232  LEU A N   
52   C  CA  . LEU A 8   ? 0.2698 0.2859 0.2673 -0.0029 -0.0161 0.0110  232  LEU A CA  
53   C  C   . LEU A 8   ? 0.2867 0.3052 0.2863 -0.0021 -0.0189 0.0104  232  LEU A C   
54   O  O   . LEU A 8   ? 0.2752 0.2943 0.2779 -0.0007 -0.0201 0.0110  232  LEU A O   
55   C  CB  . LEU A 8   ? 0.2825 0.2989 0.2842 -0.0033 -0.0145 0.0097  232  LEU A CB  
56   C  CG  . LEU A 8   ? 0.2989 0.3137 0.3001 -0.0043 -0.0124 0.0094  232  LEU A CG  
57   C  CD1 . LEU A 8   ? 0.2936 0.3082 0.2982 -0.0039 -0.0118 0.0082  232  LEU A CD1 
58   C  CD2 . LEU A 8   ? 0.2820 0.2981 0.2813 -0.0053 -0.0116 0.0082  232  LEU A CD2 
59   N  N   . LYS A 9   ? 0.2940 0.3143 0.2928 -0.0028 -0.0198 0.0088  233  LYS A N   
60   C  CA  . LYS A 9   ? 0.2780 0.3013 0.2808 -0.0026 -0.0222 0.0075  233  LYS A CA  
61   C  C   . LYS A 9   ? 0.2618 0.2868 0.2709 -0.0030 -0.0205 0.0066  233  LYS A C   
62   O  O   . LYS A 9   ? 0.2374 0.2611 0.2463 -0.0035 -0.0178 0.0064  233  LYS A O   
63   C  CB  . LYS A 9   ? 0.2955 0.3196 0.2962 -0.0035 -0.0235 0.0057  233  LYS A CB  
64   C  CG  . LYS A 9   ? 0.3384 0.3605 0.3316 -0.0028 -0.0250 0.0063  233  LYS A CG  
65   C  CD  . LYS A 9   ? 0.4004 0.4225 0.3910 -0.0039 -0.0253 0.0040  233  LYS A CD  
66   C  CE  . LYS A 9   ? 0.4671 0.4866 0.4490 -0.0031 -0.0254 0.0046  233  LYS A CE  
67   N  NZ  . LYS A 9   ? 0.5115 0.5305 0.4908 -0.0039 -0.0251 0.0021  233  LYS A NZ  
68   N  N   . ILE A 10  ? 0.2503 0.2784 0.2650 -0.0026 -0.0220 0.0060  234  ILE A N   
69   C  CA  . ILE A 10  ? 0.2509 0.2806 0.2713 -0.0029 -0.0197 0.0053  234  ILE A CA  
70   C  C   . ILE A 10  ? 0.2610 0.2899 0.2803 -0.0046 -0.0174 0.0041  234  ILE A C   
71   O  O   . ILE A 10  ? 0.2395 0.2671 0.2589 -0.0045 -0.0146 0.0041  234  ILE A O   
72   C  CB  . ILE A 10  ? 0.2060 0.2399 0.2338 -0.0025 -0.0215 0.0047  234  ILE A CB  
73   C  CG1 . ILE A 10  ? 0.2543 0.2889 0.2836 -0.0001 -0.0237 0.0060  234  ILE A CG1 
74   C  CG2 . ILE A 10  ? 0.2995 0.3352 0.3332 -0.0031 -0.0184 0.0040  234  ILE A CG2 
75   C  CD1 . ILE A 10  ? 0.2813 0.3136 0.3103 0.0013  -0.0213 0.0071  234  ILE A CD1 
76   N  N   . SER A 11  ? 0.2583 0.2872 0.2758 -0.0058 -0.0188 0.0030  235  SER A N   
77   C  CA  . SER A 11  ? 0.2710 0.2985 0.2873 -0.0072 -0.0169 0.0020  235  SER A CA  
78   C  C   . SER A 11  ? 0.3246 0.3492 0.3355 -0.0069 -0.0150 0.0023  235  SER A C   
79   O  O   . SER A 11  ? 0.3540 0.3771 0.3639 -0.0075 -0.0134 0.0016  235  SER A O   
80   C  CB  . SER A 11  ? 0.2791 0.3068 0.2947 -0.0084 -0.0191 0.0004  235  SER A CB  
81   O  OG  . SER A 11  ? 0.3157 0.3422 0.3254 -0.0077 -0.0209 0.0005  235  SER A OG  
82   N  N   . GLU A 12  ? 0.2577 0.2812 0.2656 -0.0061 -0.0153 0.0034  236  GLU A N   
83   C  CA  . GLU A 12  ? 0.2758 0.2973 0.2804 -0.0060 -0.0136 0.0036  236  GLU A CA  
84   C  C   . GLU A 12  ? 0.2847 0.3055 0.2909 -0.0052 -0.0121 0.0040  236  GLU A C   
85   O  O   . GLU A 12  ? 0.2832 0.3025 0.2875 -0.0051 -0.0111 0.0038  236  GLU A O   
86   C  CB  . GLU A 12  ? 0.2739 0.2945 0.2746 -0.0058 -0.0142 0.0044  236  GLU A CB  
87   C  CG  . GLU A 12  ? 0.3501 0.3710 0.3478 -0.0061 -0.0158 0.0038  236  GLU A CG  
88   C  CD  . GLU A 12  ? 0.3625 0.3821 0.3554 -0.0056 -0.0161 0.0052  236  GLU A CD  
89   O  OE1 . GLU A 12  ? 0.3846 0.4036 0.3777 -0.0049 -0.0164 0.0070  236  GLU A OE1 
90   O  OE2 . GLU A 12  ? 0.4453 0.4643 0.4342 -0.0057 -0.0159 0.0045  236  GLU A OE2 
91   N  N   . MET A 13  ? 0.3018 0.3236 0.3115 -0.0045 -0.0120 0.0043  237  MET A N   
92   C  CA  . MET A 13  ? 0.2507 0.2713 0.2612 -0.0035 -0.0107 0.0044  237  MET A CA  
93   C  C   . MET A 13  ? 0.2337 0.2537 0.2441 -0.0033 -0.0087 0.0035  237  MET A C   
94   O  O   . MET A 13  ? 0.2078 0.2288 0.2196 -0.0041 -0.0081 0.0033  237  MET A O   
95   C  CB  . MET A 13  ? 0.2065 0.2282 0.2206 -0.0023 -0.0113 0.0051  237  MET A CB  
96   C  CG  . MET A 13  ? 0.2363 0.2579 0.2499 -0.0019 -0.0134 0.0064  237  MET A CG  
97   S  SD  . MET A 13  ? 0.2602 0.2833 0.2788 0.0000  -0.0143 0.0071  237  MET A SD  
98   C  CE  . MET A 13  ? 0.2186 0.2392 0.2341 0.0008  -0.0164 0.0091  237  MET A CE  
99   N  N   . THR A 14  ? 0.2104 0.2284 0.2191 -0.0024 -0.0077 0.0031  238  THR A N   
100  C  CA  . THR A 14  ? 0.2349 0.2514 0.2419 -0.0016 -0.0059 0.0024  238  THR A CA  
101  C  C   . THR A 14  ? 0.2365 0.2528 0.2450 -0.0001 -0.0044 0.0024  238  THR A C   
102  O  O   . THR A 14  ? 0.2021 0.2177 0.2112 0.0008  -0.0051 0.0022  238  THR A O   
103  C  CB  . THR A 14  ? 0.2220 0.2363 0.2252 -0.0012 -0.0063 0.0014  238  THR A CB  
104  O  OG1 . THR A 14  ? 0.2548 0.2698 0.2573 -0.0024 -0.0074 0.0014  238  THR A OG1 
105  C  CG2 . THR A 14  ? 0.2294 0.2417 0.2294 -0.0001 -0.0048 0.0010  238  THR A CG2 
106  N  N   . ASN A 15  ? 0.2370 0.2534 0.2460 0.0003  -0.0021 0.0026  239  ASN A N   
107  C  CA  . ASN A 15  ? 0.2530 0.2688 0.2626 0.0021  0.0001  0.0024  239  ASN A CA  
108  C  C   . ASN A 15  ? 0.2767 0.2889 0.2808 0.0038  0.0000  0.0012  239  ASN A C   
109  O  O   . ASN A 15  ? 0.2174 0.2275 0.2170 0.0039  -0.0003 0.0007  239  ASN A O   
110  C  CB  . ASN A 15  ? 0.2002 0.2166 0.2110 0.0020  0.0034  0.0031  239  ASN A CB  
111  C  CG  . ASN A 15  ? 0.2036 0.2211 0.2175 0.0037  0.0060  0.0031  239  ASN A CG  
112  O  OD1 . ASN A 15  ? 0.2343 0.2492 0.2444 0.0058  0.0071  0.0024  239  ASN A OD1 
113  N  ND2 . ASN A 15  ? 0.1852 0.2067 0.2063 0.0028  0.0069  0.0038  239  ASN A ND2 
114  N  N   . SER A 16  ? 0.2530 0.2644 0.2578 0.0053  0.0000  0.0005  240  SER A N   
115  C  CA  . SER A 16  ? 0.2171 0.2249 0.2170 0.0069  -0.0006 -0.0012 240  SER A CA  
116  C  C   . SER A 16  ? 0.2353 0.2407 0.2306 0.0091  0.0022  -0.0018 240  SER A C   
117  O  O   . SER A 16  ? 0.2616 0.2636 0.2515 0.0108  0.0014  -0.0035 240  SER A O   
118  C  CB  . SER A 16  ? 0.2499 0.2569 0.2521 0.0076  -0.0020 -0.0019 240  SER A CB  
119  O  OG  . SER A 16  ? 0.2489 0.2573 0.2549 0.0088  -0.0002 -0.0013 240  SER A OG  
120  N  N   . ARG A 17  ? 0.1968 0.2038 0.1939 0.0093  0.0055  -0.0005 241  ARG A N   
121  C  CA  . ARG A 17  ? 0.2314 0.2357 0.2235 0.0115  0.0091  -0.0006 241  ARG A CA  
122  C  C   . ARG A 17  ? 0.2378 0.2409 0.2262 0.0108  0.0108  0.0008  241  ARG A C   
123  O  O   . ARG A 17  ? 0.2566 0.2566 0.2392 0.0128  0.0139  0.0010  241  ARG A O   
124  C  CB  . ARG A 17  ? 0.2314 0.2380 0.2283 0.0125  0.0126  0.0000  241  ARG A CB  
125  C  CG  . ARG A 17  ? 0.2206 0.2274 0.2203 0.0139  0.0111  -0.0015 241  ARG A CG  
126  C  CD  . ARG A 17  ? 0.2162 0.2258 0.2215 0.0153  0.0144  -0.0011 241  ARG A CD  
127  N  NE  . ARG A 17  ? 0.2306 0.2381 0.2311 0.0174  0.0192  -0.0011 241  ARG A NE  
128  C  CZ  . ARG A 17  ? 0.2495 0.2600 0.2547 0.0177  0.0239  0.0001  241  ARG A CZ  
129  N  NH1 . ARG A 17  ? 0.2524 0.2685 0.2678 0.0160  0.0238  0.0012  241  ARG A NH1 
130  N  NH2 . ARG A 17  ? 0.2422 0.2498 0.2415 0.0198  0.0287  0.0003  241  ARG A NH2 
131  N  N   . PHE A 18  ? 0.2485 0.2532 0.2394 0.0084  0.0090  0.0016  242  PHE A N   
132  C  CA  . PHE A 18  ? 0.2069 0.2098 0.1946 0.0078  0.0104  0.0029  242  PHE A CA  
133  C  C   . PHE A 18  ? 0.2333 0.2376 0.2230 0.0057  0.0070  0.0028  242  PHE A C   
134  O  O   . PHE A 18  ? 0.2410 0.2489 0.2367 0.0039  0.0053  0.0027  242  PHE A O   
135  C  CB  . PHE A 18  ? 0.2033 0.2077 0.1953 0.0067  0.0147  0.0047  242  PHE A CB  
136  C  CG  . PHE A 18  ? 0.2555 0.2560 0.2423 0.0070  0.0176  0.0063  242  PHE A CG  
137  C  CD1 . PHE A 18  ? 0.2531 0.2493 0.2321 0.0097  0.0208  0.0068  242  PHE A CD1 
138  C  CD2 . PHE A 18  ? 0.2279 0.2286 0.2170 0.0046  0.0174  0.0074  242  PHE A CD2 
139  C  CE1 . PHE A 18  ? 0.2440 0.2358 0.2174 0.0102  0.0238  0.0087  242  PHE A CE1 
140  C  CE2 . PHE A 18  ? 0.2516 0.2479 0.2358 0.0049  0.0202  0.0091  242  PHE A CE2 
141  C  CZ  . PHE A 18  ? 0.2526 0.2443 0.2288 0.0078  0.0235  0.0099  242  PHE A CZ  
142  N  N   . PRO A 19  ? 0.2414 0.2429 0.2260 0.0060  0.0059  0.0027  243  PRO A N   
143  C  CA  . PRO A 19  ? 0.2234 0.2263 0.2096 0.0046  0.0026  0.0021  243  PRO A CA  
144  C  C   . PRO A 19  ? 0.2407 0.2453 0.2311 0.0021  0.0031  0.0032  243  PRO A C   
145  O  O   . PRO A 19  ? 0.2379 0.2408 0.2263 0.0018  0.0028  0.0035  243  PRO A O   
146  C  CB  . PRO A 19  ? 0.2131 0.2124 0.1925 0.0065  0.0013  0.0014  243  PRO A CB  
147  C  CG  . PRO A 19  ? 0.2488 0.2442 0.2228 0.0082  0.0047  0.0028  243  PRO A CG  
148  C  CD  . PRO A 19  ? 0.2064 0.2032 0.1830 0.0084  0.0075  0.0031  243  PRO A CD  
149  N  N   . VAL A 20  ? 0.1931 0.2012 0.1898 0.0006  0.0035  0.0035  244  VAL A N   
150  C  CA  . VAL A 20  ? 0.2222 0.2325 0.2236 -0.0018 0.0031  0.0039  244  VAL A CA  
151  C  C   . VAL A 20  ? 0.2373 0.2514 0.2434 -0.0027 0.0007  0.0034  244  VAL A C   
152  O  O   . VAL A 20  ? 0.2508 0.2659 0.2576 -0.0017 0.0002  0.0032  244  VAL A O   
153  C  CB  . VAL A 20  ? 0.2580 0.2684 0.2628 -0.0027 0.0066  0.0051  244  VAL A CB  
154  C  CG1 . VAL A 20  ? 0.2014 0.2069 0.2005 -0.0017 0.0094  0.0062  244  VAL A CG1 
155  C  CG2 . VAL A 20  ? 0.1991 0.2122 0.2082 -0.0020 0.0084  0.0054  244  VAL A CG2 
156  N  N   . PRO A 21  ? 0.2130 0.2288 0.2218 -0.0045 -0.0010 0.0032  245  PRO A N   
157  C  CA  . PRO A 21  ? 0.2215 0.2405 0.2337 -0.0051 -0.0035 0.0030  245  PRO A CA  
158  C  C   . PRO A 21  ? 0.2210 0.2429 0.2390 -0.0050 -0.0027 0.0034  245  PRO A C   
159  O  O   . PRO A 21  ? 0.1833 0.2057 0.2043 -0.0053 -0.0002 0.0038  245  PRO A O   
160  C  CB  . PRO A 21  ? 0.2611 0.2806 0.2737 -0.0068 -0.0052 0.0024  245  PRO A CB  
161  C  CG  . PRO A 21  ? 0.2190 0.2350 0.2274 -0.0067 -0.0041 0.0022  245  PRO A CG  
162  C  CD  . PRO A 21  ? 0.2138 0.2280 0.2216 -0.0058 -0.0011 0.0030  245  PRO A CD  
163  N  N   . VAL A 22  ? 0.1825 0.2064 0.2023 -0.0044 -0.0048 0.0034  246  VAL A N   
164  C  CA  . VAL A 22  ? 0.2072 0.2345 0.2333 -0.0040 -0.0049 0.0037  246  VAL A CA  
165  C  C   . VAL A 22  ? 0.2073 0.2375 0.2384 -0.0058 -0.0064 0.0033  246  VAL A C   
166  O  O   . VAL A 22  ? 0.2180 0.2479 0.2470 -0.0068 -0.0089 0.0027  246  VAL A O   
167  C  CB  . VAL A 22  ? 0.2485 0.2762 0.2744 -0.0026 -0.0072 0.0041  246  VAL A CB  
168  C  CG1 . VAL A 22  ? 0.1759 0.2074 0.2087 -0.0019 -0.0082 0.0043  246  VAL A CG1 
169  C  CG2 . VAL A 22  ? 0.1768 0.2014 0.1990 -0.0010 -0.0057 0.0040  246  VAL A CG2 
170  N  N   . ASP A 23  ? 0.2068 0.2401 0.2450 -0.0061 -0.0048 0.0033  247  ASP A N   
171  C  CA  . ASP A 23  ? 0.2176 0.2543 0.2622 -0.0080 -0.0067 0.0025  247  ASP A CA  
172  C  C   . ASP A 23  ? 0.2502 0.2911 0.3002 -0.0071 -0.0102 0.0021  247  ASP A C   
173  O  O   . ASP A 23  ? 0.2334 0.2760 0.2849 -0.0081 -0.0140 0.0011  247  ASP A O   
174  C  CB  . ASP A 23  ? 0.2102 0.2480 0.2608 -0.0094 -0.0029 0.0026  247  ASP A CB  
175  C  CG  . ASP A 23  ? 0.3061 0.3391 0.3512 -0.0105 -0.0002 0.0029  247  ASP A CG  
176  O  OD1 . ASP A 23  ? 0.3155 0.3467 0.3579 -0.0119 -0.0025 0.0021  247  ASP A OD1 
177  O  OD2 . ASP A 23  ? 0.2455 0.2761 0.2883 -0.0098 0.0040  0.0040  247  ASP A OD2 
178  N  N   . GLN A 24  ? 0.1990 0.2415 0.2515 -0.0049 -0.0094 0.0028  248  GLN A N   
179  C  CA  . GLN A 24  ? 0.2077 0.2541 0.2657 -0.0036 -0.0130 0.0026  248  GLN A CA  
180  C  C   . GLN A 24  ? 0.1905 0.2362 0.2479 -0.0008 -0.0119 0.0035  248  GLN A C   
181  O  O   . GLN A 24  ? 0.2027 0.2462 0.2580 0.0000  -0.0080 0.0039  248  GLN A O   
182  C  CB  . GLN A 24  ? 0.2055 0.2578 0.2749 -0.0048 -0.0130 0.0016  248  GLN A CB  
183  C  CG  . GLN A 24  ? 0.2016 0.2555 0.2766 -0.0043 -0.0076 0.0021  248  GLN A CG  
184  C  CD  . GLN A 24  ? 0.2426 0.3029 0.3306 -0.0057 -0.0070 0.0011  248  GLN A CD  
185  O  OE1 . GLN A 24  ? 0.2259 0.2895 0.3207 -0.0044 -0.0037 0.0014  248  GLN A OE1 
186  N  NE2 . GLN A 24  ? 0.2540 0.3162 0.3456 -0.0082 -0.0101 -0.0002 248  GLN A NE2 
187  N  N   . MET A 25  ? 0.2035 0.2506 0.2621 0.0010  -0.0157 0.0039  249  MET A N   
188  C  CA  . MET A 25  ? 0.2128 0.2602 0.2739 0.0039  -0.0149 0.0045  249  MET A CA  
189  C  C   . MET A 25  ? 0.2632 0.3165 0.3354 0.0045  -0.0133 0.0038  249  MET A C   
190  O  O   . MET A 25  ? 0.1997 0.2576 0.2789 0.0029  -0.0149 0.0029  249  MET A O   
191  C  CB  . MET A 25  ? 0.2323 0.2786 0.2909 0.0058  -0.0194 0.0055  249  MET A CB  
192  C  CG  . MET A 25  ? 0.2709 0.3113 0.3191 0.0054  -0.0198 0.0065  249  MET A CG  
193  S  SD  . MET A 25  ? 0.2773 0.3154 0.3212 0.0075  -0.0245 0.0082  249  MET A SD  
194  C  CE  . MET A 25  ? 0.2678 0.3105 0.3147 0.0067  -0.0292 0.0072  249  MET A CE  
195  N  N   . TYR A 26  ? 0.1785 0.2315 0.2525 0.0066  -0.0099 0.0040  250  TYR A N   
196  C  CA  . TYR A 26  ? 0.2020 0.2605 0.2866 0.0074  -0.0071 0.0034  250  TYR A CA  
197  C  C   . TYR A 26  ? 0.2084 0.2665 0.2945 0.0112  -0.0062 0.0036  250  TYR A C   
198  O  O   . TYR A 26  ? 0.2293 0.2817 0.3074 0.0126  -0.0055 0.0040  250  TYR A O   
199  C  CB  . TYR A 26  ? 0.2272 0.2853 0.3119 0.0055  -0.0012 0.0032  250  TYR A CB  
200  C  CG  . TYR A 26  ? 0.2220 0.2859 0.3181 0.0059  0.0026  0.0028  250  TYR A CG  
201  C  CD1 . TYR A 26  ? 0.2476 0.3178 0.3544 0.0037  0.0013  0.0020  250  TYR A CD1 
202  C  CD2 . TYR A 26  ? 0.2394 0.3028 0.3360 0.0084  0.0076  0.0029  250  TYR A CD2 
203  C  CE1 . TYR A 26  ? 0.2822 0.3585 0.4010 0.0038  0.0051  0.0016  250  TYR A CE1 
204  C  CE2 . TYR A 26  ? 0.2033 0.2724 0.3107 0.0088  0.0119  0.0026  250  TYR A CE2 
205  C  CZ  . TYR A 26  ? 0.2522 0.3279 0.3711 0.0064  0.0107  0.0021  250  TYR A CZ  
206  O  OH  . TYR A 26  ? 0.3271 0.4092 0.4583 0.0065  0.0153  0.0018  250  TYR A OH  
207  N  N   . THR A 27  ? 0.2212 0.2855 0.3184 0.0130  -0.0064 0.0030  251  THR A N   
208  C  CA  . THR A 27  ? 0.2308 0.2949 0.3304 0.0169  -0.0051 0.0030  251  THR A CA  
209  C  C   . THR A 27  ? 0.2516 0.3219 0.3623 0.0177  -0.0002 0.0021  251  THR A C   
210  O  O   . THR A 27  ? 0.2402 0.3166 0.3599 0.0155  0.0002  0.0016  251  THR A O   
211  C  CB  . THR A 27  ? 0.2207 0.2858 0.3226 0.0196  -0.0110 0.0035  251  THR A CB  
212  O  OG1 . THR A 27  ? 0.2340 0.2975 0.3371 0.0236  -0.0094 0.0035  251  THR A OG1 
213  C  CG2 . THR A 27  ? 0.1959 0.2693 0.3096 0.0194  -0.0146 0.0028  251  THR A CG2 
214  N  N   . SER A 28  ? 0.2083 0.2767 0.3183 0.0209  0.0037  0.0018  252  SER A N   
215  C  CA  . SER A 28  ? 0.3150 0.3886 0.4344 0.0221  0.0094  0.0011  252  SER A CA  
216  C  C   . SER A 28  ? 0.3285 0.4012 0.4493 0.0269  0.0109  0.0005  252  SER A C   
217  O  O   . SER A 28  ? 0.2845 0.3505 0.3966 0.0289  0.0089  0.0006  252  SER A O   
218  C  CB  . SER A 28  ? 0.3170 0.3878 0.4309 0.0199  0.0160  0.0013  252  SER A CB  
219  O  OG  . SER A 28  ? 0.3742 0.4481 0.4943 0.0220  0.0225  0.0008  252  SER A OG  
220  N  N   A ARG A 29  ? 0.3449 0.4245 0.4779 0.0288  0.0145  -0.0003 253  ARG A N   
221  C  CA  A ARG A 29  ? 0.3676 0.4464 0.5022 0.0337  0.0171  -0.0012 253  ARG A CA  
222  C  C   A ARG A 29  ? 0.4004 0.4722 0.5242 0.0346  0.0233  -0.0017 253  ARG A C   
223  O  O   A ARG A 29  ? 0.3530 0.4200 0.4722 0.0384  0.0240  -0.0026 253  ARG A O   
224  C  CB  A ARG A 29  ? 0.4011 0.4898 0.5524 0.0356  0.0200  -0.0020 253  ARG A CB  
225  C  CG  A ARG A 29  ? 0.4208 0.5181 0.5848 0.0338  0.0148  -0.0020 253  ARG A CG  
226  C  CD  A ARG A 29  ? 0.4582 0.5657 0.6397 0.0358  0.0182  -0.0031 253  ARG A CD  
227  N  NE  A ARG A 29  ? 0.5443 0.6609 0.7395 0.0344  0.0125  -0.0036 253  ARG A NE  
228  C  CZ  A ARG A 29  ? 0.4984 0.6179 0.6990 0.0375  0.0053  -0.0039 253  ARG A CZ  
229  N  NH1 A ARG A 29  ? 0.4647 0.5785 0.6585 0.0420  0.0031  -0.0036 253  ARG A NH1 
230  N  NH2 A ARG A 29  ? 0.4392 0.5672 0.6522 0.0360  0.0000  -0.0047 253  ARG A NH2 
231  N  N   . SER A 30  ? 0.3701 0.4410 0.4897 0.0315  0.0277  -0.0012 254  SER A N   
232  C  CA  . SER A 30  ? 0.4933 0.5578 0.6022 0.0324  0.0337  -0.0016 254  SER A CA  
233  C  C   . SER A 30  ? 0.5671 0.6330 0.6800 0.0371  0.0393  -0.0029 254  SER A C   
234  O  O   . SER A 30  ? 0.5271 0.5862 0.6303 0.0401  0.0410  -0.0042 254  SER A O   
235  C  CB  . SER A 30  ? 0.4675 0.5225 0.5617 0.0325  0.0301  -0.0019 254  SER A CB  
236  O  OG  . SER A 30  ? 0.4599 0.5139 0.5507 0.0286  0.0250  -0.0007 254  SER A OG  
237  N  N   . GLU A 31  ? 0.6593 0.7343 0.7870 0.0378  0.0421  -0.0030 255  GLU A N   
238  C  CA  . GLU A 31  ? 0.6132 0.6906 0.7462 0.0423  0.0481  -0.0043 255  GLU A CA  
239  C  C   . GLU A 31  ? 0.6477 0.7208 0.7717 0.0425  0.0565  -0.0043 255  GLU A C   
240  O  O   . GLU A 31  ? 0.6374 0.7109 0.7596 0.0388  0.0596  -0.0028 255  GLU A O   
241  C  CB  . GLU A 31  ? 0.6544 0.7435 0.8068 0.0426  0.0494  -0.0044 255  GLU A CB  
242  C  CG  . GLU A 31  ? 0.7659 0.8597 0.9274 0.0425  0.0406  -0.0043 255  GLU A CG  
243  C  CD  . GLU A 31  ? 0.9228 1.0278 1.1037 0.0449  0.0414  -0.0052 255  GLU A CD  
244  O  OE1 . GLU A 31  ? 1.0098 1.1156 1.1942 0.0499  0.0445  -0.0065 255  GLU A OE1 
245  O  OE2 . GLU A 31  ? 0.7987 0.9118 0.9916 0.0418  0.0386  -0.0048 255  GLU A OE2 
246  N  N   . GLY A 32  ? 0.5869 0.6552 0.7043 0.0472  0.0601  -0.0060 256  GLY A N   
247  C  CA  . GLY A 32  ? 0.5569 0.6203 0.6641 0.0483  0.0681  -0.0062 256  GLY A CA  
248  C  C   . GLY A 32  ? 0.5452 0.6003 0.6363 0.0456  0.0666  -0.0054 256  GLY A C   
249  O  O   . GLY A 32  ? 0.6136 0.6655 0.6969 0.0454  0.0730  -0.0047 256  GLY A O   
250  N  N   . ILE A 33  ? 0.4415 0.4926 0.5273 0.0436  0.0586  -0.0053 257  ILE A N   
251  C  CA  . ILE A 33  ? 0.4612 0.5051 0.5332 0.0409  0.0564  -0.0047 257  ILE A CA  
252  C  C   . ILE A 33  ? 0.3779 0.4139 0.4397 0.0431  0.0513  -0.0068 257  ILE A C   
253  O  O   . ILE A 33  ? 0.4015 0.4383 0.4685 0.0441  0.0463  -0.0075 257  ILE A O   
254  C  CB  . ILE A 33  ? 0.4995 0.5467 0.5757 0.0357  0.0518  -0.0027 257  ILE A CB  
255  C  CG1 . ILE A 33  ? 0.5591 0.6130 0.6448 0.0331  0.0572  -0.0008 257  ILE A CG1 
256  C  CG2 . ILE A 33  ? 0.3980 0.4376 0.4604 0.0335  0.0484  -0.0024 257  ILE A CG2 
257  C  CD1 . ILE A 33  ? 0.4852 0.5421 0.5755 0.0280  0.0527  0.0007  257  ILE A CD1 
258  N  N   . VAL A 34  ? 0.3660 0.3941 0.4134 0.0437  0.0523  -0.0077 258  VAL A N   
259  C  CA  . VAL A 34  ? 0.3570 0.3773 0.3946 0.0447  0.0469  -0.0098 258  VAL A CA  
260  C  C   . VAL A 34  ? 0.2769 0.2953 0.3098 0.0403  0.0418  -0.0084 258  VAL A C   
261  O  O   . VAL A 34  ? 0.3031 0.3192 0.3285 0.0387  0.0436  -0.0075 258  VAL A O   
262  C  CB  . VAL A 34  ? 0.3164 0.3293 0.3414 0.0486  0.0505  -0.0123 258  VAL A CB  
263  C  CG1 . VAL A 34  ? 0.3409 0.3460 0.3570 0.0491  0.0445  -0.0148 258  VAL A CG1 
264  C  CG2 . VAL A 34  ? 0.4093 0.4243 0.4394 0.0532  0.0560  -0.0138 258  VAL A CG2 
265  N  N   . VAL A 35  ? 0.2773 0.2965 0.3146 0.0386  0.0354  -0.0080 259  VAL A N   
266  C  CA  . VAL A 35  ? 0.2566 0.2745 0.2904 0.0346  0.0305  -0.0068 259  VAL A CA  
267  C  C   . VAL A 35  ? 0.2645 0.2742 0.2873 0.0354  0.0275  -0.0089 259  VAL A C   
268  O  O   . VAL A 35  ? 0.2910 0.2978 0.3144 0.0363  0.0238  -0.0100 259  VAL A O   
269  C  CB  . VAL A 35  ? 0.2438 0.2662 0.2869 0.0326  0.0256  -0.0053 259  VAL A CB  
270  C  CG1 . VAL A 35  ? 0.2287 0.2494 0.2676 0.0287  0.0211  -0.0041 259  VAL A CG1 
271  C  CG2 . VAL A 35  ? 0.2752 0.3061 0.3304 0.0321  0.0281  -0.0038 259  VAL A CG2 
272  N  N   . GLN A 36  ? 0.2600 0.2658 0.2728 0.0349  0.0289  -0.0094 260  GLN A N   
273  C  CA  . GLN A 36  ? 0.2490 0.2475 0.2518 0.0358  0.0258  -0.0119 260  GLN A CA  
274  C  C   . GLN A 36  ? 0.2634 0.2600 0.2589 0.0332  0.0241  -0.0112 260  GLN A C   
275  O  O   . GLN A 36  ? 0.2434 0.2351 0.2287 0.0349  0.0250  -0.0128 260  GLN A O   
276  C  CB  . GLN A 36  ? 0.2765 0.2704 0.2724 0.0403  0.0295  -0.0147 260  GLN A CB  
277  C  CG  . GLN A 36  ? 0.3046 0.2909 0.2919 0.0417  0.0256  -0.0181 260  GLN A CG  
278  C  CD  . GLN A 36  ? 0.3261 0.3081 0.3085 0.0466  0.0288  -0.0213 260  GLN A CD  
279  O  OE1 . GLN A 36  ? 0.3476 0.3324 0.3326 0.0490  0.0344  -0.0207 260  GLN A OE1 
280  N  NE2 . GLN A 36  ? 0.2864 0.2614 0.2620 0.0480  0.0253  -0.0249 260  GLN A NE2 
281  N  N   . PRO A 37  ? 0.2385 0.2386 0.2386 0.0295  0.0213  -0.0090 261  PRO A N   
282  C  CA  . PRO A 37  ? 0.2684 0.2666 0.2621 0.0273  0.0195  -0.0085 261  PRO A CA  
283  C  C   . PRO A 37  ? 0.2774 0.2702 0.2648 0.0277  0.0150  -0.0110 261  PRO A C   
284  O  O   . PRO A 37  ? 0.2347 0.2259 0.2247 0.0281  0.0123  -0.0125 261  PRO A O   
285  C  CB  . PRO A 37  ? 0.2602 0.2634 0.2615 0.0235  0.0173  -0.0060 261  PRO A CB  
286  C  CG  . PRO A 37  ? 0.2365 0.2422 0.2460 0.0238  0.0154  -0.0059 261  PRO A CG  
287  C  CD  . PRO A 37  ? 0.2420 0.2473 0.2525 0.0274  0.0192  -0.0071 261  PRO A CD  
288  N  N   . GLN A 38  ? 0.2628 0.2526 0.2418 0.0276  0.0143  -0.0117 262  GLN A N   
289  C  CA  . GLN A 38  ? 0.2762 0.2612 0.2492 0.0281  0.0099  -0.0145 262  GLN A CA  
290  C  C   . GLN A 38  ? 0.2722 0.2584 0.2467 0.0247  0.0058  -0.0138 262  GLN A C   
291  O  O   . GLN A 38  ? 0.2905 0.2742 0.2637 0.0243  0.0017  -0.0160 262  GLN A O   
292  C  CB  . GLN A 38  ? 0.2795 0.2595 0.2409 0.0313  0.0114  -0.0165 262  GLN A CB  
293  C  CG  . GLN A 38  ? 0.2622 0.2399 0.2205 0.0352  0.0156  -0.0180 262  GLN A CG  
294  C  CD  . GLN A 38  ? 0.2919 0.2679 0.2542 0.0361  0.0134  -0.0206 262  GLN A CD  
295  O  OE1 . GLN A 38  ? 0.2868 0.2592 0.2470 0.0358  0.0086  -0.0233 262  GLN A OE1 
296  N  NE2 . GLN A 38  ? 0.2979 0.2763 0.2665 0.0373  0.0167  -0.0198 262  GLN A NE2 
297  N  N   . ASN A 39  ? 0.2245 0.2148 0.2024 0.0223  0.0068  -0.0108 263  ASN A N   
298  C  CA  . ASN A 39  ? 0.2420 0.2343 0.2227 0.0192  0.0034  -0.0098 263  ASN A CA  
299  C  C   . ASN A 39  ? 0.2708 0.2670 0.2605 0.0169  0.0025  -0.0082 263  ASN A C   
300  O  O   . ASN A 39  ? 0.2549 0.2533 0.2492 0.0175  0.0048  -0.0071 263  ASN A O   
301  C  CB  . ASN A 39  ? 0.2308 0.2243 0.2088 0.0183  0.0049  -0.0079 263  ASN A CB  
302  C  CG  . ASN A 39  ? 0.2534 0.2425 0.2216 0.0206  0.0046  -0.0094 263  ASN A CG  
303  O  OD1 . ASN A 39  ? 0.2450 0.2315 0.2101 0.0212  0.0008  -0.0120 263  ASN A OD1 
304  N  ND2 . ASN A 39  ? 0.2480 0.2359 0.2113 0.0219  0.0084  -0.0079 263  ASN A ND2 
305  N  N   . GLY A 40  ? 0.2651 0.2620 0.2571 0.0145  -0.0008 -0.0079 264  GLY A N   
306  C  CA  . GLY A 40  ? 0.2277 0.2272 0.2265 0.0127  -0.0019 -0.0063 264  GLY A CA  
307  C  C   . GLY A 40  ? 0.2648 0.2621 0.2661 0.0140  -0.0025 -0.0072 264  GLY A C   
308  O  O   . GLY A 40  ? 0.2590 0.2583 0.2654 0.0140  -0.0022 -0.0056 264  GLY A O   
309  N  N   . ARG A 41  ? 0.2286 0.2215 0.2262 0.0155  -0.0035 -0.0099 265  ARG A N   
310  C  CA  . ARG A 41  ? 0.2524 0.2422 0.2520 0.0170  -0.0041 -0.0113 265  ARG A CA  
311  C  C   . ARG A 41  ? 0.2443 0.2311 0.2450 0.0151  -0.0074 -0.0124 265  ARG A C   
312  O  O   . ARG A 41  ? 0.2603 0.2449 0.2575 0.0147  -0.0092 -0.0148 265  ARG A O   
313  C  CB  . ARG A 41  ? 0.2341 0.2204 0.2287 0.0205  -0.0022 -0.0140 265  ARG A CB  
314  C  CG  . ARG A 41  ? 0.2315 0.2207 0.2255 0.0224  0.0020  -0.0128 265  ARG A CG  
315  C  CD  . ARG A 41  ? 0.2511 0.2442 0.2530 0.0224  0.0033  -0.0105 265  ARG A CD  
316  N  NE  . ARG A 41  ? 0.2215 0.2115 0.2258 0.0244  0.0027  -0.0118 265  ARG A NE  
317  C  CZ  . ARG A 41  ? 0.2459 0.2346 0.2499 0.0278  0.0054  -0.0132 265  ARG A CZ  
318  N  NH1 . ARG A 41  ? 0.2788 0.2694 0.2805 0.0296  0.0095  -0.0133 265  ARG A NH1 
319  N  NH2 . ARG A 41  ? 0.2629 0.2482 0.2691 0.0297  0.0044  -0.0145 265  ARG A NH2 
320  N  N   . ALA A 42  ? 0.2399 0.2266 0.2456 0.0138  -0.0083 -0.0105 266  ALA A N   
321  C  CA  . ALA A 42  ? 0.2828 0.2664 0.2904 0.0117  -0.0107 -0.0112 266  ALA A CA  
322  C  C   . ALA A 42  ? 0.2940 0.2753 0.3057 0.0120  -0.0108 -0.0095 266  ALA A C   
323  O  O   . ALA A 42  ? 0.2891 0.2730 0.3030 0.0127  -0.0098 -0.0068 266  ALA A O   
324  C  CB  . ALA A 42  ? 0.2367 0.2234 0.2454 0.0085  -0.0117 -0.0095 266  ALA A CB  
325  N  N   . THR A 43  ? 0.2565 0.2325 0.2693 0.0116  -0.0123 -0.0112 267  THR A N   
326  C  CA  . THR A 43  ? 0.3296 0.3025 0.3460 0.0116  -0.0125 -0.0091 267  THR A CA  
327  C  C   . THR A 43  ? 0.2824 0.2570 0.3011 0.0083  -0.0129 -0.0056 267  THR A C   
328  O  O   . THR A 43  ? 0.2485 0.2255 0.2667 0.0058  -0.0133 -0.0058 267  THR A O   
329  C  CB  . THR A 43  ? 0.2861 0.2520 0.3033 0.0120  -0.0137 -0.0119 267  THR A CB  
330  O  OG1 . THR A 43  ? 0.2656 0.2302 0.2841 0.0087  -0.0154 -0.0132 267  THR A OG1 
331  C  CG2 . THR A 43  ? 0.2881 0.2521 0.3017 0.0153  -0.0133 -0.0159 267  THR A CG2 
332  N  N   . ILE A 44  ? 0.2696 0.2427 0.2904 0.0087  -0.0127 -0.0024 268  ILE A N   
333  C  CA  . ILE A 44  ? 0.2891 0.2633 0.3106 0.0059  -0.0127 0.0010  268  ILE A CA  
334  C  C   . ILE A 44  ? 0.3197 0.2900 0.3431 0.0029  -0.0130 0.0006  268  ILE A C   
335  O  O   . ILE A 44  ? 0.2664 0.2381 0.2902 0.0003  -0.0124 0.0030  268  ILE A O   
336  C  CB  . ILE A 44  ? 0.3078 0.2812 0.3298 0.0074  -0.0126 0.0049  268  ILE A CB  
337  C  CG1 . ILE A 44  ? 0.2896 0.2558 0.3132 0.0086  -0.0129 0.0054  268  ILE A CG1 
338  C  CG2 . ILE A 44  ? 0.2808 0.2589 0.3028 0.0104  -0.0125 0.0049  268  ILE A CG2 
339  C  CD1 . ILE A 44  ? 0.3259 0.2917 0.3497 0.0112  -0.0134 0.0089  268  ILE A CD1 
340  N  N   . ASP A 45  ? 0.2701 0.2357 0.2949 0.0030  -0.0138 -0.0026 269  ASP A N   
341  C  CA  . ASP A 45  ? 0.3563 0.3192 0.3841 -0.0004 -0.0144 -0.0038 269  ASP A CA  
342  C  C   . ASP A 45  ? 0.3659 0.3325 0.3933 -0.0015 -0.0156 -0.0075 269  ASP A C   
343  O  O   . ASP A 45  ? 0.4253 0.3903 0.4563 -0.0040 -0.0166 -0.0097 269  ASP A O   
344  C  CB  . ASP A 45  ? 0.4168 0.3719 0.4472 -0.0002 -0.0151 -0.0054 269  ASP A CB  
345  C  CG  . ASP A 45  ? 0.5199 0.4726 0.5483 0.0031  -0.0163 -0.0097 269  ASP A CG  
346  O  OD1 . ASP A 45  ? 0.4761 0.4330 0.5012 0.0047  -0.0166 -0.0120 269  ASP A OD1 
347  O  OD2 . ASP A 45  ? 0.5332 0.4791 0.5630 0.0041  -0.0167 -0.0107 269  ASP A OD2 
348  N  N   . GLY A 46  ? 0.3265 0.2980 0.3502 0.0003  -0.0155 -0.0083 270  GLY A N   
349  C  CA  . GLY A 46  ? 0.3260 0.3016 0.3487 -0.0007 -0.0165 -0.0105 270  GLY A CA  
350  C  C   . GLY A 46  ? 0.3691 0.3432 0.3891 0.0012  -0.0183 -0.0153 270  GLY A C   
351  O  O   . GLY A 46  ? 0.3425 0.3192 0.3617 0.0005  -0.0198 -0.0174 270  GLY A O   
352  N  N   . GLU A 47  ? 0.2952 0.2650 0.3132 0.0039  -0.0185 -0.0172 271  GLU A N   
353  C  CA  . GLU A 47  ? 0.3021 0.2701 0.3157 0.0063  -0.0200 -0.0217 271  GLU A CA  
354  C  C   . GLU A 47  ? 0.3246 0.2966 0.3326 0.0089  -0.0182 -0.0209 271  GLU A C   
355  O  O   . GLU A 47  ? 0.3143 0.2872 0.3218 0.0106  -0.0159 -0.0186 271  GLU A O   
356  C  CB  . GLU A 47  ? 0.3348 0.2963 0.3481 0.0084  -0.0204 -0.0242 271  GLU A CB  
357  C  CG  . GLU A 47  ? 0.3656 0.3246 0.3727 0.0116  -0.0217 -0.0290 271  GLU A CG  
358  C  CD  . GLU A 47  ? 0.4522 0.4041 0.4590 0.0138  -0.0223 -0.0321 271  GLU A CD  
359  O  OE1 . GLU A 47  ? 0.4003 0.3501 0.4103 0.0142  -0.0206 -0.0297 271  GLU A OE1 
360  O  OE2 . GLU A 47  ? 0.5297 0.4779 0.5329 0.0152  -0.0247 -0.0371 271  GLU A OE2 
361  N  N   . LEU A 48  ? 0.3083 0.2824 0.3126 0.0092  -0.0194 -0.0228 272  LEU A N   
362  C  CA  . LEU A 48  ? 0.2760 0.2529 0.2746 0.0115  -0.0176 -0.0221 272  LEU A CA  
363  C  C   . LEU A 48  ? 0.2876 0.2607 0.2804 0.0154  -0.0168 -0.0248 272  LEU A C   
364  O  O   . LEU A 48  ? 0.3487 0.3173 0.3394 0.0164  -0.0191 -0.0288 272  LEU A O   
365  C  CB  . LEU A 48  ? 0.2764 0.2560 0.2725 0.0108  -0.0192 -0.0229 272  LEU A CB  
366  C  CG  . LEU A 48  ? 0.3008 0.2843 0.3024 0.0072  -0.0199 -0.0208 272  LEU A CG  
367  C  CD1 . LEU A 48  ? 0.2902 0.2760 0.2895 0.0072  -0.0220 -0.0224 272  LEU A CD1 
368  C  CD2 . LEU A 48  ? 0.2754 0.2624 0.2787 0.0063  -0.0170 -0.0164 272  LEU A CD2 
369  N  N   . LEU A 49  ? 0.2616 0.2363 0.2519 0.0175  -0.0134 -0.0229 273  LEU A N   
370  C  CA  . LEU A 49  ? 0.2848 0.2563 0.2697 0.0215  -0.0115 -0.0251 273  LEU A CA  
371  C  C   . LEU A 49  ? 0.3164 0.2897 0.2945 0.0234  -0.0091 -0.0246 273  LEU A C   
372  O  O   . LEU A 49  ? 0.2693 0.2466 0.2479 0.0217  -0.0087 -0.0221 273  LEU A O   
373  C  CB  . LEU A 49  ? 0.2809 0.2525 0.2701 0.0227  -0.0088 -0.0234 273  LEU A CB  
374  C  CG  . LEU A 49  ? 0.2739 0.2436 0.2698 0.0207  -0.0107 -0.0226 273  LEU A CG  
375  C  CD1 . LEU A 49  ? 0.3248 0.2952 0.3248 0.0224  -0.0083 -0.0203 273  LEU A CD1 
376  C  CD2 . LEU A 49  ? 0.2981 0.2614 0.2928 0.0210  -0.0136 -0.0268 273  LEU A CD2 
377  N  N   . GLY A 50  ? 0.2644 0.2344 0.2360 0.0272  -0.0073 -0.0268 274  GLY A N   
378  C  CA  . GLY A 50  ? 0.2922 0.2629 0.2565 0.0294  -0.0042 -0.0261 274  GLY A CA  
379  C  C   . GLY A 50  ? 0.3099 0.2806 0.2691 0.0286  -0.0069 -0.0266 274  GLY A C   
380  O  O   . GLY A 50  ? 0.3212 0.2886 0.2769 0.0291  -0.0111 -0.0301 274  GLY A O   
381  N  N   . THR A 51  ? 0.3094 0.2838 0.2685 0.0275  -0.0047 -0.0232 275  THR A N   
382  C  CA  . THR A 51  ? 0.2798 0.2545 0.2346 0.0270  -0.0069 -0.0230 275  THR A CA  
383  C  C   . THR A 51  ? 0.2543 0.2336 0.2169 0.0230  -0.0087 -0.0207 275  THR A C   
384  O  O   . THR A 51  ? 0.2469 0.2278 0.2076 0.0223  -0.0090 -0.0193 275  THR A O   
385  C  CB  . THR A 51  ? 0.2960 0.2700 0.2432 0.0292  -0.0029 -0.0210 275  THR A CB  
386  O  OG1 . THR A 51  ? 0.2681 0.2462 0.2212 0.0277  0.0016  -0.0173 275  THR A OG1 
387  C  CG2 . THR A 51  ? 0.2783 0.2470 0.2156 0.0336  -0.0010 -0.0235 275  THR A CG2 
388  N  N   . THR A 52  ? 0.2756 0.2568 0.2466 0.0205  -0.0096 -0.0202 276  THR A N   
389  C  CA  . THR A 52  ? 0.2234 0.2090 0.2011 0.0170  -0.0102 -0.0175 276  THR A CA  
390  C  C   . THR A 52  ? 0.2823 0.2683 0.2611 0.0153  -0.0142 -0.0191 276  THR A C   
391  O  O   . THR A 52  ? 0.2876 0.2713 0.2674 0.0152  -0.0173 -0.0221 276  THR A O   
392  C  CB  . THR A 52  ? 0.2626 0.2495 0.2478 0.0154  -0.0096 -0.0161 276  THR A CB  
393  O  OG1 . THR A 52  ? 0.2392 0.2269 0.2248 0.0169  -0.0060 -0.0145 276  THR A OG1 
394  C  CG2 . THR A 52  ? 0.2561 0.2469 0.2469 0.0120  -0.0104 -0.0135 276  THR A CG2 
395  N  N   . LEU A 53  ? 0.2388 0.2279 0.2181 0.0140  -0.0142 -0.0172 277  LEU A N   
396  C  CA  . LEU A 53  ? 0.2803 0.2710 0.2623 0.0122  -0.0176 -0.0182 277  LEU A CA  
397  C  C   . LEU A 53  ? 0.2793 0.2741 0.2679 0.0091  -0.0166 -0.0154 277  LEU A C   
398  O  O   . LEU A 53  ? 0.3003 0.2965 0.2904 0.0084  -0.0139 -0.0127 277  LEU A O   
399  C  CB  . LEU A 53  ? 0.2711 0.2613 0.2468 0.0142  -0.0188 -0.0190 277  LEU A CB  
400  C  CG  . LEU A 53  ? 0.3786 0.3686 0.3489 0.0156  -0.0156 -0.0164 277  LEU A CG  
401  C  CD1 . LEU A 53  ? 0.2882 0.2821 0.2638 0.0129  -0.0135 -0.0131 277  LEU A CD1 
402  C  CD2 . LEU A 53  ? 0.2968 0.2850 0.2601 0.0180  -0.0177 -0.0175 277  LEU A CD2 
403  N  N   . VAL A 54  ? 0.2639 0.2606 0.2567 0.0071  -0.0189 -0.0161 278  VAL A N   
404  C  CA  . VAL A 54  ? 0.2531 0.2532 0.2517 0.0042  -0.0179 -0.0137 278  VAL A CA  
405  C  C   . VAL A 54  ? 0.2842 0.2870 0.2814 0.0040  -0.0168 -0.0118 278  VAL A C   
406  O  O   . VAL A 54  ? 0.2911 0.2960 0.2906 0.0025  -0.0150 -0.0093 278  VAL A O   
407  C  CB  . VAL A 54  ? 0.3186 0.3194 0.3231 0.0021  -0.0201 -0.0153 278  VAL A CB  
408  C  CG1 . VAL A 54  ? 0.3831 0.3872 0.3925 -0.0006 -0.0187 -0.0128 278  VAL A CG1 
409  C  CG2 . VAL A 54  ? 0.3486 0.3460 0.3552 0.0019  -0.0206 -0.0166 278  VAL A CG2 
410  N  N   . SER A 55  ? 0.3192 0.3215 0.3121 0.0059  -0.0180 -0.0130 279  SER A N   
411  C  CA  . SER A 55  ? 0.2900 0.2940 0.2813 0.0059  -0.0171 -0.0114 279  SER A CA  
412  C  C   . SER A 55  ? 0.2541 0.2579 0.2434 0.0059  -0.0139 -0.0088 279  SER A C   
413  O  O   . SER A 55  ? 0.2712 0.2727 0.2569 0.0075  -0.0124 -0.0087 279  SER A O   
414  C  CB  . SER A 55  ? 0.2678 0.2702 0.2537 0.0085  -0.0191 -0.0131 279  SER A CB  
415  O  OG  . SER A 55  ? 0.2670 0.2696 0.2502 0.0091  -0.0176 -0.0112 279  SER A OG  
416  N  N   . PRO A 56  ? 0.2811 0.2873 0.2729 0.0042  -0.0126 -0.0069 280  PRO A N   
417  C  CA  . PRO A 56  ? 0.3119 0.3183 0.3032 0.0039  -0.0101 -0.0047 280  PRO A CA  
418  C  C   . PRO A 56  ? 0.2766 0.2816 0.2636 0.0051  -0.0087 -0.0040 280  PRO A C   
419  O  O   . PRO A 56  ? 0.3123 0.3174 0.2997 0.0046  -0.0064 -0.0024 280  PRO A O   
420  C  CB  . PRO A 56  ? 0.2865 0.2959 0.2821 0.0015  -0.0100 -0.0035 280  PRO A CB  
421  C  CG  . PRO A 56  ? 0.2728 0.2832 0.2692 0.0012  -0.0116 -0.0046 280  PRO A CG  
422  C  CD  . PRO A 56  ? 0.2574 0.2664 0.2533 0.0024  -0.0136 -0.0068 280  PRO A CD  
423  N  N   . VAL A 57  ? 0.2523 0.2556 0.2356 0.0066  -0.0101 -0.0050 281  VAL A N   
424  C  CA  . VAL A 57  ? 0.2702 0.2711 0.2487 0.0080  -0.0089 -0.0040 281  VAL A CA  
425  C  C   . VAL A 57  ? 0.2911 0.2880 0.2626 0.0110  -0.0088 -0.0047 281  VAL A C   
426  O  O   . VAL A 57  ? 0.3288 0.3226 0.2949 0.0126  -0.0077 -0.0036 281  VAL A O   
427  C  CB  . VAL A 57  ? 0.3116 0.3133 0.2905 0.0079  -0.0105 -0.0042 281  VAL A CB  
428  C  CG1 . VAL A 57  ? 0.2495 0.2544 0.2337 0.0053  -0.0099 -0.0035 281  VAL A CG1 
429  C  CG2 . VAL A 57  ? 0.2462 0.2486 0.2254 0.0091  -0.0139 -0.0066 281  VAL A CG2 
430  N  N   . SER A 58  ? 0.2353 0.2316 0.2061 0.0119  -0.0099 -0.0064 282  SER A N   
431  C  CA  . SER A 58  ? 0.2499 0.2421 0.2131 0.0152  -0.0106 -0.0077 282  SER A CA  
432  C  C   . SER A 58  ? 0.2729 0.2627 0.2323 0.0165  -0.0070 -0.0069 282  SER A C   
433  O  O   . SER A 58  ? 0.2658 0.2513 0.2169 0.0195  -0.0063 -0.0071 282  SER A O   
434  C  CB  . SER A 58  ? 0.2785 0.2711 0.2429 0.0158  -0.0147 -0.0110 282  SER A CB  
435  O  OG  . SER A 58  ? 0.2830 0.2783 0.2514 0.0148  -0.0178 -0.0120 282  SER A OG  
436  N  N   . VAL A 59  ? 0.2668 0.2589 0.2317 0.0147  -0.0047 -0.0059 283  VAL A N   
437  C  CA  . VAL A 59  ? 0.2697 0.2600 0.2320 0.0162  -0.0011 -0.0054 283  VAL A CA  
438  C  C   . VAL A 59  ? 0.2522 0.2401 0.2095 0.0172  0.0027  -0.0030 283  VAL A C   
439  O  O   . VAL A 59  ? 0.2834 0.2722 0.2428 0.0155  0.0035  -0.0011 283  VAL A O   
440  C  CB  . VAL A 59  ? 0.2919 0.2857 0.2621 0.0142  0.0004  -0.0047 283  VAL A CB  
441  C  CG1 . VAL A 59  ? 0.2602 0.2574 0.2361 0.0115  0.0021  -0.0022 283  VAL A CG1 
442  C  CG2 . VAL A 59  ? 0.2462 0.2385 0.2145 0.0163  0.0036  -0.0050 283  VAL A CG2 
443  N  N   . CYS A 60  ? 0.2813 0.2652 0.2311 0.0202  0.0052  -0.0031 284  CYS A N   
444  C  CA  . CYS A 60  ? 0.2711 0.2513 0.2142 0.0218  0.0095  -0.0007 284  CYS A CA  
445  C  C   . CYS A 60  ? 0.2878 0.2642 0.2235 0.0233  0.0075  -0.0002 284  CYS A C   
446  O  O   . CYS A 60  ? 0.2789 0.2519 0.2097 0.0241  0.0111  0.0024  284  CYS A O   
447  C  CB  . CYS A 60  ? 0.2821 0.2652 0.2323 0.0190  0.0140  0.0021  284  CYS A CB  
448  S  SG  . CYS A 60  ? 0.3097 0.2967 0.2674 0.0184  0.0174  0.0019  284  CYS A SG  
449  N  N   . ASN A 61  ? 0.2776 0.2544 0.2129 0.0238  0.0020  -0.0026 285  ASN A N   
450  C  CA  . ASN A 61  ? 0.2606 0.2337 0.1882 0.0263  -0.0006 -0.0026 285  ASN A CA  
451  C  C   . ASN A 61  ? 0.2870 0.2553 0.2040 0.0305  -0.0025 -0.0048 285  ASN A C   
452  O  O   . ASN A 61  ? 0.3002 0.2691 0.2178 0.0311  -0.0034 -0.0074 285  ASN A O   
453  C  CB  . ASN A 61  ? 0.2671 0.2437 0.2007 0.0247  -0.0057 -0.0042 285  ASN A CB  
454  C  CG  . ASN A 61  ? 0.2770 0.2570 0.2184 0.0212  -0.0041 -0.0021 285  ASN A CG  
455  O  OD1 . ASN A 61  ? 0.2916 0.2754 0.2406 0.0183  -0.0023 -0.0016 285  ASN A OD1 
456  N  ND2 . ASN A 61  ? 0.2539 0.2324 0.1934 0.0218  -0.0052 -0.0011 285  ASN A ND2 
457  N  N   . PHE A 62  ? 0.2739 0.2371 0.1810 0.0338  -0.0031 -0.0039 286  PHE A N   
458  C  CA  . PHE A 62  ? 0.3333 0.2914 0.2286 0.0385  -0.0057 -0.0060 286  PHE A CA  
459  C  C   . PHE A 62  ? 0.3206 0.2770 0.2117 0.0407  -0.0110 -0.0067 286  PHE A C   
460  O  O   . PHE A 62  ? 0.3255 0.2817 0.2181 0.0398  -0.0101 -0.0040 286  PHE A O   
461  C  CB  . PHE A 62  ? 0.3351 0.2868 0.2187 0.0415  -0.0001 -0.0034 286  PHE A CB  
462  C  CG  . PHE A 62  ? 0.3032 0.2560 0.1892 0.0406  0.0052  -0.0032 286  PHE A CG  
463  C  CD1 . PHE A 62  ? 0.3885 0.3413 0.2730 0.0421  0.0032  -0.0069 286  PHE A CD1 
464  C  CD2 . PHE A 62  ? 0.2883 0.2418 0.1780 0.0384  0.0120  0.0006  286  PHE A CD2 
465  C  CE1 . PHE A 62  ? 0.3721 0.3259 0.2591 0.0416  0.0081  -0.0068 286  PHE A CE1 
466  C  CE2 . PHE A 62  ? 0.3097 0.2648 0.2026 0.0378  0.0169  0.0007  286  PHE A CE2 
467  C  CZ  . PHE A 62  ? 0.3085 0.2637 0.1998 0.0396  0.0150  -0.0029 286  PHE A CZ  
468  N  N   . LYS A 63  ? 0.2894 0.2440 0.1748 0.0439  -0.0166 -0.0104 287  LYS A N   
469  C  CA  . LYS A 63  ? 0.3511 0.3033 0.2306 0.0472  -0.0216 -0.0109 287  LYS A CA  
470  C  C   . LYS A 63  ? 0.3615 0.3089 0.2291 0.0522  -0.0260 -0.0142 287  LYS A C   
471  O  O   . LYS A 63  ? 0.3742 0.3216 0.2410 0.0525  -0.0265 -0.0172 287  LYS A O   
472  C  CB  . LYS A 63  ? 0.3411 0.2998 0.2325 0.0446  -0.0265 -0.0127 287  LYS A CB  
473  C  CG  . LYS A 63  ? 0.3552 0.3188 0.2545 0.0433  -0.0317 -0.0175 287  LYS A CG  
474  C  CD  . LYS A 63  ? 0.3964 0.3669 0.3092 0.0397  -0.0337 -0.0178 287  LYS A CD  
475  C  CE  . LYS A 63  ? 0.4631 0.4376 0.3821 0.0397  -0.0405 -0.0226 287  LYS A CE  
476  N  NZ  . LYS A 63  ? 0.6459 0.6173 0.5565 0.0447  -0.0462 -0.0245 287  LYS A NZ  
477  N  N   . GLY A 64  ? 0.3815 0.3243 0.2393 0.0565  -0.0291 -0.0136 288  GLY A N   
478  C  CA  . GLY A 64  ? 0.3909 0.3283 0.2354 0.0619  -0.0337 -0.0166 288  GLY A CA  
479  C  C   . GLY A 64  ? 0.4083 0.3391 0.2401 0.0668  -0.0349 -0.0138 288  GLY A C   
480  O  O   . GLY A 64  ? 0.4289 0.3602 0.2642 0.0657  -0.0335 -0.0105 288  GLY A O   
481  N  N   . ASN A 65  ? 0.4177 0.3418 0.2341 0.0724  -0.0375 -0.0154 289  ASN A N   
482  C  CA  . ASN A 65  ? 0.4704 0.3871 0.2723 0.0780  -0.0392 -0.0129 289  ASN A CA  
483  C  C   . ASN A 65  ? 0.5167 0.4255 0.3066 0.0793  -0.0300 -0.0071 289  ASN A C   
484  O  O   . ASN A 65  ? 0.4849 0.3919 0.2711 0.0787  -0.0245 -0.0068 289  ASN A O   
485  C  CB  . ASN A 65  ? 0.5012 0.4142 0.2913 0.0838  -0.0473 -0.0177 289  ASN A CB  
486  C  CG  . ASN A 65  ? 0.4829 0.3887 0.2588 0.0900  -0.0506 -0.0155 289  ASN A CG  
487  O  OD1 . ASN A 65  ? 0.4816 0.3892 0.2632 0.0896  -0.0523 -0.0133 289  ASN A OD1 
488  N  ND2 . ASN A 65  ? 0.4848 0.3819 0.2414 0.0960  -0.0514 -0.0158 289  ASN A ND2 
489  N  N   . LEU A 66  ? 0.4334 0.3375 0.2179 0.0810  -0.0281 -0.0023 290  LEU A N   
490  C  CA  . LEU A 66  ? 0.4550 0.3498 0.2256 0.0832  -0.0200 0.0035  290  LEU A CA  
491  C  C   . LEU A 66  ? 0.5231 0.4091 0.2730 0.0907  -0.0233 0.0023  290  LEU A C   
492  O  O   . LEU A 66  ? 0.5718 0.4527 0.3119 0.0957  -0.0284 0.0031  290  LEU A O   
493  C  CB  . LEU A 66  ? 0.4925 0.3846 0.2648 0.0823  -0.0170 0.0088  290  LEU A CB  
494  C  CG  . LEU A 66  ? 0.5174 0.4014 0.2807 0.0824  -0.0068 0.0154  290  LEU A CG  
495  C  CD1 . LEU A 66  ? 0.5220 0.4060 0.2828 0.0812  -0.0001 0.0152  290  LEU A CD1 
496  C  CD2 . LEU A 66  ? 0.5046 0.3914 0.2809 0.0769  -0.0019 0.0191  290  LEU A CD2 
497  N  N   . GLN A 67  ? 0.5171 0.4014 0.2602 0.0918  -0.0205 0.0004  291  GLN A N   
498  C  CA  . GLN A 67  ? 0.5523 0.4290 0.2760 0.0989  -0.0246 -0.0022 291  GLN A CA  
499  C  C   . GLN A 67  ? 0.6487 0.5135 0.3522 0.1043  -0.0200 0.0037  291  GLN A C   
500  O  O   . GLN A 67  ? 0.6222 0.4808 0.3113 0.1107  -0.0265 0.0030  291  GLN A O   
501  C  CB  . GLN A 67  ? 0.5884 0.4659 0.3104 0.0984  -0.0215 -0.0055 291  GLN A CB  
502  C  CG  . GLN A 67  ? 0.6597 0.5323 0.3666 0.1046  -0.0284 -0.0109 291  GLN A CG  
503  C  CD  . GLN A 67  ? 0.8061 0.6740 0.5024 0.1064  -0.0218 -0.0115 291  GLN A CD  
504  O  OE1 . GLN A 67  ? 0.8168 0.6778 0.5013 0.1083  -0.0127 -0.0061 291  GLN A OE1 
505  N  NE2 . GLN A 67  ? 0.8954 0.7671 0.5961 0.1058  -0.0258 -0.0180 291  GLN A NE2 
506  N  N   . ALA A 68  ? 0.6069 0.4686 0.3097 0.1019  -0.0090 0.0097  292  ALA A N   
507  C  CA  . ALA A 68  ? 0.6038 0.4536 0.2875 0.1065  -0.0027 0.0159  292  ALA A CA  
508  C  C   . ALA A 68  ? 0.6439 0.4939 0.3356 0.1012  0.0091  0.0221  292  ALA A C   
509  O  O   . ALA A 68  ? 0.5784 0.4370 0.2867 0.0951  0.0129  0.0208  292  ALA A O   
510  C  CB  . ALA A 68  ? 0.6103 0.4521 0.2730 0.1128  -0.0016 0.0144  292  ALA A CB  
511  N  N   . GLU A 69  ? 0.6253 0.4658 0.3055 0.1035  0.0147  0.0287  293  GLU A N   
512  C  CA  . GLU A 69  ? 0.5992 0.4367 0.2806 0.1002  0.0275  0.0348  293  GLU A CA  
513  C  C   . GLU A 69  ? 0.6622 0.4951 0.3296 0.1036  0.0334  0.0345  293  GLU A C   
514  O  O   . GLU A 69  ? 0.7067 0.5313 0.3535 0.1108  0.0304  0.0337  293  GLU A O   
515  C  CB  . GLU A 69  ? 0.6297 0.4571 0.3016 0.1019  0.0320  0.0421  293  GLU A CB  
516  C  CG  . GLU A 69  ? 0.7146 0.5449 0.3982 0.0995  0.0265  0.0427  293  GLU A CG  
517  C  CD  . GLU A 69  ? 0.7856 0.6076 0.4667 0.0983  0.0343  0.0505  293  GLU A CD  
518  O  OE1 . GLU A 69  ? 0.7620 0.5755 0.4311 0.0997  0.0439  0.0557  293  GLU A OE1 
519  O  OE2 . GLU A 69  ? 0.8447 0.6687 0.5362 0.0958  0.0311  0.0513  293  GLU A OE2 
520  N  N   . VAL A 70  ? 0.6728 0.5114 0.3512 0.0988  0.0414  0.0346  294  VAL A N   
521  C  CA  . VAL A 70  ? 0.7241 0.5595 0.3910 0.1020  0.0469  0.0335  294  VAL A CA  
522  C  C   . VAL A 70  ? 0.7956 0.6177 0.4406 0.1072  0.0548  0.0400  294  VAL A C   
523  O  O   . VAL A 70  ? 0.7557 0.5745 0.4036 0.1044  0.0631  0.0466  294  VAL A O   
524  C  CB  . VAL A 70  ? 0.7182 0.5626 0.4024 0.0960  0.0543  0.0327  294  VAL A CB  
525  C  CG1 . VAL A 70  ? 0.7148 0.5562 0.3870 0.1000  0.0590  0.0306  294  VAL A CG1 
526  C  CG2 . VAL A 70  ? 0.5713 0.4280 0.2769 0.0907  0.0466  0.0272  294  VAL A CG2 
527  N  N   . PRO A 71  ? 0.8768 0.6905 0.4994 0.1149  0.0524  0.0383  295  PRO A N   
528  C  CA  . PRO A 71  ? 0.9497 0.7497 0.5492 0.1204  0.0602  0.0447  295  PRO A CA  
529  C  C   . PRO A 71  ? 0.9202 0.7197 0.5227 0.1173  0.0753  0.0496  295  PRO A C   
530  O  O   . PRO A 71  ? 0.8829 0.6897 0.4952 0.1146  0.0790  0.0463  295  PRO A O   
531  C  CB  . PRO A 71  ? 0.9397 0.7332 0.5169 0.1288  0.0539  0.0400  295  PRO A CB  
532  C  CG  . PRO A 71  ? 0.9406 0.7424 0.5284 0.1282  0.0395  0.0323  295  PRO A CG  
533  C  CD  . PRO A 71  ? 0.8978 0.7133 0.5143 0.1191  0.0408  0.0305  295  PRO A CD  
534  N  N   . GLY A 72  ? 0.9387 0.7292 0.5333 0.1176  0.0840  0.0576  296  GLY A N   
535  C  CA  . GLY A 72  ? 0.9505 0.7402 0.5492 0.1142  0.0990  0.0632  296  GLY A CA  
536  C  C   . GLY A 72  ? 0.9152 0.7149 0.5413 0.1049  0.1028  0.0649  296  GLY A C   
537  O  O   . GLY A 72  ? 0.9482 0.7439 0.5773 0.1018  0.1125  0.0717  296  GLY A O   
538  N  N   . GLN A 73  ? 0.8880 0.7003 0.5340 0.1003  0.0952  0.0587  297  GLN A N   
539  C  CA  . GLN A 73  ? 0.8635 0.6861 0.5355 0.0917  0.0984  0.0595  297  GLN A CA  
540  C  C   . GLN A 73  ? 0.9336 0.7533 0.6111 0.0888  0.0964  0.0637  297  GLN A C   
541  O  O   . GLN A 73  ? 0.9452 0.7575 0.6097 0.0933  0.0897  0.0645  297  GLN A O   
542  C  CB  . GLN A 73  ? 0.8065 0.6423 0.4964 0.0882  0.0902  0.0520  297  GLN A CB  
543  C  CG  . GLN A 73  ? 0.8516 0.6892 0.5345 0.0920  0.0896  0.0468  297  GLN A CG  
544  C  CD  . GLN A 73  ? 0.8443 0.6851 0.5334 0.0898  0.1017  0.0485  297  GLN A CD  
545  O  OE1 . GLN A 73  ? 0.7747 0.6203 0.4800 0.0837  0.1088  0.0521  297  GLN A OE1 
546  N  NE2 . GLN A 73  ? 0.7295 0.5677 0.4060 0.0947  0.1039  0.0457  297  GLN A NE2 
547  N  N   . HIS A 74  ? 0.9301 0.7559 0.6274 0.0815  0.1022  0.0661  298  HIS A N   
548  C  CA  . HIS A 74  ? 0.9099 0.7337 0.6152 0.0779  0.1011  0.0698  298  HIS A CA  
549  C  C   . HIS A 74  ? 0.8047 0.6404 0.5300 0.0731  0.0915  0.0642  298  HIS A C   
550  O  O   . HIS A 74  ? 0.7676 0.6140 0.5112 0.0677  0.0931  0.0615  298  HIS A O   
551  C  CB  . HIS A 74  ? 0.8657 0.6876 0.5795 0.0727  0.1138  0.0761  298  HIS A CB  
552  C  CG  . HIS A 74  ? 0.9847 0.8042 0.7076 0.0686  0.1131  0.0795  298  HIS A CG  
553  N  ND1 . HIS A 74  ? 0.9480 0.7778 0.6944 0.0614  0.1106  0.0772  298  HIS A ND1 
554  C  CD2 . HIS A 74  ? 0.9979 0.8052 0.7089 0.0710  0.1144  0.0851  298  HIS A CD2 
555  C  CE1 . HIS A 74  ? 1.0066 0.8309 0.7555 0.0593  0.1104  0.0808  298  HIS A CE1 
556  N  NE2 . HIS A 74  ? 1.0697 0.8803 0.7978 0.0650  0.1127  0.0857  298  HIS A NE2 
557  N  N   . GLN A 75  ? 0.7699 0.6036 0.4914 0.0755  0.0815  0.0625  299  GLN A N   
558  C  CA  . GLN A 75  ? 0.6762 0.5199 0.4157 0.0712  0.0727  0.0580  299  GLN A CA  
559  C  C   . GLN A 75  ? 0.6229 0.4786 0.3743 0.0689  0.0691  0.0515  299  GLN A C   
560  O  O   . GLN A 75  ? 0.5431 0.4086 0.3140 0.0629  0.0681  0.0494  299  GLN A O   
561  C  CB  . GLN A 75  ? 0.7026 0.5482 0.4580 0.0646  0.0769  0.0613  299  GLN A CB  
562  C  CG  . GLN A 75  ? 0.6799 0.5213 0.4348 0.0652  0.0706  0.0624  299  GLN A CG  
563  C  CD  . GLN A 75  ? 0.7533 0.5817 0.4971 0.0669  0.0772  0.0696  299  GLN A CD  
564  O  OE1 . GLN A 75  ? 0.9166 0.7365 0.6453 0.0703  0.0843  0.0737  299  GLN A OE1 
565  N  NE2 . GLN A 75  ? 0.7497 0.5761 0.5006 0.0644  0.0752  0.0713  299  GLN A NE2 
566  N  N   . LEU A 76  ? 0.6235 0.4777 0.3624 0.0739  0.0673  0.0486  300  LEU A N   
567  C  CA  . LEU A 76  ? 0.5444 0.4080 0.2914 0.0731  0.0622  0.0420  300  LEU A CA  
568  C  C   . LEU A 76  ? 0.5456 0.4087 0.2851 0.0775  0.0504  0.0372  300  LEU A C   
569  O  O   . LEU A 76  ? 0.6045 0.4583 0.3250 0.0838  0.0481  0.0383  300  LEU A O   
570  C  CB  . LEU A 76  ? 0.6167 0.4789 0.3559 0.0756  0.0690  0.0416  300  LEU A CB  
571  C  CG  . LEU A 76  ? 0.6591 0.5279 0.4128 0.0704  0.0784  0.0429  300  LEU A CG  
572  C  CD1 . LEU A 76  ? 0.6559 0.5248 0.4021 0.0739  0.0818  0.0401  300  LEU A CD1 
573  C  CD2 . LEU A 76  ? 0.5366 0.4172 0.3135 0.0638  0.0742  0.0399  300  LEU A CD2 
574  N  N   . TYR A 77  ? 0.4878 0.3607 0.2421 0.0743  0.0430  0.0320  301  TYR A N   
575  C  CA  . TYR A 77  ? 0.5286 0.4027 0.2797 0.0774  0.0316  0.0273  301  TYR A CA  
576  C  C   . TYR A 77  ? 0.4954 0.3761 0.2511 0.0773  0.0271  0.0209  301  TYR A C   
577  O  O   . TYR A 77  ? 0.4757 0.3644 0.2463 0.0724  0.0297  0.0194  301  TYR A O   
578  C  CB  . TYR A 77  ? 0.4478 0.3267 0.2122 0.0738  0.0264  0.0272  301  TYR A CB  
579  C  CG  . TYR A 77  ? 0.4938 0.3650 0.2531 0.0742  0.0307  0.0334  301  TYR A CG  
580  C  CD1 . TYR A 77  ? 0.4824 0.3445 0.2257 0.0801  0.0268  0.0351  301  TYR A CD1 
581  C  CD2 . TYR A 77  ? 0.4361 0.3086 0.2060 0.0688  0.0386  0.0375  301  TYR A CD2 
582  C  CE1 . TYR A 77  ? 0.5767 0.4307 0.3147 0.0807  0.0309  0.0410  301  TYR A CE1 
583  C  CE2 . TYR A 77  ? 0.5466 0.4113 0.3120 0.0689  0.0427  0.0431  301  TYR A CE2 
584  C  CZ  . TYR A 77  ? 0.5313 0.3864 0.2805 0.0749  0.0390  0.0450  301  TYR A CZ  
585  O  OH  . TYR A 77  ? 0.6470 0.4935 0.3914 0.0752  0.0431  0.0508  301  TYR A OH  
586  N  N   . GLN A 78  ? 0.5114 0.3884 0.2542 0.0829  0.0201  0.0171  302  GLN A N   
587  C  CA  . GLN A 78  ? 0.4711 0.3528 0.2162 0.0835  0.0153  0.0107  302  GLN A CA  
588  C  C   . GLN A 78  ? 0.5290 0.4185 0.2873 0.0811  0.0052  0.0060  302  GLN A C   
589  O  O   . GLN A 78  ? 0.5081 0.3954 0.2613 0.0841  -0.0021 0.0050  302  GLN A O   
590  C  CB  . GLN A 78  ? 0.5135 0.3867 0.2372 0.0909  0.0131  0.0086  302  GLN A CB  
591  C  CG  . GLN A 78  ? 0.5003 0.3772 0.2258 0.0916  0.0087  0.0018  302  GLN A CG  
592  C  CD  . GLN A 78  ? 0.5400 0.4209 0.2739 0.0882  0.0170  0.0020  302  GLN A CD  
593  O  OE1 . GLN A 78  ? 0.5271 0.4026 0.2512 0.0902  0.0260  0.0054  302  GLN A OE1 
594  N  NE2 . GLN A 78  ? 0.4879 0.3782 0.2402 0.0831  0.0144  -0.0013 302  GLN A NE2 
595  N  N   . LEU A 79  ? 0.4266 0.3253 0.2022 0.0758  0.0051  0.0034  303  LEU A N   
596  C  CA  . LEU A 79  ? 0.4623 0.3685 0.2505 0.0734  -0.0036 -0.0014 303  LEU A CA  
597  C  C   . LEU A 79  ? 0.5381 0.4447 0.3225 0.0759  -0.0091 -0.0076 303  LEU A C   
598  O  O   . LEU A 79  ? 0.4857 0.3909 0.2666 0.0765  -0.0046 -0.0086 303  LEU A O   
599  C  CB  . LEU A 79  ? 0.4308 0.3460 0.2390 0.0664  -0.0011 -0.0009 303  LEU A CB  
600  C  CG  . LEU A 79  ? 0.4188 0.3361 0.2358 0.0626  0.0018  0.0036  303  LEU A CG  
601  C  CD1 . LEU A 79  ? 0.4120 0.3383 0.2475 0.0564  0.0032  0.0027  303  LEU A CD1 
602  C  CD2 . LEU A 79  ? 0.4019 0.3185 0.2177 0.0644  -0.0054 0.0029  303  LEU A CD2 
603  N  N   . GLN A 80  ? 0.4950 0.4035 0.2807 0.0773  -0.0187 -0.0120 304  GLN A N   
604  C  CA  . GLN A 80  ? 0.5106 0.4217 0.2988 0.0778  -0.0252 -0.0186 304  GLN A CA  
605  C  C   . GLN A 80  ? 0.4484 0.3695 0.2573 0.0719  -0.0287 -0.0208 304  GLN A C   
606  O  O   . GLN A 80  ? 0.4576 0.3820 0.2726 0.0713  -0.0347 -0.0218 304  GLN A O   
607  C  CB  . GLN A 80  ? 0.5177 0.4236 0.2922 0.0840  -0.0337 -0.0224 304  GLN A CB  
608  C  CG  . GLN A 80  ? 0.7229 0.6193 0.4767 0.0900  -0.0310 -0.0226 304  GLN A CG  
609  C  CD  . GLN A 80  ? 0.7729 0.6699 0.5282 0.0887  -0.0263 -0.0250 304  GLN A CD  
610  O  OE1 . GLN A 80  ? 0.7739 0.6667 0.5216 0.0897  -0.0174 -0.0214 304  GLN A OE1 
611  N  NE2 . GLN A 80  ? 0.6979 0.6000 0.4636 0.0865  -0.0321 -0.0309 304  GLN A NE2 
612  N  N   . LEU A 81  ? 0.4682 0.3936 0.2875 0.0677  -0.0247 -0.0214 305  LEU A N   
613  C  CA  . LEU A 81  ? 0.4093 0.3434 0.2475 0.0618  -0.0262 -0.0223 305  LEU A CA  
614  C  C   . LEU A 81  ? 0.4120 0.3498 0.2565 0.0615  -0.0353 -0.0280 305  LEU A C   
615  O  O   . LEU A 81  ? 0.4210 0.3554 0.2580 0.0649  -0.0398 -0.0326 305  LEU A O   
616  C  CB  . LEU A 81  ? 0.3384 0.2755 0.1847 0.0583  -0.0204 -0.0219 305  LEU A CB  
617  C  CG  . LEU A 81  ? 0.4163 0.3527 0.2625 0.0569  -0.0111 -0.0164 305  LEU A CG  
618  C  CD1 . LEU A 81  ? 0.3683 0.3091 0.2250 0.0534  -0.0071 -0.0168 305  LEU A CD1 
619  C  CD2 . LEU A 81  ? 0.3232 0.2620 0.1753 0.0542  -0.0100 -0.0122 305  LEU A CD2 
620  N  N   . THR A 82  ? 0.4131 0.3577 0.2719 0.0574  -0.0377 -0.0279 306  THR A N   
621  C  CA  . THR A 82  ? 0.4192 0.3694 0.2902 0.0546  -0.0433 -0.0326 306  THR A CA  
622  C  C   . THR A 82  ? 0.3889 0.3442 0.2731 0.0490  -0.0384 -0.0309 306  THR A C   
623  O  O   . THR A 82  ? 0.3625 0.3178 0.2471 0.0475  -0.0316 -0.0265 306  THR A O   
624  C  CB  . THR A 82  ? 0.4097 0.3643 0.2877 0.0542  -0.0497 -0.0340 306  THR A CB  
625  O  OG1 . THR A 82  ? 0.3582 0.3166 0.2439 0.0511  -0.0460 -0.0295 306  THR A OG1 
626  C  CG2 . THR A 82  ? 0.4034 0.3528 0.2679 0.0602  -0.0551 -0.0353 306  THR A CG2 
627  N  N   . ASN A 83  ? 0.4124 0.3719 0.3074 0.0461  -0.0420 -0.0346 307  ASN A N   
628  C  CA  . ASN A 83  ? 0.3725 0.3373 0.2809 0.0408  -0.0384 -0.0328 307  ASN A CA  
629  C  C   . ASN A 83  ? 0.3737 0.3434 0.2901 0.0381  -0.0377 -0.0297 307  ASN A C   
630  O  O   . ASN A 83  ? 0.4028 0.3733 0.3183 0.0396  -0.0417 -0.0303 307  ASN A O   
631  C  CB  . ASN A 83  ? 0.3989 0.3661 0.3164 0.0385  -0.0424 -0.0373 307  ASN A CB  
632  C  CG  . ASN A 83  ? 0.4510 0.4137 0.3632 0.0400  -0.0409 -0.0395 307  ASN A CG  
633  O  OD1 . ASN A 83  ? 0.4550 0.4170 0.3668 0.0393  -0.0349 -0.0367 307  ASN A OD1 
634  N  ND2 . ASN A 83  ? 0.4601 0.4198 0.3683 0.0423  -0.0465 -0.0448 307  ASN A ND2 
635  N  N   . LEU A 84  ? 0.3951 0.3681 0.3191 0.0343  -0.0327 -0.0264 308  LEU A N   
636  C  CA  . LEU A 84  ? 0.3940 0.3710 0.3245 0.0319  -0.0315 -0.0234 308  LEU A CA  
637  C  C   . LEU A 84  ? 0.4071 0.3890 0.3468 0.0303  -0.0366 -0.0258 308  LEU A C   
638  O  O   . LEU A 84  ? 0.3575 0.3418 0.2998 0.0300  -0.0370 -0.0242 308  LEU A O   
639  C  CB  . LEU A 84  ? 0.3715 0.3512 0.3088 0.0282  -0.0259 -0.0201 308  LEU A CB  
640  C  CG  . LEU A 84  ? 0.3397 0.3157 0.2698 0.0295  -0.0201 -0.0170 308  LEU A CG  
641  C  CD1 . LEU A 84  ? 0.2829 0.2623 0.2212 0.0259  -0.0156 -0.0145 308  LEU A CD1 
642  C  CD2 . LEU A 84  ? 0.3492 0.3218 0.2713 0.0318  -0.0186 -0.0143 308  LEU A CD2 
643  N  N   . ASP A 85  ? 0.3852 0.3685 0.3299 0.0294  -0.0405 -0.0298 309  ASP A N   
644  C  CA  . ASP A 85  ? 0.4455 0.4335 0.3993 0.0281  -0.0455 -0.0325 309  ASP A CA  
645  C  C   . ASP A 85  ? 0.4672 0.4537 0.4151 0.0322  -0.0516 -0.0357 309  ASP A C   
646  O  O   . ASP A 85  ? 0.5034 0.4940 0.4593 0.0315  -0.0565 -0.0387 309  ASP A O   
647  C  CB  . ASP A 85  ? 0.3985 0.3889 0.3619 0.0247  -0.0469 -0.0353 309  ASP A CB  
648  C  CG  . ASP A 85  ? 0.4753 0.4610 0.4329 0.0270  -0.0498 -0.0394 309  ASP A CG  
649  O  OD1 . ASP A 85  ? 0.4669 0.4479 0.4127 0.0314  -0.0517 -0.0406 309  ASP A OD1 
650  O  OD2 . ASP A 85  ? 0.5086 0.4949 0.4731 0.0244  -0.0503 -0.0414 309  ASP A OD2 
651  N  N   . GLY A 86  ? 0.4612 0.4417 0.3953 0.0367  -0.0514 -0.0349 310  GLY A N   
652  C  CA  . GLY A 86  ? 0.4624 0.4405 0.3889 0.0414  -0.0574 -0.0376 310  GLY A CA  
653  C  C   . GLY A 86  ? 0.4448 0.4195 0.3659 0.0438  -0.0623 -0.0426 310  GLY A C   
654  O  O   . GLY A 86  ? 0.4319 0.4023 0.3419 0.0488  -0.0665 -0.0444 310  GLY A O   
655  N  N   . SER A 87  ? 0.4546 0.4304 0.3825 0.0407  -0.0620 -0.0450 311  SER A N   
656  C  CA  . SER A 87  ? 0.4661 0.4384 0.3897 0.0427  -0.0668 -0.0504 311  SER A CA  
657  C  C   . SER A 87  ? 0.4874 0.4517 0.3939 0.0474  -0.0643 -0.0497 311  SER A C   
658  O  O   . SER A 87  ? 0.4788 0.4410 0.3798 0.0476  -0.0575 -0.0449 311  SER A O   
659  C  CB  . SER A 87  ? 0.5156 0.4903 0.4507 0.0381  -0.0661 -0.0525 311  SER A CB  
660  O  OG  . SER A 87  ? 0.4692 0.4413 0.4019 0.0369  -0.0592 -0.0494 311  SER A OG  
661  N  N   . PRO A 88  ? 0.4978 0.4576 0.3956 0.0512  -0.0697 -0.0546 312  PRO A N   
662  C  CA  . PRO A 88  ? 0.4886 0.4403 0.3689 0.0560  -0.0671 -0.0542 312  PRO A CA  
663  C  C   . PRO A 88  ? 0.4931 0.4427 0.3737 0.0542  -0.0606 -0.0531 312  PRO A C   
664  O  O   . PRO A 88  ? 0.4890 0.4418 0.3815 0.0501  -0.0605 -0.0549 312  PRO A O   
665  C  CB  . PRO A 88  ? 0.5492 0.4972 0.4218 0.0602  -0.0757 -0.0608 312  PRO A CB  
666  C  CG  . PRO A 88  ? 0.5585 0.5132 0.4476 0.0564  -0.0822 -0.0650 312  PRO A CG  
667  C  CD  . PRO A 88  ? 0.5502 0.5121 0.4523 0.0521  -0.0789 -0.0605 312  PRO A CD  
668  N  N   . ILE A 89  ? 0.5116 0.4559 0.3792 0.0574  -0.0547 -0.0500 313  ILE A N   
669  C  CA  . ILE A 89  ? 0.5289 0.4707 0.3948 0.0568  -0.0483 -0.0491 313  ILE A CA  
670  C  C   . ILE A 89  ? 0.5331 0.4705 0.3944 0.0591  -0.0526 -0.0554 313  ILE A C   
671  O  O   . ILE A 89  ? 0.5185 0.4505 0.3665 0.0641  -0.0570 -0.0588 313  ILE A O   
672  C  CB  . ILE A 89  ? 0.4490 0.3861 0.3019 0.0601  -0.0410 -0.0443 313  ILE A CB  
673  C  CG1 . ILE A 89  ? 0.4889 0.4302 0.3483 0.0570  -0.0360 -0.0381 313  ILE A CG1 
674  C  CG2 . ILE A 89  ? 0.5350 0.4690 0.3846 0.0608  -0.0352 -0.0446 313  ILE A CG2 
675  C  CD1 . ILE A 89  ? 0.4750 0.4230 0.3510 0.0512  -0.0333 -0.0366 313  ILE A CD1 
676  N  N   . ASP A 90  ? 0.5769 0.5162 0.4486 0.0556  -0.0516 -0.0572 314  ASP A N   
677  C  CA  . ASP A 90  ? 0.5606 0.4951 0.4285 0.0575  -0.0549 -0.0633 314  ASP A CA  
678  C  C   . ASP A 90  ? 0.5462 0.4774 0.4102 0.0585  -0.0475 -0.0617 314  ASP A C   
679  O  O   . ASP A 90  ? 0.5613 0.4958 0.4371 0.0545  -0.0441 -0.0602 314  ASP A O   
680  C  CB  . ASP A 90  ? 0.6125 0.5510 0.4960 0.0530  -0.0605 -0.0673 314  ASP A CB  
681  C  CG  . ASP A 90  ? 0.6196 0.5525 0.4998 0.0547  -0.0648 -0.0742 314  ASP A CG  
682  O  OD1 . ASP A 90  ? 0.6109 0.5372 0.4770 0.0595  -0.0628 -0.0757 314  ASP A OD1 
683  O  OD2 . ASP A 90  ? 0.6988 0.6339 0.5907 0.0513  -0.0700 -0.0781 314  ASP A OD2 
684  N  N   . PRO A 91  ? 0.5620 0.4867 0.4096 0.0639  -0.0446 -0.0621 315  PRO A N   
685  C  CA  . PRO A 91  ? 0.5665 0.4887 0.4111 0.0650  -0.0368 -0.0605 315  PRO A CA  
686  C  C   . PRO A 91  ? 0.5655 0.4860 0.4162 0.0641  -0.0382 -0.0652 315  PRO A C   
687  O  O   . PRO A 91  ? 0.5718 0.4912 0.4227 0.0647  -0.0317 -0.0638 315  PRO A O   
688  C  CB  . PRO A 91  ? 0.5544 0.4694 0.3787 0.0716  -0.0343 -0.0606 315  PRO A CB  
689  C  CG  . PRO A 91  ? 0.6018 0.5141 0.4178 0.0743  -0.0430 -0.0642 315  PRO A CG  
690  C  CD  . PRO A 91  ? 0.6127 0.5324 0.4437 0.0693  -0.0476 -0.0630 315  PRO A CD  
691  N  N   . THR A 92  ? 0.5624 0.4826 0.4187 0.0626  -0.0462 -0.0707 316  THR A N   
692  C  CA  . THR A 92  ? 0.6055 0.5236 0.4687 0.0612  -0.0475 -0.0750 316  THR A CA  
693  C  C   . THR A 92  ? 0.5930 0.5173 0.4750 0.0549  -0.0462 -0.0722 316  THR A C   
694  O  O   . THR A 92  ? 0.5563 0.4788 0.4453 0.0533  -0.0467 -0.0749 316  THR A O   
695  C  CB  . THR A 92  ? 0.5681 0.4819 0.4279 0.0628  -0.0567 -0.0828 316  THR A CB  
696  O  OG1 . THR A 92  ? 0.6343 0.5534 0.5046 0.0590  -0.0631 -0.0835 316  THR A OG1 
697  C  CG2 . THR A 92  ? 0.5501 0.4569 0.3895 0.0697  -0.0584 -0.0858 316  THR A CG2 
698  N  N   . ASP A 93  ? 0.5233 0.4543 0.4130 0.0514  -0.0445 -0.0669 317  ASP A N   
699  C  CA  . ASP A 93  ? 0.4969 0.4335 0.4026 0.0459  -0.0424 -0.0636 317  ASP A CA  
700  C  C   . ASP A 93  ? 0.4865 0.4220 0.3940 0.0462  -0.0358 -0.0613 317  ASP A C   
701  O  O   . ASP A 93  ? 0.4873 0.4202 0.3851 0.0499  -0.0307 -0.0599 317  ASP A O   
702  C  CB  . ASP A 93  ? 0.5044 0.4476 0.4151 0.0432  -0.0406 -0.0580 317  ASP A CB  
703  C  CG  . ASP A 93  ? 0.5891 0.5350 0.5029 0.0418  -0.0473 -0.0600 317  ASP A CG  
704  O  OD1 . ASP A 93  ? 0.6188 0.5619 0.5311 0.0429  -0.0537 -0.0657 317  ASP A OD1 
705  O  OD2 . ASP A 93  ? 0.5903 0.5414 0.5086 0.0398  -0.0463 -0.0559 317  ASP A OD2 
