data_8ZC8
# 
_entry.id   8ZC8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8ZC8         pdb_00008zc8 10.2210/pdb8zc8/pdb 
WWPDB D_1300047421 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZC8 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              fangpengfei@sioc.ac.cn 
_pdbx_contact_author.name_first         pengfei 
_pdbx_contact_author.name_last          fang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3448-5494 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xia, M.'  1 ? 
'Dong, D.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystallographic analysis of MitM, which catalyzes the post-mitosane modification in mitomycin biosynthesis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xia, M.'  1 ? 
primary 'Dong, D.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man MitM 31085.221 2 ? ? ? 
'The sequence of organism Streptomyces caespitosus is not available, replaced by Q9X5Q9 temporarily.' 
2 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE 384.411   2 ? ? ? ? 
3 non-polymer syn 
;[(1aS,8S,8aR,8bS)-6,8a-dimethoxy-5-methyl-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazireno[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
;
349.339   1 ? ? ? ?                                                                                                     
4 water       nat water 18.015    4 ? ? ? ? 
# 
_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       
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGK
;
_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 S-ADENOSYL-L-HOMOCYSTEINE SAH 
3 
;[(1aS,8S,8aR,8bS)-6,8a-dimethoxy-5-methyl-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazireno[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
;
MQA 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   HIS n 
1 4   SER n 
1 5   GLU n 
1 6   LEU n 
1 7   SER n 
1 8   GLU n 
1 9   LEU n 
1 10  PRO n 
1 11  MET n 
1 12  PRO n 
1 13  SER n 
1 14  PRO n 
1 15  ALA n 
1 16  SER n 
1 17  GLU n 
1 18  GLU n 
1 19  VAL n 
1 20  GLY n 
1 21  ALA n 
1 22  LEU n 
1 23  TYR n 
1 24  ASP n 
1 25  ARG n 
1 26  PHE n 
1 27  THR n 
1 28  ALA n 
1 29  LEU n 
1 30  GLY n 
1 31  ALA n 
1 32  ALA n 
1 33  SER n 
1 34  LEU n 
1 35  GLY n 
1 36  GLU n 
1 37  ASN n 
1 38  LEU n 
1 39  HIS n 
1 40  PHE n 
1 41  GLY n 
1 42  TYR n 
1 43  TRP n 
1 44  ASP n 
1 45  SER n 
1 46  PRO n 
1 47  ASP n 
1 48  SER n 
1 49  GLN n 
1 50  VAL n 
1 51  PRO n 
1 52  LEU n 
1 53  ALA n 
1 54  GLU n 
1 55  ALA n 
1 56  THR n 
1 57  ASP n 
1 58  ARG n 
1 59  LEU n 
1 60  THR n 
1 61  ASP n 
1 62  MET n 
1 63  MET n 
1 64  ALA n 
1 65  GLU n 
1 66  ARG n 
1 67  LEU n 
1 68  ARG n 
1 69  ILE n 
1 70  GLY n 
1 71  ALA n 
1 72  GLY n 
1 73  SER n 
1 74  ARG n 
1 75  VAL n 
1 76  LEU n 
1 77  ASP n 
1 78  LEU n 
1 79  GLY n 
1 80  CYS n 
1 81  GLY n 
1 82  VAL n 
1 83  GLY n 
1 84  THR n 
1 85  PRO n 
1 86  GLY n 
1 87  VAL n 
1 88  ARG n 
1 89  ILE n 
1 90  ALA n 
1 91  ARG n 
1 92  LEU n 
1 93  SER n 
1 94  GLY n 
1 95  ALA n 
1 96  HIS n 
1 97  VAL n 
1 98  THR n 
1 99  GLY n 
1 100 ILE n 
1 101 SER n 
1 102 VAL n 
1 103 SER n 
1 104 HIS n 
1 105 GLU n 
1 106 GLN n 
1 107 VAL n 
1 108 VAL n 
1 109 ARG n 
1 110 ALA n 
1 111 ASN n 
1 112 ALA n 
1 113 LEU n 
1 114 ALA n 
1 115 GLU n 
1 116 GLU n 
1 117 ALA n 
1 118 GLY n 
1 119 LEU n 
1 120 ALA n 
1 121 ASP n 
1 122 ARG n 
1 123 ALA n 
1 124 ARG n 
1 125 PHE n 
1 126 GLN n 
1 127 ARG n 
1 128 ALA n 
1 129 ASP n 
1 130 ALA n 
1 131 MET n 
1 132 ASP n 
1 133 LEU n 
1 134 PRO n 
1 135 PHE n 
1 136 GLU n 
1 137 ASP n 
1 138 GLU n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 ALA n 
1 143 VAL n 
1 144 ILE n 
1 145 ALA n 
1 146 LEU n 
1 147 GLU n 
1 148 SER n 
1 149 ILE n 
1 150 ILE n 
1 151 HIS n 
1 152 MET n 
1 153 PRO n 
1 154 ASP n 
1 155 ARG n 
1 156 ALA n 
1 157 GLN n 
1 158 VAL n 
1 159 LEU n 
1 160 ALA n 
1 161 GLN n 
1 162 VAL n 
1 163 GLY n 
1 164 ARG n 
1 165 VAL n 
1 166 LEU n 
1 167 ARG n 
1 168 PRO n 
1 169 GLY n 
1 170 GLY n 
1 171 ARG n 
1 172 LEU n 
1 173 VAL n 
1 174 LEU n 
1 175 THR n 
1 176 ASP n 
1 177 PHE n 
1 178 PHE n 
1 179 GLU n 
1 180 ARG n 
1 181 ALA n 
1 182 PRO n 
1 183 LEU n 
1 184 ALA n 
1 185 PRO n 
1 186 GLU n 
1 187 GLY n 
1 188 ARG n 
1 189 ALA n 
1 190 ALA n 
1 191 VAL n 
1 192 GLN n 
1 193 ARG n 
1 194 TYR n 
1 195 LEU n 
1 196 HIS n 
1 197 ASP n 
1 198 PHE n 
1 199 MET n 
1 200 MET n 
1 201 THR n 
1 202 MET n 
1 203 VAL n 
1 204 SER n 
1 205 ALA n 
1 206 GLU n 
1 207 ALA n 
1 208 TYR n 
1 209 PRO n 
1 210 PRO n 
1 211 LEU n 
1 212 LEU n 
1 213 ARG n 
1 214 GLY n 
1 215 ALA n 
1 216 GLY n 
1 217 LEU n 
1 218 TRP n 
1 219 LEU n 
1 220 GLU n 
1 221 GLU n 
1 222 PHE n 
1 223 LEU n 
1 224 ASP n 
1 225 ILE n 
1 226 SER n 
1 227 ASP n 
1 228 GLN n 
1 229 THR n 
1 230 LEU n 
1 231 GLU n 
1 232 LYS n 
1 233 THR n 
1 234 PHE n 
1 235 ARG n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 GLU n 
1 240 ARG n 
1 241 ILE n 
1 242 ASN n 
1 243 SER n 
1 244 SER n 
1 245 LYS n 
1 246 GLN n 
1 247 ARG n 
1 248 LEU n 
1 249 GLU n 
1 250 THR n 
1 251 GLN n 
1 252 PHE n 
1 253 GLY n 
1 254 GLU n 
1 255 GLU n 
1 256 MET n 
1 257 VAL n 
1 258 ASN n 
1 259 GLN n 
1 260 PHE n 
1 261 ASP n 
1 262 PRO n 
1 263 GLY n 
1 264 ASP n 
1 265 LEU n 
1 266 VAL n 
1 267 GLY n 
1 268 VAL n 
1 269 LYS n 
1 270 GLU n 
1 271 PHE n 
1 272 GLY n 
1 273 TYR n 
1 274 LEU n 
1 275 LEU n 
1 276 LEU n 
1 277 VAL n 
1 278 ALA n 
1 279 GLN n 
1 280 ARG n 
1 281 PRO n 
1 282 GLY n 
1 283 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   283 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mitM 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces caespitosus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     53502 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?             'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE ?             'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE ?             'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?             'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE ?             'C3 H7 N O2 S'    121.158 
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 
MQA non-polymer         . 
;[(1aS,8S,8aR,8bS)-6,8a-dimethoxy-5-methyl-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazireno[2',3':3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
;
'Mitomycin A' 'C16 H19 N3 O6'   349.339 
PHE 'L-peptide linking' y PHENYLALANINE ?             'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ?             'C5 H9 N O2'      115.130 
SAH non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ?             'C14 H20 N6 O5 S' 384.411 
SER 'L-peptide linking' y SERINE ?             'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ?             'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?             'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE ?             'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE ?             'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  MET 63  63  63  MET MET A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  CYS 80  80  80  CYS CYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 PHE 125 125 125 PHE PHE A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 MET 200 200 200 MET MET A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 GLN 251 251 ?   ?   ?   A . n 
A 1 252 PHE 252 252 ?   ?   ?   A . n 
A 1 253 GLY 253 253 ?   ?   ?   A . n 
A 1 254 GLU 254 254 ?   ?   ?   A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 MET 256 256 256 MET MET A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 TYR 273 273 273 TYR TYR A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   ?   ?   ?   B . n 
B 1 4   SER 4   4   ?   ?   ?   B . n 
B 1 5   GLU 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  MET 11  11  11  MET MET B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  TYR 23  23  23  TYR TYR B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  THR 27  27  27  THR THR B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  HIS 39  39  39  HIS HIS B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  TRP 43  43  43  TRP TRP B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  PRO 51  51  51  PRO PRO B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  THR 56  56  56  THR THR B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  MET 62  62  62  MET MET B . n 
B 1 63  MET 63  63  63  MET MET B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  ARG 74  74  74  ARG ARG B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  CYS 80  80  80  CYS CYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 HIS 104 104 104 HIS HIS B . n 
B 1 105 GLU 105 105 105 GLU GLU B . n 
B 1 106 GLN 106 106 106 GLN GLN B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 PHE 125 125 125 PHE PHE B . n 
B 1 126 GLN 126 126 126 GLN GLN B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 PHE 135 135 135 PHE PHE B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 HIS 151 151 151 HIS HIS B . n 
B 1 152 MET 152 152 152 MET MET B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 ARG 171 171 171 ARG ARG B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 PRO 182 182 182 PRO PRO B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 PHE 198 198 198 PHE PHE B . n 
B 1 199 MET 199 199 199 MET MET B . n 
B 1 200 MET 200 200 200 MET MET B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 MET 202 202 202 MET MET B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 PRO 210 210 210 PRO PRO B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 ILE 225 225 225 ILE ILE B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 GLN 228 228 228 GLN GLN B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 GLU 231 231 231 GLU GLU B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 GLN 246 246 246 GLN GLN B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 GLU 249 249 249 GLU GLU B . n 
B 1 250 THR 250 250 250 THR THR B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 GLU 255 255 255 GLU GLU B . n 
B 1 256 MET 256 256 256 MET MET B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 ASN 258 258 258 ASN ASN B . n 
B 1 259 GLN 259 259 259 GLN GLN B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 ASP 264 264 264 ASP ASP B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 TYR 273 273 273 TYR TYR B . n 
B 1 274 LEU 274 274 274 LEU LEU B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 PRO 281 281 281 PRO PRO B . n 
B 1 282 GLY 282 282 282 GLY GLY B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 SAH ? ? SAH ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MQA ? ? MQA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SAH 1 301 301 SAH SAH A . 
D 2 SAH 1 301 301 SAH SAH B . 
E 3 MQA 1 302 302 MQA MQA B . 
F 4 HOH 1 401 4   HOH HOH A . 
F 4 HOH 2 402 1   HOH HOH A . 
G 4 HOH 1 401 5   HOH HOH B . 
G 4 HOH 2 402 3   HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LEU 29  ? CG  ? A LEU 29  CG  
2   1 Y 1 A LEU 29  ? CD1 ? A LEU 29  CD1 
3   1 Y 1 A LEU 29  ? CD2 ? A LEU 29  CD2 
4   1 Y 1 A GLU 186 ? CG  ? A GLU 186 CG  
5   1 Y 1 A GLU 186 ? CD  ? A GLU 186 CD  
6   1 Y 1 A GLU 186 ? OE1 ? A GLU 186 OE1 
7   1 Y 1 A GLU 186 ? OE2 ? A GLU 186 OE2 
8   1 Y 1 A ASN 242 ? CG  ? A ASN 242 CG  
9   1 Y 1 A ASN 242 ? OD1 ? A ASN 242 OD1 
10  1 Y 1 A ASN 242 ? ND2 ? A ASN 242 ND2 
11  1 Y 1 A LYS 245 ? CG  ? A LYS 245 CG  
12  1 Y 1 A LYS 245 ? CD  ? A LYS 245 CD  
13  1 Y 1 A LYS 245 ? CE  ? A LYS 245 CE  
14  1 Y 1 A LYS 245 ? NZ  ? A LYS 245 NZ  
15  1 Y 1 A LYS 269 ? CG  ? A LYS 269 CG  
16  1 Y 1 A LYS 269 ? CD  ? A LYS 269 CD  
17  1 Y 1 A LYS 269 ? CE  ? A LYS 269 CE  
18  1 Y 1 A LYS 269 ? NZ  ? A LYS 269 NZ  
19  1 Y 1 B ARG 25  ? CG  ? B ARG 25  CG  
20  1 Y 1 B ARG 25  ? CD  ? B ARG 25  CD  
21  1 Y 1 B ARG 25  ? NE  ? B ARG 25  NE  
22  1 Y 1 B ARG 25  ? CZ  ? B ARG 25  CZ  
23  1 Y 1 B ARG 25  ? NH1 ? B ARG 25  NH1 
24  1 Y 1 B ARG 25  ? NH2 ? B ARG 25  NH2 
25  1 Y 1 B LEU 29  ? CG  ? B LEU 29  CG  
26  1 Y 1 B LEU 29  ? CD1 ? B LEU 29  CD1 
27  1 Y 1 B LEU 29  ? CD2 ? B LEU 29  CD2 
28  1 Y 1 B GLN 49  ? CG  ? B GLN 49  CG  
29  1 Y 1 B GLN 49  ? CD  ? B GLN 49  CD  
30  1 Y 1 B GLN 49  ? OE1 ? B GLN 49  OE1 
31  1 Y 1 B GLN 49  ? NE2 ? B GLN 49  NE2 
32  1 Y 1 B GLU 186 ? CG  ? B GLU 186 CG  
33  1 Y 1 B GLU 186 ? CD  ? B GLU 186 CD  
34  1 Y 1 B GLU 186 ? OE1 ? B GLU 186 OE1 
35  1 Y 1 B GLU 186 ? OE2 ? B GLU 186 OE2 
36  1 Y 1 B GLN 192 ? CG  ? B GLN 192 CG  
37  1 Y 1 B GLN 192 ? CD  ? B GLN 192 CD  
38  1 Y 1 B GLN 192 ? OE1 ? B GLN 192 OE1 
39  1 Y 1 B GLN 192 ? NE2 ? B GLN 192 NE2 
40  1 Y 1 B ARG 193 ? CG  ? B ARG 193 CG  
41  1 Y 1 B ARG 193 ? CD  ? B ARG 193 CD  
42  1 Y 1 B ARG 193 ? NE  ? B ARG 193 NE  
43  1 Y 1 B ARG 193 ? CZ  ? B ARG 193 CZ  
44  1 Y 1 B ARG 193 ? NH1 ? B ARG 193 NH1 
45  1 Y 1 B ARG 193 ? NH2 ? B ARG 193 NH2 
46  1 Y 1 B ARG 235 ? CG  ? B ARG 235 CG  
47  1 Y 1 B ARG 235 ? CD  ? B ARG 235 CD  
48  1 Y 1 B ARG 235 ? NE  ? B ARG 235 NE  
49  1 Y 1 B ARG 235 ? CZ  ? B ARG 235 CZ  
50  1 Y 1 B ARG 235 ? NH1 ? B ARG 235 NH1 
51  1 Y 1 B ARG 235 ? NH2 ? B ARG 235 NH2 
52  1 Y 1 B GLU 239 ? CG  ? B GLU 239 CG  
53  1 Y 1 B GLU 239 ? CD  ? B GLU 239 CD  
54  1 Y 1 B GLU 239 ? OE1 ? B GLU 239 OE1 
55  1 Y 1 B GLU 239 ? OE2 ? B GLU 239 OE2 
56  1 Y 1 B ARG 240 ? CG  ? B ARG 240 CG  
57  1 Y 1 B ARG 240 ? CD  ? B ARG 240 CD  
58  1 Y 1 B ARG 240 ? NE  ? B ARG 240 NE  
59  1 Y 1 B ARG 240 ? CZ  ? B ARG 240 CZ  
60  1 Y 1 B ARG 240 ? NH1 ? B ARG 240 NH1 
61  1 Y 1 B ARG 240 ? NH2 ? B ARG 240 NH2 
62  1 Y 1 B ILE 241 ? CG1 ? B ILE 241 CG1 
63  1 Y 1 B ILE 241 ? CG2 ? B ILE 241 CG2 
64  1 Y 1 B ILE 241 ? CD1 ? B ILE 241 CD1 
65  1 Y 1 B LYS 245 ? CG  ? B LYS 245 CG  
66  1 Y 1 B LYS 245 ? CD  ? B LYS 245 CD  
67  1 Y 1 B LYS 245 ? CE  ? B LYS 245 CE  
68  1 Y 1 B LYS 245 ? NZ  ? B LYS 245 NZ  
69  1 Y 1 B GLN 246 ? CG  ? B GLN 246 CG  
70  1 Y 1 B GLN 246 ? CD  ? B GLN 246 CD  
71  1 Y 1 B GLN 246 ? OE1 ? B GLN 246 OE1 
72  1 Y 1 B GLN 246 ? NE2 ? B GLN 246 NE2 
73  1 Y 1 B ARG 247 ? CG  ? B ARG 247 CG  
74  1 Y 1 B ARG 247 ? CD  ? B ARG 247 CD  
75  1 Y 1 B ARG 247 ? NE  ? B ARG 247 NE  
76  1 Y 1 B ARG 247 ? CZ  ? B ARG 247 CZ  
77  1 Y 1 B ARG 247 ? NH1 ? B ARG 247 NH1 
78  1 Y 1 B ARG 247 ? NH2 ? B ARG 247 NH2 
79  1 Y 1 B LEU 248 ? CG  ? B LEU 248 CG  
80  1 Y 1 B LEU 248 ? CD1 ? B LEU 248 CD1 
81  1 Y 1 B LEU 248 ? CD2 ? B LEU 248 CD2 
82  1 Y 1 B GLU 249 ? CG  ? B GLU 249 CG  
83  1 Y 1 B GLU 249 ? CD  ? B GLU 249 CD  
84  1 Y 1 B GLU 249 ? OE1 ? B GLU 249 OE1 
85  1 Y 1 B GLU 249 ? OE2 ? B GLU 249 OE2 
86  1 Y 1 B THR 250 ? OG1 ? B THR 250 OG1 
87  1 Y 1 B THR 250 ? CG2 ? B THR 250 CG2 
88  1 Y 1 B PHE 252 ? CG  ? B PHE 252 CG  
89  1 Y 1 B PHE 252 ? CD1 ? B PHE 252 CD1 
90  1 Y 1 B PHE 252 ? CD2 ? B PHE 252 CD2 
91  1 Y 1 B PHE 252 ? CE1 ? B PHE 252 CE1 
92  1 Y 1 B PHE 252 ? CE2 ? B PHE 252 CE2 
93  1 Y 1 B PHE 252 ? CZ  ? B PHE 252 CZ  
94  1 Y 1 B GLU 254 ? CG  ? B GLU 254 CG  
95  1 Y 1 B GLU 254 ? CD  ? B GLU 254 CD  
96  1 Y 1 B GLU 254 ? OE1 ? B GLU 254 OE1 
97  1 Y 1 B GLU 254 ? OE2 ? B GLU 254 OE2 
98  1 Y 1 B GLU 255 ? CG  ? B GLU 255 CG  
99  1 Y 1 B GLU 255 ? CD  ? B GLU 255 CD  
100 1 Y 1 B GLU 255 ? OE1 ? B GLU 255 OE1 
101 1 Y 1 B GLU 255 ? OE2 ? B GLU 255 OE2 
102 1 Y 1 B MET 256 ? CG  ? B MET 256 CG  
103 1 Y 1 B MET 256 ? SD  ? B MET 256 SD  
104 1 Y 1 B MET 256 ? CE  ? B MET 256 CE  
105 1 Y 1 B GLN 259 ? CG  ? B GLN 259 CG  
106 1 Y 1 B GLN 259 ? CD  ? B GLN 259 CD  
107 1 Y 1 B GLN 259 ? OE1 ? B GLN 259 OE1 
108 1 Y 1 B GLN 259 ? NE2 ? B GLN 259 NE2 
109 1 Y 1 B PHE 260 ? CG  ? B PHE 260 CG  
110 1 Y 1 B PHE 260 ? CD1 ? B PHE 260 CD1 
111 1 Y 1 B PHE 260 ? CD2 ? B PHE 260 CD2 
112 1 Y 1 B PHE 260 ? CE1 ? B PHE 260 CE1 
113 1 Y 1 B PHE 260 ? CE2 ? B PHE 260 CE2 
114 1 Y 1 B PHE 260 ? CZ  ? B PHE 260 CZ  
115 1 Y 1 B LYS 269 ? CG  ? B LYS 269 CG  
116 1 Y 1 B LYS 269 ? CD  ? B LYS 269 CD  
117 1 Y 1 B LYS 269 ? CE  ? B LYS 269 CE  
118 1 Y 1 B LYS 269 ? NZ  ? B LYS 269 NZ  
119 1 Y 1 B GLU 270 ? CG  ? B GLU 270 CG  
120 1 Y 1 B GLU 270 ? CD  ? B GLU 270 CD  
121 1 Y 1 B GLU 270 ? OE1 ? B GLU 270 OE1 
122 1 Y 1 B GLU 270 ? OE2 ? B GLU 270 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.21.1_5286: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .                    2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .                    3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 11.29                4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .                    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZC8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.953 
_cell.length_a_esd                 ? 
_cell.length_b                     113.953 
_cell.length_b_esd                 ? 
_cell.length_c                     108.771 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8ZC8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZC8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% w/v PEG 3350, 10% w/v Ethylene glycol, 0.2 M Sodium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     110 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-29 
_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   0.97861 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL17U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97861 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZC8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.80 
_reflns.d_resolution_low                               49.34 
_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                                     20544 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.80 
_reflns_shell.d_res_low                                     2.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2957 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.653 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZC8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.80 
_refine.ls_d_res_low                             49.34 
_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                     20514 
_refine.ls_number_reflns_R_free                  2001 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 9.75 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2258 
_refine.ls_R_factor_R_free                       0.2441 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2239 
_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                      8ZC7 
_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                 28.46 
_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                            0.48 
_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                       2.80 
_refine_hist.d_res_low                        49.34 
_refine_hist.number_atoms_solvent             4 
_refine_hist.number_atoms_total               4212 
_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        4131 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_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' ? 0.013  ? 4294 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.472  ? 5844 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.845 ? 1538 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065  ? 659  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.026  ? 775  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.80 2.87  . . 143 1316 100.00 . . . . 0.4132 . . . . . . . . . . . 0.4059 
'X-RAY DIFFRACTION' 2.87 2.95  . . 139 1291 100.00 . . . . 0.3652 . . . . . . . . . . . 0.4099 
'X-RAY DIFFRACTION' 2.95 3.03  . . 139 1308 100.00 . . . . 0.3359 . . . . . . . . . . . 0.3841 
'X-RAY DIFFRACTION' 3.03 3.13  . . 141 1299 100.00 . . . . 0.3404 . . . . . . . . . . . 0.3387 
'X-RAY DIFFRACTION' 3.13 3.24  . . 144 1294 100.00 . . . . 0.3285 . . . . . . . . . . . 0.3156 
'X-RAY DIFFRACTION' 3.24 3.37  . . 143 1325 100.00 . . . . 0.3199 . . . . . . . . . . . 0.3625 
'X-RAY DIFFRACTION' 3.37 3.53  . . 139 1306 100.00 . . . . 0.2951 . . . . . . . . . . . 0.3063 
'X-RAY DIFFRACTION' 3.53 3.71  . . 141 1317 100.00 . . . . 0.2537 . . . . . . . . . . . 0.3137 
'X-RAY DIFFRACTION' 3.71 3.95  . . 144 1321 100.00 . . . . 0.2366 . . . . . . . . . . . 0.2679 
'X-RAY DIFFRACTION' 3.95 4.25  . . 142 1309 100.00 . . . . 0.2101 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 4.25 4.68  . . 146 1318 100.00 . . . . 0.1692 . . . . . . . . . . . 0.2117 
'X-RAY DIFFRACTION' 4.68 5.35  . . 146 1339 100.00 . . . . 0.1753 . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 5.35 6.74  . . 145 1350 100.00 . . . . 0.2032 . . . . . . . . . . . 0.1786 
'X-RAY DIFFRACTION' 6.74 49.34 . . 149 1420 100.00 . . . . 0.1626 . . . . . . . . . . . 0.1831 
# 
_struct.entry_id                     8ZC8 
_struct.title                        'The structure of MitM and mitomycin A with SAH in mitomycin' 
_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        8ZC8 
_struct_keywords.text            'SAM-dependent methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9X5Q9_STRLA 
_struct_ref.pdbx_db_accession          Q9X5Q9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZC8 A 1 ? 283 ? Q9X5Q9 1 ? 283 ? 1 283 
2 1 8ZC8 B 1 ? 283 ? Q9X5Q9 1 ? 283 ? 1 283 
# 
_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)' 1550  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  22390 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 15  ? LEU A 29  ? ALA A 15  LEU A 29  1 ? 15 
HELX_P HELX_P2  AA2 PRO A 51  ? ARG A 68  ? PRO A 51  ARG A 68  1 ? 18 
HELX_P HELX_P3  AA3 GLY A 83  ? GLY A 94  ? GLY A 83  GLY A 94  1 ? 12 
HELX_P HELX_P4  AA4 SER A 103 ? ALA A 117 ? SER A 103 ALA A 117 1 ? 15 
HELX_P HELX_P5  AA5 SER A 148 ? MET A 152 ? SER A 148 MET A 152 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 154 ? VAL A 165 ? ASP A 154 VAL A 165 1 ? 12 
HELX_P HELX_P7  AA7 ALA A 184 ? PHE A 198 ? ALA A 184 PHE A 198 1 ? 15 
HELX_P HELX_P8  AA8 ALA A 207 ? GLY A 214 ? ALA A 207 GLY A 214 1 ? 8  
HELX_P HELX_P9  AA9 ILE A 225 ? LEU A 248 ? ILE A 225 LEU A 248 1 ? 24 
HELX_P HELX_P10 AB1 ASP A 261 ? VAL A 266 ? ASP A 261 VAL A 266 5 ? 6  
HELX_P HELX_P11 AB2 ALA B 15  ? THR B 27  ? ALA B 15  THR B 27  1 ? 13 
HELX_P HELX_P12 AB3 PRO B 51  ? ARG B 68  ? PRO B 51  ARG B 68  1 ? 18 
HELX_P HELX_P13 AB4 GLY B 83  ? GLY B 94  ? GLY B 83  GLY B 94  1 ? 12 
HELX_P HELX_P14 AB5 SER B 103 ? ALA B 117 ? SER B 103 ALA B 117 1 ? 15 
HELX_P HELX_P15 AB6 SER B 148 ? MET B 152 ? SER B 148 MET B 152 5 ? 5  
HELX_P HELX_P16 AB7 ASP B 154 ? VAL B 165 ? ASP B 154 VAL B 165 1 ? 12 
HELX_P HELX_P17 AB8 ALA B 184 ? GLU B 186 ? ALA B 184 GLU B 186 5 ? 3  
HELX_P HELX_P18 AB9 GLY B 187 ? PHE B 198 ? GLY B 187 PHE B 198 1 ? 12 
HELX_P HELX_P19 AC1 ALA B 207 ? GLY B 216 ? ALA B 207 GLY B 216 1 ? 10 
HELX_P HELX_P20 AC2 ILE B 225 ? SER B 243 ? ILE B 225 SER B 243 1 ? 19 
HELX_P HELX_P21 AC3 SER B 244 ? GLN B 246 ? SER B 244 GLN B 246 5 ? 3  
HELX_P HELX_P22 AC4 ARG B 247 ? PHE B 252 ? ARG B 247 PHE B 252 1 ? 6  
HELX_P HELX_P23 AC5 PHE B 252 ? ASP B 261 ? PHE B 252 ASP B 261 1 ? 10 
HELX_P HELX_P24 AC6 PRO B 262 ? VAL B 266 ? PRO B 262 VAL B 266 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   14 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? parallel      
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? 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  ALA A 123 ? ARG A 127 ? ALA A 123 ARG A 127 
AA1 2  HIS A 96  ? SER A 101 ? HIS A 96  SER A 101 
AA1 3  ARG A 74  ? LEU A 78  ? ARG A 74  LEU A 78  
AA1 4  PHE A 140 ? ALA A 145 ? PHE A 140 ALA A 145 
AA1 5  LEU A 166 ? GLU A 179 ? LEU A 166 GLU A 179 
AA1 6  PHE A 271 ? GLN A 279 ? PHE A 271 GLN A 279 
AA1 7  TRP A 218 ? ASP A 224 ? TRP A 218 ASP A 224 
AA1 8  TRP B 218 ? ASP B 224 ? TRP B 218 ASP B 224 
AA1 9  PHE B 271 ? GLN B 279 ? PHE B 271 GLN B 279 
AA1 10 LEU B 166 ? GLU B 179 ? LEU B 166 GLU B 179 
AA1 11 PHE B 140 ? ALA B 145 ? PHE B 140 ALA B 145 
AA1 12 ARG B 74  ? LEU B 78  ? ARG B 74  LEU B 78  
AA1 13 HIS B 96  ? SER B 101 ? HIS B 96  SER B 101 
AA1 14 ALA B 123 ? ARG B 127 ? ALA B 123 ARG B 127 
# 
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 ARG A 124 ? O ARG A 124 N VAL A 97  ? N VAL A 97  
AA1 2  3  O THR A 98  ? O THR A 98  N VAL A 75  ? N VAL A 75  
AA1 3  4  N LEU A 76  ? N LEU A 76  O ALA A 142 ? O ALA A 142 
AA1 4  5  N ALA A 145 ? N ALA A 145 O VAL A 173 ? O VAL A 173 
AA1 5  6  N ASP A 176 ? N ASP A 176 O LEU A 274 ? O LEU A 274 
AA1 6  7  O GLN A 279 ? O GLN A 279 N TRP A 218 ? N TRP A 218 
AA1 7  8  N PHE A 222 ? N PHE A 222 O PHE B 222 ? O PHE B 222 
AA1 8  9  N LEU B 223 ? N LEU B 223 O LEU B 275 ? O LEU B 275 
AA1 9  10 O GLY B 272 ? O GLY B 272 N PHE B 178 ? N PHE B 178 
AA1 10 11 O VAL B 173 ? O VAL B 173 N ALA B 145 ? N ALA B 145 
AA1 11 12 O ALA B 142 ? O ALA B 142 N LEU B 76  ? N LEU B 76  
AA1 12 13 N VAL B 75  ? N VAL B 75  O HIS B 96  ? O HIS B 96  
AA1 13 14 N GLY B 99  ? N GLY B 99  O GLN B 126 ? O GLN B 126 
# 
_pdbx_entry_details.entry_id                   8ZC8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD2 A ASP 176 ? ? OH  A TYR 208 ? ? 1.99 
2 1 CA  B SER 7   ? ? O   B HOH 401 ? ? 2.08 
3 1 N   A LEU 6   ? ? OE2 A GLU 8   ? ? 2.14 
4 1 O   B ILE 225 ? ? OG1 B THR 229 ? ? 2.17 
5 1 OG  A SER 16  ? ? OD2 A ASP 129 ? ? 2.17 
6 1 OH  B TYR 23  ? ? NE2 B HIS 151 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     121 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OD2 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    ASP 
_pdbx_validate_symm_contact.auth_seq_id_2     121 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   5_554 
_pdbx_validate_symm_contact.dist              2.08 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C B PRO 182 ? ? N B LEU 183 ? ? 1.517 1.336 0.181 0.023 Y 
2 1 C B LEU 183 ? ? N B ALA 184 ? ? 1.529 1.336 0.193 0.023 Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             O 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              182 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              182 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             N 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              183 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.57 
_pdbx_validate_rmsd_angle.angle_target_value         122.70 
_pdbx_validate_rmsd_angle.angle_deviation            9.87 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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 LEU A 29  ? ? -69.72  0.59   
2  1 LEU A 38  ? ? -100.40 68.96  
3  1 VAL A 257 ? ? -140.91 24.93  
4  1 PHE A 260 ? ? 54.96   71.29  
5  1 SER B 7   ? ? 74.22   34.99  
6  1 THR B 27  ? ? -94.48  45.49  
7  1 SER B 33  ? ? -103.10 -60.23 
8  1 GLU B 136 ? ? -49.07  152.60 
9  1 PRO B 182 ? ? -36.91  133.60 
10 1 GLU B 221 ? ? -161.29 115.00 
11 1 THR B 229 ? ? -122.53 -52.40 
12 1 SER B 244 ? ? -140.40 39.06  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 74  ? ? 0.224 'SIDE CHAIN' 
2 1 ARG A 240 ? ? 0.166 'SIDE CHAIN' 
3 1 ARG A 247 ? ? 0.276 'SIDE CHAIN' 
4 1 ARG B 213 ? ? 0.097 'SIDE CHAIN' 
# 
_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         52.3638 
_pdbx_refine_tls.origin_y         -6.2356 
_pdbx_refine_tls.origin_z         9.3857 
_pdbx_refine_tls.T[1][1]          0.7930 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0631 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0864 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4723 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.1322 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6156 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.5938 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.7232 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.6619 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.8137 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.7608 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.9410 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.2408 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1899 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.2327 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3640 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0434 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1542 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.2833 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1582 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.1717 
_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_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A HIS 3   ? A HIS 3   
4  1 Y 1 A SER 4   ? A SER 4   
5  1 Y 1 A GLU 5   ? A GLU 5   
6  1 Y 1 A GLN 251 ? A GLN 251 
7  1 Y 1 A PHE 252 ? A PHE 252 
8  1 Y 1 A GLY 253 ? A GLY 253 
9  1 Y 1 A GLU 254 ? A GLU 254 
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B PRO 2   ? B PRO 2   
12 1 Y 1 B HIS 3   ? B HIS 3   
13 1 Y 1 B SER 4   ? B SER 4   
14 1 Y 1 B GLU 5   ? B GLU 5   
# 
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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LYS N      N N N 205 
LYS CA     C N S 206 
LYS C      C N N 207 
LYS O      O N N 208 
LYS CB     C N N 209 
LYS CG     C N N 210 
LYS CD     C N N 211 
LYS CE     C N N 212 
LYS NZ     N N N 213 
LYS OXT    O N N 214 
LYS H      H N N 215 
LYS H2     H N N 216 
LYS HA     H N N 217 
LYS HB2    H N N 218 
LYS HB3    H N N 219 
LYS HG2    H N N 220 
LYS HG3    H N N 221 
LYS HD2    H N N 222 
LYS HD3    H N N 223 
LYS HE2    H N N 224 
LYS HE3    H N N 225 
LYS HZ1    H N N 226 
LYS HZ2    H N N 227 
LYS HZ3    H N N 228 
LYS HXT    H N N 229 
MET N      N N N 230 
MET CA     C N S 231 
MET C      C N N 232 
MET O      O N N 233 
MET CB     C N N 234 
MET CG     C N N 235 
MET SD     S N N 236 
MET CE     C N N 237 
MET OXT    O N N 238 
MET H      H N N 239 
MET H2     H N N 240 
MET HA     H N N 241 
MET HB2    H N N 242 
MET HB3    H N N 243 
MET HG2    H N N 244 
MET HG3    H N N 245 
MET HE1    H N N 246 
MET HE2    H N N 247 
MET HE3    H N N 248 
MET HXT    H N N 249 
MQA C1     C N S 250 
MQA C2     C N S 251 
MQA C3     C N N 252 
MQA C5     C N N 253 
MQA C6     C N N 254 
MQA C7     C N N 255 
MQA C8     C N N 256 
MQA C9     C N S 257 
MQA C10    C N N 258 
MQA C11    C N N 259 
MQA O5     O N N 260 
MQA CM6    C N N 261 
MQA O7     O N N 262 
MQA C24    C N N 263 
MQA O8     O N N 264 
MQA C4A    C N N 265 
MQA C8A    C N N 266 
MQA N4     N N N 267 
MQA C9A    C N R 268 
MQA O24    O N N 269 
MQA C25    C N N 270 
MQA N2     N N N 271 
MQA O10    O N N 272 
MQA O11    O N N 273 
MQA N12    N N N 274 
MQA H1     H N N 275 
MQA H2     H N N 276 
MQA H3     H N N 277 
MQA H3A    H N N 278 
MQA H9     H N N 279 
MQA H10    H N N 280 
MQA H10A   H N N 281 
MQA HM6    H N N 282 
MQA HM6A   H N N 283 
MQA HM6B   H N N 284 
MQA H24    H N N 285 
MQA H24A   H N N 286 
MQA H24B   H N N 287 
MQA H25    H N N 288 
MQA H25A   H N N 289 
MQA H25B   H N N 290 
MQA HN2    H N N 291 
MQA HN12   H N N 292 
MQA HN1A   H N N 293 
PHE N      N N N 294 
PHE CA     C N S 295 
PHE C      C N N 296 
PHE O      O N N 297 
PHE CB     C N N 298 
PHE CG     C Y N 299 
PHE CD1    C Y N 300 
PHE CD2    C Y N 301 
PHE CE1    C Y N 302 
PHE CE2    C Y N 303 
PHE CZ     C Y N 304 
PHE OXT    O N N 305 
PHE H      H N N 306 
PHE H2     H N N 307 
PHE HA     H N N 308 
PHE HB2    H N N 309 
PHE HB3    H N N 310 
PHE HD1    H N N 311 
PHE HD2    H N N 312 
PHE HE1    H N N 313 
PHE HE2    H N N 314 
PHE HZ     H N N 315 
PHE HXT    H N N 316 
PRO N      N N N 317 
PRO CA     C N S 318 
PRO C      C N N 319 
PRO O      O N N 320 
PRO CB     C N N 321 
PRO CG     C N N 322 
PRO CD     C N N 323 
PRO OXT    O N N 324 
PRO H      H N N 325 
PRO HA     H N N 326 
PRO HB2    H N N 327 
PRO HB3    H N N 328 
PRO HG2    H N N 329 
PRO HG3    H N N 330 
PRO HD2    H N N 331 
PRO HD3    H N N 332 
PRO HXT    H N N 333 
SAH N      N N N 334 
SAH CA     C N S 335 
SAH CB     C N N 336 
SAH CG     C N N 337 
SAH SD     S N N 338 
SAH C      C N N 339 
SAH O      O N N 340 
SAH OXT    O N N 341 
SAH "C5'"  C N N 342 
SAH "C4'"  C N S 343 
SAH "O4'"  O N N 344 
SAH "C3'"  C N S 345 
SAH "O3'"  O N N 346 
SAH "C2'"  C N R 347 
SAH "O2'"  O N N 348 
SAH "C1'"  C N R 349 
SAH N9     N Y N 350 
SAH C8     C Y N 351 
SAH N7     N Y N 352 
SAH C5     C Y N 353 
SAH C6     C Y N 354 
SAH N6     N N N 355 
SAH N1     N Y N 356 
SAH C2     C Y N 357 
SAH N3     N Y N 358 
SAH C4     C Y N 359 
SAH HN1    H N N 360 
SAH HN2    H N N 361 
SAH HA     H N N 362 
SAH HB1    H N N 363 
SAH HB2    H N N 364 
SAH HG1    H N N 365 
SAH HG2    H N N 366 
SAH HXT    H N N 367 
SAH "H5'1" H N N 368 
SAH "H5'2" H N N 369 
SAH "H4'"  H N N 370 
SAH "H3'"  H N N 371 
SAH "HO3'" H N N 372 
SAH "H2'"  H N N 373 
SAH "HO2'" H N N 374 
SAH "H1'"  H N N 375 
SAH H8     H N N 376 
SAH HN61   H N N 377 
SAH HN62   H N N 378 
SAH H2     H N N 379 
SER N      N N N 380 
SER CA     C N S 381 
SER C      C N N 382 
SER O      O N N 383 
SER CB     C N N 384 
SER OG     O N N 385 
SER OXT    O N N 386 
SER H      H N N 387 
SER H2     H N N 388 
SER HA     H N N 389 
SER HB2    H N N 390 
SER HB3    H N N 391 
SER HG     H N N 392 
SER HXT    H N N 393 
THR N      N N N 394 
THR CA     C N S 395 
THR C      C N N 396 
THR O      O N N 397 
THR CB     C N R 398 
THR OG1    O N N 399 
THR CG2    C N N 400 
THR OXT    O N N 401 
THR H      H N N 402 
THR H2     H N N 403 
THR HA     H N N 404 
THR HB     H N N 405 
THR HG1    H N N 406 
THR HG21   H N N 407 
THR HG22   H N N 408 
THR HG23   H N N 409 
THR HXT    H N N 410 
TRP N      N N N 411 
TRP CA     C N S 412 
TRP C      C N N 413 
TRP O      O N N 414 
TRP CB     C N N 415 
TRP CG     C Y N 416 
TRP CD1    C Y N 417 
TRP CD2    C Y N 418 
TRP NE1    N Y N 419 
TRP CE2    C Y N 420 
TRP CE3    C Y N 421 
TRP CZ2    C Y N 422 
TRP CZ3    C Y N 423 
TRP CH2    C Y N 424 
TRP OXT    O N N 425 
TRP H      H N N 426 
TRP H2     H N N 427 
TRP HA     H N N 428 
TRP HB2    H N N 429 
TRP HB3    H N N 430 
TRP HD1    H N N 431 
TRP HE1    H N N 432 
TRP HE3    H N N 433 
TRP HZ2    H N N 434 
TRP HZ3    H N N 435 
TRP HH2    H N N 436 
TRP HXT    H N N 437 
TYR N      N N N 438 
TYR CA     C N S 439 
TYR C      C N N 440 
TYR O      O N N 441 
TYR CB     C N N 442 
TYR CG     C Y N 443 
TYR CD1    C Y N 444 
TYR CD2    C Y N 445 
TYR CE1    C Y N 446 
TYR CE2    C Y N 447 
TYR CZ     C Y N 448 
TYR OH     O N N 449 
TYR OXT    O N N 450 
TYR H      H N N 451 
TYR H2     H N N 452 
TYR HA     H N N 453 
TYR HB2    H N N 454 
TYR HB3    H N N 455 
TYR HD1    H N N 456 
TYR HD2    H N N 457 
TYR HE1    H N N 458 
TYR HE2    H N N 459 
TYR HH     H N N 460 
TYR HXT    H N N 461 
VAL N      N N N 462 
VAL CA     C N S 463 
VAL C      C N N 464 
VAL O      O N N 465 
VAL CB     C N N 466 
VAL CG1    C N N 467 
VAL CG2    C N N 468 
VAL OXT    O N N 469 
VAL H      H N N 470 
VAL H2     H N N 471 
VAL HA     H N N 472 
VAL HB     H N N 473 
VAL HG11   H N N 474 
VAL HG12   H N N 475 
VAL HG13   H N N 476 
VAL HG21   H N N 477 
VAL HG22   H N N 478 
VAL HG23   H N N 479 
VAL HXT    H N N 480 
# 
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 
MQA C9A   C1     sing N N 237 
MQA C1    N2     sing N N 238 
MQA C1    C2     sing N N 239 
MQA C1    H1     sing N N 240 
MQA C3    C2     sing N N 241 
MQA N2    C2     sing N N 242 
MQA C2    H2     sing N N 243 
MQA N4    C3     sing N N 244 
MQA C3    H3     sing N N 245 
MQA C3    H3A    sing N N 246 
MQA C6    C5     sing N N 247 
MQA C4A   C5     sing N N 248 
MQA C5    O5     doub N N 249 
MQA C7    C6     doub N N 250 
MQA C6    CM6    sing N N 251 
MQA O7    C7     sing N N 252 
MQA C8    C7     sing N N 253 
MQA O8    C8     doub N N 254 
MQA C8    C8A    sing N N 255 
MQA C8A   C9     sing N N 256 
MQA C9    C10    sing N N 257 
MQA C9    C9A    sing N N 258 
MQA C9    H9     sing N N 259 
MQA O10   C10    sing N N 260 
MQA C10   H10    sing N N 261 
MQA C10   H10A   sing N N 262 
MQA O11   C11    doub N N 263 
MQA C11   O10    sing N N 264 
MQA C11   N12    sing N N 265 
MQA CM6   HM6    sing N N 266 
MQA CM6   HM6A   sing N N 267 
MQA CM6   HM6B   sing N N 268 
MQA O7    C24    sing N N 269 
MQA C24   H24    sing N N 270 
MQA C24   H24A   sing N N 271 
MQA C24   H24B   sing N N 272 
MQA C8A   C4A    doub N N 273 
MQA C4A   N4     sing N N 274 
MQA C9A   N4     sing N N 275 
MQA O24   C9A    sing N N 276 
MQA C25   O24    sing N N 277 
MQA C25   H25    sing N N 278 
MQA C25   H25A   sing N N 279 
MQA C25   H25B   sing N N 280 
MQA N2    HN2    sing N N 281 
MQA N12   HN12   sing N N 282 
MQA N12   HN1A   sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SAH N     CA     sing N N 324 
SAH N     HN1    sing N N 325 
SAH N     HN2    sing N N 326 
SAH CA    CB     sing N N 327 
SAH CA    C      sing N N 328 
SAH CA    HA     sing N N 329 
SAH CB    CG     sing N N 330 
SAH CB    HB1    sing N N 331 
SAH CB    HB2    sing N N 332 
SAH CG    SD     sing N N 333 
SAH CG    HG1    sing N N 334 
SAH CG    HG2    sing N N 335 
SAH SD    "C5'"  sing N N 336 
SAH C     O      doub N N 337 
SAH C     OXT    sing N N 338 
SAH OXT   HXT    sing N N 339 
SAH "C5'" "C4'"  sing N N 340 
SAH "C5'" "H5'1" sing N N 341 
SAH "C5'" "H5'2" sing N N 342 
SAH "C4'" "O4'"  sing N N 343 
SAH "C4'" "C3'"  sing N N 344 
SAH "C4'" "H4'"  sing N N 345 
SAH "O4'" "C1'"  sing N N 346 
SAH "C3'" "O3'"  sing N N 347 
SAH "C3'" "C2'"  sing N N 348 
SAH "C3'" "H3'"  sing N N 349 
SAH "O3'" "HO3'" sing N N 350 
SAH "C2'" "O2'"  sing N N 351 
SAH "C2'" "C1'"  sing N N 352 
SAH "C2'" "H2'"  sing N N 353 
SAH "O2'" "HO2'" sing N N 354 
SAH "C1'" N9     sing N N 355 
SAH "C1'" "H1'"  sing N N 356 
SAH N9    C8     sing Y N 357 
SAH N9    C4     sing Y N 358 
SAH C8    N7     doub Y N 359 
SAH C8    H8     sing N N 360 
SAH N7    C5     sing Y N 361 
SAH C5    C6     sing Y N 362 
SAH C5    C4     doub Y N 363 
SAH C6    N6     sing N N 364 
SAH C6    N1     doub Y N 365 
SAH N6    HN61   sing N N 366 
SAH N6    HN62   sing N N 367 
SAH N1    C2     sing Y N 368 
SAH C2    N3     doub Y N 369 
SAH C2    H2     sing N N 370 
SAH N3    C4     sing Y N 371 
SER N     CA     sing N N 372 
SER N     H      sing N N 373 
SER N     H2     sing N N 374 
SER CA    C      sing N N 375 
SER CA    CB     sing N N 376 
SER CA    HA     sing N N 377 
SER C     O      doub N N 378 
SER C     OXT    sing N N 379 
SER CB    OG     sing N N 380 
SER CB    HB2    sing N N 381 
SER CB    HB3    sing N N 382 
SER OG    HG     sing N N 383 
SER OXT   HXT    sing N N 384 
THR N     CA     sing N N 385 
THR N     H      sing N N 386 
THR N     H2     sing N N 387 
THR CA    C      sing N N 388 
THR CA    CB     sing N N 389 
THR CA    HA     sing N N 390 
THR C     O      doub N N 391 
THR C     OXT    sing N N 392 
THR CB    OG1    sing N N 393 
THR CB    CG2    sing N N 394 
THR CB    HB     sing N N 395 
THR OG1   HG1    sing N N 396 
THR CG2   HG21   sing N N 397 
THR CG2   HG22   sing N N 398 
THR CG2   HG23   sing N N 399 
THR OXT   HXT    sing N N 400 
TRP N     CA     sing N N 401 
TRP N     H      sing N N 402 
TRP N     H2     sing N N 403 
TRP CA    C      sing N N 404 
TRP CA    CB     sing N N 405 
TRP CA    HA     sing N N 406 
TRP C     O      doub N N 407 
TRP C     OXT    sing N N 408 
TRP CB    CG     sing N N 409 
TRP CB    HB2    sing N N 410 
TRP CB    HB3    sing N N 411 
TRP CG    CD1    doub Y N 412 
TRP CG    CD2    sing Y N 413 
TRP CD1   NE1    sing Y N 414 
TRP CD1   HD1    sing N N 415 
TRP CD2   CE2    doub Y N 416 
TRP CD2   CE3    sing Y N 417 
TRP NE1   CE2    sing Y N 418 
TRP NE1   HE1    sing N N 419 
TRP CE2   CZ2    sing Y N 420 
TRP CE3   CZ3    doub Y N 421 
TRP CE3   HE3    sing N N 422 
TRP CZ2   CH2    doub Y N 423 
TRP CZ2   HZ2    sing N N 424 
TRP CZ3   CH2    sing Y N 425 
TRP CZ3   HZ3    sing N N 426 
TRP CH2   HH2    sing N N 427 
TRP OXT   HXT    sing N N 428 
TYR N     CA     sing N N 429 
TYR N     H      sing N N 430 
TYR N     H2     sing N N 431 
TYR CA    C      sing N N 432 
TYR CA    CB     sing N N 433 
TYR CA    HA     sing N N 434 
TYR C     O      doub N N 435 
TYR C     OXT    sing N N 436 
TYR CB    CG     sing N N 437 
TYR CB    HB2    sing N N 438 
TYR CB    HB3    sing N N 439 
TYR CG    CD1    doub Y N 440 
TYR CG    CD2    sing Y N 441 
TYR CD1   CE1    sing Y N 442 
TYR CD1   HD1    sing N N 443 
TYR CD2   CE2    doub Y N 444 
TYR CD2   HD2    sing N N 445 
TYR CE1   CZ     doub Y N 446 
TYR CE1   HE1    sing N N 447 
TYR CE2   CZ     sing Y N 448 
TYR CE2   HE2    sing N N 449 
TYR CZ    OH     sing N N 450 
TYR OH    HH     sing N N 451 
TYR OXT   HXT    sing N N 452 
VAL N     CA     sing N N 453 
VAL N     H      sing N N 454 
VAL N     H2     sing N N 455 
VAL CA    C      sing N N 456 
VAL CA    CB     sing N N 457 
VAL CA    HA     sing N N 458 
VAL C     O      doub N N 459 
VAL C     OXT    sing N N 460 
VAL CB    CG1    sing N N 461 
VAL CB    CG2    sing N N 462 
VAL CB    HB     sing N N 463 
VAL CG1   HG11   sing N N 464 
VAL CG1   HG12   sing N N 465 
VAL CG1   HG13   sing N N 466 
VAL CG2   HG21   sing N N 467 
VAL CG2   HG22   sing N N 468 
VAL CG2   HG23   sing N N 469 
VAL OXT   HXT    sing N N 470 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8ZC7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZC8 
_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]   0.008776 
_atom_sites.fract_transf_matrix[1][2]   0.005067 
_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]   0.010133 
_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]   0.009194 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . LEU A 1 6   ? 40.015 9.840   10.547  1.00 87.68  ?  6   LEU A N     1 
ATOM   2    C CA    . LEU A 1 6   ? 39.782 8.875   11.614  1.00 97.70  ?  6   LEU A CA    1 
ATOM   3    C C     . LEU A 1 6   ? 38.360 8.961   12.198  1.00 102.51 ?  6   LEU A C     1 
ATOM   4    O O     . LEU A 1 6   ? 38.152 9.738   13.113  1.00 114.70 ?  6   LEU A O     1 
ATOM   5    C CB    . LEU A 1 6   ? 40.804 9.101   12.718  1.00 95.00  ?  6   LEU A CB    1 
ATOM   6    C CG    . LEU A 1 6   ? 41.280 7.909   13.534  1.00 99.56  ?  6   LEU A CG    1 
ATOM   7    C CD1   . LEU A 1 6   ? 42.314 8.406   14.531  1.00 95.61  ?  6   LEU A CD1   1 
ATOM   8    C CD2   . LEU A 1 6   ? 40.145 7.158   14.224  1.00 95.74  ?  6   LEU A CD2   1 
ATOM   9    N N     . SER A 1 7   ? 37.414 8.124   11.733  1.00 97.29  ?  7   SER A N     1 
ATOM   10   C CA    . SER A 1 7   ? 35.960 8.302   11.964  1.00 104.05 ?  7   SER A CA    1 
ATOM   11   C C     . SER A 1 7   ? 35.424 9.553   11.260  1.00 118.05 ?  7   SER A C     1 
ATOM   12   O O     . SER A 1 7   ? 34.470 10.179  11.749  1.00 123.73 ?  7   SER A O     1 
ATOM   13   C CB    . SER A 1 7   ? 35.584 8.340   13.465  1.00 106.96 ?  7   SER A CB    1 
ATOM   14   O OG    . SER A 1 7   ? 34.230 8.748   13.709  1.00 101.50 ?  7   SER A OG    1 
ATOM   15   N N     . GLU A 1 8   ? 36.040 9.921   10.110  1.00 116.10 ?  8   GLU A N     1 
ATOM   16   C CA    . GLU A 1 8   ? 35.570 11.044  9.280   1.00 108.65 ?  8   GLU A CA    1 
ATOM   17   C C     . GLU A 1 8   ? 34.119 10.870  8.866   1.00 114.39 ?  8   GLU A C     1 
ATOM   18   O O     . GLU A 1 8   ? 33.411 11.861  8.652   1.00 108.27 ?  8   GLU A O     1 
ATOM   19   C CB    . GLU A 1 8   ? 36.421 11.198  8.011   1.00 98.68  ?  8   GLU A CB    1 
ATOM   20   C CG    . GLU A 1 8   ? 37.868 11.561  8.262   1.00 98.23  ?  8   GLU A CG    1 
ATOM   21   C CD    . GLU A 1 8   ? 38.822 10.483  7.815   1.00 98.01  ?  8   GLU A CD    1 
ATOM   22   O OE1   . GLU A 1 8   ? 38.489 9.805   6.825   1.00 98.22  ?  8   GLU A OE1   1 
ATOM   23   O OE2   . GLU A 1 8   ? 39.882 10.306  8.462   1.00 95.71  -1 8   GLU A OE2   1 
ATOM   24   N N     . LEU A 1 9   ? 33.671 9.587   8.673   1.00 113.31 ?  9   LEU A N     1 
ATOM   25   C CA    . LEU A 1 9   ? 32.287 9.178   8.564   1.00 110.12 ?  9   LEU A CA    1 
ATOM   26   C C     . LEU A 1 9   ? 31.735 8.899   9.946   1.00 109.75 ?  9   LEU A C     1 
ATOM   27   O O     . LEU A 1 9   ? 32.484 8.569   10.878  1.00 111.70 ?  9   LEU A O     1 
ATOM   28   C CB    . LEU A 1 9   ? 32.148 7.931   7.705   1.00 107.73 ?  9   LEU A CB    1 
ATOM   29   C CG    . LEU A 1 9   ? 31.998 8.259   6.219   1.00 110.91 ?  9   LEU A CG    1 
ATOM   30   C CD1   . LEU A 1 9   ? 32.140 7.019   5.373   1.00 104.94 ?  9   LEU A CD1   1 
ATOM   31   C CD2   . LEU A 1 9   ? 30.675 8.975   5.899   1.00 112.68 ?  9   LEU A CD2   1 
ATOM   32   N N     . PRO A 1 10  ? 30.432 9.049   10.097  1.00 112.05 ?  10  PRO A N     1 
ATOM   33   C CA    . PRO A 1 10  ? 29.818 8.687   11.370  1.00 112.41 ?  10  PRO A CA    1 
ATOM   34   C C     . PRO A 1 10  ? 29.995 7.197   11.613  1.00 112.66 ?  10  PRO A C     1 
ATOM   35   O O     . PRO A 1 10  ? 29.774 6.367   10.728  1.00 109.23 ?  10  PRO A O     1 
ATOM   36   C CB    . PRO A 1 10  ? 28.345 9.069   11.174  1.00 111.10 ?  10  PRO A CB    1 
ATOM   37   C CG    . PRO A 1 10  ? 28.303 9.926   9.915   1.00 107.42 ?  10  PRO A CG    1 
ATOM   38   C CD    . PRO A 1 10  ? 29.450 9.491   9.095   1.00 109.34 ?  10  PRO A CD    1 
ATOM   39   N N     . MET A 1 11  ? 30.396 6.846   12.819  1.00 115.15 ?  11  MET A N     1 
ATOM   40   C CA    . MET A 1 11  ? 30.419 5.428   13.054  1.00 111.20 ?  11  MET A CA    1 
ATOM   41   C C     . MET A 1 11  ? 29.447 5.081   14.170  1.00 114.18 ?  11  MET A C     1 
ATOM   42   O O     . MET A 1 11  ? 29.482 5.720   15.239  1.00 116.48 ?  11  MET A O     1 
ATOM   43   C CB    . MET A 1 11  ? 31.829 4.945   13.386  1.00 105.46 ?  11  MET A CB    1 
ATOM   44   C CG    . MET A 1 11  ? 32.759 5.015   12.188  1.00 98.06  ?  11  MET A CG    1 
ATOM   45   S SD    . MET A 1 11  ? 34.396 4.424   12.609  1.00 87.36  ?  11  MET A SD    1 
ATOM   46   C CE    . MET A 1 11  ? 34.496 4.899   14.345  1.00 93.27  ?  11  MET A CE    1 
ATOM   47   N N     . PRO A 1 12  ? 28.532 4.133   13.943  1.00 111.63 ?  12  PRO A N     1 
ATOM   48   C CA    . PRO A 1 12  ? 27.641 3.685   15.017  1.00 108.41 ?  12  PRO A CA    1 
ATOM   49   C C     . PRO A 1 12  ? 28.416 2.937   16.085  1.00 100.23 ?  12  PRO A C     1 
ATOM   50   O O     . PRO A 1 12  ? 29.563 2.522   15.891  1.00 99.10  ?  12  PRO A O     1 
ATOM   51   C CB    . PRO A 1 12  ? 26.637 2.766   14.303  1.00 105.08 ?  12  PRO A CB    1 
ATOM   52   C CG    . PRO A 1 12  ? 27.324 2.337   13.078  1.00 103.02 ?  12  PRO A CG    1 
ATOM   53   C CD    . PRO A 1 12  ? 28.225 3.475   12.661  1.00 106.32 ?  12  PRO A CD    1 
ATOM   54   N N     . SER A 1 13  ? 27.790 2.837   17.254  1.00 99.37  ?  13  SER A N     1 
ATOM   55   C CA    . SER A 1 13  ? 28.422 2.103   18.370  1.00 98.62  ?  13  SER A CA    1 
ATOM   56   C C     . SER A 1 13  ? 27.536 0.902   18.683  1.00 95.76  ?  13  SER A C     1 
ATOM   57   O O     . SER A 1 13  ? 26.496 1.090   19.331  1.00 95.58  ?  13  SER A O     1 
ATOM   58   C CB    . SER A 1 13  ? 28.587 2.983   19.568  1.00 99.45  ?  13  SER A CB    1 
ATOM   59   O OG    . SER A 1 13  ? 29.862 3.604   19.562  1.00 109.44 ?  13  SER A OG    1 
ATOM   60   N N     . PRO A 1 14  ? 27.908 -0.319  18.247  1.00 91.75  ?  14  PRO A N     1 
ATOM   61   C CA    . PRO A 1 14  ? 27.085 -1.505  18.486  1.00 88.88  ?  14  PRO A CA    1 
ATOM   62   C C     . PRO A 1 14  ? 26.917 -1.742  19.982  1.00 87.87  ?  14  PRO A C     1 
ATOM   63   O O     . PRO A 1 14  ? 27.795 -1.420  20.787  1.00 88.19  ?  14  PRO A O     1 
ATOM   64   C CB    . PRO A 1 14  ? 27.882 -2.635  17.817  1.00 84.60  ?  14  PRO A CB    1 
ATOM   65   C CG    . PRO A 1 14  ? 28.967 -1.939  17.007  1.00 83.13  ?  14  PRO A CG    1 
ATOM   66   C CD    . PRO A 1 14  ? 29.226 -0.664  17.690  1.00 84.45  ?  14  PRO A CD    1 
ATOM   67   N N     . ALA A 1 15  ? 25.752 -2.262  20.356  1.00 86.19  ?  15  ALA A N     1 
ATOM   68   C CA    . ALA A 1 15  ? 25.588 -2.912  21.648  1.00 89.27  ?  15  ALA A CA    1 
ATOM   69   C C     . ALA A 1 15  ? 25.793 -4.394  21.411  1.00 86.81  ?  15  ALA A C     1 
ATOM   70   O O     . ALA A 1 15  ? 25.270 -4.940  20.432  1.00 90.62  ?  15  ALA A O     1 
ATOM   71   C CB    . ALA A 1 15  ? 24.202 -2.662  22.251  1.00 96.41  ?  15  ALA A CB    1 
ATOM   72   N N     . SER A 1 16  ? 26.580 -5.047  22.276  1.00 82.80  ?  16  SER A N     1 
ATOM   73   C CA    . SER A 1 16  ? 26.813 -6.465  22.027  1.00 87.14  ?  16  SER A CA    1 
ATOM   74   C C     . SER A 1 16  ? 25.507 -7.249  22.083  1.00 90.01  ?  16  SER A C     1 
ATOM   75   O O     . SER A 1 16  ? 25.403 -8.311  21.464  1.00 90.02  ?  16  SER A O     1 
ATOM   76   C CB    . SER A 1 16  ? 27.866 -7.047  22.974  1.00 81.54  ?  16  SER A CB    1 
ATOM   77   O OG    . SER A 1 16  ? 27.726 -6.571  24.285  1.00 96.56  ?  16  SER A OG    1 
ATOM   78   N N     . GLU A 1 17  ? 24.482 -6.727  22.769  1.00 90.60  ?  17  GLU A N     1 
ATOM   79   C CA    . GLU A 1 17  ? 23.160 -7.356  22.720  1.00 88.76  ?  17  GLU A CA    1 
ATOM   80   C C     . GLU A 1 17  ? 22.505 -7.182  21.350  1.00 94.79  ?  17  GLU A C     1 
ATOM   81   O O     . GLU A 1 17  ? 21.816 -8.090  20.862  1.00 94.47  ?  17  GLU A O     1 
ATOM   82   C CB    . GLU A 1 17  ? 22.259 -6.793  23.830  1.00 97.98  ?  17  GLU A CB    1 
ATOM   83   C CG    . GLU A 1 17  ? 20.922 -7.526  24.037  1.00 97.67  ?  17  GLU A CG    1 
ATOM   84   C CD    . GLU A 1 17  ? 21.082 -8.954  24.575  1.00 106.63 ?  17  GLU A CD    1 
ATOM   85   O OE1   . GLU A 1 17  ? 22.201 -9.334  24.987  1.00 105.12 ?  17  GLU A OE1   1 
ATOM   86   O OE2   . GLU A 1 17  ? 20.081 -9.705  24.584  1.00 114.85 -1 17  GLU A OE2   1 
ATOM   87   N N     . GLU A 1 18  ? 22.701 -6.024  20.712  1.00 94.46  ?  18  GLU A N     1 
ATOM   88   C CA    . GLU A 1 18  ? 22.021 -5.767  19.445  1.00 94.58  ?  18  GLU A CA    1 
ATOM   89   C C     . GLU A 1 18  ? 22.631 -6.570  18.305  1.00 93.85  ?  18  GLU A C     1 
ATOM   90   O O     . GLU A 1 18  ? 21.910 -6.937  17.363  1.00 93.70  ?  18  GLU A O     1 
ATOM   91   C CB    . GLU A 1 18  ? 22.059 -4.275  19.102  1.00 93.58  ?  18  GLU A CB    1 
ATOM   92   C CG    . GLU A 1 18  ? 21.218 -3.397  20.007  1.00 96.51  ?  18  GLU A CG    1 
ATOM   93   C CD    . GLU A 1 18  ? 21.443 -1.922  19.751  1.00 100.04 ?  18  GLU A CD    1 
ATOM   94   O OE1   . GLU A 1 18  ? 22.239 -1.570  18.843  1.00 101.18 ?  18  GLU A OE1   1 
ATOM   95   O OE2   . GLU A 1 18  ? 20.820 -1.120  20.476  1.00 98.59  -1 18  GLU A OE2   1 
ATOM   96   N N     . VAL A 1 19  ? 23.947 -6.828  18.361  1.00 92.95  ?  19  VAL A N     1 
ATOM   97   C CA    . VAL A 1 19  ? 24.609 -7.607  17.313  1.00 88.83  ?  19  VAL A CA    1 
ATOM   98   C C     . VAL A 1 19  ? 24.209 -9.078  17.418  1.00 86.39  ?  19  VAL A C     1 
ATOM   99   O O     . VAL A 1 19  ? 24.046 -9.759  16.394  1.00 85.83  ?  19  VAL A O     1 
ATOM   100  C CB    . VAL A 1 19  ? 26.139 -7.403  17.362  1.00 82.87  ?  19  VAL A CB    1 
ATOM   101  C CG1   . VAL A 1 19  ? 26.496 -5.946  17.111  1.00 82.37  ?  19  VAL A CG1   1 
ATOM   102  C CG2   . VAL A 1 19  ? 26.700 -7.802  18.693  1.00 87.89  ?  19  VAL A CG2   1 
ATOM   103  N N     . GLY A 1 20  ? 24.008 -9.580  18.643  1.00 84.08  ?  20  GLY A N     1 
ATOM   104  C CA    . GLY A 1 20  ? 23.415 -10.899 18.792  1.00 87.48  ?  20  GLY A CA    1 
ATOM   105  C C     . GLY A 1 20  ? 22.014 -10.961 18.220  1.00 84.97  ?  20  GLY A C     1 
ATOM   106  O O     . GLY A 1 20  ? 21.688 -11.844 17.428  1.00 78.65  ?  20  GLY A O     1 
ATOM   107  N N     . ALA A 1 21  ? 21.172 -10.001 18.595  1.00 88.17  ?  21  ALA A N     1 
ATOM   108  C CA    . ALA A 1 21  ? 19.852 -9.905  17.985  1.00 88.51  ?  21  ALA A CA    1 
ATOM   109  C C     . ALA A 1 21  ? 19.954 -9.791  16.472  1.00 89.15  ?  21  ALA A C     1 
ATOM   110  O O     . ALA A 1 21  ? 19.059 -10.253 15.748  1.00 88.05  ?  21  ALA A O     1 
ATOM   111  C CB    . ALA A 1 21  ? 19.105 -8.697  18.553  1.00 96.80  ?  21  ALA A CB    1 
ATOM   112  N N     . LEU A 1 22  ? 21.038 -9.175  15.984  1.00 88.45  ?  22  LEU A N     1 
ATOM   113  C CA    . LEU A 1 22  ? 21.260 -9.053  14.544  1.00 87.46  ?  22  LEU A CA    1 
ATOM   114  C C     . LEU A 1 22  ? 21.636 -10.389 13.915  1.00 85.68  ?  22  LEU A C     1 
ATOM   115  O O     . LEU A 1 22  ? 21.110 -10.765 12.858  1.00 82.01  ?  22  LEU A O     1 
ATOM   116  C CB    . LEU A 1 22  ? 22.354 -8.022  14.264  1.00 83.53  ?  22  LEU A CB    1 
ATOM   117  C CG    . LEU A 1 22  ? 22.692 -7.870  12.781  1.00 77.39  ?  22  LEU A CG    1 
ATOM   118  C CD1   . LEU A 1 22  ? 21.512 -7.299  12.021  1.00 77.39  ?  22  LEU A CD1   1 
ATOM   119  C CD2   . LEU A 1 22  ? 23.914 -7.005  12.627  1.00 77.77  ?  22  LEU A CD2   1 
ATOM   120  N N     . TYR A 1 23  ? 22.569 -11.112 14.534  1.00 83.73  ?  23  TYR A N     1 
ATOM   121  C CA    . TYR A 1 23  ? 22.928 -12.401 13.967  1.00 83.37  ?  23  TYR A CA    1 
ATOM   122  C C     . TYR A 1 23  ? 21.883 -13.479 14.282  1.00 83.57  ?  23  TYR A C     1 
ATOM   123  O O     . TYR A 1 23  ? 21.725 -14.416 13.495  1.00 84.80  ?  23  TYR A O     1 
ATOM   124  C CB    . TYR A 1 23  ? 24.339 -12.799 14.423  1.00 81.26  ?  23  TYR A CB    1 
ATOM   125  C CG    . TYR A 1 23  ? 25.444 -12.104 13.639  1.00 78.34  ?  23  TYR A CG    1 
ATOM   126  C CD1   . TYR A 1 23  ? 25.505 -12.198 12.246  1.00 79.68  ?  23  TYR A CD1   1 
ATOM   127  C CD2   . TYR A 1 23  ? 26.419 -11.368 14.285  1.00 76.69  ?  23  TYR A CD2   1 
ATOM   128  C CE1   . TYR A 1 23  ? 26.501 -11.568 11.523  1.00 76.44  ?  23  TYR A CE1   1 
ATOM   129  C CE2   . TYR A 1 23  ? 27.426 -10.735 13.574  1.00 78.63  ?  23  TYR A CE2   1 
ATOM   130  C CZ    . TYR A 1 23  ? 27.465 -10.836 12.190  1.00 77.13  ?  23  TYR A CZ    1 
ATOM   131  O OH    . TYR A 1 23  ? 28.465 -10.210 11.467  1.00 77.16  ?  23  TYR A OH    1 
ATOM   132  N N     . ASP A 1 24  ? 21.136 -13.352 15.389  1.00 85.51  ?  24  ASP A N     1 
ATOM   133  C CA    . ASP A 1 24  ? 19.991 -14.235 15.601  1.00 85.09  ?  24  ASP A CA    1 
ATOM   134  C C     . ASP A 1 24  ? 19.086 -14.205 14.386  1.00 85.13  ?  24  ASP A C     1 
ATOM   135  O O     . ASP A 1 24  ? 18.776 -15.244 13.790  1.00 86.23  ?  24  ASP A O     1 
ATOM   136  C CB    . ASP A 1 24  ? 19.204 -13.817 16.844  1.00 81.93  ?  24  ASP A CB    1 
ATOM   137  C CG    . ASP A 1 24  ? 19.751 -14.431 18.102  1.00 74.97  ?  24  ASP A CG    1 
ATOM   138  O OD1   . ASP A 1 24  ? 20.377 -15.499 17.982  1.00 76.67  ?  24  ASP A OD1   1 
ATOM   139  O OD2   . ASP A 1 24  ? 19.574 -13.856 19.199  1.00 79.34  -1 24  ASP A OD2   1 
ATOM   140  N N     . ARG A 1 25  ? 18.708 -13.004 13.959  1.00 84.17  ?  25  ARG A N     1 
ATOM   141  C CA    . ARG A 1 25  ? 17.875 -12.900 12.776  1.00 88.02  ?  25  ARG A CA    1 
ATOM   142  C C     . ARG A 1 25  ? 18.572 -13.474 11.546  1.00 88.13  ?  25  ARG A C     1 
ATOM   143  O O     . ARG A 1 25  ? 17.908 -14.057 10.682  1.00 86.72  ?  25  ARG A O     1 
ATOM   144  C CB    . ARG A 1 25  ? 17.480 -11.441 12.561  1.00 88.25  ?  25  ARG A CB    1 
ATOM   145  C CG    . ARG A 1 25  ? 15.982 -11.237 12.352  1.00 92.10  ?  25  ARG A CG    1 
ATOM   146  C CD    . ARG A 1 25  ? 15.574 -9.776  12.529  1.00 96.81  ?  25  ARG A CD    1 
ATOM   147  N NE    . ARG A 1 25  ? 16.179 -9.196  13.725  1.00 105.31 ?  25  ARG A NE    1 
ATOM   148  C CZ    . ARG A 1 25  ? 16.987 -8.140  13.729  1.00 103.20 ?  25  ARG A CZ    1 
ATOM   149  N NH1   . ARG A 1 25  ? 17.282 -7.495  12.608  1.00 102.04 ?  25  ARG A NH1   1 
ATOM   150  N NH2   . ARG A 1 25  ? 17.496 -7.712  14.888  1.00 100.87 ?  25  ARG A NH2   1 
ATOM   151  N N     . PHE A 1 26  ? 19.898 -13.324 11.434  1.00 86.30  ?  26  PHE A N     1 
ATOM   152  C CA    . PHE A 1 26  ? 20.581 -13.826 10.239  1.00 83.68  ?  26  PHE A CA    1 
ATOM   153  C C     . PHE A 1 26  ? 20.622 -15.343 10.227  1.00 89.86  ?  26  PHE A C     1 
ATOM   154  O O     . PHE A 1 26  ? 20.273 -15.976 9.223   1.00 91.44  ?  26  PHE A O     1 
ATOM   155  C CB    . PHE A 1 26  ? 22.004 -13.280 10.144  1.00 81.60  ?  26  PHE A CB    1 
ATOM   156  C CG    . PHE A 1 26  ? 22.076 -11.887 9.614   1.00 84.65  ?  26  PHE A CG    1 
ATOM   157  C CD1   . PHE A 1 26  ? 21.151 -11.440 8.681   1.00 87.62  ?  26  PHE A CD1   1 
ATOM   158  C CD2   . PHE A 1 26  ? 23.059 -11.013 10.053  1.00 84.50  ?  26  PHE A CD2   1 
ATOM   159  C CE1   . PHE A 1 26  ? 21.212 -10.158 8.195   1.00 85.82  ?  26  PHE A CE1   1 
ATOM   160  C CE2   . PHE A 1 26  ? 23.126 -9.723  9.568   1.00 85.98  ?  26  PHE A CE2   1 