706  N  N   . ASP A 94  ? 0.4495 0.3870 0.3697 0.0422  -0.0356 -0.0607 318  ASP A N   
707  C  CA  . ASP A 94  ? 0.4972 0.4339 0.4207 0.0425  -0.0300 -0.0587 318  ASP A CA  
708  C  C   . ASP A 94  ? 0.4539 0.3968 0.3827 0.0405  -0.0243 -0.0520 318  ASP A C   
709  O  O   . ASP A 94  ? 0.4232 0.3686 0.3619 0.0378  -0.0222 -0.0494 318  ASP A O   
710  C  CB  . ASP A 94  ? 0.5122 0.4471 0.4460 0.0397  -0.0327 -0.0612 318  ASP A CB  
711  C  CG  . ASP A 94  ? 0.6261 0.5549 0.5562 0.0411  -0.0389 -0.0683 318  ASP A CG  
712  O  OD1 . ASP A 94  ? 0.6011 0.5250 0.5186 0.0459  -0.0394 -0.0719 318  ASP A OD1 
713  O  OD2 . ASP A 94  ? 0.8479 0.7767 0.7877 0.0373  -0.0431 -0.0703 318  ASP A OD2 
714  N  N   . THR A 95  ? 0.4623 0.4072 0.3843 0.0419  -0.0221 -0.0493 319  THR A N   
715  C  CA  . THR A 95  ? 0.4030 0.3531 0.3287 0.0405  -0.0166 -0.0434 319  THR A CA  
716  C  C   . THR A 95  ? 0.3900 0.3378 0.3050 0.0447  -0.0111 -0.0421 319  THR A C   
717  O  O   . THR A 95  ? 0.4159 0.3583 0.3189 0.0488  -0.0122 -0.0454 319  THR A O   
718  C  CB  . THR A 95  ? 0.4514 0.4061 0.3803 0.0375  -0.0187 -0.0407 319  THR A CB  
719  O  OG1 . THR A 95  ? 0.4285 0.3805 0.3467 0.0403  -0.0215 -0.0426 319  THR A OG1 
720  C  CG2 . THR A 95  ? 0.4022 0.3594 0.3420 0.0332  -0.0234 -0.0417 319  THR A CG2 
721  N  N   . PRO A 96  ? 0.3759 0.3275 0.2947 0.0441  -0.0050 -0.0376 320  PRO A N   
722  C  CA  . PRO A 96  ? 0.3826 0.3323 0.2919 0.0478  0.0009  -0.0360 320  PRO A CA  
723  C  C   . PRO A 96  ? 0.3764 0.3250 0.2763 0.0488  0.0005  -0.0346 320  PRO A C   
724  O  O   . PRO A 96  ? 0.3852 0.3295 0.2730 0.0529  0.0037  -0.0347 320  PRO A O   
725  C  CB  . PRO A 96  ? 0.3623 0.3177 0.2812 0.0458  0.0067  -0.0315 320  PRO A CB  
726  C  CG  . PRO A 96  ? 0.3503 0.3093 0.2821 0.0418  0.0035  -0.0312 320  PRO A CG  
727  C  CD  . PRO A 96  ? 0.3692 0.3268 0.3009 0.0400  -0.0034 -0.0338 320  PRO A CD  
728  N  N   . GLY A 97  ? 0.3858 0.3377 0.2906 0.0455  -0.0033 -0.0331 321  GLY A N   
729  C  CA  . GLY A 97  ? 0.3911 0.3422 0.2885 0.0463  -0.0043 -0.0315 321  GLY A CA  
730  C  C   . GLY A 97  ? 0.3916 0.3465 0.2969 0.0427  -0.0100 -0.0315 321  GLY A C   
731  O  O   . GLY A 97  ? 0.3372 0.2949 0.2529 0.0395  -0.0126 -0.0327 321  GLY A O   
732  N  N   . PRO A 98  ? 0.3742 0.3290 0.2748 0.0431  -0.0117 -0.0301 322  PRO A N   
733  C  CA  . PRO A 98  ? 0.3545 0.3133 0.2629 0.0399  -0.0169 -0.0303 322  PRO A CA  
734  C  C   . PRO A 98  ? 0.2920 0.2569 0.2132 0.0352  -0.0143 -0.0268 322  PRO A C   
735  O  O   . PRO A 98  ? 0.3119 0.2782 0.2347 0.0346  -0.0088 -0.0233 322  PRO A O   
736  C  CB  . PRO A 98  ? 0.3846 0.3414 0.2840 0.0421  -0.0180 -0.0289 322  PRO A CB  
737  C  CG  . PRO A 98  ? 0.3569 0.3099 0.2464 0.0451  -0.0116 -0.0260 322  PRO A CG  
738  C  CD  . PRO A 98  ? 0.3339 0.2846 0.2217 0.0467  -0.0087 -0.0280 322  PRO A CD  
739  N  N   . LEU A 99  ? 0.3063 0.2748 0.2369 0.0319  -0.0185 -0.0279 323  LEU A N   
740  C  CA  . LEU A 99  ? 0.3307 0.3044 0.2723 0.0278  -0.0164 -0.0248 323  LEU A CA  
741  C  C   . LEU A 99  ? 0.3219 0.2977 0.2628 0.0271  -0.0132 -0.0206 323  LEU A C   
742  O  O   . LEU A 99  ? 0.3068 0.2811 0.2414 0.0288  -0.0143 -0.0203 323  LEU A O   
743  C  CB  . LEU A 99  ? 0.3188 0.2957 0.2696 0.0246  -0.0210 -0.0264 323  LEU A CB  
744  C  CG  . LEU A 99  ? 0.3343 0.3090 0.2875 0.0245  -0.0245 -0.0306 323  LEU A CG  
745  C  CD1 . LEU A 99  ? 0.3534 0.3318 0.3173 0.0206  -0.0276 -0.0311 323  LEU A CD1 
746  C  CD2 . LEU A 99  ? 0.3309 0.3034 0.2845 0.0252  -0.0211 -0.0305 323  LEU A CD2 
747  N  N   . GLY A 100 ? 0.3009 0.2801 0.2485 0.0247  -0.0093 -0.0176 324  GLY A N   
748  C  CA  . GLY A 100 ? 0.2902 0.2714 0.2386 0.0235  -0.0061 -0.0138 324  GLY A CA  
749  C  C   . GLY A 100 ? 0.3032 0.2814 0.2442 0.0260  -0.0012 -0.0119 324  GLY A C   
750  O  O   . GLY A 100 ? 0.3065 0.2860 0.2486 0.0248  0.0019  -0.0088 324  GLY A O   
751  N  N   . CYS A 101 ? 0.3226 0.2967 0.2561 0.0293  -0.0001 -0.0138 325  CYS A N   
752  C  CA  . CYS A 101 ? 0.2807 0.2517 0.2066 0.0319  0.0054  -0.0118 325  CYS A CA  
753  C  C   . CYS A 101 ? 0.3097 0.2846 0.2435 0.0298  0.0108  -0.0089 325  CYS A C   
754  O  O   . CYS A 101 ? 0.3020 0.2802 0.2442 0.0282  0.0104  -0.0097 325  CYS A O   
755  C  CB  . CYS A 101 ? 0.3442 0.3100 0.2604 0.0361  0.0054  -0.0148 325  CYS A CB  
756  S  SG  . CYS A 101 ? 0.3582 0.3192 0.2630 0.0399  0.0127  -0.0126 325  CYS A SG  
757  N  N   . PRO A 102 ? 0.3297 0.3041 0.2616 0.0298  0.0158  -0.0056 326  PRO A N   
758  C  CA  . PRO A 102 ? 0.2945 0.2731 0.2350 0.0279  0.0209  -0.0032 326  PRO A CA  
759  C  C   . PRO A 102 ? 0.2783 0.2570 0.2198 0.0299  0.0234  -0.0049 326  PRO A C   
760  O  O   . PRO A 102 ? 0.2864 0.2604 0.2185 0.0336  0.0243  -0.0068 326  PRO A O   
761  C  CB  . PRO A 102 ? 0.3184 0.2945 0.2539 0.0284  0.0263  0.0001  326  PRO A CB  
762  C  CG  . PRO A 102 ? 0.3371 0.3090 0.2640 0.0294  0.0229  0.0002  326  PRO A CG  
763  C  CD  . PRO A 102 ? 0.2937 0.2637 0.2160 0.0314  0.0169  -0.0038 326  PRO A CD  
764  N  N   . ASP A 103 ? 0.2784 0.2624 0.2312 0.0278  0.0243  -0.0044 327  ASP A N   
765  C  CA  . ASP A 103 ? 0.2625 0.2471 0.2177 0.0299  0.0267  -0.0059 327  ASP A CA  
766  C  C   . ASP A 103 ? 0.2875 0.2756 0.2486 0.0297  0.0333  -0.0035 327  ASP A C   
767  O  O   . ASP A 103 ? 0.2861 0.2773 0.2543 0.0303  0.0349  -0.0041 327  ASP A O   
768  C  CB  . ASP A 103 ? 0.2590 0.2464 0.2224 0.0284  0.0222  -0.0077 327  ASP A CB  
769  C  CG  . ASP A 103 ? 0.2793 0.2727 0.2538 0.0246  0.0211  -0.0054 327  ASP A CG  
770  O  OD1 . ASP A 103 ? 0.2805 0.2757 0.2565 0.0228  0.0233  -0.0029 327  ASP A OD1 
771  O  OD2 . ASP A 103 ? 0.2895 0.2852 0.2708 0.0234  0.0179  -0.0061 327  ASP A OD2 
772  N  N   . PHE A 104 ? 0.2865 0.2743 0.2456 0.0288  0.0372  -0.0006 328  PHE A N   
773  C  CA  . PHE A 104 ? 0.3071 0.2982 0.2725 0.0281  0.0440  0.0018  328  PHE A CA  
774  C  C   . PHE A 104 ? 0.2951 0.2808 0.2496 0.0304  0.0497  0.0036  328  PHE A C   
775  O  O   . PHE A 104 ? 0.3190 0.2989 0.2620 0.0318  0.0477  0.0035  328  PHE A O   
776  C  CB  . PHE A 104 ? 0.2883 0.2851 0.2653 0.0236  0.0432  0.0041  328  PHE A CB  
777  C  CG  . PHE A 104 ? 0.2840 0.2783 0.2566 0.0216  0.0401  0.0052  328  PHE A CG  
778  C  CD1 . PHE A 104 ? 0.2863 0.2810 0.2595 0.0202  0.0333  0.0038  328  PHE A CD1 
779  C  CD2 . PHE A 104 ? 0.2926 0.2837 0.2605 0.0212  0.0444  0.0079  328  PHE A CD2 
780  C  CE1 . PHE A 104 ? 0.2823 0.2749 0.2519 0.0186  0.0307  0.0047  328  PHE A CE1 
781  C  CE2 . PHE A 104 ? 0.3108 0.2992 0.2747 0.0197  0.0414  0.0089  328  PHE A CE2 
782  C  CZ  . PHE A 104 ? 0.2977 0.2871 0.2626 0.0185  0.0346  0.0072  328  PHE A CZ  
783  N  N   . THR A 105 ? 0.3109 0.2985 0.2690 0.0310  0.0571  0.0054  329  THR A N   
784  C  CA  . THR A 105 ? 0.3356 0.3180 0.2839 0.0328  0.0637  0.0079  329  THR A CA  
785  C  C   . THR A 105 ? 0.3382 0.3233 0.2943 0.0287  0.0668  0.0116  329  THR A C   
786  O  O   . THR A 105 ? 0.3405 0.3328 0.3113 0.0255  0.0678  0.0122  329  THR A O   
787  C  CB  . THR A 105 ? 0.3810 0.3627 0.3266 0.0364  0.0710  0.0076  329  THR A CB  
788  O  OG1 . THR A 105 ? 0.4508 0.4405 0.4123 0.0343  0.0748  0.0084  329  THR A OG1 
789  C  CG2 . THR A 105 ? 0.3738 0.3524 0.3118 0.0405  0.0677  0.0035  329  THR A CG2 
790  N  N   . GLY A 106 ? 0.3415 0.3206 0.2878 0.0288  0.0680  0.0139  330  GLY A N   
791  C  CA  . GLY A 106 ? 0.3821 0.3622 0.3346 0.0250  0.0713  0.0175  330  GLY A CA  
792  C  C   . GLY A 106 ? 0.3521 0.3241 0.2915 0.0260  0.0705  0.0195  330  GLY A C   
793  O  O   . GLY A 106 ? 0.2961 0.2624 0.2219 0.0297  0.0671  0.0180  330  GLY A O   
794  N  N   . LEU A 107 ? 0.3413 0.3129 0.2852 0.0227  0.0732  0.0227  331  LEU A N   
795  C  CA  . LEU A 107 ? 0.3234 0.2872 0.2562 0.0233  0.0724  0.0250  331  LEU A CA  
796  C  C   . LEU A 107 ? 0.3471 0.3132 0.2849 0.0207  0.0641  0.0233  331  LEU A C   
797  O  O   . LEU A 107 ? 0.3367 0.3061 0.2851 0.0164  0.0638  0.0243  331  LEU A O   
798  C  CB  . LEU A 107 ? 0.3511 0.3118 0.2852 0.0214  0.0805  0.0296  331  LEU A CB  
799  C  CG  . LEU A 107 ? 0.5065 0.4571 0.4261 0.0233  0.0818  0.0328  331  LEU A CG  
800  C  CD1 . LEU A 107 ? 0.4705 0.4141 0.3715 0.0295  0.0815  0.0320  331  LEU A CD1 
801  C  CD2 . LEU A 107 ? 0.5348 0.4826 0.4575 0.0210  0.0911  0.0375  331  LEU A CD2 
802  N  N   . LEU A 108 ? 0.3243 0.2886 0.2544 0.0232  0.0573  0.0205  332  LEU A N   
803  C  CA  . LEU A 108 ? 0.3121 0.2787 0.2462 0.0213  0.0497  0.0187  332  LEU A CA  
804  C  C   . LEU A 108 ? 0.3307 0.2915 0.2589 0.0210  0.0492  0.0212  332  LEU A C   
805  O  O   . LEU A 108 ? 0.3132 0.2666 0.2280 0.0246  0.0502  0.0225  332  LEU A O   
806  C  CB  . LEU A 108 ? 0.3152 0.2817 0.2436 0.0241  0.0433  0.0150  332  LEU A CB  
807  C  CG  . LEU A 108 ? 0.2690 0.2377 0.2004 0.0228  0.0354  0.0128  332  LEU A CG  
808  C  CD1 . LEU A 108 ? 0.2518 0.2278 0.1977 0.0184  0.0337  0.0122  332  LEU A CD1 
809  C  CD2 . LEU A 108 ? 0.2834 0.2514 0.2090 0.0257  0.0306  0.0092  332  LEU A CD2 
810  N  N   . TYR A 109 ? 0.3013 0.2651 0.2392 0.0170  0.0475  0.0217  333  TYR A N   
811  C  CA  . TYR A 109 ? 0.3204 0.2788 0.2546 0.0163  0.0475  0.0240  333  TYR A CA  
812  C  C   . TYR A 109 ? 0.3339 0.2934 0.2683 0.0161  0.0397  0.0217  333  TYR A C   
813  O  O   . TYR A 109 ? 0.2921 0.2582 0.2354 0.0140  0.0356  0.0190  333  TYR A O   
814  C  CB  . TYR A 109 ? 0.3447 0.3050 0.2898 0.0118  0.0520  0.0264  333  TYR A CB  
815  C  CG  . TYR A 109 ? 0.3063 0.2621 0.2510 0.0101  0.0509  0.0280  333  TYR A CG  
816  C  CD1 . TYR A 109 ? 0.3260 0.2729 0.2611 0.0117  0.0551  0.0317  333  TYR A CD1 
817  C  CD2 . TYR A 109 ? 0.3105 0.2706 0.2640 0.0070  0.0458  0.0260  333  TYR A CD2 
818  C  CE1 . TYR A 109 ? 0.3564 0.2987 0.2915 0.0103  0.0540  0.0332  333  TYR A CE1 
819  C  CE2 . TYR A 109 ? 0.2982 0.2540 0.2514 0.0057  0.0448  0.0271  333  TYR A CE2 
820  C  CZ  . TYR A 109 ? 0.3544 0.3014 0.2989 0.0073  0.0488  0.0307  333  TYR A CZ  
821  O  OH  . TYR A 109 ? 0.4183 0.3604 0.3627 0.0061  0.0478  0.0318  333  TYR A OH  
822  N  N   . GLY A 110 ? 0.3399 0.2929 0.2646 0.0186  0.0380  0.0228  334  GLY A N   
823  C  CA  . GLY A 110 ? 0.3012 0.2552 0.2261 0.0188  0.0311  0.0206  334  GLY A CA  
824  C  C   . GLY A 110 ? 0.3097 0.2558 0.2241 0.0218  0.0299  0.0224  334  GLY A C   
825  O  O   . GLY A 110 ? 0.3251 0.2648 0.2342 0.0224  0.0349  0.0260  334  GLY A O   
826  N  N   . VAL A 111 ? 0.3317 0.2783 0.2433 0.0239  0.0235  0.0200  335  VAL A N   
827  C  CA  . VAL A 111 ? 0.3288 0.2687 0.2314 0.0271  0.0213  0.0213  335  VAL A CA  
828  C  C   . VAL A 111 ? 0.2980 0.2368 0.1916 0.0318  0.0162  0.0189  335  VAL A C   
829  O  O   . VAL A 111 ? 0.3115 0.2564 0.2103 0.0314  0.0113  0.0152  335  VAL A O   
830  C  CB  . VAL A 111 ? 0.3498 0.2917 0.2597 0.0250  0.0179  0.0205  335  VAL A CB  
831  C  CG1 . VAL A 111 ? 0.3163 0.2522 0.2174 0.0291  0.0145  0.0211  335  VAL A CG1 
832  C  CG2 . VAL A 111 ? 0.3108 0.2521 0.2282 0.0206  0.0228  0.0228  335  VAL A CG2 
833  N  N   . ALA A 112 ? 0.3352 0.2660 0.2153 0.0363  0.0173  0.0210  336  ALA A N   
834  C  CA  . ALA A 112 ? 0.3523 0.2810 0.2226 0.0413  0.0117  0.0187  336  ALA A CA  
835  C  C   . ALA A 112 ? 0.3581 0.2841 0.2263 0.0434  0.0069  0.0188  336  ALA A C   
836  O  O   . ALA A 112 ? 0.3452 0.2649 0.2094 0.0439  0.0098  0.0224  336  ALA A O   
837  C  CB  . ALA A 112 ? 0.3334 0.2544 0.1887 0.0456  0.0151  0.0207  336  ALA A CB  
838  N  N   . SER A 113 ? 0.3082 0.2391 0.1797 0.0446  -0.0002 0.0148  337  SER A N   
839  C  CA  . SER A 113 ? 0.3287 0.2585 0.2000 0.0468  -0.0052 0.0143  337  SER A CA  
840  C  C   . SER A 113 ? 0.3485 0.2776 0.2123 0.0519  -0.0120 0.0113  337  SER A C   
841  O  O   . SER A 113 ? 0.3506 0.2827 0.2137 0.0523  -0.0139 0.0083  337  SER A O   
842  C  CB  . SER A 113 ? 0.2999 0.2376 0.1857 0.0427  -0.0074 0.0121  337  SER A CB  
843  O  OG  . SER A 113 ? 0.3178 0.2635 0.2114 0.0406  -0.0102 0.0082  337  SER A OG  
844  N  N   . GLN A 114 ? 0.3720 0.2970 0.2302 0.0559  -0.0158 0.0119  338  GLN A N   
845  C  CA  . GLN A 114 ? 0.3767 0.3015 0.2288 0.0610  -0.0232 0.0089  338  GLN A CA  
846  C  C   . GLN A 114 ? 0.3823 0.3105 0.2415 0.0620  -0.0287 0.0072  338  GLN A C   
847  O  O   . GLN A 114 ? 0.3520 0.2791 0.2155 0.0604  -0.0263 0.0095  338  GLN A O   
848  C  CB  . GLN A 114 ? 0.3625 0.2767 0.1964 0.0671  -0.0230 0.0115  338  GLN A CB  
849  C  CG  . GLN A 114 ? 0.4088 0.3181 0.2333 0.0671  -0.0169 0.0137  338  GLN A CG  
850  C  CD  . GLN A 114 ? 0.4778 0.3764 0.2829 0.0737  -0.0172 0.0163  338  GLN A CD  
851  O  OE1 . GLN A 114 ? 0.4498 0.3414 0.2482 0.0765  -0.0166 0.0199  338  GLN A OE1 
852  N  NE2 . GLN A 114 ? 0.4095 0.3063 0.2050 0.0767  -0.0183 0.0143  338  GLN A NE2 
853  N  N   . ARG A 115 ? 0.3603 0.2929 0.2212 0.0647  -0.0361 0.0028  339  ARG A N   
854  C  CA  . ARG A 115 ? 0.3891 0.3244 0.2547 0.0673  -0.0421 0.0011  339  ARG A CA  
855  C  C   . ARG A 115 ? 0.4174 0.3497 0.2728 0.0737  -0.0491 -0.0011 339  ARG A C   
856  O  O   . ARG A 115 ? 0.3698 0.3052 0.2249 0.0740  -0.0525 -0.0048 339  ARG A O   
857  C  CB  . ARG A 115 ? 0.4070 0.3534 0.2898 0.0630  -0.0443 -0.0028 339  ARG A CB  
858  C  CG  . ARG A 115 ? 0.3779 0.3281 0.2670 0.0658  -0.0503 -0.0050 339  ARG A CG  
859  C  CD  . ARG A 115 ? 0.4219 0.3828 0.3282 0.0612  -0.0508 -0.0081 339  ARG A CD  
860  N  NE  . ARG A 115 ? 0.4264 0.3873 0.3382 0.0576  -0.0453 -0.0055 339  ARG A NE  
861  C  CZ  . ARG A 115 ? 0.3606 0.3237 0.2775 0.0522  -0.0399 -0.0045 339  ARG A CZ  
862  N  NH1 . ARG A 115 ? 0.3568 0.3226 0.2748 0.0494  -0.0388 -0.0057 339  ARG A NH1 
863  N  NH2 . ARG A 115 ? 0.3218 0.2841 0.2427 0.0496  -0.0358 -0.0025 339  ARG A NH2 
864  N  N   . GLY A 116 ? 0.4150 0.3409 0.2621 0.0790  -0.0517 0.0010  340  GLY A N   
865  C  CA  . GLY A 116 ? 0.4274 0.3489 0.2624 0.0858  -0.0584 -0.0005 340  GLY A CA  
866  C  C   . GLY A 116 ? 0.5013 0.4100 0.3186 0.0907  -0.0554 0.0050  340  GLY A C   
867  O  O   . GLY A 116 ? 0.4795 0.3825 0.2924 0.0881  -0.0472 0.0096  340  GLY A O   
868  N  N   . PRO A 117 ? 0.5397 0.4434 0.3468 0.0978  -0.0621 0.0047  341  PRO A N   
869  C  CA  . PRO A 117 ? 0.5731 0.4837 0.3864 0.1014  -0.0723 -0.0007 341  PRO A CA  
870  C  C   . PRO A 117 ? 0.5413 0.4597 0.3717 0.0990  -0.0736 -0.0019 341  PRO A C   
871  O  O   . PRO A 117 ? 0.5632 0.4780 0.3951 0.0974  -0.0683 0.0021  341  PRO A O   
872  C  CB  . PRO A 117 ? 0.5794 0.4797 0.3741 0.1101  -0.0772 0.0012  341  PRO A CB  
873  C  CG  . PRO A 117 ? 0.5515 0.4400 0.3344 0.1106  -0.0689 0.0085  341  PRO A CG  
874  C  CD  . PRO A 117 ? 0.5577 0.4480 0.3454 0.1033  -0.0597 0.0101  341  PRO A CD  
875  N  N   . GLY A 118 ? 0.5494 0.4785 0.3932 0.0985  -0.0803 -0.0076 342  GLY A N   
876  C  CA  . GLY A 118 ? 0.4827 0.4201 0.3435 0.0959  -0.0807 -0.0090 342  GLY A CA  
877  C  C   . GLY A 118 ? 0.4543 0.3950 0.3247 0.0882  -0.0722 -0.0073 342  GLY A C   
878  O  O   . GLY A 118 ? 0.4526 0.3951 0.3238 0.0837  -0.0686 -0.0078 342  GLY A O   
879  N  N   . ASP A 119 ? 0.4764 0.4174 0.3536 0.0869  -0.0692 -0.0053 343  ASP A N   
880  C  CA  . ASP A 119 ? 0.4414 0.3849 0.3269 0.0800  -0.0616 -0.0037 343  ASP A CA  
881  C  C   . ASP A 119 ? 0.4372 0.3699 0.3123 0.0794  -0.0545 0.0021  343  ASP A C   
882  O  O   . ASP A 119 ? 0.4523 0.3858 0.3341 0.0746  -0.0488 0.0037  343  ASP A O   
883  C  CB  . ASP A 119 ? 0.4681 0.4196 0.3690 0.0783  -0.0625 -0.0059 343  ASP A CB  
884  C  CG  . ASP A 119 ? 0.5013 0.4477 0.3993 0.0834  -0.0643 -0.0041 343  ASP A CG  
885  O  OD1 . ASP A 119 ? 0.5479 0.4864 0.4334 0.0895  -0.0677 -0.0023 343  ASP A OD1 
886  O  OD2 . ASP A 119 ? 0.5401 0.4900 0.4480 0.0816  -0.0623 -0.0045 343  ASP A OD2 
887  N  N   . ALA A 120 ? 0.4305 0.3530 0.2895 0.0843  -0.0548 0.0052  344  ALA A N   
888  C  CA  . ALA A 120 ? 0.4664 0.3785 0.3153 0.0832  -0.0473 0.0108  344  ALA A CA  
889  C  C   . ALA A 120 ? 0.4307 0.3456 0.2827 0.0769  -0.0412 0.0111  344  ALA A C   
890  O  O   . ALA A 120 ? 0.3829 0.3016 0.2338 0.0765  -0.0430 0.0085  344  ALA A O   
891  C  CB  . ALA A 120 ? 0.4723 0.3733 0.3023 0.0898  -0.0489 0.0139  344  ALA A CB  
892  N  N   . THR A 121 ? 0.3971 0.3102 0.2533 0.0721  -0.0342 0.0140  345  THR A N   
893  C  CA  . THR A 121 ? 0.4045 0.3209 0.2651 0.0662  -0.0285 0.0143  345  THR A CA  
894  C  C   . THR A 121 ? 0.4329 0.3399 0.2855 0.0649  -0.0208 0.0197  345  THR A C   
895  O  O   . THR A 121 ? 0.4436 0.3420 0.2899 0.0673  -0.0191 0.0233  345  THR A O   
896  C  CB  . THR A 121 ? 0.4123 0.3383 0.2894 0.0603  -0.0274 0.0117  345  THR A CB  
897  O  OG1 . THR A 121 ? 0.4034 0.3259 0.2838 0.0588  -0.0243 0.0140  345  THR A OG1 
898  C  CG2 . THR A 121 ? 0.3911 0.3265 0.2774 0.0612  -0.0343 0.0066  345  THR A CG2 
899  N  N   . ARG A 122 ? 0.4471 0.3559 0.3008 0.0609  -0.0158 0.0202  346  ARG A N   
900  C  CA  . ARG A 122 ? 0.3956 0.2974 0.2445 0.0586  -0.0078 0.0249  346  ARG A CA  
901  C  C   . ARG A 122 ? 0.3874 0.2956 0.2433 0.0535  -0.0039 0.0237  346  ARG A C   
902  O  O   . ARG A 122 ? 0.3938 0.3077 0.2507 0.0539  -0.0069 0.0203  346  ARG A O   
903  C  CB  . ARG A 122 ? 0.4172 0.3079 0.2484 0.0641  -0.0062 0.0287  346  ARG A CB  
904  C  CG  . ARG A 122 ? 0.3941 0.2859 0.2168 0.0671  -0.0086 0.0266  346  ARG A CG  
905  C  CD  . ARG A 122 ? 0.4749 0.3559 0.2788 0.0742  -0.0097 0.0294  346  ARG A CD  
906  N  NE  . ARG A 122 ? 0.4716 0.3512 0.2732 0.0791  -0.0173 0.0282  346  ARG A NE  
907  C  CZ  . ARG A 122 ? 0.4912 0.3770 0.2949 0.0819  -0.0257 0.0232  346  ARG A CZ  
908  N  NH1 . ARG A 122 ? 0.5201 0.4128 0.3270 0.0806  -0.0278 0.0190  346  ARG A NH1 
909  N  NH2 . ARG A 122 ? 0.5044 0.3894 0.3077 0.0863  -0.0322 0.0222  346  ARG A NH2 
910  N  N   . ALA A 123 ? 0.4017 0.3088 0.2627 0.0489  0.0027  0.0263  347  ALA A N   
911  C  CA  . ALA A 123 ? 0.3706 0.2836 0.2389 0.0442  0.0068  0.0255  347  ALA A CA  
912  C  C   . ALA A 123 ? 0.4259 0.3331 0.2929 0.0415  0.0150  0.0301  347  ALA A C   
913  O  O   . ALA A 123 ? 0.3640 0.2657 0.2313 0.0407  0.0173  0.0328  347  ALA A O   
914  C  CB  . ALA A 123 ? 0.3712 0.2941 0.2548 0.0395  0.0045  0.0220  347  ALA A CB  
915  N  N   . HIS A 124 ? 0.3692 0.2776 0.2351 0.0402  0.0196  0.0307  348  HIS A N   
916  C  CA  . HIS A 124 ? 0.3894 0.2937 0.2560 0.0373  0.0278  0.0348  348  HIS A CA  
917  C  C   . HIS A 124 ? 0.4147 0.3263 0.2890 0.0338  0.0311  0.0334  348  HIS A C   
918  O  O   . HIS A 124 ? 0.3583 0.2745 0.2313 0.0354  0.0281  0.0303  348  HIS A O   
919  C  CB  . HIS A 124 ? 0.4081 0.3011 0.2587 0.0416  0.0321  0.0394  348  HIS A CB  
920  C  CG  . HIS A 124 ? 0.4416 0.3269 0.2824 0.0464  0.0281  0.0408  348  HIS A CG  
921  N  ND1 . HIS A 124 ? 0.4447 0.3251 0.2884 0.0451  0.0290  0.0431  348  HIS A ND1 
922  C  CD2 . HIS A 124 ? 0.4537 0.3356 0.2825 0.0526  0.0225  0.0398  348  HIS A CD2 
923  C  CE1 . HIS A 124 ? 0.5171 0.3913 0.3508 0.0505  0.0244  0.0438  348  HIS A CE1 
924  N  NE2 . HIS A 124 ? 0.4626 0.3378 0.2873 0.0551  0.0203  0.0418  348  HIS A NE2 
925  N  N   . GLU A 125 ? 0.4277 0.3400 0.3103 0.0292  0.0372  0.0355  349  GLU A N   
926  C  CA  . GLU A 125 ? 0.3805 0.2992 0.2704 0.0262  0.0412  0.0347  349  GLU A CA  
927  C  C   . GLU A 125 ? 0.4102 0.3260 0.2886 0.0303  0.0437  0.0353  349  GLU A C   
928  O  O   . GLU A 125 ? 0.3871 0.2939 0.2515 0.0345  0.0456  0.0383  349  GLU A O   
929  C  CB  . GLU A 125 ? 0.3969 0.3149 0.2954 0.0215  0.0482  0.0377  349  GLU A CB  
930  C  CG  . GLU A 125 ? 0.4652 0.3889 0.3783 0.0164  0.0458  0.0358  349  GLU A CG  
931  C  CD  . GLU A 125 ? 0.5384 0.4580 0.4572 0.0126  0.0520  0.0391  349  GLU A CD  
932  O  OE1 . GLU A 125 ? 0.5748 0.4847 0.4843 0.0145  0.0555  0.0431  349  GLU A OE1 
933  O  OE2 . GLU A 125 ? 0.4694 0.3952 0.4018 0.0076  0.0531  0.0379  349  GLU A OE2 
934  N  N   . ALA A 126 ? 0.3633 0.2862 0.2470 0.0293  0.0434  0.0325  350  ALA A N   
935  C  CA  . ALA A 126 ? 0.3891 0.3100 0.2626 0.0333  0.0452  0.0321  350  ALA A CA  
936  C  C   . ALA A 126 ? 0.3848 0.3133 0.2684 0.0303  0.0484  0.0305  350  ALA A C   
937  O  O   . ALA A 126 ? 0.3314 0.2676 0.2292 0.0260  0.0467  0.0287  350  ALA A O   
938  C  CB  . ALA A 126 ? 0.3714 0.2922 0.2368 0.0376  0.0372  0.0285  350  ALA A CB  
939  N  N   . ARG A 127 ? 0.3718 0.2980 0.2481 0.0330  0.0532  0.0313  351  ARG A N   
940  C  CA  A ARG A 127 ? 0.4038 0.3370 0.2891 0.0311  0.0561  0.0295  351  ARG A CA  
941  C  CA  B ARG A 127 ? 0.4087 0.3422 0.2942 0.0311  0.0557  0.0293  351  ARG A CA  
942  C  C   . ARG A 127 ? 0.3790 0.3102 0.2531 0.0359  0.0557  0.0274  351  ARG A C   
943  O  O   . ARG A 127 ? 0.3762 0.2993 0.2347 0.0405  0.0572  0.0290  351  ARG A O   
944  C  CB  A ARG A 127 ? 0.4316 0.3655 0.3243 0.0278  0.0652  0.0331  351  ARG A CB  
945  C  CB  B ARG A 127 ? 0.4308 0.3659 0.3253 0.0274  0.0644  0.0326  351  ARG A CB  
946  C  CG  A ARG A 127 ? 0.4896 0.4141 0.3706 0.0300  0.0728  0.0381  351  ARG A CG  
947  C  CG  B ARG A 127 ? 0.4868 0.4133 0.3720 0.0288  0.0722  0.0377  351  ARG A CG  
948  C  CD  A ARG A 127 ? 0.5446 0.4713 0.4374 0.0254  0.0813  0.0413  351  ARG A CD  
949  C  CD  B ARG A 127 ? 0.5424 0.4728 0.4417 0.0237  0.0796  0.0401  351  ARG A CD  
950  N  NE  A ARG A 127 ? 0.5912 0.5087 0.4742 0.0268  0.0895  0.0467  351  ARG A NE  
951  N  NE  B ARG A 127 ? 0.5943 0.5178 0.4866 0.0247  0.0892  0.0450  351  ARG A NE  
952  C  CZ  A ARG A 127 ? 0.5881 0.5037 0.4671 0.0282  0.0982  0.0490  351  ARG A CZ  
953  C  CZ  B ARG A 127 ? 0.5733 0.4910 0.4659 0.0225  0.0935  0.0493  351  ARG A CZ  
954  N  NH1 A ARG A 127 ? 0.5998 0.5221 0.4840 0.0287  0.0999  0.0464  351  ARG A NH1 
955  N  NH1 B ARG A 127 ? 0.5342 0.4521 0.4333 0.0195  0.0887  0.0490  351  ARG A NH1 
956  N  NH2 A ARG A 127 ? 0.6205 0.5269 0.4903 0.0293  0.1058  0.0543  351  ARG A NH2 
957  N  NH2 B ARG A 127 ? 0.5925 0.5039 0.4787 0.0234  0.1031  0.0539  351  ARG A NH2 
958  N  N   . ILE A 128 ? 0.3638 0.3020 0.2458 0.0350  0.0536  0.0237  352  ILE A N   
959  C  CA  . ILE A 128 ? 0.3614 0.2986 0.2351 0.0392  0.0525  0.0207  352  ILE A CA  
960  C  C   . ILE A 128 ? 0.3626 0.3049 0.2448 0.0377  0.0585  0.0205  352  ILE A C   
961  O  O   . ILE A 128 ? 0.3616 0.3119 0.2590 0.0338  0.0572  0.0192  352  ILE A O   
962  C  CB  . ILE A 128 ? 0.3782 0.3187 0.2535 0.0397  0.0431  0.0159  352  ILE A CB  
963  C  CG1 . ILE A 128 ? 0.3309 0.2668 0.1979 0.0418  0.0371  0.0158  352  ILE A CG1 
964  C  CG2 . ILE A 128 ? 0.3312 0.2714 0.2007 0.0432  0.0421  0.0123  352  ILE A CG2 
965  C  CD1 . ILE A 128 ? 0.3250 0.2663 0.1993 0.0403  0.0286  0.0117  352  ILE A CD1 
966  N  N   . ASP A 129 ? 0.3353 0.2732 0.2078 0.0412  0.0649  0.0217  353  ASP A N   
967  C  CA  . ASP A 129 ? 0.3620 0.3047 0.2423 0.0406  0.0710  0.0213  353  ASP A CA  
968  C  C   . ASP A 129 ? 0.3424 0.2873 0.2215 0.0431  0.0662  0.0163  353  ASP A C   
969  O  O   . ASP A 129 ? 0.3708 0.3098 0.2355 0.0480  0.0657  0.0145  353  ASP A O   
970  C  CB  . ASP A 129 ? 0.3942 0.3310 0.2650 0.0432  0.0810  0.0251  353  ASP A CB  
971  C  CG  . ASP A 129 ? 0.4646 0.4074 0.3462 0.0419  0.0885  0.0253  353  ASP A CG  
972  O  OD1 . ASP A 129 ? 0.3595 0.3095 0.2518 0.0408  0.0853  0.0218  353  ASP A OD1 
973  O  OD2 . ASP A 129 ? 0.4792 0.4195 0.3591 0.0420  0.0978  0.0292  353  ASP A OD2 
974  N  N   . THR A 130 ? 0.3166 0.2696 0.2103 0.0399  0.0623  0.0138  354  THR A N   
975  C  CA  . THR A 130 ? 0.3540 0.3083 0.2467 0.0421  0.0573  0.0090  354  THR A CA  
976  C  C   . THR A 130 ? 0.3405 0.2947 0.2314 0.0450  0.0634  0.0081  354  THR A C   
977  O  O   . THR A 130 ? 0.3695 0.3234 0.2578 0.0475  0.0600  0.0040  354  THR A O   
978  C  CB  . THR A 130 ? 0.3569 0.3188 0.2645 0.0381  0.0513  0.0068  354  THR A CB  
979  O  OG1 . THR A 130 ? 0.3065 0.2752 0.2285 0.0350  0.0556  0.0083  354  THR A OG1 
980  C  CG2 . THR A 130 ? 0.2916 0.2536 0.2009 0.0355  0.0455  0.0075  354  THR A CG2 
981  N  N   . GLY A 131 ? 0.3800 0.3343 0.2723 0.0448  0.0725  0.0116  355  GLY A N   
982  C  CA  . GLY A 131 ? 0.3928 0.3465 0.2821 0.0482  0.0795  0.0110  355  GLY A CA  
983  C  C   . GLY A 131 ? 0.4497 0.3939 0.3194 0.0533  0.0843  0.0122  355  GLY A C   
984  O  O   . GLY A 131 ? 0.4267 0.3696 0.2918 0.0567  0.0905  0.0115  355  GLY A O   
985  N  N   . SER A 132 ? 0.3814 0.3190 0.2390 0.0543  0.0815  0.0139  356  SER A N   
986  C  CA  . SER A 132 ? 0.4760 0.4037 0.3131 0.0597  0.0853  0.0152  356  SER A CA  
987  C  C   . SER A 132 ? 0.4508 0.3743 0.2754 0.0650  0.0807  0.0100  356  SER A C   
988  O  O   . SER A 132 ? 0.4054 0.3316 0.2343 0.0644  0.0719  0.0056  356  SER A O   
989  C  CB  . SER A 132 ? 0.4851 0.4066 0.3128 0.0597  0.0820  0.0181  356  SER A CB  
990  O  OG  . SER A 132 ? 0.5612 0.4729 0.3672 0.0659  0.0813  0.0175  356  SER A OG  
991  N  N   . ASP A 133 ? 0.5281 0.4445 0.3367 0.0703  0.0867  0.0104  357  ASP A N   
992  C  CA  . ASP A 133 ? 0.5912 0.5029 0.3871 0.0756  0.0823  0.0050  357  ASP A CA  
993  C  C   . ASP A 133 ? 0.5899 0.4959 0.3735 0.0779  0.0722  0.0026  357  ASP A C   
994  O  O   . ASP A 133 ? 0.5606 0.4644 0.3378 0.0810  0.0658  -0.0030 357  ASP A O   
995  C  CB  . ASP A 133 ? 0.6307 0.5361 0.4119 0.0811  0.0917  0.0058  357  ASP A CB  
996  C  CG  . ASP A 133 ? 0.7168 0.6131 0.4804 0.0840  0.0967  0.0107  357  ASP A CG  
997  O  OD1 . ASP A 133 ? 0.7128 0.6094 0.4805 0.0805  0.0966  0.0152  357  ASP A OD1 
998  O  OD2 . ASP A 133 ? 0.7222 0.6105 0.4671 0.0901  0.1009  0.0102  357  ASP A OD2 
999  N  N   . THR A 134 ? 0.5557 0.4595 0.3369 0.0763  0.0704  0.0063  358  THR A N   
1000 C  CA  . THR A 134 ? 0.5298 0.4297 0.3025 0.0779  0.0602  0.0041  358  THR A CA  
1001 C  C   . THR A 134 ? 0.5102 0.4181 0.2995 0.0732  0.0512  0.0010  358  THR A C   
1002 O  O   . THR A 134 ? 0.5348 0.4409 0.3196 0.0745  0.0421  -0.0022 358  THR A O   
1003 C  CB  . THR A 134 ? 0.5333 0.4273 0.2970 0.0785  0.0621  0.0096  358  THR A CB  
1004 O  OG1 . THR A 134 ? 0.5714 0.4717 0.3519 0.0723  0.0639  0.0134  358  THR A OG1 
1005 C  CG2 . THR A 134 ? 0.5999 0.4859 0.3479 0.0827  0.0723  0.0137  358  THR A CG2 
1006 N  N   . PHE A 135 ? 0.4532 0.3697 0.2614 0.0680  0.0535  0.0017  359  PHE A N   
1007 C  CA  . PHE A 135 ? 0.4470 0.3707 0.2703 0.0636  0.0458  -0.0009 359  PHE A CA  
1008 C  C   . PHE A 135 ? 0.4538 0.3778 0.2764 0.0655  0.0398  -0.0071 359  PHE A C   
1009 O  O   . PHE A 135 ? 0.3901 0.3165 0.2178 0.0657  0.0431  -0.0089 359  PHE A O   
1010 C  CB  . PHE A 135 ? 0.3828 0.3148 0.2249 0.0580  0.0501  0.0018  359  PHE A CB  
1011 C  CG  . PHE A 135 ? 0.3886 0.3276 0.2454 0.0534  0.0429  -0.0001 359  PHE A CG  
1012 C  CD1 . PHE A 135 ? 0.3810 0.3204 0.2396 0.0512  0.0381  0.0012  359  PHE A CD1 
1013 C  CD2 . PHE A 135 ? 0.3593 0.3041 0.2278 0.0516  0.0414  -0.0030 359  PHE A CD2 
1014 C  CE1 . PHE A 135 ? 0.3854 0.3310 0.2570 0.0472  0.0322  -0.0004 359  PHE A CE1 
1015 C  CE2 . PHE A 135 ? 0.3379 0.2885 0.2190 0.0475  0.0353  -0.0044 359  PHE A CE2 
1016 C  CZ  . PHE A 135 ? 0.3428 0.2940 0.2254 0.0453  0.0309  -0.0031 359  PHE A CZ  
1017 N  N   . ALA A 136 ? 0.4699 0.3913 0.2863 0.0672  0.0310  -0.0106 360  ALA A N   
1018 C  CA  . ALA A 136 ? 0.4292 0.3501 0.2447 0.0689  0.0247  -0.0168 360  ALA A CA  
1019 C  C   . ALA A 136 ? 0.3640 0.2880 0.1866 0.0663  0.0149  -0.0195 360  ALA A C   
1020 O  O   . ALA A 136 ? 0.3935 0.3135 0.2070 0.0694  0.0080  -0.0232 360  ALA A O   
1021 C  CB  . ALA A 136 ? 0.4168 0.3288 0.2124 0.0756  0.0246  -0.0196 360  ALA A CB  
1022 N  N   . PRO A 137 ? 0.3771 0.3086 0.2163 0.0608  0.0141  -0.0179 361  PRO A N   
1023 C  CA  . PRO A 137 ? 0.3782 0.3131 0.2250 0.0582  0.0056  -0.0201 361  PRO A CA  
1024 C  C   . PRO A 137 ? 0.3867 0.3213 0.2347 0.0590  -0.0011 -0.0262 361  PRO A C   
1025 O  O   . PRO A 137 ? 0.3757 0.3114 0.2259 0.0583  -0.0086 -0.0288 361  PRO A O   
1026 C  CB  . PRO A 137 ? 0.3797 0.3223 0.2434 0.0524  0.0078  -0.0171 361  PRO A CB  
1027 C  CG  . PRO A 137 ? 0.3500 0.2940 0.2175 0.0521  0.0151  -0.0158 361  PRO A CG  
1028 C  CD  . PRO A 137 ? 0.3831 0.3205 0.2354 0.0568  0.0205  -0.0144 361  PRO A CD  
1029 N  N   . LYS A 138 ? 0.3702 0.3035 0.2179 0.0603  0.0013  -0.0288 362  LYS A N   
1030 C  CA  . LYS A 138 ? 0.3989 0.3313 0.2483 0.0608  -0.0051 -0.0348 362  LYS A CA  
1031 C  C   . LYS A 138 ? 0.4007 0.3274 0.2370 0.0649  -0.0118 -0.0388 362  LYS A C   
1032 O  O   . LYS A 138 ? 0.3729 0.3004 0.2135 0.0640  -0.0195 -0.0432 362  LYS A O   
1033 C  CB  . LYS A 138 ? 0.3856 0.3161 0.2344 0.0626  -0.0007 -0.0367 362  LYS A CB  
1034 C  CG  . LYS A 138 ? 0.4057 0.3347 0.2576 0.0627  -0.0066 -0.0429 362  LYS A CG  
1035 C  CD  . LYS A 138 ? 0.4723 0.3985 0.3216 0.0654  -0.0017 -0.0447 362  LYS A CD  
1036 C  CE  . LYS A 138 ? 0.4634 0.3883 0.3186 0.0648  -0.0069 -0.0503 362  LYS A CE  
1037 N  NZ  . LYS A 138 ? 0.4891 0.4203 0.3621 0.0591  -0.0086 -0.0489 362  LYS A NZ  
1038 N  N   . ILE A 139 ? 0.4297 0.3505 0.2499 0.0696  -0.0091 -0.0372 363  ILE A N   
1039 C  CA  . ILE A 139 ? 0.4391 0.3542 0.2453 0.0741  -0.0156 -0.0404 363  ILE A CA  
1040 C  C   . ILE A 139 ? 0.4773 0.3930 0.2813 0.0739  -0.0172 -0.0364 363  ILE A C   
1041 O  O   . ILE A 139 ? 0.4242 0.3345 0.2144 0.0784  -0.0212 -0.0376 363  ILE A O   
1042 C  CB  . ILE A 139 ? 0.4977 0.4041 0.2847 0.0805  -0.0125 -0.0420 363  ILE A CB  
1043 C  CG1 . ILE A 139 ? 0.4580 0.3626 0.2387 0.0817  -0.0020 -0.0356 363  ILE A CG1 
1044 C  CG2 . ILE A 139 ? 0.4833 0.3885 0.2723 0.0812  -0.0127 -0.0472 363  ILE A CG2 
1045 C  CD1 . ILE A 139 ? 0.5336 0.4295 0.2945 0.0882  0.0024  -0.0365 363  ILE A CD1 
1046 N  N   . GLY A 140 ? 0.3993 0.3212 0.2164 0.0690  -0.0143 -0.0320 364  GLY A N   
1047 C  CA  . GLY A 140 ? 0.4325 0.3556 0.2500 0.0683  -0.0166 -0.0289 364  GLY A CA  
1048 C  C   . GLY A 140 ? 0.4672 0.3847 0.2716 0.0714  -0.0109 -0.0237 364  GLY A C   
1049 O  O   . GLY A 140 ? 0.4963 0.4122 0.2963 0.0728  -0.0141 -0.0220 364  GLY A O   
1050 N  N   . GLN A 141 ? 0.4480 0.3624 0.2466 0.0727  -0.0023 -0.0209 365  GLN A N   
1051 C  CA  . GLN A 141 ? 0.4776 0.3862 0.2639 0.0754  0.0043  -0.0156 365  GLN A CA  
1052 C  C   . GLN A 141 ? 0.4632 0.3762 0.2609 0.0708  0.0129  -0.0102 365  GLN A C   
1053 O  O   . GLN A 141 ? 0.4111 0.3268 0.2149 0.0692  0.0186  -0.0100 365  GLN A O   
1054 C  CB  . GLN A 141 ? 0.4685 0.3690 0.2366 0.0814  0.0078  -0.0168 365  GLN A CB  
1055 C  CG  . GLN A 141 ? 0.5674 0.4626 0.3224 0.0865  -0.0011 -0.0221 365  GLN A CG  
1056 C  CD  . GLN A 141 ? 0.7050 0.5927 0.4430 0.0922  0.0018  -0.0246 365  GLN A CD  
1057 O  OE1 . GLN A 141 ? 0.6837 0.5711 0.4218 0.0920  0.0106  -0.0229 365  GLN A OE1 
1058 N  NE2 . GLN A 141 ? 0.7540 0.6356 0.4773 0.0976  -0.0056 -0.0289 365  GLN A NE2 
1059 N  N   . VAL A 142 ? 0.4515 0.3652 0.2524 0.0687  0.0134  -0.0060 366  VAL A N   
1060 C  CA  A VAL A 142 ? 0.4211 0.3381 0.2318 0.0645  0.0211  -0.0008 366  VAL A CA  
1061 C  CA  B VAL A 142 ? 0.4307 0.3479 0.2417 0.0643  0.0209  -0.0008 366  VAL A CA  
1062 C  C   . VAL A 142 ? 0.4320 0.3430 0.2333 0.0661  0.0241  0.0043  366  VAL A C   
1063 O  O   . VAL A 142 ? 0.4325 0.3400 0.2265 0.0686  0.0181  0.0038  366  VAL A O   
1064 C  CB  A VAL A 142 ? 0.4038 0.3301 0.2343 0.0583  0.0183  -0.0014 366  VAL A CB  
1065 C  CB  B VAL A 142 ? 0.4036 0.3298 0.2339 0.0584  0.0175  -0.0015 366  VAL A CB  
1066 C  CG1 A VAL A 142 ? 0.4046 0.3362 0.2446 0.0565  0.0167  -0.0055 366  VAL A CG1 
1067 C  CG1 B VAL A 142 ? 0.3597 0.2890 0.1997 0.0541  0.0244  0.0034  366  VAL A CG1 
1068 C  CG2 A VAL A 142 ? 0.4022 0.3295 0.2346 0.0579  0.0103  -0.0026 366  VAL A CG2 
1069 C  CG2 B VAL A 142 ? 0.4060 0.3376 0.2458 0.0566  0.0149  -0.0061 366  VAL A CG2 
1070 N  N   . ARG A 143 ? 0.4053 0.3149 0.2072 0.0647  0.0335  0.0092  367  ARG A N   
1071 C  CA  . ARG A 143 ? 0.4341 0.3376 0.2286 0.0655  0.0377  0.0147  367  ARG A CA  
1072 C  C   . ARG A 143 ? 0.4427 0.3517 0.2533 0.0594  0.0411  0.0181  367  ARG A C   
1073 O  O   . ARG A 143 ? 0.4292 0.3454 0.2539 0.0552  0.0443  0.0176  367  ARG A O   
1074 C  CB  . ARG A 143 ? 0.4220 0.3177 0.2020 0.0692  0.0467  0.0182  367  ARG A CB  
1075 C  CG  . ARG A 143 ? 0.5237 0.4122 0.2845 0.0761  0.0436  0.0154  367  ARG A CG  
1076 C  CD  . ARG A 143 ? 0.5501 0.4320 0.2980 0.0794  0.0536  0.0184  367  ARG A CD  
1077 N  NE  . ARG A 143 ? 0.5472 0.4209 0.2742 0.0866  0.0502  0.0157  367  ARG A NE  
1078 C  CZ  . ARG A 143 ? 0.6136 0.4789 0.3233 0.0914  0.0575  0.0182  367  ARG A CZ  
1079 N  NH1 . ARG A 143 ? 0.6487 0.5133 0.3606 0.0896  0.0692  0.0234  367  ARG A NH1 
1080 N  NH2 . ARG A 143 ? 0.6122 0.4697 0.3019 0.0983  0.0530  0.0154  367  ARG A NH2 
1081 N  N   . PHE A 144 ? 0.3893 0.2947 0.1978 0.0591  0.0403  0.0214  368  PHE A N   
1082 C  CA  . PHE A 144 ? 0.4028 0.3118 0.2248 0.0536  0.0441  0.0247  368  PHE A CA  
1083 C  C   . PHE A 144 ? 0.4462 0.3465 0.2586 0.0549  0.0508  0.0307  368  PHE A C   
1084 O  O   . PHE A 144 ? 0.3971 0.2885 0.1926 0.0601  0.0498  0.0321  368  PHE A O   
1085 C  CB  . PHE A 144 ? 0.4245 0.3393 0.2581 0.0505  0.0363  0.0225  368  PHE A CB  
1086 C  CG  . PHE A 144 ? 0.4242 0.3334 0.2486 0.0537  0.0306  0.0231  368  PHE A CG  
1087 C  CD1 . PHE A 144 ? 0.4207 0.3244 0.2428 0.0533  0.0337  0.0277  368  PHE A CD1 
1088 C  CD2 . PHE A 144 ? 0.4035 0.3135 0.2237 0.0569  0.0219  0.0187  368  PHE A CD2 
1089 C  CE1 . PHE A 144 ? 0.4649 0.3635 0.2791 0.0566  0.0283  0.0282  368  PHE A CE1 
1090 C  CE2 . PHE A 144 ? 0.4387 0.3444 0.2520 0.0600  0.0162  0.0189  368  PHE A CE2 
1091 C  CZ  . PHE A 144 ? 0.4499 0.3499 0.2599 0.0601  0.0194  0.0238  368  PHE A CZ  
1092 N  N   . TYR A 145 ? 0.4496 0.3521 0.2729 0.0501  0.0577  0.0341  369  TYR A N   
1093 C  CA  . TYR A 145 ? 0.4654 0.3602 0.2832 0.0500  0.0645  0.0400  369  TYR A CA  
1094 C  C   . TYR A 145 ? 0.4172 0.3132 0.2447 0.0462  0.0611  0.0410  369  TYR A C   
1095 O  O   . TYR A 145 ? 0.4298 0.3347 0.2729 0.0419  0.0575  0.0381  369  TYR A O   
1096 C  CB  . TYR A 145 ? 0.4761 0.3722 0.2999 0.0471  0.0753  0.0431  369  TYR A CB  
1097 C  CG  . TYR A 145 ? 0.5221 0.4113 0.3446 0.0453  0.0827  0.0493  369  TYR A CG  
1098 C  CD1 . TYR A 145 ? 0.5209 0.3986 0.3252 0.0499  0.0880  0.0538  369  TYR A CD1 
1099 C  CD2 . TYR A 145 ? 0.5155 0.4092 0.3547 0.0391  0.0843  0.0506  369  TYR A CD2 
1100 C  CE1 . TYR A 145 ? 0.6322 0.5029 0.4355 0.0481  0.0951  0.0598  369  TYR A CE1 
1101 C  CE2 . TYR A 145 ? 0.5608 0.4478 0.3997 0.0371  0.0910  0.0560  369  TYR A CE2 
1102 C  CZ  . TYR A 145 ? 0.5569 0.4324 0.3782 0.0415  0.0966  0.0607  369  TYR A CZ  
1103 O  OH  . TYR A 145 ? 0.6654 0.5336 0.4866 0.0393  0.1036  0.0664  369  TYR A OH  
1104 N  N   . SER A 146 ? 0.4746 0.3615 0.2925 0.0482  0.0625  0.0451  370  SER A N   
1105 C  CA  . SER A 146 ? 0.4338 0.3204 0.2599 0.0450  0.0602  0.0465  370  SER A CA  
1106 C  C   . SER A 146 ? 0.4985 0.3744 0.3165 0.0456  0.0676  0.0528  370  SER A C   
1107 O  O   . SER A 146 ? 0.5222 0.3889 0.3229 0.0507  0.0703  0.0557  370  SER A O   
1108 C  CB  . SER A 146 ? 0.4662 0.3528 0.2887 0.0480  0.0499  0.0433  370  SER A CB  
1109 O  OG  . SER A 146 ? 0.4485 0.3347 0.2787 0.0453  0.0479  0.0444  370  SER A OG  
1110 N  N   . THR A 147 ? 0.4664 0.3432 0.2969 0.0402  0.0709  0.0550  371  THR A N   
1111 C  CA  . THR A 147 ? 0.5885 0.4544 0.4125 0.0403  0.0773  0.0611  371  THR A CA  
1112 C  C   . THR A 147 ? 0.5431 0.3999 0.3536 0.0453  0.0717  0.0624  371  THR A C   
1113 O  O   . THR A 147 ? 0.5998 0.4452 0.3987 0.0477  0.0767  0.0678  371  THR A O   
1114 C  CB  . THR A 147 ? 0.5589 0.4281 0.4004 0.0332  0.0810  0.0623  371  THR A CB  
1115 O  OG1 . THR A 147 ? 0.5853 0.4602 0.4368 0.0311  0.0726  0.0583  371  THR A OG1 
1116 C  CG2 . THR A 147 ? 0.4953 0.3735 0.3505 0.0285  0.0866  0.0612  371  THR A CG2 
1117 N  N   . SER A 148 ? 0.5508 0.4123 0.3624 0.0473  0.0617  0.0577  372  SER A N   
1118 C  CA  . SER A 148 ? 0.5446 0.3987 0.3449 0.0524  0.0556  0.0584  372  SER A CA  
1119 C  C   . SER A 148 ? 0.5596 0.4087 0.3411 0.0598  0.0526  0.0580  372  SER A C   
1120 O  O   . SER A 148 ? 0.5420 0.3968 0.3226 0.0608  0.0512  0.0545  372  SER A O   
1121 C  CB  . SER A 148 ? 0.4862 0.3481 0.2978 0.0510  0.0465  0.0535  372  SER A CB  
1122 O  OG  . SER A 148 ? 0.5084 0.3646 0.3090 0.0568  0.0398  0.0534  372  SER A OG  
1123 N  N   . SER A 149 ? 0.5760 0.4138 0.3422 0.0651  0.0515  0.0615  373  SER A N   
1124 C  CA  . SER A 149 ? 0.5963 0.4291 0.3442 0.0728  0.0463  0.0605  373  SER A CA  
1125 C  C   . SER A 149 ? 0.5473 0.3838 0.2968 0.0759  0.0346  0.0559  373  SER A C   
1126 O  O   . SER A 149 ? 0.6059 0.4387 0.3414 0.0824  0.0288  0.0545  373  SER A O   
1127 C  CB  . SER A 149 ? 0.6270 0.4445 0.3552 0.0779  0.0518  0.0673  373  SER A CB  
1128 O  OG  . SER A 149 ? 0.6834 0.4945 0.4140 0.0769  0.0524  0.0711  373  SER A OG  
1129 N  N   . ASP A 150 ? 0.5559 0.4001 0.3224 0.0713  0.0312  0.0534  374  ASP A N   
1130 C  CA  . ASP A 150 ? 0.5764 0.4240 0.3463 0.0738  0.0212  0.0497  374  ASP A CA  
1131 C  C   . ASP A 150 ? 0.5333 0.3926 0.3105 0.0733  0.0143  0.0428  374  ASP A C   
1132 O  O   . ASP A 150 ? 0.5282 0.3974 0.3216 0.0689  0.0113  0.0391  374  ASP A O   
1133 C  CB  . ASP A 150 ? 0.5519 0.4013 0.3356 0.0693  0.0216  0.0503  374  ASP A CB  
1134 C  CG  . ASP A 150 ? 0.5527 0.4044 0.3394 0.0722  0.0123  0.0472  374  ASP A CG  
1135 O  OD1 . ASP A 150 ? 0.6178 0.4646 0.3919 0.0790  0.0067  0.0470  374  ASP A OD1 
1136 O  OD2 . ASP A 150 ? 0.5388 0.3973 0.3405 0.0680  0.0107  0.0449  374  ASP A OD2 
1137 N  N   . PHE A 151 ? 0.5210 0.3782 0.2854 0.0782  0.0118  0.0413  375  PHE A N   
1138 C  CA  . PHE A 151 ? 0.5071 0.3735 0.2763 0.0786  0.0048  0.0348  375  PHE A CA  
1139 C  C   . PHE A 151 ? 0.5687 0.4301 0.3221 0.0863  -0.0025 0.0331  375  PHE A C   
1140 O  O   . PHE A 151 ? 0.5726 0.4239 0.3082 0.0911  0.0005  0.0365  375  PHE A O   
1141 C  CB  . PHE A 151 ? 0.4877 0.3589 0.2604 0.0753  0.0101  0.0335  375  PHE A CB  
1142 C  CG  . PHE A 151 ? 0.4918 0.3707 0.2826 0.0676  0.0151  0.0335  375  PHE A CG  
1143 C  CD1 . PHE A 151 ? 0.4069 0.2967 0.2137 0.0637  0.0100  0.0289  375  PHE A CD1 
1144 C  CD2 . PHE A 151 ? 0.4548 0.3300 0.2467 0.0643  0.0247  0.0383  375  PHE A CD2 
1145 C  CE1 . PHE A 151 ? 0.4568 0.3534 0.2792 0.0571  0.0141  0.0289  375  PHE A CE1 
1146 C  CE2 . PHE A 151 ? 0.4418 0.3244 0.2506 0.0575  0.0284  0.0380  375  PHE A CE2 
1147 C  CZ  . PHE A 151 ? 0.4199 0.3130 0.2434 0.0541  0.0229  0.0333  375  PHE A CZ  
1148 N  N   . GLU A 152 ? 0.5713 0.4396 0.3312 0.0876  -0.0120 0.0278  376  GLU A N   
1149 C  CA  . GLU A 152 ? 0.5444 0.4093 0.2915 0.0949  -0.0205 0.0251  376  GLU A CA  
1150 C  C   . GLU A 152 ? 0.5098 0.3787 0.2541 0.0955  -0.0228 0.0203  376  GLU A C   
1151 O  O   . GLU A 152 ? 0.5067 0.3855 0.2656 0.0906  -0.0236 0.0163  376  GLU A O   
1152 C  CB  . GLU A 152 ? 0.5113 0.3823 0.2681 0.0960  -0.0298 0.0215  376  GLU A CB  
1153 C  CG  . GLU A 152 ? 0.6212 0.4886 0.3816 0.0958  -0.0284 0.0255  376  GLU A CG  
1154 C  CD  . GLU A 152 ? 0.6904 0.5451 0.4321 0.1032  -0.0297 0.0297  376  GLU A CD  
1155 O  OE1 . GLU A 152 ? 0.7271 0.5769 0.4534 0.1090  -0.0332 0.0288  376  GLU A OE1 
1156 O  OE2 . GLU A 152 ? 0.7005 0.5497 0.4426 0.1033  -0.0272 0.0339  376  GLU A OE2 
1157 N  N   . THR A 153 ? 0.5749 0.4353 0.2997 0.1019  -0.0240 0.0208  377  THR A N   
1158 C  CA  . THR A 153 ? 0.5540 0.4171 0.2744 0.1037  -0.0279 0.0154  377  THR A CA  
1159 C  C   . THR A 153 ? 0.5546 0.4262 0.2847 0.1045  -0.0394 0.0086  377  THR A C   
1160 O  O   . THR A 153 ? 0.5198 0.3915 0.2511 0.1072  -0.0458 0.0083  377  THR A O   
1161 C  CB  . THR A 153 ? 0.6522 0.5033 0.3478 0.1112  -0.0270 0.0175  377  THR A CB  
1162 O  OG1 . THR A 153 ? 0.6187 0.4635 0.3075 0.1095  -0.0151 0.0232  377  THR A OG1 
1163 C  CG2 . THR A 153 ? 0.6167 0.4696 0.3060 0.1143  -0.0333 0.0111  377  THR A CG2 
1164 N  N   . ASN A 154 ? 0.5186 0.3977 0.2568 0.1018  -0.0418 0.0031  378  ASN A N   
1165 C  CA  . ASN A 154 ? 0.5192 0.4062 0.2662 0.1023  -0.0524 -0.0039 378  ASN A CA  
1166 C  C   . ASN A 154 ? 0.5053 0.4017 0.2723 0.0979  -0.0554 -0.0050 378  ASN A C   
1167 O  O   . ASN A 154 ? 0.5317 0.4323 0.3037 0.1001  -0.0644 -0.0089 378  ASN A O   
1168 C  CB  . ASN A 154 ? 0.5110 0.3918 0.2418 0.1106  -0.0613 -0.0062 378  ASN A CB  
1169 C  CG  . ASN A 154 ? 0.6298 0.5045 0.3442 0.1146  -0.0614 -0.0085 378  ASN A CG  
1170 O  OD1 . ASN A 154 ? 0.5971 0.4761 0.3175 0.1110  -0.0593 -0.0118 378  ASN A OD1 
1171 N  ND2 . ASN A 154 ? 0.5873 0.4516 0.2803 0.1223  -0.0640 -0.0070 378  ASN A ND2 
1172 N  N   . GLN A 155 ? 0.4379 0.3376 0.2164 0.0919  -0.0479 -0.0017 379  GLN A N   
1173 C  CA  . GLN A 155 ? 0.4395 0.3485 0.2371 0.0872  -0.0497 -0.0029 379  GLN A CA  
1174 C  C   . GLN A 155 ? 0.4508 0.3678 0.2630 0.0801  -0.0454 -0.0046 379  GLN A C   
1175 O  O   . GLN A 155 ? 0.4265 0.3408 0.2349 0.0781  -0.0384 -0.0024 379  GLN A O   
1176 C  CB  . GLN A 155 ? 0.4430 0.3482 0.2413 0.0867  -0.0454 0.0026  379  GLN A CB  
1177 C  CG  . GLN A 155 ? 0.4764 0.3736 0.2615 0.0938  -0.0500 0.0045  379  GLN A CG  
1178 C  CD  . GLN A 155 ? 0.4969 0.4003 0.2886 0.0967  -0.0606 -0.0006 379  GLN A CD  
1179 O  OE1 . GLN A 155 ? 0.5065 0.4205 0.3148 0.0926  -0.0636 -0.0049 379  GLN A OE1 
1180 N  NE2 . GLN A 155 ? 0.5337 0.4306 0.3129 0.1039  -0.0662 0.0000  379  GLN A NE2 
1181 N  N   . PRO A 156 ? 0.4514 0.3782 0.2803 0.0763  -0.0494 -0.0082 380  PRO A N   
1182 C  CA  . PRO A 156 ? 0.4252 0.3591 0.2676 0.0698  -0.0454 -0.0094 380  PRO A CA  
1183 C  C   . PRO A 156 ? 0.4014 0.3336 0.2461 0.0660  -0.0364 -0.0042 380  PRO A C   
1184 O  O   . PRO A 156 ? 0.3540 0.2843 0.1997 0.0659  -0.0347 -0.0009 380  PRO A O   
1185 C  CB  . PRO A 156 ? 0.4022 0.3457 0.2609 0.0671  -0.0508 -0.0130 380  PRO A CB  
1186 C  CG  . PRO A 156 ? 0.4141 0.3563 0.2680 0.0726  -0.0589 -0.0153 380  PRO A CG  
1187 C  CD  . PRO A 156 ? 0.4383 0.3700 0.2749 0.0779  -0.0570 -0.0110 380  PRO A CD  
1188 N  N   . THR A 157 ? 0.3742 0.3071 0.2203 0.0628  -0.0310 -0.0037 381  THR A N   
1189 C  CA  . THR A 157 ? 0.3579 0.2893 0.2060 0.0593  -0.0224 0.0009  381  THR A CA  
1190 C  C   . THR A 157 ? 0.3238 0.2629 0.1857 0.0535  -0.0200 -0.0007 381  THR A C   
1191 O  O   . THR A 157 ? 0.3550 0.2973 0.2191 0.0532  -0.0223 -0.0044 381  THR A O   
1192 C  CB  . THR A 157 ? 0.3943 0.3170 0.2272 0.0625  -0.0170 0.0040  381  THR A CB  
1193 O  OG1 . THR A 157 ? 0.3671 0.2820 0.1857 0.0685  -0.0203 0.0051  381  THR A OG1 
1194 C  CG2 . THR A 157 ? 0.3717 0.2924 0.2071 0.0590  -0.0080 0.0090  381  THR A CG2 
1195 N  N   . HIS A 158 ? 0.3342 0.2760 0.2053 0.0492  -0.0155 0.0019  382  HIS A N   
1196 C  CA  . HIS A 158 ? 0.3083 0.2571 0.1920 0.0439  -0.0131 0.0009  382  HIS A CA  
1197 C  C   . HIS A 158 ? 0.3165 0.2635 0.2013 0.0412  -0.0053 0.0049  382  HIS A C   
1198 O  O   . HIS A 158 ? 0.3091 0.2522 0.1916 0.0411  -0.0023 0.0084  382  HIS A O   
1199 C  CB  . HIS A 158 ? 0.2953 0.2510 0.1918 0.0408  -0.0166 -0.0008 382  HIS A CB  
1200 C  CG  . HIS A 158 ? 0.2994 0.2621 0.2078 0.0360  -0.0153 -0.0022 382  HIS A CG  
1201 N  ND1 . HIS A 158 ? 0.3449 0.3124 0.2590 0.0352  -0.0194 -0.0060 382  HIS A ND1 
1202 C  CD2 . HIS A 158 ? 0.2833 0.2483 0.1985 0.0320  -0.0105 -0.0002 382  HIS A CD2 
1203 C  CE1 . HIS A 158 ? 0.3350 0.3072 0.2583 0.0311  -0.0170 -0.0060 382  HIS A CE1 
1204 N  NE2 . HIS A 158 ? 0.3180 0.2891 0.2421 0.0292  -0.0119 -0.0027 382  HIS A NE2 
1205 N  N   . PHE A 159 ? 0.3126 0.2625 0.2013 0.0390  -0.0022 0.0043  383  PHE A N   
1206 C  CA  . PHE A 159 ? 0.3232 0.2735 0.2162 0.0358  0.0048  0.0073  383  PHE A CA  
1207 C  C   . PHE A 159 ? 0.2772 0.2353 0.1849 0.0308  0.0043  0.0062  383  PHE A C   
1208 O  O   . PHE A 159 ? 0.2968 0.2597 0.2100 0.0296  0.0020  0.0034  383  PHE A O   
1209 C  CB  . PHE A 159 ? 0.3146 0.2627 0.2022 0.0371  0.0093  0.0077  383  PHE A CB  
1210 C  CG  . PHE A 159 ? 0.3110 0.2601 0.2041 0.0340  0.0166  0.0108  383  PHE A CG  
1211 C  CD1 . PHE A 159 ? 0.3083 0.2517 0.1957 0.0345  0.0220  0.0150  383  PHE A CD1 
1212 C  CD2 . PHE A 159 ? 0.2892 0.2449 0.1936 0.0304  0.0178  0.0096  383  PHE A CD2 
1213 C  CE1 . PHE A 159 ? 0.3466 0.2914 0.2407 0.0312  0.0287  0.0177  383  PHE A CE1 
1214 C  CE2 . PHE A 159 ? 0.3226 0.2799 0.2333 0.0276  0.0241  0.0122  383  PHE A CE2 
1215 C  CZ  . PHE A 159 ? 0.3237 0.2759 0.2298 0.0278  0.0295  0.0161  383  PHE A CZ  
1216 N  N   . THR A 160 ? 0.2829 0.2418 0.1963 0.0280  0.0063  0.0084  384  THR A N   
1217 C  CA  . THR A 160 ? 0.2515 0.2170 0.1774 0.0235  0.0061  0.0077  384  THR A CA  
1218 C  C   . THR A 160 ? 0.2623 0.2287 0.1927 0.0208  0.0120  0.0099  384  THR A C   
1219 O  O   . THR A 160 ? 0.2821 0.2444 0.2100 0.0206  0.0162  0.0129  384  THR A O   
1220 C  CB  . THR A 160 ? 0.2770 0.2430 0.2066 0.0223  0.0040  0.0081  384  THR A CB  
1221 O  OG1 . THR A 160 ? 0.2911 0.2567 0.2172 0.0251  -0.0014 0.0060  384  THR A OG1 
1222 C  CG2 . THR A 160 ? 0.2660 0.2386 0.2073 0.0180  0.0035  0.0070  384  THR A CG2 
1223 N  N   . PRO A 161 ? 0.2702 0.2419 0.2078 0.0188  0.0124  0.0085  385  PRO A N   
1224 C  CA  . PRO A 161 ? 0.2695 0.2427 0.2121 0.0166  0.0178  0.0103  385  PRO A CA  
1225 C  C   . PRO A 161 ? 0.2815 0.2577 0.2333 0.0127  0.0184  0.0114  385  PRO A C   
1226 O  O   . PRO A 161 ? 0.3007 0.2799 0.2571 0.0112  0.0145  0.0099  385  PRO A O   
1227 C  CB  . PRO A 161 ? 0.2623 0.2400 0.2092 0.0165  0.0168  0.0081  385  PRO A CB  
1228 C  CG  . PRO A 161 ? 0.2494 0.2298 0.1984 0.0163  0.0108  0.0054  385  PRO A CG  
1229 C  CD  . PRO A 161 ? 0.2372 0.2132 0.1782 0.0188  0.0082  0.0053  385  PRO A CD  
1230 N  N   . ILE A 162 ? 0.2503 0.2256 0.2048 0.0111  0.0236  0.0138  386  ILE A N   
1231 C  CA  . ILE A 162 ? 0.2334 0.2111 0.1969 0.0072  0.0241  0.0144  386  ILE A CA  
1232 C  C   . ILE A 162 ? 0.2413 0.2236 0.2138 0.0048  0.0276  0.0149  386  ILE A C   
1233 O  O   . ILE A 162 ? 0.2444 0.2321 0.2261 0.0020  0.0257  0.0136  386  ILE A O   
1234 C  CB  . ILE A 162 ? 0.3185 0.2901 0.2782 0.0070  0.0263  0.0169  386  ILE A CB  
1235 C  CG1 . ILE A 162 ? 0.2421 0.2101 0.1948 0.0094  0.0219  0.0161  386  ILE A CG1 
1236 C  CG2 . ILE A 162 ? 0.2362 0.2101 0.2060 0.0027  0.0275  0.0173  386  ILE A CG2 
1237 C  CD1 . ILE A 162 ? 0.3737 0.3340 0.3194 0.0108  0.0242  0.0188  386  ILE A CD1 
1238 N  N   . GLY A 163 ? 0.2854 0.2657 0.2552 0.0060  0.0330  0.0166  387  GLY A N   
1239 C  CA  . GLY A 163 ? 0.2963 0.2818 0.2758 0.0040  0.0364  0.0168  387  GLY A CA  
1240 C  C   . GLY A 163 ? 0.2773 0.2606 0.2527 0.0062  0.0426  0.0185  387  GLY A C   
1241 O  O   . GLY A 163 ? 0.3172 0.2963 0.2818 0.0099  0.0428  0.0183  387  GLY A O   
1242 N  N   . ILE A 164 ? 0.2688 0.2550 0.2528 0.0039  0.0478  0.0199  388  ILE A N   
1243 C  CA  . ILE A 164 ? 0.3053 0.2905 0.2872 0.0058  0.0545  0.0214  388  ILE A CA  
1244 C  C   . ILE A 164 ? 0.3357 0.3175 0.3193 0.0038  0.0613  0.0250  388  ILE A C   
1245 O  O   . ILE A 164 ? 0.3309 0.3142 0.3229 0.0000  0.0608  0.0256  388  ILE A O   
1246 C  CB  . ILE A 164 ? 0.3597 0.3528 0.3521 0.0054  0.0549  0.0196  388  ILE A CB  
1247 C  CG1 . ILE A 164 ? 0.3929 0.3845 0.3802 0.0087  0.0610  0.0204  388  ILE A CG1 
1248 C  CG2 . ILE A 164 ? 0.3363 0.3357 0.3440 0.0010  0.0560  0.0199  388  ILE A CG2 
1249 C  CD1 . ILE A 164 ? 0.4293 0.4174 0.4047 0.0131  0.0579  0.0183  388  ILE A CD1 
1250 N  N   . TYR A 165 ? 0.3431 0.3200 0.3181 0.0065  0.0677  0.0273  389  TYR A N   
1251 C  CA  . TYR A 165 ? 0.3649 0.3367 0.3387 0.0053  0.0752  0.0313  389  TYR A CA  
1252 C  C   . TYR A 165 ? 0.3527 0.3278 0.3318 0.0056  0.0831  0.0325  389  TYR A C   
1253 O  O   . TYR A 165 ? 0.3652 0.3386 0.3354 0.0097  0.0852  0.0320  389  TYR A O   
1254 C  CB  . TYR A 165 ? 0.3561 0.3174 0.3121 0.0091  0.0760  0.0336  389  TYR A CB  
1255 C  CG  . TYR A 165 ? 0.4176 0.3716 0.3703 0.0079  0.0829  0.0382  389  TYR A CG  
1256 C  CD1 . TYR A 165 ? 0.5081 0.4611 0.4622 0.0077  0.0924  0.0413  389  TYR A CD1 
1257 C  CD2 . TYR A 165 ? 0.4638 0.4116 0.4120 0.0071  0.0803  0.0397  389  TYR A CD2 
1258 C  CE1 . TYR A 165 ? 0.5536 0.4993 0.5047 0.0064  0.0992  0.0459  389  TYR A CE1 
1259 C  CE2 . TYR A 165 ? 0.5215 0.4617 0.4665 0.0061  0.0866  0.0441  389  TYR A CE2 
1260 C  CZ  . TYR A 165 ? 0.5302 0.4692 0.4766 0.0056  0.0962  0.0474  389  TYR A CZ  
1261 O  OH  . TYR A 165 ? 0.6239 0.5548 0.5671 0.0043  0.1031  0.0522  389  TYR A OH  
1262 N  N   . ILE A 166 ? 0.3676 0.3473 0.3612 0.0013  0.0874  0.0337  390  ILE A N   
1263 C  CA  . ILE A 166 ? 0.3865 0.3709 0.3883 0.0010  0.0952  0.0347  390  ILE A CA  
1264 C  C   . ILE A 166 ? 0.5111 0.4885 0.5083 0.0005  0.1048  0.0395  390  ILE A C   
1265 O  O   . ILE A 166 ? 0.4230 0.3987 0.4267 -0.0036 0.1065  0.0416  390  ILE A O   
1266 C  CB  . ILE A 166 ? 0.3592 0.3544 0.3818 -0.0034 0.0937  0.0327  390  ILE A CB  
1267 C  CG1 . ILE A 166 ? 0.3843 0.3856 0.4104 -0.0026 0.0845  0.0284  390  ILE A CG1 
1268 C  CG2 . ILE A 166 ? 0.4330 0.4334 0.4653 -0.0035 0.1022  0.0338  390  ILE A CG2 
1269 C  CD1 . ILE A 166 ? 0.3772 0.3790 0.3957 0.0023  0.0840  0.0266  390  ILE A CD1 
1270 N  N   . GLU A 167 ? 0.5242 0.4970 0.5097 0.0048  0.1112  0.0413  391  GLU A N   
1271 C  CA  . GLU A 167 ? 0.6235 0.5894 0.6035 0.0048  0.1214  0.0462  391  GLU A CA  
1272 C  C   . GLU A 167 ? 0.7469 0.7146 0.7245 0.0082  0.1293  0.0467  391  GLU A C   
1273 O  O   . GLU A 167 ? 0.7571 0.7275 0.7303 0.0120  0.1259  0.0434  391  GLU A O   
1274 C  CB  . GLU A 167 ? 0.6557 0.6090 0.6156 0.0079  0.1209  0.0491  391  GLU A CB  
1275 C  CG  . GLU A 167 ? 0.6978 0.6451 0.6380 0.0147  0.1207  0.0485  391  GLU A CG  
1276 C  CD  . GLU A 167 ? 0.8016 0.7359 0.7221 0.0180  0.1227  0.0524  391  GLU A CD  
1277 O  OE1 . GLU A 167 ? 0.8977 0.8272 0.8202 0.0149  0.1251  0.0559  391  GLU A OE1 
1278 O  OE2 . GLU A 167 ? 0.7470 0.6754 0.6499 0.0238  0.1216  0.0519  391  GLU A OE2 
1279 N  N   . GLY A 168 ? 0.9187 0.8843 0.8990 0.0069  0.1402  0.0508  392  GLY A N   
1280 C  CA  . GLY A 168 ? 0.9252 0.8941 0.9067 0.0095  0.1487  0.0512  392  GLY A CA  
1281 C  C   . GLY A 168 ? 0.9378 0.8992 0.8973 0.0166  0.1496  0.0509  392  GLY A C   
1282 O  O   . GLY A 168 ? 0.9299 0.8958 0.8898 0.0199  0.1509  0.0483  392  GLY A O   
1283 N  N   . ASN A 169 ? 0.7253 0.6751 0.6655 0.0194  0.1484  0.0533  393  ASN A N   
1284 C  CA  . ASN A 169 ? 0.7134 0.6548 0.6311 0.0263  0.1499  0.0534  393  ASN A CA  
1285 C  C   . ASN A 169 ? 0.7077 0.6488 0.6162 0.0300  0.1383  0.0484  393  ASN A C   
1286 O  O   . ASN A 169 ? 0.6135 0.5466 0.5022 0.0357  0.1374  0.0480  393  ASN A O   
1287 C  CB  . ASN A 169 ? 0.6375 0.5658 0.5379 0.0281  0.1550  0.0589  393  ASN A CB  
1288 C  CG  . ASN A 169 ? 0.6269 0.5472 0.5074 0.0345  0.1623  0.0607  393  ASN A CG  
1289 O  OD1 . ASN A 169 ? 0.5876 0.5126 0.4710 0.0365  0.1675  0.0591  393  ASN A OD1 
1290 N  ND2 . ASN A 169 ? 0.6615 0.5692 0.5211 0.0382  0.1626  0.0640  393  ASN A ND2 
1291 N  N   . SER A 170 ? 0.6636 0.6131 0.5859 0.0268  0.1295  0.0445  394  SER A N   
1292 C  CA  . SER A 170 ? 0.6673 0.6180 0.5841 0.0297  0.1194  0.0395  394  SER A CA  
1293 C  C   . SER A 170 ? 0.6421 0.6041 0.5757 0.0281  0.1173  0.0356  394  SER A C   
1294 O  O   . SER A 170 ? 0.6022 0.5716 0.5524 0.0245  0.1222  0.0366  394  SER A O   
1295 C  CB  . SER A 170 ? 0.6428 0.5912 0.5575 0.0280  0.1098  0.0387  394  SER A CB  
1296 O  OG  . SER A 170 ? 0.6605 0.5980 0.5585 0.0305  0.1109  0.0420  394  SER A OG  
1297 N  N   . SER A 171 ? 0.5728 0.5360 0.5021 0.0309  0.1098  0.0312  395  SER A N   
1298 C  CA  . SER A 171 ? 0.6133 0.5860 0.5565 0.0302  0.1076  0.0276  395  SER A CA  
1299 C  C   . SER A 171 ? 0.5709 0.5517 0.5322 0.0246  0.1023  0.0269  395  SER A C   
1300 O  O   . SER A 171 ? 0.5238 0.5028 0.4838 0.0225  0.0958  0.0269  395  SER A O   
1301 C  CB  . SER A 171 ? 0.6315 0.6024 0.5653 0.0345  0.1006  0.0231  395  SER A CB  
1302 O  OG  . SER A 171 ? 0.5289 0.4931 0.4500 0.0356  0.0937  0.0225  395  SER A OG  
1303 N  N   . ASP A 172 ? 0.5618 0.5517 0.5401 0.0224  0.1051  0.0263  396  ASP A N   
1304 C  CA  . ASP A 172 ? 0.6266 0.6242 0.6214 0.0175  0.0996  0.0253  396  ASP A CA  
1305 C  C   . ASP A 172 ? 0.5326 0.5322 0.5269 0.0185  0.0895  0.0213  396  ASP A C   
1306 O  O   . ASP A 172 ? 0.5048 0.5020 0.4903 0.0226  0.0876  0.0190  396  ASP A O   
1307 C  CB  . ASP A 172 ? 0.6535 0.6607 0.6674 0.0152  0.1046  0.0254  396  ASP A CB  
1308 C  CG  . ASP A 172 ? 0.6484 0.6611 0.6778 0.0093  0.1021  0.0261  396  ASP A CG  
1309 O  OD1 . ASP A 172 ? 0.5911 0.6073 0.6256 0.0076  0.0934  0.0237  396  ASP A OD1 
1310 O  OD2 . ASP A 172 ? 0.6734 0.6866 0.7095 0.0063  0.1089  0.0291  396  ASP A OD2 
1311 N  N   . PHE A 173 ? 0.4546 0.4582 0.4580 0.0146  0.0832  0.0207  397  PHE A N   
1312 C  CA  . PHE A 173 ? 0.3662 0.3715 0.3697 0.0148  0.0740  0.0175  397  PHE A CA  
1313 C  C   . PHE A 173 ? 0.3140 0.3264 0.3277 0.0160  0.0732  0.0151  397  PHE A C   
1314 O  O   . PHE A 173 ? 0.2881 0.3081 0.3169 0.0135  0.0747  0.0153  397  PHE A O   
1315 C  CB  . PHE A 173 ? 0.3703 0.3776 0.3803 0.0104  0.0687  0.0178  397  PHE A CB  
1316 C  CG  . PHE A 173 ? 0.3277 0.3379 0.3402 0.0100  0.0600  0.0150  397  PHE A CG  
1317 C  CD1 . PHE A 173 ? 0.3081 0.3145 0.3102 0.0131  0.0557  0.0130  397  PHE A CD1 
1318 C  CD2 . PHE A 173 ? 0.3313 0.3477 0.3564 0.0064  0.0561  0.0144  397  PHE A CD2 
1319 C  CE1 . PHE A 173 ? 0.3130 0.3219 0.3179 0.0124  0.0484  0.0108  397  PHE A CE1 
1320 C  CE2 . PHE A 173 ? 0.3324 0.3510 0.3590 0.0062  0.0487  0.0122  397  PHE A CE2 
1321 C  CZ  . PHE A 173 ? 0.3321 0.3468 0.3487 0.0091  0.0452  0.0106  397  PHE A CZ  
1322 N  N   . ASN A 174 ? 0.2927 0.3026 0.2983 0.0199  0.0711  0.0127  398  ASN A N   
1323 C  CA  . ASN A 174 ? 0.2809 0.2961 0.2943 0.0217  0.0695  0.0103  398  ASN A CA  
1324 C  C   . ASN A 174 ? 0.3005 0.3134 0.3086 0.0225  0.0610  0.0077  398  ASN A C   
1325 O  O   . ASN A 174 ? 0.2641 0.2708 0.2596 0.0257  0.0599  0.0062  398  ASN A O   
1326 C  CB  . ASN A 174 ? 0.2909 0.3044 0.2997 0.0260  0.0765  0.0098  398  ASN A CB  
1327 C  CG  . ASN A 174 ? 0.4274 0.4460 0.4447 0.0283  0.0753  0.0072  398  ASN A CG  
1328 O  OD1 . ASN A 174 ? 0.4051 0.4269 0.4285 0.0273  0.0683  0.0055  398  ASN A OD1 
1329 N  ND2 . ASN A 174 ? 0.4847 0.5038 0.5019 0.0317  0.0824  0.0069  398  ASN A ND2 
1330 N  N   . GLN A 175 ? 0.2483 0.2661 0.2660 0.0197  0.0552  0.0071  399  GLN A N   
1331 C  CA  . GLN A 175 ? 0.2835 0.2990 0.2965 0.0196  0.0476  0.0053  399  GLN A CA  
1332 C  C   . GLN A 175 ? 0.2510 0.2654 0.2619 0.0231  0.0457  0.0027  399  GLN A C   
1333 O  O   . GLN A 175 ? 0.2721 0.2828 0.2766 0.0237  0.0405  0.0011  399  GLN A O   
1334 C  CB  . GLN A 175 ? 0.2839 0.3045 0.3069 0.0159  0.0424  0.0056  399  GLN A CB  
1335 C  CG  . GLN A 175 ? 0.2302 0.2583 0.2669 0.0156  0.0420  0.0051  399  GLN A CG  
1336 C  CD  . GLN A 175 ? 0.2581 0.2893 0.3004 0.0133  0.0350  0.0047  399  GLN A CD  
1337 O  OE1 . GLN A 175 ? 0.2296 0.2571 0.2649 0.0130  0.0304  0.0041  399  GLN A OE1 
1338 N  NE2 . GLN A 175 ? 0.2020 0.2401 0.2568 0.0118  0.0343  0.0049  399  GLN A NE2 
1339 N  N   . TRP A 176 ? 0.2536 0.2710 0.2700 0.0254  0.0500  0.0022  400  TRP A N   
1340 C  CA  . TRP A 176 ? 0.2717 0.2874 0.2863 0.0290  0.0485  -0.0004 400  TRP A CA  
1341 C  C   . TRP A 176 ? 0.3038 0.3137 0.3071 0.0331  0.0532  -0.0017 400  TRP A C   
1342 O  O   . TRP A 176 ? 0.3180 0.3260 0.3195 0.0364  0.0526  -0.0042 400  TRP A O   
1343 C  CB  . TRP A 176 ? 0.2626 0.2855 0.2912 0.0295  0.0492  -0.0007 400  TRP A CB  
1344 C  CG  . TRP A 176 ? 0.2579 0.2862 0.2967 0.0260  0.0439  0.0002  400  TRP A CG  
1345 C  CD1 . TRP A 176 ? 0.2714 0.3073 0.3233 0.0240  0.0449  0.0015  400  TRP A CD1 
1346 C  CD2 . TRP A 176 ? 0.2477 0.2740 0.2840 0.0244  0.0367  -0.0003 400  TRP A CD2 
1347 N  NE1 . TRP A 176 ? 0.2213 0.2597 0.2781 0.0214  0.0384  0.0017  400  TRP A NE1 
1348 C  CE2 . TRP A 176 ? 0.2458 0.2784 0.2929 0.0216  0.0337  0.0008  400  TRP A CE2 
1349 C  CE3 . TRP A 176 ? 0.2397 0.2599 0.2662 0.0249  0.0326  -0.0016 400  TRP A CE3 
1350 C  CZ2 . TRP A 176 ? 0.2319 0.2642 0.2790 0.0197  0.0272  0.0009  400  TRP A CZ2 
1351 C  CZ3 . TRP A 176 ? 0.2315 0.2519 0.2593 0.0226  0.0264  -0.0014 400  TRP A CZ3 
1352 C  CH2 . TRP A 176 ? 0.2277 0.2538 0.2650 0.0202  0.0241  0.0000  400  TRP A CH2 
1353 N  N   . GLN A 177 ? 0.2977 0.3041 0.2927 0.0333  0.0578  -0.0001 401  GLN A N   
1354 C  CA  . GLN A 177 ? 0.3391 0.3391 0.3212 0.0376  0.0622  -0.0012 401  GLN A CA  
1355 C  C   . GLN A 177 ? 0.3151 0.3076 0.2830 0.0384  0.0572  -0.0026 401  GLN A C   
1356 O  O   . GLN A 177 ? 0.3176 0.3082 0.2813 0.0362  0.0560  -0.0007 401  GLN A O   
1357 C  CB  . GLN A 177 ? 0.2960 0.2961 0.2766 0.0380  0.0710  0.0016  401  GLN A CB  
1358 C  CG  . GLN A 177 ? 0.3633 0.3563 0.3291 0.0429  0.0760  0.0006  401  GLN A CG  
1359 C  CD  . GLN A 177 ? 0.4646 0.4567 0.4276 0.0432  0.0852  0.0040  401  GLN A CD  