ATOM   161  C CZ    . PHE A 1 26  ? 22.203 -9.296  8.637   1.00 86.95  ?  26  PHE A CZ    1 
ATOM   162  N N     . THR A 1 27  ? 21.033 -15.938 11.352  1.00 87.02  ?  27  THR A N     1 
ATOM   163  C CA    . THR A 1 27  ? 21.377 -17.357 11.379  1.00 86.11  ?  27  THR A CA    1 
ATOM   164  C C     . THR A 1 27  ? 20.160 -18.228 11.145  1.00 85.86  ?  27  THR A C     1 
ATOM   165  O O     . THR A 1 27  ? 20.241 -19.259 10.462  1.00 88.14  ?  27  THR A O     1 
ATOM   166  C CB    . THR A 1 27  ? 22.027 -17.701 12.712  1.00 81.38  ?  27  THR A CB    1 
ATOM   167  O OG1   . THR A 1 27  ? 23.244 -16.960 12.838  1.00 81.75  ?  27  THR A OG1   1 
ATOM   168  C CG2   . THR A 1 27  ? 22.332 -19.193 12.795  1.00 86.46  ?  27  THR A CG2   1 
ATOM   169  N N     . ALA A 1 28  ? 19.032 -17.843 11.724  1.00 86.25  ?  28  ALA A N     1 
ATOM   170  C CA    . ALA A 1 28  ? 17.792 -18.587 11.562  1.00 92.37  ?  28  ALA A CA    1 
ATOM   171  C C     . ALA A 1 28  ? 17.047 -18.218 10.287  1.00 94.48  ?  28  ALA A C     1 
ATOM   172  O O     . ALA A 1 28  ? 16.118 -18.934 9.898   1.00 95.94  ?  28  ALA A O     1 
ATOM   173  C CB    . ALA A 1 28  ? 16.887 -18.373 12.782  1.00 88.86  ?  28  ALA A CB    1 
ATOM   174  N N     . LEU A 1 29  ? 17.436 -17.128 9.624   1.00 93.16  ?  29  LEU A N     1 
ATOM   175  C CA    . LEU A 1 29  ? 16.922 -16.854 8.296   1.00 93.75  ?  29  LEU A CA    1 
ATOM   176  C C     . LEU A 1 29  ? 17.461 -17.839 7.270   1.00 95.92  ?  29  LEU A C     1 
ATOM   177  O O     . LEU A 1 29  ? 17.120 -17.725 6.089   1.00 97.57  ?  29  LEU A O     1 
ATOM   178  C CB    . LEU A 1 29  ? 17.267 -15.417 7.899   1.00 90.72  ?  29  LEU A CB    1 
ATOM   179  N N     . GLY A 1 30  ? 18.291 -18.799 7.689   1.00 93.63  ?  30  GLY A N     1 
ATOM   180  C CA    . GLY A 1 30  ? 18.951 -19.717 6.780   1.00 87.27  ?  30  GLY A CA    1 
ATOM   181  C C     . GLY A 1 30  ? 20.160 -19.133 6.083   1.00 85.40  ?  30  GLY A C     1 
ATOM   182  O O     . GLY A 1 30  ? 20.897 -19.880 5.414   1.00 83.81  ?  30  GLY A O     1 
ATOM   183  N N     . ALA A 1 31  ? 20.388 -17.823 6.220   1.00 86.64  ?  31  ALA A N     1 
ATOM   184  C CA    . ALA A 1 31  ? 21.517 -17.140 5.606   1.00 85.09  ?  31  ALA A CA    1 
ATOM   185  C C     . ALA A 1 31  ? 22.829 -17.764 6.053   1.00 84.29  ?  31  ALA A C     1 
ATOM   186  O O     . ALA A 1 31  ? 23.495 -18.443 5.264   1.00 85.16  ?  31  ALA A O     1 
ATOM   187  C CB    . ALA A 1 31  ? 21.488 -15.650 5.958   1.00 86.97  ?  31  ALA A CB    1 
ATOM   188  N N     . ALA A 1 32  ? 23.178 -17.583 7.330   1.00 79.10  ?  32  ALA A N     1 
ATOM   189  C CA    . ALA A 1 32  ? 24.359 -18.217 7.909   1.00 79.29  ?  32  ALA A CA    1 
ATOM   190  C C     . ALA A 1 32  ? 24.023 -19.687 8.188   1.00 81.26  ?  32  ALA A C     1 
ATOM   191  O O     . ALA A 1 32  ? 23.797 -20.106 9.328   1.00 80.61  ?  32  ALA A O     1 
ATOM   192  C CB    . ALA A 1 32  ? 24.791 -17.472 9.172   1.00 78.36  ?  32  ALA A CB    1 
ATOM   193  N N     . SER A 1 33  ? 23.985 -20.454 7.098   1.00 76.75  ?  33  SER A N     1 
ATOM   194  C CA    . SER A 1 33  ? 23.585 -21.872 7.230   1.00 75.67  ?  33  SER A CA    1 
ATOM   195  C C     . SER A 1 33  ? 24.755 -22.753 7.654   1.00 70.78  ?  33  SER A C     1 
ATOM   196  O O     . SER A 1 33  ? 25.905 -22.296 7.605   1.00 68.96  ?  33  SER A O     1 
ATOM   197  C CB    . SER A 1 33  ? 22.941 -22.387 5.970   1.00 69.08  ?  33  SER A CB    1 
ATOM   198  O OG    . SER A 1 33  ? 21.732 -23.068 6.264   1.00 75.56  ?  33  SER A OG    1 
ATOM   199  N N     . LEU A 1 34  ? 24.445 -23.981 8.034   1.00 70.38  ?  34  LEU A N     1 
ATOM   200  C CA    . LEU A 1 34  ? 25.425 -24.944 8.517   1.00 69.85  ?  34  LEU A CA    1 
ATOM   201  C C     . LEU A 1 34  ? 26.611 -25.086 7.576   1.00 66.08  ?  34  LEU A C     1 
ATOM   202  O O     . LEU A 1 34  ? 26.457 -25.418 6.398   1.00 58.91  ?  34  LEU A O     1 
ATOM   203  C CB    . LEU A 1 34  ? 24.731 -26.294 8.714   1.00 68.47  ?  34  LEU A CB    1 
ATOM   204  C CG    . LEU A 1 34  ? 24.054 -26.328 10.083  1.00 75.11  ?  34  LEU A CG    1 
ATOM   205  C CD1   . LEU A 1 34  ? 22.712 -27.071 10.071  1.00 78.06  ?  34  LEU A CD1   1 
ATOM   206  C CD2   . LEU A 1 34  ? 25.029 -26.900 11.116  1.00 64.73  ?  34  LEU A CD2   1 
ATOM   207  N N     . GLY A 1 35  ? 27.802 -24.839 8.104   1.00 69.51  ?  35  GLY A N     1 
ATOM   208  C CA    . GLY A 1 35  ? 29.003 -25.145 7.355   1.00 66.08  ?  35  GLY A CA    1 
ATOM   209  C C     . GLY A 1 35  ? 29.480 -24.057 6.431   1.00 63.98  ?  35  GLY A C     1 
ATOM   210  O O     . GLY A 1 35  ? 30.302 -24.326 5.549   1.00 63.07  ?  35  GLY A O     1 
ATOM   211  N N     . GLU A 1 36  ? 29.004 -22.837 6.610   1.00 63.09  ?  36  GLU A N     1 
ATOM   212  C CA    . GLU A 1 36  ? 29.383 -21.717 5.772   1.00 65.82  ?  36  GLU A CA    1 
ATOM   213  C C     . GLU A 1 36  ? 30.213 -20.729 6.575   1.00 61.91  ?  36  GLU A C     1 
ATOM   214  O O     . GLU A 1 36  ? 30.035 -20.584 7.790   1.00 58.85  ?  36  GLU A O     1 
ATOM   215  C CB    . GLU A 1 36  ? 28.137 -21.061 5.204   1.00 64.30  ?  36  GLU A CB    1 
ATOM   216  C CG    . GLU A 1 36  ? 27.307 -22.073 4.457   1.00 70.50  ?  36  GLU A CG    1 
ATOM   217  C CD    . GLU A 1 36  ? 26.017 -21.499 3.914   1.00 71.22  ?  36  GLU A CD    1 
ATOM   218  O OE1   . GLU A 1 36  ? 25.313 -20.857 4.730   1.00 73.79  ?  36  GLU A OE1   1 
ATOM   219  O OE2   . GLU A 1 36  ? 25.715 -21.687 2.701   1.00 69.43  -1 36  GLU A OE2   1 
ATOM   220  N N     . ASN A 1 37  ? 31.162 -20.089 5.897   1.00 61.56  ?  37  ASN A N     1 
ATOM   221  C CA    . ASN A 1 37  ? 32.000 -19.085 6.524   1.00 58.87  ?  37  ASN A CA    1 
ATOM   222  C C     . ASN A 1 37  ? 31.320 -17.725 6.417   1.00 61.56  ?  37  ASN A C     1 
ATOM   223  O O     . ASN A 1 37  ? 30.786 -17.373 5.361   1.00 61.37  ?  37  ASN A O     1 
ATOM   224  C CB    . ASN A 1 37  ? 33.374 -19.043 5.857   1.00 59.21  ?  37  ASN A CB    1 
ATOM   225  C CG    . ASN A 1 37  ? 34.268 -20.213 6.252   1.00 58.37  ?  37  ASN A CG    1 
ATOM   226  O OD1   . ASN A 1 37  ? 34.438 -20.522 7.425   1.00 62.94  ?  37  ASN A OD1   1 
ATOM   227  N ND2   . ASN A 1 37  ? 34.862 -20.853 5.262   1.00 60.66  ?  37  ASN A ND2   1 
ATOM   228  N N     . LEU A 1 38  ? 31.280 -16.992 7.537   1.00 59.47  ?  38  LEU A N     1 
ATOM   229  C CA    . LEU A 1 38  ? 30.857 -15.586 7.545   1.00 60.93  ?  38  LEU A CA    1 
ATOM   230  C C     . LEU A 1 38  ? 32.080 -14.666 7.588   1.00 58.86  ?  38  LEU A C     1 
ATOM   231  O O     . LEU A 1 38  ? 32.351 -13.987 8.590   1.00 60.78  ?  38  LEU A O     1 
ATOM   232  C CB    . LEU A 1 38  ? 29.922 -15.311 8.721   1.00 61.38  ?  38  LEU A CB    1 
ATOM   233  C CG    . LEU A 1 38  ? 28.671 -16.166 8.777   1.00 60.07  ?  38  LEU A CG    1 
ATOM   234  C CD1   . LEU A 1 38  ? 28.270 -16.329 10.211  1.00 63.51  ?  38  LEU A CD1   1 
ATOM   235  C CD2   . LEU A 1 38  ? 27.573 -15.513 8.024   1.00 63.44  ?  38  LEU A CD2   1 
ATOM   236  N N     . HIS A 1 39  ? 32.824 -14.653 6.484   1.00 55.56  ?  39  HIS A N     1 
ATOM   237  C CA    . HIS A 1 39  ? 33.962 -13.754 6.382   1.00 58.74  ?  39  HIS A CA    1 
ATOM   238  C C     . HIS A 1 39  ? 34.511 -13.784 4.970   1.00 59.97  ?  39  HIS A C     1 
ATOM   239  O O     . HIS A 1 39  ? 34.127 -14.616 4.148   1.00 62.58  ?  39  HIS A O     1 
ATOM   240  C CB    . HIS A 1 39  ? 35.054 -14.088 7.402   1.00 61.81  ?  39  HIS A CB    1 
ATOM   241  C CG    . HIS A 1 39  ? 35.624 -15.471 7.297   1.00 60.46  ?  39  HIS A CG    1 
ATOM   242  N ND1   . HIS A 1 39  ? 35.385 -16.443 8.245   1.00 64.51  ?  39  HIS A ND1   1 
ATOM   243  C CD2   . HIS A 1 39  ? 36.481 -16.022 6.403   1.00 58.32  ?  39  HIS A CD2   1 
ATOM   244  C CE1   . HIS A 1 39  ? 36.043 -17.541 7.921   1.00 55.51  ?  39  HIS A CE1   1 
ATOM   245  N NE2   . HIS A 1 39  ? 36.720 -17.311 6.812   1.00 55.21  ?  39  HIS A NE2   1 
ATOM   246  N N     . PHE A 1 40  ? 35.415 -12.853 4.700   1.00 59.74  ?  40  PHE A N     1 
ATOM   247  C CA    . PHE A 1 40  ? 35.842 -12.615 3.331   1.00 60.19  ?  40  PHE A CA    1 
ATOM   248  C C     . PHE A 1 40  ? 36.621 -13.797 2.805   1.00 60.98  ?  40  PHE A C     1 
ATOM   249  O O     . PHE A 1 40  ? 37.280 -14.522 3.556   1.00 59.69  ?  40  PHE A O     1 
ATOM   250  C CB    . PHE A 1 40  ? 36.714 -11.357 3.211   1.00 62.20  ?  40  PHE A CB    1 
ATOM   251  C CG    . PHE A 1 40  ? 35.946 -10.070 3.308   1.00 63.01  ?  40  PHE A CG    1 
ATOM   252  C CD1   . PHE A 1 40  ? 35.203 -9.613  2.233   1.00 65.35  ?  40  PHE A CD1   1 
ATOM   253  C CD2   . PHE A 1 40  ? 35.972 -9.308  4.476   1.00 63.53  ?  40  PHE A CD2   1 
ATOM   254  C CE1   . PHE A 1 40  ? 34.487 -8.424  2.323   1.00 68.21  ?  40  PHE A CE1   1 
ATOM   255  C CE2   . PHE A 1 40  ? 35.254 -8.117  4.578   1.00 62.97  ?  40  PHE A CE2   1 
ATOM   256  C CZ    . PHE A 1 40  ? 34.514 -7.672  3.505   1.00 66.98  ?  40  PHE A CZ    1 
ATOM   257  N N     . GLY A 1 41  ? 36.521 -13.996 1.498   1.00 65.16  ?  41  GLY A N     1 
ATOM   258  C CA    . GLY A 1 41  ? 37.444 -14.873 0.828   1.00 60.52  ?  41  GLY A CA    1 
ATOM   259  C C     . GLY A 1 41  ? 38.754 -14.179 0.582   1.00 58.00  ?  41  GLY A C     1 
ATOM   260  O O     . GLY A 1 41  ? 38.833 -12.957 0.567   1.00 58.29  ?  41  GLY A O     1 
ATOM   261  N N     . TYR A 1 42  ? 39.798 -14.964 0.390   1.00 54.73  ?  42  TYR A N     1 
ATOM   262  C CA    . TYR A 1 42  ? 41.105 -14.401 0.125   1.00 59.04  ?  42  TYR A CA    1 
ATOM   263  C C     . TYR A 1 42  ? 41.724 -15.081 -1.086  1.00 63.04  ?  42  TYR A C     1 
ATOM   264  O O     . TYR A 1 42  ? 41.822 -16.311 -1.137  1.00 62.94  ?  42  TYR A O     1 
ATOM   265  C CB    . TYR A 1 42  ? 41.961 -14.554 1.346   1.00 57.44  ?  42  TYR A CB    1 
ATOM   266  C CG    . TYR A 1 42  ? 43.334 -13.968 1.272   1.00 62.53  ?  42  TYR A CG    1 
ATOM   267  C CD1   . TYR A 1 42  ? 44.300 -14.512 0.438   1.00 63.97  ?  42  TYR A CD1   1 
ATOM   268  C CD2   . TYR A 1 42  ? 43.693 -12.916 2.096   1.00 65.81  ?  42  TYR A CD2   1 
ATOM   269  C CE1   . TYR A 1 42  ? 45.563 -14.006 0.398   1.00 62.29  ?  42  TYR A CE1   1 
ATOM   270  C CE2   . TYR A 1 42  ? 44.962 -12.409 2.071   1.00 66.87  ?  42  TYR A CE2   1 
ATOM   271  C CZ    . TYR A 1 42  ? 45.894 -12.957 1.216   1.00 59.15  ?  42  TYR A CZ    1 
ATOM   272  O OH    . TYR A 1 42  ? 47.171 -12.440 1.186   1.00 58.28  ?  42  TYR A OH    1 
ATOM   273  N N     . TRP A 1 43  ? 42.148 -14.271 -2.047  1.00 64.37  ?  43  TRP A N     1 
ATOM   274  C CA    . TRP A 1 43  ? 42.809 -14.728 -3.256  1.00 63.47  ?  43  TRP A CA    1 
ATOM   275  C C     . TRP A 1 43  ? 44.160 -14.025 -3.384  1.00 68.09  ?  43  TRP A C     1 
ATOM   276  O O     . TRP A 1 43  ? 44.392 -12.986 -2.766  1.00 67.10  ?  43  TRP A O     1 
ATOM   277  C CB    . TRP A 1 43  ? 41.963 -14.435 -4.481  1.00 62.97  ?  43  TRP A CB    1 
ATOM   278  C CG    . TRP A 1 43  ? 40.565 -14.984 -4.514  1.00 65.62  ?  43  TRP A CG    1 
ATOM   279  C CD1   . TRP A 1 43  ? 40.145 -16.061 -5.224  1.00 70.10  ?  43  TRP A CD1   1 
ATOM   280  C CD2   . TRP A 1 43  ? 39.389 -14.437 -3.888  1.00 62.35  ?  43  TRP A CD2   1 
ATOM   281  N NE1   . TRP A 1 43  ? 38.793 -16.239 -5.067  1.00 69.12  ?  43  TRP A NE1   1 
ATOM   282  C CE2   . TRP A 1 43  ? 38.303 -15.254 -4.254  1.00 63.04  ?  43  TRP A CE2   1 
ATOM   283  C CE3   . TRP A 1 43  ? 39.151 -13.342 -3.054  1.00 61.27  ?  43  TRP A CE3   1 
ATOM   284  C CZ2   . TRP A 1 43  ? 36.998 -15.018 -3.813  1.00 64.02  ?  43  TRP A CZ2   1 
ATOM   285  C CZ3   . TRP A 1 43  ? 37.839 -13.105 -2.613  1.00 61.23  ?  43  TRP A CZ3   1 
ATOM   286  C CH2   . TRP A 1 43  ? 36.791 -13.944 -2.993  1.00 64.95  ?  43  TRP A CH2   1 
ATOM   287  N N     . ASP A 1 44  ? 45.065 -14.599 -4.193  1.00 75.74  ?  44  ASP A N     1 
ATOM   288  C CA    . ASP A 1 44  ? 46.406 -14.037 -4.393  1.00 77.00  ?  44  ASP A CA    1 
ATOM   289  C C     . ASP A 1 44  ? 46.475 -13.025 -5.522  1.00 77.58  ?  44  ASP A C     1 
ATOM   290  O O     . ASP A 1 44  ? 47.279 -12.084 -5.455  1.00 79.55  ?  44  ASP A O     1 
ATOM   291  C CB    . ASP A 1 44  ? 47.430 -15.126 -4.722  1.00 81.48  ?  44  ASP A CB    1 
ATOM   292  C CG    . ASP A 1 44  ? 47.244 -16.374 -3.904  1.00 84.80  ?  44  ASP A CG    1 
ATOM   293  O OD1   . ASP A 1 44  ? 47.645 -16.362 -2.714  1.00 80.76  ?  44  ASP A OD1   1 
ATOM   294  O OD2   . ASP A 1 44  ? 46.692 -17.354 -4.466  1.00 85.40  -1 44  ASP A OD2   1 
ATOM   295  N N     . SER A 1 45  ? 45.691 -13.273 -6.568  1.00 74.53  ?  45  SER A N     1 
ATOM   296  C CA    . SER A 1 45  ? 45.733 -12.392 -7.754  1.00 82.82  ?  45  SER A CA    1 
ATOM   297  C C     . SER A 1 45  ? 44.311 -11.962 -8.102  1.00 87.47  ?  45  SER A C     1 
ATOM   298  O O     . SER A 1 45  ? 43.397 -12.779 -7.954  1.00 84.75  ?  45  SER A O     1 
ATOM   299  C CB    . SER A 1 45  ? 46.364 -13.108 -8.902  1.00 86.83  ?  45  SER A CB    1 
ATOM   300  O OG    . SER A 1 45  ? 45.579 -14.223 -9.293  1.00 96.13  ?  45  SER A OG    1 
ATOM   301  N N     . PRO A 1 46  ? 44.080 -10.713 -8.542  1.00 86.13  ?  46  PRO A N     1 
ATOM   302  C CA    . PRO A 1 46  ? 42.710 -10.267 -8.819  1.00 88.89  ?  46  PRO A CA    1 
ATOM   303  C C     . PRO A 1 46  ? 42.043 -11.070 -9.921  1.00 94.18  ?  46  PRO A C     1 
ATOM   304  O O     . PRO A 1 46  ? 40.804 -11.106 -9.973  1.00 92.25  ?  46  PRO A O     1 
ATOM   305  C CB    . PRO A 1 46  ? 42.891 -8.793  -9.209  1.00 84.64  ?  46  PRO A CB    1 
ATOM   306  C CG    . PRO A 1 46  ? 44.304 -8.433  -8.749  1.00 83.47  ?  46  PRO A CG    1 
ATOM   307  C CD    . PRO A 1 46  ? 45.081 -9.694  -8.888  1.00 79.74  ?  46  PRO A CD    1 
ATOM   308  N N     . ASP A 1 47  ? 42.821 -11.831 -10.681 1.00 95.31  ?  47  ASP A N     1 
ATOM   309  C CA    . ASP A 1 47  ? 42.252 -12.623 -11.800 1.00 94.23  ?  47  ASP A CA    1 
ATOM   310  C C     . ASP A 1 47  ? 42.094 -14.078 -11.362 1.00 93.09  ?  47  ASP A C     1 
ATOM   311  O O     . ASP A 1 47  ? 41.648 -14.894 -12.183 1.00 93.41  ?  47  ASP A O     1 
ATOM   312  C CB    . ASP A 1 47  ? 43.146 -12.516 -13.033 1.00 95.17  ?  47  ASP A CB    1 
ATOM   313  C CG    . ASP A 1 47  ? 44.544 -13.054 -12.789 1.00 102.04 ?  47  ASP A CG    1 
ATOM   314  O OD1   . ASP A 1 47  ? 44.829 -13.436 -11.639 1.00 101.22 ?  47  ASP A OD1   1 
ATOM   315  O OD2   . ASP A 1 47  ? 45.338 -13.079 -13.747 1.00 104.73 -1 47  ASP A OD2   1 
ATOM   316  N N     . SER A 1 48  ? 42.432 -14.386 -10.111 1.00 97.09  ?  48  SER A N     1 
ATOM   317  C CA    . SER A 1 48  ? 42.413 -15.782 -9.648  1.00 88.23  ?  48  SER A CA    1 
ATOM   318  C C     . SER A 1 48  ? 40.994 -16.304 -9.527  1.00 80.21  ?  48  SER A C     1 
ATOM   319  O O     . SER A 1 48  ? 40.158 -15.700 -8.852  1.00 81.46  ?  48  SER A O     1 
ATOM   320  C CB    . SER A 1 48  ? 43.107 -15.931 -8.288  1.00 81.20  ?  48  SER A CB    1 
ATOM   321  O OG    . SER A 1 48  ? 42.607 -17.054 -7.575  1.00 65.42  ?  48  SER A OG    1 
ATOM   322  N N     . GLN A 1 49  ? 40.736 -17.459 -10.133 1.00 77.79  ?  49  GLN A N     1 
ATOM   323  C CA    . GLN A 1 49  ? 39.373 -17.949 -10.267 1.00 80.34  ?  49  GLN A CA    1 
ATOM   324  C C     . GLN A 1 49  ? 39.029 -19.015 -9.227  1.00 77.37  ?  49  GLN A C     1 
ATOM   325  O O     . GLN A 1 49  ? 38.172 -19.865 -9.468  1.00 78.37  ?  49  GLN A O     1 
ATOM   326  C CB    . GLN A 1 49  ? 39.126 -18.457 -11.693 1.00 88.66  ?  49  GLN A CB    1 
ATOM   327  C CG    . GLN A 1 49  ? 38.878 -17.333 -12.725 1.00 92.62  ?  49  GLN A CG    1 
ATOM   328  C CD    . GLN A 1 49  ? 37.988 -16.193 -12.175 1.00 95.98  ?  49  GLN A CD    1 
ATOM   329  O OE1   . GLN A 1 49  ? 38.482 -15.215 -11.603 1.00 94.61  ?  49  GLN A OE1   1 
ATOM   330  N NE2   . GLN A 1 49  ? 36.674 -16.327 -12.349 1.00 97.40  ?  49  GLN A NE2   1 
ATOM   331  N N     . VAL A 1 50  ? 39.667 -18.975 -8.064  1.00 75.56  ?  50  VAL A N     1 
ATOM   332  C CA    . VAL A 1 50  ? 39.225 -19.880 -6.999  1.00 67.09  ?  50  VAL A CA    1 
ATOM   333  C C     . VAL A 1 50  ? 37.806 -19.494 -6.603  1.00 71.71  ?  50  VAL A C     1 
ATOM   334  O O     . VAL A 1 50  ? 37.492 -18.287 -6.551  1.00 68.69  ?  50  VAL A O     1 
ATOM   335  C CB    . VAL A 1 50  ? 40.189 -19.803 -5.803  1.00 63.85  ?  50  VAL A CB    1 
ATOM   336  C CG1   . VAL A 1 50  ? 39.842 -20.793 -4.752  1.00 64.53  ?  50  VAL A CG1   1 
ATOM   337  C CG2   . VAL A 1 50  ? 41.603 -20.067 -6.270  1.00 64.17  ?  50  VAL A CG2   1 
ATOM   338  N N     . PRO A 1 51  ? 36.892 -20.442 -6.371  1.00 73.59  ?  51  PRO A N     1 
ATOM   339  C CA    . PRO A 1 51  ? 35.508 -20.071 -6.063  1.00 66.20  ?  51  PRO A CA    1 
ATOM   340  C C     . PRO A 1 51  ? 35.397 -19.565 -4.638  1.00 63.30  ?  51  PRO A C     1 
ATOM   341  O O     . PRO A 1 51  ? 36.300 -19.718 -3.816  1.00 59.02  ?  51  PRO A O     1 
ATOM   342  C CB    . PRO A 1 51  ? 34.728 -21.373 -6.250  1.00 70.30  ?  51  PRO A CB    1 
ATOM   343  C CG    . PRO A 1 51  ? 35.720 -22.432 -5.977  1.00 65.95  ?  51  PRO A CG    1 
ATOM   344  C CD    . PRO A 1 51  ? 37.053 -21.907 -6.453  1.00 68.15  ?  51  PRO A CD    1 
ATOM   345  N N     . LEU A 1 52  ? 34.241 -18.969 -4.356  1.00 69.87  ?  52  LEU A N     1 
ATOM   346  C CA    . LEU A 1 52  ? 34.081 -18.249 -3.101  1.00 67.06  ?  52  LEU A CA    1 
ATOM   347  C C     . LEU A 1 52  ? 34.385 -19.145 -1.904  1.00 63.15  ?  52  LEU A C     1 
ATOM   348  O O     . LEU A 1 52  ? 35.197 -18.792 -1.038  1.00 62.17  ?  52  LEU A O     1 
ATOM   349  C CB    . LEU A 1 52  ? 32.672 -17.667 -2.999  1.00 66.60  ?  52  LEU A CB    1 
ATOM   350  C CG    . LEU A 1 52  ? 32.559 -16.921 -1.673  1.00 58.97  ?  52  LEU A CG    1 
ATOM   351  C CD1   . LEU A 1 52  ? 33.722 -15.949 -1.507  1.00 54.33  ?  52  LEU A CD1   1 
ATOM   352  C CD2   . LEU A 1 52  ? 31.222 -16.214 -1.577  1.00 66.69  ?  52  LEU A CD2   1 
ATOM   353  N N     . ALA A 1 53  ? 33.784 -20.334 -1.867  1.00 66.82  ?  53  ALA A N     1 
ATOM   354  C CA    . ALA A 1 53  ? 33.901 -21.173 -0.677  1.00 66.16  ?  53  ALA A CA    1 
ATOM   355  C C     . ALA A 1 53  ? 35.370 -21.470 -0.323  1.00 63.96  ?  53  ALA A C     1 
ATOM   356  O O     . ALA A 1 53  ? 35.749 -21.459 0.856   1.00 60.41  ?  53  ALA A O     1 
ATOM   357  C CB    . ALA A 1 53  ? 33.093 -22.451 -0.897  1.00 60.26  ?  53  ALA A CB    1 
ATOM   358  N N     . GLU A 1 54  ? 36.224 -21.706 -1.330  1.00 66.08  ?  54  GLU A N     1 
ATOM   359  C CA    . GLU A 1 54  ? 37.609 -22.070 -1.044  1.00 61.61  ?  54  GLU A CA    1 
ATOM   360  C C     . GLU A 1 54  ? 38.410 -20.862 -0.606  1.00 61.87  ?  54  GLU A C     1 
ATOM   361  O O     . GLU A 1 54  ? 39.346 -20.975 0.197   1.00 61.84  ?  54  GLU A O     1 
ATOM   362  C CB    . GLU A 1 54  ? 38.274 -22.697 -2.267  1.00 67.33  ?  54  GLU A CB    1 
ATOM   363  C CG    . GLU A 1 54  ? 37.701 -24.029 -2.784  1.00 70.83  ?  54  GLU A CG    1 
ATOM   364  C CD    . GLU A 1 54  ? 38.469 -24.593 -4.011  1.00 79.93  ?  54  GLU A CD    1 
ATOM   365  O OE1   . GLU A 1 54  ? 39.706 -24.344 -4.153  1.00 78.16  ?  54  GLU A OE1   1 
ATOM   366  O OE2   . GLU A 1 54  ? 37.814 -25.287 -4.834  1.00 81.44  -1 54  GLU A OE2   1 
ATOM   367  N N     . ALA A 1 55  ? 38.093 -19.700 -1.156  1.00 61.07  ?  55  ALA A N     1 
ATOM   368  C CA    . ALA A 1 55  ? 38.815 -18.520 -0.722  1.00 62.99  ?  55  ALA A CA    1 
ATOM   369  C C     . ALA A 1 55  ? 38.558 -18.261 0.752   1.00 58.75  ?  55  ALA A C     1 
ATOM   370  O O     . ALA A 1 55  ? 39.496 -17.984 1.506   1.00 56.51  ?  55  ALA A O     1 
ATOM   371  C CB    . ALA A 1 55  ? 38.422 -17.320 -1.581  1.00 62.06  ?  55  ALA A CB    1 
ATOM   372  N N     . THR A 1 56  ? 37.287 -18.391 1.181   1.00 60.81  ?  56  THR A N     1 
ATOM   373  C CA    . THR A 1 56  ? 36.909 -18.151 2.578   1.00 61.55  ?  56  THR A CA    1 
ATOM   374  C C     . THR A 1 56  ? 37.587 -19.147 3.507   1.00 59.12  ?  56  THR A C     1 
ATOM   375  O O     . THR A 1 56  ? 38.095 -18.766 4.567   1.00 55.17  ?  56  THR A O     1 
ATOM   376  C CB    . THR A 1 56  ? 35.381 -18.228 2.776   1.00 59.08  ?  56  THR A CB    1 
ATOM   377  O OG1   . THR A 1 56  ? 34.926 -19.553 2.509   1.00 63.63  ?  56  THR A OG1   1 
ATOM   378  C CG2   . THR A 1 56  ? 34.606 -17.260 1.882   1.00 56.69  ?  56  THR A CG2   1 
ATOM   379  N N     . ASP A 1 57  ? 37.613 -20.430 3.128   1.00 55.92  ?  57  ASP A N     1 
ATOM   380  C CA    . ASP A 1 57  ? 38.398 -21.394 3.889   1.00 55.75  ?  57  ASP A CA    1 
ATOM   381  C C     . ASP A 1 57  ? 39.849 -20.963 3.959   1.00 55.36  ?  57  ASP A C     1 
ATOM   382  O O     . ASP A 1 57  ? 40.482 -21.082 5.013   1.00 55.50  ?  57  ASP A O     1 
ATOM   383  C CB    . ASP A 1 57  ? 38.290 -22.794 3.284   1.00 60.07  ?  57  ASP A CB    1 
ATOM   384  C CG    . ASP A 1 57  ? 37.111 -23.599 3.838   1.00 60.60  ?  57  ASP A CG    1 
ATOM   385  O OD1   . ASP A 1 57  ? 36.490 -23.203 4.862   1.00 62.35  ?  57  ASP A OD1   1 
ATOM   386  O OD2   . ASP A 1 57  ? 36.803 -24.649 3.239   1.00 65.76  -1 57  ASP A OD2   1 
ATOM   387  N N     . ARG A 1 58  ? 40.385 -20.410 2.861   1.00 57.75  ?  58  ARG A N     1 
ATOM   388  C CA    . ARG A 1 58  ? 41.796 -20.037 2.863   1.00 58.29  ?  58  ARG A CA    1 
ATOM   389  C C     . ARG A 1 58  ? 42.105 -18.948 3.886   1.00 57.51  ?  58  ARG A C     1 
ATOM   390  O O     . ARG A 1 58  ? 43.147 -18.996 4.548   1.00 58.90  ?  58  ARG A O     1 
ATOM   391  C CB    . ARG A 1 58  ? 42.262 -19.590 1.494   1.00 59.27  ?  58  ARG A CB    1 
ATOM   392  C CG    . ARG A 1 58  ? 43.741 -19.237 1.587   1.00 64.34  ?  58  ARG A CG    1 
ATOM   393  C CD    . ARG A 1 58  ? 44.442 -19.316 0.277   1.00 72.97  ?  58  ARG A CD    1 
ATOM   394  N NE    . ARG A 1 58  ? 45.767 -18.708 0.342   1.00 79.30  ?  58  ARG A NE    1 
ATOM   395  C CZ    . ARG A 1 58  ? 46.398 -18.222 -0.720  1.00 83.67  ?  58  ARG A CZ    1 
ATOM   396  N NH1   . ARG A 1 58  ? 45.828 -18.223 -1.919  1.00 81.16  ?  58  ARG A NH1   1 
ATOM   397  N NH2   . ARG A 1 58  ? 47.625 -17.719 -0.581  1.00 86.22  ?  58  ARG A NH2   1 
ATOM   398  N N     . LEU A 1 59  ? 41.232 -17.952 4.036   1.00 54.50  ?  59  LEU A N     1 
ATOM   399  C CA    . LEU A 1 59  ? 41.460 -16.983 5.105   1.00 55.10  ?  59  LEU A CA    1 
ATOM   400  C C     . LEU A 1 59  ? 41.492 -17.666 6.471   1.00 58.11  ?  59  LEU A C     1 
ATOM   401  O O     . LEU A 1 59  ? 42.396 -17.402 7.281   1.00 54.92  ?  59  LEU A O     1 
ATOM   402  C CB    . LEU A 1 59  ? 40.402 -15.883 5.061   1.00 57.07  ?  59  LEU A CB    1 
ATOM   403  C CG    . LEU A 1 59  ? 40.449 -14.803 6.146   1.00 56.57  ?  59  LEU A CG    1 
ATOM   404  C CD1   . LEU A 1 59  ? 41.847 -14.265 6.420   1.00 59.30  ?  59  LEU A CD1   1 
ATOM   405  C CD2   . LEU A 1 59  ? 39.559 -13.712 5.686   1.00 55.66  ?  59  LEU A CD2   1 
ATOM   406  N N     . THR A 1 60  ? 40.533 -18.571 6.732   1.00 57.45  ?  60  THR A N     1 
ATOM   407  C CA    . THR A 1 60  ? 40.506 -19.291 8.005   1.00 51.10  ?  60  THR A CA    1 
ATOM   408  C C     . THR A 1 60  ? 41.845 -19.956 8.263   1.00 55.55  ?  60  THR A C     1 
ATOM   409  O O     . THR A 1 60  ? 42.417 -19.847 9.361   1.00 52.90  ?  60  THR A O     1 
ATOM   410  C CB    . THR A 1 60  ? 39.398 -20.351 8.015   1.00 54.38  ?  60  THR A CB    1 
ATOM   411  O OG1   . THR A 1 60  ? 38.135 -19.747 7.720   1.00 63.82  ?  60  THR A OG1   1 
ATOM   412  C CG2   . THR A 1 60  ? 39.319 -21.035 9.381   1.00 53.69  ?  60  THR A CG2   1 
ATOM   413  N N     . ASP A 1 61  ? 42.366 -20.638 7.241   1.00 54.51  ?  61  ASP A N     1 
ATOM   414  C CA    . ASP A 1 61  ? 43.614 -21.372 7.406   1.00 55.04  ?  61  ASP A CA    1 
ATOM   415  C C     . ASP A 1 61  ? 44.780 -20.424 7.596   1.00 56.97  ?  61  ASP A C     1 
ATOM   416  O O     . ASP A 1 61  ? 45.745 -20.737 8.308   1.00 58.35  ?  61  ASP A O     1 
ATOM   417  C CB    . ASP A 1 61  ? 43.866 -22.268 6.196   1.00 55.62  ?  61  ASP A CB    1 
ATOM   418  C CG    . ASP A 1 61  ? 42.874 -23.405 6.087   1.00 51.25  ?  61  ASP A CG    1 
ATOM   419  O OD1   . ASP A 1 61  ? 41.947 -23.452 6.906   1.00 50.74  ?  61  ASP A OD1   1 
ATOM   420  O OD2   . ASP A 1 61  ? 43.021 -24.254 5.183   1.00 48.35  -1 61  ASP A OD2   1 
ATOM   421  N N     . MET A 1 62  ? 44.720 -19.281 6.922   1.00 58.56  ?  62  MET A N     1 
ATOM   422  C CA    . MET A 1 62  ? 45.782 -18.293 6.999   1.00 58.85  ?  62  MET A CA    1 
ATOM   423  C C     . MET A 1 62  ? 45.930 -17.756 8.412   1.00 58.61  ?  62  MET A C     1 
ATOM   424  O O     . MET A 1 62  ? 47.049 -17.548 8.896   1.00 58.48  ?  62  MET A O     1 
ATOM   425  C CB    . MET A 1 62  ? 45.444 -17.185 6.011   1.00 59.11  ?  62  MET A CB    1 
ATOM   426  C CG    . MET A 1 62  ? 46.488 -16.160 5.652   1.00 62.16  ?  62  MET A CG    1 
ATOM   427  S SD    . MET A 1 62  ? 45.722 -15.041 4.434   1.00 76.28  ?  62  MET A SD    1 
ATOM   428  C CE    . MET A 1 62  ? 44.682 -16.220 3.503   1.00 66.68  ?  62  MET A CE    1 
ATOM   429  N N     . MET A 1 63  ? 44.805 -17.483 9.073   1.00 57.02  ?  63  MET A N     1 
ATOM   430  C CA    . MET A 1 63  ? 44.867 -16.961 10.425  1.00 58.42  ?  63  MET A CA    1 
ATOM   431  C C     . MET A 1 63  ? 45.220 -18.069 11.404  1.00 54.93  ?  63  MET A C     1 
ATOM   432  O O     . MET A 1 63  ? 45.942 -17.826 12.378  1.00 57.30  ?  63  MET A O     1 
ATOM   433  C CB    . MET A 1 63  ? 43.538 -16.273 10.771  1.00 60.62  ?  63  MET A CB    1 
ATOM   434  C CG    . MET A 1 63  ? 43.027 -15.266 9.666   1.00 54.42  ?  63  MET A CG    1 
ATOM   435  S SD    . MET A 1 63  ? 41.549 -14.378 10.035  1.00 64.99  ?  63  MET A SD    1 
ATOM   436  C CE    . MET A 1 63  ? 41.879 -13.948 11.759  1.00 60.75  ?  63  MET A CE    1 
ATOM   437  N N     . ALA A 1 64  ? 44.828 -19.307 11.092  1.00 52.94  ?  64  ALA A N     1 
ATOM   438  C CA    . ALA A 1 64  ? 45.011 -20.408 12.032  1.00 58.40  ?  64  ALA A CA    1 
ATOM   439  C C     . ALA A 1 64  ? 46.479 -20.712 12.262  1.00 58.93  ?  64  ALA A C     1 
ATOM   440  O O     . ALA A 1 64  ? 46.907 -20.899 13.407  1.00 68.54  ?  64  ALA A O     1 
ATOM   441  C CB    . ALA A 1 64  ? 44.280 -21.650 11.545  1.00 56.70  ?  64  ALA A CB    1 
ATOM   442  N N     . GLU A 1 65  ? 47.274 -20.763 11.202  1.00 58.17  ?  65  GLU A N     1 
ATOM   443  C CA    . GLU A 1 65  ? 48.665 -21.118 11.433  1.00 61.11  ?  65  GLU A CA    1 
ATOM   444  C C     . GLU A 1 65  ? 49.381 -20.023 12.205  1.00 61.32  ?  65  GLU A C     1 
ATOM   445  O O     . GLU A 1 65  ? 50.300 -20.307 12.985  1.00 63.63  ?  65  GLU A O     1 
ATOM   446  C CB    . GLU A 1 65  ? 49.365 -21.443 10.120  1.00 64.27  ?  65  GLU A CB    1 
ATOM   447  C CG    . GLU A 1 65  ? 49.728 -20.264 9.253   1.00 70.05  ?  65  GLU A CG    1 
ATOM   448  C CD    . GLU A 1 65  ? 50.072 -20.677 7.805   1.00 82.50  ?  65  GLU A CD    1 
ATOM   449  O OE1   . GLU A 1 65  ? 49.246 -21.375 7.144   1.00 79.32  ?  65  GLU A OE1   1 
ATOM   450  O OE2   . GLU A 1 65  ? 51.170 -20.295 7.330   1.00 93.71  -1 65  GLU A OE2   1 
ATOM   451  N N     . ARG A 1 66  ? 48.921 -18.786 12.073  1.00 58.52  ?  66  ARG A N     1 
ATOM   452  C CA    . ARG A 1 66  ? 49.508 -17.729 12.874  1.00 60.89  ?  66  ARG A CA    1 
ATOM   453  C C     . ARG A 1 66  ? 49.338 -18.005 14.347  1.00 62.77  ?  66  ARG A C     1 
ATOM   454  O O     . ARG A 1 66  ? 50.251 -17.730 15.132  1.00 65.49  ?  66  ARG A O     1 
ATOM   455  C CB    . ARG A 1 66  ? 48.884 -16.411 12.495  1.00 60.66  ?  66  ARG A CB    1 
ATOM   456  C CG    . ARG A 1 66  ? 49.196 -16.117 11.063  1.00 54.81  ?  66  ARG A CG    1 
ATOM   457  C CD    . ARG A 1 66  ? 48.749 -14.739 10.673  1.00 62.90  ?  66  ARG A CD    1 
ATOM   458  N NE    . ARG A 1 66  ? 49.646 -14.180 9.672   1.00 64.97  ?  66  ARG A NE    1 
ATOM   459  C CZ    . ARG A 1 66  ? 49.609 -14.503 8.389   1.00 62.18  ?  66  ARG A CZ    1 
ATOM   460  N NH1   . ARG A 1 66  ? 48.739 -15.390 7.926   1.00 53.67  ?  66  ARG A NH1   1 
ATOM   461  N NH2   . ARG A 1 66  ? 50.456 -13.921 7.552   1.00 56.87  ?  66  ARG A NH2   1 
ATOM   462  N N     . LEU A 1 67  ? 48.206 -18.603 14.729  1.00 64.37  ?  67  LEU A N     1 
ATOM   463  C CA    . LEU A 1 67  ? 48.015 -18.990 16.115  1.00 62.46  ?  67  LEU A CA    1 
ATOM   464  C C     . LEU A 1 67  ? 49.126 -19.902 16.590  1.00 63.51  ?  67  LEU A C     1 
ATOM   465  O O     . LEU A 1 67  ? 49.390 -19.970 17.798  1.00 73.34  ?  67  LEU A O     1 
ATOM   466  C CB    . LEU A 1 67  ? 46.680 -19.690 16.295  1.00 59.85  ?  67  LEU A CB    1 
ATOM   467  C CG    . LEU A 1 67  ? 45.452 -18.857 16.050  1.00 60.67  ?  67  LEU A CG    1 
ATOM   468  C CD1   . LEU A 1 67  ? 44.314 -19.820 15.863  1.00 58.80  ?  67  LEU A CD1   1 
ATOM   469  C CD2   . LEU A 1 67  ? 45.206 -17.929 17.224  1.00 59.33  ?  67  LEU A CD2   1 
ATOM   470  N N     . ARG A 1 68  ? 49.765 -20.620 15.664  1.00 62.96  ?  68  ARG A N     1 
ATOM   471  C CA    . ARG A 1 68  ? 50.886 -21.510 15.961  1.00 64.07  ?  68  ARG A CA    1 
ATOM   472  C C     . ARG A 1 68  ? 50.494 -22.581 16.990  1.00 66.36  ?  68  ARG A C     1 
ATOM   473  O O     . ARG A 1 68  ? 51.091 -22.708 18.068  1.00 62.15  ?  68  ARG A O     1 
ATOM   474  C CB    . ARG A 1 68  ? 52.102 -20.711 16.421  1.00 60.79  ?  68  ARG A CB    1 
ATOM   475  C CG    . ARG A 1 68  ? 52.779 -19.899 15.333  1.00 66.91  ?  68  ARG A CG    1 
ATOM   476  C CD    . ARG A 1 68  ? 53.934 -19.176 15.987  1.00 75.08  ?  68  ARG A CD    1 
ATOM   477  N NE    . ARG A 1 68  ? 54.852 -18.483 15.089  1.00 85.79  ?  68  ARG A NE    1 
ATOM   478  C CZ    . ARG A 1 68  ? 54.610 -17.323 14.484  1.00 87.97  ?  68  ARG A CZ    1 
ATOM   479  N NH1   . ARG A 1 68  ? 53.397 -16.765 14.487  1.00 78.81  ?  68  ARG A NH1   1 
ATOM   480  N NH2   . ARG A 1 68  ? 55.609 -16.710 13.848  1.00 90.44  ?  68  ARG A NH2   1 
ATOM   481  N N     . ILE A 1 69  ? 49.494 -23.386 16.615  1.00 71.05  ?  69  ILE A N     1 
ATOM   482  C CA    . ILE A 1 69  ? 48.889 -24.370 17.506  1.00 68.02  ?  69  ILE A CA    1 
ATOM   483  C C     . ILE A 1 69  ? 49.068 -25.777 16.944  1.00 70.95  ?  69  ILE A C     1 
ATOM   484  O O     . ILE A 1 69  ? 49.209 -25.975 15.732  1.00 67.93  ?  69  ILE A O     1 
ATOM   485  C CB    . ILE A 1 69  ? 47.395 -24.061 17.713  1.00 60.75  ?  69  ILE A CB    1 
ATOM   486  C CG1   . ILE A 1 69  ? 46.674 -24.150 16.383  1.00 58.29  ?  69  ILE A CG1   1 
ATOM   487  C CG2   . ILE A 1 69  ? 47.219 -22.685 18.320  1.00 59.12  ?  69  ILE A CG2   1 
ATOM   488  C CD1   . ILE A 1 69  ? 45.255 -23.690 16.439  1.00 57.45  ?  69  ILE A CD1   1 
ATOM   489  N N     . GLY A 1 70  ? 49.069 -26.756 17.846  1.00 70.86  ?  70  GLY A N     1 
ATOM   490  C CA    . GLY A 1 70  ? 49.055 -28.157 17.470  1.00 71.15  ?  70  GLY A CA    1 
ATOM   491  C C     . GLY A 1 70  ? 47.832 -28.850 18.046  1.00 69.22  ?  70  GLY A C     1 
ATOM   492  O O     . GLY A 1 70  ? 46.873 -28.163 18.423  1.00 68.80  ?  70  GLY A O     1 
ATOM   493  N N     . ALA A 1 71  ? 47.829 -30.190 18.103  1.00 69.15  ?  71  ALA A N     1 
ATOM   494  C CA    . ALA A 1 71  ? 46.818 -30.891 18.885  1.00 64.88  ?  71  ALA A CA    1 
ATOM   495  C C     . ALA A 1 71  ? 47.099 -30.702 20.365  1.00 63.49  ?  71  ALA A C     1 
ATOM   496  O O     . ALA A 1 71  ? 48.255 -30.670 20.794  1.00 63.99  ?  71  ALA A O     1 
ATOM   497  C CB    . ALA A 1 71  ? 46.792 -32.371 18.553  1.00 58.18  ?  71  ALA A CB    1 
ATOM   498  N N     . GLY A 1 72  ? 46.041 -30.570 21.147  1.00 63.40  ?  72  GLY A N     1 
ATOM   499  C CA    . GLY A 1 72  ? 46.215 -30.235 22.539  1.00 62.31  ?  72  GLY A CA    1 
ATOM   500  C C     . GLY A 1 72  ? 46.346 -28.760 22.826  1.00 60.46  ?  72  GLY A C     1 
ATOM   501  O O     . GLY A 1 72  ? 46.733 -28.384 23.946  1.00 70.81  ?  72  GLY A O     1 
ATOM   502  N N     . SER A 1 73  ? 46.038 -27.914 21.857  1.00 62.78  ?  73  SER A N     1 
ATOM   503  C CA    . SER A 1 73  ? 45.990 -26.484 22.073  1.00 64.05  ?  73  SER A CA    1 
ATOM   504  C C     . SER A 1 73  ? 44.573 -26.076 22.425  1.00 62.54  ?  73  SER A C     1 
ATOM   505  O O     . SER A 1 73  ? 43.615 -26.549 21.808  1.00 61.64  ?  73  SER A O     1 
ATOM   506  C CB    . SER A 1 73  ? 46.454 -25.740 20.826  1.00 61.12  ?  73  SER A CB    1 
ATOM   507  O OG    . SER A 1 73  ? 47.837 -25.954 20.605  1.00 62.62  ?  73  SER A OG    1 
ATOM   508  N N     . ARG A 1 74  ? 44.378 -25.266 23.342  1.00 61.37  ?  74  ARG A N     1 
ATOM   509  C CA    . ARG A 1 74  ? 43.044 -24.740 23.685  1.00 62.03  ?  74  ARG A CA    1 
ATOM   510  C C     . ARG A 1 74  ? 42.947 -23.398 22.973  1.00 57.88  ?  74  ARG A C     1 
ATOM   511  O O     . ARG A 1 74  ? 43.748 -22.510 23.285  1.00 58.48  ?  74  ARG A O     1 
ATOM   512  C CB    . ARG A 1 74  ? 42.938 -24.573 25.198  1.00 64.17  ?  74  ARG A CB    1 
ATOM   513  C CG    . ARG A 1 74  ? 43.008 -25.876 25.978  1.00 65.28  ?  74  ARG A CG    1 
ATOM   514  C CD    . ARG A 1 74  ? 42.148 -25.797 27.222  1.00 70.08  ?  74  ARG A CD    1 
ATOM   515  N NE    . ARG A 1 74  ? 42.224 -27.012 28.018  1.00 83.75  ?  74  ARG A NE    1 
ATOM   516  C CZ    . ARG A 1 74  ? 41.859 -28.213 27.586  1.00 85.14  ?  74  ARG A CZ    1 
ATOM   517  N NH1   . ARG A 1 74  ? 40.676 -28.381 27.024  1.00 82.38  ?  74  ARG A NH1   1 
ATOM   518  N NH2   . ARG A 1 74  ? 42.679 -29.241 27.720  1.00 79.99  ?  74  ARG A NH2   1 
ATOM   519  N N     . VAL A 1 75  ? 42.092 -23.228 22.094  1.00 56.25  ?  75  VAL A N     1 
ATOM   520  C CA    . VAL A 1 75  ? 41.915 -22.064 21.237  1.00 64.86  ?  75  VAL A CA    1 
ATOM   521  C C     . VAL A 1 75  ? 40.564 -21.426 21.536  1.00 64.12  ?  75  VAL A C     1 
ATOM   522  O O     . VAL A 1 75  ? 39.540 -22.124 21.597  1.00 61.71  ?  75  VAL A O     1 
ATOM   523  C CB    . VAL A 1 75  ? 42.002 -22.446 19.752  1.00 61.37  ?  75  VAL A CB    1 
ATOM   524  C CG1   . VAL A 1 75  ? 41.720 -21.244 18.909  1.00 59.30  ?  75  VAL A CG1   1 
ATOM   525  C CG2   . VAL A 1 75  ? 43.360 -23.015 19.440  1.00 54.16  ?  75  VAL A CG2   1 
ATOM   526  N N     . LEU A 1 76  ? 40.560 -20.102 21.715  1.00 60.42  ?  76  LEU A N     1 
ATOM   527  C CA    . LEU A 1 76  ? 39.318 -19.353 21.857  1.00 59.22  ?  76  LEU A CA    1 
ATOM   528  C C     . LEU A 1 76  ? 38.864 -18.840 20.500  1.00 61.72  ?  76  LEU A C     1 
ATOM   529  O O     . LEU A 1 76  ? 39.631 -18.194 19.777  1.00 59.41  ?  76  LEU A O     1 
ATOM   530  C CB    . LEU A 1 76  ? 39.483 -18.188 22.827  1.00 63.34  ?  76  LEU A CB    1 
ATOM   531  C CG    . LEU A 1 76  ? 38.231 -17.305 22.937  1.00 61.28  ?  76  LEU A CG    1 
ATOM   532  C CD1   . LEU A 1 76  ? 36.989 -18.082 23.353  1.00 59.52  ?  76  LEU A CD1   1 
ATOM   533  C CD2   . LEU A 1 76  ? 38.458 -16.134 23.875  1.00 63.81  ?  76  LEU A CD2   1 
ATOM   534  N N     . ASP A 1 77  ? 37.621 -19.125 20.157  1.00 61.28  ?  77  ASP A N     1 
ATOM   535  C CA    . ASP A 1 77  ? 37.052 -18.663 18.904  1.00 62.78  ?  77  ASP A CA    1 
ATOM   536  C C     . ASP A 1 77  ? 36.210 -17.453 19.289  1.00 66.94  ?  77  ASP A C     1 
ATOM   537  O O     . ASP A 1 77  ? 35.007 -17.559 19.577  1.00 63.59  ?  77  ASP A O     1 
ATOM   538  C CB    . ASP A 1 77  ? 36.255 -19.766 18.226  1.00 61.59  ?  77  ASP A CB    1 
ATOM   539  C CG    . ASP A 1 77  ? 35.692 -19.330 16.904  1.00 59.50  ?  77  ASP A CG    1 
ATOM   540  O OD1   . ASP A 1 77  ? 36.098 -18.233 16.471  1.00 65.73  ?  77  ASP A OD1   1 
ATOM   541  O OD2   . ASP A 1 77  ? 34.854 -20.064 16.294  1.00 61.87  -1 77  ASP A OD2   1 
ATOM   542  N N     . LEU A 1 78  ? 36.877 -16.290 19.316  1.00 66.86  ?  78  LEU A N     1 
ATOM   543  C CA    . LEU A 1 78  ? 36.297 -15.034 19.783  1.00 65.99  ?  78  LEU A CA    1 
ATOM   544  C C     . LEU A 1 78  ? 35.341 -14.468 18.758  1.00 67.26  ?  78  LEU A C     1 
ATOM   545  O O     . LEU A 1 78  ? 35.763 -13.725 17.868  1.00 73.80  ?  78  LEU A O     1 
ATOM   546  C CB    . LEU A 1 78  ? 37.385 -14.006 20.078  1.00 65.98  ?  78  LEU A CB    1 
ATOM   547  C CG    . LEU A 1 78  ? 36.922 -12.777 20.858  1.00 68.04  ?  78  LEU A CG    1 
ATOM   548  C CD1   . LEU A 1 78  ? 36.803 -13.093 22.338  1.00 68.05  ?  78  LEU A CD1   1 
ATOM   549  C CD2   . LEU A 1 78  ? 37.872 -11.642 20.668  1.00 64.49  ?  78  LEU A CD2   1 
ATOM   550  N N     . GLY A 1 79  ? 34.076 -14.875 18.835  1.00 61.48  ?  79  GLY A N     1 
ATOM   551  C CA    . GLY A 1 79  ? 33.040 -14.391 17.940  1.00 61.25  ?  79  GLY A CA    1 
ATOM   552  C C     . GLY A 1 79  ? 32.978 -15.408 16.831  1.00 68.22  ?  79  GLY A C     1 
ATOM   553  O O     . GLY A 1 79  ? 33.685 -15.272 15.829  1.00 68.71  ?  79  GLY A O     1 
ATOM   554  N N     . CYS A 1 80  ? 32.196 -16.485 17.030  1.00 66.18  ?  80  CYS A N     1 
ATOM   555  C CA    . CYS A 1 80  ? 32.288 -17.702 16.172  1.00 59.75  ?  80  CYS A CA    1 
ATOM   556  C C     . CYS A 1 80  ? 31.189 -18.009 15.156  1.00 60.25  ?  80  CYS A C     1 
ATOM   557  O O     . CYS A 1 80  ? 31.319 -19.048 14.492  1.00 64.23  ?  80  CYS A O     1 
ATOM   558  C CB    . CYS A 1 80  ? 32.209 -18.899 17.107  1.00 61.33  ?  80  CYS A CB    1 
ATOM   559  S SG    . CYS A 1 80  ? 30.591 -19.112 17.889  1.00 64.61  ?  80  CYS A SG    1 
ATOM   560  N N     . GLY A 1 81  ? 30.110 -17.255 15.096  1.00 62.77  ?  81  GLY A N     1 
ATOM   561  C CA    . GLY A 1 81  ? 29.115 -17.515 14.041  1.00 62.23  ?  81  GLY A CA    1 
ATOM   562  C C     . GLY A 1 81  ? 28.433 -18.872 14.073  1.00 61.68  ?  81  GLY A C     1 
ATOM   563  O O     . GLY A 1 81  ? 27.732 -19.195 15.052  1.00 68.32  ?  81  GLY A O     1 
ATOM   564  N N     . VAL A 1 82  ? 28.450 -19.602 13.037  1.00 59.68  ?  82  VAL A N     1 
ATOM   565  C CA    . VAL A 1 82  ? 27.776 -20.925 12.970  1.00 53.95  ?  82  VAL A CA    1 
ATOM   566  C C     . VAL A 1 82  ? 28.858 -21.978 13.155  1.00 54.43  ?  82  VAL A C     1 
ATOM   567  O O     . VAL A 1 82  ? 28.641 -23.120 12.741  1.00 59.96  ?  82  VAL A O     1 
ATOM   568  C CB    . VAL A 1 82  ? 27.006 -21.100 11.652  1.00 59.67  ?  82  VAL A CB    1 
ATOM   569  C CG1   . VAL A 1 82  ? 25.877 -20.094 11.549  1.00 59.42  ?  82  VAL A CG1   1 
ATOM   570  C CG2   . VAL A 1 82  ? 27.921 -21.006 10.443  1.00 65.68  ?  82  VAL A CG2   1 
ATOM   571  N N     . GLY A 1 83  ? 30.031 -21.563 13.638  1.00 58.14  ?  83  GLY A N     1 
ATOM   572  C CA    . GLY A 1 83  ? 31.047 -22.532 14.077  1.00 59.53  ?  83  GLY A CA    1 
ATOM   573  C C     . GLY A 1 83  ? 31.800 -23.180 12.941  1.00 57.07  ?  83  GLY A C     1 
ATOM   574  O O     . GLY A 1 83  ? 32.472 -24.169 13.188  1.00 61.64  ?  83  GLY A O     1 
ATOM   575  N N     . THR A 1 84  ? 31.647 -22.676 11.730  1.00 57.95  ?  84  THR A N     1 
ATOM   576  C CA    . THR A 1 84  ? 32.310 -23.350 10.591  1.00 61.89  ?  84  THR A CA    1 
ATOM   577  C C     . THR A 1 84  ? 33.832 -23.229 10.754  1.00 58.24  ?  84  THR A C     1 
ATOM   578  O O     . THR A 1 84  ? 34.488 -24.278 10.798  1.00 56.28  ?  84  THR A O     1 
ATOM   579  C CB    . THR A 1 84  ? 31.757 -22.835 9.262   1.00 60.49  ?  84  THR A CB    1 
ATOM   580  O OG1   . THR A 1 84  ? 30.339 -22.990 9.304   1.00 62.27  ?  84  THR A OG1   1 
ATOM   581  C CG2   . THR A 1 84  ? 32.361 -23.549 8.075   1.00 58.37  ?  84  THR A CG2   1 
ATOM   582  N N     . PRO A 1 85  ? 34.431 -22.026 10.864  1.00 54.16  ?  85  PRO A N     1 
ATOM   583  C CA    . PRO A 1 85  ? 35.867 -21.929 11.054  1.00 53.32  ?  85  PRO A CA    1 
ATOM   584  C C     . PRO A 1 85  ? 36.349 -22.693 12.291  1.00 52.78  ?  85  PRO A C     1 
ATOM   585  O O     . PRO A 1 85  ? 37.317 -23.391 12.187  1.00 50.29  ?  85  PRO A O     1 
ATOM   586  C CB    . PRO A 1 85  ? 36.068 -20.429 11.271  1.00 51.30  ?  85  PRO A CB    1 
ATOM   587  C CG    . PRO A 1 85  ? 34.964 -19.807 10.481  1.00 50.48  ?  85  PRO A CG    1 
ATOM   588  C CD    . PRO A 1 85  ? 33.794 -20.708 10.787  1.00 58.55  ?  85  PRO A CD    1 
ATOM   589  N N     . GLY A 1 86  ? 35.657 -22.542 13.419  1.00 57.81  ?  86  GLY A N     1 
ATOM   590  C CA    . GLY A 1 86  ? 36.092 -23.203 14.637  1.00 50.83  ?  86  GLY A CA    1 
ATOM   591  C C     . GLY A 1 86  ? 36.111 -24.716 14.509  1.00 49.04  ?  86  GLY A C     1 
ATOM   592  O O     . GLY A 1 86  ? 37.078 -25.366 14.914  1.00 48.93  ?  86  GLY A O     1 
ATOM   593  N N     . VAL A 1 87  ? 35.041 -25.296 13.949  1.00 50.25  ?  87  VAL A N     1 
ATOM   594  C CA    . VAL A 1 87  ? 34.977 -26.746 13.812  1.00 49.70  ?  87  VAL A CA    1 
ATOM   595  C C     . VAL A 1 87  ? 36.090 -27.214 12.905  1.00 52.68  ?  87  VAL A C     1 
ATOM   596  O O     . VAL A 1 87  ? 36.794 -28.191 13.199  1.00 57.28  ?  87  VAL A O     1 
ATOM   597  C CB    . VAL A 1 87  ? 33.605 -27.191 13.282  1.00 49.32  ?  87  VAL A CB    1 
ATOM   598  C CG1   . VAL A 1 87  ? 33.707 -28.584 12.738  1.00 52.29  ?  87  VAL A CG1   1 
ATOM   599  C CG2   . VAL A 1 87  ? 32.584 -27.184 14.390  1.00 49.88  ?  87  VAL A CG2   1 
ATOM   600  N N     . ARG A 1 88  ? 36.284 -26.499 11.802  1.00 51.33  ?  88  ARG A N     1 
ATOM   601  C CA    . ARG A 1 88  ? 37.388 -26.802 10.906  1.00 54.72  ?  88  ARG A CA    1 
ATOM   602  C C     . ARG A 1 88  ? 38.742 -26.645 11.589  1.00 53.95  ?  88  ARG A C     1 
ATOM   603  O O     . ARG A 1 88  ? 39.675 -27.401 11.300  1.00 54.76  ?  88  ARG A O     1 
ATOM   604  C CB    . ARG A 1 88  ? 37.316 -25.909 9.682   1.00 55.56  ?  88  ARG A CB    1 
ATOM   605  C CG    . ARG A 1 88  ? 38.617 -25.861 8.917   1.00 52.57  ?  88  ARG A CG    1 
ATOM   606  C CD    . ARG A 1 88  ? 38.519 -25.004 7.666   1.00 57.48  ?  88  ARG A CD    1 
ATOM   607  N NE    . ARG A 1 88  ? 39.680 -25.203 6.810   1.00 50.12  ?  88  ARG A NE    1 
ATOM   608  C CZ    . ARG A 1 88  ? 39.655 -25.787 5.621   1.00 53.33  ?  88  ARG A CZ    1 
ATOM   609  N NH1   . ARG A 1 88  ? 38.524 -26.176 5.063   1.00 58.14  ?  88  ARG A NH1   1 
ATOM   610  N NH2   . ARG A 1 88  ? 40.796 -25.982 4.973   1.00 50.66  ?  88  ARG A NH2   1 
ATOM   611  N N     . ILE A 1 89  ? 38.899 -25.661 12.475  1.00 53.27  ?  89  ILE A N     1 
ATOM   612  C CA    . ILE A 1 89  ? 40.201 -25.562 13.123  1.00 48.97  ?  89  ILE A CA    1 
ATOM   613  C C     . ILE A 1 89  ? 40.429 -26.747 14.053  1.00 51.61  ?  89  ILE A C     1 
ATOM   614  O O     . ILE A 1 89  ? 41.538 -27.280 14.132  1.00 53.24  ?  89  ILE A O     1 
ATOM   615  C CB    . ILE A 1 89  ? 40.367 -24.221 13.855  1.00 50.64  ?  89  ILE A CB    1 
ATOM   616  C CG1   . ILE A 1 89  ? 40.308 -23.074 12.845  1.00 47.77  ?  89  ILE A CG1   1 
ATOM   617  C CG2   . ILE A 1 89  ? 41.691 -24.202 14.673  1.00 48.36  ?  89  ILE A CG2   1 
ATOM   618  C CD1   . ILE A 1 89  ? 41.126 -21.875 13.207  1.00 47.80  ?  89  ILE A CD1   1 
ATOM   619  N N     . ALA A 1 90  ? 39.395 -27.175 14.780  1.00 52.65  ?  90  ALA A N     1 
ATOM   620  C CA    . ALA A 1 90  ? 39.574 -28.339 15.642  1.00 54.00  ?  90  ALA A CA    1 
ATOM   621  C C     . ALA A 1 90  ? 39.815 -29.581 14.803  1.00 54.57  ?  90  ALA A C     1 
ATOM   622  O O     . ALA A 1 90  ? 40.665 -30.420 15.139  1.00 52.72  ?  90  ALA A O     1 
ATOM   623  C CB    . ALA A 1 90  ? 38.361 -28.520 16.551  1.00 49.74  ?  90  ALA A CB    1 
ATOM   624  N N     . ARG A 1 91  ? 39.092 -29.686 13.687  1.00 50.83  ?  91  ARG A N     1 
ATOM   625  C CA    . ARG A 1 91  ? 39.170 -30.866 12.835  1.00 53.27  ?  91  ARG A CA    1 
ATOM   626  C C     . ARG A 1 91  ? 40.549 -31.030 12.217  1.00 54.54  ?  91  ARG A C     1 
ATOM   627  O O     . ARG A 1 91  ? 41.086 -32.144 12.168  1.00 55.14  ?  91  ARG A O     1 
ATOM   628  C CB    . ARG A 1 91  ? 38.126 -30.786 11.728  1.00 53.41  ?  91  ARG A CB    1 
ATOM   629  C CG    . ARG A 1 91  ? 38.451 -31.680 10.582  1.00 49.49  ?  91  ARG A CG    1 
ATOM   630  C CD    . ARG A 1 91  ? 37.244 -31.926 9.781   1.00 51.73  ?  91  ARG A CD    1 
ATOM   631  N NE    . ARG A 1 91  ? 36.849 -30.705 9.107   1.00 58.56  ?  91  ARG A NE    1 
ATOM   632  C CZ    . ARG A 1 91  ? 37.347 -30.309 7.941   1.00 65.25  ?  91  ARG A CZ    1 
ATOM   633  N NH1   . ARG A 1 91  ? 38.293 -31.000 7.319   1.00 56.91  ?  91  ARG A NH1   1 
ATOM   634  N NH2   . ARG A 1 91  ? 36.884 -29.184 7.383   1.00 66.35  ?  91  ARG A NH2   1 
ATOM   635  N N     . LEU A 1 92  ? 41.127 -29.945 11.719  1.00 55.24  ?  92  LEU A N     1 
ATOM   636  C CA    . LEU A 1 92  ? 42.410 -30.031 11.047  1.00 50.14  ?  92  LEU A CA    1 
ATOM   637  C C     . LEU A 1 92  ? 43.599 -29.899 11.979  1.00 53.68  ?  92  LEU A C     1 
ATOM   638  O O     . LEU A 1 92  ? 44.697 -30.271 11.575  1.00 56.62  ?  92  LEU A O     1 
ATOM   639  C CB    . LEU A 1 92  ? 42.529 -28.953 9.980   1.00 53.09  ?  92  LEU A CB    1 
ATOM   640  C CG    . LEU A 1 92  ? 41.439 -29.029 8.929   1.00 55.89  ?  92  LEU A CG    1 
ATOM   641  C CD1   . LEU A 1 92  ? 41.664 -28.010 7.843   1.00 47.53  ?  92  LEU A CD1   1 
ATOM   642  C CD2   . LEU A 1 92  ? 41.388 -30.422 8.373   1.00 48.43  ?  92  LEU A CD2   1 
ATOM   643  N N     . SER A 1 93  ? 43.428 -29.370 13.197  1.00 54.50  ?  93  SER A N     1 
ATOM   644  C CA    . SER A 1 93  ? 44.536 -29.206 14.127  1.00 52.41  ?  93  SER A CA    1 
ATOM   645  C C     . SER A 1 93  ? 44.456 -30.138 15.320  1.00 60.74  ?  93  SER A C     1 
ATOM   646  O O     . SER A 1 93  ? 45.488 -30.406 15.938  1.00 61.18  ?  93  SER A O     1 
ATOM   647  C CB    . SER A 1 93  ? 44.609 -27.752 14.638  1.00 51.39  ?  93  SER A CB    1 
ATOM   648  O OG    . SER A 1 93  ? 43.579 -27.427 15.571  1.00 56.39  ?  93  SER A OG    1 
ATOM   649  N N     . GLY A 1 94  ? 43.268 -30.635 15.650  1.00 60.92  ?  94  GLY A N     1 
ATOM   650  C CA    . GLY A 1 94  ? 43.115 -31.378 16.874  1.00 63.42  ?  94  GLY A CA    1 
ATOM   651  C C     . GLY A 1 94  ? 43.221 -30.524 18.106  1.00 64.91  ?  94  GLY A C     1 
ATOM   652  O O     . GLY A 1 94  ? 43.446 -31.053 19.202  1.00 68.05  ?  94  GLY A O     1 
ATOM   653  N N     . ALA A 1 95  ? 43.101 -29.208 17.948  1.00 62.01  ?  95  ALA A N     1 
ATOM   654  C CA    . ALA A 1 95  ? 43.067 -28.308 19.085  1.00 61.52  ?  95  ALA A CA    1 
ATOM   655  C C     . ALA A 1 95  ? 41.663 -28.290 19.676  1.00 57.29  ?  95  ALA A C     1 
ATOM   656  O O     . ALA A 1 95  ? 40.670 -28.348 18.944  1.00 58.47  ?  95  ALA A O     1 
ATOM   657  C CB    . ALA A 1 95  ? 43.498 -26.903 18.663  1.00 60.04  ?  95  ALA A CB    1 
ATOM   658  N N     . HIS A 1 96  ? 41.578 -28.258 21.005  1.00 59.88  ?  96  HIS A N     1 
ATOM   659  C CA    . HIS A 1 96  ? 40.278 -28.083 21.641  1.00 60.47  ?  96  HIS A CA    1 
ATOM   660  C C     . HIS A 1 96  ? 39.869 -26.632 21.420  1.00 55.31  ?  96  HIS A C     1 
ATOM   661  O O     . HIS A 1 96  ? 40.540 -25.704 21.884  1.00 57.29  ?  96  HIS A O     1 
ATOM   662  C CB    . HIS A 1 96  ? 40.324 -28.465 23.127  1.00 63.74  ?  96  HIS A CB    1 
ATOM   663  C CG    . HIS A 1 96  ? 41.041 -29.755 23.394  1.00 67.62  ?  96  HIS A CG    1 
ATOM   664  N ND1   . HIS A 1 96  ? 40.964 -30.845 22.548  1.00 72.74  ?  96  HIS A ND1   1 
ATOM   665  C CD2   . HIS A 1 96  ? 41.870 -30.123 24.399  1.00 71.90  ?  96  HIS A CD2   1 
ATOM   666  C CE1   . HIS A 1 96  ? 41.709 -31.830 23.020  1.00 72.71  ?  96  HIS A CE1   1 
ATOM   667  N NE2   . HIS A 1 96  ? 42.268 -31.418 24.145  1.00 78.56  ?  96  HIS A NE2   1 
ATOM   668  N N     . VAL A 1 97  ? 38.808 -26.420 20.655  1.00 52.50  ?  97  VAL A N     1 
ATOM   669  C CA    . VAL A 1 97  ? 38.317 -25.075 20.389  1.00 58.53  ?  97  VAL A CA    1 
ATOM   670  C C     . VAL A 1 97  ? 37.051 -24.823 21.200  1.00 59.77  ?  97  VAL A C     1 
ATOM   671  O O     . VAL A 1 97  ? 36.106 -25.626 21.177  1.00 57.65  ?  97  VAL A O     1 
ATOM   672  C CB    . VAL A 1 97  ? 38.061 -24.842 18.895  1.00 55.34  ?  97  VAL A CB    1 
ATOM   673  C CG1   . VAL A 1 97  ? 37.411 -23.490 18.695  1.00 52.44  ?  97  VAL A CG1   1 
ATOM   674  C CG2   . VAL A 1 97  ? 39.358 -24.935 18.156  1.00 49.99  ?  97  VAL A CG2   1 
ATOM   675  N N     . THR A 1 98  ? 37.101 -23.612 21.857  1.00 60.34  ?  98  THR A N     1 
ATOM   676  C CA    . THR A 1 98  ? 35.926 -23.121 22.610  1.00 59.50  ?  98  THR A CA    1 
ATOM   677  C C     . THR A 1 98  ? 35.499 -21.809 21.952  1.00 57.61  ?  98  THR A C     1 
ATOM   678  O O     . THR A 1 98  ? 36.199 -20.818 22.146  1.00 59.35  ?  98  THR A O     1 
ATOM   679  C CB    . THR A 1 98  ? 36.240 -22.976 24.101  1.00 60.23  ?  98  THR A CB    1 
ATOM   680  O OG1   . THR A 1 98  ? 36.597 -24.257 24.620  1.00 66.51  ?  98  THR A OG1   1 
ATOM   681  C CG2   . THR A 1 98  ? 35.077 -22.416 24.888  1.00 66.12  ?  98  THR A CG2   1 
ATOM   682  N N     . GLY A 1 99  ? 34.419 -21.855 21.119  1.00 58.14  ?  99  GLY A N     1 
ATOM   683  C CA    . GLY A 1 99  ? 33.899 -20.652 20.500  1.00 60.71  ?  99  GLY A CA    1 
ATOM   684  C C     . GLY A 1 99  ? 32.902 -19.949 21.406  1.00 60.79  ?  99  GLY A C     1 
ATOM   685  O O     . GLY A 1 99  ? 32.285 -20.568 22.271  1.00 58.72  ?  99  GLY A O     1 
ATOM   686  N N     . ILE A 1 100 ? 32.795 -18.627 21.240  1.00 62.60  ?  100 ILE A N     1 
ATOM   687  C CA    . ILE A 1 100 ? 31.773 -17.833 21.907  1.00 62.90  ?  100 ILE A CA    1 
ATOM   688  C C     . ILE A 1 100 ? 31.149 -16.952 20.845  1.00 65.10  ?  100 ILE A C     1 
ATOM   689  O O     . ILE A 1 100 ? 31.822 -16.509 19.910  1.00 66.44  ?  100 ILE A O     1 
ATOM   690  C CB    . ILE A 1 100 ? 32.302 -16.969 23.083  1.00 62.99  ?  100 ILE A CB    1 
ATOM   691  C CG1   . ILE A 1 100 ? 32.810 -15.611 22.580  1.00 67.54  ?  100 ILE A CG1   1 
ATOM   692  C CG2   . ILE A 1 100 ? 33.354 -17.726 23.904  1.00 61.25  ?  100 ILE A CG2   1 
ATOM   693  C CD1   . ILE A 1 100 ? 33.434 -14.757 23.646  1.00 68.06  ?  100 ILE A CD1   1 
ATOM   694  N N     . SER A 1 101 ? 29.844 -16.739 20.973  1.00 67.20  ?  101 SER A N     1 
ATOM   695  C CA    . SER A 1 101 ? 29.080 -15.829 20.130  1.00 71.33  ?  101 SER A CA    1 
ATOM   696  C C     . SER A 1 101 ? 28.134 -15.052 21.031  1.00 69.98  ?  101 SER A C     1 
ATOM   697  O O     . SER A 1 101 ? 27.954 -15.400 22.197  1.00 68.33  ?  101 SER A O     1 
ATOM   698  C CB    . SER A 1 101 ? 28.276 -16.561 19.048  1.00 71.38  ?  101 SER A CB    1 
ATOM   699  O OG    . SER A 1 101 ? 27.512 -15.633 18.285  1.00 67.22  ?  101 SER A OG    1 
ATOM   700  N N     . VAL A 1 102 ? 27.552 -13.973 20.503  1.00 70.57  ?  102 VAL A N     1 
ATOM   701  C CA    . VAL A 1 102 ? 26.536 -13.254 21.269  1.00 71.07  ?  102 VAL A CA    1 
ATOM   702  C C     . VAL A 1 102 ? 25.164 -13.640 20.739  1.00 76.28  ?  102 VAL A C     1 
ATOM   703  O O     . VAL A 1 102 ? 24.160 -13.527 21.448  1.00 83.68  ?  102 VAL A O     1 
ATOM   704  C CB    . VAL A 1 102 ? 26.736 -11.727 21.243  1.00 70.63  ?  102 VAL A CB    1 
ATOM   705  C CG1   . VAL A 1 102 ? 27.976 -11.350 22.005  1.00 74.29  ?  102 VAL A CG1   1 
ATOM   706  C CG2   . VAL A 1 102 ? 26.803 -11.215 19.842  1.00 76.18  ?  102 VAL A CG2   1 
ATOM   707  N N     . SER A 1 103 ? 25.108 -14.117 19.500  1.00 78.09  ?  103 SER A N     1 
ATOM   708  C CA    . SER A 1 103 ? 23.863 -14.630 18.948  1.00 77.14  ?  103 SER A CA    1 
ATOM   709  C C     . SER A 1 103 ? 23.603 -16.051 19.453  1.00 72.88  ?  103 SER A C     1 
ATOM   710  O O     . SER A 1 103 ? 24.399 -16.970 19.206  1.00 68.69  ?  103 SER A O     1 
ATOM   711  C CB    . SER A 1 103 ? 23.913 -14.590 17.426  1.00 75.15  ?  103 SER A CB    1 
ATOM   712  O OG    . SER A 1 103 ? 22.769 -15.211 16.865  1.00 79.14  ?  103 SER A OG    1 
ATOM   713  N N     . HIS A 1 104 ? 22.489 -16.232 20.168  1.00 73.04  ?  104 HIS A N     1 
ATOM   714  C CA    . HIS A 1 104 ? 22.155 -17.565 20.651  1.00 72.50  ?  104 HIS A CA    1 
ATOM   715  C C     . HIS A 1 104 ? 21.881 -18.506 19.490  1.00 70.66  ?  104 HIS A C     1 
ATOM   716  O O     . HIS A 1 104 ? 22.381 -19.634 19.461  1.00 68.54  ?  104 HIS A O     1 
ATOM   717  C CB    . HIS A 1 104 ? 20.956 -17.510 21.597  1.00 73.54  ?  104 HIS A CB    1 
ATOM   718  C CG    . HIS A 1 104 ? 20.466 -18.861 22.037  1.00 74.94  ?  104 HIS A CG    1 
ATOM   719  N ND1   . HIS A 1 104 ? 19.574 -19.609 21.291  1.00 71.50  ?  104 HIS A ND1   1 
ATOM   720  C CD2   . HIS A 1 104 ? 20.744 -19.594 23.144  1.00 74.13  ?  104 HIS A CD2   1 
ATOM   721  C CE1   . HIS A 1 104 ? 19.321 -20.742 21.924  1.00 70.23  ?  104 HIS A CE1   1 
ATOM   722  N NE2   . HIS A 1 104 ? 20.020 -20.760 23.047  1.00 70.81  ?  104 HIS A NE2   1 
ATOM   723  N N     . GLU A 1 105 ? 21.125 -18.046 18.506  1.00 75.00  ?  105 GLU A N     1 
ATOM   724  C CA    . GLU A 1 105 ? 20.811 -18.903 17.375  1.00 74.16  ?  105 GLU A CA    1 
ATOM   725  C C     . GLU A 1 105 ? 22.047 -19.282 16.587  1.00 74.09  ?  105 GLU A C     1 
ATOM   726  O O     . GLU A 1 105 ? 21.980 -20.208 15.773  1.00 73.01  ?  105 GLU A O     1 
ATOM   727  C CB    . GLU A 1 105 ? 19.808 -18.210 16.468  1.00 78.75  ?  105 GLU A CB    1 
ATOM   728  C CG    . GLU A 1 105 ? 18.490 -17.893 17.165  1.00 88.56  ?  105 GLU A CG    1 
ATOM   729  C CD    . GLU A 1 105 ? 17.447 -18.959 16.930  1.00 93.05  ?  105 GLU A CD    1 
ATOM   730  O OE1   . GLU A 1 105 ? 17.344 -19.405 15.766  1.00 94.80  ?  105 GLU A OE1   1 
ATOM   731  O OE2   . GLU A 1 105 ? 16.741 -19.348 17.901  1.00 96.36  -1 105 GLU A OE2   1 
ATOM   732  N N     . GLN A 1 106 ? 23.162 -18.589 16.805  1.00 73.19  ?  106 GLN A N     1 
ATOM   733  C CA    . GLN A 1 106 ? 24.423 -19.016 16.222  1.00 67.55  ?  106 GLN A CA    1 
ATOM   734  C C     . GLN A 1 106 ? 25.043 -20.124 17.045  1.00 67.20  ?  106 GLN A C     1 
ATOM   735  O O     . GLN A 1 106 ? 25.379 -21.189 16.507  1.00 63.83  ?  106 GLN A O     1 
ATOM   736  C CB    . GLN A 1 106 ? 25.398 -17.848 16.125  1.00 67.25  ?  106 GLN A CB    1 
ATOM   737  C CG    . GLN A 1 106 ? 25.065 -16.846 15.070  1.00 71.89  ?  106 GLN A CG    1 
ATOM   738  C CD    . GLN A 1 106 ? 26.248 -15.986 14.685  1.00 66.95  ?  106 GLN A CD    1 
ATOM   739  O OE1   . GLN A 1 106 ? 26.889 -15.361 15.534  1.00 72.56  ?  106 GLN A OE1   1 
ATOM   740  N NE2   . GLN A 1 106 ? 26.550 -15.952 13.398  1.00 64.62  ?  106 GLN A NE2   1 
ATOM   741  N N     . VAL A 1 107 ? 25.210 -19.888 18.351  1.00 64.95  ?  107 VAL A N     1 
ATOM   742  C CA    . VAL A 1 107 ? 25.914 -20.884 19.148  1.00 68.41  ?  107 VAL A CA    1 
ATOM   743  C C     . VAL A 1 107 ? 25.225 -22.242 19.013  1.00 69.18  ?  107 VAL A C     1 
ATOM   744  O O     . VAL A 1 107 ? 25.892 -23.288 19.006  1.00 64.23  ?  107 VAL A O     1 
ATOM   745  C CB    . VAL A 1 107 ? 26.052 -20.432 20.621  1.00 64.14  ?  107 VAL A CB    1 
ATOM   746  C CG1   . VAL A 1 107 ? 24.772 -19.912 21.127  1.00 65.09  ?  107 VAL A CG1   1 
ATOM   747  C CG2   . VAL A 1 107 ? 26.483 -21.597 21.482  1.00 60.66  ?  107 VAL A CG2   1 
ATOM   748  N N     . VAL A 1 108 ? 23.905 -22.244 18.798  1.00 66.62  ?  108 VAL A N     1 
ATOM   749  C CA    . VAL A 1 108 ? 23.177 -23.499 18.615  1.00 65.70  ?  108 VAL A CA    1 
ATOM   750  C C     . VAL A 1 108 ? 23.691 -24.248 17.391  1.00 67.54  ?  108 VAL A C     1 
ATOM   751  O O     . VAL A 1 108 ? 24.126 -25.403 17.475  1.00 68.96  ?  108 VAL A O     1 
ATOM   752  C CB    . VAL A 1 108 ? 21.669 -23.242 18.495  1.00 66.26  ?  108 VAL A CB    1 
ATOM   753  C CG1   . VAL A 1 108 ? 20.994 -24.535 18.106  1.00 62.16  ?  108 VAL A CG1   1 
ATOM   754  C CG2   . VAL A 1 108 ? 21.109 -22.709 19.793  1.00 63.05  ?  108 VAL A CG2   1 
ATOM   755  N N     . ARG A 1 109 ? 23.621 -23.609 16.226  1.00 73.84  ?  109 ARG A N     1 
ATOM   756  C CA    . ARG A 1 109 ? 24.024 -24.312 15.020  1.00 73.83  ?  109 ARG A CA    1 
ATOM   757  C C     . ARG A 1 109 ? 25.518 -24.528 14.980  1.00 70.92  ?  109 ARG A C     1 
ATOM   758  O O     . ARG A 1 109 ? 25.972 -25.421 14.264  1.00 72.63  ?  109 ARG A O     1 
ATOM   759  C CB    . ARG A 1 109 ? 23.513 -23.571 13.779  1.00 74.79  ?  109 ARG A CB    1 
ATOM   760  C CG    . ARG A 1 109 ? 21.995 -23.737 13.714  1.00 81.75  ?  109 ARG A CG    1 
ATOM   761  C CD    . ARG A 1 109 ? 21.250 -22.557 13.126  1.00 83.84  ?  109 ARG A CD    1 
ATOM   762  N NE    . ARG A 1 109 ? 21.583 -22.410 11.717  1.00 81.21  ?  109 ARG A NE    1 
ATOM   763  C CZ    . ARG A 1 109 ? 21.245 -23.276 10.768  1.00 83.86  ?  109 ARG A CZ    1 
ATOM   764  N NH1   . ARG A 1 109 ? 20.488 -24.340 11.027  1.00 82.13  ?  109 ARG A NH1   1 
ATOM   765  N NH2   . ARG A 1 109 ? 21.690 -23.083 9.528   1.00 77.68  ?  109 ARG A NH2   1 
ATOM   766  N N     . ALA A 1 110 ? 26.290 -23.766 15.755  1.00 66.94  ?  110 ALA A N     1 
ATOM   767  C CA    . ALA A 1 110 ? 27.708 -24.076 15.866  1.00 62.16  ?  110 ALA A CA    1 
ATOM   768  C C     . ALA A 1 110 ? 27.899 -25.460 16.476  1.00 62.74  ?  110 ALA A C     1 