1360 O  OE1 . GLN A 177 ? 0.4461 0.4424 0.4181 0.0392  0.0875  0.0071  401  GLN A OE1 
1361 N  NE2 . GLN A 177 ? 0.5887 0.5748 0.5386 0.0478  0.0907  0.0034  401  GLN A NE2 
1362 N  N   . LEU A 178 ? 0.3054 0.2937 0.2669 0.0414  0.0538  -0.0061 402  LEU A N   
1363 C  CA  . LEU A 178 ? 0.3089 0.2909 0.2587 0.0421  0.0482  -0.0080 402  LEU A CA  
1364 C  C   . LEU A 178 ? 0.3066 0.2821 0.2415 0.0450  0.0521  -0.0073 402  LEU A C   
1365 O  O   . LEU A 178 ? 0.3406 0.3144 0.2710 0.0482  0.0587  -0.0072 402  LEU A O   
1366 C  CB  . LEU A 178 ? 0.3094 0.2884 0.2569 0.0445  0.0436  -0.0123 402  LEU A CB  
1367 C  CG  . LEU A 178 ? 0.3116 0.2947 0.2710 0.0419  0.0384  -0.0130 402  LEU A CG  
1368 C  CD1 . LEU A 178 ? 0.3201 0.2990 0.2768 0.0447  0.0352  -0.0172 402  LEU A CD1 
1369 C  CD2 . LEU A 178 ? 0.2810 0.2654 0.2426 0.0378  0.0327  -0.0118 402  LEU A CD2 
1370 N  N   . PRO A 179 ? 0.3270 0.2988 0.2539 0.0441  0.0483  -0.0068 403  PRO A N   
1371 C  CA  . PRO A 179 ? 0.3184 0.2828 0.2290 0.0477  0.0507  -0.0067 403  PRO A CA  
1372 C  C   . PRO A 179 ? 0.3537 0.3125 0.2538 0.0524  0.0487  -0.0112 403  PRO A C   
1373 O  O   . PRO A 179 ? 0.3504 0.3101 0.2551 0.0522  0.0435  -0.0147 403  PRO A O   
1374 C  CB  . PRO A 179 ? 0.3373 0.2998 0.2438 0.0457  0.0451  -0.0058 403  PRO A CB  
1375 C  CG  . PRO A 179 ? 0.2877 0.2555 0.2063 0.0419  0.0386  -0.0070 403  PRO A CG  
1376 C  CD  . PRO A 179 ? 0.3065 0.2806 0.2386 0.0402  0.0415  -0.0065 403  PRO A CD  
1377 N  N   . ARG A 180 ? 0.3511 0.3035 0.2366 0.0567  0.0530  -0.0112 404  ARG A N   
1378 C  CA  . ARG A 180 ? 0.4099 0.3554 0.2821 0.0615  0.0500  -0.0159 404  ARG A CA  
1379 C  C   . ARG A 180 ? 0.3422 0.2839 0.2067 0.0612  0.0418  -0.0175 404  ARG A C   
1380 O  O   . ARG A 180 ? 0.3933 0.3300 0.2454 0.0632  0.0423  -0.0159 404  ARG A O   
1381 C  CB  . ARG A 180 ? 0.4102 0.3500 0.2684 0.0665  0.0578  -0.0152 404  ARG A CB  
1382 C  CG  . ARG A 180 ? 0.5844 0.5274 0.4490 0.0680  0.0656  -0.0151 404  ARG A CG  
1383 C  CD  . ARG A 180 ? 0.6331 0.5689 0.4810 0.0739  0.0725  -0.0156 404  ARG A CD  
1384 N  NE  . ARG A 180 ? 0.7107 0.6495 0.5647 0.0759  0.0801  -0.0161 404  ARG A NE  
1385 C  CZ  . ARG A 180 ? 0.7725 0.7085 0.6228 0.0799  0.0794  -0.0210 404  ARG A CZ  
1386 N  NH1 . ARG A 180 ? 0.6895 0.6196 0.5302 0.0821  0.0714  -0.0259 404  ARG A NH1 
1387 N  NH2 . ARG A 180 ? 0.8620 0.8015 0.7192 0.0817  0.0868  -0.0210 404  ARG A NH2 
1388 N  N   . TYR A 181 ? 0.3815 0.3256 0.2537 0.0589  0.0341  -0.0205 405  TYR A N   
1389 C  CA  . TYR A 181 ? 0.3589 0.3013 0.2278 0.0578  0.0261  -0.0219 405  TYR A CA  
1390 C  C   . TYR A 181 ? 0.3697 0.3040 0.2207 0.0628  0.0234  -0.0248 405  TYR A C   
1391 O  O   . TYR A 181 ? 0.3699 0.3023 0.2156 0.0628  0.0185  -0.0247 405  TYR A O   
1392 C  CB  . TYR A 181 ? 0.3752 0.3209 0.2550 0.0549  0.0192  -0.0252 405  TYR A CB  
1393 C  CG  . TYR A 181 ? 0.3328 0.2862 0.2292 0.0499  0.0201  -0.0223 405  TYR A CG  
1394 C  CD1 . TYR A 181 ? 0.2969 0.2540 0.1989 0.0461  0.0181  -0.0193 405  TYR A CD1 
1395 C  CD2 . TYR A 181 ? 0.3168 0.2733 0.2227 0.0492  0.0226  -0.0227 405  TYR A CD2 
1396 C  CE1 . TYR A 181 ? 0.2871 0.2508 0.2031 0.0419  0.0186  -0.0170 405  TYR A CE1 
1397 C  CE2 . TYR A 181 ? 0.3157 0.2790 0.2358 0.0451  0.0227  -0.0202 405  TYR A CE2 
1398 C  CZ  . TYR A 181 ? 0.2945 0.2612 0.2192 0.0414  0.0207  -0.0174 405  TYR A CZ  
1399 O  OH  . TYR A 181 ? 0.2728 0.2457 0.2106 0.0375  0.0207  -0.0151 405  TYR A OH  
1400 N  N   . GLY A 182 ? 0.3940 0.3233 0.2354 0.0674  0.0263  -0.0276 406  GLY A N   
1401 C  CA  . GLY A 182 ? 0.4090 0.3302 0.2324 0.0727  0.0234  -0.0309 406  GLY A CA  
1402 C  C   . GLY A 182 ? 0.4878 0.4034 0.2957 0.0768  0.0304  -0.0277 406  GLY A C   
1403 O  O   . GLY A 182 ? 0.5051 0.4130 0.2959 0.0820  0.0284  -0.0305 406  GLY A O   
1404 N  N   . GLY A 183 ? 0.4358 0.3547 0.2488 0.0748  0.0384  -0.0219 407  GLY A N   
1405 C  CA  . GLY A 183 ? 0.5389 0.4524 0.3381 0.0785  0.0464  -0.0183 407  GLY A CA  
1406 C  C   . GLY A 183 ? 0.6487 0.5606 0.4443 0.0819  0.0545  -0.0192 407  GLY A C   
1407 O  O   . GLY A 183 ? 0.6425 0.5558 0.4431 0.0826  0.0529  -0.0236 407  GLY A O   
1408 N  N   . HIS A 184 ? 0.7395 0.6481 0.5261 0.0842  0.0638  -0.0148 408  HIS A N   
1409 C  CA  . HIS A 184 ? 0.7761 0.6842 0.5608 0.0869  0.0742  -0.0139 408  HIS A CA  
1410 C  C   . HIS A 184 ? 0.7965 0.7047 0.5826 0.0896  0.0732  -0.0197 408  HIS A C   
1411 O  O   . HIS A 184 ? 0.8319 0.7465 0.6322 0.0878  0.0778  -0.0195 408  HIS A O   
1412 C  CB  . HIS A 184 ? 0.8217 0.7206 0.5850 0.0922  0.0806  -0.0113 408  HIS A CB  
1413 C  CG  . HIS A 184 ? 0.9149 0.8063 0.6621 0.0947  0.0730  -0.0120 408  HIS A CG  
1414 N  ND1 . HIS A 184 ? 1.0062 0.8936 0.7449 0.0977  0.0631  -0.0183 408  HIS A ND1 
1415 C  CD2 . HIS A 184 ? 0.9928 0.8803 0.7317 0.0947  0.0736  -0.0072 408  HIS A CD2 
1416 C  CE1 . HIS A 184 ? 1.0475 0.9293 0.7735 0.0995  0.0577  -0.0175 408  HIS A CE1 
1417 N  NE2 . HIS A 184 ? 1.0774 0.9589 0.8029 0.0979  0.0639  -0.0107 408  HIS A NE2 
1418 N  N   . LEU A 185 ? 0.6667 0.5676 0.4381 0.0941  0.0670  -0.0251 409  LEU A N   
1419 C  CA  . LEU A 185 ? 0.7071 0.6056 0.4755 0.0981  0.0678  -0.0306 409  LEU A CA  
1420 C  C   . LEU A 185 ? 0.6952 0.5978 0.4773 0.0952  0.0592  -0.0356 409  LEU A C   
1421 O  O   . LEU A 185 ? 0.6917 0.5939 0.4763 0.0974  0.0606  -0.0395 409  LEU A O   
1422 C  CB  . LEU A 185 ? 0.7550 0.6425 0.4988 0.1052  0.0665  -0.0343 409  LEU A CB  
1423 C  CG  . LEU A 185 ? 0.8046 0.6863 0.5334 0.1065  0.0626  -0.0320 409  LEU A CG  
1424 C  CD1 . LEU A 185 ? 0.7098 0.5928 0.4433 0.1038  0.0497  -0.0354 409  LEU A CD1 
1425 C  CD2 . LEU A 185 ? 0.7971 0.6677 0.4999 0.1143  0.0653  -0.0337 409  LEU A CD2 
1426 N  N   . ALA A 186 ? 0.5953 0.5015 0.3863 0.0906  0.0508  -0.0354 410  ALA A N   
1427 C  CA  . ALA A 186 ? 0.5423 0.4511 0.3446 0.0880  0.0425  -0.0401 410  ALA A CA  
1428 C  C   . ALA A 186 ? 0.5627 0.4802 0.3857 0.0835  0.0455  -0.0379 410  ALA A C   
1429 O  O   . ALA A 186 ? 0.5359 0.4597 0.3689 0.0798  0.0498  -0.0325 410  ALA A O   
1430 C  CB  . ALA A 186 ? 0.5337 0.4428 0.3372 0.0850  0.0326  -0.0409 410  ALA A CB  
1431 N  N   . ASN A 187 ? 0.5102 0.4277 0.3395 0.0841  0.0431  -0.0424 411  ASN A N   
1432 C  CA  . ASN A 187 ? 0.4783 0.4034 0.3270 0.0801  0.0436  -0.0411 411  ASN A CA  
1433 C  C   . ASN A 187 ? 0.4576 0.3864 0.3167 0.0747  0.0352  -0.0409 411  ASN A C   
1434 O  O   . ASN A 187 ? 0.4672 0.3918 0.3204 0.0748  0.0275  -0.0444 411  ASN A O   
1435 C  CB  . ASN A 187 ? 0.5417 0.4643 0.3922 0.0832  0.0439  -0.0459 411  ASN A CB  
1436 C  CG  . ASN A 187 ? 0.6676 0.5934 0.5225 0.0856  0.0537  -0.0439 411  ASN A CG  
1437 O  OD1 . ASN A 187 ? 0.7548 0.6877 0.6259 0.0828  0.0555  -0.0417 411  ASN A OD1 
1438 N  ND2 . ASN A 187 ? 0.6652 0.5858 0.5056 0.0909  0.0601  -0.0447 411  ASN A ND2 
1439 N  N   . ASN A 188 ? 0.3936 0.3303 0.2685 0.0701  0.0365  -0.0369 412  ASN A N   
1440 C  CA  . ASN A 188 ? 0.3777 0.3179 0.2628 0.0650  0.0292  -0.0366 412  ASN A CA  
1441 C  C   . ASN A 188 ? 0.3912 0.3289 0.2805 0.0652  0.0235  -0.0415 412  ASN A C   
1442 O  O   . ASN A 188 ? 0.3672 0.3031 0.2572 0.0681  0.0262  -0.0439 412  ASN A O   
1443 C  CB  . ASN A 188 ? 0.3365 0.2853 0.2367 0.0605  0.0319  -0.0315 412  ASN A CB  
1444 C  CG  . ASN A 188 ? 0.3606 0.3116 0.2582 0.0590  0.0354  -0.0268 412  ASN A CG  
1445 O  OD1 . ASN A 188 ? 0.3676 0.3140 0.2532 0.0605  0.0338  -0.0270 412  ASN A OD1 
1446 N  ND2 . ASN A 188 ? 0.3297 0.2874 0.2387 0.0561  0.0398  -0.0226 412  ASN A ND2 
1447 N  N   . ASN A 189 ? 0.3790 0.3166 0.2715 0.0620  0.0158  -0.0430 413  ASN A N   
1448 C  CA  . ASN A 189 ? 0.3916 0.3265 0.2892 0.0614  0.0104  -0.0473 413  ASN A CA  
1449 C  C   . ASN A 189 ? 0.3570 0.2962 0.2659 0.0558  0.0049  -0.0458 413  ASN A C   
1450 O  O   . ASN A 189 ? 0.3816 0.3246 0.2918 0.0531  0.0041  -0.0425 413  ASN A O   
1451 C  CB  . ASN A 189 ? 0.4301 0.3567 0.3148 0.0652  0.0062  -0.0535 413  ASN A CB  
1452 C  CG  . ASN A 189 ? 0.4728 0.3976 0.3478 0.0653  0.0018  -0.0541 413  ASN A CG  
1453 O  OD1 . ASN A 189 ? 0.4725 0.4002 0.3538 0.0613  -0.0036 -0.0535 413  ASN A OD1 
1454 N  ND2 . ASN A 189 ? 0.4613 0.3810 0.3206 0.0702  0.0041  -0.0554 413  ASN A ND2 
1455 N  N   . HIS A 190 ? 0.3777 0.3158 0.2947 0.0543  0.0015  -0.0480 414  HIS A N   
1456 C  CA  . HIS A 190 ? 0.3824 0.3238 0.3104 0.0492  -0.0032 -0.0468 414  HIS A CA  
1457 C  C   . HIS A 190 ? 0.3146 0.2636 0.2518 0.0458  -0.0001 -0.0408 414  HIS A C   
1458 O  O   . HIS A 190 ? 0.2942 0.2467 0.2370 0.0418  -0.0031 -0.0388 414  HIS A O   
1459 C  CB  . HIS A 190 ? 0.3600 0.2997 0.2839 0.0477  -0.0095 -0.0493 414  HIS A CB  
1460 C  CG  . HIS A 190 ? 0.4704 0.4027 0.3868 0.0505  -0.0138 -0.0557 414  HIS A CG  
1461 N  ND1 . HIS A 190 ? 0.4596 0.3875 0.3619 0.0547  -0.0144 -0.0587 414  HIS A ND1 
1462 C  CD2 . HIS A 190 ? 0.4585 0.3866 0.3792 0.0499  -0.0177 -0.0599 414  HIS A CD2 
1463 C  CE1 . HIS A 190 ? 0.4999 0.4214 0.3981 0.0566  -0.0190 -0.0648 414  HIS A CE1 
1464 N  NE2 . HIS A 190 ? 0.5095 0.4310 0.4192 0.0535  -0.0210 -0.0657 414  HIS A NE2 
1465 N  N   . LEU A 191 ? 0.3197 0.2715 0.2593 0.0475  0.0059  -0.0382 415  LEU A N   
1466 C  CA  . LEU A 191 ? 0.3056 0.2646 0.2540 0.0446  0.0087  -0.0330 415  LEU A CA  
1467 C  C   . LEU A 191 ? 0.3493 0.3107 0.3095 0.0416  0.0063  -0.0317 415  LEU A C   
1468 O  O   . LEU A 191 ? 0.2756 0.2339 0.2386 0.0430  0.0055  -0.0338 415  LEU A O   
1469 C  CB  . LEU A 191 ? 0.3326 0.2940 0.2809 0.0474  0.0158  -0.0311 415  LEU A CB  
1470 C  CG  . LEU A 191 ? 0.3651 0.3246 0.3022 0.0503  0.0201  -0.0310 415  LEU A CG  
1471 C  CD1 . LEU A 191 ? 0.3415 0.3024 0.2797 0.0536  0.0273  -0.0302 415  LEU A CD1 
1472 C  CD2 . LEU A 191 ? 0.2854 0.2487 0.2224 0.0473  0.0204  -0.0271 415  LEU A CD2 
1473 N  N   . ALA A 192 ? 0.2745 0.2412 0.2412 0.0377  0.0052  -0.0280 416  ALA A N   
1474 C  CA  . ALA A 192 ? 0.3147 0.2843 0.2919 0.0355  0.0043  -0.0258 416  ALA A CA  
1475 C  C   . ALA A 192 ? 0.2888 0.2607 0.2703 0.0383  0.0089  -0.0247 416  ALA A C   
1476 O  O   . ALA A 192 ? 0.3183 0.2924 0.2971 0.0402  0.0134  -0.0239 416  ALA A O   
1477 C  CB  . ALA A 192 ? 0.2478 0.2228 0.2301 0.0314  0.0031  -0.0221 416  ALA A CB  
1478 N  N   . PRO A 193 ? 0.2959 0.2669 0.2840 0.0388  0.0079  -0.0248 417  PRO A N   
1479 C  CA  . PRO A 193 ? 0.2757 0.2487 0.2680 0.0422  0.0120  -0.0244 417  PRO A CA  
1480 C  C   . PRO A 193 ? 0.3128 0.2939 0.3128 0.0408  0.0145  -0.0203 417  PRO A C   
1481 O  O   . PRO A 193 ? 0.2965 0.2812 0.2999 0.0371  0.0123  -0.0176 417  PRO A O   
1482 C  CB  . PRO A 193 ? 0.3082 0.2773 0.3053 0.0430  0.0093  -0.0255 417  PRO A CB  
1483 C  CG  . PRO A 193 ? 0.3439 0.3124 0.3431 0.0386  0.0045  -0.0240 417  PRO A CG  
1484 C  CD  . PRO A 193 ? 0.3340 0.3016 0.3257 0.0369  0.0034  -0.0254 417  PRO A CD  
1485 N  N   . ALA A 194 ? 0.3239 0.3078 0.3271 0.0439  0.0191  -0.0202 418  ALA A N   
1486 C  CA  . ALA A 194 ? 0.3418 0.3338 0.3545 0.0431  0.0214  -0.0169 418  ALA A CA  
1487 C  C   . ALA A 194 ? 0.3102 0.3040 0.3315 0.0419  0.0174  -0.0151 418  ALA A C   
1488 O  O   . ALA A 194 ? 0.3215 0.3102 0.3426 0.0432  0.0147  -0.0165 418  ALA A O   
1489 C  CB  . ALA A 194 ? 0.2508 0.2451 0.2657 0.0471  0.0274  -0.0177 418  ALA A CB  
1490 N  N   . VAL A 195 ? 0.2840 0.2846 0.3125 0.0396  0.0169  -0.0120 419  VAL A N   
1491 C  CA  . VAL A 195 ? 0.3143 0.3168 0.3499 0.0386  0.0130  -0.0100 419  VAL A CA  
1492 C  C   . VAL A 195 ? 0.3325 0.3426 0.3784 0.0401  0.0149  -0.0085 419  VAL A C   
1493 O  O   . VAL A 195 ? 0.2863 0.3016 0.3347 0.0398  0.0187  -0.0081 419  VAL A O   
1494 C  CB  . VAL A 195 ? 0.2883 0.2915 0.3226 0.0342  0.0091  -0.0079 419  VAL A CB  
1495 C  CG1 . VAL A 195 ? 0.3227 0.3190 0.3487 0.0327  0.0069  -0.0095 419  VAL A CG1 
1496 C  CG2 . VAL A 195 ? 0.2797 0.2887 0.3151 0.0317  0.0110  -0.0064 419  VAL A CG2 
1497 N  N   . SER A 196 ? 0.3359 0.3466 0.3880 0.0418  0.0121  -0.0076 420  SER A N   
1498 C  CA  . SER A 196 ? 0.3944 0.4129 0.4575 0.0433  0.0127  -0.0064 420  SER A CA  
1499 C  C   . SER A 196 ? 0.3875 0.4051 0.4546 0.0441  0.0075  -0.0047 420  SER A C   
1500 O  O   . SER A 196 ? 0.3609 0.3710 0.4233 0.0450  0.0052  -0.0051 420  SER A O   
1501 C  CB  . SER A 196 ? 0.3913 0.4114 0.4582 0.0477  0.0178  -0.0084 420  SER A CB  
1502 O  OG  . SER A 196 ? 0.4216 0.4341 0.4839 0.0510  0.0176  -0.0106 420  SER A OG  
1503 N  N   . PRO A 197 ? 0.3453 0.3699 0.4210 0.0439  0.0055  -0.0028 421  PRO A N   
1504 C  CA  . PRO A 197 ? 0.3576 0.3811 0.4364 0.0454  0.0005  -0.0010 421  PRO A CA  
1505 C  C   . PRO A 197 ? 0.3800 0.4011 0.4627 0.0507  0.0013  -0.0023 421  PRO A C   
1506 O  O   . PRO A 197 ? 0.3848 0.4103 0.4735 0.0535  0.0054  -0.0040 421  PRO A O   
1507 C  CB  . PRO A 197 ? 0.2727 0.3053 0.3601 0.0443  -0.0016 0.0005  421  PRO A CB  
1508 C  CG  . PRO A 197 ? 0.3449 0.3842 0.4381 0.0443  0.0036  -0.0010 421  PRO A CG  
1509 C  CD  . PRO A 197 ? 0.3453 0.3792 0.4290 0.0428  0.0078  -0.0024 421  PRO A CD  
1510 N  N   . LEU A 198 ? 0.4044 0.4182 0.4838 0.0521  -0.0021 -0.0015 422  LEU A N   
1511 C  CA  . LEU A 198 ? 0.4823 0.4926 0.5648 0.0573  -0.0016 -0.0027 422  LEU A CA  
1512 C  C   . LEU A 198 ? 0.4746 0.4873 0.5644 0.0604  -0.0058 -0.0004 422  LEU A C   
1513 O  O   . LEU A 198 ? 0.5310 0.5446 0.6272 0.0653  -0.0050 -0.0015 422  LEU A O   
1514 C  CB  . LEU A 198 ? 0.5634 0.5622 0.6370 0.0574  -0.0019 -0.0038 422  LEU A CB  
1515 C  CG  . LEU A 198 ? 0.6214 0.6183 0.6880 0.0550  0.0020  -0.0066 422  LEU A CG  
1516 C  CD1 . LEU A 198 ? 0.6383 0.6244 0.6966 0.0544  0.0012  -0.0083 422  LEU A CD1 
1517 C  CD2 . LEU A 198 ? 0.5644 0.5661 0.6349 0.0582  0.0073  -0.0092 422  LEU A CD2 
1518 N  N   . PHE A 199 ? 0.3797 0.3936 0.4686 0.0581  -0.0103 0.0025  423  PHE A N   
1519 C  CA  . PHE A 199 ? 0.3545 0.3700 0.4488 0.0613  -0.0150 0.0048  423  PHE A CA  
1520 C  C   . PHE A 199 ? 0.3237 0.3513 0.4291 0.0621  -0.0155 0.0045  423  PHE A C   
1521 O  O   . PHE A 199 ? 0.2786 0.3120 0.3845 0.0581  -0.0146 0.0043  423  PHE A O   
1522 C  CB  . PHE A 199 ? 0.3154 0.3256 0.4022 0.0587  -0.0195 0.0081  423  PHE A CB  
1523 C  CG  . PHE A 199 ? 0.3405 0.3488 0.4294 0.0625  -0.0245 0.0108  423  PHE A CG  
1524 C  CD1 . PHE A 199 ? 0.3842 0.3846 0.4726 0.0668  -0.0248 0.0111  423  PHE A CD1 
1525 C  CD2 . PHE A 199 ? 0.3104 0.3241 0.4013 0.0622  -0.0291 0.0130  423  PHE A CD2 
1526 C  CE1 . PHE A 199 ? 0.3877 0.3858 0.4775 0.0708  -0.0295 0.0139  423  PHE A CE1 
1527 C  CE2 . PHE A 199 ? 0.3429 0.3545 0.4348 0.0662  -0.0341 0.0156  423  PHE A CE2 
1528 C  CZ  . PHE A 199 ? 0.3461 0.3497 0.4374 0.0706  -0.0342 0.0163  423  PHE A CZ  
1529 N  N   . PRO A 200 ? 0.3523 0.3840 0.4673 0.0672  -0.0170 0.0043  424  PRO A N   
1530 C  CA  . PRO A 200 ? 0.3226 0.3667 0.4501 0.0679  -0.0175 0.0036  424  PRO A CA  
1531 C  C   . PRO A 200 ? 0.3254 0.3740 0.4526 0.0644  -0.0224 0.0055  424  PRO A C   
1532 O  O   . PRO A 200 ? 0.2757 0.3187 0.3956 0.0641  -0.0273 0.0081  424  PRO A O   
1533 C  CB  . PRO A 200 ? 0.2989 0.3447 0.4353 0.0745  -0.0198 0.0036  424  PRO A CB  
1534 C  CG  . PRO A 200 ? 0.3445 0.3798 0.4746 0.0773  -0.0173 0.0029  424  PRO A CG  
1535 C  CD  . PRO A 200 ? 0.3417 0.3672 0.4576 0.0727  -0.0174 0.0041  424  PRO A CD  
1536 N  N   . GLY A 201 ? 0.2746 0.3332 0.4099 0.0619  -0.0208 0.0042  425  GLY A N   
1537 C  CA  . GLY A 201 ? 0.2437 0.3073 0.3797 0.0584  -0.0251 0.0052  425  GLY A CA  
1538 C  C   . GLY A 201 ? 0.2944 0.3537 0.4193 0.0527  -0.0238 0.0058  425  GLY A C   
1539 O  O   . GLY A 201 ? 0.2122 0.2752 0.3371 0.0496  -0.0270 0.0064  425  GLY A O   
1540 N  N   . GLU A 202 ? 0.2310 0.2826 0.3467 0.0513  -0.0195 0.0055  426  GLU A N   
1541 C  CA  . GLU A 202 ? 0.2404 0.2877 0.3458 0.0463  -0.0185 0.0061  426  GLU A CA  
1542 C  C   . GLU A 202 ? 0.2188 0.2695 0.3254 0.0434  -0.0126 0.0041  426  GLU A C   
1543 O  O   . GLU A 202 ? 0.2093 0.2621 0.3209 0.0455  -0.0079 0.0024  426  GLU A O   
1544 C  CB  . GLU A 202 ? 0.2196 0.2558 0.3135 0.0463  -0.0186 0.0071  426  GLU A CB  
1545 C  CG  . GLU A 202 ? 0.2645 0.2959 0.3541 0.0476  -0.0242 0.0100  426  GLU A CG  
1546 C  CD  . GLU A 202 ? 0.3563 0.3766 0.4355 0.0471  -0.0239 0.0113  426  GLU A CD  
1547 O  OE1 . GLU A 202 ? 0.2674 0.2839 0.3418 0.0448  -0.0200 0.0098  426  GLU A OE1 
1548 O  OE2 . GLU A 202 ? 0.3080 0.3233 0.3839 0.0490  -0.0277 0.0139  426  GLU A OE2 
1549 N  N   . GLN A 203 ? 0.2052 0.2558 0.3065 0.0388  -0.0126 0.0045  427  GLN A N   
1550 C  CA  . GLN A 203 ? 0.2282 0.2801 0.3282 0.0358  -0.0073 0.0032  427  GLN A CA  
1551 C  C   . GLN A 203 ? 0.2083 0.2533 0.2961 0.0324  -0.0074 0.0038  427  GLN A C   
1552 O  O   . GLN A 203 ? 0.2078 0.2493 0.2902 0.0314  -0.0117 0.0054  427  GLN A O   
1553 C  CB  . GLN A 203 ? 0.2086 0.2696 0.3178 0.0335  -0.0069 0.0028  427  GLN A CB  
1554 C  CG  . GLN A 203 ? 0.2518 0.3209 0.3749 0.0366  -0.0059 0.0018  427  GLN A CG  
1555 C  CD  . GLN A 203 ? 0.2910 0.3693 0.4247 0.0338  -0.0052 0.0011  427  GLN A CD  
1556 O  OE1 . GLN A 203 ? 0.2369 0.3224 0.3827 0.0355  -0.0025 0.0001  427  GLN A OE1 
1557 N  NE2 . GLN A 203 ? 0.2267 0.3047 0.3563 0.0295  -0.0074 0.0016  427  GLN A NE2 
1558 N  N   . ILE A 204 ? 0.2134 0.2562 0.2967 0.0310  -0.0027 0.0027  428  ILE A N   
1559 C  CA  . ILE A 204 ? 0.2254 0.2628 0.2984 0.0277  -0.0029 0.0030  428  ILE A CA  
1560 C  C   . ILE A 204 ? 0.2320 0.2733 0.3058 0.0241  -0.0052 0.0040  428  ILE A C   
1561 O  O   . ILE A 204 ? 0.1909 0.2389 0.2725 0.0233  -0.0045 0.0037  428  ILE A O   
1562 C  CB  . ILE A 204 ? 0.2152 0.2497 0.2832 0.0274  0.0022  0.0015  428  ILE A CB  
1563 C  CG1 . ILE A 204 ? 0.2819 0.3108 0.3469 0.0309  0.0035  0.0002  428  ILE A CG1 
1564 C  CG2 . ILE A 204 ? 0.2120 0.2426 0.2710 0.0239  0.0018  0.0017  428  ILE A CG2 
1565 C  CD1 . ILE A 204 ? 0.3050 0.3307 0.3641 0.0313  0.0081  -0.0017 428  ILE A CD1 
1566 N  N   . LEU A 205 ? 0.2174 0.2543 0.2835 0.0220  -0.0080 0.0050  429  LEU A N   
1567 C  CA  . LEU A 205 ? 0.2012 0.2402 0.2657 0.0186  -0.0098 0.0056  429  LEU A CA  
1568 C  C   . LEU A 205 ? 0.2269 0.2629 0.2849 0.0161  -0.0065 0.0049  429  LEU A C   
1569 O  O   . LEU A 205 ? 0.2355 0.2658 0.2864 0.0161  -0.0061 0.0047  429  LEU A O   
1570 C  CB  . LEU A 205 ? 0.2331 0.2690 0.2927 0.0182  -0.0144 0.0072  429  LEU A CB  
1571 C  CG  . LEU A 205 ? 0.2511 0.2882 0.3076 0.0150  -0.0166 0.0076  429  LEU A CG  
1572 C  CD1 . LEU A 205 ? 0.2373 0.2812 0.3017 0.0150  -0.0190 0.0072  429  LEU A CD1 
1573 C  CD2 . LEU A 205 ? 0.2771 0.3093 0.3263 0.0149  -0.0197 0.0094  429  LEU A CD2 
1574 N  N   . PHE A 206 ? 0.1956 0.2354 0.2565 0.0141  -0.0044 0.0044  430  PHE A N   
1575 C  CA  . PHE A 206 ? 0.2045 0.2416 0.2594 0.0121  -0.0014 0.0040  430  PHE A CA  
1576 C  C   . PHE A 206 ? 0.2009 0.2382 0.2530 0.0090  -0.0037 0.0045  430  PHE A C   
1577 O  O   . PHE A 206 ? 0.2128 0.2538 0.2693 0.0080  -0.0067 0.0048  430  PHE A O   
1578 C  CB  . PHE A 206 ? 0.2123 0.2523 0.2714 0.0122  0.0035  0.0034  430  PHE A CB  
1579 C  CG  . PHE A 206 ? 0.2559 0.2956 0.3170 0.0155  0.0068  0.0026  430  PHE A CG  
1580 C  CD1 . PHE A 206 ? 0.2240 0.2582 0.2772 0.0168  0.0095  0.0018  430  PHE A CD1 
1581 C  CD2 . PHE A 206 ? 0.2592 0.3042 0.3301 0.0174  0.0071  0.0025  430  PHE A CD2 
1582 C  CE1 . PHE A 206 ? 0.2152 0.2488 0.2697 0.0202  0.0127  0.0007  430  PHE A CE1 
1583 C  CE2 . PHE A 206 ? 0.2269 0.2717 0.2999 0.0208  0.0105  0.0016  430  PHE A CE2 
1584 C  CZ  . PHE A 206 ? 0.2531 0.2918 0.3174 0.0222  0.0135  0.0007  430  PHE A CZ  
1585 N  N   . PHE A 207 ? 0.1815 0.2148 0.2263 0.0076  -0.0025 0.0043  431  PHE A N   
1586 C  CA  . PHE A 207 ? 0.1889 0.2219 0.2305 0.0049  -0.0038 0.0045  431  PHE A CA  
1587 C  C   . PHE A 207 ? 0.1796 0.2131 0.2215 0.0038  0.0000  0.0041  431  PHE A C   
1588 O  O   . PHE A 207 ? 0.2020 0.2319 0.2386 0.0045  0.0027  0.0038  431  PHE A O   
1589 C  CB  . PHE A 207 ? 0.1842 0.2126 0.2181 0.0044  -0.0054 0.0046  431  PHE A CB  
1590 C  CG  . PHE A 207 ? 0.2177 0.2451 0.2513 0.0054  -0.0085 0.0054  431  PHE A CG  
1591 C  CD1 . PHE A 207 ? 0.2231 0.2481 0.2568 0.0076  -0.0082 0.0054  431  PHE A CD1 
1592 C  CD2 . PHE A 207 ? 0.2213 0.2497 0.2544 0.0043  -0.0117 0.0063  431  PHE A CD2 
1593 C  CE1 . PHE A 207 ? 0.1915 0.2149 0.2249 0.0086  -0.0109 0.0066  431  PHE A CE1 
1594 C  CE2 . PHE A 207 ? 0.2274 0.2542 0.2593 0.0055  -0.0143 0.0075  431  PHE A CE2 
1595 C  CZ  . PHE A 207 ? 0.2349 0.2591 0.2672 0.0075  -0.0138 0.0078  431  PHE A CZ  
1596 N  N   . ARG A 208 ? 0.1785 0.2160 0.2265 0.0021  0.0000  0.0042  432  ARG A N   
1597 C  CA  . ARG A 208 ? 0.1795 0.2178 0.2300 0.0010  0.0043  0.0043  432  ARG A CA  
1598 C  C   . ARG A 208 ? 0.1964 0.2325 0.2428 -0.0015 0.0041  0.0044  432  ARG A C   
1599 O  O   . ARG A 208 ? 0.2011 0.2380 0.2479 -0.0031 0.0005  0.0040  432  ARG A O   
1600 C  CB  . ARG A 208 ? 0.1918 0.2363 0.2536 0.0006  0.0050  0.0041  432  ARG A CB  
1601 C  CG  . ARG A 208 ? 0.2153 0.2612 0.2815 -0.0015 0.0091  0.0044  432  ARG A CG  
1602 C  CD  . ARG A 208 ? 0.2179 0.2707 0.2971 -0.0014 0.0106  0.0041  432  ARG A CD  
1603 N  NE  . ARG A 208 ? 0.2055 0.2589 0.2860 0.0015  0.0146  0.0043  432  ARG A NE  
1604 C  CZ  . ARG A 208 ? 0.2064 0.2648 0.2968 0.0019  0.0185  0.0043  432  ARG A CZ  
1605 N  NH1 . ARG A 208 ? 0.2285 0.2924 0.3299 -0.0007 0.0185  0.0040  432  ARG A NH1 
1606 N  NH2 . ARG A 208 ? 0.1989 0.2567 0.2885 0.0049  0.0227  0.0044  432  ARG A NH2 
1607 N  N   . SER A 209 ? 0.1879 0.2207 0.2300 -0.0016 0.0080  0.0048  433  SER A N   
1608 C  CA  . SER A 209 ? 0.1937 0.2241 0.2329 -0.0037 0.0085  0.0051  433  SER A CA  
1609 C  C   . SER A 209 ? 0.2135 0.2446 0.2572 -0.0048 0.0133  0.0059  433  SER A C   
1610 O  O   . SER A 209 ? 0.2010 0.2329 0.2465 -0.0032 0.0171  0.0064  433  SER A O   
1611 C  CB  . SER A 209 ? 0.2050 0.2300 0.2340 -0.0028 0.0085  0.0052  433  SER A CB  
1612 O  OG  . SER A 209 ? 0.2174 0.2419 0.2433 -0.0023 0.0045  0.0045  433  SER A OG  
1613 N  N   . PHE A 210 ? 0.2126 0.2431 0.2580 -0.0074 0.0134  0.0061  434  PHE A N   
1614 C  CA  . PHE A 210 ? 0.2321 0.2622 0.2813 -0.0088 0.0185  0.0073  434  PHE A CA  
1615 C  C   . PHE A 210 ? 0.2287 0.2519 0.2679 -0.0085 0.0204  0.0084  434  PHE A C   
1616 O  O   . PHE A 210 ? 0.2437 0.2644 0.2808 -0.0101 0.0184  0.0081  434  PHE A O   
1617 C  CB  . PHE A 210 ? 0.2297 0.2638 0.2893 -0.0121 0.0171  0.0066  434  PHE A CB  
1618 C  CG  . PHE A 210 ? 0.2485 0.2895 0.3176 -0.0120 0.0140  0.0053  434  PHE A CG  
1619 C  CD1 . PHE A 210 ? 0.2133 0.2587 0.2899 -0.0109 0.0172  0.0056  434  PHE A CD1 
1620 C  CD2 . PHE A 210 ? 0.2140 0.2571 0.2842 -0.0126 0.0078  0.0037  434  PHE A CD2 
1621 C  CE1 . PHE A 210 ? 0.2349 0.2868 0.3206 -0.0103 0.0139  0.0044  434  PHE A CE1 
1622 C  CE2 . PHE A 210 ? 0.2335 0.2826 0.3116 -0.0120 0.0045  0.0026  434  PHE A CE2 
1623 C  CZ  . PHE A 210 ? 0.2043 0.2579 0.2904 -0.0108 0.0073  0.0030  434  PHE A CZ  
1624 N  N   . ILE A 211 ? 0.2362 0.2558 0.2684 -0.0060 0.0240  0.0094  435  ILE A N   
1625 C  CA  . ILE A 211 ? 0.2200 0.2329 0.2415 -0.0049 0.0248  0.0103  435  ILE A CA  
1626 C  C   . ILE A 211 ? 0.2314 0.2414 0.2544 -0.0068 0.0290  0.0121  435  ILE A C   
1627 O  O   . ILE A 211 ? 0.2224 0.2357 0.2542 -0.0086 0.0325  0.0128  435  ILE A O   
1628 C  CB  . ILE A 211 ? 0.2337 0.2433 0.2464 -0.0012 0.0266  0.0105  435  ILE A CB  
1629 C  CG1 . ILE A 211 ? 0.2520 0.2612 0.2658 -0.0003 0.0331  0.0120  435  ILE A CG1 
1630 C  CG2 . ILE A 211 ? 0.2413 0.2537 0.2544 0.0003  0.0226  0.0086  435  ILE A CG2 
1631 C  CD1 . ILE A 211 ? 0.2763 0.2804 0.2788 0.0036  0.0352  0.0122  435  ILE A CD1 
1632 N  N   . PRO A 212 ? 0.2282 0.2323 0.2436 -0.0067 0.0289  0.0129  436  PRO A N   
1633 C  CA  . PRO A 212 ? 0.2293 0.2296 0.2457 -0.0086 0.0329  0.0149  436  PRO A CA  
1634 C  C   . PRO A 212 ? 0.2415 0.2393 0.2558 -0.0074 0.0399  0.0174  436  PRO A C   
1635 O  O   . PRO A 212 ? 0.2540 0.2499 0.2606 -0.0040 0.0414  0.0178  436  PRO A O   
1636 C  CB  . PRO A 212 ? 0.2265 0.2205 0.2334 -0.0075 0.0306  0.0152  436  PRO A CB  
1637 C  CG  . PRO A 212 ? 0.2694 0.2666 0.2756 -0.0068 0.0243  0.0126  436  PRO A CG  
1638 C  CD  . PRO A 212 ? 0.2441 0.2455 0.2517 -0.0052 0.0242  0.0118  436  PRO A CD  
1639 N  N   . GLY A 213 ? 0.2426 0.2401 0.2638 -0.0102 0.0444  0.0191  437  GLY A N   
1640 C  CA  . GLY A 213 ? 0.2641 0.2580 0.2828 -0.0095 0.0520  0.0221  437  GLY A CA  
1641 C  C   . GLY A 213 ? 0.2713 0.2564 0.2821 -0.0097 0.0544  0.0247  437  GLY A C   
1642 O  O   . GLY A 213 ? 0.3115 0.2950 0.3254 -0.0122 0.0517  0.0242  437  GLY A O   
1643 N  N   . ALA A 214 ? 0.2888 0.2676 0.2887 -0.0066 0.0592  0.0273  438  ALA A N   
1644 C  CA  . ALA A 214 ? 0.3101 0.2796 0.3012 -0.0061 0.0621  0.0304  438  ALA A CA  
1645 C  C   . ALA A 214 ? 0.3252 0.2921 0.3211 -0.0085 0.0707  0.0339  438  ALA A C   
1646 O  O   . ALA A 214 ? 0.3392 0.2986 0.3314 -0.0095 0.0732  0.0366  438  ALA A O   
1647 C  CB  . ALA A 214 ? 0.3781 0.3410 0.3524 -0.0008 0.0617  0.0313  438  ALA A CB  
1648 N  N   . SER A 215 ? 0.3457 0.3186 0.3503 -0.0095 0.0753  0.0340  439  SER A N   
1649 C  CA  . SER A 215 ? 0.3501 0.3213 0.3603 -0.0118 0.0843  0.0375  439  SER A CA  
1650 C  C   . SER A 215 ? 0.3836 0.3644 0.4063 -0.0128 0.0873  0.0362  439  SER A C   
1651 O  O   . SER A 215 ? 0.3577 0.3435 0.3792 -0.0101 0.0838  0.0335  439  SER A O   
1652 C  CB  . SER A 215 ? 0.3936 0.3548 0.3881 -0.0082 0.0907  0.0417  439  SER A CB  
1653 O  OG  . SER A 215 ? 0.4527 0.4117 0.4528 -0.0108 0.1000  0.0454  439  SER A OG  
1654 N  N   . GLY A 216 ? 0.3970 0.3802 0.4320 -0.0166 0.0939  0.0380  440  GLY A N   
1655 C  CA  . GLY A 216 ? 0.3438 0.3365 0.3921 -0.0175 0.0973  0.0369  440  GLY A CA  
1656 C  C   . GLY A 216 ? 0.3238 0.3268 0.3865 -0.0199 0.0896  0.0325  440  GLY A C   
1657 O  O   . GLY A 216 ? 0.3397 0.3424 0.4026 -0.0213 0.0820  0.0303  440  GLY A O   
1658 N  N   . HIS A 217 ? 0.2731 0.2850 0.3475 -0.0199 0.0917  0.0312  441  HIS A N   
1659 C  CA  . HIS A 217 ? 0.2962 0.3184 0.3849 -0.0217 0.0850  0.0273  441  HIS A CA  
1660 C  C   . HIS A 217 ? 0.3366 0.3614 0.4185 -0.0171 0.0801  0.0250  441  HIS A C   
1661 O  O   . HIS A 217 ? 0.3213 0.3470 0.3999 -0.0138 0.0848  0.0256  441  HIS A O   
1662 C  CB  . HIS A 217 ? 0.3293 0.3603 0.4371 -0.0246 0.0901  0.0272  441  HIS A CB  
1663 C  CG  . HIS A 217 ? 0.3653 0.3941 0.4819 -0.0296 0.0955  0.0295  441  HIS A CG  
1664 N  ND1 . HIS A 217 ? 0.3710 0.4041 0.5020 -0.0345 0.0911  0.0274  441  HIS A ND1 
1665 C  CD2 . HIS A 217 ? 0.3908 0.4131 0.5037 -0.0303 0.1051  0.0337  441  HIS A CD2 
1666 C  CE1 . HIS A 217 ? 0.4583 0.4876 0.5949 -0.0385 0.0976  0.0301  441  HIS A CE1 
1667 N  NE2 . HIS A 217 ? 0.4690 0.4917 0.5948 -0.0360 0.1064  0.0342  441  HIS A NE2 
1668 N  N   . THR A 218 ? 0.3350 0.3609 0.4150 -0.0170 0.0711  0.0222  442  THR A N   
1669 C  CA  . THR A 218 ? 0.2857 0.3145 0.3614 -0.0134 0.0661  0.0199  442  THR A CA  
1670 C  C   . THR A 218 ? 0.3133 0.3455 0.3928 -0.0149 0.0569  0.0170  442  THR A C   
1671 O  O   . THR A 218 ? 0.3158 0.3442 0.3925 -0.0171 0.0537  0.0170  442  THR A O   
1672 C  CB  . THR A 218 ? 0.3281 0.3490 0.3854 -0.0090 0.0667  0.0209  442  THR A CB  
1673 O  OG1 . THR A 218 ? 0.3519 0.3754 0.4061 -0.0060 0.0615  0.0184  442  THR A OG1 
1674 C  CG2 . THR A 218 ? 0.2529 0.2658 0.2994 -0.0097 0.0637  0.0217  442  THR A CG2 
1675 N  N   . ASN A 219 ? 0.2783 0.3172 0.3638 -0.0135 0.0527  0.0148  443  ASN A N   
1676 C  CA  . ASN A 219 ? 0.2937 0.3346 0.3796 -0.0141 0.0441  0.0124  443  ASN A CA  
1677 C  C   . ASN A 219 ? 0.2840 0.3198 0.3555 -0.0109 0.0403  0.0119  443  ASN A C   
1678 O  O   . ASN A 219 ? 0.2473 0.2841 0.3177 -0.0111 0.0337  0.0102  443  ASN A O   
1679 C  CB  . ASN A 219 ? 0.3306 0.3806 0.4296 -0.0141 0.0408  0.0103  443  ASN A CB  
1680 C  CG  . ASN A 219 ? 0.4329 0.4888 0.5478 -0.0181 0.0418  0.0098  443  ASN A CG  
1681 O  OD1 . ASN A 219 ? 0.4422 0.4972 0.5594 -0.0213 0.0383  0.0089  443  ASN A OD1 
1682 N  ND2 . ASN A 219 ? 0.3500 0.4117 0.4761 -0.0180 0.0468  0.0102  443  ASN A ND2 
1683 N  N   . GLY A 220 ? 0.3052 0.3354 0.3657 -0.0080 0.0444  0.0134  444  GLY A N   
1684 C  CA  . GLY A 220 ? 0.2830 0.3079 0.3302 -0.0054 0.0408  0.0128  444  GLY A CA  
1685 C  C   . GLY A 220 ? 0.2294 0.2577 0.2771 -0.0035 0.0356  0.0107  444  GLY A C   
1686 O  O   . GLY A 220 ? 0.2394 0.2649 0.2798 -0.0027 0.0309  0.0098  444  GLY A O   
1687 N  N   . GLU A 221 ? 0.2329 0.2670 0.2896 -0.0026 0.0365  0.0100  445  GLU A N   
1688 C  CA  . GLU A 221 ? 0.2201 0.2574 0.2786 -0.0010 0.0313  0.0083  445  GLU A CA  
1689 C  C   . GLU A 221 ? 0.2147 0.2471 0.2620 0.0025  0.0308  0.0078  445  GLU A C   
1690 O  O   . GLU A 221 ? 0.2435 0.2739 0.2871 0.0049  0.0355  0.0081  445  GLU A O   
1691 C  CB  . GLU A 221 ? 0.2453 0.2901 0.3168 -0.0006 0.0323  0.0077  445  GLU A CB  
1692 C  CG  . GLU A 221 ? 0.2721 0.3227 0.3555 -0.0040 0.0293  0.0071  445  GLU A CG  
1693 C  CD  . GLU A 221 ? 0.4225 0.4796 0.5197 -0.0050 0.0340  0.0074  445  GLU A CD  
1694 O  OE1 . GLU A 221 ? 0.5016 0.5582 0.5984 -0.0031 0.0403  0.0083  445  GLU A OE1 
1695 O  OE2 . GLU A 221 ? 0.4311 0.4937 0.5397 -0.0077 0.0313  0.0065  445  GLU A OE2 
1696 N  N   . MET A 222 ? 0.2254 0.2559 0.2675 0.0026  0.0253  0.0068  446  MET A N   
1697 C  CA  . MET A 222 ? 0.2034 0.2294 0.2361 0.0054  0.0239  0.0059  446  MET A CA  
1698 C  C   . MET A 222 ? 0.2034 0.2315 0.2387 0.0058  0.0186  0.0048  446  MET A C   
1699 O  O   . MET A 222 ? 0.2245 0.2527 0.2594 0.0040  0.0144  0.0047  446  MET A O   
1700 C  CB  . MET A 222 ? 0.2525 0.2728 0.2749 0.0051  0.0230  0.0062  446  MET A CB  
1701 C  CG  . MET A 222 ? 0.2115 0.2273 0.2248 0.0076  0.0210  0.0049  446  MET A CG  
1702 S  SD  . MET A 222 ? 0.3287 0.3406 0.3348 0.0113  0.0261  0.0046  446  MET A SD  
1703 C  CE  . MET A 222 ? 0.3483 0.3563 0.3485 0.0106  0.0303  0.0068  446  MET A CE  
1704 N  N   . ASP A 223 ? 0.2143 0.2432 0.2514 0.0084  0.0191  0.0040  447  ASP A N   
1705 C  CA  . ASP A 223 ? 0.1902 0.2207 0.2304 0.0091  0.0147  0.0033  447  ASP A CA  
1706 C  C   . ASP A 223 ? 0.2440 0.2692 0.2758 0.0109  0.0129  0.0023  447  ASP A C   
1707 O  O   . ASP A 223 ? 0.2211 0.2433 0.2486 0.0133  0.0156  0.0014  447  ASP A O   
1708 C  CB  . ASP A 223 ? 0.2055 0.2407 0.2547 0.0109  0.0161  0.0031  447  ASP A CB  
1709 C  CG  . ASP A 223 ? 0.2324 0.2738 0.2919 0.0089  0.0171  0.0038  447  ASP A CG  
1710 O  OD1 . ASP A 223 ? 0.2464 0.2892 0.3075 0.0064  0.0135  0.0041  447  ASP A OD1 
1711 O  OD2 . ASP A 223 ? 0.2513 0.2961 0.3173 0.0098  0.0215  0.0039  447  ASP A OD2 
1712 N  N   . CYS A 224 ? 0.2006 0.2245 0.2303 0.0097  0.0085  0.0023  448  CYS A N   
1713 C  CA  . CYS A 224 ? 0.1981 0.2175 0.2221 0.0110  0.0066  0.0012  448  CYS A CA  
1714 C  C   . CYS A 224 ? 0.2193 0.2395 0.2473 0.0118  0.0036  0.0014  448  CYS A C   
1715 O  O   . CYS A 224 ? 0.2183 0.2424 0.2522 0.0110  0.0019  0.0025  448  CYS A O   
1716 C  CB  . CYS A 224 ? 0.2093 0.2257 0.2269 0.0094  0.0046  0.0010  448  CYS A CB  
1717 S  SG  . CYS A 224 ? 0.2556 0.2741 0.2752 0.0065  0.0007  0.0022  448  CYS A SG  
1718 N  N   . LEU A 225 ? 0.1931 0.2091 0.2178 0.0134  0.0028  0.0003  449  LEU A N   
1719 C  CA  . LEU A 225 ? 0.2164 0.2319 0.2443 0.0146  0.0004  0.0006  449  LEU A CA  
1720 C  C   . LEU A 225 ? 0.2272 0.2411 0.2533 0.0125  -0.0031 0.0017  449  LEU A C   
1721 O  O   . LEU A 225 ? 0.2270 0.2412 0.2560 0.0129  -0.0053 0.0029  449  LEU A O   
1722 C  CB  . LEU A 225 ? 0.1987 0.2097 0.2242 0.0172  0.0013  -0.0012 449  LEU A CB  
1723 C  CG  . LEU A 225 ? 0.2745 0.2863 0.3010 0.0200  0.0053  -0.0024 449  LEU A CG  
1724 C  CD1 . LEU A 225 ? 0.2168 0.2230 0.2392 0.0226  0.0057  -0.0046 449  LEU A CD1 
1725 C  CD2 . LEU A 225 ? 0.2566 0.2738 0.2918 0.0211  0.0062  -0.0013 449  LEU A CD2 
1726 N  N   . LEU A 226 ? 0.2083 0.2204 0.2296 0.0105  -0.0036 0.0013  450  LEU A N   
1727 C  CA  . LEU A 226 ? 0.1939 0.2046 0.2134 0.0085  -0.0061 0.0022  450  LEU A CA  
1728 C  C   . LEU A 226 ? 0.2100 0.2221 0.2268 0.0064  -0.0059 0.0022  450  LEU A C   
1729 O  O   . LEU A 226 ? 0.2630 0.2740 0.2766 0.0067  -0.0045 0.0009  450  LEU A O   
1730 C  CB  . LEU A 226 ? 0.2299 0.2357 0.2467 0.0088  -0.0070 0.0011  450  LEU A CB  
1731 C  CG  . LEU A 226 ? 0.3144 0.3170 0.3331 0.0106  -0.0075 0.0010  450  LEU A CG  
1732 C  CD1 . LEU A 226 ? 0.3329 0.3305 0.3490 0.0102  -0.0083 -0.0008 450  LEU A CD1 
1733 C  CD2 . LEU A 226 ? 0.3014 0.3046 0.3227 0.0103  -0.0093 0.0036  450  LEU A CD2 
1734 N  N   . PRO A 227 ? 0.2460 0.2601 0.2633 0.0046  -0.0074 0.0035  451  PRO A N   
1735 C  CA  . PRO A 227 ? 0.2807 0.2953 0.2951 0.0028  -0.0074 0.0032  451  PRO A CA  
1736 C  C   . PRO A 227 ? 0.2687 0.2801 0.2796 0.0025  -0.0077 0.0020  451  PRO A C   
1737 O  O   . PRO A 227 ? 0.2071 0.2161 0.2182 0.0027  -0.0085 0.0019  451  PRO A O   
1738 C  CB  . PRO A 227 ? 0.2554 0.2718 0.2705 0.0014  -0.0092 0.0047  451  PRO A CB  
1739 C  CG  . PRO A 227 ? 0.2651 0.2807 0.2820 0.0024  -0.0105 0.0059  451  PRO A CG  
1740 C  CD  . PRO A 227 ? 0.2519 0.2674 0.2716 0.0045  -0.0094 0.0052  451  PRO A CD  
1741 N  N   . GLN A 228 ? 0.2660 0.2774 0.2740 0.0020  -0.0072 0.0011  452  GLN A N   
1742 C  CA  . GLN A 228 ? 0.2272 0.2363 0.2327 0.0020  -0.0079 -0.0004 452  GLN A CA  
1743 C  C   . GLN A 228 ? 0.2444 0.2532 0.2511 0.0003  -0.0094 0.0001  452  GLN A C   
1744 O  O   . GLN A 228 ? 0.2296 0.2364 0.2365 0.0002  -0.0102 -0.0012 452  GLN A O   
1745 C  CB  . GLN A 228 ? 0.2510 0.2602 0.2532 0.0020  -0.0075 -0.0011 452  GLN A CB  
1746 C  CG  . GLN A 228 ? 0.2638 0.2710 0.2634 0.0025  -0.0088 -0.0031 452  GLN A CG  
1747 C  CD  . GLN A 228 ? 0.3016 0.3059 0.2994 0.0044  -0.0090 -0.0049 452  GLN A CD  
1748 O  OE1 . GLN A 228 ? 0.2981 0.3017 0.2959 0.0057  -0.0074 -0.0046 452  GLN A OE1 
1749 N  NE2 . GLN A 228 ? 0.3166 0.3192 0.3133 0.0047  -0.0110 -0.0071 452  GLN A NE2 
1750 N  N   . GLU A 229 ? 0.2145 0.2253 0.2223 -0.0009 -0.0096 0.0018  453  GLU A N   
1751 C  CA  . GLU A 229 ? 0.2225 0.2329 0.2310 -0.0024 -0.0101 0.0027  453  GLU A CA  
1752 C  C   . GLU A 229 ? 0.2143 0.2220 0.2244 -0.0021 -0.0105 0.0035  453  GLU A C   
1753 O  O   . GLU A 229 ? 0.2209 0.2270 0.2320 -0.0033 -0.0105 0.0036  453  GLU A O   
1754 C  CB  . GLU A 229 ? 0.2707 0.2830 0.2783 -0.0033 -0.0102 0.0043  453  GLU A CB  
1755 C  CG  . GLU A 229 ? 0.2632 0.2774 0.2692 -0.0039 -0.0099 0.0035  453  GLU A CG  
1756 C  CD  . GLU A 229 ? 0.2765 0.2916 0.2822 -0.0032 -0.0096 0.0029  453  GLU A CD  
1757 O  OE1 . GLU A 229 ? 0.2310 0.2464 0.2383 -0.0023 -0.0094 0.0034  453  GLU A OE1 
1758 O  OE2 . GLU A 229 ? 0.2643 0.2798 0.2684 -0.0034 -0.0092 0.0021  453  GLU A OE2 
1759 N  N   . PHE A 230 ? 0.2000 0.2072 0.2111 -0.0006 -0.0105 0.0040  454  PHE A N   
1760 C  CA  . PHE A 230 ? 0.2359 0.2398 0.2485 0.0001  -0.0108 0.0046  454  PHE A CA  
1761 C  C   . PHE A 230 ? 0.2145 0.2155 0.2273 0.0003  -0.0109 0.0021  454  PHE A C   
1762 O  O   . PHE A 230 ? 0.2583 0.2562 0.2725 -0.0006 -0.0113 0.0021  454  PHE A O   
1763 C  CB  . PHE A 230 ? 0.2189 0.2232 0.2330 0.0022  -0.0109 0.0054  454  PHE A CB  
1764 C  CG  . PHE A 230 ? 0.2567 0.2631 0.2711 0.0022  -0.0119 0.0078  454  PHE A CG  
1765 C  CD1 . PHE A 230 ? 0.2828 0.2909 0.2951 0.0006  -0.0122 0.0088  454  PHE A CD1 
1766 C  CD2 . PHE A 230 ? 0.3324 0.3391 0.3491 0.0042  -0.0127 0.0088  454  PHE A CD2 
1767 C  CE1 . PHE A 230 ? 0.2802 0.2897 0.2917 0.0009  -0.0135 0.0106  454  PHE A CE1 
1768 C  CE2 . PHE A 230 ? 0.3128 0.3213 0.3294 0.0046  -0.0143 0.0107  454  PHE A CE2 
1769 C  CZ  . PHE A 230 ? 0.3055 0.3153 0.3192 0.0029  -0.0148 0.0115  454  PHE A CZ  
1770 N  N   . VAL A 231 ? 0.2301 0.2318 0.2414 0.0014  -0.0106 0.0000  455  VAL A N   
1771 C  CA  . VAL A 231 ? 0.2220 0.2209 0.2324 0.0020  -0.0113 -0.0029 455  VAL A CA  
1772 C  C   . VAL A 231 ? 0.2486 0.2473 0.2601 -0.0001 -0.0124 -0.0037 455  VAL A C   
1773 O  O   . VAL A 231 ? 0.2261 0.2220 0.2396 -0.0007 -0.0134 -0.0052 455  VAL A O   
1774 C  CB  . VAL A 231 ? 0.2375 0.2371 0.2444 0.0038  -0.0106 -0.0046 455  VAL A CB  
1775 C  CG1 . VAL A 231 ? 0.2586 0.2553 0.2634 0.0046  -0.0120 -0.0079 455  VAL A CG1 
1776 C  CG2 . VAL A 231 ? 0.2480 0.2479 0.2549 0.0060  -0.0089 -0.0040 455  VAL A CG2 
1777 N  N   . GLN A 232 ? 0.2308 0.2328 0.2419 -0.0013 -0.0122 -0.0030 456  GLN A N   
1778 C  CA  . GLN A 232 ? 0.2625 0.2653 0.2757 -0.0033 -0.0129 -0.0038 456  GLN A CA  
1779 C  C   . GLN A 232 ? 0.2476 0.2489 0.2643 -0.0052 -0.0123 -0.0021 456  GLN A C   
1780 O  O   . GLN A 232 ? 0.2821 0.2823 0.3022 -0.0067 -0.0130 -0.0035 456  GLN A O   
1781 C  CB  . GLN A 232 ? 0.2289 0.2352 0.2408 -0.0038 -0.0124 -0.0032 456  GLN A CB  
1782 C  CG  . GLN A 232 ? 0.2491 0.2562 0.2573 -0.0020 -0.0126 -0.0044 456  GLN A CG  
1783 C  CD  . GLN A 232 ? 0.2799 0.2897 0.2869 -0.0025 -0.0121 -0.0035 456  GLN A CD  
1784 O  OE1 . GLN A 232 ? 0.3156 0.3268 0.3227 -0.0033 -0.0111 -0.0015 456  GLN A OE1 
1785 N  NE2 . GLN A 232 ? 0.3350 0.3454 0.3407 -0.0018 -0.0130 -0.0052 456  GLN A NE2 
1786 N  N   . HIS A 233 ? 0.2508 0.2520 0.2667 -0.0052 -0.0112 0.0009  457  HIS A N   
1787 C  CA  . HIS A 233 ? 0.2479 0.2470 0.2658 -0.0068 -0.0103 0.0032  457  HIS A CA  
1788 C  C   . HIS A 233 ? 0.2551 0.2495 0.2754 -0.0068 -0.0108 0.0025  457  HIS A C   
1789 O  O   . HIS A 233 ? 0.2680 0.2604 0.2918 -0.0088 -0.0103 0.0027  457  HIS A O   
1790 C  CB  . HIS A 233 ? 0.2950 0.2945 0.3102 -0.0061 -0.0096 0.0064  457  HIS A CB  
1791 C  CG  . HIS A 233 ? 0.3148 0.3117 0.3302 -0.0074 -0.0084 0.0094  457  HIS A CG  
1792 N  ND1 . HIS A 233 ? 0.3258 0.3240 0.3413 -0.0094 -0.0068 0.0105  457  HIS A ND1 
1793 C  CD2 . HIS A 233 ? 0.3241 0.3168 0.3394 -0.0069 -0.0083 0.0117  457  HIS A CD2 
1794 C  CE1 . HIS A 233 ? 0.4128 0.4076 0.4278 -0.0101 -0.0054 0.0135  457  HIS A CE1 
1795 N  NE2 . HIS A 233 ? 0.3413 0.3325 0.3559 -0.0086 -0.0065 0.0144  457  HIS A NE2 
1796 N  N   . PHE A 234 ? 0.2657 0.2582 0.2848 -0.0044 -0.0116 0.0016  458  PHE A N   
1797 C  CA  . PHE A 234 ? 0.2631 0.2505 0.2842 -0.0040 -0.0122 0.0005  458  PHE A CA  
1798 C  C   . PHE A 234 ? 0.2759 0.2623 0.2995 -0.0052 -0.0134 -0.0031 458  PHE A C   
1799 O  O   . PHE A 234 ? 0.2507 0.2333 0.2780 -0.0068 -0.0137 -0.0036 458  PHE A O   
1800 C  CB  . PHE A 234 ? 0.2439 0.2302 0.2632 -0.0008 -0.0125 -0.0003 458  PHE A CB  
1801 C  CG  . PHE A 234 ? 0.2453 0.2330 0.2635 0.0006  -0.0119 0.0028  458  PHE A CG  
1802 C  CD1 . PHE A 234 ? 0.2375 0.2252 0.2556 -0.0007 -0.0114 0.0062  458  PHE A CD1 
1803 C  CD2 . PHE A 234 ? 0.2748 0.2641 0.2921 0.0032  -0.0117 0.0022  458  PHE A CD2 
1804 C  CE1 . PHE A 234 ? 0.3101 0.2991 0.3269 0.0009  -0.0116 0.0087  458  PHE A CE1 
1805 C  CE2 . PHE A 234 ? 0.2546 0.2460 0.2721 0.0045  -0.0116 0.0047  458  PHE A CE2 
1806 C  CZ  . PHE A 234 ? 0.2433 0.2345 0.2605 0.0034  -0.0120 0.0078  458  PHE A CZ  
1807 N  N   . TYR A 235 ? 0.2719 0.2614 0.2938 -0.0046 -0.0144 -0.0056 459  TYR A N   
1808 C  CA  . TYR A 235 ? 0.2828 0.2720 0.3069 -0.0055 -0.0163 -0.0093 459  TYR A CA  
1809 C  C   . TYR A 235 ? 0.2552 0.2457 0.2849 -0.0089 -0.0159 -0.0085 459  TYR A C   
1810 O  O   . TYR A 235 ? 0.2750 0.2631 0.3093 -0.0105 -0.0171 -0.0107 459  TYR A O   
1811 C  CB  . TYR A 235 ? 0.3004 0.2928 0.3206 -0.0038 -0.0174 -0.0113 459  TYR A CB  
1812 C  CG  . TYR A 235 ? 0.3254 0.3174 0.3467 -0.0038 -0.0202 -0.0155 459  TYR A CG  
1813 C  CD1 . TYR A 235 ? 0.3428 0.3306 0.3624 -0.0021 -0.0220 -0.0188 459  TYR A CD1 
1814 C  CD2 . TYR A 235 ? 0.2969 0.2927 0.3207 -0.0052 -0.0213 -0.0165 459  TYR A CD2 
1815 C  CE1 . TYR A 235 ? 0.3886 0.3757 0.4085 -0.0018 -0.0253 -0.0230 459  TYR A CE1 
1816 C  CE2 . TYR A 235 ? 0.4031 0.3988 0.4282 -0.0048 -0.0246 -0.0206 459  TYR A CE2 
1817 C  CZ  . TYR A 235 ? 0.3695 0.3607 0.3924 -0.0031 -0.0268 -0.0239 459  TYR A CZ  
1818 O  OH  . TYR A 235 ? 0.5235 0.5144 0.5471 -0.0025 -0.0307 -0.0284 459  TYR A OH  
1819 N  N   . GLN A 236 ? 0.2530 0.2470 0.2825 -0.0100 -0.0140 -0.0056 460  GLN A N   
1820 C  CA  . GLN A 236 ? 0.3077 0.3032 0.3425 -0.0131 -0.0127 -0.0046 460  GLN A CA  
1821 C  C   . GLN A 236 ? 0.3401 0.3308 0.3783 -0.0149 -0.0113 -0.0026 460  GLN A C   
1822 O  O   . GLN A 236 ? 0.3154 0.3053 0.3599 -0.0175 -0.0112 -0.0037 460  GLN A O   
1823 C  CB  . GLN A 236 ? 0.2954 0.2949 0.3281 -0.0135 -0.0106 -0.0018 460  GLN A CB  
1824 C  CG  . GLN A 236 ? 0.3223 0.3266 0.3537 -0.0125 -0.0117 -0.0038 460  GLN A CG  
1825 C  CD  . GLN A 236 ? 0.3333 0.3399 0.3707 -0.0139 -0.0132 -0.0070 460  GLN A CD  
1826 O  OE1 . GLN A 236 ? 0.3254 0.3328 0.3688 -0.0165 -0.0118 -0.0064 460  GLN A OE1 
1827 N  NE2 . GLN A 236 ? 0.3053 0.3127 0.3411 -0.0120 -0.0161 -0.0103 460  GLN A NE2 
1828 N  N   . GLU A 237 ? 0.3042 0.2915 0.3387 -0.0136 -0.0103 0.0003  461  GLU A N   
1829 C  CA  . GLU A 237 ? 0.3570 0.3394 0.3935 -0.0151 -0.0084 0.0034  461  GLU A CA  
1830 C  C   . GLU A 237 ? 0.3598 0.3365 0.4000 -0.0154 -0.0098 0.0011  461  GLU A C   
1831 O  O   . GLU A 237 ? 0.3706 0.3437 0.4155 -0.0181 -0.0084 0.0022  461  GLU A O   
1832 C  CB  . GLU A 237 ? 0.3568 0.3377 0.3879 -0.0131 -0.0074 0.0074  461  GLU A CB  
1833 C  CG  . GLU A 237 ? 0.3742 0.3592 0.4018 -0.0134 -0.0057 0.0101  461  GLU A CG  
1834 C  CD  . GLU A 237 ? 0.5071 0.4917 0.5375 -0.0164 -0.0028 0.0123  461  GLU A CD  
1835 O  OE1 . GLU A 237 ? 0.5894 0.5690 0.6193 -0.0170 -0.0009 0.0158  461  GLU A OE1 
1836 O  OE2 . GLU A 237 ? 0.4868 0.4759 0.5201 -0.0180 -0.0021 0.0108  461  GLU A OE2 
1837 N  N   . ALA A 238 ? 0.3408 0.3162 0.3787 -0.0128 -0.0122 -0.0020 462  ALA A N   
1838 C  CA  . ALA A 238 ? 0.3707 0.3400 0.4110 -0.0125 -0.0136 -0.0044 462  ALA A CA  
1839 C  C   . ALA A 238 ? 0.3978 0.3609 0.4392 -0.0132 -0.0118 -0.0007 462  ALA A C   
1840 O  O   . ALA A 238 ? 0.3807 0.3386 0.4269 -0.0152 -0.0118 -0.0015 462  ALA A O   
1841 C  CB  . ALA A 238 ? 0.4144 0.3837 0.4606 -0.0149 -0.0156 -0.0088 462  ALA A CB  
1842 N  N   . ALA A 239 ? 0.3437 0.3071 0.3806 -0.0114 -0.0103 0.0035  463  ALA A N   
1843 C  CA  . ALA A 239 ? 0.4044 0.3618 0.4410 -0.0114 -0.0087 0.0077  463  ALA A CA  
1844 C  C   . ALA A 239 ? 0.4116 0.3632 0.4475 -0.0085 -0.0101 0.0064  463  ALA A C   
1845 O  O   . ALA A 239 ? 0.4390 0.3928 0.4724 -0.0055 -0.0117 0.0039  463  ALA A O   
1846 C  CB  . ALA A 239 ? 0.3878 0.3477 0.4193 -0.0101 -0.0073 0.0124  463  ALA A CB  
1847 N  N   . THR A 240 ? 0.3808 0.3249 0.4189 -0.0093 -0.0093 0.0083  464  THR A N   
1848 C  CA  . THR A 240 ? 0.4271 0.3650 0.4648 -0.0063 -0.0106 0.0070  464  THR A CA  
1849 C  C   . THR A 240 ? 0.3411 0.2794 0.3741 -0.0023 -0.0106 0.0104  464  THR A C   
1850 O  O   . THR A 240 ? 0.3766 0.3147 0.4072 -0.0025 -0.0093 0.0153  464  THR A O   
1851 C  CB  . THR A 240 ? 0.5182 0.4470 0.5602 -0.0084 -0.0099 0.0077  464  THR A CB  
1852 O  OG1 . THR A 240 ? 0.6156 0.5419 0.6568 -0.0101 -0.0072 0.0137  464  THR A OG1 
1853 C  CG2 . THR A 240 ? 0.4544 0.3832 0.5024 -0.0122 -0.0107 0.0033  464  THR A CG2 
1854 N  N   . ALA A 241 ? 0.2828 0.2219 0.3144 0.0015  -0.0121 0.0078  465  ALA A N   
1855 C  CA  . ALA A 241 ? 0.3766 0.3163 0.4055 0.0055  -0.0124 0.0105  465  ALA A CA  
1856 C  C   . ALA A 241 ? 0.3417 0.2723 0.3715 0.0069  -0.0123 0.0130  465  ALA A C   
1857 O  O   . ALA A 241 ? 0.3770 0.3018 0.4089 0.0080  -0.0129 0.0101  465  ALA A O   
1858 C  CB  . ALA A 241 ? 0.3219 0.2658 0.3502 0.0089  -0.0134 0.0068  465  ALA A CB  
1859 N  N   . ARG A 242 ? 0.3307 0.2593 0.3581 0.0071  -0.0116 0.0184  466  ARG A N   
1860 C  CA  . ARG A 242 ? 0.3059 0.2252 0.3332 0.0086  -0.0114 0.0217  466  ARG A CA  
1861 C  C   . ARG A 242 ? 0.3714 0.2891 0.3984 0.0140  -0.0132 0.0213  466  ARG A C   
1862 O  O   . ARG A 242 ? 0.3265 0.2357 0.3541 0.0159  -0.0133 0.0229  466  ARG A O   
1863 C  CB  . ARG A 242 ? 0.3261 0.2438 0.3495 0.0074  -0.0101 0.0278  466  ARG A CB  
1864 C  CG  . ARG A 242 ? 0.3395 0.2591 0.3637 0.0022  -0.0077 0.0284  466  ARG A CG  
1865 C  CD  . ARG A 242 ? 0.4658 0.3769 0.4943 -0.0010 -0.0060 0.0282  466  ARG A CD  
1866 N  NE  . ARG A 242 ? 0.4430 0.3446 0.4690 0.0003  -0.0050 0.0335  466  ARG A NE  
1867 C  CZ  . ARG A 242 ? 0.4693 0.3611 0.4987 -0.0008 -0.0041 0.0339  466  ARG A CZ  
1868 N  NH1 . ARG A 242 ? 0.4626 0.3526 0.4982 -0.0031 -0.0046 0.0287  466  ARG A NH1 
1869 N  NH2 . ARG A 242 ? 0.4754 0.3583 0.5014 0.0006  -0.0028 0.0395  466  ARG A NH2 
1870 N  N   . SER A 243 ? 0.3476 0.2734 0.3743 0.0166  -0.0143 0.0193  467  SER A N   
1871 C  CA  . SER A 243 ? 0.3684 0.2943 0.3964 0.0218  -0.0156 0.0182  467  SER A CA  
1872 C  C   . SER A 243 ? 0.3425 0.2770 0.3716 0.0226  -0.0155 0.0138  467  SER A C   
1873 O  O   . SER A 243 ? 0.3526 0.2916 0.3810 0.0194  -0.0148 0.0119  467  SER A O   
1874 C  CB  . SER A 243 ? 0.3037 0.2303 0.3297 0.0251  -0.0170 0.0229  467  SER A CB  
1875 O  OG  . SER A 243 ? 0.2691 0.2048 0.2934 0.0244  -0.0175 0.0239  467  SER A OG  
1876 N  N   . GLU A 244 ? 0.3521 0.2888 0.3831 0.0271  -0.0161 0.0124  468  GLU A N   
1877 C  CA  . GLU A 244 ? 0.3535 0.2977 0.3856 0.0281  -0.0154 0.0086  468  GLU A CA  
1878 C  C   . GLU A 244 ? 0.3192 0.2730 0.3510 0.0275  -0.0156 0.0102  468  GLU A C   
1879 O  O   . GLU A 244 ? 0.3058 0.2658 0.3381 0.0274  -0.0146 0.0074  468  GLU A O   
1880 C  CB  . GLU A 244 ? 0.3662 0.3094 0.4012 0.0332  -0.0151 0.0062  468  GLU A CB  
1881 C  CG  . GLU A 244 ? 0.4474 0.3820 0.4823 0.0339  -0.0146 0.0027  468  GLU A CG  
1882 C  CD  . GLU A 244 ? 0.5867 0.5223 0.6194 0.0312  -0.0137 -0.0018 468  GLU A CD  
1883 O  OE1 . GLU A 244 ? 0.6682 0.6102 0.7004 0.0324  -0.0125 -0.0043 468  GLU A OE1 
1884 O  OE2 . GLU A 244 ? 0.6525 0.5826 0.6843 0.0278  -0.0142 -0.0028 468  GLU A OE2 
1885 N  N   . VAL A 245 ? 0.2853 0.2399 0.3159 0.0274  -0.0170 0.0145  469  VAL A N   
1886 C  CA  . VAL A 245 ? 0.2513 0.2145 0.2818 0.0271  -0.0178 0.0158  469  VAL A CA  
1887 C  C   . VAL A 245 ? 0.2492 0.2113 0.2754 0.0241  -0.0184 0.0194  469  VAL A C   
1888 O  O   . VAL A 245 ? 0.2662 0.2223 0.2903 0.0247  -0.0192 0.0229  469  VAL A O   
1889 C  CB  . VAL A 245 ? 0.2882 0.2551 0.3222 0.0316  -0.0195 0.0169  469  VAL A CB  
1890 C  CG1 . VAL A 245 ? 0.2394 0.2147 0.2735 0.0307  -0.0208 0.0180  469  VAL A CG1 
1891 C  CG2 . VAL A 245 ? 0.2566 0.2254 0.2953 0.0347  -0.0182 0.0132  469  VAL A CG2 
1892 N  N   . ALA A 246 ? 0.2380 0.2058 0.2627 0.0211  -0.0178 0.0188  470  ALA A N   
1893 C  CA  . ALA A 246 ? 0.2379 0.2064 0.2585 0.0188  -0.0183 0.0220  470  ALA A CA  
1894 C  C   . ALA A 246 ? 0.2360 0.2105 0.2567 0.0210  -0.0206 0.0233  470  ALA A C   
1895 O  O   . ALA A 246 ? 0.2623 0.2439 0.2861 0.0213  -0.0207 0.0209  470  ALA A O   
1896 C  CB  . ALA A 246 ? 0.2322 0.2034 0.2513 0.0146  -0.0166 0.0203  470  ALA A CB  
1897 N  N   . LEU A 247 ? 0.2423 0.2139 0.2599 0.0228  -0.0226 0.0271  471  LEU A N   
1898 C  CA  . LEU A 247 ? 0.2416 0.2187 0.2590 0.0249  -0.0256 0.0281  471  LEU A CA  
1899 C  C   . LEU A 247 ? 0.2496 0.2305 0.2627 0.0217  -0.0255 0.0285  471  LEU A C   
1900 O  O   . LEU A 247 ? 0.2536 0.2302 0.2612 0.0196  -0.0241 0.0307  471  LEU A O   
1901 C  CB  . LEU A 247 ? 0.2512 0.2233 0.2658 0.0285  -0.0283 0.0320  471  LEU A CB  
1902 C  CG  . LEU A 247 ? 0.2523 0.2295 0.2660 0.0310  -0.0324 0.0332  471  LEU A CG  
1903 C  CD1 . LEU A 247 ? 0.2475 0.2322 0.2697 0.0337  -0.0342 0.0303  471  LEU A CD1 
1904 C  CD2 . LEU A 247 ? 0.2637 0.2342 0.2716 0.0342  -0.0350 0.0377  471  LEU A CD2 
1905 N  N   . LEU A 248 ? 0.2311 0.2198 0.2471 0.0215  -0.0265 0.0262  472  LEU A N   
1906 C  CA  . LEU A 248 ? 0.2366 0.2292 0.2492 0.0188  -0.0266 0.0258  472  LEU A CA  
1907 C  C   . LEU A 248 ? 0.2725 0.2692 0.2845 0.0209  -0.0306 0.0266  472  LEU A C   
1908 O  O   . LEU A 248 ? 0.2577 0.2573 0.2750 0.0240  -0.0330 0.0261  472  LEU A O   
1909 C  CB  . LEU A 248 ? 0.2278 0.2257 0.2442 0.0163  -0.0244 0.0222  472  LEU A CB  
1910 C  CG  . LEU A 248 ? 0.3175 0.3129 0.3320 0.0130  -0.0211 0.0211  472  LEU A CG  
1911 C  CD1 . LEU A 248 ? 0.2481 0.2364 0.2620 0.0131  -0.0197 0.0221  472  LEU A CD1 
1912 C  CD2 . LEU A 248 ? 0.2392 0.2392 0.2575 0.0119  -0.0195 0.0176  472  LEU A CD2 
1913 N  N   . ARG A 249 ? 0.2421 0.2393 0.2481 0.0194  -0.0314 0.0276  473  ARG A N   
1914 C  CA  . ARG A 249 ? 0.2521 0.2530 0.2564 0.0212  -0.0357 0.0278  473  ARG A CA  
1915 C  C   . ARG A 249 ? 0.2758 0.2817 0.2794 0.0182  -0.0354 0.0254  473  ARG A C   
1916 O  O   . ARG A 249 ? 0.2522 0.2559 0.2509 0.0155  -0.0326 0.0257  473  ARG A O   
1917 C  CB  . ARG A 249 ? 0.2631 0.2581 0.2585 0.0232  -0.0377 0.0318  473  ARG A CB  
1918 C  CG  . ARG A 249 ? 0.2951 0.2931 0.2879 0.0259  -0.0432 0.0320  473  ARG A CG  
1919 C  CD  . ARG A 249 ? 0.2693 0.2601 0.2517 0.0286  -0.0449 0.0363  473  ARG A CD  
1920 N  NE  . ARG A 249 ? 0.3409 0.3267 0.3250 0.0317  -0.0454 0.0389  473  ARG A NE  
1921 C  CZ  . ARG A 249 ? 0.3264 0.3035 0.3027 0.0331  -0.0444 0.0433  473  ARG A CZ  
1922 N  NH1 . ARG A 249 ? 0.3051 0.2776 0.2709 0.0319  -0.0426 0.0459  473  ARG A NH1 
1923 N  NH2 . ARG A 249 ? 0.3376 0.3102 0.3167 0.0359  -0.0447 0.0451  473  ARG A NH2 
1924 N  N   . PHE A 250 ? 0.2581 0.2706 0.2673 0.0187  -0.0381 0.0230  474  PHE A N   
1925 C  CA  . PHE A 250 ? 0.2676 0.2844 0.2766 0.0161  -0.0382 0.0206  474  PHE A CA  
1926 C  C   . PHE A 250 ? 0.2579 0.2742 0.2598 0.0171  -0.0422 0.0214  474  PHE A C   
1927 O  O   . PHE A 250 ? 0.2420 0.2601 0.2453 0.0200  -0.0469 0.0217  474  PHE A O   
1928 C  CB  . PHE A 250 ? 0.2362 0.2600 0.2554 0.0157  -0.0386 0.0175  474  PHE A CB  
1929 C  CG  . PHE A 250 ? 0.2508 0.2779 0.2708 0.0124  -0.0373 0.0150  474  PHE A CG  
1930 C  CD1 . PHE A 250 ? 0.2364 0.2624 0.2562 0.0099  -0.0328 0.0141  474  PHE A CD1 
1931 C  CD2 . PHE A 250 ? 0.2722 0.3032 0.2930 0.0121  -0.0410 0.0133  474  PHE A CD2 
1932 C  CE1 . PHE A 250 ? 0.2633 0.2918 0.2836 0.0072  -0.0317 0.0120  474  PHE A CE1 
1933 C  CE2 . PHE A 250 ? 0.2209 0.2542 0.2426 0.0091  -0.0397 0.0110  474  PHE A CE2 
1934 C  CZ  . PHE A 250 ? 0.2428 0.2746 0.2641 0.0068  -0.0350 0.0106  474  PHE A CZ  
1935 N  N   . VAL A 251 ? 0.2308 0.2445 0.2248 0.0152  -0.0406 0.0218  475  VAL A N   
1936 C  CA  . VAL A 251 ? 0.2466 0.2584 0.2317 0.0165  -0.0439 0.0227  475  VAL A CA  
1937 C  C   . VAL A 251 ? 0.2681 0.2828 0.2513 0.0141  -0.0439 0.0199  475  VAL A C   
1938 O  O   . VAL A 251 ? 0.2351 0.2507 0.2205 0.0112  -0.0401 0.0184  475  VAL A O   
1939 C  CB  . VAL A 251 ? 0.3115 0.3157 0.2862 0.0175  -0.0419 0.0268  475  VAL A CB  
1940 C  CG1 . VAL A 251 ? 0.3443 0.3448 0.3213 0.0197  -0.0415 0.0297  475  VAL A CG1 
1941 C  CG2 . VAL A 251 ? 0.3238 0.3259 0.2955 0.0141  -0.0364 0.0269  475  VAL A CG2 
1942 N  N   . ASN A 252 ? 0.2675 0.2831 0.2462 0.0156  -0.0487 0.0190  476  ASN A N   
1943 C  CA  . ASN A 252 ? 0.3289 0.3462 0.3046 0.0138  -0.0494 0.0161  476  ASN A CA  
1944 C  C   . ASN A 252 ? 0.3081 0.3197 0.2705 0.0144  -0.0480 0.0181  476  ASN A C   
1945 O  O   . ASN A 252 ? 0.2781 0.2867 0.2324 0.0174  -0.0515 0.0199  476  ASN A O   
1946 C  CB  . ASN A 252 ? 0.3726 0.3946 0.3521 0.0150  -0.0558 0.0132  476  ASN A CB  
1947 C  CG  . ASN A 252 ? 0.3816 0.4050 0.3586 0.0130  -0.0569 0.0097  476  ASN A CG  
1948 O  OD1 . ASN A 252 ? 0.3834 0.4044 0.3559 0.0110  -0.0527 0.0096  476  ASN A OD1 
1949 N  ND2 . ASN A 252 ? 0.3843 0.4117 0.3650 0.0137  -0.0627 0.0067  476  ASN A ND2 
1950 N  N   . PRO A 253 ? 0.3832 0.3931 0.3428 0.0119  -0.0430 0.0180  477  PRO A N   
1951 C  CA  . PRO A 253 ? 0.3453 0.3500 0.2928 0.0125  -0.0407 0.0202  477  PRO A CA  
1952 C  C   . PRO A 253 ? 0.4111 0.4153 0.3500 0.0139  -0.0445 0.0182  477  PRO A C   
1953 O  O   . PRO A 253 ? 0.4616 0.4610 0.3888 0.0156  -0.0437 0.0205  477  PRO A O   
1954 C  CB  . PRO A 253 ? 0.3280 0.3326 0.2776 0.0093  -0.0347 0.0196  477  PRO A CB  
1955 C  CG  . PRO A 253 ? 0.4112 0.4213 0.3709 0.0073  -0.0355 0.0160  477  PRO A CG  
1956 C  CD  . PRO A 253 ? 0.3782 0.3910 0.3454 0.0087  -0.0392 0.0159  477  PRO A CD  
1957 N  N   . ASP A 254 ? 0.3843 0.3932 0.3285 0.0131  -0.0484 0.0141  478  ASP A N   
1958 C  CA  . ASP A 254 ? 0.4558 0.4639 0.3919 0.0145  -0.0526 0.0116  478  ASP A CA  
1959 C  C   . ASP A 254 ? 0.4810 0.4864 0.4089 0.0185  -0.0577 0.0135  478  ASP A C   
1960 O  O   . ASP A 254 ? 0.4914 0.4929 0.4067 0.0206  -0.0592 0.0137  478  ASP A O   
1961 C  CB  . ASP A 254 ? 0.4685 0.4821 0.4136 0.0128  -0.0563 0.0067  478  ASP A CB  
1962 C  CG  . ASP A 254 ? 0.5143 0.5301 0.4671 0.0091  -0.0516 0.0049  478  ASP A CG  
1963 O  OD1 . ASP A 254 ? 0.5222 0.5353 0.4712 0.0080  -0.0460 0.0066  478  ASP A OD1 
1964 O  OD2 . ASP A 254 ? 0.6009 0.6211 0.5635 0.0073  -0.0535 0.0018  478  ASP A OD2 
1965 N  N   . THR A 255 ? 0.4422 0.4495 0.3768 0.0201  -0.0606 0.0150  479  THR A N   
1966 C  CA  . THR A 255 ? 0.4916 0.4968 0.4200 0.0244  -0.0665 0.0166  479  THR A CA  
1967 C  C   . THR A 255 ? 0.4415 0.4423 0.3674 0.0266  -0.0644 0.0220  479  THR A C   
1968 O  O   . THR A 255 ? 0.4190 0.4170 0.3382 0.0306  -0.0690 0.0240  479  THR A O   
1969 C  CB  . THR A 255 ? 0.4847 0.4967 0.4241 0.0251  -0.0735 0.0131  479  THR A CB  
1970 O  OG1 . THR A 255 ? 0.4581 0.4742 0.4114 0.0236  -0.0713 0.0136  479  THR A OG1 
1971 C  CG2 . THR A 255 ? 0.5385 0.5544 0.4812 0.0226  -0.0758 0.0077  479  THR A CG2 
1972 N  N   . GLY A 256 ? 0.4380 0.4377 0.3688 0.0242  -0.0580 0.0241  480  GLY A N   
1973 C  CA  . GLY A 256 ? 0.4722 0.4675 0.4021 0.0260  -0.0561 0.0288  480  GLY A CA  
1974 C  C   . GLY A 256 ? 0.3406 0.3392 0.2803 0.0282  -0.0605 0.0287  480  GLY A C   
1975 O  O   . GLY A 256 ? 0.4763 0.4708 0.4153 0.0301  -0.0595 0.0324  480  GLY A O   
1976 N  N   . ARG A 257 ? 0.3478 0.3535 0.2968 0.0279  -0.0650 0.0245  481  ARG A N   
1977 C  CA  . ARG A 257 ? 0.4065 0.4168 0.3669 0.0297  -0.0686 0.0239  481  ARG A CA  
1978 C  C   . ARG A 257 ? 0.3809 0.3925 0.3515 0.0274  -0.0631 0.0244  481  ARG A C   
1979 O  O   . ARG A 257 ? 0.3421 0.3558 0.3169 0.0235  -0.0587 0.0224  481  ARG A O   
1980 C  CB  . ARG A 257 ? 0.4500 0.4682 0.4189 0.0293  -0.0742 0.0190  481  ARG A CB  
1981 C  CG  . ARG A 257 ? 0.4461 0.4694 0.4255 0.0323  -0.0795 0.0183  481  ARG A CG  
1982 C  CD  . ARG A 257 ? 0.4778 0.5097 0.4685 0.0305  -0.0836 0.0131  481  ARG A CD  
1983 N  NE  . ARG A 257 ? 0.5317 0.5694 0.5334 0.0335  -0.0889 0.0122  481  ARG A NE  
1984 C  CZ  . ARG A 257 ? 0.5321 0.5714 0.5320 0.0372  -0.0970 0.0113  481  ARG A CZ  
1985 N  NH1 . ARG A 257 ? 0.5064 0.5419 0.4933 0.0385  -0.1010 0.0108  481  ARG A NH1 
1986 N  NH2 . ARG A 257 ? 0.4861 0.5310 0.4975 0.0401  -0.1013 0.0106  481  ARG A NH2 
1987 N  N   . ALA A 258 ? 0.3022 0.3120 0.2761 0.0300  -0.0634 0.0269  482  ALA A N   
1988 C  CA  . ALA A 258 ? 0.3142 0.3253 0.2980 0.0285  -0.0591 0.0268  482  ALA A CA  
1989 C  C   . ALA A 258 ? 0.2861 0.3053 0.2834 0.0293  -0.0624 0.0237  482  ALA A C   
1990 O  O   . ALA A 258 ? 0.3042 0.3257 0.3033 0.0328  -0.0683 0.0235  482  ALA A O   
1991 C  CB  . ALA A 258 ? 0.3248 0.3287 0.3048 0.0307  -0.0571 0.0311  482  ALA A CB  
1992 N  N   . LEU A 259 ? 0.2588 0.2824 0.2654 0.0263  -0.0586 0.0212  483  LEU A N   
1993 C  CA  . LEU A 259 ? 0.2522 0.2841 0.2717 0.0262  -0.0608 0.0178  483  LEU A CA  
1994 C  C   . LEU A 259 ? 0.2982 0.3321 0.3275 0.0280  -0.0592 0.0182  483  LEU A C   
1995 O  O   . LEU A 259 ? 0.2405 0.2798 0.2786 0.0305  -0.0630 0.0169  483  LEU A O   
1996 C  CB  . LEU A 259 ? 0.2844 0.3201 0.3077 0.0217  -0.0577 0.0147  483  LEU A CB  
1997 C  CG  . LEU A 259 ? 0.3304 0.3649 0.3450 0.0204  -0.0601 0.0138  483  LEU A CG  
1998 C  CD1 . LEU A 259 ? 0.3137 0.3473 0.3265 0.0163  -0.0551 0.0125  483  LEU A CD1 
1999 C  CD2 . LEU A 259 ? 0.3945 0.4352 0.4151 0.0211  -0.0663 0.0107  483  LEU A CD2 
2000 N  N   . PHE A 260 ? 0.2281 0.2579 0.2566 0.0269  -0.0537 0.0194  484  PHE A N   
2001 C  CA  . PHE A 260 ? 0.2327 0.2629 0.2688 0.0291  -0.0520 0.0197  484  PHE A CA  
2002 C  C   . PHE A 260 ? 0.2271 0.2497 0.2574 0.0282  -0.0471 0.0218  484  PHE A C   
2003 O  O   . PHE A 260 ? 0.2291 0.2478 0.2517 0.0254  -0.0446 0.0225  484  PHE A O   
2004 C  CB  . PHE A 260 ? 0.2531 0.2910 0.3016 0.0278  -0.0499 0.0165  484  PHE A CB  
2005 C  CG  . PHE A 260 ? 0.2297 0.2677 0.2776 0.0235  -0.0446 0.0149  484  PHE A CG  
2006 C  CD1 . PHE A 260 ? 0.2088 0.2490 0.2547 0.0203  -0.0451 0.0134  484  PHE A CD1 
2007 C  CD2 . PHE A 260 ? 0.2192 0.2548 0.2684 0.0229  -0.0395 0.0148  484  PHE A CD2 
2008 C  CE1 . PHE A 260 ? 0.2451 0.2851 0.2903 0.0168  -0.0405 0.0121  484  PHE A CE1 
2009 C  CE2 . PHE A 260 ? 0.2155 0.2510 0.2636 0.0194  -0.0352 0.0134  484  PHE A CE2 
2010 C  CZ  . PHE A 260 ? 0.2335 0.2712 0.2796 0.0164  -0.0357 0.0122  484  PHE A CZ  
2011 N  N   . GLU A 261 ? 0.2281 0.2490 0.2629 0.0307  -0.0458 0.0224  485  GLU A N   
2012 C  CA  . GLU A 261 ? 0.2286 0.2426 0.2598 0.0298  -0.0414 0.0236  485  GLU A CA  
2013 C  C   . GLU A 261 ? 0.2222 0.2393 0.2615 0.0293  -0.0377 0.0209  485  GLU A C   