ATOM   769  O O     . ALA A 1 110 ? 28.554 -26.327 15.889  1.00 60.98  ?  110 ALA A O     1 
ATOM   770  C CB    . ALA A 1 110 ? 28.426 -22.990 16.677  1.00 56.35  ?  110 ALA A CB    1 
ATOM   771  N N     . ASN A 1 111 ? 27.259 -25.706 17.616  1.00 58.46  ?  111 ASN A N     1 
ATOM   772  C CA    . ASN A 1 111 ? 27.390 -26.994 18.277  1.00 56.88  ?  111 ASN A CA    1 
ATOM   773  C C     . ASN A 1 111 ? 26.862 -28.135 17.419  1.00 61.35  ?  111 ASN A C     1 
ATOM   774  O O     . ASN A 1 111 ? 27.400 -29.248 17.455  1.00 58.21  ?  111 ASN A O     1 
ATOM   775  C CB    . ASN A 1 111 ? 26.673 -26.955 19.615  1.00 57.41  ?  111 ASN A CB    1 
ATOM   776  C CG    . ASN A 1 111 ? 27.611 -26.693 20.711  1.00 57.92  ?  111 ASN A CG    1 
ATOM   777  O OD1   . ASN A 1 111 ? 28.648 -27.360 20.808  1.00 63.55  ?  111 ASN A OD1   1 
ATOM   778  N ND2   . ASN A 1 111 ? 27.313 -25.701 21.523  1.00 53.97  ?  111 ASN A ND2   1 
ATOM   779  N N     . ALA A 1 112 ? 25.796 -27.892 16.656  1.00 62.04  ?  112 ALA A N     1 
ATOM   780  C CA    . ALA A 1 112 ? 25.279 -28.932 15.775  1.00 55.11  ?  112 ALA A CA    1 
ATOM   781  C C     . ALA A 1 112 ? 26.312 -29.333 14.722  1.00 58.87  ?  112 ALA A C     1 
ATOM   782  O O     . ALA A 1 112 ? 26.439 -30.511 14.379  1.00 59.43  ?  112 ALA A O     1 
ATOM   783  C CB    . ALA A 1 112 ? 23.992 -28.446 15.117  1.00 53.18  ?  112 ALA A CB    1 
ATOM   784  N N     . LEU A 1 113 ? 27.059 -28.362 14.204  1.00 54.74  ?  113 LEU A N     1 
ATOM   785  C CA    . LEU A 1 113 ? 28.103 -28.645 13.229  1.00 57.29  ?  113 LEU A CA    1 
ATOM   786  C C     . LEU A 1 113 ? 29.218 -29.482 13.843  1.00 58.77  ?  113 LEU A C     1 
ATOM   787  O O     . LEU A 1 113 ? 29.685 -30.460 13.241  1.00 59.25  ?  113 LEU A O     1 
ATOM   788  C CB    . LEU A 1 113 ? 28.654 -27.331 12.690  1.00 60.94  ?  113 LEU A CB    1 
ATOM   789  C CG    . LEU A 1 113 ? 29.560 -27.348 11.461  1.00 56.20  ?  113 LEU A CG    1 
ATOM   790  C CD1   . LEU A 1 113 ? 28.735 -27.235 10.203  1.00 59.38  ?  113 LEU A CD1   1 
ATOM   791  C CD2   . LEU A 1 113 ? 30.547 -26.221 11.564  1.00 49.87  ?  113 LEU A CD2   1 
ATOM   792  N N     . ALA A 1 114 ? 29.671 -29.113 15.044  1.00 57.30  ?  114 ALA A N     1 
ATOM   793  C CA    . ALA A 1 114 ? 30.671 -29.942 15.705  1.00 59.36  ?  114 ALA A CA    1 
ATOM   794  C C     . ALA A 1 114 ? 30.143 -31.352 15.930  1.00 57.42  ?  114 ALA A C     1 
ATOM   795  O O     . ALA A 1 114 ? 30.874 -32.331 15.731  1.00 55.48  ?  114 ALA A O     1 
ATOM   796  C CB    . ALA A 1 114 ? 31.116 -29.313 17.023  1.00 55.92  ?  114 ALA A CB    1 
ATOM   797  N N     . GLU A 1 115 ? 28.865 -31.476 16.308  1.00 58.91  ?  115 GLU A N     1 
ATOM   798  C CA    . GLU A 1 115 ? 28.247 -32.795 16.454  1.00 60.98  ?  115 GLU A CA    1 
ATOM   799  C C     . GLU A 1 115 ? 28.328 -33.589 15.147  1.00 60.12  ?  115 GLU A C     1 
ATOM   800  O O     . GLU A 1 115 ? 28.766 -34.750 15.133  1.00 62.54  ?  115 GLU A O     1 
ATOM   801  C CB    . GLU A 1 115 ? 26.784 -32.656 16.939  1.00 60.55  ?  115 GLU A CB    1 
ATOM   802  C CG    . GLU A 1 115 ? 26.636 -32.339 18.456  1.00 62.44  ?  115 GLU A CG    1 
ATOM   803  C CD    . GLU A 1 115 ? 25.193 -32.289 18.971  1.00 64.37  ?  115 GLU A CD    1 
ATOM   804  O OE1   . GLU A 1 115 ? 24.271 -32.663 18.215  1.00 65.80  ?  115 GLU A OE1   1 
ATOM   805  O OE2   . GLU A 1 115 ? 24.991 -31.866 20.139  1.00 65.93  -1 115 GLU A OE2   1 
ATOM   806  N N     . GLU A 1 116 ? 27.942 -32.977 14.027  1.00 57.88  ?  116 GLU A N     1 
ATOM   807  C CA    . GLU A 1 116 ? 27.916 -33.770 12.813  1.00 60.08  ?  116 GLU A CA    1 
ATOM   808  C C     . GLU A 1 116 ? 29.310 -34.162 12.373  1.00 59.66  ?  116 GLU A C     1 
ATOM   809  O O     . GLU A 1 116 ? 29.455 -35.116 11.614  1.00 63.94  ?  116 GLU A O     1 
ATOM   810  C CB    . GLU A 1 116 ? 27.201 -33.025 11.705  1.00 56.45  ?  116 GLU A CB    1 
ATOM   811  C CG    . GLU A 1 116 ? 25.926 -32.396 12.202  1.00 58.13  ?  116 GLU A CG    1 
ATOM   812  C CD    . GLU A 1 116 ? 24.834 -33.393 12.593  1.00 63.69  ?  116 GLU A CD    1 
ATOM   813  O OE1   . GLU A 1 116 ? 24.033 -33.761 11.711  1.00 60.47  ?  116 GLU A OE1   1 
ATOM   814  O OE2   . GLU A 1 116 ? 24.729 -33.772 13.785  1.00 69.56  -1 116 GLU A OE2   1 
ATOM   815  N N     . ALA A 1 117 ? 30.336 -33.486 12.858  1.00 57.50  ?  117 ALA A N     1 
ATOM   816  C CA    . ALA A 1 117 ? 31.696 -33.789 12.446  1.00 54.45  ?  117 ALA A CA    1 
ATOM   817  C C     . ALA A 1 117 ? 32.368 -34.880 13.286  1.00 61.75  ?  117 ALA A C     1 
ATOM   818  O O     . ALA A 1 117 ? 33.480 -35.306 12.957  1.00 60.13  ?  117 ALA A O     1 
ATOM   819  C CB    . ALA A 1 117 ? 32.525 -32.503 12.489  1.00 50.77  ?  117 ALA A CB    1 
ATOM   820  N N     . GLY A 1 118 ? 31.728 -35.370 14.341  1.00 58.42  ?  118 GLY A N     1 
ATOM   821  C CA    . GLY A 1 118 ? 32.450 -36.215 15.264  1.00 60.42  ?  118 GLY A CA    1 
ATOM   822  C C     . GLY A 1 118 ? 33.332 -35.436 16.192  1.00 60.66  ?  118 GLY A C     1 
ATOM   823  O O     . GLY A 1 118 ? 34.212 -36.023 16.840  1.00 61.79  ?  118 GLY A O     1 
ATOM   824  N N     . LEU A 1 119 ? 33.105 -34.122 16.281  1.00 54.89  ?  119 LEU A N     1 
ATOM   825  C CA    . LEU A 1 119 ? 33.980 -33.198 16.989  1.00 56.66  ?  119 LEU A CA    1 
ATOM   826  C C     . LEU A 1 119 ? 33.303 -32.505 18.154  1.00 61.67  ?  119 LEU A C     1 
ATOM   827  O O     . LEU A 1 119 ? 33.888 -31.574 18.726  1.00 57.22  ?  119 LEU A O     1 
ATOM   828  C CB    . LEU A 1 119 ? 34.514 -32.137 16.041  1.00 51.21  ?  119 LEU A CB    1 
ATOM   829  C CG    . LEU A 1 119 ? 35.592 -32.673 15.127  1.00 50.61  ?  119 LEU A CG    1 
ATOM   830  C CD1   . LEU A 1 119 ? 36.010 -31.569 14.224  1.00 50.01  ?  119 LEU A CD1   1 
ATOM   831  C CD2   . LEU A 1 119 ? 36.770 -33.215 15.928  1.00 50.91  ?  119 LEU A CD2   1 
ATOM   832  N N     . ALA A 1 120 ? 32.104 -32.948 18.541  1.00 62.88  ?  120 ALA A N     1 
ATOM   833  C CA    . ALA A 1 120 ? 31.389 -32.253 19.604  1.00 61.57  ?  120 ALA A CA    1 
ATOM   834  C C     . ALA A 1 120 ? 32.202 -32.220 20.895  1.00 61.63  ?  120 ALA A C     1 
ATOM   835  O O     . ALA A 1 120 ? 31.992 -31.347 21.747  1.00 62.33  ?  120 ALA A O     1 
ATOM   836  C CB    . ALA A 1 120 ? 30.035 -32.919 19.827  1.00 60.15  ?  120 ALA A CB    1 
ATOM   837  N N     . ASP A 1 121 ? 33.153 -33.121 21.035  1.00 59.21  ?  121 ASP A N     1 
ATOM   838  C CA    . ASP A 1 121 ? 34.004 -33.081 22.198  1.00 60.24  ?  121 ASP A CA    1 
ATOM   839  C C     . ASP A 1 121 ? 35.157 -32.112 22.039  1.00 62.39  ?  121 ASP A C     1 
ATOM   840  O O     . ASP A 1 121 ? 35.614 -31.569 23.044  1.00 69.14  ?  121 ASP A O     1 
ATOM   841  C CB    . ASP A 1 121 ? 34.528 -34.479 22.511  1.00 60.26  ?  121 ASP A CB    1 
ATOM   842  C CG    . ASP A 1 121 ? 35.103 -35.179 21.303  1.00 63.31  ?  121 ASP A CG    1 
ATOM   843  O OD1   . ASP A 1 121 ? 34.560 -35.064 20.177  1.00 67.95  ?  121 ASP A OD1   1 
ATOM   844  O OD2   . ASP A 1 121 ? 36.122 -35.866 21.498  1.00 62.63  -1 121 ASP A OD2   1 
ATOM   845  N N     . ARG A 1 122 ? 35.640 -31.858 20.822  1.00 60.78  ?  122 ARG A N     1 
ATOM   846  C CA    . ARG A 1 122 ? 36.813 -31.002 20.660  1.00 58.63  ?  122 ARG A CA    1 
ATOM   847  C C     . ARG A 1 122 ? 36.457 -29.616 20.117  1.00 54.27  ?  122 ARG A C     1 
ATOM   848  O O     . ARG A 1 122 ? 37.297 -28.718 20.145  1.00 51.43  ?  122 ARG A O     1 
ATOM   849  C CB    . ARG A 1 122 ? 37.880 -31.715 19.776  1.00 62.92  ?  122 ARG A CB    1 
ATOM   850  C CG    . ARG A 1 122 ? 38.897 -32.743 20.540  1.00 69.80  ?  122 ARG A CG    1 
ATOM   851  C CD    . ARG A 1 122 ? 39.431 -33.979 19.689  1.00 75.74  ?  122 ARG A CD    1 
ATOM   852  N NE    . ARG A 1 122 ? 38.560 -35.176 19.705  1.00 92.01  ?  122 ARG A NE    1 
ATOM   853  C CZ    . ARG A 1 122 ? 38.386 -36.049 18.702  1.00 88.47  ?  122 ARG A CZ    1 
ATOM   854  N NH1   . ARG A 1 122 ? 39.019 -35.916 17.546  1.00 86.46  ?  122 ARG A NH1   1 
ATOM   855  N NH2   . ARG A 1 122 ? 37.537 -37.073 18.857  1.00 68.75  ?  122 ARG A NH2   1 
ATOM   856  N N     . ALA A 1 123 ? 35.212 -29.397 19.706  1.00 56.70  ?  123 ALA A N     1 
ATOM   857  C CA    . ALA A 1 123 ? 34.738 -28.101 19.203  1.00 54.72  ?  123 ALA A CA    1 
ATOM   858  C C     . ALA A 1 123 ? 33.468 -27.748 19.961  1.00 59.22  ?  123 ALA A C     1 
ATOM   859  O O     . ALA A 1 123 ? 32.380 -28.186 19.573  1.00 59.60  ?  123 ALA A O     1 
ATOM   860  C CB    . ALA A 1 123 ? 34.438 -28.138 17.705  1.00 50.53  ?  123 ALA A CB    1 
ATOM   861  N N     . ARG A 1 124 ? 33.804 -26.830 21.062  1.00 60.30  ?  124 ARG A N     1 
ATOM   862  C CA    . ARG A 1 124 ? 32.709 -26.441 21.989  1.00 59.66  ?  124 ARG A CA    1 
ATOM   863  C C     . ARG A 1 124 ? 32.298 -24.985 21.752  1.00 60.38  ?  124 ARG A C     1 
ATOM   864  O O     . ARG A 1 124 ? 33.178 -24.176 21.464  1.00 61.99  ?  124 ARG A O     1 
ATOM   865  C CB    . ARG A 1 124 ? 33.131 -26.744 23.428  1.00 62.17  ?  124 ARG A CB    1 
ATOM   866  C CG    . ARG A 1 124 ? 33.232 -28.226 23.748  1.00 63.17  ?  124 ARG A CG    1 
ATOM   867  C CD    . ARG A 1 124 ? 33.335 -28.427 25.244  1.00 70.06  ?  124 ARG A CD    1 
ATOM   868  N NE    . ARG A 1 124 ? 34.542 -27.828 25.785  1.00 71.40  ?  124 ARG A NE    1 
ATOM   869  C CZ    . ARG A 1 124 ? 35.718 -28.437 25.826  1.00 73.40  ?  124 ARG A CZ    1 
ATOM   870  N NH1   . ARG A 1 124 ? 35.917 -29.532 25.118  1.00 69.44  ?  124 ARG A NH1   1 
ATOM   871  N NH2   . ARG A 1 124 ? 36.689 -27.949 26.578  1.00 78.84  ?  124 ARG A NH2   1 
ATOM   872  N N     . PHE A 1 125 ? 30.883 -24.734 21.784  1.00 58.07  ?  125 PHE A N     1 
ATOM   873  C CA    . PHE A 1 125 ? 30.453 -23.358 21.610  1.00 61.12  ?  125 PHE A CA    1 
ATOM   874  C C     . PHE A 1 125 ? 29.529 -22.954 22.740  1.00 60.31  ?  125 PHE A C     1 
ATOM   875  O O     . PHE A 1 125 ? 28.928 -23.804 23.402  1.00 70.59  ?  125 PHE A O     1 
ATOM   876  C CB    . PHE A 1 125 ? 29.733 -23.179 20.300  1.00 59.38  ?  125 PHE A CB    1 
ATOM   877  C CG    . PHE A 1 125 ? 30.573 -23.528 19.143  1.00 59.50  ?  125 PHE A CG    1 
ATOM   878  C CD1   . PHE A 1 125 ? 31.499 -22.627 18.660  1.00 62.03  ?  125 PHE A CD1   1 
ATOM   879  C CD2   . PHE A 1 125 ? 30.493 -24.775 18.569  1.00 58.21  ?  125 PHE A CD2   1 
ATOM   880  C CE1   . PHE A 1 125 ? 32.310 -22.944 17.586  1.00 62.28  ?  125 PHE A CE1   1 
ATOM   881  C CE2   . PHE A 1 125 ? 31.308 -25.106 17.496  1.00 58.58  ?  125 PHE A CE2   1 
ATOM   882  C CZ    . PHE A 1 125 ? 32.215 -24.185 17.003  1.00 59.52  ?  125 PHE A CZ    1 
ATOM   883  N N     . GLN A 1 126 ? 29.488 -21.636 22.976  1.00 58.30  ?  126 GLN A N     1 
ATOM   884  C CA    . GLN A 1 126 ? 28.664 -21.075 24.074  1.00 63.73  ?  126 GLN A CA    1 
ATOM   885  C C     . GLN A 1 126 ? 28.291 -19.627 23.762  1.00 62.08  ?  126 GLN A C     1 
ATOM   886  O O     . GLN A 1 126 ? 29.011 -18.990 22.990  1.00 62.39  ?  126 GLN A O     1 
ATOM   887  C CB    . GLN A 1 126 ? 29.434 -21.106 25.393  1.00 56.60  ?  126 GLN A CB    1 
ATOM   888  C CG    . GLN A 1 126 ? 30.581 -20.115 25.476  1.00 61.19  ?  126 GLN A CG    1 
ATOM   889  C CD    . GLN A 1 126 ? 31.460 -20.429 26.659  1.00 66.46  ?  126 GLN A CD    1 
ATOM   890  O OE1   . GLN A 1 126 ? 31.677 -19.596 27.535  1.00 75.28  ?  126 GLN A OE1   1 
ATOM   891  N NE2   . GLN A 1 126 ? 31.962 -21.651 26.699  1.00 64.80  ?  126 GLN A NE2   1 
ATOM   892  N N     . ARG A 1 127 ? 27.164 -19.155 24.285  1.00 63.51  ?  127 ARG A N     1 
ATOM   893  C CA    . ARG A 1 127 ? 26.772 -17.757 24.160  1.00 65.54  ?  127 ARG A CA    1 
ATOM   894  C C     . ARG A 1 127 ? 27.522 -16.910 25.189  1.00 66.74  ?  127 ARG A C     1 
ATOM   895  O O     . ARG A 1 127 ? 27.512 -17.241 26.379  1.00 66.96  ?  127 ARG A O     1 
ATOM   896  C CB    . ARG A 1 127 ? 25.261 -17.633 24.343  1.00 70.49  ?  127 ARG A CB    1 
ATOM   897  C CG    . ARG A 1 127 ? 24.758 -16.208 24.350  1.00 72.76  ?  127 ARG A CG    1 
ATOM   898  C CD    . ARG A 1 127 ? 24.004 -15.912 25.636  1.00 84.63  ?  127 ARG A CD    1 
ATOM   899  N NE    . ARG A 1 127 ? 22.625 -16.375 25.581  1.00 90.11  ?  127 ARG A NE    1 
ATOM   900  C CZ    . ARG A 1 127 ? 21.612 -15.649 25.127  1.00 94.50  ?  127 ARG A CZ    1 
ATOM   901  N NH1   . ARG A 1 127 ? 21.792 -14.413 24.683  1.00 93.05  ?  127 ARG A NH1   1 
ATOM   902  N NH2   . ARG A 1 127 ? 20.388 -16.176 25.116  1.00 96.26  ?  127 ARG A NH2   1 
ATOM   903  N N     . ALA A 1 128 ? 28.204 -15.846 24.737  1.00 63.52  ?  128 ALA A N     1 
ATOM   904  C CA    . ALA A 1 128 ? 29.013 -14.989 25.616  1.00 59.71  ?  128 ALA A CA    1 
ATOM   905  C C     . ALA A 1 128 ? 29.513 -13.765 24.862  1.00 70.00  ?  128 ALA A C     1 
ATOM   906  O O     . ALA A 1 128 ? 29.694 -13.795 23.642  1.00 71.91  ?  128 ALA A O     1 
ATOM   907  C CB    . ALA A 1 128 ? 30.217 -15.730 26.216  1.00 59.34  ?  128 ALA A CB    1 
ATOM   908  N N     . ASP A 1 129 ? 29.796 -12.707 25.625  1.00 73.31  ?  129 ASP A N     1 
ATOM   909  C CA    . ASP A 1 129 ? 30.250 -11.418 25.105  1.00 73.37  ?  129 ASP A CA    1 
ATOM   910  C C     . ASP A 1 129 ? 31.750 -11.281 25.317  1.00 76.63  ?  129 ASP A C     1 
ATOM   911  O O     . ASP A 1 129 ? 32.226 -11.382 26.451  1.00 78.37  ?  129 ASP A O     1 
ATOM   912  C CB    . ASP A 1 129 ? 29.537 -10.249 25.803  1.00 75.27  ?  129 ASP A CB    1 
ATOM   913  C CG    . ASP A 1 129 ? 29.737 -8.903  25.090  1.00 80.58  ?  129 ASP A CG    1 
ATOM   914  O OD1   . ASP A 1 129 ? 30.634 -8.770  24.236  1.00 82.32  ?  129 ASP A OD1   1 
ATOM   915  O OD2   . ASP A 1 129 ? 28.981 -7.960  25.387  1.00 85.99  -1 129 ASP A OD2   1 
ATOM   916  N N     . ALA A 1 130 ? 32.483 -11.003 24.233  1.00 75.69  ?  130 ALA A N     1 
ATOM   917  C CA    . ALA A 1 130 ? 33.930 -10.838 24.331  1.00 76.20  ?  130 ALA A CA    1 
ATOM   918  C C     . ALA A 1 130 ? 34.286 -9.781  25.354  1.00 76.13  ?  130 ALA A C     1 
ATOM   919  O O     . ALA A 1 130 ? 35.337 -9.859  25.999  1.00 77.71  ?  130 ALA A O     1 
ATOM   920  C CB    . ALA A 1 130 ? 34.506 -10.456 22.970  1.00 74.80  ?  130 ALA A CB    1 
ATOM   921  N N     . MET A 1 131 ? 33.410 -8.798  25.524  1.00 74.52  ?  131 MET A N     1 
ATOM   922  C CA    . MET A 1 131 ? 33.658 -7.745  26.481  1.00 78.62  ?  131 MET A CA    1 
ATOM   923  C C     . MET A 1 131 ? 33.806 -8.294  27.879  1.00 83.09  ?  131 MET A C     1 
ATOM   924  O O     . MET A 1 131 ? 34.501 -7.703  28.711  1.00 87.55  ?  131 MET A O     1 
ATOM   925  C CB    . MET A 1 131 ? 32.515 -6.745  26.463  1.00 81.45  ?  131 MET A CB    1 
ATOM   926  C CG    . MET A 1 131 ? 32.977 -5.335  26.798  1.00 92.68  ?  131 MET A CG    1 
ATOM   927  S SD    . MET A 1 131 ? 33.368 -4.407  25.300  1.00 84.37  ?  131 MET A SD    1 
ATOM   928  C CE    . MET A 1 131 ? 31.771 -4.621  24.542  1.00 84.29  ?  131 MET A CE    1 
ATOM   929  N N     . ASP A 1 132 ? 33.175 -9.419  28.165  1.00 82.22  ?  132 ASP A N     1 
ATOM   930  C CA    . ASP A 1 132 ? 33.283 -10.013 29.488  1.00 77.81  ?  132 ASP A CA    1 
ATOM   931  C C     . ASP A 1 132 ? 33.424 -11.517 29.266  1.00 78.98  ?  132 ASP A C     1 
ATOM   932  O O     . ASP A 1 132 ? 32.426 -12.235 29.092  1.00 77.97  ?  132 ASP A O     1 
ATOM   933  C CB    . ASP A 1 132 ? 32.075 -9.647  30.333  1.00 84.71  ?  132 ASP A CB    1 
ATOM   934  C CG    . ASP A 1 132 ? 32.377 -9.678  31.801  1.00 90.01  ?  132 ASP A CG    1 
ATOM   935  O OD1   . ASP A 1 132 ? 33.536 -9.999  32.159  1.00 87.19  ?  132 ASP A OD1   1 
ATOM   936  O OD2   . ASP A 1 132 ? 31.443 -9.382  32.580  1.00 91.97  -1 132 ASP A OD2   1 
ATOM   937  N N     . LEU A 1 133 ? 34.672 -11.981 29.227  1.00 77.92  ?  133 LEU A N     1 
ATOM   938  C CA    . LEU A 1 133 ? 34.932 -13.369 28.885  1.00 75.29  ?  133 LEU A CA    1 
ATOM   939  C C     . LEU A 1 133 ? 34.681 -14.234 30.113  1.00 75.28  ?  133 LEU A C     1 
ATOM   940  O O     . LEU A 1 133 ? 35.363 -14.065 31.130  1.00 77.39  ?  133 LEU A O     1 
ATOM   941  C CB    . LEU A 1 133 ? 36.363 -13.556 28.375  1.00 71.87  ?  133 LEU A CB    1 
ATOM   942  C CG    . LEU A 1 133 ? 36.749 -13.106 26.962  1.00 74.60  ?  133 LEU A CG    1 
ATOM   943  C CD1   . LEU A 1 133 ? 38.234 -13.425 26.722  1.00 72.10  ?  133 LEU A CD1   1 
ATOM   944  C CD2   . LEU A 1 133 ? 35.837 -13.716 25.881  1.00 73.03  ?  133 LEU A CD2   1 
ATOM   945  N N     . PRO A 1 134 ? 33.738 -15.141 30.072  1.00 74.26  ?  134 PRO A N     1 
ATOM   946  C CA    . PRO A 1 134 ? 33.544 -16.057 31.202  1.00 69.85  ?  134 PRO A CA    1 
ATOM   947  C C     . PRO A 1 134 ? 34.617 -17.126 31.289  1.00 71.28  ?  134 PRO A C     1 
ATOM   948  O O     . PRO A 1 134 ? 34.307 -18.305 31.132  1.00 79.36  ?  134 PRO A O     1 
ATOM   949  C CB    . PRO A 1 134 ? 32.185 -16.690 30.894  1.00 69.10  ?  134 PRO A CB    1 
ATOM   950  C CG    . PRO A 1 134 ? 32.094 -16.633 29.395  1.00 73.90  ?  134 PRO A CG    1 
ATOM   951  C CD    . PRO A 1 134 ? 32.736 -15.331 29.010  1.00 70.26  ?  134 PRO A CD    1 
ATOM   952  N N     . PHE A 1 135 ? 35.872 -16.771 31.516  1.00 74.30  ?  135 PHE A N     1 
ATOM   953  C CA    . PHE A 1 135 ? 36.930 -17.758 31.365  1.00 78.04  ?  135 PHE A CA    1 
ATOM   954  C C     . PHE A 1 135 ? 38.034 -17.413 32.346  1.00 72.60  ?  135 PHE A C     1 
ATOM   955  O O     . PHE A 1 135 ? 38.311 -16.238 32.609  1.00 70.62  ?  135 PHE A O     1 
ATOM   956  C CB    . PHE A 1 135 ? 37.511 -17.813 29.921  1.00 72.80  ?  135 PHE A CB    1 
ATOM   957  C CG    . PHE A 1 135 ? 36.551 -18.358 28.854  1.00 70.73  ?  135 PHE A CG    1 
ATOM   958  C CD1   . PHE A 1 135 ? 36.321 -19.720 28.725  1.00 70.25  ?  135 PHE A CD1   1 
ATOM   959  C CD2   . PHE A 1 135 ? 35.917 -17.503 27.953  1.00 72.48  ?  135 PHE A CD2   1 
ATOM   960  C CE1   . PHE A 1 135 ? 35.452 -20.217 27.746  1.00 66.95  ?  135 PHE A CE1   1 
ATOM   961  C CE2   . PHE A 1 135 ? 35.046 -17.996 26.978  1.00 68.81  ?  135 PHE A CE2   1 
ATOM   962  C CZ    . PHE A 1 135 ? 34.822 -19.353 26.878  1.00 63.20  ?  135 PHE A CZ    1 
ATOM   963  N N     . GLU A 1 136 ? 38.682 -18.442 32.864  1.00 74.55  ?  136 GLU A N     1 
ATOM   964  C CA    . GLU A 1 136 ? 39.736 -18.195 33.829  1.00 77.36  ?  136 GLU A CA    1 
ATOM   965  C C     . GLU A 1 136 ? 40.912 -17.484 33.171  1.00 75.07  ?  136 GLU A C     1 
ATOM   966  O O     . GLU A 1 136 ? 41.167 -17.630 31.974  1.00 81.36  ?  136 GLU A O     1 
ATOM   967  C CB    . GLU A 1 136 ? 40.199 -19.502 34.468  1.00 83.52  ?  136 GLU A CB    1 
ATOM   968  C CG    . GLU A 1 136 ? 40.391 -19.363 35.987  1.00 99.95  ?  136 GLU A CG    1 
ATOM   969  C CD    . GLU A 1 136 ? 40.034 -20.626 36.769  1.00 114.40 ?  136 GLU A CD    1 
ATOM   970  O OE1   . GLU A 1 136 ? 38.846 -20.776 37.150  1.00 117.12 ?  136 GLU A OE1   1 
ATOM   971  O OE2   . GLU A 1 136 ? 40.940 -21.466 37.008  1.00 122.94 -1 136 GLU A OE2   1 
ATOM   972  N N     . ASP A 1 137 ? 41.623 -16.690 33.971  1.00 74.72  ?  137 ASP A N     1 
ATOM   973  C CA    . ASP A 1 137 ? 42.859 -16.080 33.505  1.00 77.05  ?  137 ASP A CA    1 
ATOM   974  C C     . ASP A 1 137 ? 43.810 -17.157 33.005  1.00 74.93  ?  137 ASP A C     1 
ATOM   975  O O     . ASP A 1 137 ? 43.896 -18.243 33.580  1.00 75.24  ?  137 ASP A O     1 
ATOM   976  C CB    . ASP A 1 137 ? 43.534 -15.296 34.635  1.00 79.64  ?  137 ASP A CB    1 
ATOM   977  C CG    . ASP A 1 137 ? 42.709 -14.103 35.124  1.00 82.66  ?  137 ASP A CG    1 
ATOM   978  O OD1   . ASP A 1 137 ? 41.550 -13.939 34.657  1.00 82.71  ?  137 ASP A OD1   1 
ATOM   979  O OD2   . ASP A 1 137 ? 43.238 -13.334 35.979  1.00 86.31  -1 137 ASP A OD2   1 
ATOM   980  N N     . GLU A 1 138 ? 44.509 -16.856 31.910  1.00 76.60  ?  138 GLU A N     1 
ATOM   981  C CA    . GLU A 1 138 ? 45.587 -17.709 31.395  1.00 77.74  ?  138 GLU A CA    1 
ATOM   982  C C     . GLU A 1 138 ? 45.091 -19.097 30.991  1.00 78.35  ?  138 GLU A C     1 
ATOM   983  O O     . GLU A 1 138 ? 45.739 -20.116 31.265  1.00 79.66  ?  138 GLU A O     1 
ATOM   984  C CB    . GLU A 1 138 ? 46.729 -17.821 32.414  1.00 77.52  ?  138 GLU A CB    1 
ATOM   985  C CG    . GLU A 1 138 ? 47.367 -16.486 32.756  1.00 77.51  ?  138 GLU A CG    1 
ATOM   986  C CD    . GLU A 1 138 ? 48.754 -16.621 33.356  1.00 81.29  ?  138 GLU A CD    1 
ATOM   987  O OE1   . GLU A 1 138 ? 49.242 -17.763 33.558  1.00 79.47  ?  138 GLU A OE1   1 
ATOM   988  O OE2   . GLU A 1 138 ? 49.355 -15.559 33.623  1.00 82.96  -1 138 GLU A OE2   1 
ATOM   989  N N     . SER A 1 139 ? 43.938 -19.144 30.330  1.00 73.30  ?  139 SER A N     1 
ATOM   990  C CA    . SER A 1 139 ? 43.288 -20.411 30.044  1.00 70.93  ?  139 SER A CA    1 
ATOM   991  C C     . SER A 1 139 ? 43.479 -20.879 28.620  1.00 73.49  ?  139 SER A C     1 
ATOM   992  O O     . SER A 1 139 ? 43.218 -22.052 28.342  1.00 77.90  ?  139 SER A O     1 
ATOM   993  C CB    . SER A 1 139 ? 41.790 -20.305 30.316  1.00 72.80  ?  139 SER A CB    1 
ATOM   994  O OG    . SER A 1 139 ? 41.208 -19.350 29.450  1.00 78.16  ?  139 SER A OG    1 
ATOM   995  N N     . PHE A 1 140 ? 43.906 -20.001 27.718  1.00 74.42  ?  140 PHE A N     1 
ATOM   996  C CA    . PHE A 1 140 ? 43.912 -20.279 26.289  1.00 69.39  ?  140 PHE A CA    1 
ATOM   997  C C     . PHE A 1 140 ? 45.311 -20.122 25.718  1.00 66.74  ?  140 PHE A C     1 
ATOM   998  O O     . PHE A 1 140 ? 45.994 -19.129 25.998  1.00 67.15  ?  140 PHE A O     1 
ATOM   999  C CB    . PHE A 1 140 ? 42.962 -19.356 25.562  1.00 67.17  ?  140 PHE A CB    1 
ATOM   1000 C CG    . PHE A 1 140 ? 41.573 -19.815 25.615  1.00 69.08  ?  140 PHE A CG    1 
ATOM   1001 C CD1   . PHE A 1 140 ? 41.184 -20.922 24.882  1.00 66.52  ?  140 PHE A CD1   1 
ATOM   1002 C CD2   . PHE A 1 140 ? 40.646 -19.159 26.408  1.00 67.55  ?  140 PHE A CD2   1 
ATOM   1003 C CE1   . PHE A 1 140 ? 39.875 -21.364 24.922  1.00 65.82  ?  140 PHE A CE1   1 
ATOM   1004 C CE2   . PHE A 1 140 ? 39.330 -19.587 26.467  1.00 64.18  ?  140 PHE A CE2   1 
ATOM   1005 C CZ    . PHE A 1 140 ? 38.941 -20.691 25.725  1.00 67.25  ?  140 PHE A CZ    1 
ATOM   1006 N N     . ASP A 1 141 ? 45.728 -21.095 24.897  1.00 67.24  ?  141 ASP A N     1 
ATOM   1007 C CA    . ASP A 1 141 ? 46.988 -20.968 24.175  1.00 65.17  ?  141 ASP A CA    1 
ATOM   1008 C C     . ASP A 1 141 ? 46.890 -19.959 23.025  1.00 62.12  ?  141 ASP A C     1 
ATOM   1009 O O     . ASP A 1 141 ? 47.922 -19.550 22.487  1.00 67.95  ?  141 ASP A O     1 
ATOM   1010 C CB    . ASP A 1 141 ? 47.433 -22.333 23.636  1.00 60.12  ?  141 ASP A CB    1 
ATOM   1011 C CG    . ASP A 1 141 ? 47.561 -23.411 24.719  1.00 63.46  ?  141 ASP A CG    1 
ATOM   1012 O OD1   . ASP A 1 141 ? 48.403 -23.280 25.625  1.00 68.42  ?  141 ASP A OD1   1 
ATOM   1013 O OD2   . ASP A 1 141 ? 46.845 -24.430 24.631  1.00 66.45  -1 141 ASP A OD2   1 
ATOM   1014 N N     . ALA A 1 142 ? 45.682 -19.548 22.633  1.00 63.69  ?  142 ALA A N     1 
ATOM   1015 C CA    . ALA A 1 142 ? 45.523 -18.661 21.483  1.00 63.00  ?  142 ALA A CA    1 
ATOM   1016 C C     . ALA A 1 142 ? 44.071 -18.239 21.299  1.00 62.44  ?  142 ALA A C     1 
ATOM   1017 O O     . ALA A 1 142 ? 43.137 -18.939 21.703  1.00 64.59  ?  142 ALA A O     1 
ATOM   1018 C CB    . ALA A 1 142 ? 46.034 -19.326 20.199  1.00 63.55  ?  142 ALA A CB    1 
ATOM   1019 N N     . VAL A 1 143 ? 43.874 -17.089 20.686  1.00 59.29  ?  143 VAL A N     1 
ATOM   1020 C CA    . VAL A 1 143 ? 42.548 -16.549 20.474  1.00 57.30  ?  143 VAL A CA    1 
ATOM   1021 C C     . VAL A 1 143 ? 42.518 -16.055 19.052  1.00 60.74  ?  143 VAL A C     1 
ATOM   1022 O O     . VAL A 1 143 ? 43.472 -15.417 18.597  1.00 67.64  ?  143 VAL A O     1 
ATOM   1023 C CB    . VAL A 1 143 ? 42.239 -15.395 21.437  1.00 58.56  ?  143 VAL A CB    1 
ATOM   1024 C CG1   . VAL A 1 143 ? 40.788 -14.997 21.331  1.00 64.26  ?  143 VAL A CG1   1 
ATOM   1025 C CG2   . VAL A 1 143 ? 42.585 -15.784 22.839  1.00 60.54  ?  143 VAL A CG2   1 
ATOM   1026 N N     . ILE A 1 144 ? 41.447 -16.339 18.348  1.00 56.05  ?  144 ILE A N     1 
ATOM   1027 C CA    . ILE A 1 144 ? 41.290 -15.839 16.998  1.00 61.43  ?  144 ILE A CA    1 
ATOM   1028 C C     . ILE A 1 144 ? 39.986 -15.062 16.945  1.00 68.11  ?  144 ILE A C     1 
ATOM   1029 O O     . ILE A 1 144 ? 38.975 -15.479 17.530  1.00 67.87  ?  144 ILE A O     1 
ATOM   1030 C CB    . ILE A 1 144 ? 41.353 -16.993 15.969  1.00 62.75  ?  144 ILE A CB    1 
ATOM   1031 C CG1   . ILE A 1 144 ? 40.811 -16.598 14.587  1.00 63.47  ?  144 ILE A CG1   1 
ATOM   1032 C CG2   . ILE A 1 144 ? 40.635 -18.195 16.480  1.00 59.43  ?  144 ILE A CG2   1 
ATOM   1033 C CD1   . ILE A 1 144 ? 41.024 -17.675 13.543  1.00 54.48  ?  144 ILE A CD1   1 
ATOM   1034 N N     . ALA A 1 145 ? 40.031 -13.898 16.286  1.00 68.42  ?  145 ALA A N     1 
ATOM   1035 C CA    . ALA A 1 145 ? 38.884 -13.002 16.151  1.00 68.78  ?  145 ALA A CA    1 
ATOM   1036 C C     . ALA A 1 145 ? 38.639 -12.766 14.661  1.00 66.64  ?  145 ALA A C     1 
ATOM   1037 O O     . ALA A 1 145 ? 38.954 -11.714 14.083  1.00 66.29  ?  145 ALA A O     1 
ATOM   1038 C CB    . ALA A 1 145 ? 39.127 -11.703 16.916  1.00 65.33  ?  145 ALA A CB    1 
ATOM   1039 N N     . LEU A 1 146 ? 38.228 -13.722 13.981  1.00 57.72  ?  146 LEU A N     1 
ATOM   1040 C CA    . LEU A 1 146 ? 37.988 -13.636 12.527  1.00 63.47  ?  146 LEU A CA    1 
ATOM   1041 C C     . LEU A 1 146 ? 36.742 -12.795 12.310  1.00 64.65  ?  146 LEU A C     1 
ATOM   1042 O O     . LEU A 1 146 ? 35.651 -13.249 12.674  1.00 62.66  ?  146 LEU A O     1 
ATOM   1043 C CB    . LEU A 1 146 ? 37.756 -15.064 12.027  1.00 60.10  ?  146 LEU A CB    1 
ATOM   1044 C CG    . LEU A 1 146 ? 37.411 -15.267 10.552  1.00 60.14  ?  146 LEU A CG    1 
ATOM   1045 C CD1   . LEU A 1 146 ? 38.529 -14.816 9.626   1.00 56.48  ?  146 LEU A CD1   1 
ATOM   1046 C CD2   . LEU A 1 146 ? 37.056 -16.719 10.286  1.00 59.61  ?  146 LEU A CD2   1 
ATOM   1047 N N     . GLU A 1 147 ? 36.838 -11.710 11.780  1.00 66.29  ?  147 GLU A N     1 
ATOM   1048 C CA    . GLU A 1 147 ? 35.791 -10.755 11.441  1.00 66.74  ?  147 GLU A CA    1 
ATOM   1049 C C     . GLU A 1 147 ? 34.835 -10.542 12.610  1.00 66.48  ?  147 GLU A C     1 
ATOM   1050 O O     . GLU A 1 147 ? 33.624 -10.402 12.447  1.00 67.63  ?  147 GLU A O     1 
ATOM   1051 C CB    . GLU A 1 147 ? 35.041 -11.193 10.196  1.00 61.06  ?  147 GLU A CB    1 
ATOM   1052 C CG    . GLU A 1 147 ? 35.601 -10.573 8.976   1.00 61.46  ?  147 GLU A CG    1 
ATOM   1053 C CD    . GLU A 1 147 ? 34.713 -10.734 7.734   1.00 65.14  ?  147 GLU A CD    1 
ATOM   1054 O OE1   . GLU A 1 147 ? 33.438 -10.781 7.831   1.00 72.07  ?  147 GLU A OE1   1 
ATOM   1055 O OE2   . GLU A 1 147 ? 35.323 -10.814 6.644   1.00 62.42  -1 147 GLU A OE2   1 
ATOM   1056 N N     . SER A 1 148 ? 35.377 -10.520 13.813  1.00 65.04  ?  148 SER A N     1 
ATOM   1057 C CA    . SER A 1 148 ? 34.505 -10.330 14.949  1.00 69.31  ?  148 SER A CA    1 
ATOM   1058 C C     . SER A 1 148 ? 34.707 -8.974  15.595  1.00 71.52  ?  148 SER A C     1 
ATOM   1059 O O     . SER A 1 148 ? 33.722 -8.255  15.781  1.00 70.27  ?  148 SER A O     1 
ATOM   1060 C CB    . SER A 1 148 ? 34.731 -11.458 15.953  1.00 68.68  ?  148 SER A CB    1 
ATOM   1061 O OG    . SER A 1 148 ? 36.123 -11.693 16.086  1.00 71.12  ?  148 SER A OG    1 
ATOM   1062 N N     . ILE A 1 149 ? 35.961 -8.569  15.861  1.00 70.83  ?  149 ILE A N     1 
ATOM   1063 C CA    . ILE A 1 149 ? 36.225 -7.384  16.684  1.00 70.31  ?  149 ILE A CA    1 
ATOM   1064 C C     . ILE A 1 149 ? 35.514 -6.163  16.141  1.00 70.79  ?  149 ILE A C     1 
ATOM   1065 O O     . ILE A 1 149 ? 35.289 -5.196  16.877  1.00 72.82  ?  149 ILE A O     1 
ATOM   1066 C CB    . ILE A 1 149 ? 37.734 -7.087  16.800  1.00 73.82  ?  149 ILE A CB    1 
ATOM   1067 C CG1   . ILE A 1 149 ? 38.054 -6.478  18.168  1.00 66.39  ?  149 ILE A CG1   1 
ATOM   1068 C CG2   . ILE A 1 149 ? 38.152 -6.107  15.726  1.00 66.67  ?  149 ILE A CG2   1 
ATOM   1069 C CD1   . ILE A 1 149 ? 39.539 -6.314  18.472  1.00 62.43  ?  149 ILE A CD1   1 
ATOM   1070 N N     . ILE A 1 150 ? 35.128 -6.204  14.868  1.00 68.86  ?  150 ILE A N     1 
ATOM   1071 C CA    . ILE A 1 150 ? 34.511 -5.062  14.214  1.00 71.77  ?  150 ILE A CA    1 
ATOM   1072 C C     . ILE A 1 150 ? 33.138 -4.756  14.803  1.00 73.25  ?  150 ILE A C     1 
ATOM   1073 O O     . ILE A 1 150 ? 32.738 -3.588  14.919  1.00 77.27  ?  150 ILE A O     1 
ATOM   1074 C CB    . ILE A 1 150 ? 34.444 -5.348  12.709  1.00 71.10  ?  150 ILE A CB    1 
ATOM   1075 C CG1   . ILE A 1 150 ? 33.698 -6.651  12.458  1.00 67.89  ?  150 ILE A CG1   1 
ATOM   1076 C CG2   . ILE A 1 150 ? 35.844 -5.491  12.163  1.00 65.63  ?  150 ILE A CG2   1 
ATOM   1077 C CD1   . ILE A 1 150 ? 33.612 -7.002  11.020  1.00 68.39  ?  150 ILE A CD1   1 
ATOM   1078 N N     . HIS A 1 151 ? 32.388 -5.790  15.159  1.00 75.21  ?  151 HIS A N     1 
ATOM   1079 C CA    . HIS A 1 151 ? 31.088 -5.612  15.771  1.00 76.48  ?  151 HIS A CA    1 
ATOM   1080 C C     . HIS A 1 151 ? 31.181 -5.200  17.230  1.00 78.35  ?  151 HIS A C     1 
ATOM   1081 O O     . HIS A 1 151 ? 30.152 -4.880  17.834  1.00 86.99  ?  151 HIS A O     1 
ATOM   1082 C CB    . HIS A 1 151 ? 30.293 -6.912  15.716  1.00 73.71  ?  151 HIS A CB    1 
ATOM   1083 C CG    . HIS A 1 151 ? 29.998 -7.428  14.339  1.00 77.27  ?  151 HIS A CG    1 
ATOM   1084 N ND1   . HIS A 1 151 ? 29.127 -6.798  13.476  1.00 75.27  ?  151 HIS A ND1   1 
ATOM   1085 C CD2   . HIS A 1 151 ? 30.381 -8.570  13.718  1.00 76.04  ?  151 HIS A CD2   1 
ATOM   1086 C CE1   . HIS A 1 151 ? 29.016 -7.509  12.365  1.00 70.30  ?  151 HIS A CE1   1 
ATOM   1087 N NE2   . HIS A 1 151 ? 29.762 -8.591  12.489  1.00 73.02  ?  151 HIS A NE2   1 
ATOM   1088 N N     . MET A 1 152 ? 32.352 -5.261  17.824  1.00 75.67  ?  152 MET A N     1 
ATOM   1089 C CA    . MET A 1 152 ? 32.312 -5.148  19.267  1.00 80.04  ?  152 MET A CA    1 
ATOM   1090 C C     . MET A 1 152 ? 32.352 -3.687  19.697  1.00 85.17  ?  152 MET A C     1 
ATOM   1091 O O     . MET A 1 152 ? 32.844 -2.825  18.958  1.00 86.88  ?  152 MET A O     1 
ATOM   1092 C CB    . MET A 1 152 ? 33.456 -5.925  19.894  1.00 78.13  ?  152 MET A CB    1 
ATOM   1093 C CG    . MET A 1 152 ? 33.301 -7.404  19.628  1.00 77.76  ?  152 MET A CG    1 
ATOM   1094 S SD    . MET A 1 152 ? 34.701 -8.417  20.094  1.00 74.32  ?  152 MET A SD    1 
ATOM   1095 C CE    . MET A 1 152 ? 34.088 -9.977  19.492  1.00 72.28  ?  152 MET A CE    1 
ATOM   1096 N N     . PRO A 1 153 ? 31.787 -3.390  20.869  1.00 86.42  ?  153 PRO A N     1 
ATOM   1097 C CA    . PRO A 1 153 ? 31.676 -1.988  21.310  1.00 84.26  ?  153 PRO A CA    1 
ATOM   1098 C C     . PRO A 1 153 ? 32.983 -1.345  21.749  1.00 86.90  ?  153 PRO A C     1 
ATOM   1099 O O     . PRO A 1 153 ? 33.061 -0.114  21.749  1.00 90.03  ?  153 PRO A O     1 
ATOM   1100 C CB    . PRO A 1 153 ? 30.686 -2.064  22.475  1.00 83.70  ?  153 PRO A CB    1 
ATOM   1101 C CG    . PRO A 1 153 ? 29.841 -3.277  22.155  1.00 85.11  ?  153 PRO A CG    1 
ATOM   1102 C CD    . PRO A 1 153 ? 30.771 -4.259  21.493  1.00 87.83  ?  153 PRO A CD    1 
ATOM   1103 N N     . ASP A 1 154 ? 34.011 -2.096  22.124  1.00 87.81  ?  154 ASP A N     1 
ATOM   1104 C CA    . ASP A 1 154 ? 35.244 -1.445  22.557  1.00 85.73  ?  154 ASP A CA    1 
ATOM   1105 C C     . ASP A 1 154 ? 36.421 -2.383  22.337  1.00 82.30  ?  154 ASP A C     1 
ATOM   1106 O O     . ASP A 1 154 ? 36.505 -3.438  22.975  1.00 81.23  ?  154 ASP A O     1 
ATOM   1107 C CB    . ASP A 1 154 ? 35.141 -1.035  24.032  1.00 84.94  ?  154 ASP A CB    1 
ATOM   1108 C CG    . ASP A 1 154 ? 36.446 -0.472  24.584  1.00 84.57  ?  154 ASP A CG    1 
ATOM   1109 O OD1   . ASP A 1 154 ? 36.750 0.694   24.279  1.00 85.89  ?  154 ASP A OD1   1 
ATOM   1110 O OD2   . ASP A 1 154 ? 37.170 -1.181  25.314  1.00 85.05  -1 154 ASP A OD2   1 
ATOM   1111 N N     . ARG A 1 155 ? 37.339 -2.002  21.452  1.00 75.83  ?  155 ARG A N     1 
ATOM   1112 C CA    . ARG A 1 155 ? 38.493 -2.863  21.231  1.00 74.12  ?  155 ARG A CA    1 
ATOM   1113 C C     . ARG A 1 155 ? 39.418 -2.886  22.443  1.00 77.93  ?  155 ARG A C     1 
ATOM   1114 O O     . ARG A 1 155 ? 39.879 -3.957  22.851  1.00 78.30  ?  155 ARG A O     1 
ATOM   1115 C CB    . ARG A 1 155 ? 39.219 -2.425  19.971  1.00 71.61  ?  155 ARG A CB    1 
ATOM   1116 C CG    . ARG A 1 155 ? 38.341 -2.632  18.752  1.00 73.56  ?  155 ARG A CG    1 
ATOM   1117 C CD    . ARG A 1 155 ? 39.037 -2.204  17.505  1.00 71.66  ?  155 ARG A CD    1 
ATOM   1118 N NE    . ARG A 1 155 ? 38.226 -2.357  16.308  1.00 69.82  ?  155 ARG A NE    1 
ATOM   1119 C CZ    . ARG A 1 155 ? 37.121 -1.670  16.047  1.00 74.46  ?  155 ARG A CZ    1 
ATOM   1120 N NH1   . ARG A 1 155 ? 36.533 -0.918  16.971  1.00 74.00  ?  155 ARG A NH1   1 
ATOM   1121 N NH2   . ARG A 1 155 ? 36.599 -1.732  14.826  1.00 76.63  ?  155 ARG A NH2   1 
ATOM   1122 N N     . ALA A 1 156 ? 39.659 -1.733  23.067  1.00 76.96  ?  156 ALA A N     1 
ATOM   1123 C CA    . ALA A 1 156 ? 40.614 -1.680  24.167  1.00 74.42  ?  156 ALA A CA    1 
ATOM   1124 C C     . ALA A 1 156 ? 40.192 -2.537  25.362  1.00 75.08  ?  156 ALA A C     1 
ATOM   1125 O O     . ALA A 1 156 ? 41.039 -2.867  26.204  1.00 77.70  ?  156 ALA A O     1 
ATOM   1126 C CB    . ALA A 1 156 ? 40.816 -0.228  24.580  1.00 73.26  ?  156 ALA A CB    1 
ATOM   1127 N N     . GLN A 1 157 ? 38.908 -2.892  25.468  1.00 76.05  ?  157 GLN A N     1 
ATOM   1128 C CA    . GLN A 1 157 ? 38.449 -3.799  26.519  1.00 77.37  ?  157 GLN A CA    1 
ATOM   1129 C C     . GLN A 1 157 ? 38.455 -5.250  26.044  1.00 80.10  ?  157 GLN A C     1 
ATOM   1130 O O     . GLN A 1 157 ? 38.979 -6.136  26.734  1.00 80.62  ?  157 GLN A O     1 
ATOM   1131 C CB    . GLN A 1 157 ? 37.036 -3.417  27.003  1.00 79.33  ?  157 GLN A CB    1 
ATOM   1132 C CG    . GLN A 1 157 ? 36.542 -4.226  28.234  1.00 84.38  ?  157 GLN A CG    1 
ATOM   1133 C CD    . GLN A 1 157 ? 35.135 -3.858  28.715  1.00 87.01  ?  157 GLN A CD    1 
ATOM   1134 O OE1   . GLN A 1 157 ? 34.606 -2.815  28.367  1.00 94.91  ?  157 GLN A OE1   1 
ATOM   1135 N NE2   . GLN A 1 157 ? 34.532 -4.727  29.521  1.00 83.74  ?  157 GLN A NE2   1 
ATOM   1136 N N     . VAL A 1 158 ? 37.867 -5.513  24.871  1.00 76.78  ?  158 VAL A N     1 
ATOM   1137 C CA    . VAL A 1 158 ? 37.972 -6.850  24.295  1.00 74.64  ?  158 VAL A CA    1 
ATOM   1138 C C     . VAL A 1 158 ? 39.440 -7.270  24.273  1.00 74.10  ?  158 VAL A C     1 
ATOM   1139 O O     . VAL A 1 158 ? 39.789 -8.377  24.702  1.00 71.99  ?  158 VAL A O     1 
ATOM   1140 C CB    . VAL A 1 158 ? 37.320 -6.895  22.890  1.00 78.82  ?  158 VAL A CB    1 
ATOM   1141 C CG1   . VAL A 1 158 ? 37.478 -8.252  22.251  1.00 75.28  ?  158 VAL A CG1   1 
ATOM   1142 C CG2   . VAL A 1 158 ? 35.834 -6.560  22.950  1.00 76.78  ?  158 VAL A CG2   1 
ATOM   1143 N N     . LEU A 1 159 ? 40.336 -6.361  23.860  1.00 74.23  ?  159 LEU A N     1 
ATOM   1144 C CA    . LEU A 1 159 ? 41.761 -6.694  23.849  1.00 76.14  ?  159 LEU A CA    1 
ATOM   1145 C C     . LEU A 1 159 ? 42.264 -6.984  25.256  1.00 71.60  ?  159 LEU A C     1 
ATOM   1146 O O     . LEU A 1 159 ? 42.946 -7.989  25.494  1.00 72.77  ?  159 LEU A O     1 
ATOM   1147 C CB    . LEU A 1 159 ? 42.571 -5.572  23.196  1.00 71.72  ?  159 LEU A CB    1 
ATOM   1148 C CG    . LEU A 1 159 ? 42.288 -5.441  21.692  1.00 67.92  ?  159 LEU A CG    1 
ATOM   1149 C CD1   . LEU A 1 159 ? 42.832 -4.153  21.199  1.00 72.06  ?  159 LEU A CD1   1 
ATOM   1150 C CD2   . LEU A 1 159 ? 42.858 -6.569  20.877  1.00 62.62  ?  159 LEU A CD2   1 
ATOM   1151 N N     . ALA A 1 160 ? 41.910 -6.142  26.215  1.00 75.55  ?  160 ALA A N     1 
ATOM   1152 C CA    . ALA A 1 160 ? 42.301 -6.446  27.580  1.00 80.45  ?  160 ALA A CA    1 
ATOM   1153 C C     . ALA A 1 160 ? 41.748 -7.808  28.013  1.00 74.39  ?  160 ALA A C     1 
ATOM   1154 O O     . ALA A 1 160 ? 42.450 -8.586  28.669  1.00 74.33  ?  160 ALA A O     1 
ATOM   1155 C CB    . ALA A 1 160 ? 41.861 -5.304  28.503  1.00 71.87  ?  160 ALA A CB    1 
ATOM   1156 N N     . GLN A 1 161 ? 40.519 -8.143  27.600  1.00 70.81  ?  161 GLN A N     1 
ATOM   1157 C CA    . GLN A 1 161 ? 39.918 -9.404  28.034  1.00 71.64  ?  161 GLN A CA    1 
ATOM   1158 C C     . GLN A 1 161 ? 40.643 -10.600 27.435  1.00 75.92  ?  161 GLN A C     1 
ATOM   1159 O O     . GLN A 1 161 ? 40.971 -11.557 28.147  1.00 76.61  ?  161 GLN A O     1 
ATOM   1160 C CB    . GLN A 1 161 ? 38.430 -9.454  27.672  1.00 75.54  ?  161 GLN A CB    1 
ATOM   1161 C CG    . GLN A 1 161 ? 37.487 -8.729  28.663  1.00 81.35  ?  161 GLN A CG    1 
ATOM   1162 C CD    . GLN A 1 161 ? 37.502 -9.301  30.088  1.00 80.72  ?  161 GLN A CD    1 
ATOM   1163 O OE1   . GLN A 1 161 ? 36.766 -10.247 30.394  1.00 77.35  ?  161 GLN A OE1   1 
ATOM   1164 N NE2   . GLN A 1 161 ? 38.332 -8.716  30.965  1.00 79.93  ?  161 GLN A NE2   1 
ATOM   1165 N N     . VAL A 1 162 ? 40.881 -10.568 26.117  1.00 74.82  ?  162 VAL A N     1 
ATOM   1166 C CA    . VAL A 1 162 ? 41.676 -11.608 25.469  1.00 69.11  ?  162 VAL A CA    1 
ATOM   1167 C C     . VAL A 1 162 ? 43.043 -11.689 26.115  1.00 70.75  ?  162 VAL A C     1 
ATOM   1168 O O     . VAL A 1 162 ? 43.513 -12.774 26.465  1.00 71.93  ?  162 VAL A O     1 
ATOM   1169 C CB    . VAL A 1 162 ? 41.811 -11.332 23.962  1.00 67.11  ?  162 VAL A CB    1 
ATOM   1170 C CG1   . VAL A 1 162 ? 42.986 -12.110 23.384  1.00 61.57  ?  162 VAL A CG1   1 
ATOM   1171 C CG2   . VAL A 1 162 ? 40.535 -11.685 23.225  1.00 69.55  ?  162 VAL A CG2   1 
ATOM   1172 N N     . GLY A 1 163 ? 43.695 -10.530 26.299  1.00 68.47  ?  163 GLY A N     1 
ATOM   1173 C CA    . GLY A 1 163 ? 45.022 -10.512 26.897  1.00 67.54  ?  163 GLY A CA    1 
ATOM   1174 C C     . GLY A 1 163 ? 45.057 -11.138 28.273  1.00 72.04  ?  163 GLY A C     1 
ATOM   1175 O O     . GLY A 1 163 ? 46.098 -11.644 28.708  1.00 72.82  ?  163 GLY A O     1 
ATOM   1176 N N     . ARG A 1 164 ? 43.920 -11.119 28.967  1.00 75.02  ?  164 ARG A N     1 
ATOM   1177 C CA    . ARG A 1 164 ? 43.818 -11.764 30.269  1.00 73.37  ?  164 ARG A CA    1 
ATOM   1178 C C     . ARG A 1 164 ? 43.873 -13.283 30.138  1.00 75.79  ?  164 ARG A C     1 
ATOM   1179 O O     . ARG A 1 164 ? 44.685 -13.948 30.799  1.00 74.64  ?  164 ARG A O     1 
ATOM   1180 C CB    . ARG A 1 164 ? 42.517 -11.318 30.953  1.00 74.57  ?  164 ARG A CB    1 
ATOM   1181 C CG    . ARG A 1 164 ? 42.305 -11.850 32.356  1.00 72.74  ?  164 ARG A CG    1 
ATOM   1182 C CD    . ARG A 1 164 ? 41.153 -11.137 33.031  1.00 73.13  ?  164 ARG A CD    1 
ATOM   1183 N NE    . ARG A 1 164 ? 39.932 -11.184 32.237  1.00 79.80  ?  164 ARG A NE    1 
ATOM   1184 C CZ    . ARG A 1 164 ? 39.161 -12.257 32.088  1.00 78.49  ?  164 ARG A CZ    1 
ATOM   1185 N NH1   . ARG A 1 164 ? 39.484 -13.430 32.629  1.00 72.08  ?  164 ARG A NH1   1 
ATOM   1186 N NH2   . ARG A 1 164 ? 38.043 -12.155 31.369  1.00 76.71  ?  164 ARG A NH2   1 
ATOM   1187 N N     . VAL A 1 165 ? 43.020 -13.840 29.264  1.00 77.46  ?  165 VAL A N     1 
ATOM   1188 C CA    . VAL A 1 165 ? 42.831 -15.288 29.176  1.00 76.52  ?  165 VAL A CA    1 
ATOM   1189 C C     . VAL A 1 165 ? 43.952 -15.937 28.394  1.00 73.56  ?  165 VAL A C     1 
ATOM   1190 O O     . VAL A 1 165 ? 44.240 -17.124 28.586  1.00 74.72  ?  165 VAL A O     1 
ATOM   1191 C CB    . VAL A 1 165 ? 41.470 -15.632 28.546  1.00 73.67  ?  165 VAL A CB    1 
ATOM   1192 C CG1   . VAL A 1 165 ? 40.352 -14.911 29.268  1.00 76.83  ?  165 VAL A CG1   1 
ATOM   1193 C CG2   . VAL A 1 165 ? 41.451 -15.290 27.060  1.00 66.71  ?  165 VAL A CG2   1 
ATOM   1194 N N     . LEU A 1 166 ? 44.590 -15.191 27.501  1.00 72.74  ?  166 LEU A N     1 
ATOM   1195 C CA    . LEU A 1 166 ? 45.710 -15.728 26.745  1.00 74.14  ?  166 LEU A CA    1 
ATOM   1196 C C     . LEU A 1 166 ? 46.856 -16.046 27.676  1.00 74.35  ?  166 LEU A C     1 
ATOM   1197 O O     . LEU A 1 166 ? 47.291 -15.188 28.451  1.00 79.75  ?  166 LEU A O     1 
ATOM   1198 C CB    . LEU A 1 166 ? 46.162 -14.732 25.687  1.00 73.10  ?  166 LEU A CB    1 
ATOM   1199 C CG    . LEU A 1 166 ? 45.813 -15.194 24.299  1.00 67.75  ?  166 LEU A CG    1 
ATOM   1200 C CD1   . LEU A 1 166 ? 45.989 -14.018 23.420  1.00 66.94  ?  166 LEU A CD1   1 
ATOM   1201 C CD2   . LEU A 1 166 ? 46.741 -16.306 23.927  1.00 67.03  ?  166 LEU A CD2   1 
ATOM   1202 N N     . ARG A 1 167 ? 47.349 -17.269 27.596  1.00 69.42  ?  167 ARG A N     1 
ATOM   1203 C CA    . ARG A 1 167 ? 48.497 -17.619 28.405  1.00 74.30  ?  167 ARG A CA    1 
ATOM   1204 C C     . ARG A 1 167 ? 49.742 -16.890 27.886  1.00 81.26  ?  167 ARG A C     1 
ATOM   1205 O O     . ARG A 1 167 ? 49.834 -16.585 26.694  1.00 79.45  ?  167 ARG A O     1 
ATOM   1206 C CB    . ARG A 1 167 ? 48.709 -19.127 28.389  1.00 74.83  ?  167 ARG A CB    1 
ATOM   1207 C CG    . ARG A 1 167 ? 47.451 -19.958 28.654  1.00 75.92  ?  167 ARG A CG    1 
ATOM   1208 C CD    . ARG A 1 167 ? 47.797 -21.439 28.802  1.00 71.90  ?  167 ARG A CD    1 
ATOM   1209 N NE    . ARG A 1 167 ? 46.631 -22.305 28.934  1.00 75.36  ?  167 ARG A NE    1 
ATOM   1210 C CZ    . ARG A 1 167 ? 46.690 -23.632 28.910  1.00 77.50  ?  167 ARG A CZ    1 
ATOM   1211 N NH1   . ARG A 1 167 ? 47.846 -24.269 28.772  1.00 85.14  ?  167 ARG A NH1   1 
ATOM   1212 N NH2   . ARG A 1 167 ? 45.565 -24.339 29.021  1.00 80.61  ?  167 ARG A NH2   1 
ATOM   1213 N N     . PRO A 1 168 ? 50.690 -16.560 28.768  1.00 81.01  ?  168 PRO A N     1 
ATOM   1214 C CA    . PRO A 1 168 ? 51.963 -15.991 28.312  1.00 81.95  ?  168 PRO A CA    1 
ATOM   1215 C C     . PRO A 1 168 ? 52.621 -16.830 27.226  1.00 81.19  ?  168 PRO A C     1 
ATOM   1216 O O     . PRO A 1 168 ? 52.797 -18.043 27.367  1.00 85.50  ?  168 PRO A O     1 
ATOM   1217 C CB    . PRO A 1 168 ? 52.799 -15.962 29.595  1.00 82.04  ?  168 PRO A CB    1 
ATOM   1218 C CG    . PRO A 1 168 ? 51.795 -15.592 30.605  1.00 81.02  ?  168 PRO A CG    1 
ATOM   1219 C CD    . PRO A 1 168 ? 50.507 -16.328 30.207  1.00 80.17  ?  168 PRO A CD    1 
ATOM   1220 N N     . GLY A 1 169 ? 53.004 -16.152 26.144  1.00 78.78  ?  169 GLY A N     1 
ATOM   1221 C CA    . GLY A 1 169 ? 53.451 -16.777 24.930  1.00 78.17  ?  169 GLY A CA    1 
ATOM   1222 C C     . GLY A 1 169 ? 52.376 -16.970 23.884  1.00 76.26  ?  169 GLY A C     1 
ATOM   1223 O O     . GLY A 1 169 ? 52.697 -17.003 22.694  1.00 75.44  ?  169 GLY A O     1 
ATOM   1224 N N     . GLY A 1 170 ? 51.107 -17.058 24.282  1.00 72.10  ?  170 GLY A N     1 
ATOM   1225 C CA    . GLY A 1 170 ? 50.038 -17.284 23.330  1.00 72.19  ?  170 GLY A CA    1 
ATOM   1226 C C     . GLY A 1 170 ? 49.812 -16.068 22.455  1.00 71.06  ?  170 GLY A C     1 
ATOM   1227 O O     . GLY A 1 170 ? 50.309 -14.980 22.744  1.00 70.17  ?  170 GLY A O     1 
ATOM   1228 N N     . ARG A 1 171 ? 49.064 -16.252 21.355  1.00 64.08  ?  171 ARG A N     1 
ATOM   1229 C CA    . ARG A 1 171 ? 48.943 -15.218 20.329  1.00 64.93  ?  171 ARG A CA    1 
ATOM   1230 C C     . ARG A 1 171 ? 47.486 -14.891 20.012  1.00 62.36  ?  171 ARG A C     1 
ATOM   1231 O O     . ARG A 1 171 ? 46.574 -15.695 20.224  1.00 62.59  ?  171 ARG A O     1 
ATOM   1232 C CB    . ARG A 1 171 ? 49.660 -15.616 19.019  1.00 67.83  ?  171 ARG A CB    1 
ATOM   1233 C CG    . ARG A 1 171 ? 51.188 -15.586 19.069  1.00 71.25  ?  171 ARG A CG    1 
ATOM   1234 C CD    . ARG A 1 171 ? 51.779 -16.066 17.744  1.00 72.66  ?  171 ARG A CD    1 
ATOM   1235 N NE    . ARG A 1 171 ? 53.219 -15.853 17.603  1.00 72.80  ?  171 ARG A NE    1 
ATOM   1236 C CZ    . ARG A 1 171 ? 54.165 -16.658 18.075  1.00 71.45  ?  171 ARG A CZ    1 
ATOM   1237 N NH1   . ARG A 1 171 ? 53.876 -17.689 18.862  1.00 74.55  ?  171 ARG A NH1   1 
ATOM   1238 N NH2   . ARG A 1 171 ? 55.431 -16.433 17.737  1.00 79.14  ?  171 ARG A NH2   1 
ATOM   1239 N N     . LEU A 1 172 ? 47.274 -13.695 19.503  1.00 55.01  ?  172 LEU A N     1 
ATOM   1240 C CA    . LEU A 1 172 ? 45.956 -13.268 19.111  1.00 56.55  ?  172 LEU A CA    1 
ATOM   1241 C C     . LEU A 1 172 ? 46.005 -13.004 17.621  1.00 62.49  ?  172 LEU A C     1 
ATOM   1242 O O     . LEU A 1 172 ? 46.924 -12.339 17.130  1.00 62.93  ?  172 LEU A O     1 
ATOM   1243 C CB    . LEU A 1 172 ? 45.542 -12.037 19.904  1.00 54.89  ?  172 LEU A CB    1 
ATOM   1244 C CG    . LEU A 1 172 ? 44.591 -11.073 19.212  1.00 57.23  ?  172 LEU A CG    1 
ATOM   1245 C CD1   . LEU A 1 172 ? 43.219 -11.675 18.980  1.00 59.16  ?  172 LEU A CD1   1 
ATOM   1246 C CD2   . LEU A 1 172 ? 44.495 -9.831  20.018  1.00 54.81  ?  172 LEU A CD2   1 
ATOM   1247 N N     . VAL A 1 173 ? 45.052 -13.566 16.888  1.00 57.02  ?  173 VAL A N     1 
ATOM   1248 C CA    . VAL A 1 173 ? 44.912 -13.309 15.465  1.00 58.58  ?  173 VAL A CA    1 
ATOM   1249 C C     . VAL A 1 173 ? 43.507 -12.780 15.230  1.00 63.26  ?  173 VAL A C     1 
ATOM   1250 O O     . VAL A 1 173 ? 42.529 -13.385 15.683  1.00 66.24  ?  173 VAL A O     1 
ATOM   1251 C CB    . VAL A 1 173 ? 45.188 -14.565 14.619  1.00 56.50  ?  173 VAL A CB    1 
ATOM   1252 C CG1   . VAL A 1 173 ? 45.180 -14.216 13.143  1.00 54.53  ?  173 VAL A CG1   1 
ATOM   1253 C CG2   . VAL A 1 173 ? 46.519 -15.167 15.016  1.00 56.32  ?  173 VAL A CG2   1 
ATOM   1254 N N     . LEU A 1 174 ? 43.411 -11.640 14.551  1.00 59.89  ?  174 LEU A N     1 
ATOM   1255 C CA    . LEU A 1 174 ? 42.133 -11.016 14.248  1.00 62.85  ?  174 LEU A CA    1 
ATOM   1256 C C     . LEU A 1 174 ? 42.206 -10.405 12.864  1.00 62.77  ?  174 LEU A C     1 
ATOM   1257 O O     . LEU A 1 174 ? 43.283 -10.050 12.384  1.00 65.05  ?  174 LEU A O     1 
ATOM   1258 C CB    . LEU A 1 174 ? 41.775 -9.920  15.263  1.00 62.40  ?  174 LEU A CB    1 
ATOM   1259 C CG    . LEU A 1 174 ? 42.773 -8.761  15.371  1.00 63.03  ?  174 LEU A CG    1 
ATOM   1260 C CD1   . LEU A 1 174 ? 42.203 -7.532  14.718  1.00 64.04  ?  174 LEU A CD1   1 
ATOM   1261 C CD2   . LEU A 1 174 ? 43.195 -8.479  16.808  1.00 58.94  ?  174 LEU A CD2   1 
ATOM   1262 N N     . THR A 1 175 ? 41.062 -10.284 12.222  1.00 60.16  ?  175 THR A N     1 
ATOM   1263 C CA    . THR A 1 175 ? 40.945 -9.270  11.196  1.00 62.47  ?  175 THR A CA    1 
ATOM   1264 C C     . THR A 1 175 ? 40.168 -8.107  11.789  1.00 64.09  ?  175 THR A C     1 
ATOM   1265 O O     . THR A 1 175 ? 39.526 -8.244  12.833  1.00 65.73  ?  175 THR A O     1 
ATOM   1266 C CB    . THR A 1 175 ? 40.268 -9.784  9.925   1.00 57.23  ?  175 THR A CB    1 
ATOM   1267 O OG1   . THR A 1 175 ? 38.968 -10.304 10.218  1.00 61.99  ?  175 THR A OG1   1 
ATOM   1268 C CG2   . THR A 1 175 ? 41.092 -10.839 9.272   1.00 61.00  ?  175 THR A CG2   1 
ATOM   1269 N N     . ASP A 1 176 ? 40.278 -6.952  11.133  1.00 65.36  ?  176 ASP A N     1 
ATOM   1270 C CA    . ASP A 1 176 ? 39.628 -5.715  11.543  1.00 63.74  ?  176 ASP A CA    1 
ATOM   1271 C C     . ASP A 1 176 ? 39.465 -4.834  10.318  1.00 67.34  ?  176 ASP A C     1 
ATOM   1272 O O     . ASP A 1 176 ? 40.136 -5.023  9.301   1.00 69.66  ?  176 ASP A O     1 
ATOM   1273 C CB    . ASP A 1 176 ? 40.440 -4.971  12.607  1.00 68.28  ?  176 ASP A CB    1 
ATOM   1274 C CG    . ASP A 1 176 ? 39.583 -4.088  13.502  1.00 71.91  ?  176 ASP A CG    1 
ATOM   1275 O OD1   . ASP A 1 176 ? 38.412 -3.800  13.150  1.00 68.93  ?  176 ASP A OD1   1 
ATOM   1276 O OD2   . ASP A 1 176 ? 40.099 -3.696  14.576  1.00 73.78  -1 176 ASP A OD2   1 
ATOM   1277 N N     . PHE A 1 177 ? 38.575 -3.857  10.428  1.00 65.96  ?  177 PHE A N     1 
ATOM   1278 C CA    . PHE A 1 177 ? 38.469 -2.799  9.434   1.00 69.83  ?  177 PHE A CA    1 
ATOM   1279 C C     . PHE A 1 177 ? 39.290 -1.576  9.842   1.00 73.40  ?  177 PHE A C     1 
ATOM   1280 O O     . PHE A 1 177 ? 39.550 -1.339  11.032  1.00 75.54  ?  177 PHE A O     1 
ATOM   1281 C CB    . PHE A 1 177 ? 37.019 -2.403  9.250   1.00 72.27  ?  177 PHE A CB    1 
ATOM   1282 C CG    . PHE A 1 177 ? 36.241 -3.345  8.391   1.00 73.19  ?  177 PHE A CG    1 
ATOM   1283 C CD1   . PHE A 1 177 ? 36.740 -3.762  7.172   1.00 70.59  ?  177 PHE A CD1   1 
ATOM   1284 C CD2   . PHE A 1 177 ? 34.984 -3.802  8.794   1.00 74.40  ?  177 PHE A CD2   1 
ATOM   1285 C CE1   . PHE A 1 177 ? 36.003 -4.621  6.363   1.00 70.80  ?  177 PHE A CE1   1 
ATOM   1286 C CE2   . PHE A 1 177 ? 34.231 -4.656  7.994   1.00 71.07  ?  177 PHE A CE2   1 
ATOM   1287 C CZ    . PHE A 1 177 ? 34.736 -5.067  6.774   1.00 69.18  ?  177 PHE A CZ    1 
ATOM   1288 N N     . PHE A 1 178 ? 39.711 -0.799  8.841   1.00 73.27  ?  178 PHE A N     1 
ATOM   1289 C CA    . PHE A 1 178 ? 40.513 0.393   9.115   1.00 76.66  ?  178 PHE A CA    1 
ATOM   1290 C C     . PHE A 1 178 ? 40.484 1.331   7.916   1.00 76.40  ?  178 PHE A C     1 
ATOM   1291 O O     . PHE A 1 178 ? 40.099 0.942   6.809   1.00 74.44  ?  178 PHE A O     1 
ATOM   1292 C CB    . PHE A 1 178 ? 41.967 0.046   9.483   1.00 74.10  ?  178 PHE A CB    1 
ATOM   1293 C CG    . PHE A 1 178 ? 42.824 -0.357  8.308   1.00 76.34  ?  178 PHE A CG    1 
ATOM   1294 C CD1   . PHE A 1 178 ? 42.456 -1.413  7.479   1.00 72.63  ?  178 PHE A CD1   1 
ATOM   1295 C CD2   . PHE A 1 178 ? 44.016 0.303   8.053   1.00 74.51  ?  178 PHE A CD2   1 
ATOM   1296 C CE1   . PHE A 1 178 ? 43.248 -1.786  6.420   1.00 67.18  ?  178 PHE A CE1   1 
ATOM   1297 C CE2   . PHE A 1 178 ? 44.803 -0.068  6.994   1.00 72.94  ?  178 PHE A CE2   1 
ATOM   1298 C CZ    . PHE A 1 178 ? 44.421 -1.116  6.175   1.00 72.04  ?  178 PHE A CZ    1 
ATOM   1299 N N     . GLU A 1 179 ? 40.898 2.579   8.157   1.00 80.11  ?  179 GLU A N     1 
ATOM   1300 C CA    . GLU A 1 179 ? 40.977 3.600   7.113   1.00 75.32  ?  179 GLU A CA    1 
ATOM   1301 C C     . GLU A 1 179 ? 42.391 3.579   6.539   1.00 77.22  ?  179 GLU A C     1 
ATOM   1302 O O     . GLU A 1 179 ? 43.372 3.880   7.239   1.00 75.93  ?  179 GLU A O     1 
ATOM   1303 C CB    . GLU A 1 179 ? 40.606 4.980   7.660   1.00 82.85  ?  179 GLU A CB    1 
ATOM   1304 C CG    . GLU A 1 179 ? 39.272 5.020   8.414   1.00 90.68  ?  179 GLU A CG    1 
ATOM   1305 C CD    . GLU A 1 179 ? 39.066 6.263   9.260   1.00 94.15  ?  179 GLU A CD    1 
ATOM   1306 O OE1   . GLU A 1 179 ? 39.520 6.253   10.442  1.00 94.45  ?  179 GLU A OE1   1 
ATOM   1307 O OE2   . GLU A 1 179 ? 38.450 7.220   8.738   1.00 93.14  -1 179 GLU A OE2   1 
ATOM   1308 N N     . ARG A 1 180 ? 42.498 3.187   5.271   1.00 75.09  ?  180 ARG A N     1 
ATOM   1309 C CA    . ARG A 1 180 ? 43.795 3.242   4.616   1.00 77.88  ?  180 ARG A CA    1 
ATOM   1310 C C     . ARG A 1 180 ? 44.284 4.682   4.505   1.00 81.81  ?  180 ARG A C     1 
ATOM   1311 O O     . ARG A 1 180 ? 45.472 4.962   4.684   1.00 82.77  ?  180 ARG A O     1 
ATOM   1312 C CB    . ARG A 1 180 ? 43.694 2.577   3.247   1.00 72.68  ?  180 ARG A CB    1 
ATOM   1313 C CG    . ARG A 1 180 ? 43.189 1.144   3.341   1.00 72.55  ?  180 ARG A CG    1 
ATOM   1314 C CD    . ARG A 1 180 ? 43.012 0.451   1.980   1.00 71.99  ?  180 ARG A CD    1 
ATOM   1315 N NE    . ARG A 1 180 ? 44.164 -0.369  1.631   1.00 69.55  ?  180 ARG A NE    1 
ATOM   1316 C CZ    . ARG A 1 180 ? 44.301 -1.043  0.499   1.00 67.13  ?  180 ARG A CZ    1 
ATOM   1317 N NH1   . ARG A 1 180 ? 43.345 -1.069  -0.414  1.00 62.92  ?  180 ARG A NH1   1 
ATOM   1318 N NH2   . ARG A 1 180 ? 45.430 -1.700  0.278   1.00 71.33  ?  180 ARG A NH2   1 
ATOM   1319 N N     . ALA A 1 181 ? 43.373 5.601   4.262   1.00 81.99  ?  181 ALA A N     1 
ATOM   1320 C CA    . ALA A 1 181 ? 43.646 7.005   4.024   1.00 85.24  ?  181 ALA A CA    1 
ATOM   1321 C C     . ALA A 1 181 ? 42.294 7.698   3.931   1.00 89.85  ?  181 ALA A C     1 
ATOM   1322 O O     . ALA A 1 181 ? 41.293 7.026   3.661   1.00 84.05  ?  181 ALA A O     1 
ATOM   1323 C CB    . ALA A 1 181 ? 44.453 7.181   2.744   1.00 84.45  ?  181 ALA A CB    1 
ATOM   1324 N N     . PRO A 1 182 ? 42.226 9.018   4.118   1.00 93.21  ?  182 PRO A N     1 
ATOM   1325 C CA    . PRO A 1 182 ? 40.921 9.697   4.187   1.00 93.67  ?  182 PRO A CA    1 
ATOM   1326 C C     . PRO A 1 182 ? 39.977 9.249   3.085   1.00 90.90  ?  182 PRO A C     1 
ATOM   1327 O O     . PRO A 1 182 ? 40.409 8.916   1.988   1.00 87.65  ?  182 PRO A O     1 
ATOM   1328 C CB    . PRO A 1 182 ? 41.294 11.172  4.048   1.00 92.97  ?  182 PRO A CB    1 
ATOM   1329 C CG    . PRO A 1 182 ? 42.668 11.240  4.679   1.00 94.43  ?  182 PRO A CG    1 
ATOM   1330 C CD    . PRO A 1 182 ? 43.348 9.952   4.340   1.00 90.66  ?  182 PRO A CD    1 
ATOM   1331 N N     . LEU A 1 183 ? 38.682 9.199   3.391   1.00 92.94  ?  183 LEU A N     1 
ATOM   1332 C CA    . LEU A 1 183 ? 37.750 8.566   2.472   1.00 91.45  ?  183 LEU A CA    1 
ATOM   1333 C C     . LEU A 1 183 ? 37.260 9.543   1.411   1.00 95.22  ?  183 LEU A C     1 
ATOM   1334 O O     . LEU A 1 183 ? 36.953 10.702  1.696   1.00 97.13  ?  183 LEU A O     1 
ATOM   1335 C CB    . LEU A 1 183 ? 36.554 7.963   3.211   1.00 94.91  ?  183 LEU A CB    1 
ATOM   1336 C CG    . LEU A 1 183 ? 35.892 6.820   2.413   1.00 93.09  ?  183 LEU A CG    1 
ATOM   1337 C CD1   . LEU A 1 183 ? 36.767 5.584   2.399   1.00 80.87  ?  183 LEU A CD1   1 
ATOM   1338 C CD2   . LEU A 1 183 ? 34.518 6.456   2.902   1.00 92.02  ?  183 LEU A CD2   1 
ATOM   1339 N N     . ALA A 1 184 ? 37.170 9.048   0.196   1.00 95.69  ?  184 ALA A N     1 
ATOM   1340 C CA    . ALA A 1 184 ? 36.796 9.768   -1.006  1.00 98.80  ?  184 ALA A CA    1 
ATOM   1341 C C     . ALA A 1 184 ? 35.298 10.037  -1.032  1.00 102.15 ?  184 ALA A C     1 
ATOM   1342 O O     . ALA A 1 184 ? 34.499 9.150   -0.716  1.00 99.76  ?  184 ALA A O     1 
ATOM   1343 C CB    . ALA A 1 184 ? 37.186 8.968   -2.241  1.00 101.40 ?  184 ALA A CB    1 
ATOM   1344 N N     . PRO A 1 185 ? 34.900 11.230  -1.461  1.00 101.20 ?  185 PRO A N     1 
ATOM   1345 C CA    . PRO A 1 185 ? 33.483 11.597  -1.379  1.00 101.83 ?  185 PRO A CA    1 
ATOM   1346 C C     . PRO A 1 185 ? 32.569 10.669  -2.138  1.00 102.73 ?  185 PRO A C     1 
ATOM   1347 O O     . PRO A 1 185 ? 31.554 10.227  -1.588  1.00 107.33 ?  185 PRO A O     1 
ATOM   1348 C CB    . PRO A 1 185 ? 33.461 12.998  -1.989  1.00 94.10  ?  185 PRO A CB    1 
ATOM   1349 C CG    . PRO A 1 185 ? 34.592 12.950  -2.969  1.00 101.61 ?  185 PRO A CG    1 
ATOM   1350 C CD    . PRO A 1 185 ? 35.667 12.192  -2.256  1.00 97.64  ?  185 PRO A CD    1 
ATOM   1351 N N     . GLU A 1 186 ? 32.903 10.343  -3.385  1.00 102.84 ?  186 GLU A N     1 
ATOM   1352 C CA    . GLU A 1 186 ? 31.997 9.523   -4.180  1.00 104.18 ?  186 GLU A CA    1 
ATOM   1353 C C     . GLU A 1 186 ? 31.759 8.156   -3.544  1.00 105.39 ?  186 GLU A C     1 
ATOM   1354 O O     . GLU A 1 186 ? 30.920 7.396   -4.047  1.00 109.07 ?  186 GLU A O     1 
ATOM   1355 C CB    . GLU A 1 186 ? 32.529 9.370   -5.619  1.00 106.27 ?  186 GLU A CB    1 
ATOM   1356 N N     . GLY A 1 187 ? 32.469 7.843   -2.452  1.00 101.55 ?  187 GLY A N     1 
ATOM   1357 C CA    . GLY A 1 187 ? 32.378 6.566   -1.774  1.00 99.97  ?  187 GLY A CA    1 
ATOM   1358 C C     . GLY A 1 187 ? 32.237 6.645   -0.265  1.00 101.16 ?  187 GLY A C     1 
ATOM   1359 O O     . GLY A 1 187 ? 32.215 5.614   0.411   1.00 91.29  ?  187 GLY A O     1 
ATOM   1360 N N     . ARG A 1 188 ? 32.145 7.856   0.288   1.00 105.60 ?  188 ARG A N     1 
ATOM   1361 C CA    . ARG A 1 188 ? 31.758 7.989   1.691   1.00 103.34 ?  188 ARG A CA    1 
ATOM   1362 C C     . ARG A 1 188 ? 30.344 7.478   1.928   1.00 102.34 ?  188 ARG A C     1 
ATOM   1363 O O     . ARG A 1 188 ? 29.946 7.278   3.082   1.00 101.12 ?  188 ARG A O     1 
ATOM   1364 C CB    . ARG A 1 188 ? 31.880 9.452   2.149   1.00 105.47 ?  188 ARG A CB    1 
ATOM   1365 C CG    . ARG A 1 188 ? 33.301 9.910   2.381   1.00 106.41 ?  188 ARG A CG    1 
ATOM   1366 C CD    . ARG A 1 188 ? 33.342 11.355  2.808   1.00 108.42 ?  188 ARG A CD    1 
ATOM   1367 N NE    . ARG A 1 188 ? 32.749 11.576  4.122   1.00 108.37 ?  188 ARG A NE    1 
ATOM   1368 C CZ    . ARG A 1 188 ? 33.443 11.665  5.255   1.00 109.10 ?  188 ARG A CZ    1 
ATOM   1369 N NH1   . ARG A 1 188 ? 34.760 11.485  5.285   1.00 109.76 ?  188 ARG A NH1   1 
ATOM   1370 N NH2   . ARG A 1 188 ? 32.802 11.950  6.388   1.00 108.35 ?  188 ARG A NH2   1 
ATOM   1371 N N     . ALA A 1 189 ? 29.571 7.298   0.853   1.00 105.82 ?  189 ALA A N     1 
ATOM   1372 C CA    . ALA A 1 189 ? 28.163 6.923   0.966   1.00 103.76 ?  189 ALA A CA    1 
ATOM   1373 C C     . ALA A 1 189 ? 28.010 5.464   1.352   1.00 100.73 ?  189 ALA A C     1 
ATOM   1374 O O     . ALA A 1 189 ? 27.408 5.140   2.383   1.00 99.44  ?  189 ALA A O     1 
ATOM   1375 C CB    . ALA A 1 189 ? 27.435 7.197   -0.357  1.00 104.07 ?  189 ALA A CB    1 
ATOM   1376 N N     . ALA A 1 190 ? 28.545 4.571   0.519   1.00 99.67  ?  190 ALA A N     1 
ATOM   1377 C CA    . ALA A 1 190 ? 28.366 3.146   0.749   1.00 97.58  ?  190 ALA A CA    1 