2014 O  O   . GLU A 261 ? 0.2192 0.2429 0.2676 0.0307  -0.0384 0.0189  485  GLU A O   
2015 C  CB  . GLU A 261 ? 0.2755 0.2822 0.3024 0.0334  -0.0430 0.0270  485  GLU A CB  
2016 C  CG  . GLU A 261 ? 0.2598 0.2610 0.2757 0.0332  -0.0448 0.0303  485  GLU A CG  
2017 C  CD  . GLU A 261 ? 0.3331 0.3266 0.3440 0.0371  -0.0467 0.0343  485  GLU A CD  
2018 O  OE1 . GLU A 261 ? 0.3280 0.3200 0.3444 0.0399  -0.0467 0.0343  485  GLU A OE1 
2019 O  OE2 . GLU A 261 ? 0.2751 0.2637 0.2762 0.0374  -0.0481 0.0374  485  GLU A OE2 
2020 N  N   . SER A 262 ? 0.2206 0.2329 0.2567 0.0272  -0.0335 0.0207  486  SER A N   
2021 C  CA  . SER A 262 ? 0.2157 0.2295 0.2568 0.0265  -0.0296 0.0181  486  SER A CA  
2022 C  C   . SER A 262 ? 0.2194 0.2253 0.2570 0.0268  -0.0273 0.0188  486  SER A C   
2023 O  O   . SER A 262 ? 0.2236 0.2234 0.2547 0.0258  -0.0275 0.0211  486  SER A O   
2024 C  CB  . SER A 262 ? 0.2088 0.2261 0.2493 0.0226  -0.0271 0.0161  486  SER A CB  
2025 O  OG  . SER A 262 ? 0.2881 0.3056 0.3313 0.0222  -0.0233 0.0139  486  SER A OG  
2026 N  N   . LYS A 263 ? 0.2184 0.2242 0.2605 0.0282  -0.0248 0.0167  487  LYS A N   
2027 C  CA  . LYS A 263 ? 0.2526 0.2509 0.2924 0.0286  -0.0228 0.0166  487  LYS A CA  
2028 C  C   . LYS A 263 ? 0.2362 0.2342 0.2743 0.0257  -0.0194 0.0140  487  LYS A C   
2029 O  O   . LYS A 263 ? 0.2385 0.2405 0.2802 0.0262  -0.0173 0.0114  487  LYS A O   
2030 C  CB  . LYS A 263 ? 0.2267 0.2239 0.2717 0.0331  -0.0230 0.0161  487  LYS A CB  
2031 C  CG  . LYS A 263 ? 0.2425 0.2377 0.2878 0.0364  -0.0269 0.0191  487  LYS A CG  
2032 C  CD  . LYS A 263 ? 0.2709 0.2696 0.3242 0.0412  -0.0278 0.0181  487  LYS A CD  
2033 C  CE  . LYS A 263 ? 0.2984 0.2916 0.3531 0.0432  -0.0251 0.0164  487  LYS A CE  
2034 N  NZ  . LYS A 263 ? 0.2442 0.2403 0.3068 0.0484  -0.0259 0.0156  487  LYS A NZ  
2035 N  N   . LEU A 264 ? 0.2188 0.2120 0.2515 0.0228  -0.0187 0.0147  488  LEU A N   
2036 C  CA  . LEU A 264 ? 0.2155 0.2080 0.2463 0.0202  -0.0162 0.0121  488  LEU A CA  
2037 C  C   . LEU A 264 ? 0.2445 0.2305 0.2752 0.0215  -0.0151 0.0106  488  LEU A C   
2038 O  O   . LEU A 264 ? 0.2253 0.2049 0.2540 0.0208  -0.0156 0.0120  488  LEU A O   
2039 C  CB  . LEU A 264 ? 0.2283 0.2200 0.2544 0.0165  -0.0163 0.0133  488  LEU A CB  
2040 C  CG  . LEU A 264 ? 0.2293 0.2194 0.2534 0.0139  -0.0144 0.0109  488  LEU A CG  
2041 C  CD1 . LEU A 264 ? 0.2094 0.2041 0.2349 0.0142  -0.0129 0.0082  488  LEU A CD1 
2042 C  CD2 . LEU A 264 ? 0.2224 0.2123 0.2430 0.0105  -0.0144 0.0122  488  LEU A CD2 
2043 N  N   . HIS A 265 ? 0.2314 0.2188 0.2645 0.0234  -0.0134 0.0077  489  HIS A N   
2044 C  CA  . HIS A 265 ? 0.2475 0.2287 0.2805 0.0252  -0.0126 0.0056  489  HIS A CA  
2045 C  C   . HIS A 265 ? 0.2534 0.2307 0.2826 0.0221  -0.0119 0.0037  489  HIS A C   
2046 O  O   . HIS A 265 ? 0.2660 0.2467 0.2931 0.0196  -0.0114 0.0029  489  HIS A O   
2047 C  CB  . HIS A 265 ? 0.2311 0.2152 0.2673 0.0285  -0.0106 0.0030  489  HIS A CB  
2048 C  CG  . HIS A 265 ? 0.2511 0.2398 0.2928 0.0316  -0.0113 0.0045  489  HIS A CG  
2049 N  ND1 . HIS A 265 ? 0.3221 0.3074 0.3669 0.0354  -0.0121 0.0049  489  HIS A ND1 
2050 C  CD2 . HIS A 265 ? 0.2858 0.2821 0.3311 0.0315  -0.0117 0.0057  489  HIS A CD2 
2051 C  CE1 . HIS A 265 ? 0.3303 0.3216 0.3806 0.0377  -0.0131 0.0061  489  HIS A CE1 
2052 N  NE2 . HIS A 265 ? 0.3046 0.3028 0.3556 0.0352  -0.0129 0.0065  489  HIS A NE2 
2053 N  N   . LYS A 266 ? 0.2439 0.2137 0.2726 0.0225  -0.0123 0.0029  490  LYS A N   
2054 C  CA  . LYS A 266 ? 0.2925 0.2582 0.3189 0.0195  -0.0124 0.0010  490  LYS A CA  
2055 C  C   . LYS A 266 ? 0.2632 0.2315 0.2874 0.0191  -0.0113 -0.0028 490  LYS A C   
2056 O  O   . LYS A 266 ? 0.2919 0.2606 0.3142 0.0161  -0.0117 -0.0038 490  LYS A O   
2057 C  CB  . LYS A 266 ? 0.3603 0.3173 0.3876 0.0204  -0.0129 0.0001  490  LYS A CB  
2058 C  CG  . LYS A 266 ? 0.4274 0.3794 0.4538 0.0175  -0.0134 -0.0025 490  LYS A CG  
2059 C  CD  . LYS A 266 ? 0.4644 0.4074 0.4923 0.0188  -0.0139 -0.0037 490  LYS A CD  
2060 C  CE  . LYS A 266 ? 0.5246 0.4627 0.5527 0.0159  -0.0148 -0.0071 490  LYS A CE  
2061 N  NZ  . LYS A 266 ? 0.6656 0.5944 0.6955 0.0172  -0.0154 -0.0086 490  LYS A NZ  
2062 N  N   . GLN A 267 ? 0.2750 0.2453 0.2993 0.0224  -0.0099 -0.0048 491  GLN A N   
2063 C  CA  . GLN A 267 ? 0.3004 0.2719 0.3211 0.0227  -0.0087 -0.0083 491  GLN A CA  
2064 C  C   . GLN A 267 ? 0.3379 0.3165 0.3576 0.0213  -0.0076 -0.0072 491  GLN A C   
2065 O  O   . GLN A 267 ? 0.3019 0.2815 0.3180 0.0217  -0.0063 -0.0095 491  GLN A O   
2066 C  CB  . GLN A 267 ? 0.4044 0.3740 0.4249 0.0269  -0.0069 -0.0111 491  GLN A CB  
2067 C  CG  . GLN A 267 ? 0.4452 0.4063 0.4652 0.0283  -0.0081 -0.0136 491  GLN A CG  
2068 C  CD  . GLN A 267 ? 0.4940 0.4507 0.5110 0.0253  -0.0101 -0.0162 491  GLN A CD  
2069 O  OE1 . GLN A 267 ? 0.5083 0.4653 0.5209 0.0254  -0.0099 -0.0194 491  GLN A OE1 
2070 N  NE2 . GLN A 267 ? 0.3399 0.2925 0.3595 0.0226  -0.0119 -0.0146 491  GLN A NE2 
2071 N  N   . GLY A 268 ? 0.2503 0.2331 0.2725 0.0198  -0.0082 -0.0038 492  GLY A N   
2072 C  CA  . GLY A 268 ? 0.2623 0.2503 0.2832 0.0175  -0.0078 -0.0028 492  GLY A CA  
2073 C  C   . GLY A 268 ? 0.2628 0.2571 0.2863 0.0185  -0.0063 -0.0016 492  GLY A C   
2074 O  O   . GLY A 268 ? 0.2809 0.2782 0.3026 0.0180  -0.0047 -0.0025 492  GLY A O   
2075 N  N   . PHE A 269 ? 0.2573 0.2535 0.2853 0.0200  -0.0070 0.0003  493  PHE A N   
2076 C  CA  . PHE A 269 ? 0.2405 0.2434 0.2724 0.0204  -0.0062 0.0014  493  PHE A CA  
2077 C  C   . PHE A 269 ? 0.2306 0.2350 0.2666 0.0213  -0.0087 0.0040  493  PHE A C   
2078 O  O   . PHE A 269 ? 0.2786 0.2782 0.3142 0.0224  -0.0103 0.0049  493  PHE A O   
2079 C  CB  . PHE A 269 ? 0.2108 0.2158 0.2449 0.0232  -0.0030 -0.0005 493  PHE A CB  
2080 C  CG  . PHE A 269 ? 0.2688 0.2716 0.3062 0.0269  -0.0027 -0.0012 493  PHE A CG  
2081 C  CD1 . PHE A 269 ? 0.3032 0.2994 0.3370 0.0284  -0.0024 -0.0033 493  PHE A CD1 
2082 C  CD2 . PHE A 269 ? 0.2786 0.2861 0.3231 0.0291  -0.0028 0.0000  493  PHE A CD2 
2083 C  CE1 . PHE A 269 ? 0.3966 0.3902 0.4334 0.0321  -0.0020 -0.0041 493  PHE A CE1 
2084 C  CE2 . PHE A 269 ? 0.3067 0.3123 0.3546 0.0329  -0.0025 -0.0007 493  PHE A CE2 
2085 C  CZ  . PHE A 269 ? 0.3264 0.3248 0.3703 0.0345  -0.0020 -0.0027 493  PHE A CZ  
2086 N  N   . MET A 270 ? 0.2088 0.2193 0.2484 0.0209  -0.0092 0.0051  494  MET A N   
2087 C  CA  . MET A 270 ? 0.2468 0.2592 0.2895 0.0217  -0.0123 0.0074  494  MET A CA  
2088 C  C   . MET A 270 ? 0.2056 0.2236 0.2561 0.0245  -0.0121 0.0070  494  MET A C   
2089 O  O   . MET A 270 ? 0.2145 0.2369 0.2683 0.0243  -0.0093 0.0055  494  MET A O   
2090 C  CB  . MET A 270 ? 0.2181 0.2331 0.2585 0.0187  -0.0142 0.0087  494  MET A CB  
2091 C  CG  . MET A 270 ? 0.3030 0.3132 0.3367 0.0160  -0.0142 0.0092  494  MET A CG  
2092 S  SD  . MET A 270 ? 0.3529 0.3659 0.3832 0.0126  -0.0154 0.0101  494  MET A SD  
2093 C  CE  . MET A 270 ? 0.2658 0.2813 0.2984 0.0143  -0.0191 0.0123  494  MET A CE  
2094 N  N   . THR A 271 ? 0.2059 0.2236 0.2596 0.0271  -0.0148 0.0084  495  THR A N   
2095 C  CA  . THR A 271 ? 0.2058 0.2298 0.2682 0.0299  -0.0156 0.0082  495  THR A CA  
2096 C  C   . THR A 271 ? 0.2151 0.2414 0.2787 0.0301  -0.0205 0.0104  495  THR A C   
2097 O  O   . THR A 271 ? 0.2093 0.2307 0.2664 0.0293  -0.0229 0.0124  495  THR A O   
2098 C  CB  . THR A 271 ? 0.2225 0.2442 0.2886 0.0342  -0.0146 0.0075  495  THR A CB  
2099 O  OG1 . THR A 271 ? 0.2461 0.2606 0.3080 0.0357  -0.0172 0.0093  495  THR A OG1 
2100 C  CG2 . THR A 271 ? 0.2111 0.2305 0.2753 0.0343  -0.0098 0.0049  495  THR A CG2 
2101 N  N   . ILE A 272 ? 0.2047 0.2387 0.2768 0.0312  -0.0217 0.0098  496  ILE A N   
2102 C  CA  . ILE A 272 ? 0.2062 0.2436 0.2809 0.0322  -0.0269 0.0111  496  ILE A CA  
2103 C  C   . ILE A 272 ? 0.2077 0.2509 0.2933 0.0361  -0.0279 0.0103  496  ILE A C   
2104 O  O   . ILE A 272 ? 0.2263 0.2724 0.3182 0.0372  -0.0239 0.0085  496  ILE A O   
2105 C  CB  . ILE A 272 ? 0.2059 0.2482 0.2807 0.0286  -0.0281 0.0106  496  ILE A CB  
2106 C  CG1 . ILE A 272 ? 0.1969 0.2455 0.2796 0.0271  -0.0241 0.0083  496  ILE A CG1 
2107 C  CG2 . ILE A 272 ? 0.2012 0.2378 0.2652 0.0253  -0.0277 0.0116  496  ILE A CG2 
2108 C  CD1 . ILE A 272 ? 0.2014 0.2562 0.2881 0.0241  -0.0256 0.0074  496  ILE A CD1 
2109 N  N   . ALA A 273 ? 0.2113 0.2563 0.2992 0.0386  -0.0334 0.0116  497  ALA A N   
2110 C  CA  . ALA A 273 ? 0.2340 0.2860 0.3337 0.0423  -0.0354 0.0107  497  ALA A CA  
2111 C  C   . ALA A 273 ? 0.2456 0.3072 0.3540 0.0398  -0.0359 0.0088  497  ALA A C   
2112 O  O   . ALA A 273 ? 0.2204 0.2839 0.3270 0.0382  -0.0404 0.0091  497  ALA A O   
2113 C  CB  . ALA A 273 ? 0.2259 0.2755 0.3242 0.0464  -0.0416 0.0129  497  ALA A CB  
2114 N  N   . SER A 274 ? 0.2323 0.2996 0.3498 0.0392  -0.0311 0.0067  498  SER A N   
2115 C  CA  . SER A 274 ? 0.2572 0.3334 0.3840 0.0364  -0.0308 0.0049  498  SER A CA  
2116 C  C   . SER A 274 ? 0.2639 0.3465 0.4029 0.0378  -0.0256 0.0032  498  SER A C   
2117 O  O   . SER A 274 ? 0.2867 0.3659 0.4245 0.0403  -0.0215 0.0031  498  SER A O   
2118 C  CB  . SER A 274 ? 0.2773 0.3511 0.3966 0.0311  -0.0287 0.0048  498  SER A CB  
2119 O  OG  . SER A 274 ? 0.3037 0.3846 0.4303 0.0284  -0.0309 0.0035  498  SER A OG  
2120 N  N   . SER A 275 ? 0.2584 0.3502 0.4093 0.0360  -0.0256 0.0016  499  SER A N   
2121 C  CA  . SER A 275 ? 0.2852 0.3843 0.4492 0.0369  -0.0202 0.0001  499  SER A CA  
2122 C  C   . SER A 275 ? 0.3038 0.4080 0.4733 0.0318  -0.0168 -0.0010 499  SER A C   
2123 O  O   . SER A 275 ? 0.3337 0.4413 0.5059 0.0290  -0.0214 -0.0015 499  SER A O   
2124 C  CB  . SER A 275 ? 0.3059 0.4130 0.4841 0.0411  -0.0243 -0.0008 499  SER A CB  
2125 O  OG  . SER A 275 ? 0.4321 0.5464 0.6235 0.0422  -0.0182 -0.0023 499  SER A OG  
2126 N  N   . GLY A 276 ? 0.2926 0.3967 0.4632 0.0308  -0.0087 -0.0014 500  GLY A N   
2127 C  CA  . GLY A 276 ? 0.2746 0.3830 0.4508 0.0262  -0.0045 -0.0020 500  GLY A CA  
2128 C  C   . GLY A 276 ? 0.3053 0.4057 0.4673 0.0225  -0.0018 -0.0010 500  GLY A C   
2129 O  O   . GLY A 276 ? 0.2911 0.3832 0.4394 0.0230  -0.0039 0.0000  500  GLY A O   
2130 N  N   . ASP A 277 ? 0.2954 0.3984 0.4616 0.0188  0.0030  -0.0013 501  ASP A N   
2131 C  CA  . ASP A 277 ? 0.2552 0.3514 0.4096 0.0152  0.0058  -0.0004 501  ASP A CA  
2132 C  C   . ASP A 277 ? 0.2962 0.3942 0.4523 0.0112  0.0008  -0.0009 501  ASP A C   
2133 O  O   . ASP A 277 ? 0.2578 0.3626 0.4262 0.0087  0.0014  -0.0018 501  ASP A O   
2134 C  CB  . ASP A 277 ? 0.3038 0.4002 0.4601 0.0140  0.0148  -0.0001 501  ASP A CB  
2135 C  CG  . ASP A 277 ? 0.3687 0.4643 0.5246 0.0184  0.0201  -0.0001 501  ASP A CG  
2136 O  OD1 . ASP A 277 ? 0.3576 0.4506 0.5096 0.0221  0.0168  -0.0003 501  ASP A OD1 
2137 O  OD2 . ASP A 277 ? 0.4669 0.5640 0.6262 0.0182  0.0277  0.0001  501  ASP A OD2 
2138 N  N   . HIS A 278 ? 0.2400 0.3319 0.3842 0.0106  -0.0042 -0.0003 502  HIS A N   
2139 C  CA  . HIS A 278 ? 0.2530 0.3460 0.3975 0.0073  -0.0092 -0.0011 502  HIS A CA  
2140 C  C   . HIS A 278 ? 0.2513 0.3359 0.3799 0.0066  -0.0117 -0.0001 502  HIS A C   
2141 O  O   . HIS A 278 ? 0.2315 0.3108 0.3513 0.0093  -0.0117 0.0010  502  HIS A O   
2142 C  CB  . HIS A 278 ? 0.2482 0.3480 0.4027 0.0087  -0.0164 -0.0024 502  HIS A CB  
2143 C  CG  . HIS A 278 ? 0.2481 0.3460 0.3984 0.0134  -0.0204 -0.0016 502  HIS A CG  
2144 N  ND1 . HIS A 278 ? 0.3212 0.4129 0.4592 0.0143  -0.0255 -0.0006 502  HIS A ND1 
2145 C  CD2 . HIS A 278 ? 0.2740 0.3750 0.4310 0.0175  -0.0199 -0.0015 502  HIS A CD2 
2146 C  CE1 . HIS A 278 ? 0.2655 0.3562 0.4025 0.0186  -0.0278 0.0003  502  HIS A CE1 
2147 N  NE2 . HIS A 278 ? 0.3193 0.4154 0.4677 0.0208  -0.0248 -0.0004 502  HIS A NE2 
2148 N  N   . PRO A 279 ? 0.2546 0.3376 0.3797 0.0032  -0.0135 -0.0006 503  PRO A N   
2149 C  CA  . PRO A 279 ? 0.2470 0.3229 0.3582 0.0028  -0.0164 0.0002  503  PRO A CA  
2150 C  C   . PRO A 279 ? 0.2598 0.3357 0.3684 0.0052  -0.0233 0.0003  503  PRO A C   
2151 O  O   . PRO A 279 ? 0.2367 0.3185 0.3545 0.0065  -0.0274 -0.0007 503  PRO A O   
2152 C  CB  . PRO A 279 ? 0.2546 0.3300 0.3652 -0.0013 -0.0166 -0.0008 503  PRO A CB  
2153 C  CG  . PRO A 279 ? 0.2652 0.3483 0.3907 -0.0029 -0.0172 -0.0024 503  PRO A CG  
2154 C  CD  . PRO A 279 ? 0.2471 0.3347 0.3816 -0.0006 -0.0132 -0.0020 503  PRO A CD  
2155 N  N   . ILE A 280 ? 0.2561 0.3253 0.3522 0.0059  -0.0245 0.0015  504  ILE A N   
2156 C  CA  . ILE A 280 ? 0.2422 0.3095 0.3328 0.0080  -0.0304 0.0022  504  ILE A CA  
2157 C  C   . ILE A 280 ? 0.2566 0.3213 0.3398 0.0054  -0.0331 0.0017  504  ILE A C   
2158 O  O   . ILE A 280 ? 0.2790 0.3380 0.3523 0.0043  -0.0310 0.0026  504  ILE A O   
2159 C  CB  . ILE A 280 ? 0.2390 0.3004 0.3214 0.0107  -0.0293 0.0042  504  ILE A CB  
2160 C  CG1 . ILE A 280 ? 0.2314 0.2950 0.3209 0.0135  -0.0264 0.0044  504  ILE A CG1 
2161 C  CG2 . ILE A 280 ? 0.2601 0.3187 0.3359 0.0127  -0.0349 0.0055  504  ILE A CG2 
2162 C  CD1 . ILE A 280 ? 0.2658 0.3360 0.3663 0.0161  -0.0299 0.0037  504  ILE A CD1 
2163 N  N   . ILE A 281 ? 0.2526 0.3216 0.3410 0.0046  -0.0377 -0.0001 505  ILE A N   
2164 C  CA  . ILE A 281 ? 0.3325 0.3991 0.4146 0.0021  -0.0401 -0.0012 505  ILE A CA  
2165 C  C   . ILE A 281 ? 0.2929 0.3562 0.3656 0.0045  -0.0455 -0.0003 505  ILE A C   
2166 O  O   . ILE A 281 ? 0.2921 0.3583 0.3682 0.0072  -0.0502 -0.0003 505  ILE A O   
2167 C  CB  . ILE A 281 ? 0.3513 0.4236 0.4438 -0.0004 -0.0422 -0.0040 505  ILE A CB  
2168 C  CG1 . ILE A 281 ? 0.3596 0.4350 0.4618 -0.0026 -0.0361 -0.0042 505  ILE A CG1 
2169 C  CG2 . ILE A 281 ? 0.3677 0.4367 0.4531 -0.0029 -0.0442 -0.0054 505  ILE A CG2 
2170 C  CD1 . ILE A 281 ? 0.3993 0.4830 0.5172 -0.0021 -0.0373 -0.0056 505  ILE A CD1 
2171 N  N   . MET A 282 ? 0.2837 0.3411 0.3447 0.0036  -0.0446 0.0005  506  MET A N   
2172 C  CA  . MET A 282 ? 0.3117 0.3648 0.3619 0.0057  -0.0481 0.0020  506  MET A CA  
2173 C  C   . MET A 282 ? 0.2859 0.3359 0.3278 0.0038  -0.0491 0.0008  506  MET A C   
2174 O  O   . MET A 282 ? 0.2631 0.3132 0.3066 0.0008  -0.0463 -0.0007 506  MET A O   
2175 C  CB  . MET A 282 ? 0.2826 0.3305 0.3261 0.0072  -0.0445 0.0050  506  MET A CB  
2176 C  CG  . MET A 282 ? 0.2574 0.3072 0.3077 0.0098  -0.0439 0.0061  506  MET A CG  
2177 S  SD  . MET A 282 ? 0.3146 0.3654 0.3645 0.0139  -0.0509 0.0070  506  MET A SD  
2178 C  CE  . MET A 282 ? 0.2458 0.3034 0.3106 0.0161  -0.0510 0.0063  506  MET A CE  
2179 N  N   . PRO A 283 ? 0.3210 0.3679 0.3535 0.0056  -0.0530 0.0015  507  PRO A N   
2180 C  CA  . PRO A 283 ? 0.3305 0.3738 0.3536 0.0042  -0.0534 0.0004  507  PRO A CA  
2181 C  C   . PRO A 283 ? 0.3068 0.3465 0.3261 0.0020  -0.0472 0.0012  507  PRO A C   
2182 O  O   . PRO A 283 ? 0.2664 0.3041 0.2847 0.0025  -0.0435 0.0035  507  PRO A O   
2183 C  CB  . PRO A 283 ? 0.2845 0.3237 0.2965 0.0073  -0.0566 0.0024  507  PRO A CB  
2184 C  CG  . PRO A 283 ? 0.3579 0.4005 0.3760 0.0102  -0.0611 0.0029  507  PRO A CG  
2185 C  CD  . PRO A 283 ? 0.2734 0.3202 0.3038 0.0093  -0.0578 0.0029  507  PRO A CD  
2186 N  N   . THR A 284 ? 0.3008 0.3398 0.3182 -0.0003 -0.0467 -0.0010 508  THR A N   
2187 C  CA  A THR A 284 ? 0.2912 0.3278 0.3070 -0.0023 -0.0412 -0.0007 508  THR A CA  
2188 C  CA  B THR A 284 ? 0.2922 0.3287 0.3076 -0.0023 -0.0413 -0.0008 508  THR A CA  
2189 C  C   . THR A 284 ? 0.2594 0.2913 0.2659 -0.0013 -0.0385 0.0018  508  THR A C   
2190 O  O   . THR A 284 ? 0.2731 0.3037 0.2800 -0.0022 -0.0341 0.0028  508  THR A O   
2191 C  CB  A THR A 284 ? 0.3081 0.3441 0.3233 -0.0046 -0.0415 -0.0035 508  THR A CB  
2192 C  CB  B THR A 284 ? 0.3084 0.3440 0.3219 -0.0043 -0.0421 -0.0036 508  THR A CB  
2193 O  OG1 A THR A 284 ? 0.3070 0.3404 0.3130 -0.0036 -0.0444 -0.0044 508  THR A OG1 
2194 O  OG1 B THR A 284 ? 0.3172 0.3568 0.3389 -0.0053 -0.0457 -0.0062 508  THR A OG1 
2195 C  CG2 A THR A 284 ? 0.3262 0.3668 0.3520 -0.0061 -0.0438 -0.0060 508  THR A CG2 
2196 C  CG2 B THR A 284 ? 0.3337 0.3675 0.3478 -0.0063 -0.0370 -0.0036 508  THR A CG2 
2197 N  N   . ASN A 285 ? 0.2464 0.2758 0.2446 0.0006  -0.0408 0.0029  509  ASN A N   
2198 C  CA  . ASN A 285 ? 0.3413 0.3663 0.3313 0.0012  -0.0376 0.0054  509  ASN A CA  
2199 C  C   . ASN A 285 ? 0.3254 0.3491 0.3159 0.0029  -0.0367 0.0086  509  ASN A C   
2200 O  O   . ASN A 285 ? 0.2937 0.3136 0.2782 0.0032  -0.0342 0.0109  509  ASN A O   
2201 C  CB  . ASN A 285 ? 0.3526 0.3747 0.3323 0.0022  -0.0394 0.0053  509  ASN A CB  
2202 C  CG  . ASN A 285 ? 0.3659 0.3877 0.3436 0.0005  -0.0387 0.0023  509  ASN A CG  
2203 O  OD1 . ASN A 285 ? 0.3458 0.3689 0.3291 -0.0016 -0.0362 0.0010  509  ASN A OD1 
2204 N  ND2 . ASN A 285 ? 0.3832 0.4028 0.3523 0.0016  -0.0410 0.0013  509  ASN A ND2 
2205 N  N   . GLY A 286 ? 0.2801 0.3067 0.2781 0.0039  -0.0385 0.0087  510  GLY A N   
2206 C  CA  . GLY A 286 ? 0.2642 0.2889 0.2625 0.0058  -0.0380 0.0114  510  GLY A CA  
2207 C  C   . GLY A 286 ? 0.2276 0.2504 0.2276 0.0046  -0.0331 0.0124  510  GLY A C   
2208 O  O   . GLY A 286 ? 0.2250 0.2493 0.2286 0.0026  -0.0304 0.0108  510  GLY A O   
2209 N  N   . TYR A 287 ? 0.2504 0.2695 0.2476 0.0060  -0.0320 0.0151  511  TYR A N   
2210 C  CA  . TYR A 287 ? 0.2370 0.2540 0.2361 0.0050  -0.0280 0.0158  511  TYR A CA  
2211 C  C   . TYR A 287 ? 0.2466 0.2605 0.2462 0.0071  -0.0283 0.0182  511  TYR A C   
2212 O  O   . TYR A 287 ? 0.2295 0.2417 0.2257 0.0093  -0.0310 0.0201  511  TYR A O   
2213 C  CB  . TYR A 287 ? 0.2360 0.2502 0.2295 0.0031  -0.0249 0.0162  511  TYR A CB  
2214 C  CG  . TYR A 287 ? 0.2614 0.2714 0.2470 0.0040  -0.0249 0.0190  511  TYR A CG  
2215 C  CD1 . TYR A 287 ? 0.2607 0.2663 0.2449 0.0044  -0.0231 0.0217  511  TYR A CD1 
2216 C  CD2 . TYR A 287 ? 0.3035 0.3133 0.2824 0.0044  -0.0267 0.0189  511  TYR A CD2 
2217 C  CE1 . TYR A 287 ? 0.3143 0.3154 0.2909 0.0052  -0.0225 0.0247  511  TYR A CE1 
2218 C  CE2 . TYR A 287 ? 0.3912 0.3966 0.3617 0.0055  -0.0262 0.0217  511  TYR A CE2 
2219 C  CZ  . TYR A 287 ? 0.4054 0.4065 0.3748 0.0059  -0.0239 0.0249  511  TYR A CZ  
2220 O  OH  . TYR A 287 ? 0.5275 0.5237 0.4883 0.0069  -0.0228 0.0282  511  TYR A OH  
2221 N  N   . PHE A 288 ? 0.2397 0.2523 0.2429 0.0066  -0.0255 0.0180  512  PHE A N   
2222 C  CA  . PHE A 288 ? 0.2419 0.2508 0.2461 0.0084  -0.0252 0.0199  512  PHE A CA  
2223 C  C   . PHE A 288 ? 0.2501 0.2532 0.2485 0.0076  -0.0232 0.0224  512  PHE A C   
2224 O  O   . PHE A 288 ? 0.2559 0.2584 0.2520 0.0052  -0.0207 0.0220  512  PHE A O   
2225 C  CB  . PHE A 288 ? 0.2316 0.2413 0.2419 0.0082  -0.0231 0.0181  512  PHE A CB  
2226 C  CG  . PHE A 288 ? 0.2496 0.2641 0.2666 0.0098  -0.0245 0.0165  512  PHE A CG  
2227 C  CD1 . PHE A 288 ? 0.2312 0.2459 0.2511 0.0127  -0.0269 0.0175  512  PHE A CD1 
2228 C  CD2 . PHE A 288 ? 0.2731 0.2918 0.2937 0.0083  -0.0231 0.0140  512  PHE A CD2 
2229 C  CE1 . PHE A 288 ? 0.2698 0.2898 0.2973 0.0141  -0.0278 0.0158  512  PHE A CE1 
2230 C  CE2 . PHE A 288 ? 0.2600 0.2833 0.2876 0.0094  -0.0236 0.0127  512  PHE A CE2 
2231 C  CZ  . PHE A 288 ? 0.2224 0.2467 0.2538 0.0123  -0.0259 0.0135  512  PHE A CZ  
2232 N  N   . ARG A 289 ? 0.2728 0.2715 0.2695 0.0096  -0.0241 0.0251  513  ARG A N   
2233 C  CA  . ARG A 289 ? 0.2923 0.2848 0.2839 0.0090  -0.0219 0.0281  513  ARG A CA  
2234 C  C   . ARG A 289 ? 0.2696 0.2574 0.2639 0.0107  -0.0218 0.0296  513  ARG A C   
2235 O  O   . ARG A 289 ? 0.2602 0.2487 0.2569 0.0137  -0.0246 0.0298  513  ARG A O   
2236 C  CB  . ARG A 289 ? 0.3612 0.3518 0.3445 0.0101  -0.0234 0.0308  513  ARG A CB  
2237 C  CG  . ARG A 289 ? 0.4668 0.4507 0.4436 0.0094  -0.0205 0.0345  513  ARG A CG  
2238 C  CD  . ARG A 289 ? 0.4911 0.4734 0.4583 0.0110  -0.0221 0.0368  513  ARG A CD  
2239 N  NE  . ARG A 289 ? 0.5878 0.5677 0.5520 0.0149  -0.0261 0.0390  513  ARG A NE  
2240 C  CZ  . ARG A 289 ? 0.6425 0.6221 0.5991 0.0173  -0.0294 0.0403  513  ARG A CZ  
2241 N  NH1 . ARG A 289 ? 0.6111 0.5926 0.5620 0.0162  -0.0291 0.0392  513  ARG A NH1 
2242 N  NH2 . ARG A 289 ? 0.5534 0.5305 0.5078 0.0212  -0.0334 0.0424  513  ARG A NH2 
2243 N  N   . PHE A 290 ? 0.2347 0.2180 0.2295 0.0089  -0.0187 0.0302  514  PHE A N   
2244 C  CA  . PHE A 290 ? 0.2581 0.2357 0.2551 0.0103  -0.0184 0.0315  514  PHE A CA  
2245 C  C   . PHE A 290 ? 0.2470 0.2189 0.2383 0.0127  -0.0197 0.0360  514  PHE A C   
2246 O  O   . PHE A 290 ? 0.2629 0.2323 0.2476 0.0117  -0.0185 0.0387  514  PHE A O   
2247 C  CB  . PHE A 290 ? 0.2911 0.2650 0.2902 0.0072  -0.0150 0.0309  514  PHE A CB  
2248 C  CG  . PHE A 290 ? 0.3149 0.2816 0.3156 0.0083  -0.0145 0.0325  514  PHE A CG  
2249 C  CD1 . PHE A 290 ? 0.2625 0.2288 0.2680 0.0104  -0.0157 0.0303  514  PHE A CD1 
2250 C  CD2 . PHE A 290 ? 0.2941 0.2539 0.2913 0.0072  -0.0125 0.0363  514  PHE A CD2 
2251 C  CE1 . PHE A 290 ? 0.2899 0.2490 0.2969 0.0114  -0.0154 0.0315  514  PHE A CE1 
2252 C  CE2 . PHE A 290 ? 0.3338 0.2861 0.3326 0.0080  -0.0120 0.0378  514  PHE A CE2 
2253 C  CZ  . PHE A 290 ? 0.2569 0.2087 0.2606 0.0102  -0.0136 0.0353  514  PHE A CZ  
2254 N  N   . GLU A 291 ? 0.2509 0.2205 0.2443 0.0161  -0.0219 0.0368  515  GLU A N   
2255 C  CA  . GLU A 291 ? 0.2619 0.2253 0.2496 0.0190  -0.0235 0.0412  515  GLU A CA  
2256 C  C   . GLU A 291 ? 0.2838 0.2388 0.2728 0.0199  -0.0221 0.0433  515  GLU A C   
2257 O  O   . GLU A 291 ? 0.3325 0.2802 0.3156 0.0201  -0.0209 0.0476  515  GLU A O   
2258 C  CB  . GLU A 291 ? 0.2661 0.2337 0.2544 0.0232  -0.0285 0.0411  515  GLU A CB  
2259 C  CG  . GLU A 291 ? 0.3068 0.2816 0.2929 0.0226  -0.0306 0.0394  515  GLU A CG  
2260 C  CD  . GLU A 291 ? 0.3311 0.3029 0.3072 0.0215  -0.0297 0.0422  515  GLU A CD  
2261 O  OE1 . GLU A 291 ? 0.3433 0.3074 0.3128 0.0226  -0.0287 0.0464  515  GLU A OE1 
2262 O  OE2 . GLU A 291 ? 0.3894 0.3662 0.3639 0.0197  -0.0297 0.0402  515  GLU A OE2 
2263 N  N   . ALA A 292 ? 0.2665 0.2219 0.2628 0.0205  -0.0221 0.0404  516  ALA A N   
2264 C  CA  . ALA A 292 ? 0.2819 0.2287 0.2794 0.0220  -0.0214 0.0422  516  ALA A CA  
2265 C  C   . ALA A 292 ? 0.2700 0.2179 0.2752 0.0219  -0.0207 0.0378  516  ALA A C   
2266 O  O   . ALA A 292 ? 0.2588 0.2143 0.2682 0.0219  -0.0213 0.0340  516  ALA A O   
2267 C  CB  . ALA A 292 ? 0.2817 0.2252 0.2765 0.0271  -0.0248 0.0455  516  ALA A CB  
2268 N  N   . TRP A 293 ? 0.2739 0.2137 0.2806 0.0218  -0.0192 0.0385  517  TRP A N   
2269 C  CA  . TRP A 293 ? 0.2851 0.2238 0.2978 0.0224  -0.0188 0.0345  517  TRP A CA  
2270 C  C   . TRP A 293 ? 0.2828 0.2196 0.2976 0.0278  -0.0213 0.0350  517  TRP A C   
2271 O  O   . TRP A 293 ? 0.2959 0.2247 0.3084 0.0299  -0.0218 0.0386  517  TRP A O   
2272 C  CB  . TRP A 293 ? 0.3146 0.2452 0.3283 0.0193  -0.0162 0.0344  517  TRP A CB  
2273 C  CG  . TRP A 293 ? 0.3160 0.2496 0.3299 0.0142  -0.0138 0.0328  517  TRP A CG  
2274 C  CD1 . TRP A 293 ? 0.3100 0.2404 0.3211 0.0107  -0.0115 0.0359  517  TRP A CD1 
2275 C  CD2 . TRP A 293 ? 0.2696 0.2099 0.2867 0.0122  -0.0135 0.0279  517  TRP A CD2 
2276 N  NE1 . TRP A 293 ? 0.2672 0.2025 0.2805 0.0067  -0.0100 0.0329  517  TRP A NE1 
2277 C  CE2 . TRP A 293 ? 0.2594 0.2005 0.2760 0.0077  -0.0114 0.0280  517  TRP A CE2 
2278 C  CE3 . TRP A 293 ? 0.2601 0.2055 0.2802 0.0141  -0.0146 0.0236  517  TRP A CE3 
2279 C  CZ2 . TRP A 293 ? 0.3105 0.2574 0.3295 0.0053  -0.0110 0.0239  517  TRP A CZ2 
2280 C  CZ3 . TRP A 293 ? 0.2769 0.2274 0.2984 0.0116  -0.0138 0.0198  517  TRP A CZ3 
2281 C  CH2 . TRP A 293 ? 0.2650 0.2162 0.2859 0.0073  -0.0123 0.0200  517  TRP A CH2 
2282 N  N   . VAL A 294 ? 0.2702 0.2143 0.2897 0.0301  -0.0225 0.0315  518  VAL A N   
2283 C  CA  . VAL A 294 ? 0.2745 0.2179 0.2974 0.0356  -0.0247 0.0316  518  VAL A CA  
2284 C  C   . VAL A 294 ? 0.2721 0.2160 0.3006 0.0368  -0.0233 0.0269  518  VAL A C   
2285 O  O   . VAL A 294 ? 0.2878 0.2312 0.3167 0.0336  -0.0210 0.0238  518  VAL A O   
2286 C  CB  . VAL A 294 ? 0.2861 0.2381 0.3100 0.0382  -0.0278 0.0323  518  VAL A CB  
2287 C  CG1 . VAL A 294 ? 0.2816 0.2324 0.2984 0.0374  -0.0295 0.0368  518  VAL A CG1 
2288 C  CG2 . VAL A 294 ? 0.2598 0.2220 0.2877 0.0365  -0.0269 0.0283  518  VAL A CG2 
2289 N  N   . ASN A 295 ? 0.3053 0.2502 0.3382 0.0417  -0.0247 0.0261  519  ASN A N   
2290 C  CA  . ASN A 295 ? 0.3345 0.2800 0.3720 0.0432  -0.0229 0.0214  519  ASN A CA  
2291 C  C   . ASN A 295 ? 0.3523 0.3088 0.3949 0.0452  -0.0231 0.0191  519  ASN A C   
2292 O  O   . ASN A 295 ? 0.3176 0.2809 0.3608 0.0454  -0.0251 0.0208  519  ASN A O   
2293 C  CB  . ASN A 295 ? 0.3290 0.2656 0.3681 0.0472  -0.0232 0.0216  519  ASN A CB  
2294 C  CG  . ASN A 295 ? 0.3631 0.3005 0.4046 0.0526  -0.0262 0.0244  519  ASN A CG  
2295 O  OD1 . ASN A 295 ? 0.3710 0.3177 0.4162 0.0546  -0.0276 0.0240  519  ASN A OD1 
2296 N  ND2 . ASN A 295 ? 0.4687 0.3960 0.5085 0.0551  -0.0273 0.0272  519  ASN A ND2 
2297 N  N   . GLN A 296 ? 0.3397 0.2976 0.3860 0.0468  -0.0209 0.0149  520  GLN A N   
2298 C  CA  . GLN A 296 ? 0.3879 0.3559 0.4395 0.0483  -0.0199 0.0124  520  GLN A CA  
2299 C  C   . GLN A 296 ? 0.3819 0.3551 0.4396 0.0529  -0.0223 0.0139  520  GLN A C   
2300 O  O   . GLN A 296 ? 0.3538 0.3365 0.4168 0.0535  -0.0218 0.0125  520  GLN A O   
2301 C  CB  . GLN A 296 ? 0.4575 0.4242 0.5103 0.0494  -0.0165 0.0078  520  GLN A CB  
2302 C  CG  . GLN A 296 ? 0.5052 0.4635 0.5591 0.0535  -0.0163 0.0067  520  GLN A CG  
2303 C  CD  . GLN A 296 ? 0.6394 0.5862 0.6880 0.0511  -0.0166 0.0068  520  GLN A CD  
2304 O  OE1 . GLN A 296 ? 0.4987 0.4439 0.5430 0.0463  -0.0167 0.0079  520  GLN A OE1 
2305 N  NE2 . GLN A 296 ? 0.7237 0.6625 0.7734 0.0546  -0.0165 0.0056  520  GLN A NE2 
2306 N  N   . PHE A 297 ? 0.3503 0.3175 0.4074 0.0561  -0.0252 0.0169  521  PHE A N   
2307 C  CA  . PHE A 297 ? 0.3732 0.3449 0.4363 0.0611  -0.0283 0.0184  521  PHE A CA  
2308 C  C   . PHE A 297 ? 0.3312 0.3052 0.3915 0.0605  -0.0325 0.0224  521  PHE A C   
2309 O  O   . PHE A 297 ? 0.3498 0.3269 0.4142 0.0648  -0.0361 0.0239  521  PHE A O   
2310 C  CB  . PHE A 297 ? 0.4550 0.4182 0.5194 0.0662  -0.0291 0.0191  521  PHE A CB  
2311 C  CG  . PHE A 297 ? 0.4994 0.4588 0.5654 0.0671  -0.0252 0.0150  521  PHE A CG  
2312 C  CD1 . PHE A 297 ? 0.5154 0.4827 0.5884 0.0695  -0.0227 0.0112  521  PHE A CD1 
2313 C  CD2 . PHE A 297 ? 0.5610 0.5091 0.6215 0.0656  -0.0240 0.0147  521  PHE A CD2 
2314 C  CE1 . PHE A 297 ? 0.6525 0.6159 0.7256 0.0707  -0.0191 0.0072  521  PHE A CE1 
2315 C  CE2 . PHE A 297 ? 0.6041 0.5484 0.6654 0.0666  -0.0209 0.0104  521  PHE A CE2 
2316 C  CZ  . PHE A 297 ? 0.6293 0.5811 0.6963 0.0694  -0.0184 0.0066  521  PHE A CZ  
2317 N  N   . TYR A 298 ? 0.3022 0.2748 0.3554 0.0556  -0.0323 0.0240  522  TYR A N   
2318 C  CA  . TYR A 298 ? 0.3187 0.2938 0.3681 0.0549  -0.0359 0.0272  522  TYR A CA  
2319 C  C   . TYR A 298 ? 0.2773 0.2645 0.3338 0.0557  -0.0378 0.0254  522  TYR A C   
2320 O  O   . TYR A 298 ? 0.2744 0.2683 0.3345 0.0530  -0.0351 0.0223  522  TYR A O   
2321 C  CB  . TYR A 298 ? 0.2646 0.2369 0.3059 0.0492  -0.0342 0.0284  522  TYR A CB  
2322 C  CG  . TYR A 298 ? 0.2689 0.2396 0.3034 0.0488  -0.0374 0.0324  522  TYR A CG  
2323 C  CD1 . TYR A 298 ? 0.2799 0.2407 0.3082 0.0507  -0.0387 0.0367  522  TYR A CD1 
2324 C  CD2 . TYR A 298 ? 0.2632 0.2415 0.2967 0.0468  -0.0391 0.0321  522  TYR A CD2 
2325 C  CE1 . TYR A 298 ? 0.3078 0.2664 0.3283 0.0507  -0.0413 0.0406  522  TYR A CE1 
2326 C  CE2 . TYR A 298 ? 0.2686 0.2450 0.2946 0.0467  -0.0420 0.0356  522  TYR A CE2 
2327 C  CZ  . TYR A 298 ? 0.3111 0.2776 0.3303 0.0489  -0.0430 0.0399  522  TYR A CZ  
2328 O  OH  . TYR A 298 ? 0.3280 0.2919 0.3383 0.0493  -0.0456 0.0436  522  TYR A OH  
2329 N  N   . SER A 299 ? 0.2646 0.2544 0.3227 0.0593  -0.0427 0.0275  523  SER A N   
2330 C  CA  . SER A 299 ? 0.2652 0.2667 0.3324 0.0609  -0.0452 0.0255  523  SER A CA  
2331 C  C   . SER A 299 ? 0.2577 0.2638 0.3209 0.0577  -0.0480 0.0263  523  SER A C   
2332 O  O   . SER A 299 ? 0.2631 0.2649 0.3189 0.0588  -0.0519 0.0296  523  SER A O   
2333 C  CB  . SER A 299 ? 0.2666 0.2690 0.3398 0.0674  -0.0494 0.0265  523  SER A CB  
2334 O  OG  . SER A 299 ? 0.3534 0.3678 0.4372 0.0687  -0.0518 0.0242  523  SER A OG  
2335 N  N   . LEU A 300 ? 0.2816 0.2961 0.3495 0.0542  -0.0461 0.0233  524  LEU A N   
2336 C  CA  . LEU A 300 ? 0.2529 0.2715 0.3172 0.0507  -0.0482 0.0234  524  LEU A CA  
2337 C  C   . LEU A 300 ? 0.3234 0.3516 0.3961 0.0528  -0.0532 0.0221  524  LEU A C   
2338 O  O   . LEU A 300 ? 0.2757 0.3108 0.3601 0.0553  -0.0531 0.0200  524  LEU A O   
2339 C  CB  . LEU A 300 ? 0.2343 0.2556 0.2985 0.0454  -0.0433 0.0209  524  LEU A CB  
2340 C  CG  . LEU A 300 ? 0.3104 0.3241 0.3681 0.0427  -0.0383 0.0210  524  LEU A CG  
2341 C  CD1 . LEU A 300 ? 0.2249 0.2427 0.2836 0.0383  -0.0342 0.0183  524  LEU A CD1 
2342 C  CD2 . LEU A 300 ? 0.2432 0.2480 0.2897 0.0415  -0.0392 0.0244  524  LEU A CD2 
2343 N  N   . ALA A 301 ? 0.2676 0.2966 0.3346 0.0518  -0.0575 0.0233  525  ALA A N   
2344 C  CA  . ALA A 301 ? 0.3223 0.3609 0.3973 0.0529  -0.0625 0.0214  525  ALA A CA  
2345 C  C   . ALA A 301 ? 0.2708 0.3177 0.3537 0.0485  -0.0592 0.0178  525  ALA A C   
2346 O  O   . ALA A 301 ? 0.2632 0.3074 0.3402 0.0440  -0.0550 0.0175  525  ALA A O   
2347 C  CB  . ALA A 301 ? 0.2803 0.3166 0.3457 0.0532  -0.0683 0.0233  525  ALA A CB  
2348 N  N   . PRO A 302 ? 0.2330 0.2897 0.3294 0.0496  -0.0608 0.0152  526  PRO A N   
2349 C  CA  . PRO A 302 ? 0.2797 0.3438 0.3843 0.0454  -0.0568 0.0120  526  PRO A CA  
2350 C  C   . PRO A 302 ? 0.3077 0.3724 0.4065 0.0408  -0.0580 0.0114  526  PRO A C   
2351 O  O   . PRO A 302 ? 0.2560 0.3189 0.3481 0.0414  -0.0636 0.0123  526  PRO A O   
2352 C  CB  . PRO A 302 ? 0.2628 0.3375 0.3837 0.0481  -0.0595 0.0098  526  PRO A CB  
2353 C  CG  . PRO A 302 ? 0.2987 0.3704 0.4206 0.0541  -0.0619 0.0115  526  PRO A CG  
2354 C  CD  . PRO A 302 ? 0.3363 0.3975 0.4424 0.0552  -0.0650 0.0150  526  PRO A CD  
2355 N  N   . VAL A 303 ? 0.3171 0.3840 0.4182 0.0364  -0.0527 0.0096  527  VAL A N   
2356 C  CA  . VAL A 303 ? 0.2673 0.3357 0.3654 0.0320  -0.0533 0.0083  527  VAL A CA  
2357 C  C   . VAL A 303 ? 0.3953 0.4722 0.5062 0.0293  -0.0503 0.0054  527  VAL A C   
2358 O  O   . VAL A 303 ? 0.3917 0.4721 0.5117 0.0304  -0.0462 0.0047  527  VAL A O   
2359 C  CB  . VAL A 303 ? 0.2785 0.3389 0.3636 0.0289  -0.0493 0.0097  527  VAL A CB  
2360 C  CG1 . VAL A 303 ? 0.2968 0.3552 0.3831 0.0280  -0.0423 0.0095  527  VAL A CG1 
2361 C  CG2 . VAL A 303 ? 0.2996 0.3617 0.3821 0.0247  -0.0499 0.0082  527  VAL A CG2 
2362 N  N   . LYS B 1   ? 0.7518 0.7319 0.7446 -0.0244 0.0447  0.0478  225  LYS B N   
2363 C  CA  . LYS B 1   ? 0.7342 0.7186 0.7362 -0.0250 0.0390  0.0428  225  LYS B CA  
2364 C  C   . LYS B 1   ? 0.6952 0.6872 0.7094 -0.0276 0.0405  0.0388  225  LYS B C   
2365 O  O   . LYS B 1   ? 0.6583 0.6554 0.6715 -0.0269 0.0423  0.0373  225  LYS B O   
2366 C  CB  . LYS B 1   ? 0.7604 0.7467 0.7553 -0.0214 0.0329  0.0402  225  LYS B CB  
2367 C  CG  . LYS B 1   ? 0.6876 0.6789 0.6907 -0.0217 0.0278  0.0350  225  LYS B CG  
2368 C  CD  . LYS B 1   ? 0.5870 0.5800 0.5835 -0.0185 0.0226  0.0328  225  LYS B CD  
2369 C  CE  . LYS B 1   ? 0.6780 0.6656 0.6688 -0.0165 0.0193  0.0350  225  LYS B CE  
2370 N  NZ  . LYS B 1   ? 0.7127 0.7024 0.6981 -0.0136 0.0146  0.0330  225  LYS B NZ  
2371 N  N   . ALA B 2   ? 0.6131 0.6056 0.6388 -0.0303 0.0392  0.0368  226  ALA B N   
2372 C  CA  . ALA B 2   ? 0.5068 0.5062 0.5454 -0.0328 0.0400  0.0329  226  ALA B CA  
2373 C  C   . ALA B 2   ? 0.4266 0.4322 0.4664 -0.0308 0.0344  0.0277  226  ALA B C   
2374 O  O   . ALA B 2   ? 0.3957 0.3997 0.4316 -0.0288 0.0291  0.0261  226  ALA B O   
2375 C  CB  . ALA B 2   ? 0.5061 0.5035 0.5563 -0.0363 0.0397  0.0321  226  ALA B CB  
2376 N  N   . PHE B 3   ? 0.3863 0.3988 0.4318 -0.0313 0.0360  0.0251  227  PHE B N   
2377 C  CA  . PHE B 3   ? 0.3401 0.3582 0.3874 -0.0294 0.0312  0.0203  227  PHE B CA  
2378 C  C   . PHE B 3   ? 0.2718 0.2908 0.3279 -0.0306 0.0263  0.0167  227  PHE B C   
2379 O  O   . PHE B 3   ? 0.2870 0.3060 0.3530 -0.0336 0.0276  0.0163  227  PHE B O   
2380 C  CB  . PHE B 3   ? 0.3397 0.3648 0.3919 -0.0295 0.0343  0.0185  227  PHE B CB  
2381 C  CG  . PHE B 3   ? 0.3113 0.3418 0.3662 -0.0276 0.0296  0.0138  227  PHE B CG  
2382 C  CD1 . PHE B 3   ? 0.2747 0.3047 0.3197 -0.0244 0.0267  0.0131  227  PHE B CD1 
2383 C  CD2 . PHE B 3   ? 0.2864 0.3224 0.3536 -0.0289 0.0280  0.0101  227  PHE B CD2 
2384 C  CE1 . PHE B 3   ? 0.2566 0.2907 0.3035 -0.0226 0.0228  0.0091  227  PHE B CE1 
2385 C  CE2 . PHE B 3   ? 0.2491 0.2894 0.3177 -0.0268 0.0236  0.0061  227  PHE B CE2 
2386 C  CZ  . PHE B 3   ? 0.2904 0.3294 0.3485 -0.0236 0.0212  0.0058  227  PHE B CZ  
2387 N  N   . THR B 4   ? 0.3127 0.3321 0.3650 -0.0281 0.0208  0.0139  228  THR B N   
2388 C  CA  . THR B 4   ? 0.3169 0.3367 0.3754 -0.0285 0.0160  0.0103  228  THR B CA  
2389 C  C   . THR B 4   ? 0.2741 0.2978 0.3305 -0.0258 0.0117  0.0066  228  THR B C   
2390 O  O   . THR B 4   ? 0.3064 0.3310 0.3554 -0.0236 0.0118  0.0072  228  THR B O   
2391 C  CB  . THR B 4   ? 0.2800 0.2931 0.3344 -0.0281 0.0137  0.0115  228  THR B CB  
2392 O  OG1 . THR B 4   ? 0.3002 0.3112 0.3438 -0.0252 0.0122  0.0129  228  THR B OG1 
2393 C  CG2 . THR B 4   ? 0.3103 0.3181 0.3666 -0.0307 0.0176  0.0153  228  THR B CG2 
2394 N  N   . ILE B 5   ? 0.2974 0.3229 0.3602 -0.0260 0.0078  0.0028  229  ILE B N   
2395 C  CA  . ILE B 5   ? 0.3200 0.3481 0.3811 -0.0234 0.0033  -0.0008 229  ILE B CA  
2396 C  C   . ILE B 5   ? 0.3078 0.3314 0.3657 -0.0225 -0.0006 -0.0020 229  ILE B C   
2397 O  O   . ILE B 5   ? 0.2948 0.3155 0.3573 -0.0243 -0.0009 -0.0022 229  ILE B O   
2398 C  CB  . ILE B 5   ? 0.3198 0.3538 0.3909 -0.0240 0.0018  -0.0045 229  ILE B CB  
2399 C  CG1 . ILE B 5   ? 0.3887 0.4276 0.4643 -0.0250 0.0062  -0.0035 229  ILE B CG1 
2400 C  CG2 . ILE B 5   ? 0.3639 0.3996 0.4320 -0.0210 -0.0030 -0.0078 229  ILE B CG2 
2401 C  CD1 . ILE B 5   ? 0.3182 0.3581 0.3853 -0.0223 0.0074  -0.0024 229  ILE B CD1 
2402 N  N   . PRO B 6   ? 0.3237 0.3465 0.3745 -0.0197 -0.0034 -0.0028 230  PRO B N   
2403 C  CA  . PRO B 6   ? 0.2964 0.3156 0.3451 -0.0185 -0.0068 -0.0045 230  PRO B CA  
2404 C  C   . PRO B 6   ? 0.3529 0.3739 0.4076 -0.0186 -0.0104 -0.0088 230  PRO B C   
2405 O  O   . PRO B 6   ? 0.2911 0.3168 0.3494 -0.0182 -0.0114 -0.0109 230  PRO B O   
2406 C  CB  . PRO B 6   ? 0.3197 0.3383 0.3597 -0.0156 -0.0080 -0.0041 230  PRO B CB  
2407 C  CG  . PRO B 6   ? 0.2870 0.3098 0.3263 -0.0151 -0.0068 -0.0040 230  PRO B CG  
2408 C  CD  . PRO B 6   ? 0.2903 0.3148 0.3344 -0.0175 -0.0030 -0.0021 230  PRO B CD  
2409 N  N   . VAL B 7   ? 0.2942 0.3113 0.3498 -0.0187 -0.0127 -0.0105 231  VAL B N   
2410 C  CA  . VAL B 7   ? 0.2817 0.2996 0.3426 -0.0187 -0.0167 -0.0150 231  VAL B CA  
2411 C  C   . VAL B 7   ? 0.2944 0.3118 0.3481 -0.0151 -0.0203 -0.0174 231  VAL B C   
2412 O  O   . VAL B 7   ? 0.3173 0.3304 0.3646 -0.0134 -0.0210 -0.0172 231  VAL B O   
2413 C  CB  . VAL B 7   ? 0.3327 0.3459 0.3977 -0.0207 -0.0174 -0.0160 231  VAL B CB  
2414 C  CG1 . VAL B 7   ? 0.3430 0.3569 0.4131 -0.0205 -0.0223 -0.0213 231  VAL B CG1 
2415 C  CG2 . VAL B 7   ? 0.3564 0.3693 0.4283 -0.0244 -0.0134 -0.0131 231  VAL B CG2 
2416 N  N   . LEU B 8   ? 0.2918 0.3134 0.3465 -0.0137 -0.0224 -0.0195 232  LEU B N   
2417 C  CA  . LEU B 8   ? 0.2751 0.2959 0.3219 -0.0100 -0.0252 -0.0211 232  LEU B CA  
2418 C  C   . LEU B 8   ? 0.2602 0.2842 0.3107 -0.0087 -0.0295 -0.0251 232  LEU B C   
2419 O  O   . LEU B 8   ? 0.2369 0.2659 0.2947 -0.0098 -0.0293 -0.0256 232  LEU B O   
2420 C  CB  . LEU B 8   ? 0.2912 0.3132 0.3320 -0.0086 -0.0226 -0.0181 232  LEU B CB  
2421 C  CG  . LEU B 8   ? 0.2804 0.3002 0.3172 -0.0095 -0.0189 -0.0141 232  LEU B CG  
2422 C  CD1 . LEU B 8   ? 0.3421 0.3645 0.3759 -0.0087 -0.0169 -0.0122 232  LEU B CD1 
2423 C  CD2 . LEU B 8   ? 0.3418 0.3572 0.3718 -0.0076 -0.0196 -0.0139 232  LEU B CD2 
2424 N  N   . LYS B 9   ? 0.2825 0.3035 0.3274 -0.0060 -0.0334 -0.0279 233  LYS B N   
2425 C  CA  . LYS B 9   ? 0.2836 0.3071 0.3288 -0.0035 -0.0379 -0.0313 233  LYS B CA  
2426 C  C   . LYS B 9   ? 0.2684 0.2937 0.3083 -0.0011 -0.0368 -0.0293 233  LYS B C   
2427 O  O   . LYS B 9   ? 0.2756 0.2992 0.3098 -0.0009 -0.0331 -0.0258 233  LYS B O   
2428 C  CB  . LYS B 9   ? 0.2840 0.3027 0.3222 -0.0006 -0.0421 -0.0345 233  LYS B CB  
2429 C  CG  . LYS B 9   ? 0.4194 0.4355 0.4624 -0.0026 -0.0439 -0.0373 233  LYS B CG  
2430 C  CD  . LYS B 9   ? 0.4653 0.4765 0.5003 0.0007  -0.0482 -0.0409 233  LYS B CD  
2431 C  CE  . LYS B 9   ? 0.5337 0.5393 0.5582 0.0025  -0.0451 -0.0385 233  LYS B CE  
2432 N  NZ  . LYS B 9   ? 0.5949 0.5950 0.6144 0.0044  -0.0483 -0.0423 233  LYS B NZ  
2433 N  N   . ILE B 10  ? 0.2599 0.2886 0.3021 0.0009  -0.0403 -0.0317 234  ILE B N   
2434 C  CA  . ILE B 10  ? 0.3483 0.3777 0.3849 0.0036  -0.0395 -0.0300 234  ILE B CA  
2435 C  C   . ILE B 10  ? 0.3270 0.3506 0.3510 0.0063  -0.0389 -0.0284 234  ILE B C   
2436 O  O   . ILE B 10  ? 0.3037 0.3262 0.3227 0.0068  -0.0357 -0.0253 234  ILE B O   
2437 C  CB  . ILE B 10  ? 0.3257 0.3590 0.3662 0.0060  -0.0442 -0.0332 234  ILE B CB  
2438 C  CG1 . ILE B 10  ? 0.2751 0.3153 0.3300 0.0031  -0.0440 -0.0347 234  ILE B CG1 
2439 C  CG2 . ILE B 10  ? 0.3770 0.4099 0.4109 0.0092  -0.0435 -0.0313 234  ILE B CG2 
2440 C  CD1 . ILE B 10  ? 0.3319 0.3750 0.3907 0.0006  -0.0382 -0.0312 234  ILE B CD1 
2441 N  N   . SER B 11  ? 0.3405 0.3600 0.3593 0.0080  -0.0418 -0.0306 235  SER B N   
2442 C  CA  . SER B 11  ? 0.3696 0.3836 0.3765 0.0108  -0.0410 -0.0293 235  SER B CA  
2443 C  C   . SER B 11  ? 0.3772 0.3888 0.3816 0.0090  -0.0361 -0.0260 235  SER B C   
2444 O  O   . SER B 11  ? 0.4625 0.4701 0.4581 0.0110  -0.0345 -0.0245 235  SER B O   
2445 C  CB  . SER B 11  ? 0.3901 0.4003 0.3918 0.0134  -0.0454 -0.0329 235  SER B CB  
2446 O  OG  . SER B 11  ? 0.3682 0.3772 0.3740 0.0111  -0.0455 -0.0345 235  SER B OG  
2447 N  N   . GLU B 12  ? 0.3338 0.3476 0.3456 0.0054  -0.0337 -0.0248 236  GLU B N   
2448 C  CA  . GLU B 12  ? 0.3739 0.3859 0.3837 0.0039  -0.0295 -0.0216 236  GLU B CA  
2449 C  C   . GLU B 12  ? 0.3144 0.3291 0.3256 0.0026  -0.0262 -0.0184 236  GLU B C   
2450 O  O   . GLU B 12  ? 0.3297 0.3434 0.3393 0.0015  -0.0231 -0.0157 236  GLU B O   
2451 C  CB  . GLU B 12  ? 0.3081 0.3196 0.3237 0.0012  -0.0290 -0.0220 236  GLU B CB  
2452 C  CG  . GLU B 12  ? 0.3758 0.3834 0.3890 0.0026  -0.0319 -0.0253 236  GLU B CG  
2453 C  CD  . GLU B 12  ? 0.4037 0.4105 0.4240 -0.0001 -0.0322 -0.0264 236  GLU B CD  
2454 O  OE1 . GLU B 12  ? 0.3703 0.3805 0.3989 -0.0031 -0.0313 -0.0256 236  GLU B OE1 
2455 O  OE2 . GLU B 12  ? 0.4785 0.4811 0.4962 0.0007  -0.0332 -0.0281 236  GLU B OE2 
2456 N  N   . MET B 13  ? 0.2634 0.2815 0.2774 0.0029  -0.0270 -0.0188 237  MET B N   
2457 C  CA  . MET B 13  ? 0.2591 0.2796 0.2744 0.0018  -0.0241 -0.0164 237  MET B CA  
2458 C  C   . MET B 13  ? 0.2539 0.2721 0.2617 0.0040  -0.0232 -0.0149 237  MET B C   
2459 O  O   . MET B 13  ? 0.2680 0.2840 0.2707 0.0068  -0.0252 -0.0159 237  MET B O   
2460 C  CB  . MET B 13  ? 0.2782 0.3035 0.3008 0.0012  -0.0250 -0.0178 237  MET B CB  
2461 C  CG  . MET B 13  ? 0.2747 0.3027 0.3061 -0.0016 -0.0249 -0.0188 237  MET B CG  
2462 S  SD  . MET B 13  ? 0.3091 0.3436 0.3501 -0.0021 -0.0254 -0.0205 237  MET B SD  
2463 C  CE  . MET B 13  ? 0.3103 0.3470 0.3616 -0.0063 -0.0238 -0.0208 237  MET B CE  
2464 N  N   . THR B 14  ? 0.2165 0.2352 0.2238 0.0027  -0.0201 -0.0124 238  THR B N   
2465 C  CA  . THR B 14  ? 0.2513 0.2679 0.2530 0.0040  -0.0187 -0.0108 238  THR B CA  
2466 C  C   . THR B 14  ? 0.2196 0.2386 0.2232 0.0042  -0.0182 -0.0107 238  THR B C   
2467 O  O   . THR B 14  ? 0.2242 0.2462 0.2325 0.0023  -0.0169 -0.0104 238  THR B O   
2468 C  CB  . THR B 14  ? 0.2450 0.2602 0.2449 0.0025  -0.0161 -0.0085 238  THR B CB  
2469 O  OG1 . THR B 14  ? 0.2411 0.2543 0.2397 0.0026  -0.0163 -0.0087 238  THR B OG1 
2470 C  CG2 . THR B 14  ? 0.2321 0.2452 0.2274 0.0034  -0.0147 -0.0070 238  THR B CG2 
2471 N  N   . ASN B 15  ? 0.2321 0.2491 0.2316 0.0066  -0.0190 -0.0107 239  ASN B N   
2472 C  CA  . ASN B 15  ? 0.2019 0.2204 0.2027 0.0070  -0.0184 -0.0107 239  ASN B CA  
2473 C  C   . ASN B 15  ? 0.2369 0.2549 0.2369 0.0050  -0.0154 -0.0088 239  ASN B C   
2474 O  O   . ASN B 15  ? 0.2274 0.2427 0.2238 0.0044  -0.0142 -0.0073 239  ASN B O   
2475 C  CB  . ASN B 15  ? 0.1976 0.2129 0.1935 0.0102  -0.0199 -0.0108 239  ASN B CB  
2476 C  CG  . ASN B 15  ? 0.2426 0.2600 0.2413 0.0116  -0.0203 -0.0117 239  ASN B CG  
2477 O  OD1 . ASN B 15  ? 0.2247 0.2425 0.2242 0.0105  -0.0181 -0.0110 239  ASN B OD1 
2478 N  ND2 . ASN B 15  ? 0.2135 0.2322 0.2138 0.0141  -0.0235 -0.0136 239  ASN B ND2 
2479 N  N   . SER B 16  ? 0.2252 0.2462 0.2288 0.0041  -0.0142 -0.0091 240  SER B N   
2480 C  CA  . SER B 16  ? 0.2111 0.2315 0.2132 0.0025  -0.0119 -0.0078 240  SER B CA  
2481 C  C   . SER B 16  ? 0.2233 0.2412 0.2221 0.0039  -0.0115 -0.0077 240  SER B C   
2482 O  O   . SER B 16  ? 0.2137 0.2306 0.2109 0.0027  -0.0101 -0.0070 240  SER B O   
2483 C  CB  . SER B 16  ? 0.2232 0.2474 0.2296 0.0010  -0.0103 -0.0080 240  SER B CB  
2484 O  OG  . SER B 16  ? 0.2257 0.2527 0.2358 0.0024  -0.0107 -0.0096 240  SER B OG  
2485 N  N   . ARG B 17  ? 0.1967 0.2130 0.1941 0.0064  -0.0130 -0.0085 241  ARG B N   
2486 C  CA  . ARG B 17  ? 0.2449 0.2577 0.2390 0.0077  -0.0125 -0.0083 241  ARG B CA  
2487 C  C   . ARG B 17  ? 0.2627 0.2703 0.2515 0.0088  -0.0128 -0.0070 241  ARG B C   
2488 O  O   . ARG B 17  ? 0.2149 0.2187 0.2009 0.0094  -0.0120 -0.0064 241  ARG B O   
2489 C  CB  . ARG B 17  ? 0.2312 0.2455 0.2274 0.0103  -0.0135 -0.0099 241  ARG B CB  
2490 C  CG  . ARG B 17  ? 0.1934 0.2128 0.1948 0.0092  -0.0123 -0.0110 241  ARG B CG  
2491 C  CD  . ARG B 17  ? 0.2127 0.2342 0.2174 0.0119  -0.0131 -0.0128 241  ARG B CD  
2492 N  NE  . ARG B 17  ? 0.2197 0.2368 0.2204 0.0138  -0.0128 -0.0128 241  ARG B NE  
2493 C  CZ  . ARG B 17  ? 0.2264 0.2422 0.2270 0.0171  -0.0144 -0.0136 241  ARG B CZ  
2494 N  NH1 . ARG B 17  ? 0.2180 0.2373 0.2228 0.0192  -0.0168 -0.0148 241  ARG B NH1 
2495 N  NH2 . ARG B 17  ? 0.2256 0.2361 0.2220 0.0185  -0.0140 -0.0133 241  ARG B NH2 
2496 N  N   . PHE B 18  ? 0.2680 0.2751 0.2555 0.0089  -0.0135 -0.0064 242  PHE B N   
2497 C  CA  . PHE B 18  ? 0.2240 0.2261 0.2061 0.0099  -0.0130 -0.0049 242  PHE B CA  
2498 C  C   . PHE B 18  ? 0.2564 0.2593 0.2382 0.0091  -0.0129 -0.0046 242  PHE B C   
2499 O  O   . PHE B 18  ? 0.2396 0.2455 0.2241 0.0093  -0.0147 -0.0060 242  PHE B O   
2500 C  CB  . PHE B 18  ? 0.2211 0.2199 0.1992 0.0135  -0.0148 -0.0051 242  PHE B CB  
2501 C  CG  . PHE B 18  ? 0.2398 0.2322 0.2116 0.0146  -0.0132 -0.0030 242  PHE B CG  
2502 C  CD1 . PHE B 18  ? 0.2269 0.2159 0.1978 0.0141  -0.0115 -0.0020 242  PHE B CD1 
2503 C  CD2 . PHE B 18  ? 0.2147 0.2042 0.1813 0.0161  -0.0132 -0.0021 242  PHE B CD2 
2504 C  CE1 . PHE B 18  ? 0.2793 0.2620 0.2449 0.0147  -0.0095 0.0002  242  PHE B CE1 
2505 C  CE2 . PHE B 18  ? 0.2527 0.2359 0.2132 0.0171  -0.0111 0.0002  242  PHE B CE2 
2506 C  CZ  . PHE B 18  ? 0.2262 0.2061 0.1867 0.0162  -0.0091 0.0016  242  PHE B CZ  
2507 N  N   . PRO B 19  ? 0.2809 0.2813 0.2604 0.0081  -0.0109 -0.0030 243  PRO B N   
2508 C  CA  . PRO B 19  ? 0.2308 0.2326 0.2112 0.0072  -0.0106 -0.0030 243  PRO B CA  
2509 C  C   . PRO B 19  ? 0.2499 0.2496 0.2261 0.0097  -0.0119 -0.0035 243  PRO B C   
2510 O  O   . PRO B 19  ? 0.2720 0.2686 0.2440 0.0104  -0.0102 -0.0024 243  PRO B O   
2511 C  CB  . PRO B 19  ? 0.2438 0.2443 0.2243 0.0054  -0.0078 -0.0012 243  PRO B CB  
2512 C  CG  . PRO B 19  ? 0.2707 0.2670 0.2477 0.0063  -0.0066 -0.0001 243  PRO B CG  
2513 C  CD  . PRO B 19  ? 0.2079 0.2046 0.1852 0.0075  -0.0086 -0.0013 243  PRO B CD  
2514 N  N   . VAL B 20  ? 0.2119 0.2132 0.1891 0.0111  -0.0148 -0.0055 244  VAL B N   
2515 C  CA  . VAL B 20  ? 0.2614 0.2610 0.2347 0.0137  -0.0171 -0.0068 244  VAL B CA  
2516 C  C   . VAL B 20  ? 0.2358 0.2397 0.2148 0.0130  -0.0200 -0.0093 244  VAL B C   
2517 O  O   . VAL B 20  ? 0.2333 0.2412 0.2186 0.0112  -0.0200 -0.0097 244  VAL B O   
2518 C  CB  . VAL B 20  ? 0.2387 0.2346 0.2060 0.0172  -0.0187 -0.0067 244  VAL B CB  
2519 C  CG1 . VAL B 20  ? 0.2400 0.2306 0.2012 0.0178  -0.0154 -0.0039 244  VAL B CG1 
2520 C  CG2 . VAL B 20  ? 0.2572 0.2558 0.2288 0.0176  -0.0205 -0.0076 244  VAL B CG2 
2521 N  N   . PRO B 21  ? 0.2558 0.2588 0.2329 0.0144  -0.0222 -0.0110 245  PRO B N   
2522 C  CA  . PRO B 21  ? 0.2545 0.2613 0.2381 0.0135  -0.0250 -0.0136 245  PRO B CA  
2523 C  C   . PRO B 21  ? 0.2378 0.2476 0.2252 0.0146  -0.0278 -0.0153 245  PRO B C   
2524 O  O   . PRO B 21  ? 0.2347 0.2425 0.2177 0.0174  -0.0289 -0.0150 245  PRO B O   
2525 C  CB  . PRO B 21  ? 0.2822 0.2861 0.2612 0.0154  -0.0272 -0.0155 245  PRO B CB  
2526 C  CG  . PRO B 21  ? 0.2870 0.2863 0.2583 0.0165  -0.0241 -0.0133 245  PRO B CG  
2527 C  CD  . PRO B 21  ? 0.2771 0.2753 0.2461 0.0169  -0.0221 -0.0108 245  PRO B CD  
2528 N  N   . VAL B 22  ? 0.2209 0.2356 0.2169 0.0125  -0.0288 -0.0169 246  VAL B N   
2529 C  CA  . VAL B 22  ? 0.2409 0.2595 0.2425 0.0136  -0.0318 -0.0191 246  VAL B CA  
2530 C  C   . VAL B 22  ? 0.2474 0.2645 0.2461 0.0167  -0.0367 -0.0219 246  VAL B C   
2531 O  O   . VAL B 22  ? 0.2554 0.2708 0.2526 0.0164  -0.0380 -0.0233 246  VAL B O   
2532 C  CB  . VAL B 22  ? 0.2437 0.2678 0.2558 0.0102  -0.0309 -0.0200 246  VAL B CB  
2533 C  CG1 . VAL B 22  ? 0.2241 0.2530 0.2437 0.0113  -0.0341 -0.0228 246  VAL B CG1 
2534 C  CG2 . VAL B 22  ? 0.1948 0.2200 0.2084 0.0079  -0.0264 -0.0173 246  VAL B CG2 
2535 N  N   . ASP B 23  ? 0.2516 0.2693 0.2494 0.0199  -0.0397 -0.0230 247  ASP B N   
2536 C  CA  . ASP B 23  ? 0.2609 0.2776 0.2561 0.0233  -0.0452 -0.0260 247  ASP B CA  
2537 C  C   . ASP B 23  ? 0.2701 0.2934 0.2768 0.0225  -0.0491 -0.0296 247  ASP B C   
2538 O  O   . ASP B 23  ? 0.2880 0.3115 0.2959 0.0230  -0.0532 -0.0328 247  ASP B O   
2539 C  CB  . ASP B 23  ? 0.2728 0.2855 0.2593 0.0279  -0.0469 -0.0249 247  ASP B CB  
2540 C  CG  . ASP B 23  ? 0.3925 0.3978 0.3669 0.0290  -0.0435 -0.0217 247  ASP B CG  
2541 O  OD1 . ASP B 23  ? 0.3801 0.3817 0.3481 0.0298  -0.0440 -0.0222 247  ASP B OD1 
2542 O  OD2 . ASP B 23  ? 0.2863 0.2894 0.2580 0.0291  -0.0402 -0.0187 247  ASP B OD2 
2543 N  N   . GLN B 24  ? 0.2403 0.2690 0.2559 0.0213  -0.0479 -0.0295 248  GLN B N   
2544 C  CA  . GLN B 24  ? 0.2358 0.2715 0.2636 0.0206  -0.0511 -0.0329 248  GLN B CA  
2545 C  C   . GLN B 24  ? 0.2497 0.2910 0.2871 0.0177  -0.0468 -0.0317 248  GLN B C   
2546 O  O   . GLN B 24  ? 0.2298 0.2694 0.2633 0.0177  -0.0429 -0.0288 248  GLN B O   
2547 C  CB  . GLN B 24  ? 0.2555 0.2921 0.2825 0.0254  -0.0571 -0.0355 248  GLN B CB  
2548 C  CG  . GLN B 24  ? 0.2492 0.2859 0.2744 0.0280  -0.0557 -0.0336 248  GLN B CG  
2549 C  CD  . GLN B 24  ? 0.2729 0.3096 0.2960 0.0335  -0.0618 -0.0356 248  GLN B CD  
2550 O  OE1 . GLN B 24  ? 0.2897 0.3289 0.3162 0.0356  -0.0618 -0.0353 248  GLN B OE1 
2551 N  NE2 . GLN B 24  ? 0.2758 0.3093 0.2928 0.0361  -0.0670 -0.0378 248  GLN B NE2 
2552 N  N   . MET B 25  ? 0.2446 0.2922 0.2945 0.0152  -0.0475 -0.0340 249  MET B N   
2553 C  CA  . MET B 25  ? 0.2562 0.3100 0.3161 0.0135  -0.0442 -0.0336 249  MET B CA  
2554 C  C   . MET B 25  ? 0.2229 0.2802 0.2858 0.0176  -0.0475 -0.0354 249  MET B C   
2555 O  O   . MET B 25  ? 0.2242 0.2810 0.2854 0.0210  -0.0535 -0.0379 249  MET B O   
2556 C  CB  . MET B 25  ? 0.2497 0.3091 0.3226 0.0093  -0.0433 -0.0353 249  MET B CB  
2557 C  CG  . MET B 25  ? 0.2423 0.2982 0.3129 0.0053  -0.0395 -0.0331 249  MET B CG  
2558 S  SD  . MET B 25  ? 0.2918 0.3530 0.3775 0.0002  -0.0380 -0.0346 249  MET B SD  
2559 C  CE  . MET B 25  ? 0.2793 0.3414 0.3696 0.0015  -0.0460 -0.0399 249  MET B CE  
2560 N  N   . TYR B 26  ? 0.2345 0.2949 0.3012 0.0176  -0.0438 -0.0341 250  TYR B N   
2561 C  CA  . TYR B 26  ? 0.2391 0.3019 0.3075 0.0221  -0.0465 -0.0354 250  TYR B CA  
2562 C  C   . TYR B 26  ? 0.2226 0.2922 0.3016 0.0208  -0.0422 -0.0355 250  TYR B C   
2563 O  O   . TYR B 26  ? 0.2412 0.3104 0.3198 0.0176  -0.0363 -0.0331 250  TYR B O   
2564 C  CB  . TYR B 26  ? 0.2344 0.2894 0.2887 0.0256  -0.0464 -0.0329 250  TYR B CB  
2565 C  CG  . TYR B 26  ? 0.2514 0.3073 0.3059 0.0308  -0.0498 -0.0341 250  TYR B CG  
2566 C  CD1 . TYR B 26  ? 0.2776 0.3330 0.3306 0.0349  -0.0567 -0.0365 250  TYR B CD1 
2567 C  CD2 . TYR B 26  ? 0.3016 0.3583 0.3573 0.0320  -0.0464 -0.0329 250  TYR B CD2 
2568 C  CE1 . TYR B 26  ? 0.3021 0.3580 0.3551 0.0401  -0.0602 -0.0374 250  TYR B CE1 
2569 C  CE2 . TYR B 26  ? 0.2911 0.3481 0.3470 0.0371  -0.0495 -0.0339 250  TYR B CE2 
2570 C  CZ  . TYR B 26  ? 0.3305 0.3873 0.3853 0.0412  -0.0565 -0.0361 250  TYR B CZ  
2571 O  OH  . TYR B 26  ? 0.4327 0.4895 0.4875 0.0467  -0.0599 -0.0369 250  TYR B OH  
2572 N  N   . THR B 27  ? 0.2255 0.3014 0.3139 0.0236  -0.0452 -0.0382 251  THR B N   
2573 C  CA  . THR B 27  ? 0.2187 0.3009 0.3166 0.0232  -0.0408 -0.0383 251  THR B CA  
2574 C  C   . THR B 27  ? 0.2327 0.3149 0.3290 0.0288  -0.0432 -0.0391 251  THR B C   
2575 O  O   . THR B 27  ? 0.2465 0.3264 0.3387 0.0329  -0.0494 -0.0404 251  THR B O   
2576 C  CB  . THR B 27  ? 0.2060 0.2978 0.3211 0.0203  -0.0405 -0.0410 251  THR B CB  
2577 O  OG1 . THR B 27  ? 0.1948 0.2916 0.3171 0.0192  -0.0342 -0.0402 251  THR B OG1 
2578 C  CG2 . THR B 27  ? 0.2293 0.3267 0.3535 0.0237  -0.0479 -0.0452 251  THR B CG2 
2579 N  N   . SER B 28  ? 0.2153 0.2994 0.3138 0.0291  -0.0382 -0.0381 252  SER B N   
2580 C  CA  . SER B 28  ? 0.2403 0.3234 0.3366 0.0344  -0.0395 -0.0385 252  SER B CA  
2581 C  C   . SER B 28  ? 0.2577 0.3478 0.3645 0.0343  -0.0345 -0.0393 252  SER B C   
2582 O  O   . SER B 28  ? 0.2324 0.3248 0.3424 0.0301  -0.0284 -0.0382 252  SER B O   
2583 C  CB  . SER B 28  ? 0.3058 0.3784 0.3859 0.0358  -0.0381 -0.0354 252  SER B CB  
2584 O  OG  . SER B 28  ? 0.3376 0.4089 0.4164 0.0402  -0.0378 -0.0355 252  SER B OG  
2585 N  N   . ARG B 29  ? 0.2325 0.3257 0.3440 0.0394  -0.0370 -0.0412 253  ARG B N   
2586 C  CA  . ARG B 29  ? 0.2733 0.3720 0.3929 0.0406  -0.0321 -0.0421 253  ARG B CA  
2587 C  C   . ARG B 29  ? 0.3084 0.3994 0.4161 0.0414  -0.0273 -0.0396 253  ARG B C   
2588 O  O   . ARG B 29  ? 0.2929 0.3872 0.4048 0.0411  -0.0217 -0.0398 253  ARG B O   
2589 C  CB  . ARG B 29  ? 0.3344 0.4389 0.4635 0.0463  -0.0372 -0.0453 253  ARG B CB  
2590 C  CG  . ARG B 29  ? 0.4466 0.5598 0.5887 0.0476  -0.0327 -0.0471 253  ARG B CG  
2591 C  CD  . ARG B 29  ? 0.4288 0.5475 0.5802 0.0537  -0.0387 -0.0502 253  ARG B CD  
2592 N  NE  . ARG B 29  ? 0.4972 0.6185 0.6529 0.0543  -0.0468 -0.0523 253  ARG B NE  
2593 C  CZ  . ARG B 29  ? 0.4922 0.6237 0.6638 0.0518  -0.0483 -0.0551 253  ARG B CZ  
2594 N  NH1 . ARG B 29  ? 0.4957 0.6360 0.6810 0.0482  -0.0418 -0.0557 253  ARG B NH1 
2595 N  NH2 . ARG B 29  ? 0.4144 0.5474 0.5886 0.0530  -0.0567 -0.0573 253  ARG B NH2 
2596 N  N   . SER B 30  ? 0.2668 0.3477 0.3599 0.0422  -0.0294 -0.0374 254  SER B N   
2597 C  CA  . SER B 30  ? 0.2994 0.3723 0.3813 0.0427  -0.0255 -0.0353 254  SER B CA  
2598 C  C   . SER B 30  ? 0.3172 0.3911 0.4020 0.0475  -0.0245 -0.0368 254  SER B C   
2599 O  O   . SER B 30  ? 0.3115 0.3834 0.3933 0.0471  -0.0193 -0.0364 254  SER B O   
2600 C  CB  . SER B 30  ? 0.3123 0.3850 0.3920 0.0374  -0.0191 -0.0336 254  SER B CB  
2601 O  OG  . SER B 30  ? 0.2824 0.3536 0.3592 0.0333  -0.0201 -0.0322 254  SER B OG  
2602 N  N   . GLU B 31  ? 0.3166 0.3933 0.4069 0.0524  -0.0298 -0.0388 255  GLU B N   
2603 C  CA  . GLU B 31  ? 0.3616 0.4388 0.4548 0.0578  -0.0295 -0.0403 255  GLU B CA  
2604 C  C   . GLU B 31  ? 0.4181 0.4836 0.4972 0.0595  -0.0281 -0.0382 255  GLU B C   
2605 O  O   . GLU B 31  ? 0.3435 0.4003 0.4115 0.0599  -0.0312 -0.0361 255  GLU B O   
2606 C  CB  . GLU B 31  ? 0.4023 0.4830 0.5018 0.0633  -0.0367 -0.0424 255  GLU B CB  
2607 C  CG  . GLU B 31  ? 0.4916 0.5857 0.6094 0.0632  -0.0375 -0.0457 255  GLU B CG  
2608 C  CD  . GLU B 31  ? 0.5986 0.6995 0.7258 0.0625  -0.0302 -0.0469 255  GLU B CD  
2609 O  OE1 . GLU B 31  ? 0.6723 0.7719 0.7995 0.0671  -0.0290 -0.0478 255  GLU B OE1 
2610 O  OE2 . GLU B 31  ? 0.5751 0.6820 0.7091 0.0573  -0.0255 -0.0469 255  GLU B OE2 
2611 N  N   . GLY B 32  ? 0.3791 0.4445 0.4588 0.0604  -0.0230 -0.0390 256  GLY B N   
2612 C  CA  . GLY B 32  ? 0.4257 0.4803 0.4935 0.0618  -0.0215 -0.0376 256  GLY B CA  
2613 C  C   . GLY B 32  ? 0.4095 0.4565 0.4657 0.0568  -0.0195 -0.0349 256  GLY B C   
2614 O  O   . GLY B 32  ? 0.3629 0.3998 0.4087 0.0578  -0.0199 -0.0334 256  GLY B O   
2615 N  N   . ILE B 33  ? 0.3318 0.3832 0.3901 0.0516  -0.0171 -0.0342 257  ILE B N   
2616 C  CA  . ILE B 33  ? 0.3388 0.3840 0.3874 0.0469  -0.0160 -0.0316 257  ILE B CA  
2617 C  C   . ILE B 33  ? 0.3681 0.4168 0.4180 0.0426  -0.0103 -0.0315 257  ILE B C   
2618 O  O   . ILE B 33  ? 0.2949 0.3523 0.3544 0.0414  -0.0082 -0.0327 257  ILE B O   
2619 C  CB  . ILE B 33  ? 0.3450 0.3907 0.3930 0.0452  -0.0202 -0.0303 257  ILE B CB  
2620 C  CG1 . ILE B 33  ? 0.3666 0.4048 0.4073 0.0490  -0.0251 -0.0292 257  ILE B CG1 
2621 C  CG2 . ILE B 33  ? 0.3462 0.3903 0.3894 0.0396  -0.0178 -0.0283 257  ILE B CG2 
2622 C  CD1 . ILE B 33  ? 0.4316 0.4710 0.4725 0.0488  -0.0298 -0.0288 257  ILE B CD1 
2623 N  N   . VAL B 34  ? 0.3383 0.3801 0.3787 0.0403  -0.0079 -0.0302 258  VAL B N   
2624 C  CA  . VAL B 34  ? 0.2716 0.3150 0.3105 0.0363  -0.0032 -0.0297 258  VAL B CA  
2625 C  C   . VAL B 34  ? 0.2869 0.3279 0.3210 0.0320  -0.0045 -0.0272 258  VAL B C   
2626 O  O   . VAL B 34  ? 0.2598 0.2934 0.2859 0.0316  -0.0065 -0.0258 258  VAL B O   
2627 C  CB  . VAL B 34  ? 0.2821 0.3199 0.3139 0.0370  -0.0002 -0.0305 258  VAL B CB  
2628 C  CG1 . VAL B 34  ? 0.2525 0.2913 0.2811 0.0332  0.0042  -0.0298 258  VAL B CG1 
2629 C  CG2 . VAL B 34  ? 0.3362 0.3764 0.3731 0.0417  0.0012  -0.0331 258  VAL B CG2 
2630 N  N   . VAL B 35  ? 0.2148 0.2618 0.2542 0.0289  -0.0031 -0.0267 259  VAL B N   
2631 C  CA  . VAL B 35  ? 0.2573 0.3026 0.2934 0.0251  -0.0042 -0.0245 259  VAL B CA  
2632 C  C   . VAL B 35  ? 0.2528 0.2952 0.2824 0.0221  -0.0005 -0.0233 259  VAL B C   
2633 O  O   . VAL B 35  ? 0.2253 0.2719 0.2577 0.0204  0.0033  -0.0233 259  VAL B O   
2634 C  CB  . VAL B 35  ? 0.2537 0.3062 0.2989 0.0233  -0.0049 -0.0247 259  VAL B CB  
2635 C  CG1 . VAL B 35  ? 0.2296 0.2795 0.2707 0.0197  -0.0061 -0.0226 259  VAL B CG1 
2636 C  CG2 . VAL B 35  ? 0.2590 0.3147 0.3108 0.0268  -0.0092 -0.0265 259  VAL B CG2 
2637 N  N   . GLN B 36  ? 0.2039 0.2390 0.2246 0.0214  -0.0017 -0.0222 260  GLN B N   
2638 C  CA  . GLN B 36  ? 0.2347 0.2671 0.2493 0.0189  0.0009  -0.0214 260  GLN B CA  
2639 C  C   . GLN B 36  ? 0.2545 0.2815 0.2629 0.0166  -0.0013 -0.0195 260  GLN B C   
2640 O  O   . GLN B 36  ? 0.2524 0.2741 0.2546 0.0162  -0.0012 -0.0195 260  GLN B O   
2641 C  CB  . GLN B 36  ? 0.2059 0.2352 0.2166 0.0210  0.0029  -0.0232 260  GLN B CB  
2642 C  CG  . GLN B 36  ? 0.2192 0.2467 0.2238 0.0189  0.0058  -0.0230 260  GLN B CG  
2643 C  CD  . GLN B 36  ? 0.2188 0.2441 0.2201 0.0214  0.0080  -0.0254 260  GLN B CD  
2644 O  OE1 . GLN B 36  ? 0.2397 0.2643 0.2434 0.0247  0.0074  -0.0272 260  GLN B OE1 
2645 N  NE2 . GLN B 36  ? 0.2294 0.2531 0.2247 0.0202  0.0103  -0.0257 260  GLN B NE2 
2646 N  N   . PRO B 37  ? 0.2561 0.2845 0.2665 0.0151  -0.0032 -0.0180 261  PRO B N   
2647 C  CA  . PRO B 37  ? 0.2063 0.2301 0.2115 0.0131  -0.0047 -0.0163 261  PRO B CA  
2648 C  C   . PRO B 37  ? 0.2260 0.2489 0.2274 0.0104  -0.0027 -0.0155 261  PRO B C   
2649 O  O   . PRO B 37  ? 0.2246 0.2509 0.2274 0.0096  -0.0002 -0.0156 261  PRO B O   
2650 C  CB  . PRO B 37  ? 0.2104 0.2369 0.2191 0.0123  -0.0066 -0.0154 261  PRO B CB  
2651 C  CG  . PRO B 37  ? 0.2046 0.2376 0.2202 0.0117  -0.0049 -0.0161 261  PRO B CG  
2652 C  CD  . PRO B 37  ? 0.1918 0.2263 0.2096 0.0145  -0.0035 -0.0181 261  PRO B CD  
2653 N  N   . GLN B 38  ? 0.2107 0.2289 0.2071 0.0091  -0.0038 -0.0145 262  GLN B N   
2654 C  CA  . GLN B 38  ? 0.2280 0.2451 0.2207 0.0068  -0.0029 -0.0139 262  GLN B CA  
2655 C  C   . GLN B 38  ? 0.2129 0.2305 0.2058 0.0044  -0.0039 -0.0119 262  GLN B C   
2656 O  O   . GLN B 38  ? 0.2216 0.2396 0.2125 0.0027  -0.0032 -0.0111 262  GLN B O   
2657 C  CB  . GLN B 38  ? 0.1995 0.2112 0.1875 0.0070  -0.0036 -0.0149 262  GLN B CB  
2658 C  CG  . GLN B 38  ? 0.2040 0.2146 0.1913 0.0095  -0.0025 -0.0172 262  GLN B CG  
2659 C  CD  . GLN B 38  ? 0.2080 0.2222 0.1950 0.0097  0.0002  -0.0181 262  GLN B CD  
2660 O  OE1 . GLN B 38  ? 0.2070 0.2209 0.1903 0.0081  0.0009  -0.0178 262  GLN B OE1 
2661 N  NE2 . GLN B 38  ? 0.2354 0.2533 0.2267 0.0119  0.0019  -0.0191 262  GLN B NE2 
2662 N  N   . ASN B 39  ? 0.2254 0.2426 0.2200 0.0046  -0.0055 -0.0110 263  ASN B N   
2663 C  CA  . ASN B 39  ? 0.2305 0.2485 0.2259 0.0028  -0.0061 -0.0094 263  ASN B CA  
2664 C  C   . ASN B 39  ? 0.2583 0.2807 0.2585 0.0028  -0.0059 -0.0094 263  ASN B C   
2665 O  O   . ASN B 39  ? 0.2035 0.2283 0.2071 0.0044  -0.0059 -0.0106 263  ASN B O   
2666 C  CB  . ASN B 39  ? 0.1877 0.2024 0.1816 0.0032  -0.0077 -0.0086 263  ASN B CB  
2667 C  CG  . ASN B 39  ? 0.2301 0.2407 0.2205 0.0025  -0.0077 -0.0084 263  ASN B CG  
2668 O  OD1 . ASN B 39  ? 0.2393 0.2500 0.2288 0.0008  -0.0073 -0.0082 263  ASN B OD1 
2669 N  ND2 . ASN B 39  ? 0.2015 0.2082 0.1903 0.0039  -0.0081 -0.0086 263  ASN B ND2 
2670 N  N   . GLY B 40  ? 0.2163 0.2396 0.2172 0.0009  -0.0058 -0.0081 264  GLY B N   
2671 C  CA  . GLY B 40  ? 0.2303 0.2575 0.2364 0.0003  -0.0053 -0.0081 264  GLY B CA  
2672 C  C   . GLY B 40  ? 0.2128 0.2431 0.2212 0.0000  -0.0027 -0.0084 264  GLY B C   
2673 O  O   . GLY B 40  ? 0.2311 0.2651 0.2454 0.0002  -0.0021 -0.0093 264  GLY B O   
2674 N  N   . ARG B 41  ? 0.1883 0.2172 0.1923 -0.0005 -0.0009 -0.0079 265  ARG B N   
2675 C  CA  . ARG B 41  ? 0.1864 0.2175 0.1907 -0.0005 0.0023  -0.0080 265  ARG B CA  
2676 C  C   . ARG B 41  ? 0.2340 0.2644 0.2354 -0.0024 0.0038  -0.0059 265  ARG B C   
2677 O  O   . ARG B 41  ? 0.2285 0.2558 0.2241 -0.0026 0.0029  -0.0052 265  ARG B O   
2678 C  CB  . ARG B 41  ? 0.2050 0.2344 0.2052 0.0013  0.0029  -0.0096 265  ARG B CB  
2679 C  CG  . ARG B 41  ? 0.2041 0.2336 0.2070 0.0036  0.0015  -0.0115 265  ARG B CG  
2680 C  CD  . ARG B 41  ? 0.2139 0.2485 0.2244 0.0044  0.0025  -0.0124 265  ARG B CD  
2681 N  NE  . ARG B 41  ? 0.2210 0.2587 0.2332 0.0045  0.0065  -0.0127 265  ARG B NE  
2682 C  CZ  . ARG B 41  ? 0.2424 0.2810 0.2547 0.0067  0.0082  -0.0145 265  ARG B CZ  
2683 N  NH1 . ARG B 41  ? 0.2034 0.2396 0.2145 0.0091  0.0061  -0.0162 265  ARG B NH1 
2684 N  NH2 . ARG B 41  ? 0.2188 0.2603 0.2324 0.0067  0.0124  -0.0146 265  ARG B NH2 
2685 N  N   . ALA B 42  ? 0.2476 0.2806 0.2533 -0.0036 0.0060  -0.0048 266  ALA B N   
2686 C  CA  . ALA B 42  ? 0.2672 0.2989 0.2701 -0.0052 0.0078  -0.0023 266  ALA B CA  
2687 C  C   . ALA B 42  ? 0.2206 0.2555 0.2285 -0.0062 0.0118  -0.0015 266  ALA B C   
2688 O  O   . ALA B 42  ? 0.1982 0.2365 0.2143 -0.0066 0.0117  -0.0025 266  ALA B O   
2689 C  CB  . ALA B 42  ? 0.2224 0.2523 0.2260 -0.0065 0.0053  -0.0009 266  ALA B CB  
2690 N  N   . THR B 43  ? 0.2174 0.2511 0.2204 -0.0064 0.0152  0.0004  267  THR B N   
2691 C  CA  . THR B 43  ? 0.2722 0.3083 0.2798 -0.0078 0.0197  0.0018  267  THR B CA  
2692 C  C   . THR B 43  ? 0.2839 0.3191 0.2955 -0.0101 0.0193  0.0039  267  THR B C   
2693 O  O   . THR B 43  ? 0.2801 0.3120 0.2884 -0.0104 0.0161  0.0048  267  THR B O   
2694 C  CB  . THR B 43  ? 0.2509 0.2851 0.2507 -0.0071 0.0239  0.0035  267  THR B CB  
2695 O  OG1 . THR B 43  ? 0.2818 0.3113 0.2738 -0.0075 0.0227  0.0061  267  THR B OG1 
2696 C  CG2 . THR B 43  ? 0.2720 0.3061 0.2665 -0.0046 0.0240  0.0011  267  THR B CG2 
2697 N  N   . ILE B 44  ? 0.2621 0.3001 0.2815 -0.0118 0.0227  0.0046  268  ILE B N   
2698 C  CA  . ILE B 44  ? 0.2697 0.3063 0.2937 -0.0142 0.0222  0.0063  268  ILE B CA  
2699 C  C   . ILE B 44  ? 0.2592 0.2908 0.2758 -0.0150 0.0243  0.0102  268  ILE B C   
2700 O  O   . ILE B 44  ? 0.2310 0.2600 0.2496 -0.0165 0.0233  0.0118  268  ILE B O   
2701 C  CB  . ILE B 44  ? 0.2576 0.2986 0.2936 -0.0164 0.0249  0.0057  268  ILE B CB  
2702 C  CG1 . ILE B 44  ? 0.2521 0.2943 0.2883 -0.0171 0.0316  0.0079  268  ILE B CG1 
2703 C  CG2 . ILE B 44  ? 0.2168 0.2631 0.2607 -0.0152 0.0222  0.0018  268  ILE B CG2 
2704 C  CD1 . ILE B 44  ? 0.2346 0.2816 0.2842 -0.0197 0.0349  0.0075  268  ILE B CD1 
2705 N  N   . ASP B 45  ? 0.2341 0.2638 0.2417 -0.0136 0.0269  0.0116  269  ASP B N   
2706 C  CA  . ASP B 45  ? 0.3061 0.3304 0.3049 -0.0135 0.0277  0.0152  269  ASP B CA  
2707 C  C   . ASP B 45  ? 0.3320 0.3533 0.3220 -0.0115 0.0229  0.0146  269  ASP B C   
2708 O  O   . ASP B 45  ? 0.3703 0.3876 0.3512 -0.0106 0.0231  0.0170  269  ASP B O   
2709 C  CB  . ASP B 45  ? 0.3110 0.3341 0.3043 -0.0133 0.0338  0.0178  269  ASP B CB  
2710 C  CG  . ASP B 45  ? 0.3777 0.4027 0.3661 -0.0110 0.0352  0.0156  269  ASP B CG  
2711 O  OD1 . ASP B 45  ? 0.3791 0.4066 0.3695 -0.0098 0.0317  0.0121  269  ASP B OD1 
2712 O  OD2 . ASP B 45  ? 0.4475 0.4710 0.4294 -0.0103 0.0400  0.0176  269  ASP B OD2 
2713 N  N   . GLY B 46  ? 0.3008 0.3240 0.2936 -0.0108 0.0186  0.0115  270  GLY B N   
2714 C  CA  . GLY B 46  ? 0.2446 0.2654 0.2326 -0.0098 0.0139  0.0111  270  GLY B CA  
2715 C  C   . GLY B 46  ? 0.3164 0.3368 0.2978 -0.0079 0.0120  0.0092  270  GLY B C   
2716 O  O   . GLY B 46  ? 0.2468 0.2651 0.2243 -0.0072 0.0084  0.0092  270  GLY B O   
2717 N  N   . GLU B 47  ? 0.2912 0.3134 0.2720 -0.0070 0.0141  0.0074  271  GLU B N   
2718 C  CA  . GLU B 47  ? 0.2920 0.3132 0.2666 -0.0052 0.0122  0.0053  271  GLU B CA  
2719 C  C   . GLU B 47  ? 0.2454 0.2685 0.2252 -0.0049 0.0094  0.0023  271  GLU B C   
2720 O  O   . GLU B 47  ? 0.2312 0.2573 0.2175 -0.0050 0.0108  0.0011  271  GLU B O   
2721 C  CB  . GLU B 47  ? 0.3439 0.3652 0.3136 -0.0039 0.0162  0.0049  271  GLU B CB  
2722 C  CG  . GLU B 47  ? 0.3737 0.3933 0.3367 -0.0020 0.0141  0.0022  271  GLU B CG  
2723 C  CD  . GLU B 47  ? 0.5325 0.5521 0.4904 -0.0004 0.0184  0.0014  271  GLU B CD  
2724 O  OE1 . GLU B 47  ? 0.5292 0.5510 0.4904 -0.0009 0.0233  0.0028  271  GLU B OE1 
2725 O  OE2 . GLU B 47  ? 0.6017 0.6190 0.5526 0.0013  0.0169  -0.0009 271  GLU B OE2 
2726 N  N   . LEU B 48  ? 0.2372 0.2584 0.2144 -0.0045 0.0056  0.0013  272  LEU B N   
2727 C  CA  . LEU B 48  ? 0.2460 0.2679 0.2267 -0.0041 0.0033  -0.0011 272  LEU B CA  
2728 C  C   . LEU B 48  ? 0.2560 0.2774 0.2336 -0.0026 0.0039  -0.0035 272  LEU B C   
2729 O  O   . LEU B 48  ? 0.2334 0.2528 0.2042 -0.0019 0.0040  -0.0040 272  LEU B O   
2730 C  CB  . LEU B 48  ? 0.2813 0.3015 0.2615 -0.0045 -0.0004 -0.0010 272  LEU B CB  
2731 C  CG  . LEU B 48  ? 0.3487 0.3687 0.3311 -0.0056 -0.0015 0.0011  272  LEU B CG  
2732 C  CD1 . LEU B 48  ? 0.3068 0.3257 0.2890 -0.0057 -0.0048 0.0007  272  LEU B CD1 
2733 C  CD2 . LEU B 48  ? 0.2495 0.2713 0.2383 -0.0062 -0.0006 0.0013  272  LEU B CD2 
2734 N  N   . LEU B 49  ? 0.2153 0.2381 0.1973 -0.0019 0.0040  -0.0053 273  LEU B N   
2735 C  CA  . LEU B 49  ? 0.2436 0.2658 0.2235 -0.0001 0.0047  -0.0078 273  LEU B CA  
2736 C  C   . LEU B 49  ? 0.2456 0.2660 0.2269 0.0004  0.0019  -0.0095 273  LEU B C   
2737 O  O   . LEU B 49  ? 0.1957 0.2159 0.1801 -0.0004 -0.0001 -0.0087 273  LEU B O   
2738 C  CB  . LEU B 49  ? 0.2439 0.2696 0.2281 0.0008  0.0083  -0.0084 273  LEU B CB  
2739 C  CG  . LEU B 49  ? 0.2833 0.3112 0.2680 -0.0001 0.0119  -0.0062 273  LEU B CG  
2740 C  CD1 . LEU B 49  ? 0.2726 0.3051 0.2648 0.0003  0.0152  -0.0069 273  LEU B CD1 
2741 C  CD2 . LEU B 49  ? 0.3191 0.3443 0.2946 0.0006  0.0138  -0.0058 273  LEU B CD2 
2742 N  N   . GLY B 50  ? 0.2569 0.2753 0.2353 0.0020  0.0020  -0.0118 274  GLY B N   
2743 C  CA  . GLY B 50  ? 0.2186 0.2344 0.1980 0.0026  -0.0002 -0.0132 274  GLY B CA  
2744 C  C   . GLY B 50  ? 0.2515 0.2647 0.2298 0.0010  -0.0030 -0.0126 274  GLY B C   
2745 O  O   . GLY B 50  ? 0.2310 0.2427 0.2053 0.0001  -0.0041 -0.0128 274  GLY B O   
2746 N  N   . THR B 51  ? 0.2055 0.2182 0.1874 0.0007  -0.0043 -0.0119 275  THR B N   
2747 C  CA  . THR B 51  ? 0.2171 0.2278 0.1991 -0.0009 -0.0063 -0.0110 275  THR B CA  
2748 C  C   . THR B 51  ? 0.2190 0.2320 0.2038 -0.0019 -0.0066 -0.0088 275  THR B C   
2749 O  O   . THR B 51  ? 0.2447 0.2566 0.2309 -0.0027 -0.0076 -0.0080 275  THR B O   
2750 C  CB  . THR B 51  ? 0.2386 0.2458 0.2214 -0.0003 -0.0071 -0.0117 275  THR B CB  
2751 O  OG1 . THR B 51  ? 0.2639 0.2719 0.2491 0.0013  -0.0065 -0.0113 275  THR B OG1 
2752 C  CG2 . THR B 51  ? 0.2562 0.2600 0.2361 0.0006  -0.0071 -0.0142 275  THR B CG2 
2753 N  N   . THR B 52  ? 0.2143 0.2302 0.2000 -0.0020 -0.0053 -0.0079 276  THR B N   
2754 C  CA  . THR B 52  ? 0.2334 0.2512 0.2223 -0.0027 -0.0054 -0.0062 276  THR B CA  
2755 C  C   . THR B 52  ? 0.2336 0.2510 0.2214 -0.0041 -0.0066 -0.0048 276  THR B C   
2756 O  O   . THR B 52  ? 0.2056 0.2230 0.1904 -0.0045 -0.0065 -0.0045 276  THR B O   
2757 C  CB  . THR B 52  ? 0.2073 0.2281 0.1984 -0.0026 -0.0035 -0.0058 276  THR B CB  
2758 O  OG1 . THR B 52  ? 0.1922 0.2142 0.1857 -0.0011 -0.0029 -0.0073 276  THR B OG1 
2759 C  CG2 . THR B 52  ? 0.1976 0.2197 0.1919 -0.0036 -0.0039 -0.0043 276  THR B CG2 
2760 N  N   . LEU B 53  ? 0.1970 0.2141 0.1870 -0.0046 -0.0075 -0.0040 277  LEU B N   
2761 C  CA  . LEU B 53  ? 0.2243 0.2416 0.2146 -0.0055 -0.0085 -0.0026 277  LEU B CA  
2762 C  C   . LEU B 53  ? 0.2170 0.2355 0.2100 -0.0056 -0.0081 -0.0014 277  LEU B C   
2763 O  O   . LEU B 53  ? 0.2449 0.2640 0.2397 -0.0051 -0.0075 -0.0019 277  LEU B O   
2764 C  CB  . LEU B 53  ? 0.2257 0.2416 0.2169 -0.0060 -0.0097 -0.0029 277  LEU B CB  
2765 C  CG  . LEU B 53  ? 0.2561 0.2703 0.2483 -0.0055 -0.0092 -0.0034 277  LEU B CG  
2766 C  CD1 . LEU B 53  ? 0.2077 0.2223 0.2014 -0.0048 -0.0087 -0.0026 277  LEU B CD1 
2767 C  CD2 . LEU B 53  ? 0.2343 0.2471 0.2277 -0.0064 -0.0097 -0.0034 277  LEU B CD2 
2768 N  N   . VAL B 54  ? 0.2208 0.2395 0.2143 -0.0062 -0.0087 0.0000  278  VAL B N   
2769 C  CA  . VAL B 54  ? 0.2347 0.2538 0.2306 -0.0062 -0.0083 0.0009  278  VAL B CA  
2770 C  C   . VAL B 54  ? 0.2323 0.2508 0.2301 -0.0058 -0.0089 0.0007  278  VAL B C   
2771 O  O   . VAL B 54  ? 0.2952 0.3136 0.2947 -0.0055 -0.0087 0.0005  278  VAL B O   
2772 C  CB  . VAL B 54  ? 0.2884 0.3074 0.2838 -0.0067 -0.0084 0.0026  278  VAL B CB  
2773 C  CG1 . VAL B 54  ? 0.3371 0.3563 0.3298 -0.0069 -0.0071 0.0032  278  VAL B CG1 
2774 C  CG2 . VAL B 54  ? 0.3077 0.3264 0.3026 -0.0066 -0.0100 0.0032  278  VAL B CG2 
2775 N  N   . SER B 55  ? 0.2208 0.2387 0.2184 -0.0058 -0.0093 0.0005  279  SER B N   
2776 C  CA  . SER B 55  ? 0.2284 0.2455 0.2272 -0.0053 -0.0091 0.0006  279  SER B CA  
2777 C  C   . SER B 55  ? 0.2746 0.2905 0.2724 -0.0042 -0.0087 -0.0004 279  SER B C   
2778 O  O   . SER B 55  ? 0.2551 0.2703 0.2515 -0.0040 -0.0086 -0.0011 279  SER B O   
2779 C  CB  . SER B 55  ? 0.2282 0.2450 0.2278 -0.0057 -0.0091 0.0006  279  SER B CB  
2780 O  OG  . SER B 55  ? 0.2541 0.2694 0.2537 -0.0050 -0.0080 0.0006  279  SER B OG  
2781 N  N   . PRO B 56  ? 0.2622 0.2774 0.2603 -0.0034 -0.0087 -0.0005 280  PRO B N   
2782 C  CA  . PRO B 56  ? 0.2313 0.2455 0.2280 -0.0020 -0.0091 -0.0016 280  PRO B CA  
2783 C  C   . PRO B 56  ? 0.2796 0.2912 0.2735 -0.0008 -0.0084 -0.0015 280  PRO B C   
2784 O  O   . PRO B 56  ? 0.2734 0.2836 0.2651 0.0007  -0.0090 -0.0022 280  PRO B O   
2785 C  CB  . PRO B 56  ? 0.2286 0.2429 0.2266 -0.0016 -0.0098 -0.0021 280  PRO B CB  
2786 C  CG  . PRO B 56  ? 0.2476 0.2616 0.2463 -0.0021 -0.0092 -0.0010 280  PRO B CG  
2787 C  CD  . PRO B 56  ? 0.2265 0.2418 0.2261 -0.0034 -0.0088 0.0000  280  PRO B CD  
2788 N  N   . VAL B 57  ? 0.2168 0.2277 0.2109 -0.0014 -0.0072 -0.0005 281  VAL B N   
2789 C  CA  . VAL B 57  ? 0.1919 0.2001 0.1835 -0.0005 -0.0057 0.0001  281  VAL B CA  
2790 C  C   . VAL B 57  ? 0.2348 0.2420 0.2267 -0.0016 -0.0050 0.0005  281  VAL B C   
2791 O  O   . VAL B 57  ? 0.3134 0.3181 0.3042 -0.0015 -0.0033 0.0014  281  VAL B O   
2792 C  CB  . VAL B 57  ? 0.2396 0.2476 0.2320 -0.0004 -0.0041 0.0010  281  VAL B CB  
2793 C  CG1 . VAL B 57  ? 0.2837 0.2910 0.2743 0.0012  -0.0047 0.0002  281  VAL B CG1 
2794 C  CG2 . VAL B 57  ? 0.2048 0.2158 0.2018 -0.0021 -0.0042 0.0014  281  VAL B CG2 
2795 N  N   . SER B 58  ? 0.2505 0.2592 0.2437 -0.0026 -0.0061 -0.0002 282  SER B N   
2796 C  CA  . SER B 58  ? 0.2384 0.2462 0.2323 -0.0039 -0.0058 -0.0003 282  SER B CA  
2797 C  C   . SER B 58  ? 0.2613 0.2669 0.2529 -0.0031 -0.0061 -0.0011 282  SER B C   
2798 O  O   . SER B 58  ? 0.2579 0.2611 0.2494 -0.0038 -0.0056 -0.0011 282  SER B O   
2799 C  CB  . SER B 58  ? 0.2432 0.2539 0.2397 -0.0055 -0.0070 -0.0007 282  SER B CB  
2800 O  OG  . SER B 58  ? 0.2962 0.3088 0.2957 -0.0062 -0.0068 0.0001  282  SER B OG  
2801 N  N   . VAL B 59  ? 0.1985 0.2048 0.1888 -0.0016 -0.0070 -0.0019 283  VAL B N   
2802 C  CA  . VAL B 59  ? 0.2345 0.2392 0.2233 -0.0005 -0.0074 -0.0028 283  VAL B CA  
2803 C  C   . VAL B 59  ? 0.2392 0.2391 0.2252 0.0007  -0.0066 -0.0020 283  VAL B C   
2804 O  O   . VAL B 59  ? 0.2496 0.2478 0.2335 0.0017  -0.0060 -0.0009 283  VAL B O   
2805 C  CB  . VAL B 59  ? 0.2422 0.2493 0.2315 0.0009  -0.0085 -0.0038 283  VAL B CB  
2806 C  CG1 . VAL B 59  ? 0.2522 0.2586 0.2402 0.0027  -0.0092 -0.0036 283  VAL B CG1 
2807 C  CG2 . VAL B 59  ? 0.2521 0.2585 0.2409 0.0021  -0.0087 -0.0051 283  VAL B CG2 
2808 N  N   . CYS B 60  ? 0.2217 0.2188 0.2069 0.0006  -0.0063 -0.0025 284  CYS B N   
2809 C  CA  . CYS B 60  ? 0.2290 0.2206 0.2116 0.0015  -0.0052 -0.0016 284  CYS B CA  
2810 C  C   . CYS B 60  ? 0.2319 0.2212 0.2152 -0.0003 -0.0032 0.0001  284  CYS B C   
2811 O  O   . CYS B 60  ? 0.2632 0.2474 0.2440 0.0004  -0.0016 0.0015  284  CYS B O   
2812 C  CB  . CYS B 60  ? 0.2251 0.2146 0.2039 0.0047  -0.0058 -0.0010 284  CYS B CB  
2813 S  SG  . CYS B 60  ? 0.2796 0.2711 0.2588 0.0072  -0.0080 -0.0030 284  CYS B SG  
2814 N  N   . ASN B 61  ? 0.1982 0.1912 0.1853 -0.0025 -0.0030 0.0001  285  ASN B N   
2815 C  CA  . ASN B 61  ? 0.2123 0.2042 0.2021 -0.0046 -0.0010 0.0012  285  ASN B CA  
2816 C  C   . ASN B 61  ? 0.2392 0.2303 0.2322 -0.0069 -0.0016 -0.0001 285  ASN B C   
2817 O  O   . ASN B 61  ? 0.2436 0.2363 0.2365 -0.0070 -0.0037 -0.0020 285  ASN B O   
2818 C  CB  . ASN B 61  ? 0.2257 0.2221 0.2189 -0.0057 -0.0008 0.0016  285  ASN B CB  
2819 C  CG  . ASN B 61  ? 0.2454 0.2415 0.2357 -0.0037 0.0003  0.0029  285  ASN B CG  
2820 O  OD1 . ASN B 61  ? 0.2343 0.2292 0.2250 -0.0039 0.0029  0.0044  285  ASN B OD1 
2821 N  ND2 . ASN B 61  ? 0.2014 0.1985 0.1888 -0.0018 -0.0014 0.0021  285  ASN B ND2 
2822 N  N   . PHE B 62  ? 0.2389 0.2273 0.2345 -0.0087 0.0004  0.0009  286  PHE B N   
2823 C  CA  . PHE B 62  ? 0.2289 0.2168 0.2288 -0.0114 -0.0004 -0.0006 286  PHE B CA  
2824 C  C   . PHE B 62  ? 0.2626 0.2530 0.2691 -0.0140 0.0009  0.0001  286  PHE B C   
2825 O  O   . PHE B 62  ? 0.2948 0.2847 0.3017 -0.0138 0.0039  0.0023  286  PHE B O   
2826 C  CB  . PHE B 62  ? 0.2167 0.1978 0.2148 -0.0114 0.0006  -0.0006 286  PHE B CB  
2827 C  CG  . PHE B 62  ? 0.2515 0.2302 0.2444 -0.0088 -0.0010 -0.0019 286  PHE B CG  
2828 C  CD1 . PHE B 62  ? 0.2404 0.2202 0.2337 -0.0091 -0.0034 -0.0047 286  PHE B CD1 
2829 C  CD2 . PHE B 62  ? 0.2410 0.2163 0.2288 -0.0058 0.0000  -0.0003 286  PHE B CD2 
2830 C  CE1 . PHE B 62  ? 0.3004 0.2783 0.2896 -0.0066 -0.0044 -0.0059 286  PHE B CE1 
2831 C  CE2 . PHE B 62  ? 0.2681 0.2418 0.2524 -0.0032 -0.0015 -0.0016 286  PHE B CE2 
2832 C  CZ  . PHE B 62  ? 0.2822 0.2573 0.2675 -0.0037 -0.0034 -0.0044 286  PHE B CZ  
2833 N  N   . LYS B 63  ? 0.2162 0.2091 0.2278 -0.0163 -0.0013 -0.0020 287  LYS B N   
2834 C  CA  A LYS B 63  ? 0.2912 0.2871 0.3108 -0.0190 -0.0006 -0.0019 287  LYS B CA  
2835 C  CA  B LYS B 63  ? 0.2866 0.2828 0.3063 -0.0190 -0.0008 -0.0021 287  LYS B CA  
2836 C  C   . LYS B 63  ? 0.2216 0.2159 0.2456 -0.0217 -0.0025 -0.0044 287  LYS B C   
2837 O  O   . LYS B 63  ? 0.2484 0.2421 0.2695 -0.0213 -0.0057 -0.0069 287  LYS B O   
2838 C  CB  A LYS B 63  ? 0.2609 0.2635 0.2836 -0.0189 -0.0025 -0.0023 287  LYS B CB  
2839 C  CB  B LYS B 63  ? 0.2623 0.2652 0.2847 -0.0189 -0.0033 -0.0028 287  LYS B CB  
2840 C  CG  A LYS B 63  ? 0.3130 0.3179 0.3390 -0.0187 0.0007  0.0000  287  LYS B CG  
2841 C  CG  B LYS B 63  ? 0.3136 0.3191 0.3350 -0.0171 -0.0014 -0.0007 287  LYS B CG  
2842 C  CD  A LYS B 63  ? 0.3156 0.3270 0.3456 -0.0185 -0.0014 -0.0006 287  LYS B CD  
2843 C  CD  B LYS B 63  ? 0.2871 0.2987 0.3126 -0.0172 -0.0039 -0.0015 287  LYS B CD  
2844 C  CE  A LYS B 63  ? 0.3343 0.3473 0.3639 -0.0168 0.0016  0.0016  287  LYS B CE  
2845 C  CE  B LYS B 63  ? 0.3233 0.3372 0.3490 -0.0157 -0.0018 0.0004  287  LYS B CE  
2846 N  NZ  A LYS B 63  ? 0.2591 0.2703 0.2919 -0.0176 0.0065  0.0034  287  LYS B NZ  
2847 N  NZ  B LYS B 63  ? 0.3196 0.3391 0.3517 -0.0161 -0.0034 0.0000  287  LYS B NZ  
2848 N  N   . GLY B 64  ? 0.2573 0.2512 0.2887 -0.0245 -0.0005 -0.0039 288  GLY B N   
2849 C  CA  . GLY B 64  ? 0.2543 0.2468 0.2909 -0.0273 -0.0027 -0.0067 288  GLY B CA  
2850 C  C   . GLY B 64  ? 0.2948 0.2866 0.3406 -0.0307 0.0005  -0.0056 288  GLY B C   
2851 O  O   . GLY B 64  ? 0.2962 0.2889 0.3440 -0.0306 0.0048  -0.0026 288  GLY B O   
2852 N  N   . ASN B 65  ? 0.2584 0.2485 0.3098 -0.0336 -0.0015 -0.0083 289  ASN B N   
2853 C  CA  . ASN B 65  ? 0.2737 0.2623 0.3349 -0.0374 0.0015  -0.0077 289  ASN B CA  
2854 C  C   . ASN B 65  ? 0.2894 0.2685 0.3462 -0.0375 0.0056  -0.0055 289  ASN B C   
2855 O  O   . ASN B 65  ? 0.3168 0.2904 0.3659 -0.0357 0.0039  -0.0067 289  ASN B O   
2856 C  CB  . ASN B 65  ? 0.2921 0.2831 0.3621 -0.0407 -0.0031 -0.0121 289  ASN B CB  
2857 C  CG  . ASN B 65  ? 0.2999 0.2901 0.3820 -0.0451 -0.0001 -0.0117 289  ASN B CG  
2858 O  OD1 . ASN B 65  ? 0.2617 0.2566 0.3512 -0.0463 0.0034  -0.0095 289  ASN B OD1 
2859 N  ND2 . ASN B 65  ? 0.2969 0.2811 0.3815 -0.0477 -0.0011 -0.0139 289  ASN B ND2 
2860 N  N   . LEU B 66  ? 0.3000 0.2768 0.3611 -0.0392 0.0113  -0.0022 290  LEU B N   
2861 C  CA  . LEU B 66  ? 0.3137 0.2806 0.3716 -0.0397 0.0152  -0.0001 290  LEU B CA  
2862 C  C   . LEU B 66  ? 0.3147 0.2792 0.3820 -0.0442 0.0135  -0.0031 290  LEU B C   
2863 O  O   . LEU B 66  ? 0.3349 0.3019 0.4139 -0.0482 0.0157  -0.0030 290  LEU B O   
2864 C  CB  . LEU B 66  ? 0.3677 0.3318 0.4248 -0.0395 0.0224  0.0050  290  LEU B CB  
2865 C  CG  . LEU B 66  ? 0.3239 0.2769 0.3716 -0.0377 0.0257  0.0080  290  LEU B CG  
2866 C  CD1 . LEU B 66  ? 0.3311 0.2818 0.3733 -0.0356 0.0319  0.0131  290  LEU B CD1 
2867 C  CD2 . LEU B 66  ? 0.3049 0.2506 0.3587 -0.0415 0.0272  0.0075  290  LEU B CD2 
2868 N  N   . GLN B 67  ? 0.3190 0.2785 0.3816 -0.0436 0.0097  -0.0062 291  GLN B N   
2869 C  CA  . GLN B 67  ? 0.2989 0.2561 0.3699 -0.0476 0.0069  -0.0101 291  GLN B CA  
2870 C  C   . GLN B 67  ? 0.3970 0.3458 0.4729 -0.0508 0.0123  -0.0076 291  GLN B C   
2871 O  O   . GLN B 67  ? 0.3044 0.2547 0.3930 -0.0556 0.0132  -0.0086 291  GLN B O   
2872 C  CB  . GLN B 67  ? 0.3662 0.3199 0.4297 -0.0455 0.0016  -0.0141 291  GLN B CB  
2873 C  CG  . GLN B 67  ? 0.4436 0.3913 0.5130 -0.0491 -0.0004 -0.0178 291  GLN B CG  
2874 C  CD  . GLN B 67  ? 0.5506 0.4973 0.6141 -0.0472 -0.0066 -0.0230 291  GLN B CD  
2875 O  OE1 . GLN B 67  ? 0.5437 0.4897 0.5962 -0.0428 -0.0076 -0.0228 291  GLN B OE1 
2876 N  NE2 . GLN B 67  ? 0.6295 0.5763 0.7006 -0.0506 -0.0109 -0.0280 291  GLN B NE2 
2877 N  N   . ALA B 68  ? 0.3525 0.2922 0.4188 -0.0482 0.0160  -0.0041 292  ALA B N   
2878 C  CA  . ALA B 68  ? 0.3620 0.2921 0.4312 -0.0509 0.0213  -0.0013 292  ALA B CA  
2879 C  C   . ALA B 68  ? 0.3103 0.2320 0.3663 -0.0464 0.0249  0.0033  292  ALA B C   
2880 O  O   . ALA B 68  ? 0.3151 0.2377 0.3606 -0.0416 0.0221  0.0029  292  ALA B O   
2881 C  CB  . ALA B 68  ? 0.4163 0.3404 0.4908 -0.0541 0.0181  -0.0056 292  ALA B CB  
2882 N  N   . GLU B 69  ? 0.3470 0.2605 0.4037 -0.0479 0.0312  0.0076  293  GLU B N   
2883 C  CA  . GLU B 69  ? 0.3952 0.2979 0.4396 -0.0439 0.0339  0.0113  293  GLU B CA  
2884 C  C   . GLU B 69  ? 0.3656 0.2609 0.4076 -0.0435 0.0297  0.0077  293  GLU B C   
2885 O  O   . GLU B 69  ? 0.4044 0.2981 0.4558 -0.0479 0.0281  0.0043  293  GLU B O   
2886 C  CB  . GLU B 69  ? 0.3818 0.2765 0.4271 -0.0458 0.0419  0.0171  293  GLU B CB  
2887 C  CG  . GLU B 69  ? 0.4239 0.3099 0.4546 -0.0405 0.0452  0.0223  293  GLU B CG  
2888 C  CD  . GLU B 69  ? 0.5123 0.3893 0.5433 -0.0424 0.0535  0.0283  293  GLU B CD  
2889 O  OE1 . GLU B 69  ? 0.6598 0.5297 0.6984 -0.0468 0.0557  0.0282  293  GLU B OE1 
2890 O  OE2 . GLU B 69  ? 0.5153 0.3919 0.5388 -0.0396 0.0581  0.0330  293  GLU B OE2 
2891 N  N   . VAL B 70  ? 0.4067 0.2979 0.4367 -0.0381 0.0277  0.0081  294  VAL B N   
2892 C  CA  . VAL B 70  ? 0.3522 0.2359 0.3796 -0.0371 0.0242  0.0046  294  VAL B CA  
2893 C  C   . VAL B 70  ? 0.4613 0.3324 0.4916 -0.0399 0.0285  0.0070  294  VAL B C   
2894 O  O   . VAL B 70  ? 0.4729 0.3370 0.4979 -0.0385 0.0339  0.0129  294  VAL B O   
2895 C  CB  . VAL B 70  ? 0.4061 0.2880 0.4207 -0.0304 0.0219  0.0050  294  VAL B CB  
2896 C  CG1 . VAL B 70  ? 0.4419 0.3145 0.4534 -0.0289 0.0195  0.0022  294  VAL B CG1 
2897 C  CG2 . VAL B 70  ? 0.3660 0.2600 0.3790 -0.0283 0.0175  0.0020  294  VAL B CG2 
2898 N  N   . PRO B 71  ? 0.4779 0.3451 0.5161 -0.0439 0.0263  0.0028  295  PRO B N   
2899 C  CA  . PRO B 71  ? 0.5243 0.3796 0.5673 -0.0476 0.0308  0.0052  295  PRO B CA  
2900 C  C   . PRO B 71  ? 0.4716 0.3139 0.5029 -0.0430 0.0335  0.0094  295  PRO B C   
2901 O  O   . PRO B 71  ? 0.4845 0.3240 0.5073 -0.0382 0.0296  0.0072  295  PRO B O   
2902 C  CB  . PRO B 71  ? 0.5174 0.3718 0.5694 -0.0517 0.0259  -0.0016 295  PRO B CB  
2903 C  CG  . PRO B 71  ? 0.4741 0.3427 0.5296 -0.0518 0.0203  -0.0065 295  PRO B CG  
2904 C  CD  . PRO B 71  ? 0.4426 0.3161 0.4860 -0.0455 0.0196  -0.0044 295  PRO B CD  
2905 N  N   . GLY B 72  ? 0.4899 0.3241 0.5204 -0.0442 0.0404  0.0157  296  GLY B N   
2906 C  CA  . GLY B 72  ? 0.4491 0.2702 0.4681 -0.0396 0.0434  0.0205  296  GLY B CA  
2907 C  C   . GLY B 72  ? 0.4996 0.3230 0.5051 -0.0328 0.0438  0.0244  296  GLY B C   
2908 O  O   . GLY B 72  ? 0.5537 0.3664 0.5492 -0.0288 0.0467  0.0293  296  GLY B O   
2909 N  N   . GLN B 73  ? 0.4674 0.3042 0.4723 -0.0311 0.0406  0.0223  297  GLN B N   
2910 C  CA  . GLN B 73  ? 0.4933 0.3329 0.4861 -0.0248 0.0401  0.0252  297  GLN B CA  
2911 C  C   . GLN B 73  ? 0.4730 0.3208 0.4675 -0.0262 0.0439  0.0282  297  GLN B C   
2912 O  O   . GLN B 73  ? 0.4379 0.2981 0.4358 -0.0265 0.0409  0.0252  297  GLN B O   
2913 C  CB  . GLN B 73  ? 0.4833 0.3305 0.4728 -0.0209 0.0331  0.0200  297  GLN B CB  
2914 C  CG  . GLN B 73  ? 0.5051 0.3453 0.4948 -0.0201 0.0296  0.0160  297  GLN B CG  
2915 C  CD  . GLN B 73  ? 0.5183 0.3637 0.5021 -0.0148 0.0240  0.0123  297  GLN B CD  
2916 O  OE1 . GLN B 73  ? 0.5548 0.4012 0.5298 -0.0094 0.0235  0.0147  297  GLN B OE1 
2917 N  NE2 . GLN B 73  ? 0.4875 0.3362 0.4761 -0.0162 0.0197  0.0062  297  GLN B NE2 
2918 N  N   . HIS B 74  ? 0.4894 0.3297 0.4811 -0.0268 0.0508  0.0343  298  HIS B N   
2919 C  CA  . HIS B 74  ? 0.4350 0.2819 0.4291 -0.0286 0.0555  0.0374  298  HIS B CA  
2920 C  C   . HIS B 74  ? 0.4123 0.2684 0.3985 -0.0236 0.0524  0.0369  298  HIS B C   
2921 O  O   . HIS B 74  ? 0.3979 0.2506 0.3723 -0.0177 0.0498  0.0378  298  HIS B O   
2922 C  CB  . HIS B 74  ? 0.4201 0.2559 0.4091 -0.0286 0.0637  0.0446  298  HIS B CB  
2923 C  CG  . HIS B 74  ? 0.4976 0.3220 0.4928 -0.0329 0.0671  0.0457  298  HIS B CG  
2924 N  ND1 . HIS B 74  ? 0.6063 0.4342 0.6177 -0.0403 0.0684  0.0431  298  HIS B ND1 
2925 C  CD2 . HIS B 74  ? 0.4310 0.2405 0.4188 -0.0309 0.0691  0.0491  298  HIS B CD2 
2926 C  CE1 . HIS B 74  ? 0.5115 0.3269 0.5255 -0.0429 0.0712  0.0447  298  HIS B CE1 
2927 N  NE2 . HIS B 74  ? 0.5278 0.3316 0.5274 -0.0373 0.0719  0.0485  298  HIS B NE2 
2928 N  N   . GLN B 75  ? 0.3530 0.2209 0.3465 -0.0262 0.0525  0.0352  299  GLN B N   
2929 C  CA  . GLN B 75  ? 0.3574 0.2348 0.3456 -0.0225 0.0503  0.0347  299  GLN B CA  
2930 C  C   . GLN B 75  ? 0.3279 0.2109 0.3131 -0.0192 0.0426  0.0299  299  GLN B C   
2931 O  O   . GLN B 75  ? 0.3301 0.2184 0.3085 -0.0152 0.0403  0.0298  299  GLN B O   
2932 C  CB  . GLN B 75  ? 0.3561 0.2274 0.3312 -0.0179 0.0547  0.0404  299  GLN B CB  
2933 C  CG  . GLN B 75  ? 0.4332 0.3026 0.4124 -0.0213 0.0629  0.0448  299  GLN B CG  
2934 C  CD  . GLN B 75  ? 0.4341 0.2952 0.3995 -0.0170 0.0684  0.0509  299  GLN B CD  
2935 O  OE1 . GLN B 75  ? 0.4072 0.2615 0.3733 -0.0193 0.0759  0.0556  299  GLN B OE1 
2936 N  NE2 . GLN B 75  ? 0.4245 0.2862 0.3775 -0.0108 0.0647  0.0510  299  GLN B NE2 
2937 N  N   . LEU B 76  ? 0.3197 0.2016 0.3101 -0.0211 0.0387  0.0258  300  LEU B N   
2938 C  CA  . LEU B 76  ? 0.3097 0.1988 0.3004 -0.0194 0.0319  0.0206  300  LEU B CA  
2939 C  C   . LEU B 76  ? 0.3013 0.1993 0.3043 -0.0246 0.0300  0.0165  300  LEU B C   
2940 O  O   . LEU B 76  ? 0.3407 0.2353 0.3521 -0.0291 0.0310  0.0153  300  LEU B O   
2941 C  CB  . LEU B 76  ? 0.3457 0.2271 0.3322 -0.0169 0.0289  0.0187  300  LEU B CB  
2942 C  CG  . LEU B 76  ? 0.3609 0.2493 0.3469 -0.0147 0.0226  0.0135  300  LEU B CG  
2943 C  CD1 . LEU B 76  ? 0.3392 0.2324 0.3169 -0.0094 0.0208  0.0145  300  LEU B CD1 
2944 C  CD2 . LEU B 76  ? 0.3218 0.2026 0.3067 -0.0137 0.0202  0.0109  300  LEU B CD2 
2945 N  N   . TYR B 77  ? 0.3101 0.2190 0.3143 -0.0239 0.0271  0.0143  301  TYR B N   
2946 C  CA  . TYR B 77  ? 0.2824 0.2004 0.2976 -0.0282 0.0257  0.0114  301  TYR B CA  
2947 C  C   . TYR B 77  ? 0.2932 0.2176 0.3089 -0.0274 0.0192  0.0062  301  TYR B C   
2948 O  O   . TYR B 77  ? 0.3366 0.2637 0.3450 -0.0232 0.0167  0.0057  301  TYR B O   
2949 C  CB  . TYR B 77  ? 0.2969 0.2222 0.3134 -0.0282 0.0285  0.0138  301  TYR B CB  
2950 C  CG  . TYR B 77  ? 0.3373 0.2567 0.3535 -0.0292 0.0356  0.0190  301  TYR B CG  
2951 C  CD1 . TYR B 77  ? 0.3490 0.2676 0.3763 -0.0344 0.0394  0.0196  301  TYR B CD1 
2952 C  CD2 . TYR B 77  ? 0.2956 0.2101 0.3004 -0.0248 0.0386  0.0232  301  TYR B CD2 
2953 C  CE1 . TYR B 77  ? 0.3643 0.2773 0.3912 -0.0354 0.0467  0.0247  301  TYR B CE1 
2954 C  CE2 . TYR B 77  ? 0.3209 0.2294 0.3241 -0.0254 0.0456  0.0282  301  TYR B CE2 
2955 C  CZ  . TYR B 77  ? 0.3247 0.2325 0.3389 -0.0308 0.0499  0.0291  301  TYR B CZ  
2956 O  OH  . TYR B 77  ? 0.4274 0.3290 0.4399 -0.0315 0.0576  0.0343  301  TYR B OH  
2957 N  N   . GLN B 78  ? 0.2990 0.2257 0.3236 -0.0313 0.0167  0.0023  302  GLN B N   
2958 C  CA  . GLN B 78  ? 0.2932 0.2253 0.3180 -0.0308 0.0108  -0.0027 302  GLN B CA  
2959 C  C   . GLN B 78  ? 0.3404 0.2837 0.3700 -0.0318 0.0090  -0.0038 302  GLN B C   
2960 O  O   . GLN B 78  ? 0.2871 0.2341 0.3263 -0.0356 0.0100  -0.0039 302  GLN B O   
2961 C  CB  . GLN B 78  ? 0.3277 0.2557 0.3585 -0.0341 0.0084  -0.0067 302  GLN B CB  
2962 C  CG  . GLN B 78  ? 0.3193 0.2518 0.3488 -0.0332 0.0024  -0.0121 302  GLN B CG  
2963 C  CD  . GLN B 78  ? 0.3220 0.2513 0.3409 -0.0282 0.0010  -0.0126 302  GLN B CD  
2964 O  OE1 . GLN B 78  ? 0.2812 0.2016 0.2967 -0.0270 0.0018  -0.0127 302  GLN B OE1 
2965 N  NE2 . GLN B 78  ? 0.3134 0.2499 0.3277 -0.0252 -0.0009 -0.0129 302  GLN B NE2 
2966 N  N   . LEU B 79  ? 0.2907 0.2394 0.3143 -0.0283 0.0063  -0.0046 303  LEU B N   
2967 C  CA  . LEU B 79  ? 0.2644 0.2229 0.2916 -0.0289 0.0038  -0.0060 303  LEU B CA  
2968 C  C   . LEU B 79  ? 0.3364 0.2975 0.3649 -0.0296 -0.0016 -0.0110 303  LEU B C   
2969 O  O   . LEU B 79  ? 0.2961 0.2529 0.3189 -0.0278 -0.0036 -0.0131 303  LEU B O   
2970 C  CB  . LEU B 79  ? 0.3002 0.2627 0.3203 -0.0250 0.0040  -0.0041 303  LEU B CB  
2971 C  CG  . LEU B 79  ? 0.3189 0.2802 0.3360 -0.0234 0.0084  0.0004  303  LEU B CG  
2972 C  CD1 . LEU B 79  ? 0.2822 0.2466 0.2916 -0.0193 0.0071  0.0009  303  LEU B CD1 
2973 C  CD2 . LEU B 79  ? 0.3020 0.2684 0.3270 -0.0261 0.0108  0.0017  303  LEU B CD2 
2974 N  N   . GLN B 80  ? 0.3041 0.2722 0.3397 -0.0320 -0.0041 -0.0128 304  GLN B N   
2975 C  CA  . GLN B 80  ? 0.3214 0.2940 0.3562 -0.0316 -0.0095 -0.0170 304  GLN B CA  
2976 C  C   . GLN B 80  ? 0.2868 0.2667 0.3184 -0.0291 -0.0102 -0.0155 304  GLN B C   
2977 O  O   . GLN B 80  ? 0.2466 0.2323 0.2842 -0.0304 -0.0099 -0.0144 304  GLN B O   
2978 C  CB  . GLN B 80  ? 0.3511 0.3264 0.3960 -0.0356 -0.0125 -0.0202 304  GLN B CB  
2979 C  CG  . GLN B 80  ? 0.4123 0.3803 0.4615 -0.0386 -0.0122 -0.0222 304  GLN B CG  
2980 C  CD  . GLN B 80  ? 0.5262 0.4974 0.5884 -0.0433 -0.0139 -0.0244 304  GLN B CD  
2981 O  OE1 . GLN B 80  ? 0.3958 0.3728 0.4658 -0.0449 -0.0119 -0.0222 304  GLN B OE1 
2982 N  NE2 . GLN B 80  ? 0.5600 0.5276 0.6251 -0.0454 -0.0176 -0.0289 304  GLN B NE2 
2983 N  N   . LEU B 81  ? 0.2682 0.2478 0.2911 -0.0257 -0.0110 -0.0156 305  LEU B N   
2984 C  CA  . LEU B 81  ? 0.2604 0.2457 0.2801 -0.0234 -0.0111 -0.0139 305  LEU B CA  
2985 C  C   . LEU B 81  ? 0.2560 0.2477 0.2786 -0.0242 -0.0149 -0.0158 305  LEU B C   
2986 O  O   . LEU B 81  ? 0.2800 0.2716 0.3035 -0.0252 -0.0185 -0.0193 305  LEU B O   
2987 C  CB  . LEU B 81  ? 0.2397 0.2234 0.2505 -0.0199 -0.0111 -0.0138 305  LEU B CB  
2988 C  CG  . LEU B 81  ? 0.2508 0.2292 0.2570 -0.0177 -0.0081 -0.0118 305  LEU B CG  
2989 C  CD1 . LEU B 81  ? 0.2547 0.2340 0.2541 -0.0143 -0.0089 -0.0123 305  LEU B CD1 
2990 C  CD2 . LEU B 81  ? 0.2436 0.2223 0.2511 -0.0176 -0.0047 -0.0080 305  LEU B CD2 
2991 N  N   . THR B 82  ? 0.2441 0.2411 0.2680 -0.0234 -0.0142 -0.0137 306  THR B N   
2992 C  CA  . THR B 82  ? 0.2663 0.2687 0.2888 -0.0223 -0.0175 -0.0146 306  THR B CA  
2993 C  C   . THR B 82  ? 0.2755 0.2783 0.2905 -0.0192 -0.0162 -0.0128 306  THR B C   
2994 O  O   . THR B 82  ? 0.2185 0.2185 0.2307 -0.0181 -0.0132 -0.0109 306  THR B O   
2995 C  CB  . THR B 82  ? 0.3167 0.3248 0.3471 -0.0236 -0.0179 -0.0136 306  THR B CB  
2996 O  OG1 . THR B 82  ? 0.2692 0.2781 0.3000 -0.0227 -0.0139 -0.0102 306  THR B OG1 
2997 C  CG2 . THR B 82  ? 0.2808 0.2891 0.3206 -0.0270 -0.0187 -0.0153 306  THR B CG2 
2998 N  N   . ASN B 83  ? 0.2720 0.2783 0.2840 -0.0180 -0.0187 -0.0132 307  ASN B N   
2999 C  CA  . ASN B 83  ? 0.2823 0.2900 0.2895 -0.0156 -0.0173 -0.0112 307  ASN B CA  
3000 C  C   . ASN B 83  ? 0.2707 0.2807 0.2817 -0.0156 -0.0150 -0.0085 307  ASN B C   
3001 O  O   . ASN B 83  ? 0.2743 0.2864 0.2918 -0.0172 -0.0149 -0.0082 307  ASN B O   
3002 C  CB  . ASN B 83  ? 0.3119 0.3222 0.3152 -0.0145 -0.0200 -0.0119 307  ASN B CB  
3003 C  CG  . ASN B 83  ? 0.3345 0.3422 0.3314 -0.0134 -0.0210 -0.0141 307  ASN B CG  
3004 O  OD1 . ASN B 83  ? 0.3659 0.3712 0.3593 -0.0122 -0.0188 -0.0138 307  ASN B OD1 
3005 N  ND2 . ASN B 83  ? 0.3021 0.3100 0.2973 -0.0136 -0.0244 -0.0164 307  ASN B ND2 
3006 N  N   . LEU B 84  ? 0.2686 0.2786 0.2759 -0.0138 -0.0131 -0.0068 308  LEU B N   
3007 C  CA  . LEU B 84  ? 0.3393 0.3506 0.3489 -0.0134 -0.0109 -0.0045 308  LEU B CA  
3008 C  C   . LEU B 84  ? 0.3242 0.3400 0.3380 -0.0137 -0.0122 -0.0040 308  LEU B C   
3009 O  O   . LEU B 84  ? 0.3269 0.3440 0.3446 -0.0138 -0.0103 -0.0027 308  LEU B O   
3010 C  CB  . LEU B 84  ? 0.2370 0.2472 0.2417 -0.0113 -0.0094 -0.0034 308  LEU B CB  
3011 C  CG  . LEU B 84  ? 0.2689 0.2747 0.2708 -0.0106 -0.0078 -0.0034 308  LEU B CG  
3012 C  CD1 . LEU B 84  ? 0.2151 0.2204 0.2126 -0.0084 -0.0073 -0.0029 308  LEU B CD1 
3013 C  CD2 . LEU B 84  ? 0.2438 0.2473 0.2482 -0.0114 -0.0052 -0.0019 308  LEU B CD2 
3014 N  N   . ASP B 85  ? 0.3074 0.3253 0.3202 -0.0135 -0.0153 -0.0050 309  ASP B N   
3015 C  CA  . ASP B 85  ? 0.3327 0.3546 0.3493 -0.0134 -0.0171 -0.0046 309  ASP B CA  
3016 C  C   . ASP B 85  ? 0.3567 0.3808 0.3802 -0.0152 -0.0192 -0.0061 309  ASP B C   
3017 O  O   . ASP B 85  ? 0.3169 0.3448 0.3445 -0.0149 -0.0213 -0.0060 309  ASP B O   
3018 C  CB  . ASP B 85  ? 0.3190 0.3416 0.3305 -0.0119 -0.0194 -0.0045 309  ASP B CB  
3019 C  CG  . ASP B 85  ? 0.3938 0.4150 0.4010 -0.0121 -0.0221 -0.0066 309  ASP B CG  
3020 O  OD1 . ASP B 85  ? 0.3424 0.3623 0.3515 -0.0135 -0.0228 -0.0085 309  ASP B OD1 
3021 O  OD2 . ASP B 85  ? 0.4169 0.4380 0.4187 -0.0108 -0.0233 -0.0063 309  ASP B OD2 
3022 N  N   . GLY B 86  ? 0.2985 0.3204 0.3238 -0.0169 -0.0189 -0.0076 310  GLY B N   
3023 C  CA  . GLY B 86  ? 0.3238 0.3478 0.3569 -0.0191 -0.0209 -0.0093 310  GLY B CA  
3024 C  C   . GLY B 86  ? 0.2946 0.3181 0.3259 -0.0196 -0.0254 -0.0124 310  GLY B C   
3025 O  O   . GLY B 86  ? 0.2736 0.2978 0.3113 -0.0218 -0.0272 -0.0145 310  GLY B O   
3026 N  N   . SER B 87  ? 0.2620 0.2842 0.2848 -0.0177 -0.0273 -0.0128 311  SER B N   
3027 C  CA  . SER B 87  ? 0.3207 0.3419 0.3401 -0.0177 -0.0315 -0.0158 311  SER B CA  
3028 C  C   . SER B 87  ? 0.2946 0.3110 0.3127 -0.0191 -0.0306 -0.0180 311  SER B C   
3029 O  O   . SER B 87  ? 0.2710 0.2844 0.2876 -0.0190 -0.0267 -0.0166 311  SER B O   
3030 C  CB  . SER B 87  ? 0.3048 0.3253 0.3146 -0.0151 -0.0328 -0.0153 311  SER B CB  
3031 O  OG  . SER B 87  ? 0.3717 0.3894 0.3760 -0.0141 -0.0289 -0.0137 311  SER B OG  
3032 N  N   . PRO B 88  ? 0.2870 0.3024 0.3058 -0.0202 -0.0345 -0.0215 312  PRO B N   
3033 C  CA  . PRO B 88  ? 0.2614 0.2716 0.2797 -0.0216 -0.0337 -0.0237 312  PRO B CA  
3034 C  C   . PRO B 88  ? 0.3649 0.3709 0.3731 -0.0193 -0.0318 -0.0237 312  PRO B C   
3035 O  O   . PRO B 88  ? 0.3498 0.3569 0.3509 -0.0169 -0.0323 -0.0230 312  PRO B O   
3036 C  CB  . PRO B 88  ? 0.3230 0.3335 0.3435 -0.0228 -0.0392 -0.0280 312  PRO B CB  
3037 C  CG  . PRO B 88  ? 0.3803 0.3947 0.3970 -0.0207 -0.0430 -0.0280 312  PRO B CG  
3038 C  CD  . PRO B 88  ? 0.3332 0.3516 0.3527 -0.0199 -0.0401 -0.0238 312  PRO B CD  
3039 N  N   . ILE B 89  ? 0.3463 0.3475 0.3543 -0.0199 -0.0293 -0.0241 313  ILE B N   
3040 C  CA  . ILE B 89  ? 0.3273 0.3248 0.3269 -0.0177 -0.0278 -0.0247 313  ILE B CA  
3041 C  C   . ILE B 89  ? 0.3384 0.3345 0.3322 -0.0168 -0.0317 -0.0285 313  ILE B C   
3042 O  O   . ILE B 89  ? 0.3712 0.3657 0.3680 -0.0185 -0.0350 -0.0318 313  ILE B O   
3043 C  CB  . ILE B 89  ? 0.3281 0.3201 0.3288 -0.0182 -0.0249 -0.0246 313  ILE B CB  
3044 C  CG1 . ILE B 89  ? 0.3305 0.3233 0.3345 -0.0183 -0.0209 -0.0206 313  ILE B CG1 
3045 C  CG2 . ILE B 89  ? 0.2906 0.2788 0.2834 -0.0157 -0.0241 -0.0261 313  ILE B CG2 
3046 C  CD1 . ILE B 89  ? 0.3720 0.3663 0.3706 -0.0155 -0.0187 -0.0182 313  ILE B CD1 
3047 N  N   . ASP B 90  ? 0.3392 0.3357 0.3247 -0.0141 -0.0313 -0.0282 314  ASP B N   
3048 C  CA  . ASP B 90  ? 0.3494 0.3438 0.3272 -0.0126 -0.0341 -0.0316 314  ASP B CA  
3049 C  C   . ASP B 90  ? 0.3680 0.3587 0.3392 -0.0103 -0.0310 -0.0323 314  ASP B C   
3050 O  O   . ASP B 90  ? 0.3288 0.3212 0.2953 -0.0082 -0.0284 -0.0301 314  ASP B O   
3051 C  CB  . ASP B 90  ? 0.3520 0.3500 0.3250 -0.0111 -0.0364 -0.0307 314  ASP B CB  
3052 C  CG  . ASP B 90  ? 0.3877 0.3834 0.3524 -0.0095 -0.0400 -0.0345 314  ASP B CG  
3053 O  OD1 . ASP B 90  ? 0.4084 0.3996 0.3699 -0.0092 -0.0400 -0.0378 314  ASP B OD1 
3054 O  OD2 . ASP B 90  ? 0.3463 0.3441 0.3068 -0.0083 -0.0429 -0.0341 314  ASP B OD2 
3055 N  N   . PRO B 91  ? 0.3623 0.3479 0.3333 -0.0107 -0.0312 -0.0354 315  PRO B N   
3056 C  CA  . PRO B 91  ? 0.3104 0.2925 0.2758 -0.0082 -0.0282 -0.0361 315  PRO B CA  
3057 C  C   . PRO B 91  ? 0.3543 0.3364 0.3099 -0.0054 -0.0285 -0.0380 315  PRO B C   
3058 O  O   . PRO B 91  ? 0.3561 0.3362 0.3073 -0.0030 -0.0256 -0.0385 315  PRO B O   
3059 C  CB  . PRO B 91  ? 0.3211 0.2972 0.2891 -0.0093 -0.0291 -0.0394 315  PRO B CB  
3060 C  CG  . PRO B 91  ? 0.3011 0.2781 0.2782 -0.0130 -0.0310 -0.0387 315  PRO B CG  
3061 C  CD  . PRO B 91  ? 0.3407 0.3234 0.3179 -0.0135 -0.0338 -0.0381 315  PRO B CD  
3062 N  N   . THR B 92  ? 0.3652 0.3492 0.3170 -0.0053 -0.0319 -0.0389 316  THR B N   
3063 C  CA  . THR B 92  ? 0.3542 0.3380 0.2955 -0.0024 -0.0315 -0.0396 316  THR B CA  
3064 C  C   . THR B 92  ? 0.3827 0.3709 0.3227 -0.0011 -0.0278 -0.0351 316  THR B C   
3065 O  O   . THR B 92  ? 0.4105 0.3985 0.3421 0.0013  -0.0260 -0.0350 316  THR B O   
3066 C  CB  . THR B 92  ? 0.3752 0.3588 0.3116 -0.0023 -0.0369 -0.0423 316  THR B CB  
3067 O  OG1 . THR B 92  ? 0.3328 0.3211 0.2743 -0.0038 -0.0390 -0.0394 316  THR B OG1 
3068 C  CG2 . THR B 92  ? 0.3177 0.2971 0.2561 -0.0038 -0.0413 -0.0475 316  THR B CG2 
3069 N  N   . ASP B 93  ? 0.3282 0.3197 0.2758 -0.0028 -0.0263 -0.0314 317  ASP B N   
3070 C  CA  . ASP B 93  ? 0.3760 0.3712 0.3231 -0.0019 -0.0230 -0.0274 317  ASP B CA  
3071 C  C   . ASP B 93  ? 0.3978 0.3923 0.3416 0.0003  -0.0185 -0.0273 317  ASP B C   
3072 O  O   . ASP B 93  ? 0.3389 0.3308 0.2838 0.0008  -0.0173 -0.0293 317  ASP B O   
3073 C  CB  . ASP B 93  ? 0.3632 0.3613 0.3193 -0.0038 -0.0222 -0.0243 317  ASP B CB  
3074 C  CG  . ASP B 93  ? 0.3883 0.3887 0.3482 -0.0055 -0.0257 -0.0234 317  ASP B CG  
3075 O  OD1 . ASP B 93  ? 0.3386 0.3392 0.2937 -0.0049 -0.0288 -0.0244 317  ASP B OD1 
3076 O  OD2 . ASP B 93  ? 0.3864 0.3885 0.3539 -0.0072 -0.0254 -0.0217 317  ASP B OD2 
3077 N  N   . ASP B 94  ? 0.3781 0.3751 0.3184 0.0015  -0.0157 -0.0248 318  ASP B N   
3078 C  CA  . ASP B 94  ? 0.4383 0.4357 0.3767 0.0035  -0.0111 -0.0246 318  ASP B CA  
3079 C  C   . ASP B 94  ? 0.3881 0.3884 0.3348 0.0028  -0.0085 -0.0222 318  ASP B C   
3080 O  O   . ASP B 94  ? 0.3548 0.3581 0.3024 0.0034  -0.0052 -0.0200 318  ASP B O   
3081 C  CB  . ASP B 94  ? 0.5072 0.5058 0.4385 0.0049  -0.0087 -0.0228 318  ASP B CB  
3082 C  CG  . ASP B 94  ? 0.6066 0.6017 0.5274 0.0066  -0.0106 -0.0256 318  ASP B CG  
3083 O  OD1 . ASP B 94  ? 0.5798 0.5715 0.4986 0.0071  -0.0126 -0.0296 318  ASP B OD1 
3084 O  OD2 . ASP B 94  ? 0.7388 0.7340 0.6529 0.0074  -0.0104 -0.0237 318  ASP B OD2 
3085 N  N   . THR B 95  ? 0.3444 0.3436 0.2970 0.0016  -0.0101 -0.0228 319  THR B N   
3086 C  CA  . THR B 95  ? 0.2984 0.2995 0.2578 0.0014  -0.0084 -0.0209 319  THR B CA  
3087 C  C   . THR B 95  ? 0.3055 0.3031 0.2666 0.0022  -0.0083 -0.0230 319  THR B C   
3088 O  O   . THR B 95  ? 0.3081 0.3017 0.2671 0.0019  -0.0103 -0.0256 319  THR B O   
3089 C  CB  . THR B 95  ? 0.3452 0.3478 0.3095 -0.0009 -0.0101 -0.0184 319  THR B CB  
3090 O  OG1 . THR B 95  ? 0.3053 0.3053 0.2706 -0.0024 -0.0132 -0.0199 319  THR B OG1 
3091 C  CG2 . THR B 95  ? 0.3281 0.3339 0.2913 -0.0014 -0.0101 -0.0160 319  THR B CG2 
3092 N  N   . PRO B 96  ? 0.2716 0.2704 0.2368 0.0034  -0.0063 -0.0221 320  PRO B N   
3093 C  CA  . PRO B 96  ? 0.2894 0.2843 0.2562 0.0044  -0.0066 -0.0236 320  PRO B CA  
3094 C  C   . PRO B 96  ? 0.2845 0.2758 0.2534 0.0023  -0.0090 -0.0234 320  PRO B C   
3095 O  O   . PRO B 96  ? 0.2867 0.2729 0.2548 0.0024  -0.0098 -0.0255 320  PRO B O   
3096 C  CB  . PRO B 96  ? 0.2662 0.2639 0.2373 0.0059  -0.0048 -0.0219 320  PRO B CB  
3097 C  CG  . PRO B 96  ? 0.2754 0.2785 0.2471 0.0058  -0.0030 -0.0204 320  PRO B CG  
3098 C  CD  . PRO B 96  ? 0.2791 0.2827 0.2477 0.0038  -0.0042 -0.0196 320  PRO B CD  
3099 N  N   . GLY B 97  ? 0.2658 0.2595 0.2376 0.0003  -0.0098 -0.0209 321  GLY B N   
3100 C  CA  . GLY B 97  ? 0.2526 0.2440 0.2276 -0.0019 -0.0113 -0.0202 321  GLY B CA  
3101 C  C   . GLY B 97  ? 0.2916 0.2869 0.2689 -0.0038 -0.0120 -0.0179 321  GLY B C   
3102 O  O   . GLY B 97  ? 0.2500 0.2489 0.2257 -0.0035 -0.0118 -0.0171 321  GLY B O   
3103 N  N   . PRO B 98  ? 0.2727 0.2669 0.2538 -0.0056 -0.0126 -0.0167 322  PRO B N   
3104 C  CA  . PRO B 98  ? 0.2331 0.2312 0.2170 -0.0072 -0.0133 -0.0148 322  PRO B CA  
3105 C  C   . PRO B 98  ? 0.2436 0.2448 0.2280 -0.0060 -0.0117 -0.0124 322  PRO B C   
3106 O  O   . PRO B 98  ? 0.2547 0.2549 0.2391 -0.0046 -0.0102 -0.0118 322  PRO B O   
3107 C  CB  . PRO B 98  ? 0.2797 0.2756 0.2681 -0.0092 -0.0134 -0.0142 322  PRO B CB  
3108 C  CG  . PRO B 98  ? 0.2744 0.2651 0.2621 -0.0085 -0.0124 -0.0149 322  PRO B CG  
3109 C  CD  . PRO B 98  ? 0.2591 0.2485 0.2424 -0.0066 -0.0127 -0.0173 322  PRO B CD  
3110 N  N   . LEU B 99  ? 0.2431 0.2479 0.2279 -0.0066 -0.0122 -0.0111 323  LEU B N   
3111 C  CA  . LEU B 99  ? 0.2425 0.2499 0.2282 -0.0058 -0.0109 -0.0091 323  LEU B CA  
3112 C  C   . LEU B 99  ? 0.2350 0.2415 0.2234 -0.0058 -0.0100 -0.0078 323  LEU B C   
3113 O  O   . LEU B 99  ? 0.2509 0.2560 0.2415 -0.0070 -0.0102 -0.0074 323  LEU B O   
3114 C  CB  . LEU B 99  ? 0.2631 0.2736 0.2492 -0.0065 -0.0117 -0.0079 323  LEU B CB  
3115 C  CG  . LEU B 99  ? 0.2640 0.2751 0.2458 -0.0062 -0.0125 -0.0087 323  LEU B CG  
3116 C  CD1 . LEU B 99  ? 0.3267 0.3402 0.3087 -0.0065 -0.0131 -0.0067 323  LEU B CD1 
3117 C  CD2 . LEU B 99  ? 0.2359 0.2469 0.2148 -0.0047 -0.0105 -0.0094 323  LEU B CD2 
3118 N  N   . GLY B 100 ? 0.2169 0.2240 0.2052 -0.0043 -0.0090 -0.0071 324  GLY B N   
3119 C  CA  . GLY B 100 ? 0.2055 0.2112 0.1947 -0.0036 -0.0083 -0.0060 324  GLY B CA  
3120 C  C   . GLY B 100 ? 0.2101 0.2115 0.1979 -0.0025 -0.0079 -0.0065 324  GLY B C   
3121 O  O   . GLY B 100 ? 0.2623 0.2618 0.2496 -0.0014 -0.0073 -0.0054 324  GLY B O   
3122 N  N   . CYS B 101 ? 0.2374 0.2366 0.2241 -0.0026 -0.0082 -0.0081 325  CYS B N   
3123 C  CA  . CYS B 101 ? 0.2519 0.2462 0.2372 -0.0014 -0.0077 -0.0086 325  CYS B CA  
3124 C  C   . CYS B 101 ? 0.2622 0.2565 0.2465 0.0015  -0.0075 -0.0084 325  CYS B C   
3125 O  O   . CYS B 101 ? 0.2272 0.2254 0.2121 0.0025  -0.0077 -0.0092 325  CYS B O   
3126 C  CB  . CYS B 101 ? 0.2529 0.2450 0.2371 -0.0017 -0.0083 -0.0110 325  CYS B CB  
3127 S  SG  . CYS B 101 ? 0.3108 0.2958 0.2934 -0.0002 -0.0078 -0.0119 325  CYS B SG  
3128 N  N   . PRO B 102 ? 0.2703 0.2604 0.2532 0.0029  -0.0072 -0.0074 326  PRO B N   
3129 C  CA  . PRO B 102 ? 0.2424 0.2323 0.2242 0.0062  -0.0077 -0.0075 326  PRO B CA  
3130 C  C   . PRO B 102 ? 0.2764 0.2678 0.2588 0.0077  -0.0080 -0.0098 326  PRO B C   
3131 O  O   . PRO B 102 ? 0.2693 0.2585 0.2510 0.0070  -0.0077 -0.0112 326  PRO B O   
3132 C  CB  . PRO B 102 ? 0.2740 0.2571 0.2528 0.0075  -0.0073 -0.0061 326  PRO B CB  
3133 C  CG  . PRO B 102 ? 0.2961 0.2771 0.2752 0.0046  -0.0059 -0.0045 326  PRO B CG  
3134 C  CD  . PRO B 102 ? 0.2163 0.2015 0.1985 0.0017  -0.0062 -0.0058 326  PRO B CD  
3135 N  N   . ASP B 103 ? 0.2173 0.2126 0.2014 0.0098  -0.0086 -0.0103 327  ASP B N   
3136 C  CA  . ASP B 103 ? 0.2425 0.2399 0.2281 0.0116  -0.0084 -0.0124 327  ASP B CA  
3137 C  C   . ASP B 103 ? 0.2606 0.2562 0.2463 0.0154  -0.0094 -0.0129 327  ASP B C   
3138 O  O   . ASP B 103 ? 0.2785 0.2780 0.2673 0.0174  -0.0095 -0.0145 327  ASP B O   
3139 C  CB  . ASP B 103 ? 0.2040 0.2084 0.1930 0.0107  -0.0078 -0.0130 327  ASP B CB  
3140 C  CG  . ASP B 103 ? 0.2460 0.2539 0.2379 0.0114  -0.0090 -0.0122 327  ASP B CG  
3141 O  OD1 . ASP B 103 ? 0.2458 0.2509 0.2361 0.0129  -0.0105 -0.0113 327  ASP B OD1 
3142 O  OD2 . ASP B 103 ? 0.2262 0.2393 0.2216 0.0104  -0.0084 -0.0125 327  ASP B OD2 
3143 N  N   . PHE B 104 ? 0.2614 0.2511 0.2438 0.0165  -0.0101 -0.0114 328  PHE B N   
3144 C  CA  . PHE B 104 ? 0.2606 0.2474 0.2420 0.0205  -0.0115 -0.0114 328  PHE B CA  
3145 C  C   . PHE B 104 ? 0.2739 0.2520 0.2509 0.0210  -0.0109 -0.0102 328  PHE B C   
3146 O  O   . PHE B 104 ? 0.2938 0.2687 0.2691 0.0179  -0.0096 -0.0090 328  PHE B O   
3147 C  CB  . PHE B 104 ? 0.2555 0.2443 0.2368 0.0221  -0.0134 -0.0103 328  PHE B CB  
3148 C  CG  . PHE B 104 ? 0.3009 0.2870 0.2787 0.0199  -0.0129 -0.0079 328  PHE B CG  
3149 C  CD1 . PHE B 104 ? 0.3033 0.2820 0.2758 0.0210  -0.0125 -0.0057 328  PHE B CD1 
3150 C  CD2 . PHE B 104 ? 0.2664 0.2571 0.2463 0.0170  -0.0124 -0.0077 328  PHE B CD2 
3151 C  CE1 . PHE B 104 ? 0.2897 0.2663 0.2594 0.0192  -0.0114 -0.0036 328  PHE B CE1 
3152 C  CE2 . PHE B 104 ? 0.2708 0.2594 0.2480 0.0153  -0.0116 -0.0057 328  PHE B CE2 
3153 C  CZ  . PHE B 104 ? 0.3132 0.2949 0.2854 0.0165  -0.0110 -0.0037 328  PHE B CZ  
3154 N  N   . THR B 105 ? 0.2658 0.2399 0.2413 0.0248  -0.0119 -0.0104 329  THR B N   
3155 C  CA  . THR B 105 ? 0.3038 0.2685 0.2748 0.0256  -0.0113 -0.0088 329  THR B CA  
3156 C  C   . THR B 105 ? 0.3235 0.2843 0.2900 0.0281  -0.0124 -0.0060 329  THR B C   
3157 O  O   . THR B 105 ? 0.3165 0.2807 0.2834 0.0313  -0.0147 -0.0064 329  THR B O   
3158 C  CB  . THR B 105 ? 0.3161 0.2772 0.2873 0.0286  -0.0115 -0.0108 329  THR B CB  
3159 O  OG1 . THR B 105 ? 0.3921 0.3562 0.3648 0.0332  -0.0136 -0.0115 329  THR B OG1 
3160 C  CG2 . THR B 105 ? 0.2744 0.2392 0.2488 0.0268  -0.0103 -0.0138 329  THR B CG2 
3161 N  N   . GLY B 106 ? 0.3004 0.2542 0.2627 0.0265  -0.0107 -0.0034 330  GLY B N   
3162 C  CA  . GLY B 106 ? 0.3124 0.2612 0.2688 0.0291  -0.0111 -0.0004 330  GLY B CA  
3163 C  C   . GLY B 106 ? 0.3203 0.2633 0.2736 0.0259  -0.0080 0.0026  330  GLY B C   
3164 O  O   . GLY B 106 ? 0.2987 0.2421 0.2554 0.0217  -0.0060 0.0020  330  GLY B O   
3165 N  N   . LEU B 107 ? 0.3061 0.2439 0.2530 0.0281  -0.0076 0.0057  331  LEU B N   
3166 C  CA  . LEU B 107 ? 0.2946 0.2271 0.2384 0.0254  -0.0039 0.0088  331  LEU B CA  
3167 C  C   . LEU B 107 ? 0.3062 0.2453 0.2512 0.0233  -0.0035 0.0089  331  LEU B C   
3168 O  O   . LEU B 107 ? 0.2959 0.2352 0.2360 0.0260  -0.0046 0.0100  331  LEU B O   
3169 C  CB  . LEU B 107 ? 0.3113 0.2338 0.2464 0.0289  -0.0030 0.0125  331  LEU B CB  
3170 C  CG  . LEU B 107 ? 0.4571 0.3717 0.3905 0.0314  -0.0033 0.0128  331  LEU B CG  
3171 C  CD1 . LEU B 107 ? 0.4259 0.3295 0.3499 0.0345  -0.0016 0.0173  331  LEU B CD1 
3172 C  CD2 . LEU B 107 ? 0.4086 0.3218 0.3481 0.0270  -0.0012 0.0114  331  LEU B CD2 
3173 N  N   . LEU B 108 ? 0.3016 0.2461 0.2529 0.0188  -0.0023 0.0075  332  LEU B N   
3174 C  CA  . LEU B 108 ? 0.2799 0.2304 0.2330 0.0168  -0.0019 0.0074  332  LEU B CA  
3175 C  C   . LEU B 108 ? 0.2968 0.2425 0.2461 0.0158  0.0018  0.0108  332  LEU B C   
3176 O  O   . LEU B 108 ? 0.2646 0.2061 0.2156 0.0131  0.0049  0.0122  332  LEU B O   
3177 C  CB  . LEU B 108 ? 0.2620 0.2191 0.2226 0.0127  -0.0018 0.0050  332  LEU B CB  
3178 C  CG  . LEU B 108 ? 0.3030 0.2665 0.2667 0.0104  -0.0015 0.0048  332  LEU B CG  
3179 C  CD1 . LEU B 108 ? 0.2779 0.2458 0.2400 0.0129  -0.0039 0.0040  332  LEU B CD1 
3180 C  CD2 . LEU B 108 ? 0.2683 0.2370 0.2384 0.0070  -0.0019 0.0025  332  LEU B CD2 
3181 N  N   . TYR B 109 ? 0.3054 0.2515 0.2496 0.0180  0.0016  0.0119  333  TYR B N   
3182 C  CA  . TYR B 109 ? 0.3079 0.2493 0.2473 0.0178  0.0055  0.0152  333  TYR B CA  
3183 C  C   . TYR B 109 ? 0.2831 0.2310 0.2269 0.0148  0.0069  0.0145  333  TYR B C   
3184 O  O   . TYR B 109 ? 0.2462 0.2009 0.1928 0.0150  0.0040  0.0121  333  TYR B O   
3185 C  CB  . TYR B 109 ? 0.3474 0.2840 0.2766 0.0229  0.0043  0.0169  333  TYR B CB  
3186 C  CG  . TYR B 109 ? 0.3763 0.3088 0.2990 0.0233  0.0083  0.0199  333  TYR B CG  
3187 C  CD1 . TYR B 109 ? 0.3773 0.3012 0.2955 0.0231  0.0130  0.0238  333  TYR B CD1 
3188 C  CD2 . TYR B 109 ? 0.3500 0.2867 0.2706 0.0243  0.0076  0.0190  333  TYR B CD2 
3189 C  CE1 . TYR B 109 ? 0.4308 0.3508 0.3427 0.0237  0.0174  0.0268  333  TYR B CE1 
3190 C  CE2 . TYR B 109 ? 0.4163 0.3490 0.3302 0.0251  0.0115  0.0217  333  TYR B CE2 
3191 C  CZ  . TYR B 109 ? 0.4417 0.3663 0.3512 0.0249  0.0166  0.0257  333  TYR B CZ  
3192 O  OH  . TYR B 109 ? 0.6172 0.5378 0.5197 0.0259  0.0213  0.0285  333  TYR B OH  
3193 N  N   . GLY B 110 ? 0.2630 0.2087 0.2082 0.0121  0.0114  0.0168  334  GLY B N   
3194 C  CA  . GLY B 110 ? 0.2540 0.2056 0.2038 0.0096  0.0130  0.0163  334  GLY B CA  
3195 C  C   . GLY B 110 ? 0.2789 0.2275 0.2300 0.0073  0.0186  0.0191  334  GLY B C   
3196 O  O   . GLY B 110 ? 0.3044 0.2451 0.2497 0.0085  0.0219  0.0222  334  GLY B O   
3197 N  N   . VAL B 111 ? 0.2484 0.2029 0.2073 0.0040  0.0201  0.0183  335  VAL B N   
3198 C  CA  . VAL B 111 ? 0.2576 0.2108 0.2201 0.0014  0.0255  0.0207  335  VAL B CA  
3199 C  C   . VAL B 111 ? 0.2945 0.2531 0.2688 -0.0033 0.0251  0.0188  335  VAL B C   
3200 O  O   . VAL B 111 ? 0.2617 0.2273 0.2409 -0.0041 0.0216  0.0161  335  VAL B O   
3201 C  CB  . VAL B 111 ? 0.2574 0.2125 0.2169 0.0029  0.0282  0.0217  335  VAL B CB  
3202 C  CG1 . VAL B 111 ? 0.2533 0.2106 0.2207 -0.0006 0.0335  0.0231  335  VAL B CG1 
3203 C  CG2 . VAL B 111 ? 0.2641 0.2117 0.2110 0.0072  0.0299  0.0242  335  VAL B CG2 
3204 N  N   . ALA B 112 ? 0.2642 0.2190 0.2427 -0.0061 0.0284  0.0203  336  ALA B N   
3205 C  CA  . ALA B 112 ? 0.2455 0.2049 0.2356 -0.0107 0.0282  0.0186  336  ALA B CA  
3206 C  C   . ALA B 112 ? 0.2767 0.2392 0.2727 -0.0127 0.0330  0.0202  336  ALA B C   
3207 O  O   . ALA B 112 ? 0.2592 0.2164 0.2524 -0.0125 0.0385  0.0236  336  ALA B O   
3208 C  CB  . ALA B 112 ? 0.2883 0.2417 0.2807 -0.0129 0.0286  0.0188  336  ALA B CB  
3209 N  N   . SER B 113 ? 0.2368 0.2077 0.2405 -0.0142 0.0311  0.0180  337  SER B N   
3210 C  CA  . SER B 113 ? 0.2475 0.2228 0.2586 -0.0160 0.0352  0.0190  337  SER B CA  
3211 C  C   . SER B 113 ? 0.2760 0.2570 0.3004 -0.0203 0.0336  0.0168  337  SER B C   
3212 O  O   . SER B 113 ? 0.2454 0.2287 0.2722 -0.0213 0.0283  0.0139  337  SER B O   
3213 C  CB  . SER B 113 ? 0.2318 0.2121 0.2403 -0.0133 0.0344  0.0184  337  SER B CB  
3214 O  OG  . SER B 113 ? 0.2389 0.2245 0.2491 -0.0130 0.0283  0.0153  337  SER B OG  
3215 N  N   . GLN B 114 ? 0.2571 0.2405 0.2901 -0.0227 0.0383  0.0181  338  GLN B N   
3216 C  CA  . GLN B 114 ? 0.2670 0.2567 0.3141 -0.0268 0.0371  0.0160  338  GLN B CA  
3217 C  C   . GLN B 114 ? 0.2667 0.2636 0.3214 -0.0269 0.0400  0.0164  338  GLN B C   
3218 O  O   . GLN B 114 ? 0.2731 0.2682 0.3236 -0.0250 0.0455  0.0191  338  GLN B O   
3219 C  CB  . GLN B 114 ? 0.2366 0.2218 0.2903 -0.0308 0.0404  0.0170  338  GLN B CB  
3220 C  CG  . GLN B 114 ? 0.2594 0.2371 0.3073 -0.0310 0.0375  0.0163  338  GLN B CG  
3221 C  CD  . GLN B 114 ? 0.2716 0.2452 0.3278 -0.0354 0.0402  0.0167  338  GLN B CD  
3222 O  OE1 . GLN B 114 ? 0.3279 0.2997 0.3886 -0.0372 0.0468  0.0197  338  GLN B OE1 
3223 N  NE2 . GLN B 114 ? 0.2757 0.2475 0.3342 -0.0372 0.0355  0.0137  338  GLN B NE2 
3224 N  N   . ARG B 115 ? 0.2453 0.2502 0.3111 -0.0289 0.0362  0.0136  339  ARG B N   
3225 C  CA  . ARG B 115 ? 0.3108 0.3232 0.3875 -0.0297 0.0389  0.0136  339  ARG B CA  
3226 C  C   . ARG B 115 ? 0.2591 0.2761 0.3509 -0.0343 0.0373  0.0115  339  ARG B C   
3227 O  O   . ARG B 115 ? 0.2820 0.3016 0.3765 -0.0353 0.0306  0.0083  339  ARG B O   
3228 C  CB  . ARG B 115 ? 0.2366 0.2552 0.3120 -0.0267 0.0351  0.0120  339  ARG B CB  
3229 C  CG  . ARG B 115 ? 0.2816 0.3085 0.3694 -0.0273 0.0373  0.0117  339  ARG B CG  
3230 C  CD  . ARG B 115 ? 0.2868 0.3181 0.3715 -0.0235 0.0348  0.0108  339  ARG B CD  
3231 N  NE  . ARG B 115 ? 0.2732 0.3003 0.3476 -0.0201 0.0395  0.0131  339  ARG B NE  
3232 C  CZ  . ARG B 115 ? 0.2730 0.2957 0.3345 -0.0169 0.0372  0.0131  339  ARG B CZ  
3233 N  NH1 . ARG B 115 ? 0.2634 0.2854 0.3207 -0.0168 0.0308  0.0113  339  ARG B NH1 
3234 N  NH2 . ARG B 115 ? 0.2674 0.2863 0.3200 -0.0138 0.0414  0.0148  339  ARG B NH2 
3235 N  N   . GLY B 116 ? 0.2883 0.3064 0.3900 -0.0371 0.0434  0.0132  340  GLY B N   
3236 C  CA  . GLY B 116 ? 0.2852 0.3077 0.4027 -0.0418 0.0423  0.0111  340  GLY B CA  
3237 C  C   . GLY B 116 ? 0.2969 0.3131 0.4180 -0.0454 0.0487  0.0136  340  GLY B C   
3238 O  O   . GLY B 116 ? 0.3095 0.3163 0.4187 -0.0441 0.0520  0.0164  340  GLY B O   
3239 N  N   . PRO B 117 ? 0.3286 0.3498 0.4667 -0.0499 0.0507  0.0127  341  PRO B N   
3240 C  CA  . PRO B 117 ? 0.3336 0.3664 0.4879 -0.0515 0.0472  0.0095  341  PRO B CA  
3241 C  C   . PRO B 117 ? 0.3574 0.3969 0.5131 -0.0481 0.0507  0.0109  341  PRO B C   
3242 O  O   . PRO B 117 ? 0.3210 0.3569 0.4704 -0.0463 0.0584  0.0147  341  PRO B O   
3243 C  CB  . PRO B 117 ? 0.3470 0.3810 0.5181 -0.0573 0.0510  0.0093  341  PRO B CB  
3244 C  CG  . PRO B 117 ? 0.3422 0.3662 0.5056 -0.0578 0.0600  0.0142  341  PRO B CG  
3245 C  CD  . PRO B 117 ? 0.2844 0.2992 0.4273 -0.0539 0.0572  0.0152  341  PRO B CD  
3246 N  N   . GLY B 118 ? 0.3511 0.3999 0.5140 -0.0470 0.0448  0.0078  342  GLY B N   
3247 C  CA  . GLY B 118 ? 0.3490 0.4037 0.5127 -0.0434 0.0474  0.0088  342  GLY B CA  
3248 C  C   . GLY B 118 ? 0.3345 0.3827 0.4790 -0.0385 0.0482  0.0108  342  GLY B C   
3249 O  O   . GLY B 118 ? 0.3158 0.3594 0.4486 -0.0370 0.0426  0.0098  342  GLY B O   
3250 N  N   . ASP B 119 ? 0.2855 0.3333 0.4267 -0.0359 0.0554  0.0136  343  ASP B N   
3251 C  CA  . ASP B 119 ? 0.3037 0.3456 0.4273 -0.0312 0.0565  0.0153  343  ASP B CA  
3252 C  C   . ASP B 119 ? 0.3267 0.3583 0.4386 -0.0310 0.0632  0.0191  343  ASP B C   
3253 O  O   . ASP B 119 ? 0.2985 0.3253 0.3969 -0.0270 0.0657  0.0208  343  ASP B O   
3254 C  CB  . ASP B 119 ? 0.3219 0.3694 0.4473 -0.0276 0.0591  0.0155  343  ASP B CB  
3255 C  CG  . ASP B 119 ? 0.3917 0.4421 0.5269 -0.0287 0.0684  0.0176  343  ASP B CG  
3256 O  OD1 . ASP B 119 ? 0.4286 0.4788 0.5733 -0.0331 0.0720  0.0186  343  ASP B OD1 
3257 O  OD2 . ASP B 119 ? 0.4571 0.5098 0.5907 -0.0253 0.0724  0.0183  343  ASP B OD2 
3258 N  N   . ALA B 120 ? 0.2989 0.3268 0.4157 -0.0350 0.0660  0.0203  344  ALA B N   
3259 C  CA  . ALA B 120 ? 0.2870 0.3040 0.3915 -0.0345 0.0716  0.0240  344  ALA B CA  
3260 C  C   . ALA B 120 ? 0.2902 0.3004 0.3788 -0.0319 0.0655  0.0233  344  ALA B C   
3261 O  O   . ALA B 120 ? 0.2784 0.2902 0.3690 -0.0331 0.0580  0.0202  344  ALA B O   
3262 C  CB  . ALA B 120 ? 0.2771 0.2912 0.3912 -0.0398 0.0755  0.0253  344  ALA B CB  
3263 N  N   . THR B 121 ? 0.2559 0.2586 0.3289 -0.0280 0.0687  0.0259  345  THR B N   
3264 C  CA  . THR B 121 ? 0.2854 0.2823 0.3441 -0.0252 0.0631  0.0253  345  THR B CA  
3265 C  C   . THR B 121 ? 0.3178 0.3036 0.3644 -0.0241 0.0675  0.0289  345  THR B C   
3266 O  O   . THR B 121 ? 0.3560 0.3381 0.4023 -0.0245 0.0755  0.0324  345  THR B O   
3267 C  CB  . THR B 121 ? 0.2679 0.2672 0.3179 -0.0205 0.0600  0.0240  345  THR B CB  
3268 O  OG1 . THR B 121 ? 0.2860 0.2816 0.3271 -0.0172 0.0664  0.0267  345  THR B OG1 
3269 C  CG2 . THR B 121 ? 0.2714 0.2809 0.3327 -0.0211 0.0564  0.0210  345  THR B CG2 
3270 N  N   . ARG B 122 ? 0.2623 0.2427 0.2991 -0.0226 0.0624  0.0281  346  ARG B N   
3271 C  CA  . ARG B 122 ? 0.2962 0.2657 0.3202 -0.0207 0.0651  0.0313  346  ARG B CA  
3272 C  C   . ARG B 122 ? 0.2709 0.2377 0.2846 -0.0178 0.0579  0.0293  346  ARG B C   
3273 O  O   . ARG B 122 ? 0.2842 0.2563 0.3031 -0.0189 0.0515  0.0258  346  ARG B O   
3274 C  CB  . ARG B 122 ? 0.2963 0.2604 0.3263 -0.0249 0.0688  0.0332  346  ARG B CB  
3275 C  CG  . ARG B 122 ? 0.2777 0.2433 0.3152 -0.0281 0.0624  0.0299  346  ARG B CG  
3276 C  CD  . ARG B 122 ? 0.2979 0.2612 0.3470 -0.0334 0.0664  0.0309  346  ARG B CD  
3277 N  NE  . ARG B 122 ? 0.3339 0.3052 0.3970 -0.0364 0.0706  0.0309  346  ARG B NE  
3278 C  CZ  . ARG B 122 ? 0.3489 0.3303 0.4254 -0.0388 0.0661  0.0270  346  ARG B CZ  
3279 N  NH1 . ARG B 122 ? 0.2689 0.2530 0.3461 -0.0390 0.0577  0.0230  346  ARG B NH1 
3280 N  NH2 . ARG B 122 ? 0.2928 0.2816 0.3819 -0.0409 0.0702  0.0272  346  ARG B NH2 
3281 N  N   . ALA B 123 ? 0.2679 0.2269 0.2672 -0.0138 0.0590  0.0316  347  ALA B N   
3282 C  CA  . ALA B 123 ? 0.2649 0.2218 0.2552 -0.0108 0.0524  0.0297  347  ALA B CA  
3283 C  C   . ALA B 123 ? 0.2916 0.2378 0.2683 -0.0076 0.0544  0.0329  347  ALA B C   
3284 O  O   . ALA B 123 ? 0.2861 0.2274 0.2557 -0.0056 0.0601  0.0363  347  ALA B O   
3285 C  CB  . ALA B 123 ? 0.2794 0.2421 0.2664 -0.0078 0.0486  0.0273  347  ALA B CB  
3286 N  N   . HIS B 124 ? 0.2766 0.2191 0.2494 -0.0067 0.0496  0.0318  348  HIS B N   
3287 C  CA  . HIS B 124 ? 0.3379 0.2701 0.2985 -0.0034 0.0505  0.0347  348  HIS B CA  
3288 C  C   . HIS B 124 ? 0.3324 0.2644 0.2884 -0.0008 0.0433  0.0320  348  HIS B C   
3289 O  O   . HIS B 124 ? 0.2928 0.2308 0.2564 -0.0029 0.0387  0.0284  348  HIS B O   
3290 C  CB  . HIS B 124 ? 0.2961 0.2209 0.2598 -0.0064 0.0552  0.0376  348  HIS B CB  
3291 C  CG  . HIS B 124 ? 0.3158 0.2413 0.2863 -0.0096 0.0628  0.0402  348  HIS B CG  
3292 N  ND1 . HIS B 124 ? 0.3876 0.3084 0.3496 -0.0072 0.0693  0.0442  348  HIS B ND1 
3293 C  CD2 . HIS B 124 ? 0.3079 0.2391 0.2934 -0.0149 0.0649  0.0392  348  HIS B CD2 
3294 C  CE1 . HIS B 124 ? 0.3387 0.2622 0.3105 -0.0110 0.0757  0.0457  348  HIS B CE1 
3295 N  NE2 . HIS B 124 ? 0.3393 0.2694 0.3261 -0.0158 0.0730  0.0427  348  HIS B NE2 
3296 N  N   . GLU B 125 ? 0.3581 0.2830 0.3014 0.0038  0.0425  0.0338  349  GLU B N   
3297 C  CA  . GLU B 125 ? 0.3659 0.2906 0.3051 0.0067  0.0360  0.0313  349  GLU B CA  
3298 C  C   . GLU B 125 ? 0.3480 0.2705 0.2932 0.0041  0.0343  0.0303  349  GLU B C   
3299 O  O   . GLU B 125 ? 0.3666 0.2833 0.3143 0.0016  0.0384  0.0327  349  GLU B O   
3300 C  CB  . GLU B 125 ? 0.3935 0.3107 0.3183 0.0124  0.0354  0.0335  349  GLU B CB  
3301 C  CG  . GLU B 125 ? 0.5430 0.4489 0.4611 0.0133  0.0399  0.0381  349  GLU B CG  
3302 C  CD  . GLU B 125 ? 0.6751 0.5735 0.5779 0.0197  0.0383  0.0401  349  GLU B CD  
3303 O  OE1 . GLU B 125 ? 0.6512 0.5532 0.5483 0.0229  0.0356  0.0385  349  GLU B OE1 
3304 O  OE2 . GLU B 125 ? 0.6144 0.5032 0.5111 0.0214  0.0396  0.0431  349  GLU B OE2 
3305 N  N   . ALA B 126 ? 0.2922 0.2193 0.2400 0.0047  0.0284  0.0266  350  ALA B N   
3306 C  CA  . ALA B 126 ? 0.3354 0.2617 0.2892 0.0024  0.0263  0.0247  350  ALA B CA  
3307 C  C   . ALA B 126 ? 0.3492 0.2765 0.2994 0.0059  0.0206  0.0222  350  ALA B C   
3308 O  O   . ALA B 126 ? 0.2932 0.2247 0.2397 0.0088  0.0177  0.0210  350  ALA B O   
3309 C  CB  . ALA B 126 ? 0.3031 0.2371 0.2690 -0.0026 0.0258  0.0219  350  ALA B CB  
3310 N  N   . ARG B 127 ? 0.3090 0.2323 0.2609 0.0055  0.0192  0.0211  351  ARG B N   
3311 C  CA  A ARG B 127 ? 0.3160 0.2401 0.2656 0.0087  0.0143  0.0186  351  ARG B CA  
3312 C  CA  B ARG B 127 ? 0.3245 0.2486 0.2741 0.0087  0.0144  0.0186  351  ARG B CA  
3313 C  C   . ARG B 127 ? 0.3178 0.2445 0.2751 0.0058  0.0124  0.0152  351  ARG B C   
3314 O  O   . ARG B 127 ? 0.3106 0.2328 0.2717 0.0027  0.0145  0.0156  351  ARG B O   
3315 C  CB  A ARG B 127 ? 0.3600 0.2745 0.3006 0.0132  0.0143  0.0211  351  ARG B CB  
3316 C  CB  B ARG B 127 ? 0.3601 0.2747 0.3006 0.0132  0.0145  0.0213  351  ARG B CB  
3317 C  CG  A ARG B 127 ? 0.3728 0.2777 0.3137 0.0114  0.0178  0.0235  351  ARG B CG  
3318 C  CG  B ARG B 127 ? 0.3679 0.2792 0.3085 0.0152  0.0115  0.0194  351  ARG B CG  
3319 C  CD  A ARG B 127 ? 0.4152 0.3095 0.3461 0.0163  0.0180  0.0266  351  ARG B CD  
3320 C  CD  B ARG B 127 ? 0.4041 0.3079 0.3347 0.0210  0.0103  0.0218  351  ARG B CD  
3321 N  NE  A ARG B 127 ? 0.4063 0.3003 0.3362 0.0200  0.0132  0.0240  351  ARG B NE  
3322 N  NE  B ARG B 127 ? 0.4356 0.3335 0.3583 0.0223  0.0139  0.0262  351  ARG B NE  