ATOM   1378 C C     . ALA A 1 190 ? 29.035 2.687   2.043   1.00 94.51  ?  190 ALA A C     1 
ATOM   1379 O O     . ALA A 1 190 ? 28.534 1.769   2.699   1.00 98.30  ?  190 ALA A O     1 
ATOM   1380 C CB    . ALA A 1 190 ? 28.881 2.350   -0.453  1.00 92.58  ?  190 ALA A CB    1 
ATOM   1381 N N     . VAL A 1 191 ? 30.153 3.300   2.436   1.00 91.70  ?  191 VAL A N     1 
ATOM   1382 C CA    . VAL A 1 191 ? 30.815 2.880   3.670   1.00 86.25  ?  191 VAL A CA    1 
ATOM   1383 C C     . VAL A 1 191 ? 29.957 3.205   4.888   1.00 96.62  ?  191 VAL A C     1 
ATOM   1384 O O     . VAL A 1 191 ? 29.774 2.364   5.781   1.00 92.88  ?  191 VAL A O     1 
ATOM   1385 C CB    . VAL A 1 191 ? 32.203 3.523   3.793   1.00 81.37  ?  191 VAL A CB    1 
ATOM   1386 C CG1   . VAL A 1 191 ? 32.778 3.245   5.175   1.00 82.63  ?  191 VAL A CG1   1 
ATOM   1387 C CG2   . VAL A 1 191 ? 33.126 2.992   2.727   1.00 81.67  ?  191 VAL A CG2   1 
ATOM   1388 N N     . GLN A 1 192 ? 29.430 4.437   4.949   1.00 100.07 ?  192 GLN A N     1 
ATOM   1389 C CA    . GLN A 1 192 ? 28.614 4.850   6.091   1.00 95.69  ?  192 GLN A CA    1 
ATOM   1390 C C     . GLN A 1 192 ? 27.425 3.917   6.279   1.00 95.62  ?  192 GLN A C     1 
ATOM   1391 O O     . GLN A 1 192 ? 27.025 3.639   7.417   1.00 98.12  ?  192 GLN A O     1 
ATOM   1392 C CB    . GLN A 1 192 ? 28.143 6.293   5.894   1.00 99.32  ?  192 GLN A CB    1 
ATOM   1393 C CG    . GLN A 1 192 ? 27.330 6.937   7.030   1.00 100.81 ?  192 GLN A CG    1 
ATOM   1394 C CD    . GLN A 1 192 ? 26.829 8.363   6.702   1.00 111.13 ?  192 GLN A CD    1 
ATOM   1395 O OE1   . GLN A 1 192 ? 27.561 9.346   6.839   1.00 115.87 ?  192 GLN A OE1   1 
ATOM   1396 N NE2   . GLN A 1 192 ? 25.570 8.470   6.286   1.00 108.21 ?  192 GLN A NE2   1 
ATOM   1397 N N     . ARG A 1 193 ? 26.857 3.424   5.162   1.00 94.90  ?  193 ARG A N     1 
ATOM   1398 C CA    . ARG A 1 193 ? 25.697 2.526   5.199   1.00 97.75  ?  193 ARG A CA    1 
ATOM   1399 C C     . ARG A 1 193 ? 26.082 1.144   5.733   1.00 100.06 ?  193 ARG A C     1 
ATOM   1400 O O     . ARG A 1 193 ? 25.392 0.584   6.598   1.00 100.37 ?  193 ARG A O     1 
ATOM   1401 C CB    . ARG A 1 193 ? 25.067 2.430   3.795   1.00 99.47  ?  193 ARG A CB    1 
ATOM   1402 C CG    . ARG A 1 193 ? 23.773 1.574   3.674   1.00 106.08 ?  193 ARG A CG    1 
ATOM   1403 C CD    . ARG A 1 193 ? 22.443 2.343   3.966   1.00 106.37 ?  193 ARG A CD    1 
ATOM   1404 N NE    . ARG A 1 193 ? 21.646 1.744   5.045   1.00 114.66 ?  193 ARG A NE    1 
ATOM   1405 C CZ    . ARG A 1 193 ? 20.507 2.227   5.543   1.00 116.46 ?  193 ARG A CZ    1 
ATOM   1406 N NH1   . ARG A 1 193 ? 19.940 3.315   5.051   1.00 115.36 ?  193 ARG A NH1   1 
ATOM   1407 N NH2   . ARG A 1 193 ? 19.924 1.602   6.567   1.00 108.43 ?  193 ARG A NH2   1 
ATOM   1408 N N     . TYR A 1 194 ? 27.203 0.597   5.245   1.00 99.27  ?  194 TYR A N     1 
ATOM   1409 C CA    . TYR A 1 194 ? 27.696 -0.716  5.673   1.00 92.92  ?  194 TYR A CA    1 
ATOM   1410 C C     . TYR A 1 194 ? 27.958 -0.758  7.186   1.00 90.32  ?  194 TYR A C     1 
ATOM   1411 O O     . TYR A 1 194 ? 27.496 -1.671  7.883   1.00 87.79  ?  194 TYR A O     1 
ATOM   1412 C CB    . TYR A 1 194 ? 28.965 -1.035  4.859   1.00 89.92  ?  194 TYR A CB    1 
ATOM   1413 C CG    . TYR A 1 194 ? 29.537 -2.461  4.839   1.00 89.79  ?  194 TYR A CG    1 
ATOM   1414 C CD1   . TYR A 1 194 ? 28.866 -3.512  4.211   1.00 88.93  ?  194 TYR A CD1   1 
ATOM   1415 C CD2   . TYR A 1 194 ? 30.799 -2.730  5.385   1.00 85.60  ?  194 TYR A CD2   1 
ATOM   1416 C CE1   . TYR A 1 194 ? 29.410 -4.785  4.169   1.00 81.93  ?  194 TYR A CE1   1 
ATOM   1417 C CE2   . TYR A 1 194 ? 31.345 -4.008  5.350   1.00 80.10  ?  194 TYR A CE2   1 
ATOM   1418 C CZ    . TYR A 1 194 ? 30.647 -5.017  4.736   1.00 75.85  ?  194 TYR A CZ    1 
ATOM   1419 O OH    . TYR A 1 194 ? 31.191 -6.265  4.695   1.00 81.60  ?  194 TYR A OH    1 
ATOM   1420 N N     . LEU A 1 195 ? 28.673 0.241   7.718   1.00 88.37  ?  195 LEU A N     1 
ATOM   1421 C CA    . LEU A 1 195 ? 28.997 0.234   9.138   1.00 88.73  ?  195 LEU A CA    1 
ATOM   1422 C C     . LEU A 1 195 ? 27.783 0.397   10.044  1.00 93.14  ?  195 LEU A C     1 
ATOM   1423 O O     . LEU A 1 195 ? 27.837 -0.046  11.201  1.00 89.65  ?  195 LEU A O     1 
ATOM   1424 C CB    . LEU A 1 195 ? 29.971 1.342   9.457   1.00 87.99  ?  195 LEU A CB    1 
ATOM   1425 C CG    . LEU A 1 195 ? 31.460 1.078   9.273   1.00 88.56  ?  195 LEU A CG    1 
ATOM   1426 C CD1   . LEU A 1 195 ? 31.783 0.975   7.813   1.00 85.53  ?  195 LEU A CD1   1 
ATOM   1427 C CD2   . LEU A 1 195 ? 32.273 2.193   9.991   1.00 89.11  ?  195 LEU A CD2   1 
ATOM   1428 N N     . HIS A 1 196 ? 26.712 1.052   9.564   1.00 93.74  ?  196 HIS A N     1 
ATOM   1429 C CA    . HIS A 1 196 ? 25.465 1.152   10.327  1.00 97.20  ?  196 HIS A CA    1 
ATOM   1430 C C     . HIS A 1 196 ? 24.652 -0.127  10.219  1.00 94.44  ?  196 HIS A C     1 
ATOM   1431 O O     . HIS A 1 196 ? 24.222 -0.688  11.234  1.00 95.61  ?  196 HIS A O     1 
ATOM   1432 C CB    . HIS A 1 196 ? 24.614 2.345   9.851   1.00 98.10  ?  196 HIS A CB    1 
ATOM   1433 C CG    . HIS A 1 196 ? 23.439 2.669   10.741  1.00 102.87 ?  196 HIS A CG    1 
ATOM   1434 N ND1   . HIS A 1 196 ? 22.130 2.429   10.368  1.00 99.21  ?  196 HIS A ND1   1 
ATOM   1435 C CD2   . HIS A 1 196 ? 23.375 3.234   11.976  1.00 110.91 ?  196 HIS A CD2   1 
ATOM   1436 C CE1   . HIS A 1 196 ? 21.316 2.824   11.335  1.00 109.80 ?  196 HIS A CE1   1 
ATOM   1437 N NE2   . HIS A 1 196 ? 22.045 3.314   12.322  1.00 113.78 ?  196 HIS A NE2   1 
ATOM   1438 N N     . ASP A 1 197 ? 24.449 -0.608  8.995   1.00 92.38  ?  197 ASP A N     1 
ATOM   1439 C CA    . ASP A 1 197 ? 23.584 -1.751  8.759   1.00 90.42  ?  197 ASP A CA    1 
ATOM   1440 C C     . ASP A 1 197 ? 24.116 -3.053  9.319   1.00 88.08  ?  197 ASP A C     1 
ATOM   1441 O O     . ASP A 1 197 ? 23.370 -4.033  9.371   1.00 87.09  ?  197 ASP A O     1 
ATOM   1442 C CB    . ASP A 1 197 ? 23.356 -1.914  7.276   1.00 90.89  ?  197 ASP A CB    1 
ATOM   1443 C CG    . ASP A 1 197 ? 22.532 -0.815  6.724   1.00 100.72 ?  197 ASP A CG    1 
ATOM   1444 O OD1   . ASP A 1 197 ? 22.309 0.153   7.495   1.00 104.90 ?  197 ASP A OD1   1 
ATOM   1445 O OD2   . ASP A 1 197 ? 22.110 -0.929  5.546   1.00 104.63 -1 197 ASP A OD2   1 
ATOM   1446 N N     . PHE A 1 198 ? 25.371 -3.111  9.709   1.00 89.63  ?  198 PHE A N     1 
ATOM   1447 C CA    . PHE A 1 198 ? 25.879 -4.332  10.292  1.00 85.66  ?  198 PHE A CA    1 
ATOM   1448 C C     . PHE A 1 198 ? 26.538 -4.063  11.627  1.00 84.89  ?  198 PHE A C     1 
ATOM   1449 O O     . PHE A 1 198 ? 27.211 -4.942  12.161  1.00 85.44  ?  198 PHE A O     1 
ATOM   1450 C CB    . PHE A 1 198 ? 26.842 -5.019  9.331   1.00 82.84  ?  198 PHE A CB    1 
ATOM   1451 C CG    . PHE A 1 198 ? 26.162 -5.633  8.139   1.00 85.14  ?  198 PHE A CG    1 
ATOM   1452 C CD1   . PHE A 1 198 ? 25.933 -4.895  6.997   1.00 80.81  ?  198 PHE A CD1   1 
ATOM   1453 C CD2   . PHE A 1 198 ? 25.754 -6.961  8.163   1.00 91.52  ?  198 PHE A CD2   1 
ATOM   1454 C CE1   . PHE A 1 198 ? 25.313 -5.467  5.897   1.00 82.06  ?  198 PHE A CE1   1 
ATOM   1455 C CE2   . PHE A 1 198 ? 25.129 -7.544  7.064   1.00 91.13  ?  198 PHE A CE2   1 
ATOM   1456 C CZ    . PHE A 1 198 ? 24.909 -6.792  5.928   1.00 88.99  ?  198 PHE A CZ    1 
ATOM   1457 N N     . MET A 1 199 ? 26.350 -2.877  12.186  1.00 83.42  ?  199 MET A N     1 
ATOM   1458 C CA    . MET A 1 199 ? 26.826 -2.566  13.526  1.00 83.48  ?  199 MET A CA    1 
ATOM   1459 C C     . MET A 1 199 ? 28.339 -2.781  13.639  1.00 83.20  ?  199 MET A C     1 
ATOM   1460 O O     . MET A 1 199 ? 28.810 -3.642  14.391  1.00 85.14  ?  199 MET A O     1 
ATOM   1461 C CB    . MET A 1 199 ? 26.064 -3.399  14.569  1.00 76.98  ?  199 MET A CB    1 
ATOM   1462 C CG    . MET A 1 199 ? 24.570 -3.583  14.289  1.00 77.80  ?  199 MET A CG    1 
ATOM   1463 S SD    . MET A 1 199 ? 23.660 -4.113  15.763  1.00 88.35  ?  199 MET A SD    1 
ATOM   1464 C CE    . MET A 1 199 ? 21.985 -4.249  15.162  1.00 88.17  ?  199 MET A CE    1 
ATOM   1465 N N     . MET A 1 200 ? 29.105 -1.992  12.870  1.00 81.10  ?  200 MET A N     1 
ATOM   1466 C CA    . MET A 1 200 ? 30.557 -2.152  12.834  1.00 80.33  ?  200 MET A CA    1 
ATOM   1467 C C     . MET A 1 200 ? 31.279 -0.813  12.838  1.00 84.35  ?  200 MET A C     1 
ATOM   1468 O O     . MET A 1 200 ? 30.752 0.209   12.390  1.00 86.92  ?  200 MET A O     1 
ATOM   1469 C CB    . MET A 1 200 ? 31.011 -2.926  11.601  1.00 82.35  ?  200 MET A CB    1 
ATOM   1470 C CG    . MET A 1 200 ? 30.296 -4.227  11.381  1.00 80.86  ?  200 MET A CG    1 
ATOM   1471 S SD    . MET A 1 200 ? 30.677 -4.817  9.748   1.00 77.42  ?  200 MET A SD    1 
ATOM   1472 C CE    . MET A 1 200 ? 29.959 -3.522  8.766   1.00 82.28  ?  200 MET A CE    1 
ATOM   1473 N N     . THR A 1 201 ? 32.528 -0.861  13.318  1.00 83.73  ?  201 THR A N     1 
ATOM   1474 C CA    . THR A 1 201 ? 33.389 0.302   13.477  1.00 82.23  ?  201 THR A CA    1 
ATOM   1475 C C     . THR A 1 201 ? 34.778 0.029   12.897  1.00 81.77  ?  201 THR A C     1 
ATOM   1476 O O     . THR A 1 201 ? 35.269 -1.102  12.917  1.00 79.44  ?  201 THR A O     1 
ATOM   1477 C CB    . THR A 1 201 ? 33.511 0.685   14.953  1.00 78.47  ?  201 THR A CB    1 
ATOM   1478 O OG1   . THR A 1 201 ? 34.598 -0.037  15.539  1.00 71.75  ?  201 THR A OG1   1 
ATOM   1479 C CG2   . THR A 1 201 ? 32.225 0.331   15.696  1.00 85.44  ?  201 THR A CG2   1 
ATOM   1480 N N     . MET A 1 202 ? 35.410 1.083   12.385  1.00 81.21  ?  202 MET A N     1 
ATOM   1481 C CA    . MET A 1 202 ? 36.770 1.043   11.864  1.00 75.52  ?  202 MET A CA    1 
ATOM   1482 C C     . MET A 1 202 ? 37.750 1.624   12.876  1.00 77.25  ?  202 MET A C     1 
ATOM   1483 O O     . MET A 1 202 ? 37.374 2.283   13.846  1.00 82.33  ?  202 MET A O     1 
ATOM   1484 C CB    . MET A 1 202 ? 36.846 1.816   10.550  1.00 80.39  ?  202 MET A CB    1 
ATOM   1485 C CG    . MET A 1 202 ? 35.675 1.517   9.619   1.00 85.94  ?  202 MET A CG    1 
ATOM   1486 S SD    . MET A 1 202 ? 35.541 2.616   8.177   1.00 85.26  ?  202 MET A SD    1 
ATOM   1487 C CE    . MET A 1 202 ? 37.215 2.492   7.587   1.00 71.83  ?  202 MET A CE    1 
ATOM   1488 N N     . VAL A 1 203 ? 39.034 1.392   12.643  1.00 76.03  ?  203 VAL A N     1 
ATOM   1489 C CA    . VAL A 1 203 ? 40.049 1.987   13.489  1.00 79.89  ?  203 VAL A CA    1 
ATOM   1490 C C     . VAL A 1 203 ? 41.106 2.655   12.622  1.00 85.47  ?  203 VAL A C     1 
ATOM   1491 O O     . VAL A 1 203 ? 41.215 2.424   11.418  1.00 79.84  ?  203 VAL A O     1 
ATOM   1492 C CB    . VAL A 1 203 ? 40.691 0.963   14.437  1.00 75.30  ?  203 VAL A CB    1 
ATOM   1493 C CG1   . VAL A 1 203 ? 39.644 0.337   15.254  1.00 71.08  ?  203 VAL A CG1   1 
ATOM   1494 C CG2   . VAL A 1 203 ? 41.392 -0.096  13.664  1.00 77.63  ?  203 VAL A CG2   1 
ATOM   1495 N N     . SER A 1 204 ? 41.865 3.530   13.257  1.00 87.66  ?  204 SER A N     1 
ATOM   1496 C CA    . SER A 1 204 ? 43.146 3.923   12.705  1.00 87.65  ?  204 SER A CA    1 
ATOM   1497 C C     . SER A 1 204 ? 44.134 2.784   12.931  1.00 86.81  ?  204 SER A C     1 
ATOM   1498 O O     . SER A 1 204 ? 44.124 2.129   13.975  1.00 83.52  ?  204 SER A O     1 
ATOM   1499 C CB    . SER A 1 204 ? 43.636 5.218   13.364  1.00 84.69  ?  204 SER A CB    1 
ATOM   1500 O OG    . SER A 1 204 ? 43.257 5.293   14.739  1.00 88.22  ?  204 SER A OG    1 
ATOM   1501 N N     . ALA A 1 205 ? 44.963 2.521   11.925  1.00 83.19  ?  205 ALA A N     1 
ATOM   1502 C CA    . ALA A 1 205 ? 45.977 1.483   12.079  1.00 77.01  ?  205 ALA A CA    1 
ATOM   1503 C C     . ALA A 1 205 ? 46.981 1.827   13.176  1.00 81.52  ?  205 ALA A C     1 
ATOM   1504 O O     . ALA A 1 205 ? 47.537 0.920   13.812  1.00 80.86  ?  205 ALA A O     1 
ATOM   1505 C CB    . ALA A 1 205 ? 46.697 1.257   10.752  1.00 75.72  ?  205 ALA A CB    1 
ATOM   1506 N N     . GLU A 1 206 ? 47.246 3.124   13.390  1.00 80.54  ?  206 GLU A N     1 
ATOM   1507 C CA    . GLU A 1 206 ? 48.068 3.546   14.516  1.00 77.56  ?  206 GLU A CA    1 
ATOM   1508 C C     . GLU A 1 206 ? 47.344 3.359   15.839  1.00 83.05  ?  206 GLU A C     1 
ATOM   1509 O O     . GLU A 1 206 ? 47.990 3.407   16.893  1.00 80.71  ?  206 GLU A O     1 
ATOM   1510 C CB    . GLU A 1 206 ? 48.523 5.007   14.349  1.00 77.12  ?  206 GLU A CB    1 
ATOM   1511 C CG    . GLU A 1 206 ? 47.425 6.035   14.097  1.00 80.48  ?  206 GLU A CG    1 
ATOM   1512 C CD    . GLU A 1 206 ? 46.904 6.004   12.663  1.00 76.00  ?  206 GLU A CD    1 
ATOM   1513 O OE1   . GLU A 1 206 ? 47.237 5.052   11.943  1.00 67.97  ?  206 GLU A OE1   1 
ATOM   1514 O OE2   . GLU A 1 206 ? 46.149 6.911   12.246  1.00 81.01  -1 206 GLU A OE2   1 
ATOM   1515 N N     . ALA A 1 207 ? 46.029 3.112   15.806  1.00 85.18  ?  207 ALA A N     1 
ATOM   1516 C CA    . ALA A 1 207 ? 45.305 2.811   17.035  1.00 80.38  ?  207 ALA A CA    1 
ATOM   1517 C C     . ALA A 1 207 ? 45.812 1.527   17.679  1.00 78.98  ?  207 ALA A C     1 
ATOM   1518 O O     . ALA A 1 207 ? 46.001 1.473   18.897  1.00 80.20  ?  207 ALA A O     1 
ATOM   1519 C CB    . ALA A 1 207 ? 43.801 2.714   16.766  1.00 81.53  ?  207 ALA A CB    1 
ATOM   1520 N N     . TYR A 1 208 ? 46.047 0.483   16.872  1.00 78.71  ?  208 TYR A N     1 
ATOM   1521 C CA    . TYR A 1 208 ? 46.196 -0.871  17.421  1.00 79.06  ?  208 TYR A CA    1 
ATOM   1522 C C     . TYR A 1 208 ? 47.385 -1.032  18.358  1.00 79.40  ?  208 TYR A C     1 
ATOM   1523 O O     . TYR A 1 208 ? 47.208 -1.610  19.446  1.00 80.56  ?  208 TYR A O     1 
ATOM   1524 C CB    . TYR A 1 208 ? 46.238 -1.924  16.300  1.00 66.52  ?  208 TYR A CB    1 
ATOM   1525 C CG    . TYR A 1 208 ? 44.934 -2.680  16.152  1.00 66.91  ?  208 TYR A CG    1 
ATOM   1526 C CD1   . TYR A 1 208 ? 44.523 -3.595  17.121  1.00 60.26  ?  208 TYR A CD1   1 
ATOM   1527 C CD2   . TYR A 1 208 ? 44.110 -2.470  15.037  1.00 71.40  ?  208 TYR A CD2   1 
ATOM   1528 C CE1   . TYR A 1 208 ? 43.337 -4.271  16.987  1.00 66.24  ?  208 TYR A CE1   1 
ATOM   1529 C CE2   . TYR A 1 208 ? 42.922 -3.145  14.898  1.00 71.46  ?  208 TYR A CE2   1 
ATOM   1530 C CZ    . TYR A 1 208 ? 42.546 -4.040  15.875  1.00 69.28  ?  208 TYR A CZ    1 
ATOM   1531 O OH    . TYR A 1 208 ? 41.367 -4.709  15.736  1.00 69.13  ?  208 TYR A OH    1 
ATOM   1532 N N     . PRO A 1 209 ? 48.592 -0.595  18.024  1.00 77.29  ?  209 PRO A N     1 
ATOM   1533 C CA    . PRO A 1 209 ? 49.746 -0.901  18.890  1.00 78.97  ?  209 PRO A CA    1 
ATOM   1534 C C     . PRO A 1 209 ? 49.581 -0.329  20.290  1.00 81.69  ?  209 PRO A C     1 
ATOM   1535 O O     . PRO A 1 209 ? 50.078 -0.926  21.264  1.00 84.88  ?  209 PRO A O     1 
ATOM   1536 C CB    . PRO A 1 209 ? 50.931 -0.260  18.154  1.00 77.13  ?  209 PRO A CB    1 
ATOM   1537 C CG    . PRO A 1 209 ? 50.476 -0.121  16.764  1.00 71.47  ?  209 PRO A CG    1 
ATOM   1538 C CD    . PRO A 1 209 ? 48.999 0.114   16.799  1.00 73.87  ?  209 PRO A CD    1 
ATOM   1539 N N     . PRO A 1 210 ? 48.921 0.873   20.446  1.00 83.90  ?  210 PRO A N     1 
ATOM   1540 C CA    . PRO A 1 210 ? 48.458 1.259   21.783  1.00 80.91  ?  210 PRO A CA    1 
ATOM   1541 C C     . PRO A 1 210 ? 47.452 0.279   22.379  1.00 81.55  ?  210 PRO A C     1 
ATOM   1542 O O     . PRO A 1 210 ? 47.709 -0.295  23.449  1.00 81.83  ?  210 PRO A O     1 
ATOM   1543 C CB    . PRO A 1 210 ? 47.828 2.630   21.527  1.00 73.38  ?  210 PRO A CB    1 
ATOM   1544 C CG    . PRO A 1 210 ? 48.653 3.200   20.477  1.00 78.10  ?  210 PRO A CG    1 
ATOM   1545 C CD    . PRO A 1 210 ? 48.927 2.057   19.555  1.00 82.84  ?  210 PRO A CD    1 
ATOM   1546 N N     . LEU A 1 211 ? 46.319 0.069   21.691  1.00 80.51  ?  211 LEU A N     1 
ATOM   1547 C CA    . LEU A 1 211 ? 45.269 -0.788  22.238  1.00 79.45  ?  211 LEU A CA    1 
ATOM   1548 C C     . LEU A 1 211 ? 45.847 -2.120  22.674  1.00 77.28  ?  211 LEU A C     1 
ATOM   1549 O O     . LEU A 1 211 ? 45.606 -2.586  23.792  1.00 76.82  ?  211 LEU A O     1 
ATOM   1550 C CB    . LEU A 1 211 ? 44.177 -0.998  21.201  1.00 74.09  ?  211 LEU A CB    1 
ATOM   1551 C CG    . LEU A 1 211 ? 43.086 0.043   21.011  1.00 79.01  ?  211 LEU A CG    1 
ATOM   1552 C CD1   . LEU A 1 211 ? 43.650 1.456   20.761  1.00 84.83  ?  211 LEU A CD1   1 
ATOM   1553 C CD2   . LEU A 1 211 ? 42.213 -0.416  19.856  1.00 75.77  ?  211 LEU A CD2   1 
ATOM   1554 N N     . LEU A 1 212 ? 46.664 -2.718  21.810  1.00 78.14  ?  212 LEU A N     1 
ATOM   1555 C CA    . LEU A 1 212 ? 47.297 -3.989  22.142  1.00 81.85  ?  212 LEU A CA    1 
ATOM   1556 C C     . LEU A 1 212 ? 48.222 -3.842  23.346  1.00 79.20  ?  212 LEU A C     1 
ATOM   1557 O O     . LEU A 1 212 ? 48.218 -4.695  24.242  1.00 79.98  ?  212 LEU A O     1 
ATOM   1558 C CB    . LEU A 1 212 ? 48.064 -4.547  20.929  1.00 76.76  ?  212 LEU A CB    1 
ATOM   1559 C CG    . LEU A 1 212 ? 47.400 -4.858  19.574  1.00 71.13  ?  212 LEU A CG    1 
ATOM   1560 C CD1   . LEU A 1 212 ? 48.472 -5.297  18.646  1.00 68.06  ?  212 LEU A CD1   1 
ATOM   1561 C CD2   . LEU A 1 212 ? 46.322 -5.931  19.634  1.00 65.91  ?  212 LEU A CD2   1 
ATOM   1562 N N     . ARG A 1 213 ? 49.026 -2.776  23.382  1.00 79.01  ?  213 ARG A N     1 
ATOM   1563 C CA    . ARG A 1 213 ? 49.833 -2.532  24.571  1.00 83.98  ?  213 ARG A CA    1 
ATOM   1564 C C     . ARG A 1 213 ? 48.934 -2.313  25.791  1.00 91.47  ?  213 ARG A C     1 
ATOM   1565 O O     . ARG A 1 213 ? 49.227 -2.815  26.894  1.00 86.12  ?  213 ARG A O     1 
ATOM   1566 C CB    . ARG A 1 213 ? 50.778 -1.348  24.335  1.00 82.17  ?  213 ARG A CB    1 
ATOM   1567 C CG    . ARG A 1 213 ? 52.082 -1.716  23.644  1.00 85.13  ?  213 ARG A CG    1 
ATOM   1568 C CD    . ARG A 1 213 ? 53.152 -0.636  23.829  1.00 90.76  ?  213 ARG A CD    1 
ATOM   1569 N NE    . ARG A 1 213 ? 52.599 0.652   23.449  1.00 87.61  ?  213 ARG A NE    1 
ATOM   1570 C CZ    . ARG A 1 213 ? 52.632 1.165   22.224  1.00 89.25  ?  213 ARG A CZ    1 
ATOM   1571 N NH1   . ARG A 1 213 ? 53.350 0.618   21.253  1.00 86.05  ?  213 ARG A NH1   1 
ATOM   1572 N NH2   . ARG A 1 213 ? 51.920 2.253   21.965  1.00 84.94  ?  213 ARG A NH2   1 
ATOM   1573 N N     . GLY A 1 214 ? 47.807 -1.614  25.592  1.00 88.38  ?  214 GLY A N     1 
ATOM   1574 C CA    . GLY A 1 214 ? 46.798 -1.399  26.619  1.00 85.16  ?  214 GLY A CA    1 
ATOM   1575 C C     . GLY A 1 214 ? 46.138 -2.667  27.102  1.00 86.50  ?  214 GLY A C     1 
ATOM   1576 O O     . GLY A 1 214 ? 45.312 -2.624  28.021  1.00 88.92  ?  214 GLY A O     1 
ATOM   1577 N N     . ALA A 1 215 ? 46.453 -3.785  26.469  1.00 87.07  ?  215 ALA A N     1 
ATOM   1578 C CA    . ALA A 1 215 ? 46.026 -5.100  26.908  1.00 82.72  ?  215 ALA A CA    1 
ATOM   1579 C C     . ALA A 1 215 ? 47.214 -5.972  27.299  1.00 82.20  ?  215 ALA A C     1 
ATOM   1580 O O     . ALA A 1 215 ? 47.086 -7.204  27.374  1.00 79.50  ?  215 ALA A O     1 
ATOM   1581 C CB    . ALA A 1 215 ? 45.201 -5.764  25.808  1.00 79.23  ?  215 ALA A CB    1 
ATOM   1582 N N     . GLY A 1 216 ? 48.376 -5.364  27.521  1.00 81.41  ?  216 GLY A N     1 
ATOM   1583 C CA    . GLY A 1 216 ? 49.549 -6.183  27.753  1.00 81.01  ?  216 GLY A CA    1 
ATOM   1584 C C     . GLY A 1 216 ? 49.841 -7.172  26.642  1.00 81.03  ?  216 GLY A C     1 
ATOM   1585 O O     . GLY A 1 216 ? 50.149 -8.337  26.926  1.00 88.31  ?  216 GLY A O     1 
ATOM   1586 N N     . LEU A 1 217 ? 49.728 -6.739  25.377  1.00 79.67  ?  217 LEU A N     1 
ATOM   1587 C CA    . LEU A 1 217 ? 50.133 -7.516  24.204  1.00 79.17  ?  217 LEU A CA    1 
ATOM   1588 C C     . LEU A 1 217 ? 51.016 -6.670  23.291  1.00 81.76  ?  217 LEU A C     1 
ATOM   1589 O O     . LEU A 1 217 ? 50.604 -5.583  22.873  1.00 84.96  ?  217 LEU A O     1 
ATOM   1590 C CB    . LEU A 1 217 ? 48.911 -7.987  23.413  1.00 74.61  ?  217 LEU A CB    1 
ATOM   1591 C CG    . LEU A 1 217 ? 47.854 -8.751  24.198  1.00 78.40  ?  217 LEU A CG    1 
ATOM   1592 C CD1   . LEU A 1 217 ? 46.545 -8.851  23.408  1.00 72.59  ?  217 LEU A CD1   1 
ATOM   1593 C CD2   . LEU A 1 217 ? 48.382 -10.125 24.564  1.00 74.25  ?  217 LEU A CD2   1 
ATOM   1594 N N     . TRP A 1 218 ? 52.216 -7.169  22.968  1.00 75.26  ?  218 TRP A N     1 
ATOM   1595 C CA    . TRP A 1 218 ? 53.047 -6.566  21.924  1.00 75.91  ?  218 TRP A CA    1 
ATOM   1596 C C     . TRP A 1 218 ? 52.559 -7.005  20.552  1.00 72.57  ?  218 TRP A C     1 
ATOM   1597 O O     . TRP A 1 218 ? 52.364 -8.195  20.310  1.00 72.14  ?  218 TRP A O     1 
ATOM   1598 C CB    . TRP A 1 218 ? 54.511 -6.984  22.063  1.00 74.93  ?  218 TRP A CB    1 
ATOM   1599 C CG    . TRP A 1 218 ? 55.173 -6.637  23.347  1.00 85.05  ?  218 TRP A CG    1 
ATOM   1600 C CD1   . TRP A 1 218 ? 54.689 -5.842  24.336  1.00 85.95  ?  218 TRP A CD1   1 
ATOM   1601 C CD2   . TRP A 1 218 ? 56.464 -7.073  23.779  1.00 86.45  ?  218 TRP A CD2   1 
ATOM   1602 N NE1   . TRP A 1 218 ? 55.599 -5.759  25.361  1.00 87.11  ?  218 TRP A NE1   1 
ATOM   1603 C CE2   . TRP A 1 218 ? 56.700 -6.503  25.040  1.00 85.32  ?  218 TRP A CE2   1 
ATOM   1604 C CE3   . TRP A 1 218 ? 57.444 -7.877  23.216  1.00 84.11  ?  218 TRP A CE3   1 
ATOM   1605 C CZ2   . TRP A 1 218 ? 57.869 -6.722  25.751  1.00 87.99  ?  218 TRP A CZ2   1 
ATOM   1606 C CZ3   . TRP A 1 218 ? 58.608 -8.096  23.931  1.00 89.73  ?  218 TRP A CZ3   1 
ATOM   1607 C CH2   . TRP A 1 218 ? 58.809 -7.525  25.182  1.00 89.25  ?  218 TRP A CH2   1 
ATOM   1608 N N     . LEU A 1 219 ? 52.401 -6.071  19.635  1.00 68.99  ?  219 LEU A N     1 
ATOM   1609 C CA    . LEU A 1 219 ? 52.082 -6.493  18.280  1.00 70.36  ?  219 LEU A CA    1 
ATOM   1610 C C     . LEU A 1 219 ? 53.226 -7.312  17.676  1.00 74.27  ?  219 LEU A C     1 
ATOM   1611 O O     . LEU A 1 219 ? 54.400 -7.131  18.019  1.00 75.70  ?  219 LEU A O     1 
ATOM   1612 C CB    . LEU A 1 219 ? 51.797 -5.296  17.397  1.00 65.93  ?  219 LEU A CB    1 
ATOM   1613 C CG    . LEU A 1 219 ? 51.464 -5.696  15.988  1.00 64.58  ?  219 LEU A CG    1 
ATOM   1614 C CD1   . LEU A 1 219 ? 50.181 -6.493  16.033  1.00 67.64  ?  219 LEU A CD1   1 
ATOM   1615 C CD2   . LEU A 1 219 ? 51.314 -4.476  15.160  1.00 61.16  ?  219 LEU A CD2   1 
ATOM   1616 N N     . GLU A 1 220 ? 52.867 -8.252  16.794  1.00 67.29  ?  220 GLU A N     1 
ATOM   1617 C CA    . GLU A 1 220 ? 53.832 -9.061  16.064  1.00 65.22  ?  220 GLU A CA    1 
ATOM   1618 C C     . GLU A 1 220 ? 53.791 -8.824  14.568  1.00 65.25  ?  220 GLU A C     1 
ATOM   1619 O O     . GLU A 1 220 ? 54.841 -8.862  13.922  1.00 64.40  ?  220 GLU A O     1 
ATOM   1620 C CB    . GLU A 1 220 ? 53.601 -10.557 16.354  1.00 63.27  ?  220 GLU A CB    1 
ATOM   1621 C CG    . GLU A 1 220 ? 54.330 -11.518 15.437  1.00 72.23  ?  220 GLU A CG    1 
ATOM   1622 C CD    . GLU A 1 220 ? 54.650 -12.842 16.097  1.00 77.14  ?  220 GLU A CD    1 
ATOM   1623 O OE1   . GLU A 1 220 ? 54.325 -13.037 17.286  1.00 67.22  ?  220 GLU A OE1   1 
ATOM   1624 O OE2   . GLU A 1 220 ? 55.249 -13.692 15.412  1.00 86.20  -1 220 GLU A OE2   1 
ATOM   1625 N N     . GLU A 1 221 ? 52.615 -8.527  14.017  1.00 60.49  ?  221 GLU A N     1 
ATOM   1626 C CA    . GLU A 1 221 ? 52.446 -8.483  12.567  1.00 62.53  ?  221 GLU A CA    1 
ATOM   1627 C C     . GLU A 1 221 ? 51.176 -7.730  12.204  1.00 61.90  ?  221 GLU A C     1 
ATOM   1628 O O     . GLU A 1 221 ? 50.083 -8.119  12.647  1.00 64.76  ?  221 GLU A O     1 
ATOM   1629 C CB    . GLU A 1 221 ? 52.394 -9.907  12.036  1.00 67.40  ?  221 GLU A CB    1 
ATOM   1630 C CG    . GLU A 1 221 ? 52.177 -10.058 10.550  1.00 61.85  ?  221 GLU A CG    1 
ATOM   1631 C CD    . GLU A 1 221 ? 52.032 -11.521 10.147  1.00 65.44  ?  221 GLU A CD    1 
ATOM   1632 O OE1   . GLU A 1 221 ? 52.253 -12.411 11.013  1.00 73.25  ?  221 GLU A OE1   1 
ATOM   1633 O OE2   . GLU A 1 221 ? 51.684 -11.772 8.971   1.00 61.67  -1 221 GLU A OE2   1 
ATOM   1634 N N     . PHE A 1 222 ? 51.321 -6.656  11.414  1.00 62.29  ?  222 PHE A N     1 
ATOM   1635 C CA    . PHE A 1 222 ? 50.199 -5.917  10.839  1.00 62.84  ?  222 PHE A CA    1 
ATOM   1636 C C     . PHE A 1 222 ? 50.252 -6.094  9.338   1.00 65.27  ?  222 PHE A C     1 
ATOM   1637 O O     . PHE A 1 222 ? 51.315 -5.916  8.738   1.00 67.33  ?  222 PHE A O     1 
ATOM   1638 C CB    . PHE A 1 222 ? 50.212 -4.410  11.146  1.00 58.44  ?  222 PHE A CB    1 
ATOM   1639 C CG    . PHE A 1 222 ? 49.029 -3.673  10.554  1.00 61.46  ?  222 PHE A CG    1 
ATOM   1640 C CD1   . PHE A 1 222 ? 49.061 -3.198  9.258   1.00 59.90  ?  222 PHE A CD1   1 
ATOM   1641 C CD2   . PHE A 1 222 ? 47.882 -3.483  11.287  1.00 63.12  ?  222 PHE A CD2   1 
ATOM   1642 C CE1   . PHE A 1 222 ? 47.987 -2.556  8.707   1.00 60.18  ?  222 PHE A CE1   1 
ATOM   1643 C CE2   . PHE A 1 222 ? 46.804 -2.834  10.742  1.00 67.98  ?  222 PHE A CE2   1 
ATOM   1644 C CZ    . PHE A 1 222 ? 46.857 -2.376  9.439   1.00 67.50  ?  222 PHE A CZ    1 
ATOM   1645 N N     . LEU A 1 223 ? 49.096 -6.381  8.731   1.00 63.36  ?  223 LEU A N     1 
ATOM   1646 C CA    . LEU A 1 223 ? 49.051 -6.837  7.340   1.00 62.16  ?  223 LEU A CA    1 
ATOM   1647 C C     . LEU A 1 223 ? 47.800 -6.274  6.671   1.00 66.73  ?  223 LEU A C     1 
ATOM   1648 O O     . LEU A 1 223 ? 46.690 -6.769  6.902   1.00 65.46  ?  223 LEU A O     1 
ATOM   1649 C CB    . LEU A 1 223 ? 49.068 -8.357  7.276   1.00 60.50  ?  223 LEU A CB    1 
ATOM   1650 C CG    . LEU A 1 223 ? 49.519 -9.091  6.012   1.00 65.16  ?  223 LEU A CG    1 
ATOM   1651 C CD1   . LEU A 1 223 ? 50.583 -8.271  5.290   1.00 61.48  ?  223 LEU A CD1   1 
ATOM   1652 C CD2   . LEU A 1 223 ? 50.057 -10.491 6.387   1.00 59.90  ?  223 LEU A CD2   1 
ATOM   1653 N N     . ASP A 1 224 ? 47.982 -5.247  5.846   1.00 66.86  ?  224 ASP A N     1 
ATOM   1654 C CA    . ASP A 1 224 ? 46.882 -4.731  5.052   1.00 64.60  ?  224 ASP A CA    1 
ATOM   1655 C C     . ASP A 1 224 ? 46.604 -5.770  3.988   1.00 66.11  ?  224 ASP A C     1 
ATOM   1656 O O     . ASP A 1 224 ? 47.439 -5.988  3.108   1.00 70.12  ?  224 ASP A O     1 
ATOM   1657 C CB    . ASP A 1 224 ? 47.259 -3.375  4.459   1.00 67.07  ?  224 ASP A CB    1 
ATOM   1658 C CG    . ASP A 1 224 ? 46.114 -2.708  3.712   1.00 71.06  ?  224 ASP A CG    1 
ATOM   1659 O OD1   . ASP A 1 224 ? 45.047 -3.328  3.568   1.00 70.39  ?  224 ASP A OD1   1 
ATOM   1660 O OD2   . ASP A 1 224 ? 46.286 -1.553  3.257   1.00 77.24  -1 224 ASP A OD2   1 
ATOM   1661 N N     . ILE A 1 225 ? 45.477 -6.467  4.094   1.00 62.67  ?  225 ILE A N     1 
ATOM   1662 C CA    . ILE A 1 225 ? 45.134 -7.495  3.119   1.00 65.38  ?  225 ILE A CA    1 
ATOM   1663 C C     . ILE A 1 225 ? 44.028 -7.020  2.174   1.00 72.18  ?  225 ILE A C     1 
ATOM   1664 O O     . ILE A 1 225 ? 43.478 -7.823  1.402   1.00 71.03  ?  225 ILE A O     1 
ATOM   1665 C CB    . ILE A 1 225 ? 44.758 -8.815  3.805   1.00 61.22  ?  225 ILE A CB    1 
ATOM   1666 C CG1   . ILE A 1 225 ? 43.484 -8.637  4.633   1.00 61.47  ?  225 ILE A CG1   1 
ATOM   1667 C CG2   . ILE A 1 225 ? 45.916 -9.284  4.632   1.00 59.62  ?  225 ILE A CG2   1 
ATOM   1668 C CD1   . ILE A 1 225 ? 43.047 -9.878  5.388   1.00 63.23  ?  225 ILE A CD1   1 
ATOM   1669 N N     . SER A 1 226 ? 43.735 -5.714  2.187   1.00 70.39  ?  226 SER A N     1 
ATOM   1670 C CA    . SER A 1 226 ? 42.557 -5.205  1.495   1.00 67.06  ?  226 SER A CA    1 
ATOM   1671 C C     . SER A 1 226 ? 42.546 -5.633  0.040   1.00 69.80  ?  226 SER A C     1 
ATOM   1672 O O     . SER A 1 226 ? 41.514 -6.076  -0.474  1.00 68.70  ?  226 SER A O     1 
ATOM   1673 C CB    . SER A 1 226 ? 42.493 -3.680  1.604   1.00 67.67  ?  226 SER A CB    1 
ATOM   1674 O OG    . SER A 1 226 ? 42.459 -3.260  2.956   1.00 73.15  ?  226 SER A OG    1 
ATOM   1675 N N     . ASP A 1 227 ? 43.691 -5.549  -0.634  1.00 71.55  ?  227 ASP A N     1 
ATOM   1676 C CA    . ASP A 1 227 ? 43.696 -5.766  -2.075  1.00 72.61  ?  227 ASP A CA    1 
ATOM   1677 C C     . ASP A 1 227 ? 43.506 -7.229  -2.449  1.00 71.16  ?  227 ASP A C     1 
ATOM   1678 O O     . ASP A 1 227 ? 43.325 -7.520  -3.635  1.00 73.04  ?  227 ASP A O     1 
ATOM   1679 C CB    . ASP A 1 227 ? 44.992 -5.223  -2.686  1.00 74.63  ?  227 ASP A CB    1 
ATOM   1680 C CG    . ASP A 1 227 ? 45.104 -3.680  -2.610  1.00 78.94  ?  227 ASP A CG    1 
ATOM   1681 O OD1   . ASP A 1 227 ? 44.058 -2.979  -2.727  1.00 76.11  ?  227 ASP A OD1   1 