3323 C  CZ  A ARG B 127 ? 0.3917 0.2841 0.3267 0.0186  0.0121  0.0216  351  ARG B CZ  
3324 C  CZ  B ARG B 127 ? 0.4527 0.3397 0.3699 0.0230  0.0175  0.0303  351  ARG B CZ  
3325 N  NH1 A ARG B 127 ? 0.4190 0.3107 0.3611 0.0134  0.0145  0.0208  351  ARG B NH1 
3326 N  NH1 B ARG B 127 ? 0.4666 0.3467 0.3854 0.0227  0.0178  0.0304  351  ARG B NH1 
3327 N  NH2 A ARG B 127 ? 0.4061 0.2975 0.3391 0.0228  0.0083  0.0197  351  ARG B NH2 
3328 N  NH2 B ARG B 127 ? 0.4771 0.3592 0.3865 0.0243  0.0212  0.0343  351  ARG B NH2 
3329 N  N   . ILE B 128 ? 0.2964 0.2302 0.2560 0.0067  0.0084  0.0118  352  ILE B N   
3330 C  CA  . ILE B 128 ? 0.2571 0.1934 0.2222 0.0047  0.0063  0.0083  352  ILE B CA  
3331 C  C   . ILE B 128 ? 0.3043 0.2398 0.2662 0.0089  0.0032  0.0066  352  ILE B C   
3332 O  O   . ILE B 128 ? 0.2562 0.1960 0.2157 0.0119  0.0011  0.0061  352  ILE B O   
3333 C  CB  . ILE B 128 ? 0.2642 0.2101 0.2353 0.0019  0.0049  0.0058  352  ILE B CB  
3334 C  CG1 . ILE B 128 ? 0.2629 0.2101 0.2386 -0.0021 0.0078  0.0072  352  ILE B CG1 
3335 C  CG2 . ILE B 128 ? 0.2554 0.2036 0.2301 0.0009  0.0024  0.0021  352  ILE B CG2 
3336 C  CD1 . ILE B 128 ? 0.2505 0.2070 0.2317 -0.0044 0.0062  0.0051  352  ILE B CD1 
3337 N  N   . ASP B 129 ? 0.2821 0.2119 0.2444 0.0091  0.0030  0.0055  353  ASP B N   
3338 C  CA  . ASP B 129 ? 0.2864 0.2147 0.2462 0.0133  0.0005  0.0038  353  ASP B CA  
3339 C  C   . ASP B 129 ? 0.3120 0.2472 0.2766 0.0122  -0.0016 -0.0004 353  ASP B C   
3340 O  O   . ASP B 129 ? 0.2907 0.2233 0.2577 0.0103  -0.0016 -0.0025 353  ASP B O   
3341 C  CB  . ASP B 129 ? 0.3275 0.2449 0.2845 0.0146  0.0016  0.0050  353  ASP B CB  
3342 C  CG  . ASP B 129 ? 0.3872 0.3028 0.3418 0.0196  -0.0010 0.0034  353  ASP B CG  
3343 O  OD1 . ASP B 129 ? 0.3833 0.3067 0.3392 0.0217  -0.0035 0.0012  353  ASP B OD1 
3344 O  OD2 . ASP B 129 ? 0.3650 0.2712 0.3166 0.0214  -0.0003 0.0046  353  ASP B OD2 
3345 N  N   . THR B 130 ? 0.2508 0.1942 0.2163 0.0135  -0.0035 -0.0016 354  THR B N   
3346 C  CA  . THR B 130 ? 0.2607 0.2104 0.2299 0.0124  -0.0048 -0.0052 354  THR B CA  
3347 C  C   . THR B 130 ? 0.2816 0.2290 0.2503 0.0156  -0.0059 -0.0076 354  THR B C   
3348 O  O   . THR B 130 ? 0.2718 0.2237 0.2428 0.0152  -0.0066 -0.0106 354  THR B O   
3349 C  CB  . THR B 130 ? 0.2374 0.1962 0.2083 0.0127  -0.0059 -0.0057 354  THR B CB  
3350 O  OG1 . THR B 130 ? 0.2585 0.2181 0.2274 0.0169  -0.0074 -0.0053 354  THR B OG1 
3351 C  CG2 . THR B 130 ? 0.2471 0.2079 0.2186 0.0098  -0.0048 -0.0035 354  THR B CG2 
3352 N  N   . GLY B 131 ? 0.2751 0.2154 0.2405 0.0189  -0.0060 -0.0063 355  GLY B N   
3353 C  CA  . GLY B 131 ? 0.2882 0.2250 0.2531 0.0221  -0.0068 -0.0085 355  GLY B CA  
3354 C  C   . GLY B 131 ? 0.3630 0.2906 0.3273 0.0207  -0.0057 -0.0090 355  GLY B C   
3355 O  O   . GLY B 131 ? 0.3122 0.2363 0.2761 0.0233  -0.0063 -0.0113 355  GLY B O   
3356 N  N   . SER B 132 ? 0.3334 0.2570 0.2980 0.0167  -0.0039 -0.0072 356  SER B N   
3357 C  CA  . SER B 132 ? 0.3121 0.2260 0.2766 0.0152  -0.0028 -0.0074 356  SER B CA  
3358 C  C   . SER B 132 ? 0.3246 0.2398 0.2923 0.0129  -0.0037 -0.0120 356  SER B C   
3359 O  O   . SER B 132 ? 0.3097 0.2330 0.2797 0.0111  -0.0046 -0.0141 356  SER B O   
3360 C  CB  . SER B 132 ? 0.2933 0.2029 0.2584 0.0113  -0.0002 -0.0040 356  SER B CB  
3361 O  OG  . SER B 132 ? 0.3233 0.2410 0.2922 0.0075  -0.0001 -0.0045 356  SER B OG  
3362 N  N   . ASP B 133 ? 0.3247 0.2309 0.2919 0.0132  -0.0035 -0.0134 357  ASP B N   
3363 C  CA  . ASP B 133 ? 0.3157 0.2214 0.2848 0.0117  -0.0046 -0.0182 357  ASP B CA  
3364 C  C   . ASP B 133 ? 0.2967 0.2074 0.2697 0.0063  -0.0051 -0.0197 357  ASP B C   
3365 O  O   . ASP B 133 ? 0.2890 0.2046 0.2625 0.0058  -0.0067 -0.0235 357  ASP B O   
3366 C  CB  . ASP B 133 ? 0.3439 0.2376 0.3122 0.0122  -0.0042 -0.0191 357  ASP B CB  
3367 C  CG  . ASP B 133 ? 0.3894 0.2792 0.3542 0.0181  -0.0047 -0.0198 357  ASP B CG  
3368 O  OD1 . ASP B 133 ? 0.4076 0.3052 0.3716 0.0216  -0.0056 -0.0205 357  ASP B OD1 
3369 O  OD2 . ASP B 133 ? 0.4823 0.3614 0.4457 0.0194  -0.0042 -0.0198 357  ASP B OD2 
3370 N  N   . THR B 134 ? 0.3116 0.2212 0.2871 0.0026  -0.0036 -0.0166 358  THR B N   
3371 C  CA  . THR B 134 ? 0.2822 0.1960 0.2626 -0.0024 -0.0042 -0.0181 358  THR B CA  
3372 C  C   . THR B 134 ? 0.2921 0.2164 0.2736 -0.0033 -0.0045 -0.0167 358  THR B C   
3373 O  O   . THR B 134 ? 0.2665 0.1951 0.2522 -0.0071 -0.0052 -0.0177 358  THR B O   
3374 C  CB  . THR B 134 ? 0.3039 0.2110 0.2883 -0.0065 -0.0022 -0.0160 358  THR B CB  
3375 O  OG1 . THR B 134 ? 0.3136 0.2197 0.2964 -0.0056 0.0007  -0.0107 358  THR B OG1 
3376 C  CG2 . THR B 134 ? 0.3352 0.2312 0.3194 -0.0064 -0.0021 -0.0178 358  THR B CG2 
3377 N  N   . PHE B 135 ? 0.2656 0.1940 0.2440 0.0002  -0.0041 -0.0146 359  PHE B N   
3378 C  CA  . PHE B 135 ? 0.2861 0.2240 0.2654 -0.0004 -0.0046 -0.0139 359  PHE B CA  
3379 C  C   . PHE B 135 ? 0.2524 0.1960 0.2321 -0.0008 -0.0068 -0.0178 359  PHE B C   
3380 O  O   . PHE B 135 ? 0.2545 0.1990 0.2315 0.0024  -0.0074 -0.0198 359  PHE B O   
3381 C  CB  . PHE B 135 ? 0.2531 0.1936 0.2292 0.0034  -0.0041 -0.0113 359  PHE B CB  
3382 C  CG  . PHE B 135 ? 0.2516 0.2013 0.2288 0.0029  -0.0046 -0.0107 359  PHE B CG  
3383 C  CD1 . PHE B 135 ? 0.2559 0.2078 0.2351 0.0003  -0.0035 -0.0082 359  PHE B CD1 
3384 C  CD2 . PHE B 135 ? 0.2392 0.1950 0.2158 0.0049  -0.0059 -0.0125 359  PHE B CD2 
3385 C  CE1 . PHE B 135 ? 0.2403 0.2000 0.2205 -0.0001 -0.0040 -0.0077 359  PHE B CE1 
3386 C  CE2 . PHE B 135 ? 0.2316 0.1950 0.2093 0.0043  -0.0062 -0.0118 359  PHE B CE2 
3387 C  CZ  . PHE B 135 ? 0.2350 0.2003 0.2145 0.0018  -0.0055 -0.0095 359  PHE B CZ  
3388 N  N   . ALA B 136 ? 0.2496 0.1968 0.2325 -0.0044 -0.0078 -0.0190 360  ALA B N   
3389 C  CA  . ALA B 136 ? 0.2484 0.1996 0.2306 -0.0048 -0.0100 -0.0228 360  ALA B CA  
3390 C  C   . ALA B 136 ? 0.2416 0.2002 0.2264 -0.0072 -0.0110 -0.0221 360  ALA B C   
3391 O  O   . ALA B 136 ? 0.2427 0.2021 0.2300 -0.0101 -0.0129 -0.0241 360  ALA B O   
3392 C  CB  . ALA B 136 ? 0.2564 0.2015 0.2391 -0.0064 -0.0115 -0.0265 360  ALA B CB  
3393 N  N   . PRO B 137 ? 0.2349 0.1990 0.2191 -0.0060 -0.0100 -0.0194 361  PRO B N   
3394 C  CA  . PRO B 137 ? 0.2414 0.2120 0.2282 -0.0080 -0.0108 -0.0184 361  PRO B CA  
3395 C  C   . PRO B 137 ? 0.2605 0.2349 0.2457 -0.0084 -0.0131 -0.0212 361  PRO B C   
3396 O  O   . PRO B 137 ? 0.2473 0.2256 0.2352 -0.0105 -0.0145 -0.0210 361  PRO B O   
3397 C  CB  . PRO B 137 ? 0.2231 0.1976 0.2087 -0.0059 -0.0093 -0.0155 361  PRO B CB  
3398 C  CG  . PRO B 137 ? 0.2255 0.1978 0.2075 -0.0025 -0.0087 -0.0162 361  PRO B CG  
3399 C  CD  . PRO B 137 ? 0.2331 0.1977 0.2147 -0.0025 -0.0086 -0.0176 361  PRO B CD  
3400 N  N   . LYS B 138 ? 0.2670 0.2403 0.2478 -0.0062 -0.0136 -0.0238 362  LYS B N   
3401 C  CA  . LYS B 138 ? 0.2471 0.2232 0.2248 -0.0062 -0.0156 -0.0263 362  LYS B CA  
3402 C  C   . LYS B 138 ? 0.2565 0.2311 0.2365 -0.0090 -0.0185 -0.0288 362  LYS B C   
3403 O  O   . LYS B 138 ? 0.2634 0.2417 0.2424 -0.0098 -0.0207 -0.0297 362  LYS B O   
3404 C  CB  . LYS B 138 ? 0.2379 0.2121 0.2102 -0.0032 -0.0150 -0.0290 362  LYS B CB  
3405 C  CG  . LYS B 138 ? 0.2835 0.2604 0.2511 -0.0028 -0.0165 -0.0312 362  LYS B CG  
3406 C  CD  . LYS B 138 ? 0.3833 0.3585 0.3451 0.0003  -0.0154 -0.0339 362  LYS B CD  
3407 C  CE  . LYS B 138 ? 0.4369 0.4168 0.3937 0.0015  -0.0149 -0.0337 362  LYS B CE  
3408 N  NZ  . LYS B 138 ? 0.4074 0.3910 0.3650 -0.0008 -0.0171 -0.0321 362  LYS B NZ  
3409 N  N   . ILE B 139 ? 0.2505 0.2194 0.2335 -0.0106 -0.0187 -0.0298 363  ILE B N   
3410 C  CA  . ILE B 139 ? 0.2693 0.2367 0.2561 -0.0137 -0.0216 -0.0324 363  ILE B CA  
3411 C  C   . ILE B 139 ? 0.3123 0.2803 0.3071 -0.0169 -0.0206 -0.0297 363  ILE B C   
3412 O  O   . ILE B 139 ? 0.2958 0.2617 0.2960 -0.0200 -0.0222 -0.0316 363  ILE B O   
3413 C  CB  . ILE B 139 ? 0.2562 0.2163 0.2412 -0.0136 -0.0227 -0.0365 363  ILE B CB  
3414 C  CG1 . ILE B 139 ? 0.2568 0.2108 0.2422 -0.0124 -0.0195 -0.0347 363  ILE B CG1 
3415 C  CG2 . ILE B 139 ? 0.2589 0.2192 0.2360 -0.0107 -0.0241 -0.0398 363  ILE B CG2 
3416 C  CD1 . ILE B 139 ? 0.2667 0.2121 0.2517 -0.0127 -0.0205 -0.0384 363  ILE B CD1 
3417 N  N   . GLY B 140 ? 0.2791 0.2500 0.2750 -0.0162 -0.0178 -0.0256 364  GLY B N   
3418 C  CA  . GLY B 140 ? 0.2623 0.2348 0.2649 -0.0188 -0.0163 -0.0228 364  GLY B CA  
3419 C  C   . GLY B 140 ? 0.3001 0.2662 0.3058 -0.0201 -0.0135 -0.0212 364  GLY B C   
3420 O  O   . GLY B 140 ? 0.2896 0.2565 0.3015 -0.0227 -0.0119 -0.0193 364  GLY B O   
3421 N  N   . GLN B 141 ? 0.2685 0.2281 0.2699 -0.0181 -0.0125 -0.0219 365  GLN B N   
3422 C  CA  . GLN B 141 ? 0.2783 0.2302 0.2815 -0.0190 -0.0099 -0.0202 365  GLN B CA  
3423 C  C   . GLN B 141 ? 0.2983 0.2488 0.2970 -0.0159 -0.0068 -0.0163 365  GLN B C   
3424 O  O   . GLN B 141 ? 0.2857 0.2346 0.2789 -0.0123 -0.0070 -0.0168 365  GLN B O   
3425 C  CB  . GLN B 141 ? 0.2567 0.2013 0.2583 -0.0189 -0.0113 -0.0238 365  GLN B CB  
3426 C  CG  . GLN B 141 ? 0.3012 0.2472 0.3067 -0.0218 -0.0150 -0.0282 365  GLN B CG  
3427 C  CD  . GLN B 141 ? 0.3059 0.2444 0.3092 -0.0216 -0.0167 -0.0324 365  GLN B CD  
3428 O  OE1 . GLN B 141 ? 0.2847 0.2174 0.2833 -0.0187 -0.0152 -0.0321 365  GLN B OE1 
3429 N  NE2 . GLN B 141 ? 0.3036 0.2422 0.3107 -0.0244 -0.0203 -0.0366 365  GLN B NE2 
3430 N  N   . VAL B 142 ? 0.2447 0.1960 0.2459 -0.0170 -0.0041 -0.0125 366  VAL B N   
3431 C  CA  . VAL B 142 ? 0.2541 0.2034 0.2508 -0.0140 -0.0013 -0.0087 366  VAL B CA  
3432 C  C   . VAL B 142 ? 0.3154 0.2590 0.3146 -0.0160 0.0024  -0.0054 366  VAL B C   
3433 O  O   . VAL B 142 ? 0.2495 0.1951 0.2554 -0.0197 0.0034  -0.0051 366  VAL B O   
3434 C  CB  . VAL B 142 ? 0.2856 0.2427 0.2809 -0.0125 -0.0016 -0.0073 366  VAL B CB  
3435 C  CG1 . VAL B 142 ? 0.2523 0.2072 0.2432 -0.0099 0.0010  -0.0035 366  VAL B CG1 
3436 C  CG2 . VAL B 142 ? 0.2324 0.1939 0.2245 -0.0103 -0.0044 -0.0099 366  VAL B CG2 
3437 N  N   . ARG B 143 ? 0.2937 0.2302 0.2877 -0.0133 0.0045  -0.0029 367  ARG B N   
3438 C  CA  . ARG B 143 ? 0.3064 0.2364 0.3007 -0.0144 0.0086  0.0010  367  ARG B CA  
3439 C  C   . ARG B 143 ? 0.3115 0.2419 0.2996 -0.0111 0.0107  0.0049  367  ARG B C   
3440 O  O   . ARG B 143 ? 0.2877 0.2197 0.2701 -0.0071 0.0087  0.0045  367  ARG B O   
3441 C  CB  . ARG B 143 ? 0.3148 0.2341 0.3070 -0.0139 0.0095  0.0012  367  ARG B CB  
3442 C  CG  . ARG B 143 ? 0.2761 0.1933 0.2740 -0.0173 0.0076  -0.0028 367  ARG B CG  
3443 C  CD  . ARG B 143 ? 0.3498 0.2564 0.3440 -0.0154 0.0078  -0.0031 367  ARG B CD  
3444 N  NE  . ARG B 143 ? 0.2994 0.2027 0.2996 -0.0191 0.0063  -0.0069 367  ARG B NE  
3445 C  CZ  . ARG B 143 ? 0.3963 0.2895 0.3953 -0.0187 0.0065  -0.0079 367  ARG B CZ  
3446 N  NH1 . ARG B 143 ? 0.3487 0.2342 0.3408 -0.0147 0.0082  -0.0050 367  ARG B NH1 
3447 N  NH2 . ARG B 143 ? 0.3931 0.2837 0.3980 -0.0223 0.0047  -0.0119 367  ARG B NH2 
3448 N  N   . PHE B 144 ? 0.2882 0.2169 0.2774 -0.0127 0.0148  0.0084  368  PHE B N   
3449 C  CA  . PHE B 144 ? 0.2894 0.2162 0.2713 -0.0093 0.0171  0.0122  368  PHE B CA  
3450 C  C   . PHE B 144 ? 0.3009 0.2180 0.2806 -0.0098 0.0220  0.0164  368  PHE B C   
3451 O  O   . PHE B 144 ? 0.3029 0.2175 0.2893 -0.0141 0.0247  0.0168  368  PHE B O   
3452 C  CB  . PHE B 144 ? 0.2669 0.2022 0.2506 -0.0098 0.0177  0.0128  368  PHE B CB  
3453 C  CG  . PHE B 144 ? 0.2601 0.1973 0.2514 -0.0141 0.0214  0.0141  368  PHE B CG  
3454 C  CD1 . PHE B 144 ? 0.2606 0.2043 0.2614 -0.0179 0.0196  0.0111  368  PHE B CD1 
3455 C  CD2 . PHE B 144 ? 0.2714 0.2044 0.2603 -0.0140 0.0267  0.0183  368  PHE B CD2 
3456 C  CE1 . PHE B 144 ? 0.2713 0.2178 0.2806 -0.0217 0.0227  0.0120  368  PHE B CE1 
3457 C  CE2 . PHE B 144 ? 0.2668 0.2023 0.2638 -0.0179 0.0306  0.0194  368  PHE B CE2 
3458 C  CZ  . PHE B 144 ? 0.2851 0.2278 0.2930 -0.0218 0.0284  0.0162  368  PHE B CZ  
3459 N  N   . TYR B 145 ? 0.3129 0.2242 0.2828 -0.0054 0.0230  0.0194  369  TYR B N   
3460 C  CA  . TYR B 145 ? 0.3177 0.2192 0.2829 -0.0049 0.0280  0.0241  369  TYR B CA  
3461 C  C   . TYR B 145 ? 0.3147 0.2184 0.2754 -0.0036 0.0312  0.0273  369  TYR B C   
3462 O  O   . TYR B 145 ? 0.3253 0.2353 0.2826 -0.0008 0.0286  0.0262  369  TYR B O   
3463 C  CB  . TYR B 145 ? 0.3297 0.2219 0.2856 -0.0001 0.0267  0.0256  369  TYR B CB  
3464 C  CG  . TYR B 145 ? 0.3666 0.2475 0.3165 0.0006  0.0320  0.0309  369  TYR B CG  
3465 C  CD1 . TYR B 145 ? 0.4152 0.2883 0.3699 -0.0031 0.0354  0.0322  369  TYR B CD1 
3466 C  CD2 . TYR B 145 ? 0.4036 0.2810 0.3427 0.0050  0.0337  0.0348  369  TYR B CD2 
3467 C  CE1 . TYR B 145 ? 0.3773 0.2393 0.3264 -0.0026 0.0409  0.0376  369  TYR B CE1 
3468 C  CE2 . TYR B 145 ? 0.3817 0.2479 0.3140 0.0059  0.0390  0.0401  369  TYR B CE2 
3469 C  CZ  . TYR B 145 ? 0.3978 0.2563 0.3352 0.0020  0.0429  0.0417  369  TYR B CZ  
3470 O  OH  . TYR B 145 ? 0.4565 0.3032 0.3872 0.0028  0.0487  0.0474  369  TYR B OH  
3471 N  N   . SER B 146 ? 0.3524 0.2504 0.3131 -0.0055 0.0373  0.0314  370  SER B N   
3472 C  CA  . SER B 146 ? 0.3552 0.2537 0.3106 -0.0040 0.0414  0.0347  370  SER B CA  
3473 C  C   . SER B 146 ? 0.3487 0.2353 0.2970 -0.0031 0.0474  0.0402  370  SER B C   
3474 O  O   . SER B 146 ? 0.3688 0.2490 0.3219 -0.0063 0.0502  0.0414  370  SER B O   
3475 C  CB  . SER B 146 ? 0.3386 0.2463 0.3044 -0.0084 0.0436  0.0336  370  SER B CB  
3476 O  OG  . SER B 146 ? 0.3057 0.2131 0.2666 -0.0070 0.0485  0.0369  370  SER B OG  
3477 N  N   . THR B 147 ? 0.3660 0.2492 0.3025 0.0014  0.0493  0.0435  371  THR B N   
3478 C  CA  . THR B 147 ? 0.4236 0.2957 0.3521 0.0025  0.0561  0.0493  371  THR B CA  
3479 C  C   . THR B 147 ? 0.3736 0.2475 0.3103 -0.0025 0.0636  0.0515  371  THR B C   
3480 O  O   . THR B 147 ? 0.4274 0.2920 0.3597 -0.0028 0.0704  0.0566  371  THR B O   
3481 C  CB  . THR B 147 ? 0.4450 0.3135 0.3579 0.0090  0.0558  0.0518  371  THR B CB  
3482 O  OG1 . THR B 147 ? 0.4092 0.2877 0.3234 0.0093  0.0550  0.0497  371  THR B OG1 
3483 C  CG2 . THR B 147 ? 0.3835 0.2491 0.2885 0.0143  0.0488  0.0501  371  THR B CG2 
3484 N  N   . SER B 148 ? 0.3464 0.2318 0.2951 -0.0063 0.0626  0.0480  372  SER B N   
3485 C  CA  . SER B 148 ? 0.3973 0.2860 0.3562 -0.0112 0.0691  0.0495  372  SER B CA  
3486 C  C   . SER B 148 ? 0.3598 0.2506 0.3340 -0.0174 0.0685  0.0470  372  SER B C   
3487 O  O   . SER B 148 ? 0.3985 0.2933 0.3773 -0.0181 0.0618  0.0425  372  SER B O   
3488 C  CB  . SER B 148 ? 0.3562 0.2564 0.3188 -0.0111 0.0685  0.0472  372  SER B CB  
3489 O  OG  . SER B 148 ? 0.3916 0.2963 0.3663 -0.0160 0.0742  0.0480  372  SER B OG  
3490 N  N   . SER B 149 ? 0.3559 0.2438 0.3379 -0.0219 0.0755  0.0498  373  SER B N   
3491 C  CA  . SER B 149 ? 0.3513 0.2425 0.3498 -0.0283 0.0752  0.0471  373  SER B CA  
3492 C  C   . SER B 149 ? 0.3982 0.3018 0.4103 -0.0321 0.0765  0.0450  373  SER B C   
3493 O  O   . SER B 149 ? 0.3342 0.2417 0.3614 -0.0376 0.0765  0.0427  373  SER B O   
3494 C  CB  . SER B 149 ? 0.4362 0.3160 0.4368 -0.0315 0.0817  0.0513  373  SER B CB  
3495 O  OG  . SER B 149 ? 0.4288 0.3070 0.4298 -0.0326 0.0908  0.0561  373  SER B OG  
3496 N  N   . ASP B 150 ? 0.3804 0.2901 0.3877 -0.0289 0.0772  0.0454  374  ASP B N   
3497 C  CA  . ASP B 150 ? 0.3762 0.2973 0.3957 -0.0317 0.0790  0.0437  374  ASP B CA  
3498 C  C   . ASP B 150 ? 0.3004 0.2321 0.3261 -0.0319 0.0704  0.0378  374  ASP B C   
3499 O  O   . ASP B 150 ? 0.3266 0.2650 0.3487 -0.0289 0.0677  0.0363  374  ASP B O   
3500 C  CB  . ASP B 150 ? 0.3235 0.2450 0.3344 -0.0280 0.0846  0.0471  374  ASP B CB  
3501 C  CG  . ASP B 150 ? 0.3803 0.3140 0.4025 -0.0297 0.0857  0.0450  374  ASP B CG  
3502 O  OD1 . ASP B 150 ? 0.3697 0.3089 0.4083 -0.0350 0.0873  0.0437  374  ASP B OD1 
3503 O  OD2 . ASP B 150 ? 0.4043 0.3420 0.4193 -0.0256 0.0847  0.0445  374  ASP B OD2 
3504 N  N   . PHE B 151 ? 0.3416 0.2742 0.3765 -0.0356 0.0660  0.0345  375  PHE B N   
3505 C  CA  . PHE B 151 ? 0.2897 0.2320 0.3323 -0.0368 0.0584  0.0290  375  PHE B CA  
3506 C  C   . PHE B 151 ? 0.3030 0.2490 0.3625 -0.0429 0.0583  0.0266  375  PHE B C   
3507 O  O   . PHE B 151 ? 0.3120 0.2505 0.3750 -0.0460 0.0614  0.0280  375  PHE B O   
3508 C  CB  . PHE B 151 ? 0.3331 0.2724 0.3673 -0.0340 0.0513  0.0262  375  PHE B CB  
3509 C  CG  . PHE B 151 ? 0.2771 0.2157 0.2973 -0.0282 0.0495  0.0272  375  PHE B CG  
3510 C  CD1 . PHE B 151 ? 0.2691 0.2165 0.2892 -0.0264 0.0451  0.0245  375  PHE B CD1 
3511 C  CD2 . PHE B 151 ? 0.3456 0.2743 0.3529 -0.0246 0.0520  0.0308  375  PHE B CD2 
3512 C  CE1 . PHE B 151 ? 0.3296 0.2765 0.3378 -0.0214 0.0434  0.0250  375  PHE B CE1 
3513 C  CE2 . PHE B 151 ? 0.2935 0.2220 0.2886 -0.0192 0.0497  0.0312  375  PHE B CE2 
3514 C  CZ  . PHE B 151 ? 0.3204 0.2580 0.3164 -0.0178 0.0455  0.0282  375  PHE B CZ  
3515 N  N   . GLU B 152 ? 0.2884 0.2455 0.3585 -0.0446 0.0545  0.0229  376  GLU B N   
3516 C  CA  . GLU B 152 ? 0.3086 0.2707 0.3955 -0.0501 0.0530  0.0198  376  GLU B CA  
3517 C  C   . GLU B 152 ? 0.3451 0.3095 0.4330 -0.0505 0.0440  0.0144  376  GLU B C   
3518 O  O   . GLU B 152 ? 0.2854 0.2539 0.3663 -0.0470 0.0388  0.0124  376  GLU B O   
3519 C  CB  . GLU B 152 ? 0.3346 0.3078 0.4336 -0.0516 0.0548  0.0192  376  GLU B CB  
3520 C  CG  . GLU B 152 ? 0.3680 0.3403 0.4653 -0.0506 0.0638  0.0241  376  GLU B CG  
3521 C  CD  . GLU B 152 ? 0.5733 0.5499 0.6883 -0.0558 0.0693  0.0248  376  GLU B CD  
3522 O  OE1 . GLU B 152 ? 0.6387 0.6145 0.7647 -0.0606 0.0674  0.0226  376  GLU B OE1 
3523 O  OE2 . GLU B 152 ? 0.6071 0.5879 0.7253 -0.0552 0.0755  0.0274  376  GLU B OE2 
3524 N  N   . THR B 153 ? 0.3321 0.2938 0.4290 -0.0548 0.0423  0.0119  377  THR B N   
3525 C  CA  . THR B 153 ? 0.3481 0.3121 0.4466 -0.0554 0.0339  0.0064  377  THR B CA  
3526 C  C   . THR B 153 ? 0.3500 0.3264 0.4589 -0.0565 0.0292  0.0027  377  THR B C   
3527 O  O   . THR B 153 ? 0.2897 0.2725 0.4099 -0.0588 0.0326  0.0037  377  THR B O   
3528 C  CB  . THR B 153 ? 0.3328 0.2898 0.4379 -0.0597 0.0333  0.0044  377  THR B CB  
3529 O  OG1 . THR B 153 ? 0.4663 0.4268 0.5877 -0.0650 0.0370  0.0047  377  THR B OG1 
3530 C  CG2 . THR B 153 ? 0.3854 0.3293 0.4797 -0.0581 0.0377  0.0082  377  THR B CG2 
3531 N  N   . ASN B 154 ? 0.2932 0.2727 0.3977 -0.0545 0.0216  -0.0013 378  ASN B N   
3532 C  CA  . ASN B 154 ? 0.3176 0.3077 0.4298 -0.0550 0.0157  -0.0052 378  ASN B CA  
3533 C  C   . ASN B 154 ? 0.3206 0.3186 0.4335 -0.0526 0.0180  -0.0029 378  ASN B C   
3534 O  O   . ASN B 154 ? 0.3182 0.3251 0.4425 -0.0541 0.0164  -0.0045 378  ASN B O   
3535 C  CB  . ASN B 154 ? 0.2963 0.2897 0.4249 -0.0604 0.0137  -0.0086 378  ASN B CB  
3536 C  CG  . ASN B 154 ? 0.3919 0.3785 0.5193 -0.0622 0.0093  -0.0124 378  ASN B CG  
3537 O  OD1 . ASN B 154 ? 0.3546 0.3382 0.4703 -0.0590 0.0048  -0.0143 378  ASN B OD1 
3538 N  ND2 . ASN B 154 ? 0.3602 0.3439 0.4994 -0.0673 0.0110  -0.0135 378  ASN B ND2 
3539 N  N   . GLN B 155 ? 0.2903 0.2850 0.3908 -0.0486 0.0213  0.0006  379  GLN B N   
3540 C  CA  . GLN B 155 ? 0.2790 0.2801 0.3776 -0.0456 0.0226  0.0024  379  GLN B CA  
3541 C  C   . GLN B 155 ? 0.2756 0.2755 0.3601 -0.0410 0.0188  0.0020  379  GLN B C   
3542 O  O   . GLN B 155 ? 0.2658 0.2585 0.3405 -0.0395 0.0181  0.0022  379  GLN B O   
3543 C  CB  . GLN B 155 ? 0.2803 0.2788 0.3780 -0.0452 0.0312  0.0072  379  GLN B CB  
3544 C  CG  . GLN B 155 ? 0.2781 0.2787 0.3909 -0.0498 0.0362  0.0080  379  GLN B CG  
3545 C  CD  . GLN B 155 ? 0.3288 0.3408 0.4564 -0.0517 0.0330  0.0050  379  GLN B CD  
3546 O  OE1 . GLN B 155 ? 0.3063 0.3246 0.4318 -0.0488 0.0286  0.0034  379  GLN B OE1 
3547 N  NE2 . GLN B 155 ? 0.3060 0.3207 0.4492 -0.0565 0.0352  0.0043  379  GLN B NE2 
3548 N  N   . PRO B 156 ? 0.2735 0.2804 0.3576 -0.0387 0.0164  0.0014  380  PRO B N   
3549 C  CA  . PRO B 156 ? 0.2363 0.2423 0.3082 -0.0347 0.0130  0.0011  380  PRO B CA  
3550 C  C   . PRO B 156 ? 0.2691 0.2688 0.3298 -0.0317 0.0174  0.0045  380  PRO B C   
3551 O  O   . PRO B 156 ? 0.2831 0.2822 0.3441 -0.0312 0.0229  0.0075  380  PRO B O   
3552 C  CB  . PRO B 156 ? 0.2557 0.2702 0.3314 -0.0332 0.0105  0.0002  380  PRO B CB  
3553 C  CG  . PRO B 156 ? 0.2817 0.3009 0.3696 -0.0355 0.0145  0.0012  380  PRO B CG  
3554 C  CD  . PRO B 156 ? 0.2567 0.2727 0.3522 -0.0396 0.0162  0.0007  380  PRO B CD  
3555 N  N   . THR B 157 ? 0.2221 0.2172 0.2726 -0.0295 0.0148  0.0039  381  THR B N   
3556 C  CA  . THR B 157 ? 0.2201 0.2085 0.2601 -0.0268 0.0179  0.0066  381  THR B CA  
3557 C  C   . THR B 157 ? 0.2165 0.2060 0.2476 -0.0231 0.0143  0.0058  381  THR B C   
3558 O  O   . THR B 157 ? 0.2389 0.2305 0.2696 -0.0231 0.0096  0.0030  381  THR B O   
3559 C  CB  . THR B 157 ? 0.2734 0.2536 0.3112 -0.0280 0.0189  0.0069  381  THR B CB  
3560 O  OG1 . THR B 157 ? 0.2628 0.2423 0.3107 -0.0321 0.0219  0.0073  381  THR B OG1 
3561 C  CG2 . THR B 157 ? 0.2325 0.2054 0.2595 -0.0248 0.0221  0.0101  381  THR B CG2 
3562 N  N   . HIS B 158 ? 0.2159 0.2040 0.2398 -0.0201 0.0166  0.0080  382  HIS B N   
3563 C  CA  . HIS B 158 ? 0.2123 0.2013 0.2286 -0.0168 0.0134  0.0072  382  HIS B CA  
3564 C  C   . HIS B 158 ? 0.2535 0.2358 0.2601 -0.0140 0.0151  0.0091  382  HIS B C   
3565 O  O   . HIS B 158 ? 0.2483 0.2264 0.2525 -0.0135 0.0195  0.0118  382  HIS B O   
3566 C  CB  . HIS B 158 ? 0.2404 0.2354 0.2578 -0.0155 0.0133  0.0073  382  HIS B CB  
3567 C  CG  . HIS B 158 ? 0.2489 0.2451 0.2600 -0.0128 0.0100  0.0063  382  HIS B CG  
3568 N  ND1 . HIS B 158 ? 0.2827 0.2837 0.2960 -0.0131 0.0060  0.0043  382  HIS B ND1 
3569 C  CD2 . HIS B 158 ? 0.2495 0.2427 0.2525 -0.0098 0.0101  0.0071  382  HIS B CD2 
3570 C  CE1 . HIS B 158 ? 0.2701 0.2710 0.2776 -0.0107 0.0043  0.0040  382  HIS B CE1 
3571 N  NE2 . HIS B 158 ? 0.2700 0.2667 0.2717 -0.0087 0.0065  0.0054  382  HIS B NE2 
3572 N  N   . PHE B 159 ? 0.2315 0.2128 0.2327 -0.0120 0.0117  0.0077  383  PHE B N   
3573 C  CA  . PHE B 159 ? 0.2646 0.2403 0.2571 -0.0087 0.0122  0.0090  383  PHE B CA  
3574 C  C   . PHE B 159 ? 0.2546 0.2337 0.2428 -0.0059 0.0101  0.0084  383  PHE B C   
3575 O  O   . PHE B 159 ? 0.2112 0.1944 0.2006 -0.0058 0.0067  0.0062  383  PHE B O   
3576 C  CB  . PHE B 159 ? 0.2357 0.2073 0.2260 -0.0083 0.0102  0.0077  383  PHE B CB  
3577 C  CG  . PHE B 159 ? 0.2379 0.2044 0.2197 -0.0045 0.0099  0.0089  383  PHE B CG  
3578 C  CD1 . PHE B 159 ? 0.2937 0.2525 0.2709 -0.0034 0.0130  0.0116  383  PHE B CD1 
3579 C  CD2 . PHE B 159 ? 0.2239 0.1933 0.2025 -0.0018 0.0066  0.0073  383  PHE B CD2 
3580 C  CE1 . PHE B 159 ? 0.2615 0.2155 0.2305 0.0006  0.0123  0.0127  383  PHE B CE1 
3581 C  CE2 . PHE B 159 ? 0.2874 0.2527 0.2590 0.0019  0.0059  0.0081  383  PHE B CE2 
3582 C  CZ  . PHE B 159 ? 0.2739 0.2315 0.2404 0.0033  0.0084  0.0107  383  PHE B CZ  
3583 N  N   . THR B 160 ? 0.2584 0.2354 0.2414 -0.0036 0.0123  0.0103  384  THR B N   
3584 C  CA  . THR B 160 ? 0.2484 0.2279 0.2273 -0.0009 0.0103  0.0095  384  THR B CA  
3585 C  C   . THR B 160 ? 0.2431 0.2182 0.2145 0.0024  0.0086  0.0097  384  THR B C   
3586 O  O   . THR B 160 ? 0.2500 0.2189 0.2157 0.0041  0.0109  0.0118  384  THR B O   
3587 C  CB  . THR B 160 ? 0.2637 0.2437 0.2412 0.0000  0.0132  0.0110  384  THR B CB  
3588 O  OG1 . THR B 160 ? 0.2235 0.2077 0.2089 -0.0029 0.0150  0.0110  384  THR B OG1 
3589 C  CG2 . THR B 160 ? 0.2749 0.2576 0.2492 0.0024  0.0107  0.0096  384  THR B CG2 
3590 N  N   . PRO B 161 ? 0.2175 0.1953 0.1887 0.0036  0.0048  0.0076  385  PRO B N   
3591 C  CA  . PRO B 161 ? 0.2459 0.2201 0.2112 0.0069  0.0029  0.0074  385  PRO B CA  
3592 C  C   . PRO B 161 ? 0.2560 0.2289 0.2150 0.0101  0.0025  0.0079  385  PRO B C   
3593 O  O   . PRO B 161 ? 0.2451 0.2217 0.2052 0.0099  0.0021  0.0072  385  PRO B O   
3594 C  CB  . PRO B 161 ? 0.2638 0.2429 0.2329 0.0066  -0.0006 0.0047  385  PRO B CB  
3595 C  CG  . PRO B 161 ? 0.2323 0.2174 0.2061 0.0046  -0.0009 0.0038  385  PRO B CG  
3596 C  CD  . PRO B 161 ? 0.2308 0.2152 0.2070 0.0022  0.0023  0.0054  385  PRO B CD  
3597 N  N   . ILE B 162 ? 0.2511 0.2181 0.2030 0.0133  0.0023  0.0092  386  ILE B N   
3598 C  CA  . ILE B 162 ? 0.2591 0.2240 0.2035 0.0170  0.0012  0.0094  386  ILE B CA  
3599 C  C   . ILE B 162 ? 0.2771 0.2418 0.2188 0.0204  -0.0034 0.0078  386  ILE B C   
3600 O  O   . ILE B 162 ? 0.2693 0.2372 0.2105 0.0221  -0.0066 0.0058  386  ILE B O   
3601 C  CB  . ILE B 162 ? 0.2774 0.2348 0.2139 0.0186  0.0052  0.0128  386  ILE B CB  
3602 C  CG1 . ILE B 162 ? 0.2760 0.2346 0.2164 0.0153  0.0099  0.0142  386  ILE B CG1 
3603 C  CG2 . ILE B 162 ? 0.3018 0.2565 0.2290 0.0229  0.0035  0.0128  386  ILE B CG2 
3604 C  CD1 . ILE B 162 ? 0.2882 0.2520 0.2305 0.0150  0.0096  0.0127  386  ILE B CD1 
3605 N  N   . GLY B 163 ? 0.2750 0.2359 0.2157 0.0214  -0.0037 0.0085  387  GLY B N   
3606 C  CA  . GLY B 163 ? 0.2838 0.2447 0.2228 0.0249  -0.0080 0.0070  387  GLY B CA  
3607 C  C   . GLY B 163 ? 0.2961 0.2529 0.2354 0.0255  -0.0077 0.0077  387  GLY B C   
3608 O  O   . GLY B 163 ? 0.2546 0.2114 0.1986 0.0222  -0.0053 0.0079  387  GLY B O   
3609 N  N   . ILE B 164 ? 0.3053 0.2583 0.2395 0.0300  -0.0104 0.0078  388  ILE B N   
3610 C  CA  . ILE B 164 ? 0.3568 0.3053 0.2909 0.0313  -0.0106 0.0083  388  ILE B CA  
3611 C  C   . ILE B 164 ? 0.3428 0.2814 0.2667 0.0352  -0.0098 0.0116  388  ILE B C   
3612 O  O   . ILE B 164 ? 0.3399 0.2762 0.2563 0.0386  -0.0113 0.0125  388  ILE B O   
3613 C  CB  . ILE B 164 ? 0.3416 0.2954 0.2809 0.0333  -0.0148 0.0051  388  ILE B CB  
3614 C  CG1 . ILE B 164 ? 0.3515 0.3081 0.2883 0.0372  -0.0192 0.0037  388  ILE B CG1 
3615 C  CG2 . ILE B 164 ? 0.3306 0.2925 0.2794 0.0292  -0.0143 0.0025  388  ILE B CG2 
3616 C  CD1 . ILE B 164 ? 0.4156 0.3751 0.3560 0.0406  -0.0233 0.0013  388  ILE B CD1 
3617 N  N   . TYR B 165 ? 0.3501 0.2823 0.2734 0.0348  -0.0076 0.0134  389  TYR B N   
3618 C  CA  . TYR B 165 ? 0.3580 0.2795 0.2720 0.0382  -0.0063 0.0170  389  TYR B CA  
3619 C  C   . TYR B 165 ? 0.3830 0.3027 0.2971 0.0423  -0.0100 0.0157  389  TYR B C   
3620 O  O   . TYR B 165 ? 0.4020 0.3244 0.3234 0.0405  -0.0104 0.0135  389  TYR B O   
3621 C  CB  . TYR B 165 ? 0.3545 0.2698 0.2690 0.0343  -0.0006 0.0199  389  TYR B CB  
3622 C  CG  . TYR B 165 ? 0.4797 0.3834 0.3841 0.0367  0.0026  0.0246  389  TYR B CG  
3623 C  CD1 . TYR B 165 ? 0.5129 0.4083 0.4128 0.0403  0.0016  0.0261  389  TYR B CD1 
3624 C  CD2 . TYR B 165 ? 0.4948 0.3955 0.3941 0.0355  0.0071  0.0277  389  TYR B CD2 
3625 C  CE1 . TYR B 165 ? 0.5701 0.4538 0.4600 0.0426  0.0048  0.0309  389  TYR B CE1 
3626 C  CE2 . TYR B 165 ? 0.5301 0.4195 0.4194 0.0377  0.0107  0.0325  389  TYR B CE2 
3627 C  CZ  . TYR B 165 ? 0.5750 0.4557 0.4594 0.0412  0.0096  0.0342  389  TYR B CZ  
3628 O  OH  . TYR B 165 ? 0.6464 0.5151 0.5204 0.0435  0.0134  0.0393  389  TYR B OH  
3629 N  N   . ILE B 166 ? 0.4300 0.3453 0.3359 0.0480  -0.0132 0.0168  390  ILE B N   
3630 C  CA  . ILE B 166 ? 0.3785 0.2915 0.2839 0.0528  -0.0170 0.0159  390  ILE B CA  
3631 C  C   . ILE B 166 ? 0.4883 0.3883 0.3844 0.0555  -0.0147 0.0203  390  ILE B C   
3632 O  O   . ILE B 166 ? 0.4840 0.3773 0.3692 0.0586  -0.0143 0.0236  390  ILE B O   
3633 C  CB  . ILE B 166 ? 0.3965 0.3145 0.3003 0.0577  -0.0232 0.0136  390  ILE B CB  
3634 C  CG1 . ILE B 166 ? 0.4479 0.3784 0.3615 0.0547  -0.0251 0.0094  390  ILE B CG1 
3635 C  CG2 . ILE B 166 ? 0.4522 0.3678 0.3560 0.0631  -0.0272 0.0128  390  ILE B CG2 
3636 C  CD1 . ILE B 166 ? 0.4201 0.3575 0.3451 0.0521  -0.0251 0.0063  390  ILE B CD1 
3637 N  N   . GLU B 167 ? 0.5254 0.4210 0.4250 0.0544  -0.0130 0.0205  391  GLU B N   
3638 C  CA  . GLU B 167 ? 0.5762 0.4587 0.4678 0.0574  -0.0112 0.0245  391  GLU B CA  
3639 C  C   . GLU B 167 ? 0.6072 0.4868 0.4955 0.0644  -0.0163 0.0239  391  GLU B C   
3640 O  O   . GLU B 167 ? 0.5889 0.4572 0.4673 0.0686  -0.0159 0.0278  391  GLU B O   
3641 C  CB  . GLU B 167 ? 0.5514 0.4295 0.4485 0.0527  -0.0068 0.0250  391  GLU B CB  
3642 C  CG  . GLU B 167 ? 0.6318 0.5085 0.5296 0.0468  -0.0010 0.0273  391  GLU B CG  
3643 C  CD  . GLU B 167 ? 0.7296 0.6018 0.6335 0.0420  0.0027  0.0273  391  GLU B CD  
3644 O  OE1 . GLU B 167 ? 0.7533 0.6211 0.6587 0.0439  0.0013  0.0262  391  GLU B OE1 
3645 O  OE2 . GLU B 167 ? 0.7026 0.5760 0.6103 0.0365  0.0069  0.0281  391  GLU B OE2 
3646 N  N   . GLY B 168 ? 0.6279 0.5173 0.5243 0.0659  -0.0209 0.0193  392  GLY B N   
3647 C  CA  . GLY B 168 ? 0.6154 0.5036 0.5107 0.0726  -0.0261 0.0182  392  GLY B CA  
3648 C  C   . GLY B 168 ? 0.7588 0.6440 0.6596 0.0731  -0.0255 0.0169  392  GLY B C   
3649 O  O   . GLY B 168 ? 0.7622 0.6405 0.6588 0.0790  -0.0280 0.0180  392  GLY B O   
3650 N  N   . ASN B 169 ? 0.7281 0.6180 0.6379 0.0675  -0.0225 0.0144  393  ASN B N   
3651 C  CA  . ASN B 169 ? 0.7174 0.6034 0.6316 0.0674  -0.0213 0.0130  393  ASN B CA  
3652 C  C   . ASN B 169 ? 0.7083 0.6057 0.6339 0.0632  -0.0209 0.0082  393  ASN B C   
3653 O  O   . ASN B 169 ? 0.6304 0.5386 0.5605 0.0616  -0.0224 0.0059  393  ASN B O   
3654 C  CB  . ASN B 169 ? 0.7065 0.5797 0.6156 0.0646  -0.0163 0.0168  393  ASN B CB  
3655 C  CG  . ASN B 169 ? 0.7339 0.6093 0.6449 0.0573  -0.0118 0.0178  393  ASN B CG  
3656 O  OD1 . ASN B 169 ? 0.6573 0.5438 0.5747 0.0537  -0.0122 0.0149  393  ASN B OD1 
3657 N  ND2 . ASN B 169 ? 0.7402 0.6049 0.6459 0.0551  -0.0075 0.0219  393  ASN B ND2 
3658 N  N   . SER B 170 ? 0.7450 0.6390 0.6744 0.0613  -0.0187 0.0066  394  SER B N   
3659 C  CA  . SER B 170 ? 0.7689 0.6723 0.7076 0.0585  -0.0184 0.0019  394  SER B CA  
3660 C  C   . SER B 170 ? 0.6829 0.5944 0.6253 0.0522  -0.0165 0.0011  394  SER B C   
3661 O  O   . SER B 170 ? 0.6472 0.5688 0.5964 0.0506  -0.0171 -0.0024 394  SER B O   
3662 C  CB  . SER B 170 ? 0.8158 0.7121 0.7562 0.0576  -0.0163 0.0005  394  SER B CB  
3663 O  OG  . SER B 170 ? 0.9457 0.8503 0.8936 0.0564  -0.0164 -0.0042 394  SER B OG  
3664 N  N   . SER B 171 ? 0.6308 0.5380 0.5688 0.0488  -0.0140 0.0044  395  SER B N   
3665 C  CA  . SER B 171 ? 0.6183 0.5325 0.5597 0.0431  -0.0122 0.0038  395  SER B CA  
3666 C  C   . SER B 171 ? 0.5817 0.5052 0.5239 0.0440  -0.0146 0.0033  395  SER B C   
3667 O  O   . SER B 171 ? 0.5602 0.4893 0.5049 0.0397  -0.0132 0.0031  395  SER B O   
3668 C  CB  . SER B 171 ? 0.5911 0.4978 0.5286 0.0393  -0.0083 0.0075  395  SER B CB  
3669 O  OG  . SER B 171 ? 0.5242 0.4252 0.4535 0.0422  -0.0083 0.0115  395  SER B OG  
3670 N  N   . ASP B 172 ? 0.5683 0.4937 0.5092 0.0493  -0.0183 0.0028  396  ASP B N   
3671 C  CA  . ASP B 172 ? 0.5325 0.4652 0.4735 0.0502  -0.0208 0.0024  396  ASP B CA  
3672 C  C   . ASP B 172 ? 0.4555 0.3999 0.4052 0.0466  -0.0209 -0.0009 396  ASP B C   
3673 O  O   . ASP B 172 ? 0.4112 0.3595 0.3672 0.0455  -0.0203 -0.0036 396  ASP B O   
3674 C  CB  . ASP B 172 ? 0.4778 0.4106 0.4166 0.0568  -0.0256 0.0021  396  ASP B CB  
3675 C  CG  . ASP B 172 ? 0.6728 0.5945 0.6003 0.0607  -0.0260 0.0062  396  ASP B CG  
3676 O  OD1 . ASP B 172 ? 0.6197 0.5327 0.5419 0.0582  -0.0219 0.0094  396  ASP B OD1 
3677 O  OD2 . ASP B 172 ? 0.6188 0.5403 0.5427 0.0662  -0.0304 0.0063  396  ASP B OD2 
3678 N  N   . PHE B 173 ? 0.4647 0.4139 0.4141 0.0449  -0.0215 -0.0006 397  PHE B N   
3679 C  CA  . PHE B 173 ? 0.3413 0.3007 0.2979 0.0413  -0.0214 -0.0031 397  PHE B CA  
3680 C  C   . PHE B 173 ? 0.3579 0.3253 0.3223 0.0432  -0.0237 -0.0066 397  PHE B C   
3681 O  O   . PHE B 173 ? 0.3158 0.2855 0.2810 0.0474  -0.0273 -0.0075 397  PHE B O   
3682 C  CB  . PHE B 173 ? 0.3278 0.2893 0.2813 0.0410  -0.0226 -0.0021 397  PHE B CB  
3683 C  CG  . PHE B 173 ? 0.3564 0.3273 0.3166 0.0377  -0.0228 -0.0043 397  PHE B CG  
3684 C  CD1 . PHE B 173 ? 0.3630 0.3368 0.3274 0.0329  -0.0197 -0.0048 397  PHE B CD1 
3685 C  CD2 . PHE B 173 ? 0.3723 0.3487 0.3344 0.0394  -0.0262 -0.0058 397  PHE B CD2 
3686 C  CE1 . PHE B 173 ? 0.3404 0.3221 0.3103 0.0300  -0.0197 -0.0063 397  PHE B CE1 
3687 C  CE2 . PHE B 173 ? 0.3267 0.3110 0.2951 0.0361  -0.0261 -0.0076 397  PHE B CE2 
3688 C  CZ  . PHE B 173 ? 0.2883 0.2750 0.2603 0.0316  -0.0227 -0.0077 397  PHE B CZ  
3689 N  N   . ASN B 174 ? 0.2636 0.2355 0.2340 0.0401  -0.0215 -0.0086 398  ASN B N   
3690 C  CA  . ASN B 174 ? 0.2767 0.2572 0.2552 0.0410  -0.0225 -0.0118 398  ASN B CA  
3691 C  C   . ASN B 174 ? 0.2666 0.2541 0.2496 0.0361  -0.0204 -0.0127 398  ASN B C   
3692 O  O   . ASN B 174 ? 0.2551 0.2420 0.2386 0.0331  -0.0176 -0.0131 398  ASN B O   
3693 C  CB  . ASN B 174 ? 0.3034 0.2817 0.2837 0.0431  -0.0215 -0.0134 398  ASN B CB  
3694 C  CG  . ASN B 174 ? 0.3618 0.3490 0.3507 0.0450  -0.0222 -0.0166 398  ASN B CG  
3695 O  OD1 . ASN B 174 ? 0.2794 0.2750 0.2740 0.0431  -0.0224 -0.0177 398  ASN B OD1 
3696 N  ND2 . ASN B 174 ? 0.3690 0.3542 0.3593 0.0489  -0.0225 -0.0180 398  ASN B ND2 
3697 N  N   . GLN B 175 ? 0.2829 0.2767 0.2693 0.0355  -0.0221 -0.0133 399  GLN B N   
3698 C  CA  . GLN B 175 ? 0.2648 0.2639 0.2545 0.0309  -0.0202 -0.0136 399  GLN B CA  
3699 C  C   . GLN B 175 ? 0.2397 0.2446 0.2357 0.0296  -0.0180 -0.0157 399  GLN B C   
3700 O  O   . GLN B 175 ? 0.2470 0.2549 0.2445 0.0258  -0.0159 -0.0156 399  GLN B O   
3701 C  CB  . GLN B 175 ? 0.2557 0.2597 0.2478 0.0307  -0.0226 -0.0139 399  GLN B CB  
3702 C  CG  . GLN B 175 ? 0.2570 0.2682 0.2570 0.0331  -0.0251 -0.0165 399  GLN B CG  
3703 C  CD  . GLN B 175 ? 0.2616 0.2788 0.2663 0.0310  -0.0265 -0.0173 399  GLN B CD  
3704 O  OE1 . GLN B 175 ? 0.2347 0.2530 0.2395 0.0270  -0.0242 -0.0166 399  GLN B OE1 
3705 N  NE2 . GLN B 175 ? 0.2452 0.2660 0.2538 0.0337  -0.0304 -0.0191 399  GLN B NE2 
3706 N  N   . TRP B 176 ? 0.2462 0.2524 0.2455 0.0328  -0.0183 -0.0175 400  TRP B N   
3707 C  CA  . TRP B 176 ? 0.2680 0.2795 0.2727 0.0320  -0.0157 -0.0195 400  TRP B CA  
3708 C  C   . TRP B 176 ? 0.3063 0.3127 0.3076 0.0326  -0.0135 -0.0201 400  TRP B C   
3709 O  O   . TRP B 176 ? 0.3492 0.3591 0.3537 0.0324  -0.0111 -0.0220 400  TRP B O   
3710 C  CB  . TRP B 176 ? 0.2985 0.3173 0.3116 0.0350  -0.0171 -0.0217 400  TRP B CB  
3711 C  CG  . TRP B 176 ? 0.2490 0.2736 0.2669 0.0339  -0.0193 -0.0217 400  TRP B CG  
3712 C  CD1 . TRP B 176 ? 0.2435 0.2704 0.2646 0.0369  -0.0235 -0.0226 400  TRP B CD1 
3713 C  CD2 . TRP B 176 ? 0.2694 0.2978 0.2893 0.0295  -0.0178 -0.0211 400  TRP B CD2 
3714 N  NE1 . TRP B 176 ? 0.2705 0.3025 0.2958 0.0345  -0.0246 -0.0229 400  TRP B NE1 
3715 C  CE2 . TRP B 176 ? 0.2434 0.2761 0.2681 0.0299  -0.0210 -0.0218 400  TRP B CE2 
3716 C  CE3 . TRP B 176 ? 0.2267 0.2549 0.2447 0.0254  -0.0143 -0.0202 400  TRP B CE3 
3717 C  CZ2 . TRP B 176 ? 0.2688 0.3054 0.2966 0.0262  -0.0205 -0.0216 400  TRP B CZ2 
3718 C  CZ3 . TRP B 176 ? 0.2643 0.2964 0.2851 0.0221  -0.0138 -0.0196 400  TRP B CZ3 
3719 C  CH2 . TRP B 176 ? 0.2846 0.3205 0.3104 0.0224  -0.0167 -0.0203 400  TRP B CH2 
3720 N  N   . GLN B 177 ? 0.2493 0.2471 0.2441 0.0331  -0.0141 -0.0187 401  GLN B N   
3721 C  CA  . GLN B 177 ? 0.2651 0.2571 0.2565 0.0331  -0.0122 -0.0195 401  GLN B CA  
3722 C  C   . GLN B 177 ? 0.2700 0.2599 0.2580 0.0283  -0.0104 -0.0185 401  GLN B C   
3723 O  O   . GLN B 177 ? 0.2696 0.2555 0.2541 0.0265  -0.0110 -0.0163 401  GLN B O   
3724 C  CB  . GLN B 177 ? 0.3069 0.2902 0.2939 0.0363  -0.0136 -0.0185 401  GLN B CB  
3725 C  CG  . GLN B 177 ? 0.3501 0.3272 0.3346 0.0367  -0.0120 -0.0199 401  GLN B CG  
3726 C  CD  . GLN B 177 ? 0.4271 0.3952 0.4077 0.0402  -0.0133 -0.0189 401  GLN B CD  
3727 O  OE1 . GLN B 177 ? 0.4965 0.4622 0.4749 0.0421  -0.0153 -0.0165 401  GLN B OE1 
3728 N  NE2 . GLN B 177 ? 0.4820 0.4444 0.4612 0.0414  -0.0121 -0.0205 401  GLN B NE2 
3729 N  N   . LEU B 178 ? 0.2603 0.2530 0.2493 0.0265  -0.0083 -0.0203 402  LEU B N   
3730 C  CA  . LEU B 178 ? 0.2675 0.2584 0.2534 0.0224  -0.0073 -0.0197 402  LEU B CA  
3731 C  C   . LEU B 178 ? 0.2832 0.2651 0.2647 0.0220  -0.0075 -0.0196 402  LEU B C   
3732 O  O   . LEU B 178 ? 0.2570 0.2344 0.2375 0.0249  -0.0076 -0.0209 402  LEU B O   
3733 C  CB  . LEU B 178 ? 0.2703 0.2651 0.2567 0.0213  -0.0052 -0.0217 402  LEU B CB  
3734 C  CG  . LEU B 178 ? 0.2937 0.2970 0.2846 0.0205  -0.0042 -0.0215 402  LEU B CG  
3735 C  CD1 . LEU B 178 ? 0.2549 0.2609 0.2451 0.0200  -0.0015 -0.0232 402  LEU B CD1 
3736 C  CD2 . LEU B 178 ? 0.2691 0.2737 0.2598 0.0174  -0.0051 -0.0191 402  LEU B CD2 
3737 N  N   . PRO B 179 ? 0.2639 0.2432 0.2434 0.0186  -0.0076 -0.0180 403  PRO B N   
3738 C  CA  . PRO B 179 ? 0.2859 0.2573 0.2625 0.0174  -0.0075 -0.0182 403  PRO B CA  
3739 C  C   . PRO B 179 ? 0.2990 0.2696 0.2747 0.0167  -0.0069 -0.0214 403  PRO B C   
3740 O  O   . PRO B 179 ? 0.2726 0.2488 0.2489 0.0165  -0.0062 -0.0229 403  PRO B O   
3741 C  CB  . PRO B 179 ? 0.2682 0.2392 0.2447 0.0137  -0.0075 -0.0159 403  PRO B CB  
3742 C  CG  . PRO B 179 ? 0.2867 0.2657 0.2652 0.0123  -0.0075 -0.0156 403  PRO B CG  
3743 C  CD  . PRO B 179 ? 0.2477 0.2313 0.2281 0.0155  -0.0076 -0.0162 403  PRO B CD  
3744 N  N   . ARG B 180 ? 0.2430 0.2059 0.2167 0.0165  -0.0070 -0.0225 404  ARG B N   
3745 C  CA  . ARG B 180 ? 0.2704 0.2313 0.2424 0.0149  -0.0071 -0.0257 404  ARG B CA  
3746 C  C   . ARG B 180 ? 0.2871 0.2490 0.2597 0.0104  -0.0078 -0.0248 404  ARG B C   
3747 O  O   . ARG B 180 ? 0.2996 0.2563 0.2729 0.0082  -0.0082 -0.0238 404  ARG B O   
3748 C  CB  . ARG B 180 ? 0.3023 0.2543 0.2726 0.0163  -0.0073 -0.0276 404  ARG B CB  
3749 C  CG  . ARG B 180 ? 0.3820 0.3333 0.3519 0.0211  -0.0066 -0.0295 404  ARG B CG  
3750 C  CD  . ARG B 180 ? 0.4137 0.3549 0.3817 0.0224  -0.0069 -0.0312 404  ARG B CD  
3751 N  NE  . ARG B 180 ? 0.3923 0.3316 0.3580 0.0226  -0.0069 -0.0357 404  ARG B NE  
3752 C  CZ  . ARG B 180 ? 0.4528 0.3940 0.4175 0.0264  -0.0058 -0.0385 404  ARG B CZ  
3753 N  NH1 . ARG B 180 ? 0.5103 0.4567 0.4774 0.0300  -0.0048 -0.0374 404  ARG B NH1 
3754 N  NH2 . ARG B 180 ? 0.4155 0.3533 0.3770 0.0267  -0.0057 -0.0427 404  ARG B NH2 
3755 N  N   . TYR B 181 ? 0.2471 0.2156 0.2197 0.0091  -0.0079 -0.0252 405  TYR B N   
3756 C  CA  . TYR B 181 ? 0.2538 0.2241 0.2275 0.0052  -0.0088 -0.0241 405  TYR B CA  
3757 C  C   . TYR B 181 ? 0.2588 0.2239 0.2320 0.0029  -0.0103 -0.0265 405  TYR B C   
3758 O  O   . TYR B 181 ? 0.2673 0.2323 0.2431 -0.0003 -0.0111 -0.0254 405  TYR B O   
3759 C  CB  . TYR B 181 ? 0.2307 0.2081 0.2037 0.0048  -0.0088 -0.0242 405  TYR B CB  
3760 C  CG  . TYR B 181 ? 0.2368 0.2196 0.2117 0.0060  -0.0076 -0.0217 405  TYR B CG  
3761 C  CD1 . TYR B 181 ? 0.2535 0.2387 0.2308 0.0043  -0.0079 -0.0189 405  TYR B CD1 
3762 C  CD2 . TYR B 181 ? 0.2654 0.2510 0.2404 0.0090  -0.0063 -0.0225 405  TYR B CD2 
3763 C  CE1 . TYR B 181 ? 0.2592 0.2490 0.2384 0.0055  -0.0072 -0.0170 405  TYR B CE1 
3764 C  CE2 . TYR B 181 ? 0.2657 0.2564 0.2435 0.0099  -0.0056 -0.0206 405  TYR B CE2 
3765 C  CZ  . TYR B 181 ? 0.2518 0.2443 0.2315 0.0081  -0.0063 -0.0180 405  TYR B CZ  
3766 O  OH  . TYR B 181 ? 0.2311 0.2284 0.2137 0.0090  -0.0060 -0.0166 405  TYR B OH  
3767 N  N   . GLY B 182 ? 0.3113 0.2721 0.2818 0.0044  -0.0106 -0.0299 406  GLY B N   
3768 C  CA  . GLY B 182 ? 0.2626 0.2178 0.2329 0.0022  -0.0123 -0.0327 406  GLY B CA  
3769 C  C   . GLY B 182 ? 0.2632 0.2099 0.2347 0.0025  -0.0119 -0.0329 406  GLY B C   
3770 O  O   . GLY B 182 ? 0.2761 0.2171 0.2474 0.0011  -0.0133 -0.0360 406  GLY B O   
3771 N  N   . GLY B 183 ? 0.2598 0.2050 0.2323 0.0043  -0.0103 -0.0297 407  GLY B N   
3772 C  CA  . GLY B 183 ? 0.2675 0.2037 0.2402 0.0051  -0.0096 -0.0293 407  GLY B CA  
3773 C  C   . GLY B 183 ? 0.3022 0.2343 0.2718 0.0090  -0.0095 -0.0323 407  GLY B C   
3774 O  O   . GLY B 183 ? 0.3260 0.2623 0.2933 0.0112  -0.0096 -0.0348 407  GLY B O   
3775 N  N   . HIS B 184 ? 0.3070 0.2300 0.2764 0.0101  -0.0091 -0.0320 408  HIS B N   
3776 C  CA  . HIS B 184 ? 0.2879 0.2064 0.2548 0.0147  -0.0087 -0.0341 408  HIS B CA  
3777 C  C   . HIS B 184 ? 0.3278 0.2442 0.2924 0.0153  -0.0096 -0.0395 408  HIS B C   
3778 O  O   . HIS B 184 ? 0.3096 0.2237 0.2719 0.0196  -0.0091 -0.0418 408  HIS B O   
3779 C  CB  . HIS B 184 ? 0.2977 0.2061 0.2646 0.0159  -0.0080 -0.0318 408  HIS B CB  
3780 C  CG  . HIS B 184 ? 0.3628 0.2620 0.3309 0.0124  -0.0084 -0.0333 408  HIS B CG  
3781 N  ND1 . HIS B 184 ? 0.3804 0.2803 0.3518 0.0069  -0.0088 -0.0327 408  HIS B ND1 
3782 C  CD2 . HIS B 184 ? 0.3148 0.2036 0.2819 0.0136  -0.0084 -0.0354 408  HIS B CD2 
3783 C  CE1 . HIS B 184 ? 0.3244 0.2152 0.2974 0.0047  -0.0091 -0.0345 408  HIS B CE1 
3784 N  NE2 . HIS B 184 ? 0.4071 0.2905 0.3771 0.0086  -0.0089 -0.0362 408  HIS B NE2 
3785 N  N   . LEU B 185 ? 0.3012 0.2183 0.2659 0.0114  -0.0112 -0.0420 409  LEU B N   
3786 C  CA  . LEU B 185 ? 0.3183 0.2325 0.2796 0.0121  -0.0125 -0.0475 409  LEU B CA  
3787 C  C   . LEU B 185 ? 0.3428 0.2656 0.3010 0.0124  -0.0129 -0.0494 409  LEU B C   
3788 O  O   . LEU B 185 ? 0.3034 0.2244 0.2576 0.0126  -0.0142 -0.0540 409  LEU B O   
3789 C  CB  . LEU B 185 ? 0.3082 0.2154 0.2715 0.0078  -0.0147 -0.0499 409  LEU B CB  
3790 C  CG  . LEU B 185 ? 0.3149 0.2119 0.2810 0.0071  -0.0139 -0.0483 409  LEU B CG  
3791 C  CD1 . LEU B 185 ? 0.3216 0.2125 0.2908 0.0024  -0.0161 -0.0512 409  LEU B CD1 
3792 C  CD2 . LEU B 185 ? 0.3228 0.2130 0.2857 0.0122  -0.0128 -0.0498 409  LEU B CD2 
3793 N  N   . ALA B 186 ? 0.3089 0.2404 0.2682 0.0127  -0.0117 -0.0459 410  ALA B N   
3794 C  CA  . ALA B 186 ? 0.3100 0.2492 0.2663 0.0129  -0.0115 -0.0469 410  ALA B CA  
3795 C  C   . ALA B 186 ? 0.3044 0.2506 0.2616 0.0159  -0.0089 -0.0442 410  ALA B C   
3796 O  O   . ALA B 186 ? 0.2848 0.2315 0.2457 0.0166  -0.0081 -0.0408 410  ALA B O   
3797 C  CB  . ALA B 186 ? 0.2939 0.2372 0.2517 0.0085  -0.0135 -0.0456 410  ALA B CB  
3798 N  N   . ASN B 187 ? 0.3061 0.2574 0.2599 0.0177  -0.0075 -0.0458 411  ASN B N   
3799 C  CA  . ASN B 187 ? 0.2957 0.2543 0.2514 0.0202  -0.0049 -0.0436 411  ASN B CA  
3800 C  C   . ASN B 187 ? 0.2777 0.2439 0.2341 0.0177  -0.0047 -0.0409 411  ASN B C   
3801 O  O   . ASN B 187 ? 0.2945 0.2610 0.2476 0.0153  -0.0061 -0.0417 411  ASN B O   
3802 C  CB  . ASN B 187 ? 0.3260 0.2855 0.2783 0.0242  -0.0024 -0.0469 411  ASN B CB  
3803 C  CG  . ASN B 187 ? 0.3594 0.3113 0.3110 0.0273  -0.0024 -0.0500 411  ASN B CG  
3804 O  OD1 . ASN B 187 ? 0.3743 0.3221 0.3294 0.0278  -0.0033 -0.0485 411  ASN B OD1 
3805 N  ND2 . ASN B 187 ? 0.3910 0.3402 0.3372 0.0295  -0.0015 -0.0543 411  ASN B ND2 
3806 N  N   . ASN B 188 ? 0.2595 0.2314 0.2203 0.0184  -0.0033 -0.0377 412  ASN B N   
3807 C  CA  . ASN B 188 ? 0.2587 0.2374 0.2208 0.0161  -0.0030 -0.0349 412  ASN B CA  
3808 C  C   . ASN B 188 ? 0.2815 0.2638 0.2392 0.0167  -0.0011 -0.0362 412  ASN B C   
3809 O  O   . ASN B 188 ? 0.3166 0.2992 0.2723 0.0197  0.0013  -0.0385 412  ASN B O   
3810 C  CB  . ASN B 188 ? 0.2918 0.2754 0.2595 0.0171  -0.0019 -0.0319 412  ASN B CB  
3811 C  CG  . ASN B 188 ? 0.2865 0.2665 0.2571 0.0165  -0.0038 -0.0298 412  ASN B CG  
3812 O  OD1 . ASN B 188 ? 0.2860 0.2609 0.2554 0.0143  -0.0054 -0.0297 412  ASN B OD1 
3813 N  ND2 . ASN B 188 ? 0.2608 0.2436 0.2353 0.0185  -0.0034 -0.0281 412  ASN B ND2 
3814 N  N   . ASN B 189 ? 0.2970 0.2819 0.2528 0.0140  -0.0020 -0.0347 413  ASN B N   
3815 C  CA  . ASN B 189 ? 0.3521 0.3406 0.3033 0.0146  0.0002  -0.0350 413  ASN B CA  
3816 C  C   . ASN B 189 ? 0.2887 0.2824 0.2422 0.0123  0.0002  -0.0312 413  ASN B C   
3817 O  O   . ASN B 189 ? 0.3054 0.2997 0.2634 0.0102  -0.0017 -0.0290 413  ASN B O   
3818 C  CB  . ASN B 189 ? 0.4373 0.4214 0.3803 0.0147  -0.0013 -0.0383 413  ASN B CB  
3819 C  CG  . ASN B 189 ? 0.4721 0.4536 0.4147 0.0115  -0.0057 -0.0383 413  ASN B CG  
3820 O  OD1 . ASN B 189 ? 0.4650 0.4491 0.4120 0.0090  -0.0070 -0.0352 413  ASN B OD1 
3821 N  ND2 . ASN B 189 ? 0.5142 0.4904 0.4516 0.0116  -0.0082 -0.0421 413  ASN B ND2 
3822 N  N   . HIS B 190 ? 0.3541 0.3512 0.3042 0.0128  0.0028  -0.0305 414  HIS B N   
3823 C  CA  . HIS B 190 ? 0.3497 0.3511 0.3012 0.0108  0.0033  -0.0270 414  HIS B CA  
3824 C  C   . HIS B 190 ? 0.2845 0.2902 0.2446 0.0102  0.0041  -0.0243 414  HIS B C   
3825 O  O   . HIS B 190 ? 0.2892 0.2971 0.2517 0.0081  0.0032  -0.0216 414  HIS B O   
3826 C  CB  . HIS B 190 ? 0.3592 0.3587 0.3082 0.0083  -0.0005 -0.0262 414  HIS B CB  
3827 C  CG  . HIS B 190 ? 0.4401 0.4363 0.3802 0.0089  -0.0019 -0.0286 414  HIS B CG  
3828 N  ND1 . HIS B 190 ? 0.4354 0.4267 0.3731 0.0087  -0.0053 -0.0319 414  HIS B ND1 
3829 C  CD2 . HIS B 190 ? 0.4222 0.4188 0.3549 0.0099  -0.0004 -0.0283 414  HIS B CD2 
3830 C  CE1 . HIS B 190 ? 0.4598 0.4488 0.3889 0.0096  -0.0064 -0.0339 414  HIS B CE1 
3831 N  NE2 . HIS B 190 ? 0.5402 0.5322 0.4655 0.0105  -0.0034 -0.0317 414  HIS B NE2 
3832 N  N   . LEU B 191 ? 0.2416 0.2483 0.2063 0.0122  0.0055  -0.0253 415  LEU B N   
3833 C  CA  . LEU B 191 ? 0.2493 0.2599 0.2218 0.0119  0.0056  -0.0233 415  LEU B CA  
3834 C  C   . LEU B 191 ? 0.2584 0.2748 0.2340 0.0113  0.0085  -0.0213 415  LEU B C   
3835 O  O   . LEU B 191 ? 0.3035 0.3217 0.2769 0.0123  0.0120  -0.0218 415  LEU B O   
3836 C  CB  . LEU B 191 ? 0.2655 0.2758 0.2420 0.0148  0.0059  -0.0250 415  LEU B CB  
3837 C  CG  . LEU B 191 ? 0.2391 0.2432 0.2142 0.0155  0.0031  -0.0264 415  LEU B CG  
3838 C  CD1 . LEU B 191 ? 0.2529 0.2564 0.2307 0.0191  0.0041  -0.0283 415  LEU B CD1 
3839 C  CD2 . LEU B 191 ? 0.2433 0.2465 0.2212 0.0136  0.0004  -0.0240 415  LEU B CD2 
3840 N  N   . ALA B 192 ? 0.2133 0.2324 0.1940 0.0095  0.0073  -0.0189 416  ALA B N   
3841 C  CA  . ALA B 192 ? 0.2709 0.2956 0.2571 0.0090  0.0100  -0.0174 416  ALA B CA  
3842 C  C   . ALA B 192 ? 0.2428 0.2709 0.2347 0.0116  0.0120  -0.0192 416  ALA B C   
3843 O  O   . ALA B 192 ? 0.2616 0.2878 0.2549 0.0135  0.0100  -0.0208 416  ALA B O   
3844 C  CB  . ALA B 192 ? 0.2149 0.2412 0.2058 0.0070  0.0077  -0.0152 416  ALA B CB  
3845 N  N   . PRO B 193 ? 0.2124 0.2451 0.2076 0.0118  0.0161  -0.0189 417  PRO B N   
3846 C  CA  . PRO B 193 ? 0.2360 0.2724 0.2371 0.0147  0.0184  -0.0210 417  PRO B CA  
3847 C  C   . PRO B 193 ? 0.2501 0.2904 0.2609 0.0151  0.0160  -0.0211 417  PRO B C   
3848 O  O   . PRO B 193 ? 0.2088 0.2502 0.2226 0.0129  0.0138  -0.0194 417  PRO B O   
3849 C  CB  . PRO B 193 ? 0.2287 0.2692 0.2309 0.0142  0.0240  -0.0203 417  PRO B CB  
3850 C  CG  . PRO B 193 ? 0.2515 0.2921 0.2528 0.0108  0.0238  -0.0172 417  PRO B CG  
3851 C  CD  . PRO B 193 ? 0.2864 0.3210 0.2801 0.0098  0.0194  -0.0167 417  PRO B CD  
3852 N  N   . ALA B 194 ? 0.2154 0.2575 0.2307 0.0184  0.0162  -0.0234 418  ALA B N   
3853 C  CA  . ALA B 194 ? 0.2101 0.2568 0.2351 0.0195  0.0138  -0.0239 418  ALA B CA  
3854 C  C   . ALA B 194 ? 0.2374 0.2914 0.2712 0.0175  0.0165  -0.0229 418  ALA B C   
3855 O  O   . ALA B 194 ? 0.2063 0.2624 0.2396 0.0163  0.0213  -0.0223 418  ALA B O   
3856 C  CB  . ALA B 194 ? 0.2413 0.2888 0.2697 0.0238  0.0137  -0.0266 418  ALA B CB  
3857 N  N   . VAL B 195 ? 0.2561 0.3136 0.2977 0.0170  0.0133  -0.0229 419  VAL B N   
3858 C  CA  . VAL B 195 ? 0.2814 0.3457 0.3329 0.0149  0.0151  -0.0224 419  VAL B CA  
3859 C  C   . VAL B 195 ? 0.2471 0.3176 0.3100 0.0174  0.0130  -0.0248 419  VAL B C   
3860 O  O   . VAL B 195 ? 0.2766 0.3449 0.3385 0.0203  0.0085  -0.0260 419  VAL B O   
3861 C  CB  . VAL B 195 ? 0.2527 0.3155 0.3033 0.0113  0.0128  -0.0203 419  VAL B CB  
3862 C  CG1 . VAL B 195 ? 0.2528 0.3103 0.2932 0.0090  0.0149  -0.0179 419  VAL B CG1 
3863 C  CG2 . VAL B 195 ? 0.1887 0.2484 0.2376 0.0126  0.0066  -0.0208 419  VAL B CG2 
3864 N  N   . SER B 196 ? 0.2482 0.3263 0.3221 0.0164  0.0164  -0.0253 420  SER B N   
3865 C  CA  . SER B 196 ? 0.2986 0.3838 0.3851 0.0188  0.0141  -0.0279 420  SER B CA  
3866 C  C   . SER B 196 ? 0.2705 0.3636 0.3697 0.0156  0.0171  -0.0277 420  SER B C   
3867 O  O   . SER B 196 ? 0.2747 0.3678 0.3724 0.0125  0.0226  -0.0257 420  SER B O   
3868 C  CB  . SER B 196 ? 0.3064 0.3935 0.3948 0.0232  0.0161  -0.0301 420  SER B CB  
3869 O  OG  . SER B 196 ? 0.3514 0.4414 0.4410 0.0226  0.0234  -0.0299 420  SER B OG  
3870 N  N   . PRO B 197 ? 0.2223 0.3216 0.3338 0.0161  0.0133  -0.0298 421  PRO B N   
3871 C  CA  . PRO B 197 ? 0.3230 0.4305 0.4487 0.0130  0.0163  -0.0301 421  PRO B CA  
3872 C  C   . PRO B 197 ? 0.2660 0.3803 0.4001 0.0146  0.0227  -0.0312 421  PRO B C   
3873 O  O   . PRO B 197 ? 0.2681 0.3851 0.4055 0.0190  0.0213  -0.0337 421  PRO B O   
3874 C  CB  . PRO B 197 ? 0.2473 0.3591 0.3830 0.0139  0.0091  -0.0327 421  PRO B CB  
3875 C  CG  . PRO B 197 ? 0.2734 0.3824 0.4038 0.0193  0.0043  -0.0344 421  PRO B CG  
3876 C  CD  . PRO B 197 ? 0.2331 0.3325 0.3465 0.0199  0.0062  -0.0321 421  PRO B CD  
3877 N  N   . LEU B 198 ? 0.2490 0.3655 0.3857 0.0112  0.0300  -0.0293 422  LEU B N   
3878 C  CA  . LEU B 198 ? 0.2660 0.3888 0.4101 0.0126  0.0372  -0.0300 422  LEU B CA  
3879 C  C   . LEU B 198 ? 0.2644 0.3982 0.4289 0.0107  0.0392  -0.0316 422  LEU B C   
3880 O  O   . LEU B 198 ? 0.2486 0.3895 0.4225 0.0128  0.0439  -0.0332 422  LEU B O   
3881 C  CB  . LEU B 198 ? 0.2834 0.4015 0.4167 0.0106  0.0451  -0.0268 422  LEU B CB  
3882 C  CG  . LEU B 198 ? 0.3512 0.4586 0.4651 0.0120  0.0428  -0.0255 422  LEU B CG  
3883 C  CD1 . LEU B 198 ? 0.4033 0.5058 0.5061 0.0098  0.0494  -0.0222 422  LEU B CD1 
3884 C  CD2 . LEU B 198 ? 0.3026 0.4089 0.4129 0.0174  0.0410  -0.0283 422  LEU B CD2 
3885 N  N   . PHE B 199 ? 0.2069 0.3424 0.3788 0.0068  0.0358  -0.0313 423  PHE B N   
3886 C  CA  . PHE B 199 ? 0.2726 0.4181 0.4644 0.0040  0.0380  -0.0326 423  PHE B CA  
3887 C  C   . PHE B 199 ? 0.2260 0.3786 0.4312 0.0067  0.0301  -0.0370 423  PHE B C   
3888 O  O   . PHE B 199 ? 0.2256 0.3737 0.4244 0.0084  0.0217  -0.0382 423  PHE B O   
3889 C  CB  . PHE B 199 ? 0.2913 0.4341 0.4839 -0.0020 0.0387  -0.0301 423  PHE B CB  
3890 C  CG  . PHE B 199 ? 0.2873 0.4389 0.4987 -0.0060 0.0439  -0.0303 423  PHE B CG  
3891 C  CD1 . PHE B 199 ? 0.3415 0.4971 0.5571 -0.0067 0.0540  -0.0286 423  PHE B CD1 
3892 C  CD2 . PHE B 199 ? 0.3104 0.4662 0.5353 -0.0091 0.0388  -0.0322 423  PHE B CD2 
3893 C  CE1 . PHE B 199 ? 0.3629 0.5267 0.5968 -0.0107 0.0594  -0.0286 423  PHE B CE1 
3894 C  CE2 . PHE B 199 ? 0.2750 0.4391 0.5187 -0.0132 0.0437  -0.0326 423  PHE B CE2 
3895 C  CZ  . PHE B 199 ? 0.3435 0.5117 0.5920 -0.0141 0.0542  -0.0306 423  PHE B CZ  
3896 N  N   . PRO B 200 ? 0.2397 0.4034 0.4633 0.0074  0.0325  -0.0396 424  PRO B N   
3897 C  CA  . PRO B 200 ? 0.2527 0.4236 0.4891 0.0108  0.0245  -0.0441 424  PRO B CA  
3898 C  C   . PRO B 200 ? 0.2630 0.4326 0.5020 0.0084  0.0159  -0.0454 424  PRO B C   
3899 O  O   . PRO B 200 ? 0.2548 0.4241 0.4980 0.0028  0.0177  -0.0440 424  PRO B O   
3900 C  CB  . PRO B 200 ? 0.2435 0.4274 0.5017 0.0102  0.0301  -0.0461 424  PRO B CB  
3901 C  CG  . PRO B 200 ? 0.2500 0.4321 0.5019 0.0094  0.0414  -0.0430 424  PRO B CG  
3902 C  CD  . PRO B 200 ? 0.2539 0.4243 0.4871 0.0058  0.0430  -0.0386 424  PRO B CD  
3903 N  N   . GLY B 201 ? 0.2427 0.4106 0.4783 0.0128  0.0066  -0.0480 425  GLY B N   
3904 C  CA  . GLY B 201 ? 0.2374 0.4038 0.4741 0.0117  -0.0024 -0.0498 425  GLY B CA  
3905 C  C   . GLY B 201 ? 0.2336 0.3881 0.4520 0.0096  -0.0044 -0.0468 425  GLY B C   
3906 O  O   . GLY B 201 ? 0.2480 0.4006 0.4665 0.0083  -0.0111 -0.0482 425  GLY B O   
3907 N  N   . GLU B 202 ? 0.1900 0.3367 0.3929 0.0093  0.0011  -0.0431 426  GLU B N   
3908 C  CA  . GLU B 202 ? 0.2325 0.3685 0.4190 0.0073  -0.0003 -0.0402 426  GLU B CA  
3909 C  C   . GLU B 202 ? 0.2425 0.3706 0.4127 0.0120  -0.0043 -0.0397 426  GLU B C   
3910 O  O   . GLU B 202 ? 0.1879 0.3167 0.3562 0.0161  -0.0029 -0.0402 426  GLU B O   
3911 C  CB  . GLU B 202 ? 0.2502 0.3826 0.4309 0.0030  0.0084  -0.0361 426  GLU B CB  
3912 C  CG  . GLU B 202 ? 0.2170 0.3548 0.4118 -0.0025 0.0124  -0.0357 426  GLU B CG  
3913 C  CD  . GLU B 202 ? 0.2402 0.3720 0.4264 -0.0067 0.0198  -0.0311 426  GLU B CD  
3914 O  OE1 . GLU B 202 ? 0.2782 0.4017 0.4473 -0.0055 0.0209  -0.0285 426  GLU B OE1 
3915 O  OE2 . GLU B 202 ? 0.2421 0.3775 0.4389 -0.0112 0.0244  -0.0301 426  GLU B OE2 
3916 N  N   . GLN B 203 ? 0.2550 0.3754 0.4140 0.0114  -0.0091 -0.0387 427  GLN B N   
3917 C  CA  . GLN B 203 ? 0.1794 0.2911 0.3222 0.0150  -0.0121 -0.0375 427  GLN B CA  
3918 C  C   . GLN B 203 ? 0.1997 0.3027 0.3293 0.0118  -0.0107 -0.0343 427  GLN B C   
3919 O  O   . GLN B 203 ? 0.1772 0.2805 0.3101 0.0076  -0.0101 -0.0336 427  GLN B O   
3920 C  CB  . GLN B 203 ? 0.1825 0.2937 0.3250 0.0191  -0.0209 -0.0402 427  GLN B CB  
3921 C  CG  . GLN B 203 ? 0.1998 0.3190 0.3542 0.0234  -0.0233 -0.0435 427  GLN B CG  
3922 C  CD  . GLN B 203 ? 0.2391 0.3565 0.3907 0.0282  -0.0322 -0.0457 427  GLN B CD  
3923 O  OE1 . GLN B 203 ? 0.2420 0.3632 0.3986 0.0331  -0.0348 -0.0478 427  GLN B OE1 
3924 N  NE2 . GLN B 203 ? 0.2183 0.3297 0.3613 0.0273  -0.0369 -0.0453 427  GLN B NE2 
3925 N  N   . ILE B 204 ? 0.1806 0.2760 0.2959 0.0137  -0.0104 -0.0324 428  ILE B N   
3926 C  CA  . ILE B 204 ? 0.1790 0.2664 0.2822 0.0112  -0.0099 -0.0296 428  ILE B CA  
3927 C  C   . ILE B 204 ? 0.1962 0.2809 0.2974 0.0112  -0.0164 -0.0305 428  ILE B C   
3928 O  O   . ILE B 204 ? 0.1806 0.2659 0.2826 0.0148  -0.0220 -0.0327 428  ILE B O   
3929 C  CB  . ILE B 204 ? 0.2241 0.3044 0.3137 0.0133  -0.0084 -0.0277 428  ILE B CB  
3930 C  CG1 . ILE B 204 ? 0.2270 0.3090 0.3168 0.0127  -0.0015 -0.0267 428  ILE B CG1 
3931 C  CG2 . ILE B 204 ? 0.1800 0.2526 0.2579 0.0113  -0.0092 -0.0253 428  ILE B CG2 
3932 C  CD1 . ILE B 204 ? 0.1842 0.2598 0.2621 0.0150  -0.0002 -0.0257 428  ILE B CD1 
3933 N  N   . LEU B 205 ? 0.1800 0.2618 0.2787 0.0074  -0.0156 -0.0290 429  LEU B N   
3934 C  CA  . LEU B 205 ? 0.1781 0.2559 0.2725 0.0073  -0.0209 -0.0296 429  LEU B CA  
3935 C  C   . LEU B 205 ? 0.1931 0.2624 0.2724 0.0080  -0.0206 -0.0270 429  LEU B C   
3936 O  O   . LEU B 205 ? 0.2044 0.2707 0.2788 0.0056  -0.0161 -0.0243 429  LEU B O   
3937 C  CB  . LEU B 205 ? 0.2169 0.2963 0.3181 0.0029  -0.0201 -0.0297 429  LEU B CB  
3938 C  CG  . LEU B 205 ? 0.2399 0.3145 0.3360 0.0025  -0.0251 -0.0305 429  LEU B CG  
3939 C  CD1 . LEU B 205 ? 0.2530 0.3300 0.3524 0.0061  -0.0319 -0.0341 429  LEU B CD1 
3940 C  CD2 . LEU B 205 ? 0.2733 0.3487 0.3761 -0.0020 -0.0237 -0.0304 429  LEU B CD2 
3941 N  N   . PHE B 206 ? 0.1811 0.2462 0.2531 0.0114  -0.0252 -0.0276 430  PHE B N   
3942 C  CA  . PHE B 206 ? 0.2266 0.2838 0.2854 0.0121  -0.0248 -0.0252 430  PHE B CA  
3943 C  C   . PHE B 206 ? 0.2121 0.2653 0.2660 0.0114  -0.0279 -0.0252 430  PHE B C   
3944 O  O   . PHE B 206 ? 0.2469 0.3022 0.3056 0.0117  -0.0320 -0.0276 430  PHE B O   
3945 C  CB  . PHE B 206 ? 0.2278 0.2819 0.2803 0.0165  -0.0268 -0.0253 430  PHE B CB  
3946 C  CG  . PHE B 206 ? 0.2462 0.3032 0.3023 0.0180  -0.0240 -0.0256 430  PHE B CG  
3947 C  CD1 . PHE B 206 ? 0.2311 0.2949 0.2975 0.0200  -0.0256 -0.0282 430  PHE B CD1 
3948 C  CD2 . PHE B 206 ? 0.2144 0.2676 0.2638 0.0175  -0.0200 -0.0235 430  PHE B CD2 
3949 C  CE1 . PHE B 206 ? 0.2485 0.3150 0.3183 0.0217  -0.0227 -0.0286 430  PHE B CE1 
3950 C  CE2 . PHE B 206 ? 0.2390 0.2944 0.2910 0.0192  -0.0174 -0.0241 430  PHE B CE2 
3951 C  CZ  . PHE B 206 ? 0.2185 0.2805 0.2805 0.0213  -0.0185 -0.0266 430  PHE B CZ  
3952 N  N   . PHE B 207 ? 0.2237 0.2708 0.2678 0.0106  -0.0261 -0.0226 431  PHE B N   
3953 C  CA  . PHE B 207 ? 0.2086 0.2509 0.2461 0.0107  -0.0285 -0.0224 431  PHE B CA  
3954 C  C   . PHE B 207 ? 0.2280 0.2647 0.2554 0.0141  -0.0300 -0.0214 431  PHE B C   
3955 O  O   . PHE B 207 ? 0.2350 0.2683 0.2567 0.0139  -0.0270 -0.0191 431  PHE B O   
3956 C  CB  . PHE B 207 ? 0.1823 0.2224 0.2178 0.0071  -0.0252 -0.0203 431  PHE B CB  
3957 C  CG  . PHE B 207 ? 0.2273 0.2720 0.2723 0.0037  -0.0235 -0.0208 431  PHE B CG  
3958 C  CD1 . PHE B 207 ? 0.2161 0.2643 0.2658 0.0021  -0.0194 -0.0198 431  PHE B CD1 
3959 C  CD2 . PHE B 207 ? 0.2440 0.2891 0.2930 0.0023  -0.0259 -0.0224 431  PHE B CD2 
3960 C  CE1 . PHE B 207 ? 0.2483 0.3002 0.3065 -0.0010 -0.0172 -0.0199 431  PHE B CE1 
3961 C  CE2 . PHE B 207 ? 0.2432 0.2919 0.3016 -0.0010 -0.0240 -0.0227 431  PHE B CE2 
3962 C  CZ  . PHE B 207 ? 0.2824 0.3345 0.3454 -0.0027 -0.0195 -0.0212 431  PHE B CZ  
3963 N  N   . ARG B 208 ? 0.2286 0.2641 0.2539 0.0173  -0.0346 -0.0232 432  ARG B N   
3964 C  CA  . ARG B 208 ? 0.2092 0.2396 0.2257 0.0212  -0.0362 -0.0223 432  ARG B CA  
3965 C  C   . ARG B 208 ? 0.2351 0.2590 0.2415 0.0219  -0.0368 -0.0211 432  ARG B C   
3966 O  O   . ARG B 208 ? 0.2310 0.2550 0.2377 0.0213  -0.0389 -0.0225 432  ARG B O   
3967 C  CB  . ARG B 208 ? 0.2464 0.2795 0.2663 0.0252  -0.0411 -0.0249 432  ARG B CB  
3968 C  CG  . ARG B 208 ? 0.2584 0.2852 0.2679 0.0298  -0.0440 -0.0242 432  ARG B CG  
3969 C  CD  . ARG B 208 ? 0.2812 0.3110 0.2948 0.0340  -0.0486 -0.0265 432  ARG B CD  
3970 N  NE  . ARG B 208 ? 0.2552 0.2876 0.2736 0.0343  -0.0459 -0.0259 432  ARG B NE  
3971 C  CZ  . ARG B 208 ? 0.3097 0.3433 0.3301 0.0385  -0.0486 -0.0270 432  ARG B CZ  
3972 N  NH1 . ARG B 208 ? 0.2610 0.2938 0.2793 0.0428  -0.0545 -0.0287 432  ARG B NH1 
3973 N  NH2 . ARG B 208 ? 0.3040 0.3391 0.3280 0.0387  -0.0454 -0.0264 432  ARG B NH2 
3974 N  N   . SER B 209 ? 0.2242 0.2425 0.2221 0.0231  -0.0346 -0.0184 433  SER B N   
3975 C  CA  . SER B 209 ? 0.2380 0.2496 0.2256 0.0245  -0.0347 -0.0169 433  SER B CA  
3976 C  C   . SER B 209 ? 0.2615 0.2681 0.2416 0.0288  -0.0361 -0.0159 433  SER B C   
3977 O  O   . SER B 209 ? 0.2380 0.2446 0.2195 0.0297  -0.0352 -0.0152 433  SER B O   
3978 C  CB  . SER B 209 ? 0.2569 0.2658 0.2414 0.0215  -0.0298 -0.0142 433  SER B CB  
3979 O  OG  . SER B 209 ? 0.2452 0.2578 0.2355 0.0178  -0.0285 -0.0146 433  SER B OG  
3980 N  N   . PHE B 210 ? 0.2957 0.2972 0.2670 0.0317  -0.0382 -0.0157 434  PHE B N   
3981 C  CA  . PHE B 210 ? 0.2673 0.2622 0.2291 0.0358  -0.0388 -0.0138 434  PHE B CA  
3982 C  C   . PHE B 210 ? 0.2525 0.2412 0.2066 0.0344  -0.0339 -0.0103 434  PHE B C   
3983 O  O   . PHE B 210 ? 0.2637 0.2495 0.2119 0.0346  -0.0334 -0.0099 434  PHE B O   
3984 C  CB  . PHE B 210 ? 0.3133 0.3064 0.2696 0.0403  -0.0444 -0.0158 434  PHE B CB  
3985 C  CG  . PHE B 210 ? 0.2885 0.2889 0.2546 0.0410  -0.0494 -0.0197 434  PHE B CG  
3986 C  CD1 . PHE B 210 ? 0.2747 0.2783 0.2464 0.0430  -0.0514 -0.0206 434  PHE B CD1 
3987 C  CD2 . PHE B 210 ? 0.3373 0.3416 0.3079 0.0395  -0.0521 -0.0228 434  PHE B CD2 
3988 C  CE1 . PHE B 210 ? 0.3195 0.3307 0.3018 0.0435  -0.0559 -0.0244 434  PHE B CE1 
3989 C  CE2 . PHE B 210 ? 0.3314 0.3429 0.3125 0.0397  -0.0567 -0.0266 434  PHE B CE2 
3990 C  CZ  . PHE B 210 ? 0.3346 0.3499 0.3218 0.0417  -0.0585 -0.0274 434  PHE B CZ  
3991 N  N   . ILE B 211 ? 0.2794 0.2663 0.2341 0.0329  -0.0303 -0.0081 435  ILE B N   
3992 C  CA  . ILE B 211 ? 0.2528 0.2350 0.2028 0.0308  -0.0254 -0.0050 435  ILE B CA  
3993 C  C   . ILE B 211 ? 0.2786 0.2524 0.2174 0.0345  -0.0249 -0.0025 435  ILE B C   
3994 O  O   . ILE B 211 ? 0.2522 0.2236 0.1874 0.0386  -0.0282 -0.0028 435  ILE B O   
3995 C  CB  . ILE B 211 ? 0.2715 0.2551 0.2271 0.0274  -0.0220 -0.0040 435  ILE B CB  
3996 C  CG1 . ILE B 211 ? 0.2840 0.2636 0.2375 0.0297  -0.0220 -0.0030 435  ILE B CG1 
3997 C  CG2 . ILE B 211 ? 0.2537 0.2452 0.2192 0.0245  -0.0226 -0.0063 435  ILE B CG2 
3998 C  CD1 . ILE B 211 ? 0.2784 0.2589 0.2368 0.0266  -0.0190 -0.0026 435  ILE B CD1 
3999 N  N   . PRO B 212 ? 0.2656 0.2348 0.1988 0.0334  -0.0208 0.0001  436  PRO B N   
4000 C  CA  . PRO B 212 ? 0.2859 0.2465 0.2077 0.0369  -0.0195 0.0029  436  PRO B CA  
4001 C  C   . PRO B 212 ? 0.3053 0.2609 0.2253 0.0382  -0.0186 0.0051  436  PRO B C   
4002 O  O   . PRO B 212 ? 0.3238 0.2815 0.2508 0.0352  -0.0168 0.0051  436  PRO B O   
4003 C  CB  . PRO B 212 ? 0.2669 0.2251 0.1861 0.0343  -0.0142 0.0052  436  PRO B CB  
4004 C  CG  . PRO B 212 ? 0.2957 0.2613 0.2226 0.0312  -0.0149 0.0026  436  PRO B CG  
4005 C  CD  . PRO B 212 ? 0.2634 0.2353 0.2001 0.0295  -0.0176 0.0003  436  PRO B CD  
4006 N  N   . GLY B 213 ? 0.3292 0.2776 0.2391 0.0429  -0.0199 0.0068  437  GLY B N   
4007 C  CA  . GLY B 213 ? 0.3127 0.2541 0.2186 0.0447  -0.0185 0.0095  437  GLY B CA  
4008 C  C   . GLY B 213 ? 0.3618 0.2941 0.2578 0.0451  -0.0134 0.0139  437  GLY B C   
4009 O  O   . GLY B 213 ? 0.4016 0.3315 0.2897 0.0470  -0.0129 0.0146  437  GLY B O   
4010 N  N   . ALA B 214 ? 0.3688 0.2960 0.2656 0.0433  -0.0093 0.0167  438  ALA B N   
4011 C  CA  . ALA B 214 ? 0.3759 0.2949 0.2654 0.0427  -0.0034 0.0211  438  ALA B CA  
4012 C  C   . ALA B 214 ? 0.4231 0.3313 0.3015 0.0474  -0.0031 0.0246  438  ALA B C   
4013 O  O   . ALA B 214 ? 0.4562 0.3567 0.3260 0.0479  0.0017  0.0286  438  ALA B O   
4014 C  CB  . ALA B 214 ? 0.3917 0.3120 0.2901 0.0368  0.0016  0.0220  438  ALA B CB  
4015 N  N   . SER B 215 ? 0.3694 0.2767 0.2479 0.0508  -0.0079 0.0234  439  SER B N   
4016 C  CA  . SER B 215 ? 0.4643 0.3615 0.3315 0.0565  -0.0091 0.0264  439  SER B CA  
4017 C  C   . SER B 215 ? 0.4648 0.3656 0.3363 0.0599  -0.0157 0.0232  439  SER B C   
4018 O  O   . SER B 215 ? 0.4205 0.3305 0.3038 0.0572  -0.0178 0.0194  439  SER B O   
4019 C  CB  . SER B 215 ? 0.4915 0.3787 0.3558 0.0550  -0.0032 0.0310  439  SER B CB  
4020 O  OG  . SER B 215 ? 0.5943 0.4839 0.4691 0.0522  -0.0035 0.0293  439  SER B OG  
4021 N  N   . GLY B 216 ? 0.4613 0.3547 0.3230 0.0662  -0.0189 0.0250  440  GLY B N   
4022 C  CA  . GLY B 216 ? 0.4160 0.3125 0.2819 0.0700  -0.0251 0.0222  440  GLY B CA  
4023 C  C   . GLY B 216 ? 0.4948 0.4019 0.3657 0.0714  -0.0314 0.0173  440  GLY B C   
4024 O  O   . GLY B 216 ? 0.5126 0.4227 0.3808 0.0706  -0.0317 0.0163  440  GLY B O   
4025 N  N   . HIS B 217 ? 0.4226 0.3354 0.3017 0.0734  -0.0363 0.0140  441  HIS B N   
4026 C  CA  . HIS B 217 ? 0.4373 0.3598 0.3221 0.0754  -0.0428 0.0093  441  HIS B CA  
4027 C  C   . HIS B 217 ? 0.4358 0.3699 0.3365 0.0703  -0.0423 0.0055  441  HIS B C   
4028 O  O   . HIS B 217 ? 0.4544 0.3896 0.3621 0.0694  -0.0412 0.0050  441  HIS B O   
4029 C  CB  . HIS B 217 ? 0.5090 0.4295 0.3907 0.0826  -0.0494 0.0085  441  HIS B CB  
4030 C  CG  . HIS B 217 ? 0.5049 0.4147 0.3698 0.0885  -0.0511 0.0119  441  HIS B CG  
4031 N  ND1 . HIS B 217 ? 0.5270 0.4384 0.3861 0.0931  -0.0575 0.0098  441  HIS B ND1 
4032 C  CD2 . HIS B 217 ? 0.5516 0.4486 0.4039 0.0905  -0.0472 0.0173  441  HIS B CD2 
4033 C  CE1 . HIS B 217 ? 0.5736 0.4735 0.4162 0.0980  -0.0576 0.0137  441  HIS B CE1 
4034 N  NE2 . HIS B 217 ? 0.6026 0.4934 0.4407 0.0965  -0.0510 0.0186  441  HIS B NE2 
4035 N  N   . THR B 218 ? 0.4312 0.3730 0.3367 0.0671  -0.0430 0.0028  442  THR B N   
4036 C  CA  . THR B 218 ? 0.4034 0.3561 0.3232 0.0627  -0.0428 -0.0008 442  THR B CA  
4037 C  C   . THR B 218 ? 0.4328 0.3925 0.3557 0.0610  -0.0453 -0.0037 442  THR B C   
4038 O  O   . THR B 218 ? 0.3588 0.3148 0.2736 0.0608  -0.0443 -0.0024 442  THR B O   
4039 C  CB  . THR B 218 ? 0.3763 0.3288 0.3006 0.0568  -0.0364 0.0007  442  THR B CB  
4040 O  OG1 . THR B 218 ? 0.3943 0.3570 0.3310 0.0530  -0.0364 -0.0026 442  THR B OG1 
4041 C  CG2 . THR B 218 ? 0.3900 0.3381 0.3076 0.0538  -0.0319 0.0035  442  THR B CG2 
4042 N  N   . ASN B 219 ? 0.3847 0.3543 0.3195 0.0599  -0.0483 -0.0076 443  ASN B N   
4043 C  CA  . ASN B 219 ? 0.3981 0.3746 0.3381 0.0571  -0.0497 -0.0104 443  ASN B CA  
4044 C  C   . ASN B 219 ? 0.3203 0.3003 0.2662 0.0506  -0.0442 -0.0099 443  ASN B C   
4045 O  O   . ASN B 219 ? 0.3472 0.3320 0.2971 0.0479  -0.0447 -0.0118 443  ASN B O   
4046 C  CB  . ASN B 219 ? 0.4092 0.3947 0.3600 0.0586  -0.0553 -0.0148 443  ASN B CB  
4047 C  CG  . ASN B 219 ? 0.5300 0.5135 0.4746 0.0646  -0.0621 -0.0162 443  ASN B CG  
4048 O  OD1 . ASN B 219 ? 0.5331 0.5130 0.4691 0.0657  -0.0639 -0.0162 443  ASN B OD1 
4049 N  ND2 . ASN B 219 ? 0.4984 0.4837 0.4467 0.0689  -0.0662 -0.0175 443  ASN B ND2 
4050 N  N   . GLY B 220 ? 0.3353 0.3125 0.2817 0.0482  -0.0394 -0.0076 444  GLY B N   
4051 C  CA  . GLY B 220 ? 0.3048 0.2846 0.2557 0.0425  -0.0346 -0.0070 444  GLY B CA  
4052 C  C   . GLY B 220 ? 0.3012 0.2906 0.2636 0.0393  -0.0352 -0.0101 444  GLY B C   
4053 O  O   . GLY B 220 ? 0.2908 0.2827 0.2557 0.0353  -0.0329 -0.0100 444  GLY B O   
4054 N  N   . GLU B 221 ? 0.2727 0.2675 0.2426 0.0410  -0.0381 -0.0126 445  GLU B N   
4055 C  CA  . GLU B 221 ? 0.2909 0.2947 0.2721 0.0379  -0.0382 -0.0152 445  GLU B CA  
4056 C  C   . GLU B 221 ? 0.3030 0.3083 0.2881 0.0337  -0.0332 -0.0143 445  GLU B C   
4057 O  O   . GLU B 221 ? 0.3028 0.3057 0.2873 0.0342  -0.0312 -0.0134 445  GLU B O   
4058 C  CB  . GLU B 221 ? 0.3138 0.3233 0.3027 0.0410  -0.0421 -0.0181 445  GLU B CB  
4059 C  CG  . GLU B 221 ? 0.3072 0.3167 0.2937 0.0450  -0.0481 -0.0199 445  GLU B CG  
4060 C  CD  . GLU B 221 ? 0.4576 0.4682 0.4465 0.0502  -0.0522 -0.0213 445  GLU B CD  
4061 O  OE1 . GLU B 221 ? 0.5298 0.5438 0.5257 0.0501  -0.0504 -0.0218 445  GLU B OE1 
4062 O  OE2 . GLU B 221 ? 0.4579 0.4657 0.4412 0.0547  -0.0573 -0.0219 445  GLU B OE2 
4063 N  N   . MET B 222 ? 0.2506 0.2596 0.2394 0.0296  -0.0313 -0.0145 446  MET B N   
4064 C  CA  . MET B 222 ? 0.2572 0.2681 0.2494 0.0256  -0.0271 -0.0138 446  MET B CA  
4065 C  C   . MET B 222 ? 0.2617 0.2800 0.2627 0.0230  -0.0272 -0.0157 446  MET B C   
4066 O  O   . MET B 222 ? 0.2418 0.2611 0.2432 0.0214  -0.0281 -0.0160 446  MET B O   
4067 C  CB  . MET B 222 ? 0.2632 0.2692 0.2492 0.0231  -0.0242 -0.0113 446  MET B CB  
4068 C  CG  . MET B 222 ? 0.2305 0.2383 0.2195 0.0192  -0.0206 -0.0106 446  MET B CG  
4069 S  SD  . MET B 222 ? 0.3176 0.3223 0.3053 0.0197  -0.0185 -0.0101 446  MET B SD  
4070 C  CE  . MET B 222 ? 0.2964 0.2923 0.2753 0.0206  -0.0177 -0.0074 446  MET B CE  
4071 N  N   . ASP B 223 ? 0.2529 0.2762 0.2610 0.0225  -0.0259 -0.0169 447  ASP B N   
4072 C  CA  . ASP B 223 ? 0.2398 0.2702 0.2571 0.0202  -0.0255 -0.0185 447  ASP B CA  
4073 C  C   . ASP B 223 ? 0.2287 0.2602 0.2471 0.0165  -0.0211 -0.0172 447  ASP B C   
4074 O  O   . ASP B 223 ? 0.2205 0.2511 0.2377 0.0167  -0.0186 -0.0168 447  ASP B O   
4075 C  CB  . ASP B 223 ? 0.2487 0.2845 0.2738 0.0227  -0.0270 -0.0208 447  ASP B CB  
4076 C  CG  . ASP B 223 ? 0.2926 0.3278 0.3171 0.0268  -0.0322 -0.0223 447  ASP B CG  
4077 O  OD1 . ASP B 223 ? 0.2875 0.3220 0.3104 0.0266  -0.0351 -0.0229 447  ASP B OD1 
4078 O  OD2 . ASP B 223 ? 0.2523 0.2874 0.2774 0.0304  -0.0335 -0.0231 447  ASP B OD2 
4079 N  N   . CYS B 224 ? 0.2312 0.2643 0.2515 0.0134  -0.0202 -0.0168 448  CYS B N   
4080 C  CA  . CYS B 224 ? 0.1935 0.2275 0.2145 0.0102  -0.0162 -0.0155 448  CYS B CA  
4081 C  C   . CYS B 224 ? 0.2064 0.2467 0.2365 0.0084  -0.0149 -0.0165 448  CYS B C   
4082 O  O   . CYS B 224 ? 0.1899 0.2338 0.2263 0.0088  -0.0173 -0.0183 448  CYS B O   
4083 C  CB  . CYS B 224 ? 0.2030 0.2332 0.2187 0.0080  -0.0155 -0.0135 448  CYS B CB  
4084 S  SG  . CYS B 224 ? 0.2586 0.2896 0.2767 0.0064  -0.0173 -0.0139 448  CYS B SG  
4085 N  N   . LEU B 225 ? 0.2027 0.2441 0.2332 0.0063  -0.0110 -0.0154 449  LEU B N   
4086 C  CA  . LEU B 225 ? 0.2144 0.2612 0.2529 0.0045  -0.0085 -0.0158 449  LEU B CA  
4087 C  C   . LEU B 225 ? 0.1929 0.2398 0.2334 0.0013  -0.0080 -0.0147 449  LEU B C   
4088 O  O   . LEU B 225 ? 0.2293 0.2805 0.2782 -0.0002 -0.0073 -0.0155 449  LEU B O   
4089 C  CB  . LEU B 225 ? 0.1795 0.2267 0.2161 0.0041  -0.0041 -0.0150 449  LEU B CB  
4090 C  CG  . LEU B 225 ? 0.1923 0.2396 0.2279 0.0072  -0.0040 -0.0164 449  LEU B CG  
4091 C  CD1 . LEU B 225 ? 0.2090 0.2564 0.2422 0.0067  0.0005  -0.0158 449  LEU B CD1 
4092 C  CD2 . LEU B 225 ? 0.1908 0.2434 0.2354 0.0093  -0.0057 -0.0188 449  LEU B CD2 
4093 N  N   . LEU B 226 ? 0.1961 0.2382 0.2297 0.0003  -0.0083 -0.0130 450  LEU B N   
4094 C  CA  . LEU B 226 ? 0.2177 0.2587 0.2518 -0.0023 -0.0080 -0.0117 450  LEU B CA  
4095 C  C   . LEU B 226 ? 0.2073 0.2438 0.2354 -0.0015 -0.0107 -0.0114 450  LEU B C   
4096 O  O   . LEU B 226 ? 0.2487 0.2821 0.2704 -0.0001 -0.0109 -0.0107 450  LEU B O   
4097 C  CB  . LEU B 226 ? 0.2413 0.2812 0.2728 -0.0043 -0.0042 -0.0092 450  LEU B CB  
4098 C  CG  . LEU B 226 ? 0.3011 0.3445 0.3367 -0.0054 -0.0002 -0.0088 450  LEU B CG  
4099 C  CD1 . LEU B 226 ? 0.2472 0.2879 0.2765 -0.0066 0.0028  -0.0062 450  LEU B CD1 
4100 C  CD2 . LEU B 226 ? 0.2488 0.2959 0.2939 -0.0073 0.0002  -0.0095 450  LEU B CD2 
4101 N  N   . PRO B 227 ? 0.2383 0.2741 0.2683 -0.0023 -0.0126 -0.0119 451  PRO B N   
4102 C  CA  . PRO B 227 ? 0.2126 0.2439 0.2362 -0.0016 -0.0141 -0.0112 451  PRO B CA  
4103 C  C   . PRO B 227 ? 0.2080 0.2370 0.2274 -0.0031 -0.0116 -0.0087 451  PRO B C   
4104 O  O   . PRO B 227 ? 0.1762 0.2064 0.1975 -0.0049 -0.0091 -0.0074 451  PRO B O   
4105 C  CB  . PRO B 227 ? 0.1898 0.2211 0.2172 -0.0024 -0.0163 -0.0127 451  PRO B CB  
4106 C  CG  . PRO B 227 ? 0.2572 0.2924 0.2928 -0.0047 -0.0147 -0.0130 451  PRO B CG  
4107 C  CD  . PRO B 227 ? 0.2435 0.2822 0.2815 -0.0040 -0.0131 -0.0132 451  PRO B CD  
4108 N  N   . GLN B 228 ? 0.1820 0.2075 0.1955 -0.0022 -0.0122 -0.0079 452  GLN B N   
4109 C  CA  . GLN B 228 ? 0.2180 0.2418 0.2282 -0.0033 -0.0104 -0.0058 452  GLN B CA  
4110 C  C   . GLN B 228 ? 0.2139 0.2376 0.2262 -0.0051 -0.0096 -0.0046 452  GLN B C   
4111 O  O   . GLN B 228 ? 0.2191 0.2424 0.2299 -0.0062 -0.0080 -0.0028 452  GLN B O   
4112 C  CB  . GLN B 228 ? 0.2521 0.2729 0.2574 -0.0021 -0.0110 -0.0053 452  GLN B CB  
4113 C  CG  . GLN B 228 ? 0.2067 0.2263 0.2095 -0.0031 -0.0097 -0.0035 452  GLN B CG  
4114 C  CD  . GLN B 228 ? 0.2588 0.2793 0.2605 -0.0035 -0.0086 -0.0033 452  GLN B CD  
4115 O  OE1 . GLN B 228 ? 0.2570 0.2783 0.2592 -0.0026 -0.0086 -0.0044 452  GLN B OE1 
4116 N  NE2 . GLN B 228 ? 0.1950 0.2150 0.1949 -0.0045 -0.0080 -0.0021 452  GLN B NE2 
4117 N  N   . GLU B 229 ? 0.2531 0.2766 0.2686 -0.0054 -0.0109 -0.0057 453  GLU B N   
4118 C  CA  . GLU B 229 ? 0.2068 0.2294 0.2246 -0.0071 -0.0101 -0.0046 453  GLU B CA  
4119 C  C   . GLU B 229 ? 0.2446 0.2693 0.2661 -0.0090 -0.0077 -0.0034 453  GLU B C   
4120 O  O   . GLU B 229 ? 0.2209 0.2439 0.2419 -0.0103 -0.0061 -0.0013 453  GLU B O   
4121 C  CB  . GLU B 229 ? 0.2196 0.2412 0.2403 -0.0070 -0.0122 -0.0065 453  GLU B CB  
4122 C  CG  . GLU B 229 ? 0.2768 0.2954 0.2929 -0.0051 -0.0139 -0.0072 453  GLU B CG  
4123 C  CD  . GLU B 229 ? 0.2623 0.2810 0.2749 -0.0028 -0.0154 -0.0086 453  GLU B CD  
4124 O  OE1 . GLU B 229 ? 0.2317 0.2527 0.2462 -0.0024 -0.0160 -0.0096 453  GLU B OE1 
4125 O  OE2 . GLU B 229 ? 0.2878 0.3038 0.2956 -0.0013 -0.0157 -0.0085 453  GLU B OE2 
4126 N  N   . PHE B 230 ? 0.1980 0.2260 0.2231 -0.0090 -0.0072 -0.0047 454  PHE B N   
4127 C  CA  . PHE B 230 ? 0.2612 0.2912 0.2893 -0.0106 -0.0040 -0.0034 454  PHE B CA  
4128 C  C   . PHE B 230 ? 0.1949 0.2239 0.2169 -0.0103 -0.0019 -0.0013 454  PHE B C   
4129 O  O   . PHE B 230 ? 0.1971 0.2251 0.2180 -0.0115 0.0006  0.0010  454  PHE B O   
4130 C  CB  . PHE B 230 ? 0.1775 0.2119 0.2119 -0.0105 -0.0037 -0.0054 454  PHE B CB  
4131 C  CG  . PHE B 230 ? 0.2347 0.2710 0.2771 -0.0115 -0.0055 -0.0075 454  PHE B CG  
4132 C  CD1 . PHE B 230 ? 0.2815 0.3148 0.3238 -0.0119 -0.0078 -0.0080 454  PHE B CD1 
4133 C  CD2 . PHE B 230 ? 0.3120 0.3531 0.3624 -0.0119 -0.0049 -0.0092 454  PHE B CD2 
4134 C  CE1 . PHE B 230 ? 0.2816 0.3162 0.3311 -0.0129 -0.0099 -0.0104 454  PHE B CE1 
4135 C  CE2 . PHE B 230 ? 0.3270 0.3701 0.3857 -0.0130 -0.0071 -0.0116 454  PHE B CE2 
4136 C  CZ  . PHE B 230 ? 0.2545 0.2942 0.3125 -0.0135 -0.0097 -0.0123 454  PHE B CZ  
4137 N  N   . VAL B 231 ? 0.1780 0.2067 0.1957 -0.0086 -0.0029 -0.0021 455  VAL B N   
4138 C  CA  . VAL B 231 ? 0.2107 0.2380 0.2223 -0.0082 -0.0018 -0.0007 455  VAL B CA  
4139 C  C   . VAL B 231 ? 0.2013 0.2258 0.2098 -0.0089 -0.0020 0.0015  455  VAL B C   
4140 O  O   . VAL B 231 ? 0.2124 0.2360 0.2179 -0.0094 -0.0003 0.0034  455  VAL B O   
4141 C  CB  . VAL B 231 ? 0.1989 0.2255 0.2072 -0.0065 -0.0035 -0.0020 455  VAL B CB  
4142 C  CG1 . VAL B 231 ? 0.2037 0.2286 0.2064 -0.0064 -0.0030 -0.0010 455  VAL B CG1 
4143 C  CG2 . VAL B 231 ? 0.2533 0.2823 0.2643 -0.0053 -0.0033 -0.0040 455  VAL B CG2 
4144 N  N   . GLN B 232 ? 0.1808 0.2037 0.1894 -0.0086 -0.0041 0.0013  456  GLN B N   
4145 C  CA  . GLN B 232 ? 0.1983 0.2188 0.2047 -0.0088 -0.0046 0.0031  456  GLN B CA  
4146 C  C   . GLN B 232 ? 0.2314 0.2508 0.2394 -0.0102 -0.0028 0.0050  456  GLN B C   
4147 O  O   . GLN B 232 ? 0.2378 0.2554 0.2423 -0.0102 -0.0023 0.0073  456  GLN B O   
4148 C  CB  . GLN B 232 ? 0.2249 0.2441 0.2321 -0.0081 -0.0066 0.0023  456  GLN B CB  
4149 C  CG  . GLN B 232 ? 0.2251 0.2444 0.2300 -0.0069 -0.0077 0.0011  456  GLN B CG  
4150 C  CD  . GLN B 232 ? 0.2525 0.2706 0.2580 -0.0059 -0.0089 0.0001  456  GLN B CD  
4151 O  OE1 . GLN B 232 ? 0.2783 0.2961 0.2860 -0.0058 -0.0096 -0.0011 456  GLN B OE1 
4152 N  NE2 . GLN B 232 ? 0.2942 0.3114 0.2977 -0.0052 -0.0093 0.0005  456  GLN B NE2 
4153 N  N   . HIS B 233 ? 0.1995 0.2200 0.2128 -0.0113 -0.0020 0.0042  457  HIS B N   
4154 C  CA  . HIS B 233 ? 0.2527 0.2716 0.2685 -0.0129 -0.0002 0.0062  457  HIS B CA  
4155 C  C   . HIS B 233 ? 0.2519 0.2710 0.2652 -0.0135 0.0032  0.0083  457  HIS B C   
4156 O  O   . HIS B 233 ? 0.3011 0.3172 0.3115 -0.0140 0.0046  0.0112  457  HIS B O   
4157 C  CB  . HIS B 233 ? 0.2364 0.2566 0.2597 -0.0142 -0.0004 0.0043  457  HIS B CB  
4158 C  CG  . HIS B 233 ? 0.2942 0.3121 0.3211 -0.0162 0.0014  0.0061  457  HIS B CG  
4159 N  ND1 . HIS B 233 ? 0.3406 0.3545 0.3672 -0.0163 0.0002  0.0068  457  HIS B ND1 
4160 C  CD2 . HIS B 233 ? 0.2873 0.3059 0.3181 -0.0182 0.0048  0.0074  457  HIS B CD2 
4161 C  CE1 . HIS B 233 ? 0.3736 0.3853 0.4038 -0.0184 0.0024  0.0086  457  HIS B CE1 
4162 N  NE2 . HIS B 233 ? 0.3310 0.3456 0.3640 -0.0197 0.0055  0.0091  457  HIS B NE2 
4163 N  N   . PHE B 234 ? 0.2274 0.2498 0.2413 -0.0133 0.0046  0.0071  458  PHE B N   
4164 C  CA  . PHE B 234 ? 0.2462 0.2687 0.2567 -0.0135 0.0082  0.0090  458  PHE B CA  
4165 C  C   . PHE B 234 ? 0.2300 0.2497 0.2316 -0.0121 0.0073  0.0105  458  PHE B C   
4166 O  O   . PHE B 234 ? 0.2380 0.2555 0.2347 -0.0121 0.0097  0.0131  458  PHE B O   
4167 C  CB  . PHE B 234 ? 0.1927 0.2193 0.2057 -0.0130 0.0097  0.0069  458  PHE B CB  
4168 C  CG  . PHE B 234 ? 0.2279 0.2580 0.2505 -0.0141 0.0098  0.0049  458  PHE B CG  
4169 C  CD1 . PHE B 234 ? 0.2289 0.2584 0.2576 -0.0162 0.0105  0.0056  458  PHE B CD1 
4170 C  CD2 . PHE B 234 ? 0.2288 0.2628 0.2547 -0.0129 0.0090  0.0021  458  PHE B CD2 
4171 C  CE1 . PHE B 234 ? 0.2166 0.2497 0.2548 -0.0173 0.0100  0.0033  458  PHE B CE1 
4172 C  CE2 . PHE B 234 ? 0.2368 0.2743 0.2718 -0.0137 0.0084  0.0000  458  PHE B CE2 
4173 C  CZ  . PHE B 234 ? 0.2436 0.2810 0.2851 -0.0159 0.0088  0.0004  458  PHE B CZ  
4174 N  N   . TYR B 235 ? 0.2302 0.2500 0.2295 -0.0108 0.0040  0.0090  459  TYR B N   
4175 C  CA  . TYR B 235 ? 0.2181 0.2358 0.2103 -0.0096 0.0026  0.0100  459  TYR B CA  
4176 C  C   . TYR B 235 ? 0.2329 0.2473 0.2232 -0.0097 0.0021  0.0128  459  TYR B C   
4177 O  O   . TYR B 235 ? 0.2207 0.2329 0.2047 -0.0089 0.0025  0.0148  459  TYR B O   
4178 C  CB  . TYR B 235 ? 0.2261 0.2445 0.2181 -0.0086 -0.0007 0.0078  459  TYR B CB  
4179 C  CG  . TYR B 235 ? 0.2695 0.2866 0.2557 -0.0076 -0.0026 0.0082  459  TYR B CG  
4180 C  CD1 . TYR B 235 ? 0.2827 0.2997 0.2637 -0.0069 -0.0019 0.0076  459  TYR B CD1 
4181 C  CD2 . TYR B 235 ? 0.3176 0.3336 0.3038 -0.0072 -0.0052 0.0089  459  TYR B CD2 
4182 C  CE1 . TYR B 235 ? 0.3328 0.3485 0.3087 -0.0059 -0.0043 0.0075  459  TYR B CE1 
4183 C  CE2 . TYR B 235 ? 0.3572 0.3726 0.3392 -0.0063 -0.0074 0.0089  459  TYR B CE2 
4184 C  CZ  . TYR B 235 ? 0.4027 0.4179 0.3796 -0.0057 -0.0072 0.0081  459  TYR B CZ  
4185 O  OH  . TYR B 235 ? 0.5942 0.6087 0.5669 -0.0048 -0.0101 0.0076  459  TYR B OH  
4186 N  N   . GLN B 236 ? 0.2443 0.2580 0.2394 -0.0103 0.0011  0.0128  460  GLN B N   
4187 C  CA  . GLN B 236 ? 0.2869 0.2971 0.2810 -0.0102 0.0007  0.0154  460  GLN B CA  
4188 C  C   . GLN B 236 ? 0.3190 0.3267 0.3116 -0.0112 0.0042  0.0184  460  GLN B C   
4189 O  O   . GLN B 236 ? 0.2696 0.2738 0.2567 -0.0103 0.0043  0.0213  460  GLN B O   
4190 C  CB  . GLN B 236 ? 0.2753 0.2850 0.2752 -0.0106 -0.0008 0.0142  460  GLN B CB  
4191 C  CG  . GLN B 236 ? 0.2915 0.3022 0.2915 -0.0093 -0.0039 0.0124  460  GLN B CG  
4192 C  CD  . GLN B 236 ? 0.3145 0.3240 0.3101 -0.0078 -0.0057 0.0140  460  GLN B CD  
4193 O  OE1 . GLN B 236 ? 0.3138 0.3203 0.3076 -0.0073 -0.0056 0.0165  460  GLN B OE1 
4194 N  NE2 . GLN B 236 ? 0.2705 0.2822 0.2648 -0.0070 -0.0075 0.0124  460  GLN B NE2 
4195 N  N   . GLU B 237 ? 0.2526 0.2620 0.2503 -0.0130 0.0071  0.0178  461  GLU B N   
4196 C  CA  . GLU B 237 ? 0.2888 0.2956 0.2871 -0.0145 0.0110  0.0208  461  GLU B CA  
4197 C  C   . GLU B 237 ? 0.3135 0.3199 0.3051 -0.0140 0.0144  0.0228  461  GLU B C   
4198 O  O   . GLU B 237 ? 0.3166 0.3188 0.3035 -0.0140 0.0168  0.0265  461  GLU B O   
4199 C  CB  . GLU B 237 ? 0.3321 0.3412 0.3402 -0.0169 0.0127  0.0193  461  GLU B CB  
4200 C  CG  . GLU B 237 ? 0.3377 0.3458 0.3514 -0.0174 0.0097  0.0176  461  GLU B CG  
4201 C  CD  . GLU B 237 ? 0.4192 0.4215 0.4316 -0.0177 0.0100  0.0207  461  GLU B CD  
4202 O  OE1 . GLU B 237 ? 0.4488 0.4485 0.4617 -0.0193 0.0137  0.0236  461  GLU B OE1 
4203 O  OE2 . GLU B 237 ? 0.4604 0.4606 0.4712 -0.0162 0.0067  0.0203  461  GLU B OE2 
4204 N  N   . ALA B 238 ? 0.2618 0.2719 0.2524 -0.0133 0.0148  0.0205  462  ALA B N   
4205 C  CA  . ALA B 238 ? 0.3393 0.3494 0.3237 -0.0126 0.0184  0.0217  462  ALA B CA  
4206 C  C   . ALA B 238 ? 0.3182 0.3265 0.3043 -0.0144 0.0240  0.0249  462  ALA B C   
4207 O  O   . ALA B 238 ? 0.3799 0.3845 0.3579 -0.0136 0.0268  0.0282  462  ALA B O   
4208 C  CB  . ALA B 238 ? 0.3139 0.3210 0.2873 -0.0102 0.0163  0.0229  462  ALA B CB  
4209 N  N   . ALA B 239 ? 0.3596 0.3704 0.3564 -0.0168 0.0255  0.0240  463  ALA B N   
4210 C  CA  . ALA B 239 ? 0.3496 0.3591 0.3503 -0.0191 0.0310  0.0269  463  ALA B CA  
4211 C  C   . ALA B 239 ? 0.3522 0.3647 0.3521 -0.0190 0.0363  0.0270  463  ALA B C   
4212 O  O   . ALA B 239 ? 0.3333 0.3507 0.3350 -0.0180 0.0355  0.0236  463  ALA B O   
4213 C  CB  . ALA B 239 ? 0.3633 0.3748 0.3769 -0.0219 0.0305  0.0252  463  ALA B CB  
4214 N  N   . THR B 240 ? 0.3509 0.3602 0.3477 -0.0199 0.0421  0.0310  464  THR B N   
4215 C  CA  . THR B 240 ? 0.3980 0.4099 0.3938 -0.0198 0.0483  0.0315  464  THR B CA  
4216 C  C   . THR B 240 ? 0.3738 0.3928 0.3844 -0.0221 0.0502  0.0285  464  THR B C   
4217 O  O   . THR B 240 ? 0.3115 0.3312 0.3328 -0.0251 0.0505  0.0286  464  THR B O   
4218 C  CB  . THR B 240 ? 0.4605 0.4668 0.4502 -0.0205 0.0546  0.0370  464  THR B CB  
4219 O  OG1 . THR B 240 ? 0.5349 0.5344 0.5117 -0.0183 0.0517  0.0399  464  THR B OG1 
4220 C  CG2 . THR B 240 ? 0.4585 0.4670 0.4445 -0.0197 0.0613  0.0377  464  THR B CG2 
4221 N  N   . ALA B 241 ? 0.2902 0.3144 0.3015 -0.0206 0.0512  0.0256  465  ALA B N   
4222 C  CA  . ALA B 241 ? 0.3155 0.3470 0.3407 -0.0222 0.0533  0.0227  465  ALA B CA  
4223 C  C   . ALA B 241 ? 0.3211 0.3534 0.3495 -0.0240 0.0619  0.0258  465  ALA B C   
4224 O  O   . ALA B 241 ? 0.3632 0.3946 0.3829 -0.0221 0.0666  0.0272  465  ALA B O   
4225 C  CB  . ALA B 241 ? 0.3271 0.3634 0.3518 -0.0195 0.0508  0.0185  465  ALA B CB  
4226 N  N   . ARG B 242 ? 0.2975 0.3313 0.3383 -0.0276 0.0643  0.0267  466  ARG B N   
4227 C  CA  . ARG B 242 ? 0.2862 0.3202 0.3311 -0.0299 0.0731  0.0301  466  ARG B CA  
4228 C  C   . ARG B 242 ? 0.3192 0.3620 0.3743 -0.0299 0.0775  0.0274  466  ARG B C   
4229 O  O   . ARG B 242 ? 0.2624 0.3058 0.3186 -0.0309 0.0858  0.0301  466  ARG B O   
4230 C  CB  . ARG B 242 ? 0.2655 0.2973 0.3207 -0.0342 0.0742  0.0322  466  ARG B CB  
4231 C  CG  . ARG B 242 ? 0.3939 0.4169 0.4400 -0.0341 0.0703  0.0350  466  ARG B CG  
4232 C  CD  . ARG B 242 ? 0.4477 0.4630 0.4777 -0.0323 0.0747  0.0405  466  ARG B CD  
4233 N  NE  . ARG B 242 ? 0.6728 0.6799 0.6951 -0.0319 0.0706  0.0432  466  ARG B NE  
4234 C  CZ  . ARG B 242 ? 0.6632 0.6630 0.6698 -0.0294 0.0714  0.0473  466  ARG B CZ  
4235 N  NH1 . ARG B 242 ? 0.6619 0.6606 0.6577 -0.0272 0.0762  0.0494  466  ARG B NH1 
4236 N  NH2 . ARG B 242 ? 0.6474 0.6405 0.6488 -0.0288 0.0669  0.0491  466  ARG B NH2 
4237 N  N   . SER B 243 ? 0.3076 0.3568 0.3702 -0.0287 0.0722  0.0222  467  SER B N   
4238 C  CA  . SER B 243 ? 0.2494 0.3069 0.3210 -0.0278 0.0752  0.0191  467  SER B CA  
4239 C  C   . SER B 243 ? 0.2644 0.3241 0.3319 -0.0241 0.0684  0.0147  467  SER B C   
4240 O  O   . SER B 243 ? 0.2821 0.3371 0.3410 -0.0228 0.0620  0.0142  467  SER B O   
4241 C  CB  . SER B 243 ? 0.2593 0.3241 0.3513 -0.0313 0.0762  0.0171  467  SER B CB  
4242 O  OG  . SER B 243 ? 0.2606 0.3284 0.3595 -0.0310 0.0675  0.0126  467  SER B OG  
4243 N  N   . GLU B 244 ? 0.2878 0.3546 0.3624 -0.0223 0.0699  0.0114  468  GLU B N   
4244 C  CA  . GLU B 244 ? 0.2899 0.3585 0.3615 -0.0188 0.0638  0.0073  468  GLU B CA  
4245 C  C   . GLU B 244 ? 0.2638 0.3355 0.3453 -0.0194 0.0561  0.0038  468  GLU B C   
4246 O  O   . GLU B 244 ? 0.2340 0.3058 0.3119 -0.0166 0.0505  0.0009  468  GLU B O   
4247 C  CB  . GLU B 244 ? 0.3659 0.4407 0.4414 -0.0162 0.0681  0.0049  468  GLU B CB  
4248 C  CG  . GLU B 244 ? 0.4062 0.4772 0.4681 -0.0140 0.0743  0.0072  468  GLU B CG  
4249 C  CD  . GLU B 244 ? 0.5115 0.5747 0.5558 -0.0115 0.0696  0.0076  468  GLU B CD  
4250 O  OE1 . GLU B 244 ? 0.5218 0.5849 0.5651 -0.0098 0.0626  0.0044  468  GLU B OE1 
4251 O  OE2 . GLU B 244 ? 0.5199 0.5769 0.5515 -0.0114 0.0729  0.0110  468  GLU B OE2 
4252 N  N   . VAL B 245 ? 0.2688 0.3426 0.3623 -0.0230 0.0558  0.0040  469  VAL B N   
4253 C  CA  . VAL B 245 ? 0.2045 0.2818 0.3081 -0.0234 0.0487  0.0003  469  VAL B CA  
4254 C  C   . VAL B 245 ? 0.2464 0.3198 0.3533 -0.0271 0.0468  0.0018  469  VAL B C   
4255 O  O   . VAL B 245 ? 0.2301 0.3036 0.3434 -0.0305 0.0521  0.0044  469  VAL B O   
4256 C  CB  . VAL B 245 ? 0.2740 0.3611 0.3945 -0.0235 0.0496  -0.0032 469  VAL B CB  
4257 C  CG1 . VAL B 245 ? 0.2043 0.2944 0.3334 -0.0233 0.0415  -0.0072 469  VAL B CG1 
4258 C  CG2 . VAL B 245 ? 0.2333 0.3240 0.3510 -0.0196 0.0519  -0.0048 469  VAL B CG2 
4259 N  N   . ALA B 246 ? 0.2204 0.2902 0.3228 -0.0263 0.0396  0.0004  470  ALA B N   
4260 C  CA  . ALA B 246 ? 0.2474 0.3138 0.3538 -0.0292 0.0367  0.0008  470  ALA B CA  
4261 C  C   . ALA B 246 ? 0.2741 0.3464 0.3942 -0.0298 0.0316  -0.0039 470  ALA B C   
4262 O  O   . ALA B 246 ? 0.2686 0.3424 0.3866 -0.0268 0.0257  -0.0071 470  ALA B O   
4263 C  CB  . ALA B 246 ? 0.2282 0.2870 0.3211 -0.0278 0.0323  0.0021  470  ALA B CB  
4264 N  N   . LEU B 247 ? 0.2567 0.3319 0.3904 -0.0336 0.0336  -0.0042 471  LEU B N   
4265 C  CA  . LEU B 247 ? 0.2315 0.3122 0.3790 -0.0344 0.0281  -0.0090 471  LEU B CA  
4266 C  C   . LEU B 247 ? 0.2455 0.3204 0.3884 -0.0345 0.0213  -0.0103 471  LEU B C   
4267 O  O   . LEU B 247 ? 0.2411 0.3099 0.3816 -0.0371 0.0226  -0.0078 471  LEU B O   
4268 C  CB  . LEU B 247 ? 0.2362 0.3220 0.4008 -0.0388 0.0325  -0.0091 471  LEU B CB  
4269 C  CG  . LEU B 247 ? 0.2388 0.3307 0.4186 -0.0397 0.0261  -0.0146 471  LEU B CG  
4270 C  CD1 . LEU B 247 ? 0.1983 0.2981 0.3824 -0.0358 0.0231  -0.0184 471  LEU B CD1 
4271 C  CD2 . LEU B 247 ? 0.2150 0.3104 0.4124 -0.0450 0.0299  -0.0147 471  LEU B CD2 
4272 N  N   . LEU B 248 ? 0.2235 0.3000 0.3651 -0.0314 0.0142  -0.0142 472  LEU B N   
4273 C  CA  . LEU B 248 ? 0.2330 0.3046 0.3700 -0.0308 0.0076  -0.0161 472  LEU B CA  
4274 C  C   . LEU B 248 ? 0.2655 0.3419 0.4162 -0.0319 0.0023  -0.0210 472  LEU B C   
4275 O  O   . LEU B 248 ? 0.2989 0.3832 0.4605 -0.0314 0.0018  -0.0238 472  LEU B O   
4276 C  CB  . LEU B 248 ? 0.2239 0.2927 0.3473 -0.0262 0.0034  -0.0166 472  LEU B CB  
4277 C  CG  . LEU B 248 ? 0.3250 0.3862 0.4330 -0.0251 0.0049  -0.0129 472  LEU B CG  
4278 C  CD1 . LEU B 248 ? 0.2610 0.3206 0.3660 -0.0269 0.0121  -0.0084 472  LEU B CD1 
4279 C  CD2 . LEU B 248 ? 0.2315 0.2918 0.3291 -0.0209 0.0018  -0.0137 472  LEU B CD2 
4280 N  N   . ARG B 249 ? 0.2459 0.3175 0.3966 -0.0334 -0.0016 -0.0224 473  ARG B N   
4281 C  CA  . ARG B 249 ? 0.2391 0.3140 0.4005 -0.0339 -0.0080 -0.0277 473  ARG B CA  
4282 C  C   . ARG B 249 ? 0.2304 0.3000 0.3802 -0.0305 -0.0149 -0.0298 473  ARG B C   
4283 O  O   . ARG B 249 ? 0.2567 0.3188 0.3953 -0.0302 -0.0141 -0.0273 473  ARG B O   
4284 C  CB  . ARG B 249 ? 0.2191 0.2928 0.3924 -0.0392 -0.0064 -0.0280 473  ARG B CB  
4285 C  CG  . ARG B 249 ? 0.3244 0.3998 0.5070 -0.0398 -0.0141 -0.0340 473  ARG B CG  
4286 C  CD  . ARG B 249 ? 0.3621 0.4344 0.5552 -0.0451 -0.0129 -0.0344 473  ARG B CD  
4287 N  NE  . ARG B 249 ? 0.3870 0.4657 0.5968 -0.0495 -0.0073 -0.0335 473  ARG B NE  
4288 C  CZ  . ARG B 249 ? 0.3558 0.4338 0.5789 -0.0546 -0.0062 -0.0346 473  ARG B CZ  
4289 N  NH1 . ARG B 249 ? 0.3932 0.4645 0.6152 -0.0558 -0.0109 -0.0370 473  ARG B NH1 
4290 N  NH2 . ARG B 249 ? 0.3607 0.4447 0.5987 -0.0586 0.0000  -0.0333 473  ARG B NH2 
4291 N  N   . PHE B 250 ? 0.2651 0.3386 0.4171 -0.0274 -0.0213 -0.0343 474  PHE B N   
4292 C  CA  . PHE B 250 ? 0.2537 0.3223 0.3956 -0.0241 -0.0279 -0.0367 474  PHE B CA  
4293 C  C   . PHE B 250 ? 0.2904 0.3577 0.4403 -0.0264 -0.0326 -0.0408 474  PHE B C   
4294 O  O   . PHE B 250 ? 0.2127 0.2861 0.3751 -0.0269 -0.0367 -0.0452 474  PHE B O   
4295 C  CB  . PHE B 250 ? 0.2555 0.3276 0.3936 -0.0192 -0.0325 -0.0391 474  PHE B CB  
4296 C  CG  . PHE B 250 ? 0.2161 0.2815 0.3390 -0.0153 -0.0369 -0.0396 474  PHE B CG  
4297 C  CD1 . PHE B 250 ? 0.2227 0.2828 0.3320 -0.0139 -0.0334 -0.0355 474  PHE B CD1 
4298 C  CD2 . PHE B 250 ? 0.2356 0.3003 0.3580 -0.0130 -0.0443 -0.0442 474  PHE B CD2 
4299 C  CE1 . PHE B 250 ? 0.2476 0.3018 0.3438 -0.0104 -0.0367 -0.0357 474  PHE B CE1 
4300 C  CE2 . PHE B 250 ? 0.2590 0.3174 0.3669 -0.0092 -0.0476 -0.0443 474  PHE B CE2 
4301 C  CZ  . PHE B 250 ? 0.2632 0.3164 0.3583 -0.0081 -0.0435 -0.0400 474  PHE B CZ  
4302 N  N   . VAL B 251 ? 0.3013 0.3608 0.4445 -0.0277 -0.0323 -0.0396 475  VAL B N   
4303 C  CA  . VAL B 251 ? 0.3140 0.3707 0.4648 -0.0308 -0.0350 -0.0426 475  VAL B CA  
4304 C  C   . VAL B 251 ? 0.3133 0.3666 0.4572 -0.0273 -0.0430 -0.0473 475  VAL B C   
4305 O  O   . VAL B 251 ? 0.3215 0.3697 0.4505 -0.0236 -0.0439 -0.0460 475  VAL B O   
4306 C  CB  . VAL B 251 ? 0.3166 0.3660 0.4634 -0.0338 -0.0297 -0.0383 475  VAL B CB  
4307 C  CG1 . VAL B 251 ? 0.3517 0.3958 0.5025 -0.0359 -0.0334 -0.0416 475  VAL B CG1 
4308 C  CG2 . VAL B 251 ? 0.3166 0.3689 0.4714 -0.0376 -0.0220 -0.0341 475  VAL B CG2 
4309 N  N   . ASN B 252 ? 0.3125 0.3683 0.4670 -0.0284 -0.0487 -0.0529 476  ASN B N   
4310 C  CA  . ASN B 252 ? 0.3640 0.4150 0.5119 -0.0258 -0.0561 -0.0576 476  ASN B CA  
4311 C  C   . ASN B 252 ? 0.3791 0.4223 0.5268 -0.0289 -0.0548 -0.0574 476  ASN B C   
4312 O  O   . ASN B 252 ? 0.4088 0.4532 0.5704 -0.0335 -0.0545 -0.0592 476  ASN B O   
4313 C  CB  . ASN B 252 ? 0.4213 0.4783 0.5804 -0.0253 -0.0636 -0.0642 476  ASN B CB  
4314 C  CG  . ASN B 252 ? 0.4678 0.5194 0.6190 -0.0221 -0.0717 -0.0695 476  ASN B CG  
4315 O  OD1 . ASN B 252 ? 0.5116 0.5555 0.6471 -0.0193 -0.0716 -0.0681 476  ASN B OD1 
4316 N  ND2 . ASN B 252 ? 0.4862 0.5420 0.6482 -0.0224 -0.0789 -0.0758 476  ASN B ND2 
4317 N  N   . PRO B 253 ? 0.3809 0.4162 0.5140 -0.0267 -0.0538 -0.0553 477  PRO B N   
4318 C  CA  . PRO B 253 ? 0.4225 0.4501 0.5556 -0.0294 -0.0523 -0.0550 477  PRO B CA  
4319 C  C   . PRO B 253 ? 0.5344 0.5595 0.6733 -0.0301 -0.0592 -0.0618 477  PRO B C   
4320 O  O   . PRO B 253 ? 0.4851 0.5046 0.6280 -0.0333 -0.0581 -0.0622 477  PRO B O   
4321 C  CB  . PRO B 253 ? 0.4012 0.4221 0.5171 -0.0257 -0.0503 -0.0517 477  PRO B CB  
4322 C  CG  . PRO B 253 ? 0.4481 0.4717 0.5548 -0.0207 -0.0541 -0.0533 477  PRO B CG  
4323 C  CD  . PRO B 253 ? 0.4132 0.4458 0.5298 -0.0215 -0.0542 -0.0535 477  PRO B CD  
4324 N  N   A ASP B 254 ? 0.5271 0.5558 0.6663 -0.0272 -0.0664 -0.0672 478  ASP B N   
4325 C  CA  A ASP B 254 ? 0.5072 0.5338 0.6521 -0.0278 -0.0737 -0.0743 478  ASP B CA  
4326 C  C   A ASP B 254 ? 0.5707 0.6021 0.7363 -0.0338 -0.0736 -0.0765 478  ASP B C   
4327 O  O   A ASP B 254 ? 0.7405 0.7678 0.9128 -0.0364 -0.0770 -0.0808 478  ASP B O   
4328 C  CB  A ASP B 254 ? 0.6071 0.6361 0.7455 -0.0225 -0.0816 -0.0792 478  ASP B CB  
4329 C  CG  A ASP B 254 ? 0.7258 0.7504 0.8442 -0.0168 -0.0807 -0.0764 478  ASP B CG  
4330 O  OD1 A ASP B 254 ? 0.6838 0.7010 0.7927 -0.0165 -0.0770 -0.0737 478  ASP B OD1 
4331 O  OD2 A ASP B 254 ? 0.7822 0.8105 0.8947 -0.0126 -0.0834 -0.0767 478  ASP B OD2 
4332 N  N   . THR B 255 ? 0.4896 0.5295 0.6660 -0.0361 -0.0696 -0.0737 479  THR B N   
4333 C  CA  . THR B 255 ? 0.4965 0.5421 0.6938 -0.0419 -0.0686 -0.0754 479  THR B CA  
4334 C  C   . THR B 255 ? 0.4666 0.5122 0.6698 -0.0465 -0.0586 -0.0685 479  THR B C   
4335 O  O   . THR B 255 ? 0.4828 0.5312 0.7029 -0.0520 -0.0564 -0.0692 479  THR B O   
4336 C  CB  . THR B 255 ? 0.5085 0.5654 0.7168 -0.0408 -0.0728 -0.0788 479  THR B CB  
4337 O  OG1 . THR B 255 ? 0.4593 0.5217 0.6663 -0.0400 -0.0662 -0.0732 479  THR B OG1 
4338 C  CG2 . THR B 255 ? 0.5378 0.5944 0.7357 -0.0346 -0.0821 -0.0841 479  THR B CG2 
4339 N  N   . GLY B 256 ? 0.4174 0.4602 0.6074 -0.0445 -0.0525 -0.0621 480  GLY B N   
4340 C  CA  . GLY B 256 ? 0.4202 0.4634 0.6140 -0.0481 -0.0432 -0.0555 480  GLY B CA  
4341 C  C   . GLY B 256 ? 0.4628 0.5163 0.6666 -0.0491 -0.0395 -0.0538 480  GLY B C   
4342 O  O   . GLY B 256 ? 0.4538 0.5076 0.6577 -0.0511 -0.0314 -0.0479 480  GLY B O   
4343 N  N   . ARG B 257 ? 0.3887 0.4503 0.6003 -0.0475 -0.0452 -0.0588 481  ARG B N   
4344 C  CA  . ARG B 257 ? 0.3637 0.4358 0.5875 -0.0485 -0.0420 -0.0580 481  ARG B CA  
4345 C  C   . ARG B 257 ? 0.3729 0.4481 0.5847 -0.0432 -0.0413 -0.0556 481  ARG B C   
4346 O  O   . ARG B 257 ? 0.3184 0.3886 0.5139 -0.0385 -0.0446 -0.0555 481  ARG B O   
4347 C  CB  . ARG B 257 ? 0.3333 0.4135 0.5754 -0.0501 -0.0485 -0.0649 481  ARG B CB  
4348 C  CG  . ARG B 257 ? 0.3964 0.4744 0.6534 -0.0563 -0.0482 -0.0671 481  ARG B CG  
4349 C  CD  . ARG B 257 ? 0.3473 0.4349 0.6252 -0.0585 -0.0538 -0.0737 481  ARG B CD  
4350 N  NE  . ARG B 257 ? 0.3668 0.4555 0.6397 -0.0535 -0.0649 -0.0803 481  ARG B NE  
4351 C  CZ  . ARG B 257 ? 0.3903 0.4728 0.6604 -0.0533 -0.0724 -0.0856 481  ARG B CZ  
4352 N  NH1 . ARG B 257 ? 0.4132 0.4875 0.6849 -0.0576 -0.0702 -0.0851 481  ARG B NH1 
4353 N  NH2 . ARG B 257 ? 0.3731 0.4572 0.6382 -0.0483 -0.0823 -0.0915 481  ARG B NH2 
4354 N  N   . ALA B 258 ? 0.2850 0.3683 0.5055 -0.0440 -0.0365 -0.0536 482  ALA B N   
4355 C  CA  . ALA B 258 ? 0.3288 0.4152 0.5397 -0.0394 -0.0348 -0.0511 482  ALA B CA  
4356 C  C   . ALA B 258 ? 0.3209 0.4118 0.5309 -0.0345 -0.0435 -0.0563 482  ALA B C   
4357 O  O   . ALA B 258 ? 0.3167 0.4143 0.5413 -0.0353 -0.0486 -0.0615 482  ALA B O   
4358 C  CB  . ALA B 258 ? 0.2848 0.3784 0.5060 -0.0417 -0.0269 -0.0479 482  ALA B CB  
4359 N  N   . LEU B 259 ? 0.2750 0.3621 0.4679 -0.0293 -0.0452 -0.0549 483  LEU B N   
4360 C  CA  . LEU B 259 ? 0.2897 0.3810 0.4803 -0.0240 -0.0519 -0.0584 483  LEU B CA  
4361 C  C   . LEU B 259 ? 0.2405 0.3396 0.4363 -0.0226 -0.0479 -0.0565 483  LEU B C   
4362 O  O   . LEU B 259 ? 0.2933 0.4002 0.4991 -0.0206 -0.0522 -0.0602 483  LEU B O   
4363 C  CB  . LEU B 259 ? 0.3137 0.3969 0.4840 -0.0192 -0.0552 -0.0576 483  LEU B CB  
4364 C  CG  . LEU B 259 ? 0.2676 0.3430 0.4313 -0.0195 -0.0597 -0.0600 483  LEU B CG  
4365 C  CD1 . LEU B 259 ? 0.3158 0.3827 0.4592 -0.0159 -0.0589 -0.0570 483  LEU B CD1 
4366 C  CD2 . LEU B 259 ? 0.3349 0.4128 0.5041 -0.0175 -0.0693 -0.0669 483  LEU B CD2 
4367 N  N   . PHE B 260 ? 0.2131 0.3102 0.4023 -0.0233 -0.0398 -0.0509 484  PHE B N   
4368 C  CA  . PHE B 260 ? 0.2441 0.3481 0.4391 -0.0228 -0.0345 -0.0489 484  PHE B CA  
4369 C  C   . PHE B 260 ? 0.2294 0.3291 0.4179 -0.0254 -0.0253 -0.0429 484  PHE B C   
4370 O  O   . PHE B 260 ? 0.2332 0.3249 0.4121 -0.0269 -0.0239 -0.0404 484  PHE B O   
4371 C  CB  . PHE B 260 ? 0.2030 0.3085 0.3896 -0.0166 -0.0381 -0.0497 484  PHE B CB  
4372 C  CG  . PHE B 260 ? 0.2662 0.3628 0.4323 -0.0135 -0.0377 -0.0464 484  PHE B CG  
4373 C  CD1 . PHE B 260 ? 0.2455 0.3354 0.4006 -0.0112 -0.0438 -0.0481 484  PHE B CD1 
4374 C  CD2 . PHE B 260 ? 0.2206 0.3155 0.3785 -0.0127 -0.0313 -0.0420 484  PHE B CD2 
4375 C  CE1 . PHE B 260 ? 0.2691 0.3514 0.4065 -0.0085 -0.0429 -0.0450 484  PHE B CE1 
4376 C  CE2 . PHE B 260 ? 0.2225 0.3097 0.3631 -0.0101 -0.0311 -0.0392 484  PHE B CE2 
4377 C  CZ  . PHE B 260 ? 0.2434 0.3245 0.3741 -0.0082 -0.0367 -0.0406 484  PHE B CZ  
4378 N  N   . GLU B 261 ? 0.2577 0.3630 0.4514 -0.0257 -0.0191 -0.0407 485  GLU B N   
4379 C  CA  . GLU B 261 ? 0.2101 0.3118 0.3967 -0.0274 -0.0104 -0.0351 485  GLU B CA  
4380 C  C   . GLU B 261 ? 0.2495 0.3517 0.4261 -0.0230 -0.0085 -0.0334 485  GLU B C   
4381 O  O   . GLU B 261 ? 0.2078 0.3159 0.3888 -0.0196 -0.0116 -0.0362 485  GLU B O   
4382 C  CB  . GLU B 261 ? 0.2389 0.3458 0.4403 -0.0321 -0.0031 -0.0336 485  GLU B CB  
4383 C  CG  . GLU B 261 ? 0.2860 0.3897 0.4948 -0.0374 -0.0025 -0.0336 485  GLU B CG  
4384 C  CD  . GLU B 261 ? 0.4678 0.5774 0.6931 -0.0421 0.0048  -0.0323 485  GLU B CD  
4385 O  OE1 . GLU B 261 ? 0.3409 0.4578 0.5724 -0.0411 0.0091  -0.0319 485  GLU B OE1 
4386 O  OE2 . GLU B 261 ? 0.4080 0.5146 0.6402 -0.0469 0.0064  -0.0316 485  GLU B OE2 
4387 N  N   . SER B 262 ? 0.2150 0.3109 0.3782 -0.0229 -0.0036 -0.0289 486  SER B N   
4388 C  CA  . SER B 262 ? 0.1924 0.2871 0.3445 -0.0191 -0.0017 -0.0271 486  SER B CA  
4389 C  C   . SER B 262 ? 0.2252 0.3180 0.3730 -0.0210 0.0068  -0.0225 486  SER B C   
4390 O  O   . SER B 262 ? 0.2624 0.3514 0.4097 -0.0247 0.0103  -0.0198 486  SER B O   
4391 C  CB  . SER B 262 ? 0.2368 0.3240 0.3731 -0.0161 -0.0065 -0.0268 486  SER B CB  
4392 O  OG  . SER B 262 ? 0.3377 0.4236 0.4642 -0.0127 -0.0049 -0.0253 486  SER B OG  
4393 N  N   . LYS B 263 ? 0.1948 0.2897 0.3387 -0.0183 0.0101  -0.0217 487  LYS B N   
4394 C  CA  . LYS B 263 ? 0.2098 0.3023 0.3471 -0.0193 0.0178  -0.0177 487  LYS B CA  
4395 C  C   . LYS B 263 ? 0.2494 0.3345 0.3691 -0.0167 0.0166  -0.0157 487  LYS B C   
4396 O  O   . LYS B 263 ? 0.2420 0.3272 0.3566 -0.0129 0.0136  -0.0173 487  LYS B O   
4397 C  CB  . LYS B 263 ? 0.1855 0.2852 0.3303 -0.0180 0.0229  -0.0183 487  LYS B CB  
4398 C  CG  . LYS B 263 ? 0.2669 0.3739 0.4292 -0.0216 0.0271  -0.0189 487  LYS B CG  
4399 C  CD  . LYS B 263 ? 0.2910 0.4075 0.4649 -0.0192 0.0287  -0.0217 487  LYS B CD  
4400 C  CE  . LYS B 263 ? 0.2768 0.3951 0.4500 -0.0194 0.0383  -0.0189 487  LYS B CE  
4401 N  NZ  . LYS B 263 ? 0.2586 0.3872 0.4462 -0.0176 0.0404  -0.0219 487  LYS B NZ  
4402 N  N   . LEU B 264 ? 0.2213 0.2997 0.3321 -0.0187 0.0187  -0.0122 488  LEU B N   
4403 C  CA  . LEU B 264 ? 0.2082 0.2798 0.3033 -0.0166 0.0180  -0.0102 488  LEU B CA  
4404 C  C   . LEU B 264 ? 0.2315 0.3025 0.3206 -0.0163 0.0246  -0.0075 488  LEU B C   
4405 O  O   . LEU B 264 ? 0.2043 0.2736 0.2929 -0.0188 0.0297  -0.0044 488  LEU B O   
4406 C  CB  . LEU B 264 ? 0.2109 0.2759 0.2997 -0.0184 0.0160  -0.0083 488  LEU B CB  
4407 C  CG  . LEU B 264 ? 0.2237 0.2820 0.2976 -0.0169 0.0156  -0.0059 488  LEU B CG  
4408 C  CD1 . LEU B 264 ? 0.1923 0.2504 0.2601 -0.0133 0.0120  -0.0079 488  LEU B CD1 
4409 C  CD2 . LEU B 264 ? 0.2270 0.2798 0.2971 -0.0183 0.0129  -0.0046 488  LEU B CD2 
4410 N  N   . HIS B 265 ? 0.2113 0.2832 0.2955 -0.0129 0.0245  -0.0087 489  HIS B N   
4411 C  CA  . HIS B 265 ? 0.2215 0.2931 0.3000 -0.0121 0.0305  -0.0069 489  HIS B CA  
4412 C  C   . HIS B 265 ? 0.1956 0.2595 0.2592 -0.0119 0.0307  -0.0041 489  HIS B C   
4413 O  O   . HIS B 265 ? 0.2114 0.2711 0.2683 -0.0109 0.0257  -0.0044 489  HIS B O   
4414 C  CB  . HIS B 265 ? 0.2233 0.2984 0.3025 -0.0084 0.0302  -0.0097 489  HIS B CB  
4415 C  CG  . HIS B 265 ? 0.2112 0.2945 0.3056 -0.0081 0.0300  -0.0126 489  HIS B CG  
4416 N  ND1 . HIS B 265 ? 0.2479 0.3371 0.3510 -0.0087 0.0363  -0.0126 489  HIS B ND1 
4417 C  CD2 . HIS B 265 ? 0.2233 0.3100 0.3261 -0.0074 0.0243  -0.0156 489  HIS B CD2 
4418 C  CE1 . HIS B 265 ? 0.2582 0.3547 0.3755 -0.0083 0.0342  -0.0157 489  HIS B CE1 
4419 N  NE2 . HIS B 265 ? 0.2663 0.3614 0.3834 -0.0074 0.0266  -0.0176 489  HIS B NE2 
4420 N  N   . LYS B 266 ? 0.2042 0.2664 0.2629 -0.0127 0.0367  -0.0012 490  LYS B N   
4421 C  CA  . LYS B 266 ? 0.2418 0.2969 0.2869 -0.0126 0.0369  0.0017  490  LYS B CA  
4422 C  C   . LYS B 266 ? 0.2516 0.3035 0.2868 -0.0096 0.0327  0.0001  490  LYS B C   
4423 O  O   . LYS B 266 ? 0.2247 0.2714 0.2517 -0.0097 0.0296  0.0014  490  LYS B O   
4424 C  CB  . LYS B 266 ? 0.2838 0.3378 0.3243 -0.0130 0.0442  0.0046  490  LYS B CB  
4425 C  CG  . LYS B 266 ? 0.3458 0.3925 0.3713 -0.0123 0.0444  0.0076  490  LYS B CG  
4426 C  CD  . LYS B 266 ? 0.3453 0.3909 0.3654 -0.0122 0.0519  0.0104  490  LYS B CD  
4427 C  CE  . LYS B 266 ? 0.4243 0.4627 0.4283 -0.0107 0.0514  0.0128  490  LYS B CE  
4428 N  NZ  . LYS B 266 ? 0.4533 0.4902 0.4501 -0.0098 0.0587  0.0153  490  LYS B NZ  
4429 N  N   . GLN B 267 ? 0.2476 0.3023 0.2839 -0.0071 0.0325  -0.0027 491  GLN B N   
4430 C  CA  . GLN B 267 ? 0.2609 0.3119 0.2881 -0.0046 0.0287  -0.0041 491  GLN B CA  
4431 C  C   . GLN B 267 ? 0.2357 0.2857 0.2646 -0.0044 0.0223  -0.0056 491  GLN B C   
4432 O  O   . GLN B 267 ? 0.2661 0.3127 0.2884 -0.0027 0.0192  -0.0066 491  GLN B O   
4433 C  CB  . GLN B 267 ? 0.3472 0.4005 0.3740 -0.0017 0.0308  -0.0065 491  GLN B CB  
4434 C  CG  . GLN B 267 ? 0.3652 0.4174 0.3856 -0.0012 0.0369  -0.0051 491  GLN B CG  
4435 C  CD  . GLN B 267 ? 0.4381 0.4838 0.4456 -0.0017 0.0364  -0.0026 491  GLN B CD  
4436 O  OE1 . GLN B 267 ? 0.4362 0.4803 0.4421 -0.0038 0.0388  0.0006  491  GLN B OE1 
4437 N  NE2 . GLN B 267 ? 0.4294 0.4711 0.4280 0.0002  0.0332  -0.0042 491  GLN B NE2 
4438 N  N   . GLY B 268 ? 0.2313 0.2837 0.2688 -0.0061 0.0205  -0.0057 492  GLY B N   
4439 C  CA  . GLY B 268 ? 0.1967 0.2469 0.2337 -0.0061 0.0150  -0.0065 492  GLY B CA  
4440 C  C   . GLY B 268 ? 0.2472 0.3005 0.2906 -0.0043 0.0113  -0.0094 492  GLY B C   
4441 O  O   . GLY B 268 ? 0.2381 0.2884 0.2767 -0.0026 0.0075  -0.0103 492  GLY B O   
4442 N  N   . PHE B 269 ? 0.2269 0.2859 0.2809 -0.0045 0.0123  -0.0109 493  PHE B N   
4443 C  CA  . PHE B 269 ? 0.2275 0.2896 0.2881 -0.0028 0.0080  -0.0138 493  PHE B CA  
4444 C  C   . PHE B 269 ? 0.2229 0.2910 0.2965 -0.0047 0.0087  -0.0149 493  PHE B C   
4445 O  O   . PHE B 269 ? 0.1939 0.2641 0.2718 -0.0071 0.0136  -0.0134 493  PHE B O   
4446 C  CB  . PHE B 269 ? 0.2022 0.2657 0.2620 0.0008  0.0076  -0.0158 493  PHE B CB  
4447 C  CG  . PHE B 269 ? 0.2044 0.2729 0.2698 0.0013  0.0127  -0.0163 493  PHE B CG  
4448 C  CD1 . PHE B 269 ? 0.2330 0.2995 0.2920 0.0008  0.0177  -0.0145 493  PHE B CD1 
4449 C  CD2 . PHE B 269 ? 0.2138 0.2892 0.2910 0.0026  0.0123  -0.0188 493  PHE B CD2 
4450 C  CE1 . PHE B 269 ? 0.2416 0.3124 0.3050 0.0015  0.0229  -0.0150 493  PHE B CE1 
4451 C  CE2 . PHE B 269 ? 0.2179 0.2983 0.3010 0.0032  0.0174  -0.0194 493  PHE B CE2 
4452 C  CZ  . PHE B 269 ? 0.2410 0.3190 0.3170 0.0027  0.0230  -0.0174 493  PHE B CZ  
4453 N  N   . MET B 270 ? 0.2177 0.2883 0.2975 -0.0036 0.0038  -0.0175 494  MET B N   
4454 C  CA  . MET B 270 ? 0.2243 0.3003 0.3170 -0.0056 0.0029  -0.0192 494  MET B CA  
4455 C  C   . MET B 270 ? 0.1946 0.2773 0.2969 -0.0029 0.0011  -0.0224 494  MET B C   
4456 O  O   . MET B 270 ? 0.2470 0.3285 0.3451 0.0008  -0.0027 -0.0239 494  MET B O   
4457 C  CB  . MET B 270 ? 0.1948 0.2676 0.2867 -0.0066 -0.0022 -0.0199 494  MET B CB  
4458 C  CG  . MET B 270 ? 0.2647 0.3319 0.3501 -0.0095 -0.0001 -0.0168 494  MET B CG  
4459 S  SD  . MET B 270 ? 0.3985 0.4610 0.4806 -0.0099 -0.0059 -0.0178 494  MET B SD  
4460 C  CE  . MET B 270 ? 0.1995 0.2684 0.2963 -0.0105 -0.0096 -0.0219 494  MET B CE  
4461 N  N   . THR B 271 ? 0.1887 0.2785 0.3045 -0.0048 0.0038  -0.0235 495  THR B N   
4462 C  CA  . THR B 271 ? 0.2158 0.3131 0.3434 -0.0025 0.0013  -0.0270 495  THR B CA  
4463 C  C   . THR B 271 ? 0.1940 0.2960 0.3348 -0.0050 -0.0020 -0.0294 495  THR B C   
4464 O  O   . THR B 271 ? 0.2144 0.3148 0.3575 -0.0092 -0.0001 -0.0279 495  THR B O   
4465 C  CB  . THR B 271 ? 0.2204 0.3237 0.3549 -0.0019 0.0076  -0.0270 495  THR B CB  
4466 O  OG1 . THR B 271 ? 0.2358 0.3412 0.3762 -0.0062 0.0141  -0.0248 495  THR B OG1 
4467 C  CG2 . THR B 271 ? 0.2516 0.3504 0.3735 0.0012  0.0100  -0.0256 495  THR B CG2 
4468 N  N   . ILE B 272 ? 0.1790 0.2863 0.3283 -0.0023 -0.0074 -0.0331 496  ILE B N   
4469 C  CA  . ILE B 272 ? 0.2155 0.3284 0.3789 -0.0042 -0.0115 -0.0364 496  ILE B CA  
4470 C  C   . ILE B 272 ? 0.2232 0.3461 0.4012 -0.0018 -0.0121 -0.0396 496  ILE B C   
4471 O  O   . ILE B 272 ? 0.1956 0.3196 0.3705 0.0021  -0.0110 -0.0396 496  ILE B O   
4472 C  CB  . ILE B 272 ? 0.2181 0.3265 0.3755 -0.0026 -0.0199 -0.0385 496  ILE B CB  
4473 C  CG1 . ILE B 272 ? 0.2502 0.3553 0.3968 0.0032  -0.0241 -0.0390 496  ILE B CG1 
4474 C  CG2 . ILE B 272 ? 0.2289 0.3291 0.3764 -0.0057 -0.0191 -0.0359 496  ILE B CG2 
4475 C  CD1 . ILE B 272 ? 0.1885 0.2917 0.3323 0.0061  -0.0328 -0.0419 496  ILE B CD1 
4476 N  N   . ALA B 273 ? 0.1908 0.3209 0.3854 -0.0043 -0.0140 -0.0425 497  ALA B N   
4477 C  CA  . ALA B 273 ? 0.1962 0.3366 0.4065 -0.0019 -0.0161 -0.0463 497  ALA B CA  
4478 C  C   . ALA B 273 ? 0.2206 0.3604 0.4283 0.0028  -0.0264 -0.0499 497  ALA B C   
4479 O  O   . ALA B 273 ? 0.2536 0.3932 0.4650 0.0016  -0.0327 -0.0525 497  ALA B O   
4480 C  CB  . ALA B 273 ? 0.2666 0.4155 0.4972 -0.0067 -0.0136 -0.0480 497  ALA B CB  
4481 N  N   . SER B 274 ? 0.2468 0.3856 0.4473 0.0084  -0.0283 -0.0501 498  SER B N   
4482 C  CA  . SER B 274 ? 0.2267 0.3638 0.4227 0.0134  -0.0378 -0.0529 498  SER B CA  
4483 C  C   . SER B 274 ? 0.2784 0.4170 0.4722 0.0193  -0.0381 -0.0532 498  SER B C   
4484 O  O   . SER B 274 ? 0.2821 0.4211 0.4743 0.0195  -0.0310 -0.0510 498  SER B O   
4485 C  CB  . SER B 274 ? 0.2675 0.3932 0.4450 0.0137  -0.0412 -0.0511 498  SER B CB  
4486 O  OG  . SER B 274 ? 0.3130 0.4375 0.4878 0.0176  -0.0506 -0.0542 498  SER B OG  
4487 N  N   . SER B 275 ? 0.2987 0.4377 0.4917 0.0245  -0.0465 -0.0561 499  SER B N   
4488 C  CA  . SER B 275 ? 0.3183 0.4585 0.5099 0.0306  -0.0477 -0.0566 499  SER B CA  
4489 C  C   . SER B 275 ? 0.3135 0.4456 0.4906 0.0359  -0.0556 -0.0568 499  SER B C   
4490 O  O   . SER B 275 ? 0.3529 0.4853 0.5312 0.0367  -0.0633 -0.0594 499  SER B O   
4491 C  CB  . SER B 275 ? 0.2745 0.4275 0.4871 0.0323  -0.0494 -0.0606 499  SER B CB  
4492 O  OG  . SER B 275 ? 0.3850 0.5390 0.5965 0.0385  -0.0501 -0.0610 499  SER B OG  
4493 N  N   . GLY B 276 ? 0.3035 0.4283 0.4670 0.0394  -0.0538 -0.0541 500  GLY B N   
4494 C  CA  . GLY B 276 ? 0.3148 0.4313 0.4640 0.0446  -0.0602 -0.0537 500  GLY B CA  
4495 C  C   . GLY B 276 ? 0.3294 0.4343 0.4602 0.0426  -0.0585 -0.0500 500  GLY B C   
4496 O  O   . GLY B 276 ? 0.2309 0.3338 0.3592 0.0374  -0.0526 -0.0477 500  GLY B O   
4497 N  N   . ASP B 277 ? 0.2908 0.3879 0.4085 0.0471  -0.0639 -0.0493 501  ASP B N   
4498 C  CA  . ASP B 277 ? 0.3204 0.4061 0.4201 0.0462  -0.0626 -0.0458 501  ASP B CA  
4499 C  C   . ASP B 277 ? 0.3368 0.4196 0.4316 0.0466  -0.0691 -0.0473 501  ASP B C   
4500 O  O   . ASP B 277 ? 0.3126 0.3942 0.4044 0.0517  -0.0762 -0.0490 501  ASP B O   
4501 C  CB  . ASP B 277 ? 0.3076 0.3853 0.3950 0.0511  -0.0624 -0.0434 501  ASP B CB  
4502 C  CG  . ASP B 277 ? 0.3603 0.4382 0.4489 0.0500  -0.0552 -0.0416 501  ASP B CG  
4503 O  OD1 . ASP B 277 ? 0.3296 0.4163 0.4318 0.0499  -0.0531 -0.0436 501  ASP B OD1 
4504 O  OD2 . ASP B 277 ? 0.4720 0.5412 0.5480 0.0494  -0.0516 -0.0383 501  ASP B OD2 
4505 N  N   . HIS B 278 ? 0.2801 0.3613 0.3732 0.0415  -0.0669 -0.0466 502  HIS B N   
4506 C  CA  . HIS B 278 ? 0.2974 0.3763 0.3868 0.0415  -0.0727 -0.0485 502  HIS B CA  
4507 C  C   . HIS B 278 ? 0.3333 0.4086 0.4186 0.0358  -0.0682 -0.0467 502  HIS B C   
4508 O  O   . HIS B 278 ? 0.2051 0.2829 0.2958 0.0314  -0.0616 -0.0450 502  HIS B O   
4509 C  CB  . HIS B 278 ? 0.2988 0.3873 0.4040 0.0419  -0.0788 -0.0536 502  HIS B CB  
4510 C  CG  . HIS B 278 ? 0.3494 0.4474 0.4722 0.0368  -0.0741 -0.0548 502  HIS B CG  
4511 N  ND1 . HIS B 278 ? 0.3454 0.4443 0.4726 0.0308  -0.0711 -0.0548 502  HIS B ND1 
4512 C  CD2 . HIS B 278 ? 0.3207 0.4276 0.4578 0.0369  -0.0716 -0.0559 502  HIS B CD2 
4513 C  CE1 . HIS B 278 ? 0.3458 0.4533 0.4889 0.0272  -0.0668 -0.0555 502  HIS B CE1 
4514 N  NE2 . HIS B 278 ? 0.3176 0.4303 0.4670 0.0308  -0.0668 -0.0563 502  HIS B NE2 
4515 N  N   . PRO B 279 ? 0.2922 0.3613 0.3675 0.0362  -0.0717 -0.0469 503  PRO B N   
4516 C  CA  . PRO B 279 ? 0.2729 0.3390 0.3455 0.0312  -0.0680 -0.0456 503  PRO B CA  
4517 C  C   . PRO B 279 ? 0.2714 0.3452 0.3597 0.0267  -0.0684 -0.0486 503  PRO B C   
4518 O  O   . PRO B 279 ? 0.2583 0.3394 0.3589 0.0278  -0.0728 -0.0524 503  PRO B O   
4519 C  CB  . PRO B 279 ? 0.2395 0.2975 0.2979 0.0338  -0.0724 -0.0458 503  PRO B CB  
4520 C  CG  . PRO B 279 ? 0.3258 0.3838 0.3816 0.0399  -0.0794 -0.0480 503  PRO B CG  
4521 C  CD  . PRO B 279 ? 0.3103 0.3737 0.3742 0.0418  -0.0783 -0.0478 503  PRO B CD  
4522 N  N   . ILE B 280 ? 0.2644 0.3364 0.3526 0.0217  -0.0635 -0.0468 504  ILE B N   
4523 C  CA  . ILE B 280 ? 0.2725 0.3491 0.3730 0.0170  -0.0634 -0.0491 504  ILE B CA  
4524 C  C   . ILE B 280 ? 0.3256 0.3952 0.4168 0.0164  -0.0660 -0.0497 504  ILE B C   
4525 O  O   . ILE B 280 ? 0.3247 0.3887 0.4077 0.0141  -0.0614 -0.0464 504  ILE B O   
4526 C  CB  . ILE B 280 ? 0.2784 0.3576 0.3855 0.0120  -0.0552 -0.0461 504  ILE B CB  
4527 C  CG1 . ILE B 280 ? 0.2790 0.3630 0.3906 0.0135  -0.0515 -0.0448 504  ILE B CG1 
4528 C  CG2 . ILE B 280 ? 0.2273 0.3116 0.3487 0.0070  -0.0547 -0.0483 504  ILE B CG2 
4529 C  CD1 . ILE B 280 ? 0.3155 0.4096 0.4444 0.0135  -0.0533 -0.0482 504  ILE B CD1 
4530 N  N   . ILE B 281 ? 0.3324 0.4022 0.4243 0.0186  -0.0735 -0.0540 505  ILE B N   
4531 C  CA  . ILE B 281 ? 0.4296 0.4924 0.5120 0.0187  -0.0764 -0.0551 505  ILE B CA  
4532 C  C   . ILE B 281 ? 0.3639 0.4301 0.4588 0.0140  -0.0776 -0.0584 505  ILE B C   
4533 O  O   . ILE B 281 ? 0.3743 0.4479 0.4837 0.0132  -0.0813 -0.0622 505  ILE B O   
4534 C  CB  . ILE B 281 ? 0.5337 0.5928 0.6057 0.0248  -0.0841 -0.0577 505  ILE B CB  
4535 C  CG1 . ILE B 281 ? 0.4581 0.5129 0.5176 0.0292  -0.0823 -0.0539 505  ILE B CG1 
4536 C  CG2 . ILE B 281 ? 0.4982 0.5498 0.5596 0.0250  -0.0864 -0.0590 505  ILE B CG2 
4537 C  CD1 . ILE B 281 ? 0.4473 0.4948 0.4946 0.0277  -0.0754 -0.0490 505  ILE B CD1 
4538 N  N   . MET B 282 ? 0.3890 0.4497 0.4789 0.0110  -0.0744 -0.0569 506  MET B N   
4539 C  CA  . MET B 282 ? 0.3787 0.4407 0.4792 0.0060  -0.0742 -0.0590 506  MET B CA  
4540 C  C   . MET B 282 ? 0.3858 0.4399 0.4761 0.0068  -0.0772 -0.0608 506  MET B C   
4541 O  O   . MET B 282 ? 0.4057 0.4533 0.4803 0.0105  -0.0774 -0.0591 506  MET B O   
4542 C  CB  . MET B 282 ? 0.3270 0.3899 0.4326 0.0011  -0.0655 -0.0546 506  MET B CB  
4543 C  CG  . MET B 282 ? 0.3770 0.4482 0.4946 -0.0002 -0.0622 -0.0535 506  MET B CG  
4544 S  SD  . MET B 282 ? 0.3623 0.4426 0.5014 -0.0030 -0.0665 -0.0590 506  MET B SD  
4545 C  CE  . MET B 282 ? 0.3634 0.4526 0.5101 0.0001  -0.0664 -0.0591 506  MET B CE  
4546 N  N   . PRO B 283 ? 0.3609 0.4153 0.4600 0.0033  -0.0793 -0.0642 507  PRO B N   
4547 C  CA  . PRO B 283 ? 0.3747 0.4208 0.4643 0.0034  -0.0805 -0.0653 507  PRO B CA  
4548 C  C   . PRO B 283 ? 0.3581 0.3983 0.4359 0.0031  -0.0734 -0.0596 507  PRO B C   
4549 O  O   . PRO B 283 ? 0.3396 0.3820 0.4215 0.0002  -0.0669 -0.0553 507  PRO B O   
4550 C  CB  . PRO B 283 ? 0.3163 0.3645 0.4207 -0.0020 -0.0810 -0.0682 507  PRO B CB  
4551 C  CG  . PRO B 283 ? 0.3366 0.3942 0.4571 -0.0029 -0.0844 -0.0714 507  PRO B CG  
4552 C  CD  . PRO B 283 ? 0.3384 0.4005 0.4569 -0.0006 -0.0810 -0.0676 507  PRO B CD  
4553 N  N   . THR B 284 ? 0.3366 0.3693 0.3995 0.0064  -0.0748 -0.0597 508  THR B N   
4554 C  CA  . THR B 284 ? 0.4061 0.4340 0.4574 0.0072  -0.0687 -0.0544 508  THR B CA  
4555 C  C   . THR B 284 ? 0.3415 0.3675 0.3964 0.0027  -0.0629 -0.0515 508  THR B C   
4556 O  O   . THR B 284 ? 0.3164 0.3403 0.3651 0.0026  -0.0574 -0.0469 508  THR B O   
4557 C  CB  . THR B 284 ? 0.4102 0.4308 0.4452 0.0119  -0.0710 -0.0552 508  THR B CB  
4558 O  OG1 . THR B 284 ? 0.4458 0.4623 0.4804 0.0114  -0.0742 -0.0592 508  THR B OG1 
4559 C  CG2 . THR B 284 ? 0.3950 0.4163 0.4238 0.0169  -0.0762 -0.0570 508  THR B CG2 
4560 N  N   . ASN B 285 ? 0.3498 0.3762 0.4147 -0.0009 -0.0640 -0.0542 509  ASN B N   
4561 C  CA  . ASN B 285 ? 0.3248 0.3486 0.3929 -0.0049 -0.0587 -0.0512 509  ASN B CA  
4562 C  C   . ASN B 285 ? 0.3221 0.3516 0.4022 -0.0091 -0.0540 -0.0483 509  ASN B C   
4563 O  O   . ASN B 285 ? 0.3265 0.3539 0.4096 -0.0125 -0.0494 -0.0455 509  ASN B O   
4564 C  CB  . ASN B 285 ? 0.3809 0.4005 0.4527 -0.0066 -0.0617 -0.0552 509  ASN B CB  
4565 C  CG  . ASN B 285 ? 0.5101 0.5225 0.5682 -0.0026 -0.0644 -0.0572 509  ASN B CG  
4566 O  OD1 . ASN B 285 ? 0.5711 0.5807 0.6171 0.0005  -0.0619 -0.0542 509  ASN B OD1 
4567 N  ND2 . ASN B 285 ? 0.6214 0.6305 0.6816 -0.0028 -0.0692 -0.0624 509  ASN B ND2 
4568 N  N   . GLY B 286 ? 0.2864 0.3228 0.3732 -0.0087 -0.0550 -0.0489 510  GLY B N   
4569 C  CA  . GLY B 286 ? 0.2855 0.3274 0.3831 -0.0124 -0.0500 -0.0461 510  GLY B CA  
4570 C  C   . GLY B 286 ? 0.2901 0.3299 0.3802 -0.0127 -0.0433 -0.0403 510  GLY B C   
4571 O  O   . GLY B 286 ? 0.2640 0.3003 0.3419 -0.0095 -0.0428 -0.0384 510  GLY B O   
4572 N  N   . TYR B 287 ? 0.2515 0.2932 0.3492 -0.0167 -0.0380 -0.0374 511  TYR B N   
4573 C  CA  . TYR B 287 ? 0.2814 0.3214 0.3728 -0.0171 -0.0319 -0.0320 511  TYR B CA  
4574 C  C   . TYR B 287 ? 0.2577 0.3029 0.3592 -0.0203 -0.0270 -0.0299 511  TYR B C   
4575 O  O   . TYR B 287 ? 0.2491 0.2975 0.3630 -0.0234 -0.0272 -0.0318 511  TYR B O   
4576 C  CB  . TYR B 287 ? 0.2944 0.3272 0.3793 -0.0181 -0.0298 -0.0297 511  TYR B CB  
4577 C  CG  . TYR B 287 ? 0.2945 0.3256 0.3887 -0.0222 -0.0288 -0.0302 511  TYR B CG  
4578 C  CD1 . TYR B 287 ? 0.3274 0.3567 0.4263 -0.0227 -0.0336 -0.0348 511  TYR B CD1 
4579 C  CD2 . TYR B 287 ? 0.3055 0.3360 0.4032 -0.0254 -0.0230 -0.0260 511  TYR B CD2 
4580 C  CE1 . TYR B 287 ? 0.4023 0.4294 0.5102 -0.0267 -0.0327 -0.0353 511  TYR B CE1 
4581 C  CE2 . TYR B 287 ? 0.3401 0.3681 0.4461 -0.0293 -0.0216 -0.0260 511  TYR B CE2 
4582 C  CZ  . TYR B 287 ? 0.4219 0.4482 0.5334 -0.0301 -0.0264 -0.0307 511  TYR B CZ  
4583 O  OH  . TYR B 287 ? 0.4454 0.4687 0.5658 -0.0342 -0.0250 -0.0308 511  TYR B OH  
4584 N  N   . PHE B 288 ? 0.2883 0.3342 0.3844 -0.0197 -0.0225 -0.0260 512  PHE B N   
4585 C  CA  . PHE B 288 ? 0.2340 0.2837 0.3372 -0.0224 -0.0169 -0.0234 512  PHE B CA  
4586 C  C   . PHE B 288 ? 0.2867 0.3317 0.3900 -0.0258 -0.0126 -0.0201 512  PHE B C   
4587 O  O   . PHE B 288 ? 0.2677 0.3065 0.3618 -0.0250 -0.0126 -0.0182 512  PHE B O   
4588 C  CB  . PHE B 288 ? 0.2227 0.2740 0.3190 -0.0202 -0.0137 -0.0208 512  PHE B CB  
4589 C  CG  . PHE B 288 ? 0.2125 0.2692 0.3111 -0.0173 -0.0166 -0.0235 512  PHE B CG  
4590 C  CD1 . PHE B 288 ? 0.2417 0.3055 0.3525 -0.0183 -0.0157 -0.0252 512  PHE B CD1 
4591 C  CD2 . PHE B 288 ? 0.2256 0.2800 0.3142 -0.0134 -0.0199 -0.0241 512  PHE B CD2 
4592 C  CE1 . PHE B 288 ? 0.1947 0.2635 0.3078 -0.0152 -0.0185 -0.0277 512  PHE B CE1 
4593 C  CE2 . PHE B 288 ? 0.2372 0.2957 0.3273 -0.0104 -0.0226 -0.0263 512  PHE B CE2 
4594 C  CZ  . PHE B 288 ? 0.2123 0.2780 0.3146 -0.0111 -0.0222 -0.0282 512  PHE B CZ  
4595 N  N   . ARG B 289 ? 0.2370 0.2851 0.3510 -0.0293 -0.0087 -0.0191 513  ARG B N   
4596 C  CA  . ARG B 289 ? 0.2773 0.3210 0.3922 -0.0327 -0.0037 -0.0154 513  ARG B CA  
4597 C  C   . ARG B 289 ? 0.2575 0.3053 0.3768 -0.0344 0.0029  -0.0123 513  ARG B C   
4598 O  O   . ARG B 289 ? 0.2915 0.3463 0.4210 -0.0351 0.0033  -0.0144 513  ARG B O   
4599 C  CB  . ARG B 289 ? 0.2571 0.2991 0.3822 -0.0359 -0.0057 -0.0178 513  ARG B CB  
4600 C  CG  . ARG B 289 ? 0.3271 0.3649 0.4558 -0.0399 -0.0003 -0.0140 513  ARG B CG  
4601 C  CD  . ARG B 289 ? 0.4269 0.4627 0.5665 -0.0432 -0.0030 -0.0173 513  ARG B CD  
4602 N  NE  . ARG B 289 ? 0.4289 0.4716 0.5849 -0.0466 -0.0018 -0.0194 513  ARG B NE  
4603 C  CZ  . ARG B 289 ? 0.4870 0.5300 0.6552 -0.0496 -0.0048 -0.0233 513  ARG B CZ  
4604 N  NH1 . ARG B 289 ? 0.4638 0.5002 0.6290 -0.0494 -0.0094 -0.0257 513  ARG B NH1 
4605 N  NH2 . ARG B 289 ? 0.4369 0.4871 0.6212 -0.0528 -0.0033 -0.0251 513  ARG B NH2 
4606 N  N   . PHE B 290 ? 0.2365 0.2799 0.3479 -0.0348 0.0079  -0.0073 514  PHE B N   
4607 C  CA  . PHE B 290 ? 0.2301 0.2762 0.3443 -0.0364 0.0148  -0.0041 514  PHE B CA  
4608 C  C   . PHE B 290 ? 0.3194 0.3672 0.4478 -0.0410 0.0181  -0.0040 514  PHE B C   
4609 O  O   . PHE B 290 ? 0.2388 0.2813 0.3696 -0.0435 0.0179  -0.0033 514  PHE B O   
4610 C  CB  . PHE B 290 ? 0.2551 0.2952 0.3567 -0.0357 0.0189  0.0011  514  PHE B CB  
4611 C  CG  . PHE B 290 ? 0.2766 0.3181 0.3795 -0.0373 0.0264  0.0048  514  PHE B CG  
4612 C  CD1 . PHE B 290 ? 0.2674 0.3155 0.3727 -0.0360 0.0288  0.0039  514  PHE B CD1 
4613 C  CD2 . PHE B 290 ? 0.3095 0.3453 0.4108 -0.0397 0.0312  0.0093  514  PHE B CD2 
4614 C  CE1 . PHE B 290 ? 0.2776 0.3269 0.3834 -0.0372 0.0362  0.0072  514  PHE B CE1 
4615 C  CE2 . PHE B 290 ? 0.3110 0.3476 0.4124 -0.0410 0.0386  0.0130  514  PHE B CE2 
4616 C  CZ  . PHE B 290 ? 0.3097 0.3532 0.4132 -0.0397 0.0413  0.0119  514  PHE B CZ  
4617 N  N   . GLU B 291 ? 0.2512 0.3065 0.3898 -0.0422 0.0215  -0.0048 515  GLU B N   
4618 C  CA  . GLU B 291 ? 0.2586 0.3169 0.4128 -0.0467 0.0252  -0.0050 515  GLU B CA  
4619 C  C   . GLU B 291 ? 0.2786 0.3360 0.4323 -0.0488 0.0345  0.0004  515  GLU B C   
4620 O  O   . GLU B 291 ? 0.2405 0.2931 0.3977 -0.0525 0.0384  0.0033  515  GLU B O   
4621 C  CB  . GLU B 291 ? 0.2305 0.2989 0.3991 -0.0467 0.0222  -0.0102 515  GLU B CB  
4622 C  CG  . GLU B 291 ? 0.3654 0.4367 0.5519 -0.0512 0.0215  -0.0130 515  GLU B CG  
4623 C  CD  . GLU B 291 ? 0.4678 0.5327 0.6530 -0.0521 0.0152  -0.0153 515  GLU B CD  
4624 O  OE1 . GLU B 291 ? 0.4591 0.5202 0.6320 -0.0483 0.0097  -0.0166 515  GLU B OE1 
4625 O  OE2 . GLU B 291 ? 0.4610 0.5243 0.6575 -0.0565 0.0160  -0.0159 515  GLU B OE2 
4626 N  N   . ALA B 292 ? 0.2828 0.3440 0.4315 -0.0465 0.0383  0.0018  516  ALA B N   
4627 C  CA  . ALA B 292 ? 0.2538 0.3151 0.4027 -0.0482 0.0476  0.0064  516  ALA B CA  
4628 C  C   . ALA B 292 ? 0.2521 0.3159 0.3909 -0.0442 0.0500  0.0072  516  ALA B C   
4629 O  O   . ALA B 292 ? 0.2591 0.3270 0.3964 -0.0408 0.0450  0.0035  516  ALA B O   
4630 C  CB  . ALA B 292 ? 0.2429 0.3113 0.4113 -0.0523 0.0519  0.0051  516  ALA B CB  
4631 N  N   . TRP B 293 ? 0.2412 0.3024 0.3736 -0.0445 0.0579  0.0120  517  TRP B N   
4632 C  CA  . TRP B 293 ? 0.2676 0.3319 0.3929 -0.0413 0.0618  0.0127  517  TRP B CA  
4633 C  C   . TRP B 293 ? 0.2775 0.3515 0.4183 -0.0426 0.0665  0.0107  517  TRP B C   
4634 O  O   . TRP B 293 ? 0.2276 0.3032 0.3796 -0.0466 0.0724  0.0125  517  TRP B O   
4635 C  CB  . TRP B 293 ? 0.2485 0.3054 0.3591 -0.0408 0.0681  0.0185  517  TRP B CB  
4636 C  CG  . TRP B 293 ? 0.2802 0.3286 0.3761 -0.0390 0.0632  0.0202  517  TRP B CG  
4637 C  CD1 . TRP B 293 ? 0.3088 0.3492 0.4005 -0.0409 0.0633  0.0237  517  TRP B CD1 
4638 C  CD2 . TRP B 293 ? 0.2708 0.3179 0.3547 -0.0348 0.0575  0.0183  517  TRP B CD2 
4639 N  NE1 . TRP B 293 ? 0.2799 0.3148 0.3583 -0.0379 0.0578  0.0240  517  TRP B NE1 
4640 C  CE2 . TRP B 293 ? 0.2980 0.3369 0.3717 -0.0344 0.0543  0.0207  517  TRP B CE2 
4641 C  CE3 . TRP B 293 ? 0.2675 0.3193 0.3491 -0.0315 0.0548  0.0149  517  TRP B CE3 
4642 C  CZ2 . TRP B 293 ? 0.2869 0.3231 0.3489 -0.0311 0.0487  0.0197  517  TRP B CZ2 
4643 C  CZ3 . TRP B 293 ? 0.2753 0.3235 0.3447 -0.0283 0.0494  0.0140  517  TRP B CZ3 
4644 C  CH2 . TRP B 293 ? 0.3053 0.3461 0.3654 -0.0282 0.0464  0.0164  517  TRP B CH2 
4645 N  N   . VAL B 294 ? 0.2216 0.3020 0.3634 -0.0391 0.0642  0.0071  518  VAL B N   
4646 C  CA  . VAL B 294 ? 0.2174 0.3076 0.3739 -0.0395 0.0686  0.0049  518  VAL B CA  
4647 C  C   . VAL B 294 ? 0.2783 0.3702 0.4251 -0.0350 0.0715  0.0048  518  VAL B C   
4648 O  O   . VAL B 294 ? 0.2833 0.3683 0.4124 -0.0324 0.0709  0.0070  518  VAL B O   
4649 C  CB  . VAL B 294 ? 0.2223 0.3204 0.3950 -0.0398 0.0615  -0.0009 518  VAL B CB  
4650 C  CG1 . VAL B 294 ? 0.2687 0.3646 0.4509 -0.0443 0.0586  -0.0013 518  VAL B CG1 
4651 C  CG2 . VAL B 294 ? 0.2205 0.3180 0.3845 -0.0352 0.0529  -0.0044 518  VAL B CG2 
4652 N  N   . ASN B 295 ? 0.2791 0.3802 0.4376 -0.0340 0.0744  0.0022  519  ASN B N   
4653 C  CA  . ASN B 295 ? 0.2526 0.3554 0.4026 -0.0295 0.0768  0.0015  519  ASN B CA  
4654 C  C   . ASN B 295 ? 0.2831 0.3924 0.4397 -0.0260 0.0698  -0.0040 519  ASN B C   
4655 O  O   . ASN B 295 ? 0.2303 0.3423 0.3963 -0.0269 0.0627  -0.0072 519  ASN B O   
4656 C  CB  . ASN B 295 ? 0.2480 0.3547 0.4026 -0.0302 0.0880  0.0039  519  ASN B CB  
4657 C  CG  . ASN B 295 ? 0.2622 0.3801 0.4404 -0.0326 0.0908  0.0013  519  ASN B CG  
4658 O  OD1 . ASN B 295 ? 0.2852 0.4094 0.4754 -0.0321 0.0839  -0.0034 519  ASN B OD1 
4659 N  ND2 . ASN B 295 ? 0.3171 0.4374 0.5016 -0.0352 0.1011  0.0043  519  ASN B ND2 
4660 N  N   . GLN B 296 ? 0.2411 0.3520 0.3915 -0.0218 0.0716  -0.0052 520  GLN B N   
4661 C  CA  . GLN B 296 ? 0.2448 0.3603 0.3989 -0.0178 0.0651  -0.0100 520  GLN B CA  
4662 C  C   . GLN B 296 ? 0.2517 0.3785 0.4274 -0.0184 0.0649  -0.0136 520  GLN B C   
4663 O  O   . GLN B 296 ? 0.2715 0.4022 0.4522 -0.0154 0.0581  -0.0177 520  GLN B O   
4664 C  CB  . GLN B 296 ? 0.2870 0.4004 0.4284 -0.0131 0.0675  -0.0102 520  GLN B CB  
4665 C  CG  . GLN B 296 ? 0.4190 0.5223 0.5408 -0.0114 0.0627  -0.0089 520  GLN B CG  
4666 C  CD  . GLN B 296 ? 0.5190 0.6180 0.6260 -0.0082 0.0670  -0.0078 520  GLN B CD  
4667 O  OE1 . GLN B 296 ? 0.5635 0.6666 0.6735 -0.0068 0.0739  -0.0080 520  GLN B OE1 
4668 N  NE2 . GLN B 296 ? 0.4820 0.5726 0.5729 -0.0070 0.0631  -0.0067 520  GLN B NE2 
4669 N  N   . PHE B 297 ? 0.2435 0.3755 0.4324 -0.0222 0.0720  -0.0121 521  PHE B N   
4670 C  CA  . PHE B 297 ? 0.2380 0.3816 0.4494 -0.0231 0.0723  -0.0157 521  PHE B CA  
4671 C  C   . PHE B 297 ? 0.2753 0.4211 0.4998 -0.0268 0.0658  -0.0177 521  PHE B C   
4672 O  O   . PHE B 297 ? 0.2412 0.3970 0.4856 -0.0278 0.0647  -0.0211 521  PHE B O   
4673 C  CB  . PHE B 297 ? 0.2120 0.3609 0.4329 -0.0254 0.0840  -0.0133 521  PHE B CB  
4674 C  CG  . PHE B 297 ? 0.2647 0.4126 0.4744 -0.0213 0.0908  -0.0121 521  PHE B CG  
4675 C  CD1 . PHE B 297 ? 0.3346 0.4904 0.5515 -0.0168 0.0908  -0.0159 521  PHE B CD1 
4676 C  CD2 . PHE B 297 ? 0.2894 0.4283 0.4813 -0.0216 0.0971  -0.0072 521  PHE B CD2 
4677 C  CE1 . PHE B 297 ? 0.3184 0.4729 0.5248 -0.0129 0.0971  -0.0151 521  PHE B CE1 
4678 C  CE2 . PHE B 297 ? 0.3605 0.4981 0.5414 -0.0177 0.1031  -0.0065 521  PHE B CE2 
4679 C  CZ  . PHE B 297 ? 0.3223 0.4675 0.5103 -0.0134 0.1032  -0.0106 521  PHE B CZ  
4680 N  N   . TYR B 298 ? 0.2450 0.3819 0.4592 -0.0289 0.0614  -0.0159 522  TYR B N   
4681 C  CA  . TYR B 298 ? 0.2273 0.3652 0.4531 -0.0328 0.0561  -0.0177 522  TYR B CA  
4682 C  C   . TYR B 298 ? 0.2211 0.3654 0.4565 -0.0300 0.0464  -0.0235 522  TYR B C   
4683 O  O   . TYR B 298 ? 0.2139 0.3555 0.4382 -0.0253 0.0406  -0.0251 522  TYR B O   
4684 C  CB  . TYR B 298 ? 0.2605 0.3871 0.4716 -0.0345 0.0529  -0.0148 522  TYR B CB  
4685 C  CG  . TYR B 298 ? 0.2545 0.3805 0.4763 -0.0389 0.0486  -0.0162 522  TYR B CG  
4686 C  CD1 . TYR B 298 ? 0.2283 0.3547 0.4524 -0.0376 0.0383  -0.0207 522  TYR B CD1 
4687 C  CD2 . TYR B 298 ? 0.3144 0.4388 0.5436 -0.0444 0.0550  -0.0131 522  TYR B CD2 
4688 C  CE1 . TYR B 298 ? 0.2868 0.4123 0.5201 -0.0414 0.0341  -0.0224 522  TYR B CE1 
4689 C  CE2 . TYR B 298 ? 0.3078 0.4312 0.5472 -0.0485 0.0509  -0.0147 522  TYR B CE2 
4690 C  CZ  . TYR B 298 ? 0.3219 0.4459 0.5632 -0.0470 0.0403  -0.0196 522  TYR B CZ  
4691 O  OH  . TYR B 298 ? 0.3429 0.4654 0.5937 -0.0509 0.0361  -0.0216 522  TYR B OH  
4692 N  N   . SER B 299 ? 0.1897 0.3421 0.4457 -0.0330 0.0446  -0.0267 523  SER B N   
4693 C  CA  . SER B 299 ? 0.2436 0.4032 0.5104 -0.0302 0.0355  -0.0325 523  SER B CA  
4694 C  C   . SER B 299 ? 0.2441 0.3978 0.5064 -0.0310 0.0259  -0.0345 523  SER B C   
4695 O  O   . SER B 299 ? 0.2668 0.4184 0.5353 -0.0360 0.0260  -0.0340 523  SER B O   
4696 C  CB  . SER B 299 ? 0.2581 0.4304 0.5505 -0.0326 0.0379  -0.0355 523  SER B CB  
4697 O  OG  . SER B 299 ? 0.2711 0.4508 0.5733 -0.0289 0.0290  -0.0412 523  SER B OG  
4698 N  N   . LEU B 300 ? 0.1998 0.3507 0.4516 -0.0261 0.0177  -0.0367 524  LEU B N   
4699 C  CA  . LEU B 300 ? 0.2111 0.3562 0.4568 -0.0260 0.0086  -0.0388 524  LEU B CA  
4700 C  C   . LEU B 300 ? 0.2471 0.4003 0.5084 -0.0249 0.0002  -0.0448 524  LEU B C   
4701 O  O   . LEU B 300 ? 0.2381 0.3993 0.5076 -0.0213 -0.0014 -0.0475 524  LEU B O   
4702 C  CB  . LEU B 300 ? 0.2189 0.3555 0.4432 -0.0214 0.0048  -0.0375 524  LEU B CB  
4703 C  CG  . LEU B 300 ? 0.2440 0.3713 0.4510 -0.0223 0.0108  -0.0321 524  LEU B CG  
4704 C  CD1 . LEU B 300 ? 0.2134 0.3341 0.4020 -0.0174 0.0068  -0.0315 524  LEU B CD1 
4705 C  CD2 . LEU B 300 ? 0.2451 0.3662 0.4507 -0.0270 0.0110  -0.0303 524  LEU B CD2 
4706 N  N   . ALA B 301 ? 0.2704 0.4211 0.5354 -0.0276 -0.0057 -0.0471 525  ALA B N   
4707 C  CA  . ALA B 301 ? 0.2162 0.3724 0.4913 -0.0256 -0.0157 -0.0531 525  ALA B CA  
4708 C  C   . ALA B 301 ? 0.2236 0.3753 0.4826 -0.0190 -0.0230 -0.0543 525  ALA B C   
4709 O  O   . ALA B 301 ? 0.2014 0.3431 0.4413 -0.0178 -0.0229 -0.0512 525  ALA B O   
4710 C  CB  . ALA B 301 ? 0.2762 0.4293 0.5570 -0.0300 -0.0204 -0.0555 525  ALA B CB  
4711 N  N   . PRO B 302 ? 0.1785 0.3374 0.4451 -0.0147 -0.0292 -0.0585 526  PRO B N   
4712 C  CA  . PRO B 302 ? 0.2953 0.4494 0.5463 -0.0082 -0.0357 -0.0592 526  PRO B CA  
4713 C  C   . PRO B 302 ? 0.3586 0.5045 0.5982 -0.0075 -0.0437 -0.0608 526  PRO B C   
4714 O  O   . PRO B 302 ? 0.3140 0.4609 0.5624 -0.0107 -0.0478 -0.0639 526  PRO B O   
4715 C  CB  . PRO B 302 ? 0.2950 0.4596 0.5599 -0.0040 -0.0407 -0.0636 526  PRO B CB  
4716 C  CG  . PRO B 302 ? 0.3242 0.4993 0.6131 -0.0087 -0.0388 -0.0663 526  PRO B CG  
4717 C  CD  . PRO B 302 ? 0.2818 0.4537 0.5709 -0.0150 -0.0287 -0.0619 526  PRO B CD  
4718 N  N   . VAL B 303 ? 0.3283 0.4657 0.5481 -0.0034 -0.0455 -0.0586 527  VAL B N   
4719 C  CA  . VAL B 303 ? 0.3390 0.4684 0.5457 -0.0013 -0.0529 -0.0600 527  VAL B CA  
4720 C  C   . VAL B 303 ? 0.5073 0.6352 0.7041 0.0058  -0.0587 -0.0610 527  VAL B C   
4721 O  O   . VAL B 303 ? 0.5408 0.6641 0.7287 0.0091  -0.0664 -0.0632 527  VAL B O   
4722 C  CB  . VAL B 303 ? 0.3638 0.4827 0.5547 -0.0037 -0.0485 -0.0556 527  VAL B CB  
4723 C  CG1 . VAL B 303 ? 0.2935 0.4088 0.4723 -0.0018 -0.0422 -0.0509 527  VAL B CG1 
4724 C  CG2 . VAL B 303 ? 0.3845 0.4955 0.5625 -0.0016 -0.0555 -0.0571 527  VAL B CG2 
4725 O  OXT . VAL B 303 ? 0.4876 0.6186 0.6847 0.0086  -0.0556 -0.0596 527  VAL B OXT 
4726 CL CL  . CL  C .   ? 0.8301 0.8234 0.8789 -0.0145 -0.0239 -0.0208 601  CL  A CL  
4727 CL CL  . CL  D .   ? 0.8537 0.8605 0.8253 -0.0050 -0.0048 0.0182  601  CL  B CL  
4728 O  O   . HOH E .   ? 0.5048 0.4673 0.3955 0.0530  -0.0528 -0.0282 701  HOH A O   
4729 O  O   . HOH E .   ? 0.6408 0.5590 0.5350 0.0519  -0.0597 -0.0857 702  HOH A O   
4730 O  O   . HOH E .   ? 0.5383 0.4345 0.3058 0.0902  0.0191  -0.0405 703  HOH A O   
4731 O  O   . HOH E .   ? 0.7441 0.6144 0.4768 0.0813  0.0861  0.0320  704  HOH A O   
4732 O  O   . HOH E .   ? 0.3650 0.3273 0.3706 0.0299  -0.0056 -0.0220 705  HOH A O   
4733 O  O   . HOH E .   ? 0.3415 0.3151 0.3454 0.0456  -0.0483 0.0427  706  HOH A O   
4734 O  O   . HOH E .   ? 0.5966 0.4998 0.4938 0.0173  0.0680  0.0489  707  HOH A O   
4735 O  O   . HOH E .   ? 0.4053 0.4441 0.4826 0.0446  0.0351  -0.0073 708  HOH A O   
4736 O  O   . HOH E .   ? 0.5308 0.4276 0.5462 0.0010  -0.0019 0.0448  709  HOH A O   
4737 O  O   . HOH E .   ? 0.3006 0.3106 0.3015 0.0013  -0.0181 0.0161  710  HOH A O   
4738 O  O   . HOH E .   ? 0.2905 0.3300 0.3194 0.0010  -0.0358 0.0043  711  HOH A O   
4739 O  O   . HOH E .   ? 0.6923 0.5159 0.3421 0.1155  0.0058  0.0323  712  HOH A O   
4740 O  O   . HOH E .   ? 0.3495 0.3931 0.4291 0.0317  0.0175  -0.0015 713  HOH A O   
4741 O  O   . HOH E .   ? 0.3047 0.3280 0.3878 0.0533  -0.0369 0.0167  714  HOH A O   
4742 O  O   . HOH E .   ? 0.7401 0.6436 0.6294 0.0196  0.1220  0.0631  715  HOH A O   
4743 O  O   . HOH E .   ? 0.3528 0.4104 0.4646 0.0431  0.0152  -0.0027 716  HOH A O   
4744 O  O   . HOH E .   ? 0.3490 0.3922 0.4254 -0.0030 0.0480  0.0114  717  HOH A O   
4745 O  O   . HOH E .   ? 0.2727 0.3095 0.3297 0.0059  0.0465  0.0094  718  HOH A O   
4746 O  O   . HOH E .   ? 0.2706 0.2645 0.2427 0.0193  0.0168  -0.0022 719  HOH A O   
4747 O  O   . HOH E .   ? 0.3233 0.3227 0.3033 0.0094  -0.0069 -0.0058 720  HOH A O   
4748 O  O   . HOH E .   ? 0.4287 0.5237 0.5684 0.0037  -0.0334 -0.0046 721  HOH A O   
4749 O  O   . HOH E .   ? 0.3115 0.3312 0.3613 0.0438  0.0301  -0.0098 722  HOH A O   
4750 O  O   . HOH E .   ? 0.4246 0.4236 0.4786 -0.0206 -0.0118 -0.0072 723  HOH A O   
4751 O  O   . HOH E .   ? 0.5204 0.5075 0.4805 0.0059  -0.0166 0.0339  724  HOH A O   
4752 O  O   . HOH E .   ? 0.6309 0.4983 0.3264 0.1143  -0.0485 -0.0109 725  HOH A O   
4753 O  O   . HOH E .   ? 0.2376 0.2894 0.2983 -0.0003 -0.0267 0.0022  726  HOH A O   
4754 O  O   . HOH E .   ? 0.4725 0.4369 0.4791 -0.0098 0.1154  0.0485  727  HOH A O   
4755 O  O   . HOH E .   ? 0.3622 0.3746 0.4372 0.0473  -0.0120 0.0048  728  HOH A O   
4756 O  O   . HOH E .   ? 0.2865 0.3003 0.2901 -0.0031 -0.0099 -0.0003 729  HOH A O   
4757 O  O   B HOH E .   ? 0.2583 0.2524 0.2706 0.0161  -0.0044 -0.0060 730  HOH A O   
4758 O  O   . HOH E .   ? 0.2255 0.2462 0.2500 -0.0082 0.0035  0.0043  731  HOH A O   
4759 O  O   . HOH E .   ? 0.5080 0.4309 0.5482 0.0646  -0.0334 0.0340  732  HOH A O   
4760 O  O   . HOH E .   ? 0.4492 0.4206 0.3679 0.0496  -0.0447 -0.0115 733  HOH A O   
4761 O  O   . HOH E .   ? 0.3952 0.4255 0.4570 -0.0017 0.0711  0.0185  734  HOH A O   
4762 O  O   . HOH E .   ? 0.2940 0.2678 0.3216 -0.0061 -0.0114 0.0032  735  HOH A O   
4763 O  O   . HOH E .   ? 0.2145 0.2454 0.2284 -0.0003 -0.0304 0.0062  736  HOH A O   
4764 O  O   . HOH E .   ? 0.4694 0.4157 0.4909 0.0156  -0.0154 -0.0160 737  HOH A O   
4765 O  O   . HOH E .   ? 0.2979 0.2743 0.2416 0.0316  0.0119  -0.0139 738  HOH A O   
4766 O  O   . HOH E .   ? 0.5436 0.4644 0.4441 0.0197  0.0714  0.0433  739  HOH A O   
4767 O  O   . HOH E .   ? 0.4730 0.4126 0.3452 0.0538  -0.0237 -0.0432 740  HOH A O   
4768 O  O   . HOH E .   ? 0.3577 0.3344 0.3684 0.0279  -0.0023 -0.0150 741  HOH A O   
4769 O  O   . HOH E .   ? 0.3899 0.3532 0.3149 0.0351  -0.0313 -0.0382 742  HOH A O   
4770 O  O   . HOH E .   ? 0.2769 0.2697 0.2626 0.0005  0.0158  0.0098  743  HOH A O   
4771 O  O   . HOH E .   ? 0.3633 0.3271 0.3528 0.0001  -0.0059 0.0384  744  HOH A O   
4772 O  O   . HOH E .   ? 0.5598 0.4846 0.4206 0.0427  0.1027  0.0375  745  HOH A O   
4773 O  O   . HOH E .   ? 0.3412 0.4626 0.5506 0.0528  -0.0176 -0.0035 746  HOH A O   
4774 O  O   . HOH E .   ? 0.3782 0.4325 0.4646 0.0221  0.0303  0.0011  747  HOH A O   
4775 O  O   . HOH E .   ? 0.3132 0.2654 0.2099 0.0453  -0.0231 0.0015  748  HOH A O   
4776 O  O   . HOH E .   ? 0.2628 0.3145 0.3590 0.0340  0.0082  0.0000  749  HOH A O   
4777 O  O   . HOH E .   ? 0.2144 0.2330 0.2545 0.0178  -0.0046 0.0032  750  HOH A O   
4778 O  O   . HOH E .   ? 0.5328 0.5194 0.5445 -0.0138 0.0018  0.0230  751  HOH A O   
4779 O  O   . HOH E .   ? 0.4330 0.3595 0.2500 0.0820  -0.0609 -0.0191 752  HOH A O   
4780 O  O   . HOH E .   ? 0.6247 0.5612 0.5880 0.0286  -0.0389 -0.0617 753  HOH A O   
4781 O  O   . HOH E .   ? 0.3996 0.4137 0.4101 -0.0064 -0.0100 0.0000  754  HOH A O   
4782 O  O   . HOH E .   ? 0.4979 0.5262 0.4692 0.0250  -0.0839 0.0068  755  HOH A O   
4783 O  O   . HOH E .   ? 0.4150 0.4792 0.5070 0.0503  -0.0777 0.0143  756  HOH A O   
4784 O  O   . HOH E .   ? 0.3109 0.2626 0.2171 0.0322  -0.0007 0.0099  757  HOH A O   
4785 O  O   . HOH E .   ? 0.4013 0.4230 0.4140 -0.0098 -0.0120 -0.0002 758  HOH A O   
4786 O  O   . HOH E .   ? 0.3261 0.3011 0.2632 0.0244  -0.0106 0.0005  759  HOH A O   
4787 O  O   . HOH E .   ? 0.3397 0.2886 0.2155 0.0558  0.0644  -0.0017 760  HOH A O   
4788 O  O   . HOH E .   ? 0.3630 0.3420 0.4380 0.0767  -0.0432 0.0262  761  HOH A O   
4789 O  O   . HOH E .   ? 0.2343 0.3037 0.3452 -0.0061 0.0072  0.0020  762  HOH A O   
4790 O  O   . HOH E .   ? 0.2847 0.2907 0.2764 0.0049  -0.0040 -0.0018 763  HOH A O   
4791 O  O   . HOH E .   ? 0.3800 0.3484 0.2920 0.0407  -0.0310 -0.0105 764  HOH A O   
4792 O  O   . HOH E .   ? 0.4942 0.4684 0.5257 -0.0060 -0.0211 -0.0177 765  HOH A O   
4793 O  O   . HOH E .   ? 0.3487 0.3701 0.3929 -0.0154 0.0133  0.0061  766  HOH A O   
4794 O  O   . HOH E .   ? 0.5400 0.3832 0.3454 0.0537  0.0443  0.0602  767  HOH A O   
4795 O  O   . HOH E .   ? 0.3058 0.3813 0.4443 0.0521  -0.0392 0.0068  768  HOH A O   
4796 O  O   . HOH E .   ? 0.3441 0.4298 0.4984 0.0455  -0.0002 -0.0011 769  HOH A O   
4797 O  O   . HOH E .   ? 0.3914 0.4063 0.3644 0.0012  -0.0277 0.0114  770  HOH A O   
4798 O  O   . HOH E .   ? 0.4137 0.3446 0.2633 0.0705  0.0357  -0.0309 771  HOH A O   
4799 O  O   . HOH E .   ? 0.4823 0.4563 0.5026 -0.0101 -0.0045 0.0188  772  HOH A O   
4800 O  O   A HOH E .   ? 0.3537 0.3377 0.3047 0.0179  -0.0079 -0.0008 773  HOH A O   
4801 O  O   . HOH E .   ? 0.2714 0.2881 0.2805 0.0030  -0.0209 0.0135  774  HOH A O   
4802 O  O   . HOH E .   ? 0.3177 0.3134 0.3074 0.0015  -0.0147 0.0248  775  HOH A O   
4803 O  O   A HOH E .   ? 0.2399 0.2276 0.2503 0.0201  -0.0036 -0.0097 776  HOH A O   
4804 O  O   . HOH E .   ? 0.3710 0.3376 0.4083 0.0341  -0.0120 0.0021  777  HOH A O   
4805 O  O   . HOH E .   ? 0.5001 0.4381 0.3452 0.0653  -0.0558 -0.0448 778  HOH A O   
4806 O  O   . HOH E .   ? 0.2794 0.3112 0.2957 -0.0052 -0.0272 0.0017  779  HOH A O   
4807 O  O   . HOH E .   ? 0.5551 0.4147 0.3468 0.0810  -0.0091 0.0389  780  HOH A O   
4808 O  O   . HOH E .   ? 0.4624 0.4097 0.3522 0.0695  0.0527  -0.0292 781  HOH A O   
4809 O  O   . HOH E .   ? 0.5352 0.4812 0.5813 -0.0114 -0.0153 -0.0071 782  HOH A O   
4810 O  O   . HOH E .   ? 0.3840 0.3765 0.3771 -0.0060 -0.0049 0.0248  783  HOH A O   
4811 O  O   . HOH E .   ? 0.3618 0.3331 0.2889 0.0323  -0.0254 -0.0265 784  HOH A O   
4812 O  O   . HOH E .   ? 0.6641 0.6729 0.6996 0.0066  0.1311  0.0360  785  HOH A O   
4813 O  O   . HOH E .   ? 0.3733 0.3182 0.2658 0.0502  -0.0257 0.0048  786  HOH A O   
4814 O  O   . HOH E .   ? 0.5001 0.4564 0.4214 0.0376  -0.0315 -0.0440 787  HOH A O   
4815 O  O   . HOH E .   ? 0.3286 0.3147 0.2929 0.0091  0.0057  0.0060  788  HOH A O   
4816 O  O   . HOH E .   ? 0.3685 0.4208 0.4491 0.0155  0.0247  0.0026  789  HOH A O   
4817 O  O   . HOH E .   ? 0.3772 0.3147 0.2567 0.0600  0.0111  -0.0393 790  HOH A O   
4818 O  O   . HOH E .   ? 0.2588 0.2728 0.2791 -0.0077 0.0123  0.0069  791  HOH A O   
4819 O  O   . HOH E .   ? 0.3648 0.3222 0.2553 0.0428  -0.0179 -0.0169 792  HOH A O   
4820 O  O   . HOH E .   ? 0.3830 0.3420 0.3512 0.0317  -0.0093 -0.0343 793  HOH A O   
4821 O  O   . HOH E .   ? 0.4374 0.4404 0.4810 0.0523  0.0245  -0.0156 794  HOH A O   
4822 O  O   . HOH E .   ? 0.3419 0.3391 0.3291 0.0117  -0.0045 -0.0080 795  HOH A O   
4823 O  O   . HOH E .   ? 0.4476 0.3784 0.2840 0.0662  0.0610  -0.0055 796  HOH A O   
4824 O  O   . HOH E .   ? 0.2953 0.3001 0.2969 0.0338  0.0368  -0.0071 797  HOH A O   
4825 O  O   . HOH E .   ? 0.5104 0.4047 0.2712 0.0800  0.0310  0.0000  798  HOH A O   
4826 O  O   . HOH E .   ? 0.4593 0.4427 0.4509 0.0572  0.0396  -0.0248 799  HOH A O   
4827 O  O   . HOH E .   ? 0.4662 0.3743 0.3733 0.0553  -0.0315 -0.0788 800  HOH A O   
4828 O  O   . HOH E .   ? 0.8567 0.6273 0.4293 0.1232  0.0809  0.0685  801  HOH A O   
4829 O  O   . HOH E .   ? 0.3951 0.4437 0.4904 -0.0082 0.0589  0.0140  802  HOH A O   
4830 O  O   . HOH E .   ? 0.6011 0.4669 0.3919 0.0918  -0.0285 0.0315  803  HOH A O   
4831 O  O   . HOH E .   ? 0.3779 0.3686 0.3481 0.0474  0.0573  -0.0106 804  HOH A O   
4832 O  O   . HOH E .   ? 0.7325 0.5799 0.4847 0.0904  -0.0057 0.0412  805  HOH A O   
4833 O  O   . HOH E .   ? 0.6321 0.5649 0.4994 0.1036  -0.0829 -0.0047 806  HOH A O   
4834 O  O   . HOH E .   ? 0.2772 0.2793 0.2692 0.0284  0.0333  -0.0044 807  HOH A O   
4835 O  O   . HOH E .   ? 0.7571 0.6007 0.4241 0.1026  0.0818  0.0276  808  HOH A O   
4836 O  O   . HOH E .   ? 0.4727 0.3910 0.3048 0.0526  0.0634  0.0227  809  HOH A O   
4837 O  O   . HOH E .   ? 0.2703 0.2877 0.2722 -0.0054 -0.0097 0.0030  810  HOH A O   
4838 O  O   . HOH E .   ? 0.3025 0.3030 0.3394 -0.0175 0.0383  0.0166  811  HOH A O   
4839 O  O   . HOH E .   ? 0.3849 0.4521 0.4550 0.0127  -0.0644 -0.0007 812  HOH A O   
4840 O  O   . HOH E .   ? 0.2987 0.3041 0.3205 -0.0069 -0.0157 -0.0084 813  HOH A O   
4841 O  O   . HOH E .   ? 0.5086 0.4428 0.5439 0.0017  -0.0149 -0.0032 814  HOH A O   
4842 O  O   . HOH E .   ? 0.2986 0.4219 0.5008 0.0176  0.0078  -0.0036 815  HOH A O   
4843 O  O   . HOH E .   ? 0.6638 0.4888 0.4367 0.0615  0.0553  0.0690  816  HOH A O   
4844 O  O   . HOH E .   ? 0.5017 0.4289 0.3172 0.0761  -0.0547 -0.0315 817  HOH A O   
4845 O  O   . HOH E .   ? 0.2484 0.2875 0.3193 0.0354  -0.0414 0.0153  818  HOH A O   
4846 O  O   . HOH E .   ? 0.4196 0.3986 0.4436 0.0418  0.0060  -0.0162 819  HOH A O   
4847 O  O   . HOH E .   ? 0.2726 0.2791 0.2826 0.0152  0.0040  -0.0033 820  HOH A O   
4848 O  O   . HOH E .   ? 0.4427 0.3667 0.2887 0.0709  0.0158  -0.0429 821  HOH A O   
4849 O  O   . HOH E .   ? 0.3419 0.2632 0.3382 0.0206  -0.0161 0.0486  822  HOH A O   
4850 O  O   . HOH E .   ? 0.5017 0.5896 0.6469 0.0262  0.0378  -0.0003 823  HOH A O   
4851 O  O   A HOH E .   ? 0.4384 0.3552 0.2534 0.0618  0.0472  0.0091  824  HOH A O   
4852 O  O   . HOH E .   ? 0.4444 0.4681 0.4346 -0.0057 -0.0324 -0.0034 825  HOH A O   
4853 O  O   . HOH E .   ? 0.3971 0.3333 0.4086 -0.0015 -0.0042 0.0361  826  HOH A O   
4854 O  O   . HOH E .   ? 0.5307 0.5479 0.4945 -0.0009 -0.0388 -0.0043 827  HOH A O   
4855 O  O   . HOH E .   ? 0.3191 0.3497 0.3635 0.0125  0.0589  0.0102  828  HOH A O   
4856 O  O   . HOH E .   ? 0.3925 0.3664 0.3872 0.0532  0.0239  -0.0273 829  HOH A O   
4857 O  O   . HOH E .   ? 0.4932 0.4685 0.4289 0.0549  0.0649  -0.0121 830  HOH A O   
4858 O  O   B HOH E .   ? 0.3069 0.2959 0.2632 0.0174  -0.0123 -0.0047 831  HOH A O   
4859 O  O   . HOH E .   ? 0.5022 0.5218 0.5040 -0.0082 -0.0132 -0.0003 832  HOH A O   
4860 O  O   A HOH E .   ? 0.3564 0.4386 0.4669 0.0095  -0.0451 -0.0017 833  HOH A O   
4861 O  O   . HOH E .   ? 0.6346 0.6242 0.6398 0.0050  -0.0319 -0.0301 834  HOH A O   
4862 O  O   . HOH E .   ? 0.5294 0.4238 0.4067 0.0368  0.0191  0.0356  835  HOH A O   
4863 O  O   . HOH E .   ? 0.3957 0.4305 0.3898 0.0192  -0.0735 0.0066  836  HOH A O   
4864 O  O   . HOH E .   ? 0.3533 0.3478 0.3340 0.0028  0.0075  0.0063  837  HOH A O   
4865 O  O   . HOH E .   ? 0.3795 0.3535 0.3553 0.0188  -0.0206 -0.0296 838  HOH A O   
4866 O  O   . HOH E .   ? 0.3863 0.4690 0.5389 0.0496  -0.0152 0.0012  839  HOH A O   
4867 O  O   . HOH E .   ? 0.4974 0.3985 0.3017 0.0936  0.0344  -0.0561 840  HOH A O   
4868 O  O   . HOH E .   ? 0.6735 0.5461 0.4958 0.0722  -0.0101 0.0348  841  HOH A O   
4869 O  O   . HOH E .   ? 0.3824 0.3812 0.3710 0.0094  -0.0251 -0.0200 842  HOH A O   
4870 O  O   . HOH E .   ? 0.5424 0.4600 0.4279 0.0572  -0.0331 -0.0722 843  HOH A O   
4871 O  O   . HOH E .   ? 0.2710 0.2620 0.2451 0.0156  -0.0065 -0.0119 844  HOH A O   
4872 O  O   . HOH E .   ? 0.3690 0.3549 0.3468 0.0140  0.0807  0.0250  845  HOH A O   
4873 O  O   . HOH E .   ? 0.5254 0.4482 0.5602 0.0082  -0.0152 -0.0030 846  HOH A O   
4874 O  O   . HOH E .   ? 0.6154 0.5218 0.3998 0.0828  -0.0400 -0.0523 847  HOH A O   
4875 O  O   A HOH E .   ? 0.5758 0.5089 0.4156 0.0685  0.0926  0.0039  848  HOH A O   
4876 O  O   . HOH E .   ? 0.4159 0.4228 0.4868 -0.0177 0.1140  0.0385  849  HOH A O   
4877 O  O   . HOH E .   ? 0.2959 0.2797 0.2877 0.0021  -0.0124 0.0294  850  HOH A O   
4878 O  O   . HOH E .   ? 0.3556 0.3544 0.3362 0.0039  -0.0012 0.0021  851  HOH A O   
4879 O  O   . HOH E .   ? 0.3318 0.2995 0.3625 0.0309  -0.0087 -0.0047 852  HOH A O   
4880 O  O   . HOH E .   ? 0.4242 0.3895 0.3933 0.0239  -0.0198 -0.0345 853  HOH A O   
4881 O  O   . HOH E .   ? 0.7092 0.5840 0.4192 0.1022  0.0210  -0.0272 854  HOH A O   
4882 O  O   . HOH E .   ? 0.3390 0.3842 0.4305 -0.0183 0.0263  0.0073  855  HOH A O   
4883 O  O   . HOH E .   ? 0.3685 0.2912 0.4025 0.0359  -0.0180 0.0155  856  HOH A O   
4884 O  O   . HOH E .   ? 0.3832 0.2488 0.3968 0.0045  0.0001  0.0543  857  HOH A O   
4885 O  O   . HOH E .   ? 0.4646 0.4893 0.5076 -0.0154 0.0040  0.0031  858  HOH A O   
4886 O  O   . HOH E .   ? 0.3480 0.3975 0.4242 0.0134  0.0456  0.0056  859  HOH A O   
4887 O  O   . HOH E .   ? 0.5615 0.5212 0.4585 0.0543  0.0960  0.0082  860  HOH A O   
4888 O  O   . HOH E .   ? 0.5485 0.4400 0.5834 0.0099  -0.0116 0.0188  861  HOH A O   
4889 O  O   B HOH E .   ? 0.4381 0.3581 0.2639 0.0577  0.0601  0.0150  862  HOH A O   
4890 O  O   . HOH E .   ? 0.4829 0.4831 0.4412 0.0404  -0.0732 0.0337  863  HOH A O   
4891 O  O   . HOH E .   ? 0.3944 0.4282 0.4663 0.0399  0.0227  -0.0053 864  HOH A O   
4892 O  O   . HOH E .   ? 0.3182 0.3917 0.4374 -0.0128 -0.0054 -0.0019 865  HOH A O   
4893 O  O   . HOH E .   ? 0.4895 0.4910 0.5214 -0.0169 -0.0036 0.0063  866  HOH A O   
4894 O  O   . HOH E .   ? 0.4350 0.4073 0.4810 -0.0255 0.1035  0.0440  867  HOH A O   
4895 O  O   . HOH E .   ? 0.5455 0.4483 0.4183 0.0279  0.0651  0.0464  868  HOH A O   
4896 O  O   . HOH E .   ? 0.5087 0.4691 0.4703 0.0568  0.0252  -0.0345 869  HOH A O   
4897 O  O   B HOH E .   ? 0.7062 0.6260 0.5715 0.0370  0.0979  0.0425  870  HOH A O   
4898 O  O   . HOH E .   ? 0.3855 0.3997 0.3674 -0.0038 -0.0149 0.0113  871  HOH A O   
4899 O  O   . HOH E .   ? 0.5459 0.6000 0.5980 0.0252  -0.0677 0.0092  872  HOH A O   
4900 O  O   . HOH E .   ? 0.6409 0.6300 0.6098 0.0319  0.1191  0.0247  873  HOH A O   
4901 O  O   . HOH E .   ? 0.5024 0.5231 0.5274 0.0400  0.0628  -0.0040 874  HOH A O   
4902 O  O   . HOH E .   ? 0.4586 0.4133 0.3421 0.0521  -0.0364 -0.0112 875  HOH A O   
4903 O  O   . HOH E .   ? 0.4563 0.4516 0.4278 0.0088  -0.0043 0.0001  876  HOH A O   
4904 O  O   . HOH E .   ? 0.4087 0.3581 0.2903 0.0545  -0.0347 -0.0044 877  HOH A O   
4905 O  O   . HOH E .   ? 0.4646 0.4289 0.3730 0.0362  -0.0077 -0.0150 878  HOH A O   
4906 O  O   . HOH E .   ? 0.3752 0.4445 0.5248 0.0626  -0.0057 -0.0011 879  HOH A O   
4907 O  O   . HOH E .   ? 0.4668 0.5053 0.5902 0.0746  -0.0398 0.0127  880  HOH A O   
4908 O  O   . HOH E .   ? 0.4300 0.3942 0.3578 0.0592  0.0475  -0.0243 881  HOH A O   
4909 O  O   . HOH E .   ? 0.4011 0.4528 0.4836 0.0062  0.0442  0.0074  882  HOH A O   
4910 O  O   . HOH E .   ? 0.3910 0.3357 0.3218 0.0577  0.0152  -0.0431 883  HOH A O   
4911 O  O   . HOH E .   ? 0.7864 0.7851 0.7871 0.0197  0.1272  0.0316  884  HOH A O   
4912 O  O   . HOH E .   ? 0.5094 0.5030 0.5013 0.0089  -0.0273 -0.0244 885  HOH A O   
4913 O  O   . HOH E .   ? 0.4373 0.4586 0.4357 -0.0082 -0.0185 -0.0011 886  HOH A O   
4914 O  O   . HOH E .   ? 0.6216 0.5051 0.4527 0.0803  -0.0277 0.0265  887  HOH A O   
4915 O  O   . HOH E .   ? 0.4913 0.3957 0.5307 0.0031  -0.0121 0.0090  888  HOH A O   
4916 O  O   A HOH E .   ? 0.4423 0.4382 0.4124 0.0172  -0.0279 -0.0195 889  HOH A O   
4917 O  O   . HOH E .   ? 0.4129 0.4051 0.4551 0.0447  0.0070  -0.0109 890  HOH A O   
4918 O  O   . HOH E .   ? 0.4008 0.4067 0.4443 -0.0202 -0.0034 0.0025  891  HOH A O   
4919 O  O   . HOH E .   ? 0.5885 0.5716 0.6484 -0.0251 -0.0070 -0.0012 892  HOH A O   
4920 O  O   . HOH E .   ? 0.4241 0.3745 0.2938 0.0585  -0.0445 -0.0175 893  HOH A O   
4921 O  O   . HOH E .   ? 0.3601 0.4077 0.4078 -0.0010 -0.0332 0.0017  894  HOH A O   
4922 O  O   . HOH E .   ? 0.6132 0.5925 0.5514 0.0571  0.0835  -0.0068 895  HOH A O   
4923 O  O   . HOH E .   ? 0.6137 0.5610 0.6139 -0.0150 0.0137  0.0465  896  HOH A O   
4924 O  O   . HOH E .   ? 0.5798 0.4723 0.3223 0.0978  -0.0480 -0.0235 897  HOH A O   
4925 O  O   . HOH E .   ? 0.5744 0.5132 0.4415 0.0515  0.1110  0.0260  898  HOH A O   
4926 O  O   . HOH E .   ? 0.3769 0.3557 0.3974 -0.0065 -0.0083 0.0131  899  HOH A O   
4927 O  O   . HOH E .   ? 0.6259 0.6751 0.7250 0.0466  0.0276  -0.0059 900  HOH A O   
4928 O  O   . HOH E .   ? 0.3134 0.3012 0.2738 0.0125  -0.0005 0.0020  901  HOH A O   
4929 O  O   . HOH E .   ? 0.4084 0.3544 0.4498 0.0620  -0.0371 0.0339  902  HOH A O   
4930 O  O   . HOH E .   ? 0.3341 0.3448 0.3507 -0.0053 -0.0151 -0.0077 903  HOH A O   
4931 O  O   B HOH E .   ? 0.4532 0.5332 0.5554 0.0137  -0.0552 -0.0009 904  HOH A O   
4932 O  O   . HOH E .   ? 0.4518 0.4330 0.4028 0.0255  -0.0353 -0.0313 905  HOH A O   
4933 O  O   . HOH E .   ? 0.4962 0.4893 0.4801 0.0481  0.0485  -0.0146 906  HOH A O   
4934 O  O   . HOH E .   ? 0.5692 0.5413 0.5960 -0.0028 -0.0270 -0.0272 907  HOH A O   
4935 O  O   . HOH E .   ? 0.6586 0.6633 0.7002 -0.0016 0.1258  0.0386  908  HOH A O   
4936 O  O   . HOH E .   ? 0.3956 0.3822 0.3450 0.0219  -0.0181 -0.0102 909  HOH A O   
4937 O  O   . HOH E .   ? 0.3512 0.3387 0.3190 0.0384  -0.0582 0.0409  910  HOH A O   
4938 O  O   . HOH E .   ? 0.3840 0.3638 0.3340 0.0326  -0.0500 0.0434  911  HOH A O   
4939 O  O   . HOH E .   ? 0.3670 0.4047 0.4693 0.0596  -0.0418 0.0151  912  HOH A O   
4940 O  O   . HOH E .   ? 0.5330 0.4461 0.3702 0.0474  0.0770  0.0337  913  HOH A O   
4941 O  O   . HOH E .   ? 0.4939 0.5070 0.4547 0.0018  -0.0295 0.0090  914  HOH A O   
4942 O  O   . HOH E .   ? 0.5740 0.5723 0.5219 0.0044  -0.0189 0.0245  915  HOH A O   
4943 O  O   . HOH E .   ? 0.6044 0.5186 0.6372 0.0212  -0.0150 0.0079  916  HOH A O   
4944 O  O   . HOH E .   ? 0.3347 0.4244 0.4851 0.0467  -0.0434 0.0044  917  HOH A O   
4945 O  O   . HOH E .   ? 0.4968 0.4353 0.3348 0.0718  -0.0602 -0.0304 918  HOH A O   
4946 O  O   . HOH E .   ? 0.4577 0.3985 0.3030 0.0707  -0.0575 -0.0228 919  HOH A O   
4947 O  O   B HOH E .   ? 0.4356 0.4278 0.4021 0.0188  -0.0300 -0.0230 920  HOH A O   
4948 O  O   B HOH E .   ? 0.7571 0.6861 0.5874 0.0730  0.0828  -0.0040 921  HOH A O   
4949 O  O   . HOH E .   ? 0.4161 0.3719 0.3932 0.0333  -0.0074 -0.0341 922  HOH A O   
4950 O  O   . HOH E .   ? 0.5213 0.4950 0.4689 0.0278  -0.0410 -0.0404 923  HOH A O   
4951 O  O   B HOH E .   ? 0.4888 0.4986 0.4987 -0.0076 -0.0083 0.0063  924  HOH A O   
4952 O  O   . HOH E .   ? 0.2717 0.2495 0.2081 0.0291  -0.0207 -0.0048 925  HOH A O   
4953 O  O   . HOH E .   ? 0.5524 0.5653 0.5716 0.0215  0.1208  0.0252  926  HOH A O   
4954 O  O   . HOH E .   ? 0.3417 0.3096 0.2589 0.0391  -0.0272 -0.0054 927  HOH A O   
4955 O  O   . HOH E .   ? 0.4319 0.5314 0.6125 0.0577  -0.0249 0.0003  928  HOH A O   
4956 O  O   . HOH E .   ? 0.4942 0.4274 0.4275 0.0589  0.0065  -0.0518 929  HOH A O   
4957 O  O   . HOH E .   ? 0.4884 0.5554 0.6366 0.0715  -0.0432 0.0089  930  HOH A O   
4958 O  O   . HOH E .   ? 0.5809 0.4871 0.3924 0.0578  0.0795  0.0294  931  HOH A O   
4959 O  O   . HOH E .   ? 0.4066 0.4919 0.5463 -0.0060 0.0065  0.0000  932  HOH A O   
4960 O  O   B HOH E .   ? 0.5043 0.6275 0.7093 0.0278  0.0197  -0.0036 933  HOH A O   
4961 O  O   . HOH E .   ? 0.4373 0.4139 0.4568 0.0350  0.0008  -0.0146 934  HOH A O   
4962 O  O   . HOH E .   ? 0.5184 0.5141 0.5903 -0.0280 -0.0089 -0.0072 935  HOH A O   
4963 O  O   . HOH E .   ? 0.4183 0.3727 0.4100 0.0323  -0.0073 -0.0308 936  HOH A O   
4964 O  O   . HOH E .   ? 0.4651 0.4476 0.3975 0.0541  -0.0584 -0.0193 937  HOH A O   
4965 O  O   . HOH E .   ? 0.5017 0.5151 0.4764 -0.0015 -0.0199 0.0120  938  HOH A O   
4966 O  O   . HOH E .   ? 0.3674 0.3561 0.3443 0.0017  -0.0123 0.0308  939  HOH A O   
4967 O  O   . HOH E .   ? 0.3794 0.4194 0.4151 -0.0069 -0.0278 -0.0006 940  HOH A O   
4968 O  O   . HOH E .   ? 0.6314 0.5752 0.4816 0.0698  -0.0771 -0.0518 941  HOH A O   
4969 O  O   . HOH E .   ? 0.3764 0.3897 0.3957 -0.0086 -0.0110 -0.0028 942  HOH A O   
4970 O  O   . HOH E .   ? 0.4889 0.4530 0.5028 0.0430  0.0032  -0.0226 943  HOH A O   
4971 O  O   . HOH E .   ? 0.4303 0.3344 0.4335 0.0178  -0.0121 0.0485  944  HOH A O   
4972 O  O   . HOH E .   ? 0.4252 0.3876 0.3240 0.0546  -0.0466 -0.0123 945  HOH A O   
4973 O  O   . HOH E .   ? 0.4150 0.4269 0.4587 0.0533  0.0370  -0.0154 946  HOH A O   
4974 O  O   C HOH E .   ? 0.4803 0.6190 0.7095 0.0270  0.0049  -0.0058 947  HOH A O   
4975 O  O   . HOH E .   ? 0.5129 0.5066 0.6132 0.0799  -0.0179 0.0044  948  HOH A O   
4976 O  O   . HOH E .   ? 0.5076 0.4666 0.5138 0.0512  0.0092  -0.0293 949  HOH A O   
4977 O  O   . HOH E .   ? 0.4393 0.4120 0.4695 0.0377  -0.0025 -0.0110 950  HOH A O   
4978 O  O   . HOH F .   ? 0.5386 0.4284 0.4606 0.0058  0.0607  0.0493  701  HOH B O   
4979 O  O   . HOH F .   ? 0.6530 0.5084 0.6941 -0.0490 0.0521  0.0245  702  HOH B O   
4980 O  O   . HOH F .   ? 0.4050 0.5248 0.5478 0.0277  0.0137  -0.0384 703  HOH B O   
4981 O  O   . HOH F .   ? 0.5836 0.6012 0.6684 -0.0079 -0.0755 -0.0689 704  HOH B O   
4982 O  O   . HOH F .   ? 0.2724 0.3492 0.3550 0.0257  -0.0114 -0.0307 705  HOH B O   
4983 O  O   . HOH F .   ? 0.2962 0.3367 0.2945 0.0037  0.0269  -0.0093 706  HOH B O   
4984 O  O   . HOH F .   ? 0.3955 0.4023 0.3858 0.0104  -0.0277 -0.0183 707  HOH B O   
4985 O  O   . HOH F .   ? 0.3684 0.4291 0.4037 0.0116  0.0293  -0.0188 708  HOH B O   
4986 O  O   . HOH F .   ? 0.3869 0.3955 0.3948 0.0484  -0.0268 -0.0215 709  HOH B O   
4987 O  O   . HOH F .   ? 0.4618 0.4777 0.5078 -0.0252 -0.0113 -0.0083 710  HOH B O   
4988 O  O   . HOH F .   ? 0.2882 0.3225 0.3494 -0.0014 -0.0487 -0.0402 711  HOH B O   
4989 O  O   . HOH F .   ? 0.4127 0.4741 0.5911 -0.0418 0.0724  0.0162  712  HOH B O   
4990 O  O   . HOH F .   ? 0.3088 0.3154 0.2927 -0.0088 -0.0173 -0.0132 713  HOH B O   
4991 O  O   . HOH F .   ? 0.3994 0.3904 0.3646 -0.0036 -0.0171 -0.0260 714  HOH B O   
4992 O  O   . HOH F .   ? 0.3245 0.4572 0.4975 0.0347  -0.0247 -0.0488 715  HOH B O   
4993 O  O   . HOH F .   ? 0.4033 0.3193 0.3822 -0.0028 0.0024  -0.0048 716  HOH B O   
4994 O  O   . HOH F .   ? 0.4349 0.4403 0.3990 -0.0079 -0.0463 -0.0296 717  HOH B O   
4995 O  O   . HOH F .   ? 0.4860 0.4268 0.5204 -0.0359 -0.0120 -0.0268 718  HOH B O   
4996 O  O   . HOH F .   ? 0.4283 0.3904 0.4041 0.0285  -0.0081 -0.0215 719  HOH B O   
4997 O  O   . HOH F .   ? 0.4753 0.3153 0.3871 0.0081  0.0565  0.0561  720  HOH B O   
4998 O  O   . HOH F .   ? 0.4757 0.4554 0.4096 0.0392  -0.0370 -0.0115 721  HOH B O   
4999 O  O   . HOH F .   ? 0.4862 0.3892 0.4362 0.0297  -0.0044 0.0009  722  HOH B O   
5000 O  O   . HOH F .   ? 0.4401 0.3928 0.4053 0.0417  -0.0171 -0.0084 723  HOH B O   
5001 O  O   . HOH F .   ? 0.3353 0.3841 0.3921 0.0154  -0.0584 -0.0418 724  HOH B O   
5002 O  O   . HOH F .   ? 0.3008 0.3098 0.3910 -0.0422 0.0018  -0.0082 725  HOH B O   
5003 O  O   . HOH F .   ? 0.3300 0.3494 0.3413 0.0314  -0.0051 -0.0253 726  HOH B O   
5004 O  O   . HOH F .   ? 0.4133 0.3809 0.5234 -0.0611 0.0011  -0.0189 727  HOH B O   
5005 O  O   . HOH F .   ? 0.2420 0.2212 0.2336 -0.0069 0.0224  0.0144  728  HOH B O   
5006 O  O   . HOH F .   ? 0.4583 0.3521 0.4150 -0.0112 0.0876  0.0571  729  HOH B O   
5007 O  O   . HOH F .   ? 0.3055 0.4841 0.5902 -0.0272 0.0631  -0.0290 730  HOH B O   
5008 O  O   . HOH F .   ? 0.2922 0.3252 0.3635 -0.0180 -0.0171 -0.0179 731  HOH B O   
5009 O  O   . HOH F .   ? 0.3953 0.4099 0.4788 -0.0396 0.0277  0.0155  732  HOH B O   
5010 O  O   . HOH F .   ? 0.3421 0.3529 0.3319 -0.0131 -0.0358 -0.0220 733  HOH B O   
5011 O  O   . HOH F .   ? 0.3632 0.4040 0.3854 -0.0018 0.0041  -0.0086 734  HOH B O   
5012 O  O   . HOH F .   ? 0.6938 0.5790 0.5631 0.0334  0.0357  0.0439  735  HOH B O   
5013 O  O   . HOH F .   ? 0.4242 0.3389 0.3885 0.0251  -0.0065 -0.0177 736  HOH B O   
5014 O  O   . HOH F .   ? 0.4232 0.3590 0.3605 0.0389  -0.0141 0.0065  737  HOH B O   
5015 O  O   . HOH F .   ? 0.5021 0.5019 0.5330 -0.0042 -0.0344 -0.0307 738  HOH B O   
5016 O  O   . HOH F .   ? 0.4212 0.4173 0.3605 -0.0020 -0.0342 -0.0298 739  HOH B O   
5017 O  O   . HOH F .   ? 0.3170 0.4507 0.5683 -0.0357 -0.0013 -0.0413 740  HOH B O   
5018 O  O   . HOH F .   ? 0.4126 0.5134 0.5341 0.0476  -0.0136 -0.0426 741  HOH B O   
5019 O  O   . HOH F .   ? 0.3618 0.4179 0.4181 0.0347  -0.0266 -0.0291 742  HOH B O   
5020 O  O   . HOH F .   ? 0.3747 0.3819 0.4031 -0.0239 0.0193  0.0208  743  HOH B O   
5021 O  O   . HOH F .   ? 0.2849 0.2850 0.2695 0.0423  -0.0349 -0.0144 744  HOH B O   
5022 O  O   . HOH F .   ? 0.3181 0.3227 0.3140 -0.0038 0.0007  0.0033  745  HOH B O   
5023 O  O   . HOH F .   ? 0.4464 0.4566 0.4730 -0.0293 0.0506  0.0337  746  HOH B O   
5024 O  O   . HOH F .   ? 0.3138 0.3127 0.3392 -0.0259 -0.0275 -0.0246 747  HOH B O   
5025 O  O   . HOH F .   ? 0.3465 0.5100 0.5677 0.0244  0.0034  -0.0495 748  HOH B O   
5026 O  O   . HOH F .   ? 0.3756 0.4026 0.4319 -0.0262 -0.0222 -0.0133 749  HOH B O   
5027 O  O   . HOH F .   ? 0.2672 0.2437 0.2137 0.0199  -0.0077 0.0028  750  HOH B O   
5028 O  O   . HOH F .   ? 0.5187 0.5127 0.4626 -0.0049 -0.0509 -0.0404 751  HOH B O   
5029 O  O   . HOH F .   ? 0.4207 0.4090 0.3645 0.0376  -0.0445 -0.0195 752  HOH B O   
5030 O  O   . HOH F .   ? 0.2128 0.2138 0.1970 0.0045  -0.0069 -0.0128 753  HOH B O   
5031 O  O   . HOH F .   ? 0.4778 0.5093 0.4530 0.0014  0.0323  -0.0021 754  HOH B O   
5032 O  O   . HOH F .   ? 0.3219 0.3544 0.3364 0.0447  -0.0642 -0.0329 755  HOH B O   
5033 O  O   . HOH F .   ? 0.3029 0.3148 0.2961 -0.0013 -0.0086 -0.0024 756  HOH B O   
5034 O  O   . HOH F .   ? 0.2835 0.2077 0.2747 -0.0125 -0.0096 -0.0263 757  HOH B O   
5035 O  O   . HOH F .   ? 0.4248 0.2616 0.3729 -0.0081 0.0566  0.0489  758  HOH B O   
5036 O  O   . HOH F .   ? 0.3639 0.2837 0.3341 0.0008  0.0077  0.0060  759  HOH B O   
5037 O  O   . HOH F .   ? 0.3511 0.3119 0.4081 -0.0359 0.0886  0.0402  760  HOH B O   
5038 O  O   . HOH F .   ? 0.2881 0.2267 0.2600 0.0113  -0.0068 -0.0198 761  HOH B O   
5039 O  O   . HOH F .   ? 0.3325 0.3445 0.3044 -0.0072 0.0054  0.0148  762  HOH B O   
5040 O  O   . HOH F .   ? 0.2980 0.2832 0.2643 0.0080  0.0020  0.0054  763  HOH B O   
5041 O  O   . HOH F .   ? 0.2959 0.3046 0.2875 0.0072  -0.0204 -0.0121 764  HOH B O   
5042 O  O   . HOH F .   ? 0.2678 0.2795 0.2761 -0.0009 -0.0176 -0.0106 765  HOH B O   
5043 O  O   A HOH F .   ? 0.5138 0.5068 0.5050 -0.0116 0.0059  0.0277  766  HOH B O   
5044 O  O   . HOH F .   ? 0.4679 0.3564 0.4278 0.0194  -0.0017 -0.0075 767  HOH B O   
5045 O  O   . HOH F .   ? 0.4493 0.4447 0.3857 0.0171  0.0078  -0.0346 768  HOH B O   
5046 O  O   A HOH F .   ? 0.2408 0.3921 0.4744 -0.0151 0.0185  -0.0367 769  HOH B O   
5047 O  O   . HOH F .   ? 0.2597 0.3855 0.4859 -0.0240 -0.0244 -0.0489 770  HOH B O   
5048 O  O   . HOH F .   ? 0.1771 0.2400 0.2426 0.0020  -0.0049 -0.0191 771  HOH B O   
5049 O  O   . HOH F .   ? 0.4734 0.4795 0.4368 -0.0069 -0.0353 -0.0226 772  HOH B O   
5050 O  O   . HOH F .   ? 0.5029 0.4009 0.3871 0.0254  0.0455  0.0432  773  HOH B O   
5051 O  O   . HOH F .   ? 0.4085 0.4210 0.4080 0.0472  -0.0415 -0.0197 774  HOH B O   
5052 O  O   . HOH F .   ? 0.5929 0.5038 0.5140 0.0475  -0.0134 0.0129  775  HOH B O   
5053 O  O   . HOH F .   ? 0.3054 0.3682 0.3627 0.0286  0.0048  -0.0293 776  HOH B O   
5054 O  O   . HOH F .   ? 0.2763 0.2914 0.2814 -0.0029 -0.0119 -0.0039 777  HOH B O   
5055 O  O   . HOH F .   ? 0.2599 0.2769 0.2640 -0.0044 -0.0074 0.0020  778  HOH B O   
5056 O  O   . HOH F .   ? 0.4641 0.4295 0.4119 0.0559  -0.0375 -0.0048 779  HOH B O   
5057 O  O   . HOH F .   ? 0.2599 0.2631 0.2472 0.0084  -0.0101 -0.0080 780  HOH B O   
5058 O  O   . HOH F .   ? 0.4138 0.4914 0.6246 -0.0323 -0.0762 -0.0789 781  HOH B O   
5059 O  O   . HOH F .   ? 0.3784 0.4003 0.4088 0.0080  -0.0529 -0.0404 782  HOH B O   
5060 O  O   A HOH F .   ? 0.3254 0.3410 0.3004 -0.0036 -0.0060 -0.0060 783  HOH B O   
5061 O  O   . HOH F .   ? 0.6289 0.5598 0.5509 0.0743  -0.0409 0.0036  784  HOH B O   
5062 O  O   . HOH F .   ? 0.2234 0.2365 0.2175 0.0012  -0.0108 -0.0043 785  HOH B O   
5063 O  O   . HOH F .   ? 0.2474 0.2446 0.2118 0.0245  -0.0308 -0.0138 786  HOH B O   
5064 O  O   . HOH F .   ? 0.2127 0.2540 0.2294 -0.0003 0.0101  -0.0090 787  HOH B O   
5065 O  O   . HOH F .   ? 0.3283 0.3091 0.2901 0.0074  -0.0079 -0.0313 788  HOH B O   
5066 O  O   . HOH F .   ? 0.4417 0.4561 0.5134 -0.0134 -0.0447 -0.0419 789  HOH B O   
5067 O  O   . HOH F .   ? 0.1992 0.2941 0.3108 0.0243  -0.0138 -0.0351 790  HOH B O   
5068 O  O   . HOH F .   ? 0.3221 0.3679 0.3634 0.0338  -0.0323 -0.0266 791  HOH B O   
5069 O  O   . HOH F .   ? 0.2667 0.2867 0.2797 -0.0174 0.0192  0.0156  792  HOH B O   
5070 O  O   B HOH F .   ? 0.3283 0.3394 0.2887 0.0044  0.0024  -0.0166 793  HOH B O   
5071 O  O   . HOH F .   ? 0.3216 0.3185 0.3727 -0.0340 -0.0178 -0.0197 794  HOH B O   
5072 O  O   . HOH F .   ? 0.2627 0.2541 0.2425 0.0249  0.0003  -0.0305 795  HOH B O   
5073 O  O   . HOH F .   ? 0.4423 0.4396 0.4422 -0.0204 -0.0457 -0.0386 796  HOH B O   
5074 O  O   . HOH F .   ? 0.4199 0.3237 0.4455 -0.0336 0.0040  -0.0143 797  HOH B O   
5075 O  O   . HOH F .   ? 0.4997 0.4226 0.5684 -0.0516 0.0594  0.0261  798  HOH B O   
5076 O  O   . HOH F .   ? 0.3805 0.3791 0.3614 -0.0108 -0.0239 -0.0222 799  HOH B O   
5077 O  O   . HOH F .   ? 0.4599 0.4249 0.4970 -0.0257 0.0907  0.0412  800  HOH B O   
5078 O  O   . HOH F .   ? 0.4285 0.4612 0.4548 0.0223  -0.0631 -0.0413 801  HOH B O   
5079 O  O   . HOH F .   ? 0.4988 0.3943 0.5227 -0.0393 0.1007  0.0565  802  HOH B O   
5080 O  O   A HOH F .   ? 0.3707 0.3876 0.3392 0.0047  0.0064  -0.0146 803  HOH B O   
5081 O  O   . HOH F .   ? 0.4154 0.4011 0.3845 -0.0132 -0.0478 -0.0463 804  HOH B O   
5082 O  O   . HOH F .   ? 0.2635 0.3026 0.3345 -0.0131 -0.0233 -0.0230 805  HOH B O   
5083 O  O   . HOH F .   ? 0.4767 0.3151 0.3839 0.0053  0.0724  0.0647  806  HOH B O   
5084 O  O   . HOH F .   ? 0.3585 0.2617 0.3077 0.0147  -0.0164 -0.0636 807  HOH B O   
5085 O  O   . HOH F .   ? 0.2574 0.2697 0.2572 0.0205  -0.0102 -0.0168 808  HOH B O   
5086 O  O   . HOH F .   ? 0.4175 0.4367 0.4020 -0.0142 0.0500  0.0257  809  HOH B O   
5087 O  O   . HOH F .   ? 0.2890 0.3328 0.3602 0.0026  -0.0577 -0.0464 810  HOH B O   
5088 O  O   . HOH F .   ? 0.4864 0.5844 0.7448 -0.0375 -0.0895 -0.0934 811  HOH B O   
5089 O  O   . HOH F .   ? 0.3648 0.3874 0.4115 -0.0264 -0.0332 -0.0211 812  HOH B O   
5090 O  O   . HOH F .   ? 0.3850 0.3564 0.3221 0.0015  -0.0256 -0.0466 813  HOH B O   
5091 O  O   . HOH F .   ? 0.2998 0.2938 0.2840 0.0433  -0.0302 -0.0135 814  HOH B O   
5092 O  O   . HOH F .   ? 0.2714 0.3524 0.3550 -0.0099 0.0484  -0.0060 815  HOH B O   
5093 O  O   . HOH F .   ? 0.4563 0.4965 0.6524 -0.0564 -0.0171 -0.0361 816  HOH B O   
5094 O  O   . HOH F .   ? 0.5495 0.4510 0.5123 0.0315  -0.0071 -0.0260 817  HOH B O   
5095 O  O   . HOH F .   ? 0.3519 0.2845 0.3337 -0.0046 0.0016  -0.0042 818  HOH B O   
5096 O  O   . HOH F .   ? 0.4724 0.3433 0.3334 0.0618  -0.0065 0.0340  819  HOH B O   
5097 O  O   . HOH F .   ? 0.3283 0.3285 0.3245 0.0319  -0.0056 -0.0253 820  HOH B O   
5098 O  O   . HOH F .   ? 0.2127 0.2337 0.2215 0.0239  -0.0067 -0.0210 821  HOH B O   
5099 O  O   . HOH F .   ? 0.2625 0.2768 0.2543 -0.0021 -0.0077 -0.0055 822  HOH B O   
5100 O  O   . HOH F .   ? 0.4378 0.3678 0.3920 0.0314  -0.0090 -0.0011 823  HOH B O   
5101 O  O   A HOH F .   ? 0.5663 0.4332 0.5667 -0.0202 0.0059  -0.0129 824  HOH B O   
5102 O  O   . HOH F .   ? 0.1785 0.3027 0.3771 -0.0122 -0.0188 -0.0435 825  HOH B O   
5103 O  O   . HOH F .   ? 0.2740 0.2607 0.2243 0.0278  -0.0260 -0.0081 826  HOH B O   
5104 O  O   . HOH F .   ? 0.4129 0.4143 0.3947 -0.0066 -0.0028 0.0223  827  HOH B O   
5105 O  O   . HOH F .   ? 0.3550 0.4523 0.4708 -0.0184 0.0816  0.0014  828  HOH B O   
5106 O  O   . HOH F .   ? 0.2695 0.2301 0.2347 0.0119  -0.0082 -0.0343 829  HOH B O   
5107 O  O   . HOH F .   ? 0.3172 0.4687 0.5249 0.0246  -0.0217 -0.0520 830  HOH B O   
5108 O  O   . HOH F .   ? 0.6831 0.6931 0.6403 -0.0025 -0.0095 0.0108  831  HOH B O   
5109 O  O   . HOH F .   ? 0.2595 0.2531 0.2644 -0.0146 -0.0072 -0.0067 832  HOH B O   
5110 O  O   . HOH F .   ? 0.4893 0.5128 0.4685 0.0179  0.0189  -0.0255 833  HOH B O   
5111 O  O   . HOH F .   ? 0.3395 0.3257 0.2998 0.0133  -0.0057 0.0015  834  HOH B O   
5112 O  O   . HOH F .   ? 0.2937 0.3128 0.2910 -0.0013 -0.0077 -0.0053 835  HOH B O   
5113 O  O   . HOH F .   ? 0.4380 0.4236 0.5080 -0.0317 0.0911  0.0367  836  HOH B O   
5114 O  O   . HOH F .   ? 0.3068 0.3139 0.3028 -0.0107 -0.0134 -0.0083 837  HOH B O   
5115 O  O   . HOH F .   ? 0.3900 0.3423 0.4149 -0.0302 -0.0112 -0.0226 838  HOH B O   
5116 O  O   . HOH F .   ? 0.2691 0.2180 0.2406 0.0173  -0.0072 -0.0174 839  HOH B O   
5117 O  O   B HOH F .   ? 0.5122 0.5022 0.5153 -0.0134 0.0046  0.0257  840  HOH B O   
5118 O  O   . HOH F .   ? 0.5413 0.5653 0.5107 -0.0067 0.0511  0.0177  841  HOH B O   
5119 O  O   . HOH F .   ? 0.4815 0.3722 0.5609 -0.0609 0.0325  0.0026  842  HOH B O   
5120 O  O   . HOH F .   ? 0.2846 0.3295 0.2984 0.0027  0.0203  -0.0106 843  HOH B O   
5121 O  O   . HOH F .   ? 0.4351 0.3903 0.5512 -0.0633 0.0574  0.0182  844  HOH B O   
5122 O  O   . HOH F .   ? 0.2882 0.2100 0.2604 0.0007  -0.0138 -0.0397 845  HOH B O   
5123 O  O   . HOH F .   ? 0.2380 0.2714 0.2545 0.0052  -0.0072 -0.0124 846  HOH B O   
5124 O  O   . HOH F .   ? 0.2755 0.2764 0.3072 -0.0175 0.0251  0.0117  847  HOH B O   
5125 O  O   . HOH F .   ? 0.3859 0.4099 0.3882 0.0352  -0.0694 -0.0395 848  HOH B O   
5126 O  O   . HOH F .   ? 0.3664 0.3285 0.3155 0.0091  -0.0124 -0.0445 849  HOH B O   
5127 O  O   . HOH F .   ? 0.3118 0.4154 0.4306 0.0033  0.0307  -0.0228 850  HOH B O   
5128 O  O   . HOH F .   ? 0.3191 0.2879 0.2864 0.0251  -0.0021 -0.0371 851  HOH B O   
5129 O  O   . HOH F .   ? 0.3662 0.4714 0.4920 0.0318  -0.0088 -0.0388 852  HOH B O   
5130 O  O   . HOH F .   ? 0.5766 0.4466 0.4058 0.0756  -0.0159 0.0342  853  HOH B O   
5131 O  O   . HOH F .   ? 0.3920 0.3919 0.3924 -0.0087 -0.0039 0.0188  854  HOH B O   
5132 O  O   . HOH F .   ? 0.3947 0.4927 0.4982 0.0324  0.0226  -0.0358 855  HOH B O   
5133 O  O   . HOH F .   ? 0.4240 0.3369 0.5090 -0.0601 0.0388  0.0085  856  HOH B O   
5134 O  O   . HOH F .   ? 0.3165 0.4349 0.4723 -0.0090 0.0405  -0.0205 857  HOH B O   
5135 O  O   . HOH F .   ? 0.3078 0.3350 0.3728 -0.0205 0.0183  0.0065  858  HOH B O   
5136 O  O   A HOH F .   ? 0.3644 0.3889 0.3978 -0.0159 -0.0101 -0.0023 859  HOH B O   
5137 O  O   . HOH F .   ? 0.4588 0.4742 0.4156 0.0123  0.0161  -0.0216 860  HOH B O   
5138 O  O   . HOH F .   ? 0.3045 0.3209 0.3034 -0.0079 -0.0065 0.0072  861  HOH B O   
5139 O  O   . HOH F .   ? 0.3815 0.5219 0.6174 -0.0411 0.0879  -0.0062 862  HOH B O   
5140 O  O   . HOH F .   ? 0.4102 0.3120 0.4527 -0.0448 0.0681  0.0359  863  HOH B O   
5141 O  O   . HOH F .   ? 0.3818 0.5199 0.5593 0.0195  0.0113  -0.0404 864  HOH B O   
5142 O  O   B HOH F .   ? 0.3722 0.4455 0.4484 0.0339  -0.0016 -0.0327 865  HOH B O   
5143 O  O   . HOH F .   ? 0.3829 0.3986 0.3463 -0.0037 0.0015  0.0036  866  HOH B O   
5144 O  O   A HOH F .   ? 0.2791 0.4529 0.5556 -0.0149 0.0097  -0.0466 867  HOH B O   
5145 O  O   . HOH F .   ? 0.3132 0.3402 0.4003 -0.0286 -0.0055 -0.0105 868  HOH B O   
5146 O  O   . HOH F .   ? 0.4787 0.4635 0.4199 0.0550  -0.0567 -0.0169 869  HOH B O   
5147 O  O   . HOH F .   ? 0.3764 0.3979 0.3976 0.0427  -0.0123 -0.0274 870  HOH B O   
5148 O  O   . HOH F .   ? 0.6073 0.4572 0.6474 -0.0515 0.0734  0.0406  871  HOH B O   
5149 O  O   . HOH F .   ? 0.5049 0.4876 0.4617 0.0620  -0.0522 -0.0127 872  HOH B O   
5150 O  O   . HOH F .   ? 0.3026 0.1919 0.2743 0.0035  0.0021  -0.0073 873  HOH B O   
5151 O  O   . HOH F .   ? 0.3067 0.3449 0.3125 0.0236  0.0225  -0.0279 874  HOH B O   
5152 O  O   . HOH F .   ? 0.3091 0.3283 0.3393 -0.0215 0.0175  0.0145  875  HOH B O   
5153 O  O   . HOH F .   ? 0.3512 0.3542 0.3108 0.0186  0.0098  -0.0318 876  HOH B O   
5154 O  O   . HOH F .   ? 0.4569 0.3538 0.3324 0.0786  -0.0345 0.0187  877  HOH B O   
5155 O  O   . HOH F .   ? 0.2891 0.2178 0.2871 -0.0161 -0.0022 -0.0140 878  HOH B O   
5156 O  O   . HOH F .   ? 0.2791 0.2870 0.3075 -0.0146 0.0162  0.0081  879  HOH B O   
5157 O  O   . HOH F .   ? 0.3178 0.3156 0.3074 -0.0017 0.0054  0.0056  880  HOH B O   
5158 O  O   . HOH F .   ? 0.5129 0.5273 0.4683 -0.0013 0.0017  -0.0016 881  HOH B O   
5159 O  O   . HOH F .   ? 0.3576 0.4391 0.4558 -0.0240 0.0854  0.0109  882  HOH B O   
5160 O  O   . HOH F .   ? 0.3157 0.3217 0.3646 -0.0240 0.0201  0.0079  883  HOH B O   
5161 O  O   . HOH F .   ? 0.4323 0.5271 0.5433 0.0583  -0.0937 -0.0586 884  HOH B O   
5162 O  O   . HOH F .   ? 0.3491 0.3390 0.3263 -0.0081 -0.0187 -0.0239 885  HOH B O   
5163 O  O   . HOH F .   ? 0.2567 0.2751 0.2532 -0.0070 -0.0116 0.0003  886  HOH B O   
5164 O  O   . HOH F .   ? 0.3187 0.3365 0.3804 -0.0373 0.0512  0.0288  887  HOH B O   
5165 O  O   . HOH F .   ? 0.5036 0.5038 0.4367 0.0016  -0.0185 -0.0199 888  HOH B O   
5166 O  O   B HOH F .   ? 0.5475 0.4101 0.5320 -0.0093 0.0078  -0.0065 889  HOH B O   
5167 O  O   . HOH F .   ? 0.4071 0.4446 0.5848 -0.0610 0.0278  -0.0026 890  HOH B O   
5168 O  O   . HOH F .   ? 0.3699 0.3740 0.3422 -0.0062 -0.0176 -0.0167 891  HOH B O   
5169 O  O   . HOH F .   ? 0.4111 0.2993 0.3870 -0.0032 0.0081  0.0004  892  HOH B O   
5170 O  O   . HOH F .   ? 0.4456 0.5281 0.5156 0.0198  0.0356  -0.0264 893  HOH B O   
5171 O  O   . HOH F .   ? 0.3840 0.4008 0.3884 -0.0088 -0.0102 -0.0007 894  HOH B O   
5172 O  O   . HOH F .   ? 0.3877 0.4340 0.4496 0.0115  -0.0633 -0.0471 895  HOH B O   
5173 O  O   . HOH F .   ? 0.4577 0.2997 0.4468 -0.0313 0.0816  0.0558  896  HOH B O   
5174 O  O   . HOH F .   ? 0.3868 0.4083 0.3999 0.0440  -0.0358 -0.0218 897  HOH B O   
5175 O  O   . HOH F .   ? 0.3426 0.3915 0.4788 -0.0527 0.0706  0.0220  898  HOH B O   
5176 O  O   . HOH F .   ? 0.3790 0.3952 0.3633 0.0252  0.0141  -0.0316 899  HOH B O   
5177 O  O   . HOH F .   ? 0.5521 0.5889 0.6015 0.0212  -0.0914 -0.0658 900  HOH B O   
5178 O  O   . HOH F .   ? 0.5746 0.4407 0.4509 0.0243  0.0543  0.0551  901  HOH B O   
5179 O  O   . HOH F .   ? 0.6510 0.5186 0.5382 0.0289  0.0305  0.0444  902  HOH B O   
5180 O  O   . HOH F .   ? 0.5760 0.4227 0.5362 -0.0040 0.0302  0.0262  903  HOH B O   
5181 O  O   . HOH F .   ? 0.4616 0.5636 0.5867 0.0600  -0.0690 -0.0519 904  HOH B O   
5182 O  O   . HOH F .   ? 0.3309 0.4242 0.5935 -0.0671 0.0198  -0.0257 905  HOH B O   
5183 O  O   . HOH F .   ? 0.3627 0.3579 0.3571 -0.0090 -0.0080 -0.0069 906  HOH B O   
5184 O  O   . HOH F .   ? 0.4028 0.4353 0.3894 -0.0056 0.0373  0.0073  907  HOH B O   
5185 O  O   . HOH F .   ? 0.3159 0.3334 0.3223 0.0310  0.0009  -0.0281 908  HOH B O   
5186 O  O   . HOH F .   ? 0.3511 0.4270 0.4396 0.0549  -0.0448 -0.0399 909  HOH B O   
5187 O  O   . HOH F .   ? 0.5439 0.5724 0.5477 0.0492  -0.0791 -0.0399 910  HOH B O   
5188 O  O   . HOH F .   ? 0.6664 0.5242 0.6850 -0.0417 0.0769  0.0468  911  HOH B O   
5189 O  O   . HOH F .   ? 0.2559 0.3240 0.3109 -0.0054 0.0419  -0.0058 912  HOH B O   
5190 O  O   . HOH F .   ? 0.3294 0.4234 0.4292 -0.0001 0.0394  -0.0169 913  HOH B O   
5191 O  O   . HOH F .   ? 0.4504 0.4403 0.4184 0.0510  -0.0431 -0.0128 914  HOH B O   
5192 O  O   . HOH F .   ? 0.5175 0.5249 0.5623 -0.0100 -0.0300 -0.0262 915  HOH B O   
5193 O  O   . HOH F .   ? 0.3313 0.3582 0.4200 -0.0327 0.0067  -0.0018 916  HOH B O   
5194 O  O   . HOH F .   ? 0.6128 0.5134 0.5293 0.0195  0.0234  0.0319  917  HOH B O   
5195 O  O   . HOH F .   ? 0.5394 0.5266 0.5526 -0.0248 -0.0328 -0.0335 918  HOH B O   
5196 O  O   C HOH F .   ? 0.6157 0.6139 0.5976 0.0132  -0.0297 -0.0227 919  HOH B O   
5197 O  O   . HOH F .   ? 0.3470 0.3798 0.3568 0.0302  0.0162  -0.0318 920  HOH B O   
5198 O  O   . HOH F .   ? 0.6343 0.6435 0.6298 0.0599  -0.0526 -0.0214 921  HOH B O   
5199 O  O   . HOH F .   ? 0.3182 0.3264 0.3202 -0.0073 -0.0026 0.0016  922  HOH B O   
5200 O  O   . HOH F .   ? 0.4444 0.4316 0.6082 -0.0743 0.0280  -0.0054 923  HOH B O   
5201 O  O   . HOH F .   ? 0.3291 0.2955 0.2895 0.0072  -0.0108 -0.0366 924  HOH B O   
5202 O  O   B HOH F .   ? 0.3822 0.3967 0.3518 -0.0018 -0.0038 -0.0085 925  HOH B O   
5203 O  O   . HOH F .   ? 0.5237 0.3824 0.4403 0.0003  0.0864  0.0663  926  HOH B O   
5204 O  O   . HOH F .   ? 0.4725 0.4052 0.4372 0.0345  -0.0099 -0.0133 927  HOH B O   
5205 O  O   . HOH F .   ? 0.4654 0.4739 0.5110 -0.0244 0.0058  0.0010  928  HOH B O   
5206 O  O   . HOH F .   ? 0.3391 0.3573 0.3276 -0.0067 -0.0118 0.0002  929  HOH B O   
5207 O  O   B HOH F .   ? 0.2896 0.4555 0.5424 -0.0088 0.0123  -0.0435 930  HOH B O   
5208 O  O   . HOH F .   ? 0.3261 0.3242 0.3241 -0.0051 0.0112  0.0078  931  HOH B O   
5209 O  O   . HOH F .   ? 0.5152 0.5166 0.4597 -0.0032 -0.0432 -0.0286 932  HOH B O   
5210 O  O   . HOH F .   ? 0.3964 0.3629 0.4192 -0.0290 -0.0199 -0.0282 933  HOH B O   
5211 O  O   . HOH F .   ? 0.5427 0.5541 0.5039 0.0011  -0.0019 -0.0129 934  HOH B O   
5212 O  O   . HOH F .   ? 0.3637 0.3763 0.3756 -0.0108 -0.0036 0.0009  935  HOH B O   
5213 O  O   . HOH F .   ? 0.3358 0.3523 0.3386 -0.0067 -0.0087 0.0046  936  HOH B O   
5214 O  O   . HOH F .   ? 0.2710 0.2655 0.2505 0.0028  0.0002  0.0036  937  HOH B O   
5215 O  O   . HOH F .   ? 0.3255 0.4048 0.3938 0.0120  0.0316  -0.0216 938  HOH B O   
5216 O  O   A HOH F .   ? 0.2968 0.3755 0.3792 0.0270  -0.0007 -0.0309 939  HOH B O   
5217 O  O   . HOH F .   ? 0.5221 0.5202 0.5204 0.0096  -0.0391 -0.0328 940  HOH B O   
5218 O  O   . HOH F .   ? 0.4533 0.4268 0.4286 0.0572  -0.0317 -0.0123 941  HOH B O   
5219 O  O   . HOH F .   ? 0.4697 0.4449 0.4712 -0.0222 -0.0324 -0.0382 942  HOH B O   
5220 O  O   . HOH F .   ? 0.3671 0.3819 0.3653 -0.0107 -0.0163 -0.0063 943  HOH B O   
5221 O  O   . HOH F .   ? 0.3907 0.4062 0.4110 -0.0110 -0.0072 0.0010  944  HOH B O   
5222 O  O   . HOH F .   ? 0.4876 0.4947 0.4489 -0.0095 0.0317  0.0262  945  HOH B O   
5223 O  O   . HOH F .   ? 0.3852 0.4001 0.4046 -0.0108 0.0017  0.0033  946  HOH B O   
5224 O  O   . HOH F .   ? 0.5009 0.4717 0.5993 -0.0570 -0.0135 -0.0286 947  HOH B O   
5225 O  O   . HOH F .   ? 0.4653 0.3622 0.3912 0.0114  0.0337  0.0358  948  HOH B O   
5226 O  O   B HOH F .   ? 0.5258 0.4439 0.5436 -0.0300 -0.0151 -0.0348 949  HOH B O   
5227 O  O   . HOH F .   ? 0.4494 0.4813 0.4706 -0.0107 -0.0285 -0.0048 950  HOH B O   
5228 O  O   A HOH F .   ? 0.3837 0.3098 0.4024 -0.0292 -0.0096 -0.0261 951  HOH B O   
5229 O  O   . HOH F .   ? 0.5235 0.5327 0.5360 0.0492  -0.0205 -0.0247 952  HOH B O   
5230 O  O   . HOH F .   ? 0.3906 0.3064 0.3932 -0.0199 -0.0057 -0.0220 953  HOH B O   
5231 O  O   . HOH F .   ? 0.4305 0.3348 0.4011 0.0007  0.0077  0.0040  954  HOH B O   
5232 O  O   . HOH F .   ? 0.3386 0.3484 0.4085 -0.0353 -0.0052 -0.0094 955  HOH B O   
5233 O  O   B HOH F .   ? 0.3859 0.2875 0.3398 0.0077  0.0131  0.0158  956  HOH B O   
5234 O  O   . HOH F .   ? 0.5663 0.5889 0.5233 0.0050  0.0243  -0.0070 957  HOH B O   
5235 O  O   . HOH F .   ? 0.6133 0.4952 0.6037 -0.0286 0.1087  0.0653  958  HOH B O   
5236 O  O   . HOH F .   ? 0.2961 0.2103 0.2771 -0.0047 -0.0108 -0.0318 959  HOH B O   
5237 O  O   . HOH F .   ? 0.4653 0.4990 0.5030 0.0175  -0.0684 -0.0483 960  HOH B O   
5238 O  O   . HOH F .   ? 0.5714 0.5803 0.5477 0.0369  -0.0603 -0.0314 961  HOH B O   
5239 O  O   . HOH F .   ? 0.4020 0.3300 0.3702 0.0192  -0.0070 -0.0234 962  HOH B O   
5240 O  O   . HOH F .   ? 0.6028 0.4538 0.4981 0.0238  0.0355  0.0475  963  HOH B O   
5241 O  O   . HOH F .   ? 0.5382 0.5319 0.6006 -0.0398 -0.0256 -0.0284 964  HOH B O   
5242 O  O   . HOH F .   ? 0.4951 0.4897 0.4180 0.0025  -0.0282 -0.0273 965  HOH B O   
5243 O  O   . HOH F .   ? 0.4073 0.5287 0.5643 0.0502  -0.0879 -0.0643 966  HOH B O   
5244 O  O   . HOH F .   ? 0.2460 0.2519 0.2592 -0.0093 0.0115  0.0072  967  HOH B O   
5245 O  O   . HOH F .   ? 0.4038 0.4157 0.3881 -0.0091 -0.0207 -0.0111 968  HOH B O   
5246 O  O   . HOH F .   ? 0.3470 0.2929 0.3175 0.0277  -0.0083 -0.0191 969  HOH B O   
5247 O  O   . HOH F .   ? 0.4032 0.4721 0.4764 -0.0237 0.0956  0.0193  970  HOH B O   
5248 O  O   . HOH F .   ? 0.5520 0.5832 0.5829 0.0249  -0.0836 -0.0574 971  HOH B O   
5249 O  O   . HOH F .   ? 0.3949 0.4034 0.4600 -0.0352 -0.0144 -0.0155 972  HOH B O   
5250 O  O   . HOH F .   ? 0.3911 0.4143 0.3622 0.0067  0.0153  -0.0141 973  HOH B O   
5251 O  O   . HOH F .   ? 0.4302 0.4399 0.4168 -0.0133 -0.0463 -0.0294 974  HOH B O   
5252 O  O   . HOH F .   ? 0.5359 0.5476 0.4874 -0.0029 0.0090  0.0100  975  HOH B O   
5253 O  O   . HOH F .   ? 0.7362 0.7038 0.6745 0.0306  0.0057  -0.0534 976  HOH B O   
5254 O  O   . HOH F .   ? 0.3805 0.5813 0.6842 0.0019  0.0075  -0.0557 977  HOH B O   
5255 O  O   . HOH F .   ? 0.5152 0.4602 0.5530 -0.0382 -0.0218 -0.0366 978  HOH B O   
5256 O  O   . HOH F .   ? 0.4613 0.4608 0.4350 -0.0129 -0.0588 -0.0440 979  HOH B O   
5257 O  O   . HOH F .   ? 0.5242 0.6023 0.7186 -0.0400 0.0581  0.0094  980  HOH B O   
5258 O  O   . HOH F .   ? 0.4670 0.3760 0.5143 -0.0440 0.0090  -0.0116 981  HOH B O   
5259 O  O   . HOH F .   ? 0.6320 0.6403 0.5806 0.0003  -0.0074 -0.0116 982  HOH B O   
5260 O  O   . HOH F .   ? 0.4135 0.4444 0.3917 0.0058  0.0242  -0.0107 983  HOH B O   
5261 O  O   . HOH F .   ? 0.4331 0.4563 0.4540 0.0161  -0.0594 -0.0420 984  HOH B O   
5262 O  O   . HOH F .   ? 0.3046 0.3458 0.3897 -0.0211 0.0156  0.0043  985  HOH B O   
5263 O  O   . HOH F .   ? 0.3802 0.5302 0.5726 0.0262  0.0185  -0.0439 986  HOH B O   
5264 O  O   . HOH F .   ? 0.4276 0.4329 0.4217 -0.0171 -0.0504 -0.0364 987  HOH B O   
5265 O  O   . HOH F .   ? 0.5013 0.5098 0.5042 0.0499  -0.0348 -0.0197 988  HOH B O   
5266 O  O   . HOH F .   ? 0.5464 0.5551 0.6122 -0.0425 0.0606  0.0365  989  HOH B O   
5267 O  O   . HOH F .   ? 0.3763 0.3982 0.4442 -0.0255 0.0159  0.0048  990  HOH B O   
5268 O  O   . HOH F .   ? 0.3721 0.4664 0.4783 0.0340  0.0012  -0.0365 991  HOH B O   
5269 O  O   A HOH F .   ? 0.3407 0.3542 0.3481 -0.0070 -0.0086 0.0047  992  HOH B O   
5270 O  O   . HOH F .   ? 0.4503 0.4650 0.4204 -0.0044 -0.0100 -0.0041 993  HOH B O   
5271 O  O   . HOH F .   ? 0.4168 0.4598 0.4458 0.0535  -0.0773 -0.0397 994  HOH B O   
5272 O  O   . HOH F .   ? 0.3739 0.3851 0.4205 -0.0302 -0.0314 -0.0249 995  HOH B O   
5273 O  O   . HOH F .   ? 0.5988 0.6041 0.5662 0.0564  -0.0718 -0.0290 996  HOH B O   
5274 O  O   . HOH F .   ? 0.4570 0.4648 0.5121 -0.0113 -0.0369 -0.0339 997  HOH B O   
5275 O  O   . HOH F .   ? 0.3319 0.3981 0.3769 0.0021  0.0380  -0.0112 998  HOH B O   
5276 O  O   . HOH F .   ? 0.4459 0.5277 0.5171 0.0054  0.0408  -0.0166 999  HOH B O   
5277 O  O   . HOH F .   ? 0.4369 0.4953 0.4693 0.0052  0.0300  -0.0134 1000 HOH B O   
5278 O  O   . HOH F .   ? 0.3324 0.4773 0.5997 -0.0497 0.0751  -0.0120 1001 HOH B O   
5279 O  O   . HOH F .   ? 0.3354 0.3980 0.3898 0.0331  0.0136  -0.0323 1002 HOH B O   
5280 O  O   . HOH F .   ? 0.5143 0.5943 0.5728 0.0069  0.0555  -0.0143 1003 HOH B O   
5281 O  O   . HOH F .   ? 0.3755 0.4229 0.4072 0.0350  0.0176  -0.0337 1004 HOH B O   
5282 O  O   . HOH F .   ? 0.4685 0.5398 0.5381 0.0419  0.0153  -0.0374 1005 HOH B O   
5283 O  O   . HOH F .   ? 0.5935 0.6036 0.6772 -0.0436 -0.0359 -0.0339 1006 HOH B O   
5284 O  O   . HOH F .   ? 0.4880 0.6098 0.7583 -0.0286 -0.0928 -0.0942 1007 HOH B O   
# 