ATOM   1682 O OD2   . ASP A 1 227 ? 46.259 -3.184  -2.449  1.00 82.43  -1 227 ASP A OD2   1 
ATOM   1683 N N     . GLN A 1 228 ? 43.538 -8.139  -1.472  1.00 70.75  ?  228 GLN A N     1 
ATOM   1684 C CA    . GLN A 1 228 ? 43.302 -9.568  -1.673  1.00 69.35  ?  228 GLN A CA    1 
ATOM   1685 C C     . GLN A 1 228 ? 41.884 -10.021 -1.330  1.00 67.69  ?  228 GLN A C     1 
ATOM   1686 O O     . GLN A 1 228 ? 41.483 -11.121 -1.733  1.00 64.88  ?  228 GLN A O     1 
ATOM   1687 C CB    . GLN A 1 228 ? 44.264 -10.394 -0.809  1.00 69.18  ?  228 GLN A CB    1 
ATOM   1688 C CG    . GLN A 1 228 ? 45.718 -10.334 -1.191  1.00 68.10  ?  228 GLN A CG    1 
ATOM   1689 C CD    . GLN A 1 228 ? 46.365 -9.002  -0.868  1.00 74.20  ?  228 GLN A CD    1 
ATOM   1690 O OE1   . GLN A 1 228 ? 46.839 -8.726  0.262   1.00 70.33  ?  228 GLN A OE1   1 
ATOM   1691 N NE2   . GLN A 1 228 ? 46.402 -8.161  -1.879  1.00 77.29  ?  228 GLN A NE2   1 
ATOM   1692 N N     . THR A 1 229 ? 41.132 -9.226  -0.567  1.00 70.52  ?  229 THR A N     1 
ATOM   1693 C CA    . THR A 1 229 ? 39.923 -9.701  0.090   1.00 63.32  ?  229 THR A CA    1 
ATOM   1694 C C     . THR A 1 229 ? 38.660 -9.017  -0.408  1.00 65.37  ?  229 THR A C     1 
ATOM   1695 O O     . THR A 1 229 ? 37.767 -9.691  -0.940  1.00 64.81  ?  229 THR A O     1 
ATOM   1696 C CB    . THR A 1 229 ? 40.087 -9.472  1.596   1.00 67.45  ?  229 THR A CB    1 
ATOM   1697 O OG1   . THR A 1 229 ? 40.805 -8.247  1.808   1.00 65.58  ?  229 THR A OG1   1 
ATOM   1698 C CG2   . THR A 1 229 ? 40.849 -10.623 2.256   1.00 62.55  ?  229 THR A CG2   1 
ATOM   1699 N N     . LEU A 1 230 ? 38.593 -7.684  -0.289  1.00 68.99  ?  230 LEU A N     1 
ATOM   1700 C CA    . LEU A 1 230 ? 37.324 -6.963  -0.323  1.00 64.29  ?  230 LEU A CA    1 
ATOM   1701 C C     . LEU A 1 230 ? 36.677 -7.029  -1.701  1.00 69.49  ?  230 LEU A C     1 
ATOM   1702 O O     . LEU A 1 230 ? 35.480 -7.325  -1.812  1.00 69.37  ?  230 LEU A O     1 
ATOM   1703 C CB    . LEU A 1 230 ? 37.538 -5.512  0.127   1.00 59.14  ?  230 LEU A CB    1 
ATOM   1704 C CG    . LEU A 1 230 ? 38.061 -5.323  1.561   1.00 61.87  ?  230 LEU A CG    1 
ATOM   1705 C CD1   . LEU A 1 230 ? 38.869 -4.062  1.789   1.00 57.77  ?  230 LEU A CD1   1 
ATOM   1706 C CD2   . LEU A 1 230 ? 36.898 -5.327  2.511   1.00 63.28  ?  230 LEU A CD2   1 
ATOM   1707 N N     . GLU A 1 231 ? 37.461 -6.809  -2.770  1.00 72.59  ?  231 GLU A N     1 
ATOM   1708 C CA    . GLU A 1 231 ? 36.877 -6.497  -4.080  1.00 69.49  ?  231 GLU A CA    1 
ATOM   1709 C C     . GLU A 1 231 ? 36.209 -7.706  -4.719  1.00 69.85  ?  231 GLU A C     1 
ATOM   1710 O O     . GLU A 1 231 ? 35.035 -7.650  -5.102  1.00 73.02  ?  231 GLU A O     1 
ATOM   1711 C CB    . GLU A 1 231 ? 37.931 -5.956  -5.027  1.00 79.79  ?  231 GLU A CB    1 
ATOM   1712 C CG    . GLU A 1 231 ? 37.498 -6.138  -6.450  1.00 80.37  ?  231 GLU A CG    1 
ATOM   1713 C CD    . GLU A 1 231 ? 37.953 -5.016  -7.330  1.00 88.75  ?  231 GLU A CD    1 
ATOM   1714 O OE1   . GLU A 1 231 ? 38.853 -4.256  -6.895  1.00 93.56  ?  231 GLU A OE1   1 
ATOM   1715 O OE2   . GLU A 1 231 ? 37.402 -4.896  -8.450  1.00 95.07  -1 231 GLU A OE2   1 
ATOM   1716 N N     . LYS A 1 232 ? 36.957 -8.800  -4.882  1.00 69.09  ?  232 LYS A N     1 
ATOM   1717 C CA    . LYS A 1 232 ? 36.393 -10.005 -5.488  1.00 71.99  ?  232 LYS A CA    1 
ATOM   1718 C C     . LYS A 1 232 ? 35.188 -10.501 -4.704  1.00 73.03  ?  232 LYS A C     1 
ATOM   1719 O O     . LYS A 1 232 ? 34.199 -10.953 -5.291  1.00 72.32  ?  232 LYS A O     1 
ATOM   1720 C CB    . LYS A 1 232 ? 37.464 -11.089 -5.563  1.00 65.36  ?  232 LYS A CB    1 
ATOM   1721 C CG    . LYS A 1 232 ? 37.513 -11.844 -6.876  1.00 76.54  ?  232 LYS A CG    1 
ATOM   1722 C CD    . LYS A 1 232 ? 38.888 -12.472 -7.071  1.00 76.74  ?  232 LYS A CD    1 
ATOM   1723 C CE    . LYS A 1 232 ? 39.019 -13.028 -8.466  1.00 82.32  ?  232 LYS A CE    1 
ATOM   1724 N NZ    . LYS A 1 232 ? 38.016 -14.099 -8.754  1.00 81.21  ?  232 LYS A NZ    1 
ATOM   1725 N N     . THR A 1 233 ? 35.262 -10.423 -3.373  1.00 70.45  ?  233 THR A N     1 
ATOM   1726 C CA    . THR A 1 233 ? 34.151 -10.833 -2.524  1.00 70.57  ?  233 THR A CA    1 
ATOM   1727 C C     . THR A 1 233 ? 32.893 -10.035 -2.830  1.00 74.46  ?  233 THR A C     1 
ATOM   1728 O O     . THR A 1 233 ? 31.813 -10.597 -3.045  1.00 78.16  ?  233 THR A O     1 
ATOM   1729 C CB    . THR A 1 233 ? 34.523 -10.658 -1.053  1.00 70.00  ?  233 THR A CB    1 
ATOM   1730 O OG1   . THR A 1 233 ? 35.678 -11.449 -0.727  1.00 69.69  ?  233 THR A OG1   1 
ATOM   1731 C CG2   . THR A 1 233 ? 33.346 -11.051 -0.183  1.00 69.50  ?  233 THR A CG2   1 
ATOM   1732 N N     . PHE A 1 234 ? 33.003 -8.715  -2.834  1.00 72.99  ?  234 PHE A N     1 
ATOM   1733 C CA    . PHE A 1 234 ? 31.805 -7.920  -3.042  1.00 79.60  ?  234 PHE A CA    1 
ATOM   1734 C C     . PHE A 1 234 ? 31.245 -8.138  -4.433  1.00 78.92  ?  234 PHE A C     1 
ATOM   1735 O O     . PHE A 1 234 ? 30.025 -8.251  -4.595  1.00 84.21  ?  234 PHE A O     1 
ATOM   1736 C CB    . PHE A 1 234 ? 32.105 -6.454  -2.784  1.00 80.42  ?  234 PHE A CB    1 
ATOM   1737 C CG    . PHE A 1 234 ? 32.424 -6.181  -1.371  1.00 76.31  ?  234 PHE A CG    1 
ATOM   1738 C CD1   . PHE A 1 234 ? 31.702 -6.790  -0.386  1.00 76.44  ?  234 PHE A CD1   1 
ATOM   1739 C CD2   . PHE A 1 234 ? 33.465 -5.360  -1.016  1.00 76.12  ?  234 PHE A CD2   1 
ATOM   1740 C CE1   . PHE A 1 234 ? 31.991 -6.566  0.930   1.00 76.83  ?  234 PHE A CE1   1 
ATOM   1741 C CE2   . PHE A 1 234 ? 33.761 -5.134  0.304   1.00 74.49  ?  234 PHE A CE2   1 
ATOM   1742 C CZ    . PHE A 1 234 ? 33.016 -5.732  1.278   1.00 75.90  ?  234 PHE A CZ    1 
ATOM   1743 N N     . ARG A 1 235 ? 32.115 -8.207  -5.445  1.00 75.49  ?  235 ARG A N     1 
ATOM   1744 C CA    . ARG A 1 235 ? 31.657 -8.582  -6.776  1.00 79.86  ?  235 ARG A CA    1 
ATOM   1745 C C     . ARG A 1 235 ? 30.861 -9.874  -6.700  1.00 83.10  ?  235 ARG A C     1 
ATOM   1746 O O     . ARG A 1 235 ? 29.669 -9.910  -7.021  1.00 85.04  ?  235 ARG A O     1 
ATOM   1747 C CB    . ARG A 1 235 ? 32.841 -8.741  -7.729  1.00 81.29  ?  235 ARG A CB    1 
ATOM   1748 C CG    . ARG A 1 235 ? 33.588 -7.473  -7.995  1.00 80.75  ?  235 ARG A CG    1 
ATOM   1749 C CD    . ARG A 1 235 ? 34.023 -7.406  -9.442  1.00 84.70  ?  235 ARG A CD    1 
ATOM   1750 N NE    . ARG A 1 235 ? 34.564 -6.093  -9.787  1.00 85.86  ?  235 ARG A NE    1 
ATOM   1751 C CZ    . ARG A 1 235 ? 34.271 -5.426  -10.896 1.00 86.07  ?  235 ARG A CZ    1 
ATOM   1752 N NH1   . ARG A 1 235 ? 33.389 -5.882  -11.774 1.00 81.91  ?  235 ARG A NH1   1 
ATOM   1753 N NH2   . ARG A 1 235 ? 34.877 -4.266  -11.131 1.00 92.77  ?  235 ARG A NH2   1 
ATOM   1754 N N     . LEU A 1 236 ? 31.495 -10.927 -6.180  1.00 82.31  ?  236 LEU A N     1 
ATOM   1755 C CA    . LEU A 1 236 ? 30.859 -12.236 -6.130  1.00 79.14  ?  236 LEU A CA    1 
ATOM   1756 C C     . LEU A 1 236 ? 29.566 -12.191 -5.335  1.00 81.74  ?  236 LEU A C     1 
ATOM   1757 O O     . LEU A 1 236 ? 28.568 -12.797 -5.734  1.00 90.12  ?  236 LEU A O     1 
ATOM   1758 C CB    . LEU A 1 236 ? 31.821 -13.266 -5.543  1.00 72.07  ?  236 LEU A CB    1 
ATOM   1759 C CG    . LEU A 1 236 ? 32.572 -14.134 -6.555  1.00 71.89  ?  236 LEU A CG    1 
ATOM   1760 C CD1   . LEU A 1 236 ? 33.110 -13.287 -7.713  1.00 76.92  ?  236 LEU A CD1   1 
ATOM   1761 C CD2   . LEU A 1 236 ? 33.692 -14.921 -5.872  1.00 68.60  ?  236 LEU A CD2   1 
ATOM   1762 N N     . LEU A 1 237 ? 29.551 -11.458 -4.223  1.00 84.92  ?  237 LEU A N     1 
ATOM   1763 C CA    . LEU A 1 237 ? 28.334 -11.361 -3.418  1.00 87.99  ?  237 LEU A CA    1 
ATOM   1764 C C     . LEU A 1 237 ? 27.209 -10.663 -4.175  1.00 90.45  ?  237 LEU A C     1 
ATOM   1765 O O     . LEU A 1 237 ? 26.049 -11.087 -4.110  1.00 93.06  ?  237 LEU A O     1 
ATOM   1766 C CB    . LEU A 1 237 ? 28.636 -10.629 -2.110  1.00 87.78  ?  237 LEU A CB    1 
ATOM   1767 C CG    . LEU A 1 237 ? 28.856 -11.586 -0.935  1.00 93.85  ?  237 LEU A CG    1 
ATOM   1768 C CD1   . LEU A 1 237 ? 29.710 -12.783 -1.366  1.00 91.48  ?  237 LEU A CD1   1 
ATOM   1769 C CD2   . LEU A 1 237 ? 29.469 -10.896 0.297   1.00 94.82  ?  237 LEU A CD2   1 
ATOM   1770 N N     . SER A 1 238 ? 27.544 -9.565  -4.850  1.00 88.22  ?  238 SER A N     1 
ATOM   1771 C CA    . SER A 1 238 ? 26.504 -8.759  -5.538  1.00 88.22  ?  238 SER A CA    1 
ATOM   1772 C C     . SER A 1 238 ? 25.777 -9.595  -6.585  1.00 92.66  ?  238 SER A C     1 
ATOM   1773 O O     . SER A 1 238 ? 24.543 -9.524  -6.628  1.00 95.68  ?  238 SER A O     1 
ATOM   1774 C CB    . SER A 1 238 ? 27.111 -7.555  -6.175  1.00 90.36  ?  238 SER A CB    1 
ATOM   1775 O OG    . SER A 1 238 ? 26.159 -6.897  -6.995  1.00 94.23  ?  238 SER A OG    1 
ATOM   1776 N N     . GLU A 1 239 ? 26.521 -10.321 -7.418  1.00 95.69  ?  239 GLU A N     1 
ATOM   1777 C CA    . GLU A 1 239 ? 25.858 -11.082 -8.504  1.00 97.91  ?  239 GLU A CA    1 
ATOM   1778 C C     . GLU A 1 239 ? 24.738 -11.904 -7.878  1.00 98.28  ?  239 GLU A C     1 
ATOM   1779 O O     . GLU A 1 239 ? 23.605 -11.785 -8.340  1.00 101.98 ?  239 GLU A O     1 
ATOM   1780 C CB    . GLU A 1 239 ? 26.824 -12.010 -9.235  1.00 98.53  ?  239 GLU A CB    1 
ATOM   1781 C CG    . GLU A 1 239 ? 28.285 -11.703 -8.998  1.00 98.84  ?  239 GLU A CG    1 
ATOM   1782 C CD    . GLU A 1 239 ? 28.972 -10.947 -10.121 1.00 105.63 ?  239 GLU A CD    1 
ATOM   1783 O OE1   . GLU A 1 239 ? 29.529 -11.606 -11.018 1.00 109.82 ?  239 GLU A OE1   1 
ATOM   1784 O OE2   . GLU A 1 239 ? 28.952 -9.701  -10.092 1.00 107.53 -1 239 GLU A OE2   1 
ATOM   1785 N N     . ARG A 1 240 ? 25.061 -12.694 -6.858  1.00 98.28  ?  240 ARG A N     1 
ATOM   1786 C CA    . ARG A 1 240 ? 24.046 -13.525 -6.163  1.00 100.47 ?  240 ARG A CA    1 
ATOM   1787 C C     . ARG A 1 240 ? 22.830 -12.662 -5.836  1.00 99.01  ?  240 ARG A C     1 
ATOM   1788 O O     . ARG A 1 240 ? 21.749 -12.943 -6.368  1.00 103.28 ?  240 ARG A O     1 
ATOM   1789 C CB    . ARG A 1 240 ? 24.658 -14.096 -4.885  1.00 96.78  ?  240 ARG A CB    1 
ATOM   1790 C CG    . ARG A 1 240 ? 23.675 -14.785 -3.951  1.00 99.26  ?  240 ARG A CG    1 
ATOM   1791 C CD    . ARG A 1 240 ? 24.448 -15.475 -2.845  1.00 103.44 ?  240 ARG A CD    1 
ATOM   1792 N NE    . ARG A 1 240 ? 25.685 -16.057 -3.348  1.00 103.99 ?  240 ARG A NE    1 
ATOM   1793 C CZ    . ARG A 1 240 ? 26.876 -15.900 -2.785  1.00 103.36 ?  240 ARG A CZ    1 
ATOM   1794 N NH1   . ARG A 1 240 ? 26.983 -15.835 -1.470  1.00 105.17 ?  240 ARG A NH1   1 
ATOM   1795 N NH2   . ARG A 1 240 ? 27.957 -15.810 -3.539  1.00 100.20 ?  240 ARG A NH2   1 
ATOM   1796 N N     . ILE A 1 241 ? 23.016 -11.656 -4.987  1.00 96.53  ?  241 ILE A N     1 
ATOM   1797 C CA    . ILE A 1 241 ? 21.884 -10.783 -4.574  1.00 96.78  ?  241 ILE A CA    1 
ATOM   1798 C C     . ILE A 1 241 ? 21.109 -10.363 -5.822  1.00 102.35 ?  241 ILE A C     1 
ATOM   1799 O O     . ILE A 1 241 ? 19.885 -10.560 -5.854  1.00 105.30 ?  241 ILE A O     1 
ATOM   1800 C CB    . ILE A 1 241 ? 22.413 -9.567  -3.798  1.00 95.30  ?  241 ILE A CB    1 
ATOM   1801 C CG1   . ILE A 1 241 ? 23.412 -9.987  -2.719  1.00 91.10  ?  241 ILE A CG1   1 
ATOM   1802 C CG2   . ILE A 1 241 ? 21.265 -8.755  -3.224  1.00 90.78  ?  241 ILE A CG2   1 
ATOM   1803 C CD1   . ILE A 1 241 ? 23.440 -9.074  -1.520  1.00 86.98  ?  241 ILE A CD1   1 
ATOM   1804 N N     . ASN A 1 242 ? 21.802 -9.804  -6.809  1.00 97.36  ?  242 ASN A N     1 
ATOM   1805 C CA    . ASN A 1 242 ? 21.103 -9.305  -8.018  1.00 103.02 ?  242 ASN A CA    1 
ATOM   1806 C C     . ASN A 1 242 ? 20.410 -10.481 -8.711  1.00 112.78 ?  242 ASN A C     1 
ATOM   1807 O O     . ASN A 1 242 ? 19.198 -10.388 -8.957  1.00 118.23 ?  242 ASN A O     1 
ATOM   1808 C CB    . ASN A 1 242 ? 22.057 -8.568  -8.958  1.00 99.13  ?  242 ASN A CB    1 
ATOM   1809 N N     . SER A 1 243 ? 21.160 -11.538 -9.018  1.00 109.21 ?  243 SER A N     1 
ATOM   1810 C CA    . SER A 1 243 ? 20.578 -12.737 -9.672  1.00 110.23 ?  243 SER A CA    1 
ATOM   1811 C C     . SER A 1 243 ? 19.331 -13.162 -8.902  1.00 114.88 ?  243 SER A C     1 
ATOM   1812 O O     . SER A 1 243 ? 18.273 -13.312 -9.527  1.00 120.61 ?  243 SER A O     1 
ATOM   1813 C CB    . SER A 1 243 ? 21.580 -13.852 -9.722  1.00 110.86 ?  243 SER A CB    1 
ATOM   1814 O OG    . SER A 1 243 ? 22.836 -13.384 -10.189 1.00 109.22 ?  243 SER A OG    1 
ATOM   1815 N N     . SER A 1 244 ? 19.469 -13.340 -7.590  1.00 115.60 ?  244 SER A N     1 
ATOM   1816 C CA    . SER A 1 244 ? 18.321 -13.753 -6.747  1.00 120.07 ?  244 SER A CA    1 
ATOM   1817 C C     . SER A 1 244 ? 17.114 -12.856 -7.032  1.00 123.99 ?  244 SER A C     1 
ATOM   1818 O O     . SER A 1 244 ? 16.020 -13.394 -7.246  1.00 126.12 ?  244 SER A O     1 
ATOM   1819 C CB    . SER A 1 244 ? 18.690 -13.723 -5.287  1.00 114.49 ?  244 SER A CB    1 
ATOM   1820 O OG    . SER A 1 244 ? 18.487 -12.430 -4.737  1.00 115.01 ?  244 SER A OG    1 
ATOM   1821 N N     . LYS A 1 245 ? 17.304 -11.538 -7.003  1.00 119.64 ?  245 LYS A N     1 
ATOM   1822 C CA    . LYS A 1 245 ? 16.158 -10.616 -7.195  1.00 119.78 ?  245 LYS A CA    1 
ATOM   1823 C C     . LYS A 1 245 ? 15.501 -10.932 -8.538  1.00 130.48 ?  245 LYS A C     1 
ATOM   1824 O O     . LYS A 1 245 ? 14.270 -11.059 -8.579  1.00 130.97 ?  245 LYS A O     1 
ATOM   1825 C CB    . LYS A 1 245 ? 16.642 -9.166  -7.146  1.00 114.84 ?  245 LYS A CB    1 
ATOM   1826 N N     . GLN A 1 246 ? 16.305 -11.049 -9.593  1.00 128.84 ?  246 GLN A N     1 
ATOM   1827 C CA    . GLN A 1 246 ? 15.755 -11.326 -10.944 1.00 130.81 ?  246 GLN A CA    1 
ATOM   1828 C C     . GLN A 1 246 ? 15.141 -12.724 -10.942 1.00 134.85 ?  246 GLN A C     1 
ATOM   1829 O O     . GLN A 1 246 ? 14.167 -12.939 -11.675 1.00 137.52 ?  246 GLN A O     1 
ATOM   1830 C CB    . GLN A 1 246 ? 16.859 -11.218 -11.993 1.00 126.62 ?  246 GLN A CB    1 
ATOM   1831 C CG    . GLN A 1 246 ? 17.604 -9.891  -11.957 1.00 133.04 ?  246 GLN A CG    1 
ATOM   1832 C CD    . GLN A 1 246 ? 16.699 -8.724  -11.643 1.00 138.40 ?  246 GLN A CD    1 
ATOM   1833 O OE1   . GLN A 1 246 ? 16.792 -8.113  -10.581 1.00 135.94 ?  246 GLN A OE1   1 
ATOM   1834 N NE2   . GLN A 1 246 ? 15.813 -8.403  -12.572 1.00 138.44 ?  246 GLN A NE2   1 
ATOM   1835 N N     . ARG A 1 247 ? 15.702 -13.634 -10.147 1.00 131.00 ?  247 ARG A N     1 
ATOM   1836 C CA    . ARG A 1 247 ? 15.128 -14.995 -10.026 1.00 131.99 ?  247 ARG A CA    1 
ATOM   1837 C C     . ARG A 1 247 ? 13.783 -14.883 -9.311  1.00 135.66 ?  247 ARG A C     1 
ATOM   1838 O O     . ARG A 1 247 ? 12.942 -15.756 -9.521  1.00 138.66 ?  247 ARG A O     1 
ATOM   1839 C CB    . ARG A 1 247 ? 16.063 -15.899 -9.224  1.00 126.71 ?  247 ARG A CB    1 
ATOM   1840 C CG    . ARG A 1 247 ? 17.079 -16.654 -10.067 1.00 124.76 ?  247 ARG A CG    1 
ATOM   1841 C CD    . ARG A 1 247 ? 18.281 -17.066 -9.239  1.00 117.32 ?  247 ARG A CD    1 
ATOM   1842 N NE    . ARG A 1 247 ? 19.516 -17.031 -10.007 1.00 117.44 ?  247 ARG A NE    1 
ATOM   1843 C CZ    . ARG A 1 247 ? 19.595 -17.265 -11.311 1.00 120.95 ?  247 ARG A CZ    1 
ATOM   1844 N NH1   . ARG A 1 247 ? 19.409 -18.488 -11.775 1.00 123.17 ?  247 ARG A NH1   1 
ATOM   1845 N NH2   . ARG A 1 247 ? 19.861 -16.276 -12.147 1.00 115.67 ?  247 ARG A NH2   1 
ATOM   1846 N N     . LEU A 1 248 ? 13.604 -13.853 -8.487  1.00 137.88 ?  248 LEU A N     1 
ATOM   1847 C CA    . LEU A 1 248 ? 12.302 -13.642 -7.807  1.00 136.15 ?  248 LEU A CA    1 
ATOM   1848 C C     . LEU A 1 248 ? 11.416 -12.781 -8.710  1.00 139.47 ?  248 LEU A C     1 
ATOM   1849 O O     . LEU A 1 248 ? 10.907 -11.753 -8.229  1.00 140.61 ?  248 LEU A O     1 
ATOM   1850 C CB    . LEU A 1 248 ? 12.553 -12.957 -6.463  1.00 132.34 ?  248 LEU A CB    1 
ATOM   1851 C CG    . LEU A 1 248 ? 12.555 -13.879 -5.246  1.00 134.08 ?  248 LEU A CG    1 
ATOM   1852 C CD1   . LEU A 1 248 ? 13.706 -14.872 -5.312  1.00 128.32 ?  248 LEU A CD1   1 
ATOM   1853 C CD2   . LEU A 1 248 ? 12.622 -13.070 -3.962  1.00 134.02 ?  248 LEU A CD2   1 
ATOM   1854 N N     . GLU A 1 249 ? 11.262 -13.182 -9.975  1.00 143.03 ?  249 GLU A N     1 
ATOM   1855 C CA    . GLU A 1 249 ? 10.382 -12.442 -10.914 1.00 136.59 ?  249 GLU A CA    1 
ATOM   1856 C C     . GLU A 1 249 ? 9.002  -13.100 -10.897 1.00 142.48 ?  249 GLU A C     1 
ATOM   1857 O O     . GLU A 1 249 ? 8.078  -12.555 -11.526 1.00 138.33 ?  249 GLU A O     1 
ATOM   1858 C CB    . GLU A 1 249 ? 10.970 -12.461 -12.324 1.00 131.37 ?  249 GLU A CB    1 
ATOM   1859 C CG    . GLU A 1 249 ? 11.121 -13.854 -12.898 1.00 136.40 ?  249 GLU A CG    1 
ATOM   1860 C CD    . GLU A 1 249 ? 11.856 -13.886 -14.226 1.00 137.74 ?  249 GLU A CD    1 
ATOM   1861 O OE1   . GLU A 1 249 ? 12.838 -13.135 -14.371 1.00 137.18 ?  249 GLU A OE1   1 
ATOM   1862 O OE2   . GLU A 1 249 ? 11.440 -14.655 -15.112 1.00 144.55 ?  249 GLU A OE2   1 
ATOM   1863 N N     . THR A 1 250 ? 8.890  -14.241 -10.215 1.00 139.96 ?  250 THR A N     1 
ATOM   1864 C CA    . THR A 1 250 ? 7.606  -14.985 -10.178 1.00 138.59 ?  250 THR A CA    1 
ATOM   1865 C C     . THR A 1 250 ? 7.136  -15.102 -8.726  1.00 135.20 ?  250 THR A C     1 
ATOM   1866 O O     . THR A 1 250 ? 7.749  -14.423 -7.880  1.00 136.18 ?  250 THR A O     1 
ATOM   1867 C CB    . THR A 1 250 ? 7.779  -16.356 -10.835 1.00 30.00  ?  250 THR A CB    1 
ATOM   1868 O OG1   . THR A 1 250 ? 9.030  -16.880 -10.391 1.00 30.00  ?  250 THR A OG1   1 
ATOM   1869 C CG2   . THR A 1 250 ? 7.766  -16.290 -12.346 1.00 30.00  ?  250 THR A CG2   1 
ATOM   1870 N N     . GLU A 1 255 ? 11.316 -6.464  -7.066  1.00 136.55 ?  255 GLU A N     1 
ATOM   1871 C CA    . GLU A 1 255 ? 10.278 -6.009  -6.169  1.00 142.13 ?  255 GLU A CA    1 
ATOM   1872 C C     . GLU A 1 255 ? 10.891 -5.319  -4.963  1.00 149.49 ?  255 GLU A C     1 
ATOM   1873 O O     . GLU A 1 255 ? 10.949 -4.089  -4.898  1.00 152.93 ?  255 GLU A O     1 
ATOM   1874 C CB    . GLU A 1 255 ? 9.404  -7.175  -5.721  1.00 140.62 ?  255 GLU A CB    1 
ATOM   1875 C CG    . GLU A 1 255 ? 9.082  -8.171  -6.825  1.00 137.68 ?  255 GLU A CG    1 
ATOM   1876 C CD    . GLU A 1 255 ? 7.911  -7.735  -7.685  1.00 139.50 ?  255 GLU A CD    1 
ATOM   1877 O OE1   . GLU A 1 255 ? 7.770  -6.515  -7.937  1.00 136.15 ?  255 GLU A OE1   1 
ATOM   1878 O OE2   . GLU A 1 255 ? 7.128  -8.618  -8.101  1.00 137.19 -1 255 GLU A OE2   1 
ATOM   1879 N N     . MET A 1 256 ? 11.283 -6.120  -3.984  1.00 144.87 ?  256 MET A N     1 
ATOM   1880 C CA    . MET A 1 256 ? 12.031 -5.564  -2.836  1.00 148.09 ?  256 MET A CA    1 
ATOM   1881 C C     . MET A 1 256 ? 13.412 -5.301  -3.417  1.00 154.83 ?  256 MET A C     1 
ATOM   1882 O O     . MET A 1 256 ? 14.027 -6.268  -3.901  1.00 155.61 ?  256 MET A O     1 
ATOM   1883 C CB    . MET A 1 256 ? 12.137 -6.583  -1.702  1.00 145.20 ?  256 MET A CB    1 
ATOM   1884 C CG    . MET A 1 256 ? 12.872 -6.055  -0.489  1.00 148.89 ?  256 MET A CG    1 
ATOM   1885 S SD    . MET A 1 256 ? 12.461 -6.979  1.012   1.00 157.31 ?  256 MET A SD    1 
ATOM   1886 C CE    . MET A 1 256 ? 12.071 -5.633  2.128   1.00 149.52 ?  256 MET A CE    1 
ATOM   1887 N N     . VAL A 1 257 ? 13.879 -4.072  -3.394  1.00 154.49 ?  257 VAL A N     1 
ATOM   1888 C CA    . VAL A 1 257 ? 15.118 -3.722  -4.096  1.00 154.25 ?  257 VAL A CA    1 
ATOM   1889 C C     . VAL A 1 257 ? 15.990 -2.732  -3.310  1.00 155.07 ?  257 VAL A C     1 
ATOM   1890 O O     . VAL A 1 257 ? 16.819 -2.018  -3.895  1.00 155.18 ?  257 VAL A O     1 
ATOM   1891 C CB    . VAL A 1 257 ? 14.792 -3.214  -5.524  1.00 152.74 ?  257 VAL A CB    1 
ATOM   1892 C CG1   . VAL A 1 257 ? 14.263 -1.767  -5.531  1.00 152.20 ?  257 VAL A CG1   1 
ATOM   1893 C CG2   . VAL A 1 257 ? 15.979 -3.418  -6.489  1.00 154.33 ?  257 VAL A CG2   1 
ATOM   1894 N N     . ASN A 1 258 ? 15.844 -2.704  -1.981  1.00 151.65 ?  258 ASN A N     1 
ATOM   1895 C CA    . ASN A 1 258 ? 16.709 -1.907  -1.100  1.00 148.29 ?  258 ASN A CA    1 
ATOM   1896 C C     . ASN A 1 258 ? 17.322 -2.824  -0.036  1.00 143.52 ?  258 ASN A C     1 
ATOM   1897 O O     . ASN A 1 258 ? 16.773 -2.995  1.055   1.00 143.14 ?  258 ASN A O     1 
ATOM   1898 C CB    . ASN A 1 258 ? 15.939 -0.725  -0.451  1.00 150.67 ?  258 ASN A CB    1 
ATOM   1899 C CG    . ASN A 1 258 ? 16.776 0.570   -0.376  1.00 150.20 ?  258 ASN A CG    1 
ATOM   1900 O OD1   . ASN A 1 258 ? 17.123 1.158   -1.398  1.00 148.00 ?  258 ASN A OD1   1 
ATOM   1901 N ND2   . ASN A 1 258 ? 17.080 1.018   0.843   1.00 146.50 ?  258 ASN A ND2   1 
ATOM   1902 N N     . GLN A 1 259 ? 18.479 -3.412  -0.359  1.00 138.41 ?  259 GLN A N     1 
ATOM   1903 C CA    . GLN A 1 259 ? 19.239 -4.190  0.613   1.00 135.73 ?  259 GLN A CA    1 
ATOM   1904 C C     . GLN A 1 259 ? 20.735 -3.905  0.540   1.00 134.15 ?  259 GLN A C     1 
ATOM   1905 O O     . GLN A 1 259 ? 21.529 -4.779  0.915   1.00 133.06 ?  259 GLN A O     1 
ATOM   1906 C CB    . GLN A 1 259 ? 19.008 -5.705  0.440   1.00 134.68 ?  259 GLN A CB    1 
ATOM   1907 C CG    . GLN A 1 259 ? 18.058 -6.310  1.449   1.00 136.27 ?  259 GLN A CG    1 
ATOM   1908 C CD    . GLN A 1 259 ? 16.604 -6.056  1.103   1.00 142.48 ?  259 GLN A CD    1 
ATOM   1909 O OE1   . GLN A 1 259 ? 16.282 -5.529  0.035   1.00 145.08 ?  259 GLN A OE1   1 
ATOM   1910 N NE2   . GLN A 1 259 ? 15.712 -6.444  1.999   1.00 138.75 ?  259 GLN A NE2   1 
ATOM   1911 N N     . PHE A 1 260 ? 21.137 -2.725  0.051   1.00 120.70 ?  260 PHE A N     1 
ATOM   1912 C CA    . PHE A 1 260 ? 22.545 -2.308  0.046   1.00 115.09 ?  260 PHE A CA    1 
ATOM   1913 C C     . PHE A 1 260 ? 23.424 -3.349  -0.659  1.00 113.38 ?  260 PHE A C     1 
ATOM   1914 O O     . PHE A 1 260 ? 24.130 -4.148  -0.035  1.00 113.63 ?  260 PHE A O     1 
ATOM   1915 C CB    . PHE A 1 260 ? 23.056 -2.011  1.463   1.00 117.13 ?  260 PHE A CB    1 
ATOM   1916 C CG    . PHE A 1 260 ? 24.548 -1.755  1.544   1.00 115.05 ?  260 PHE A CG    1 
ATOM   1917 C CD1   . PHE A 1 260 ? 25.115 -0.654  0.907   1.00 111.29 ?  260 PHE A CD1   1 
ATOM   1918 C CD2   . PHE A 1 260 ? 25.378 -2.614  2.252   1.00 110.13 ?  260 PHE A CD2   1 
ATOM   1919 C CE1   . PHE A 1 260 ? 26.476 -0.428  0.982   1.00 107.30 ?  260 PHE A CE1   1 
ATOM   1920 C CE2   . PHE A 1 260 ? 26.731 -2.388  2.320   1.00 105.26 ?  260 PHE A CE2   1 
ATOM   1921 C CZ    . PHE A 1 260 ? 27.284 -1.296  1.693   1.00 105.25 ?  260 PHE A CZ    1 
ATOM   1922 N N     . ASP A 1 261 ? 23.257 -3.399  -1.990  1.00 117.72 ?  261 ASP A N     1 
ATOM   1923 C CA    . ASP A 1 261 ? 24.130 -4.190  -2.845  1.00 105.60 ?  261 ASP A CA    1 
ATOM   1924 C C     . ASP A 1 261 ? 25.567 -3.912  -2.423  1.00 100.00 ?  261 ASP A C     1 
ATOM   1925 O O     . ASP A 1 261 ? 26.041 -2.774  -2.519  1.00 99.66  ?  261 ASP A O     1 
ATOM   1926 C CB    . ASP A 1 261 ? 23.898 -3.867  -4.324  1.00 98.91  ?  261 ASP A CB    1 
ATOM   1927 C CG    . ASP A 1 261 ? 24.089 -5.081  -5.209  1.00 98.48  ?  261 ASP A CG    1 
ATOM   1928 O OD1   . ASP A 1 261 ? 24.979 -5.875  -4.858  1.00 97.94  ?  261 ASP A OD1   1 
ATOM   1929 O OD2   . ASP A 1 261 ? 23.355 -5.263  -6.217  1.00 94.67  -1 261 ASP A OD2   1 
ATOM   1930 N N     . PRO A 1 262 ? 26.269 -4.907  -1.883  1.00 98.49  ?  262 PRO A N     1 
ATOM   1931 C CA    . PRO A 1 262 ? 27.645 -4.660  -1.415  1.00 92.09  ?  262 PRO A CA    1 
ATOM   1932 C C     . PRO A 1 262 ? 28.595 -4.254  -2.523  1.00 91.27  ?  262 PRO A C     1 
ATOM   1933 O O     . PRO A 1 262 ? 29.667 -3.716  -2.226  1.00 91.62  ?  262 PRO A O     1 
ATOM   1934 C CB    . PRO A 1 262 ? 28.047 -5.996  -0.762  1.00 86.30  ?  262 PRO A CB    1 
ATOM   1935 C CG    . PRO A 1 262 ? 27.084 -7.011  -1.311  1.00 91.40  ?  262 PRO A CG    1 
ATOM   1936 C CD    . PRO A 1 262 ? 25.813 -6.280  -1.613  1.00 96.66  ?  262 PRO A CD    1 
ATOM   1937 N N     . GLY A 1 263 ? 28.234 -4.496  -3.782  1.00 93.57  ?  263 GLY A N     1 
ATOM   1938 C CA    . GLY A 1 263 ? 28.982 -3.998  -4.916  1.00 92.90  ?  263 GLY A CA    1 
ATOM   1939 C C     . GLY A 1 263 ? 28.972 -2.493  -5.046  1.00 91.16  ?  263 GLY A C     1 
ATOM   1940 O O     . GLY A 1 263 ? 29.646 -1.955  -5.928  1.00 93.75  ?  263 GLY A O     1 
ATOM   1941 N N     . ASP A 1 264 ? 28.202 -1.803  -4.211  1.00 90.78  ?  264 ASP A N     1 
ATOM   1942 C CA    . ASP A 1 264 ? 28.397 -0.375  -4.041  1.00 89.21  ?  264 ASP A CA    1 
ATOM   1943 C C     . ASP A 1 264 ? 29.713 -0.064  -3.384  1.00 88.67  ?  264 ASP A C     1 
ATOM   1944 O O     . ASP A 1 264 ? 29.999 1.109   -3.157  1.00 89.48  ?  264 ASP A O     1 
ATOM   1945 C CB    . ASP A 1 264 ? 27.280 0.245   -3.209  1.00 97.68  ?  264 ASP A CB    1 
ATOM   1946 C CG    . ASP A 1 264 ? 25.956 0.240   -3.926  1.00 108.98 ?  264 ASP A CG    1 
ATOM   1947 O OD1   . ASP A 1 264 ? 25.766 -0.574  -4.861  1.00 111.06 -1 264 ASP A OD1   1 
ATOM   1948 O OD2   . ASP A 1 264 ? 25.107 1.088   -3.568  1.00 114.40 ?  264 ASP A OD2   1 
ATOM   1949 N N     . LEU A 1 265 ? 30.489 -1.071  -3.028  1.00 91.71  ?  265 LEU A N     1 
ATOM   1950 C CA    . LEU A 1 265 ? 31.762 -0.840  -2.376  1.00 88.87  ?  265 LEU A CA    1 
ATOM   1951 C C     . LEU A 1 265 ? 32.948 -1.149  -3.263  1.00 87.24  ?  265 LEU A C     1 
ATOM   1952 O O     . LEU A 1 265 ? 34.071 -0.777  -2.909  1.00 87.53  ?  265 LEU A O     1 
ATOM   1953 C CB    . LEU A 1 265 ? 31.861 -1.668  -1.096  1.00 84.85  ?  265 LEU A CB    1 
ATOM   1954 C CG    . LEU A 1 265 ? 30.919 -1.153  -0.026  1.00 86.55  ?  265 LEU A CG    1 
ATOM   1955 C CD1   . LEU A 1 265 ? 30.570 -2.273  0.901   1.00 85.92  ?  265 LEU A CD1   1 
ATOM   1956 C CD2   . LEU A 1 265 ? 31.608 -0.022  0.715   1.00 85.56  ?  265 LEU A CD2   1 
ATOM   1957 N N     . VAL A 1 266 ? 32.741 -1.824  -4.394  1.00 85.38  ?  266 VAL A N     1 
ATOM   1958 C CA    . VAL A 1 266 ? 33.858 -2.032  -5.301  1.00 88.54  ?  266 VAL A CA    1 
ATOM   1959 C C     . VAL A 1 266 ? 34.310 -0.675  -5.803  1.00 94.57  ?  266 VAL A C     1 
ATOM   1960 O O     . VAL A 1 266 ? 33.497 0.144   -6.254  1.00 95.21  ?  266 VAL A O     1 
ATOM   1961 C CB    . VAL A 1 266 ? 33.496 -2.964  -6.470  1.00 87.25  ?  266 VAL A CB    1 
ATOM   1962 C CG1   . VAL A 1 266 ? 33.479 -4.410  -6.022  1.00 85.83  ?  266 VAL A CG1   1 
ATOM   1963 C CG2   . VAL A 1 266 ? 32.186 -2.565  -7.112  1.00 94.45  ?  266 VAL A CG2   1 
ATOM   1964 N N     . GLY A 1 267 ? 35.614 -0.432  -5.718  1.00 93.60  ?  267 GLY A N     1 
ATOM   1965 C CA    . GLY A 1 267 ? 36.213 0.808   -6.162  1.00 92.72  ?  267 GLY A CA    1 
ATOM   1966 C C     . GLY A 1 267 ? 36.569 1.773   -5.057  1.00 91.21  ?  267 GLY A C     1 
ATOM   1967 O O     . GLY A 1 267 ? 37.345 2.711   -5.289  1.00 93.47  ?  267 GLY A O     1 
ATOM   1968 N N     . VAL A 1 268 ? 36.073 1.545   -3.851  1.00 89.79  ?  268 VAL A N     1 
ATOM   1969 C CA    . VAL A 1 268 ? 36.352 2.445   -2.746  1.00 81.89  ?  268 VAL A CA    1 
ATOM   1970 C C     . VAL A 1 268 ? 37.680 1.974   -2.176  1.00 78.31  ?  268 VAL A C     1 
ATOM   1971 O O     . VAL A 1 268 ? 37.756 1.252   -1.182  1.00 80.10  ?  268 VAL A O     1 
ATOM   1972 C CB    . VAL A 1 268 ? 35.223 2.435   -1.728  1.00 80.53  ?  268 VAL A CB    1 
ATOM   1973 C CG1   . VAL A 1 268 ? 35.429 3.524   -0.702  1.00 81.26  ?  268 VAL A CG1   1 
ATOM   1974 C CG2   . VAL A 1 268 ? 33.897 2.582   -2.465  1.00 86.36  ?  268 VAL A CG2   1 
ATOM   1975 N N     . LYS A 1 269 ? 38.763 2.405   -2.823  1.00 81.52  ?  269 LYS A N     1 
ATOM   1976 C CA    . LYS A 1 269 ? 40.057 1.790   -2.557  1.00 79.33  ?  269 LYS A CA    1 
ATOM   1977 C C     . LYS A 1 269 ? 40.592 2.122   -1.163  1.00 77.87  ?  269 LYS A C     1 
ATOM   1978 O O     . LYS A 1 269 ? 41.423 1.369   -0.647  1.00 78.39  ?  269 LYS A O     1 
ATOM   1979 C CB    . LYS A 1 269 ? 41.059 2.188   -3.647  1.00 77.67  ?  269 LYS A CB    1 
ATOM   1980 N N     . GLU A 1 270 ? 40.115 3.207   -0.528  1.00 78.20  ?  270 GLU A N     1 
ATOM   1981 C CA    . GLU A 1 270 ? 40.602 3.613   0.791   1.00 77.67  ?  270 GLU A CA    1 
ATOM   1982 C C     . GLU A 1 270 ? 40.027 2.784   1.931   1.00 76.63  ?  270 GLU A C     1 
ATOM   1983 O O     . GLU A 1 270 ? 40.586 2.818   3.040   1.00 74.42  ?  270 GLU A O     1 
ATOM   1984 C CB    . GLU A 1 270 ? 40.286 5.085   1.065   1.00 77.68  ?  270 GLU A CB    1 
ATOM   1985 C CG    . GLU A 1 270 ? 40.922 6.058   0.117   1.00 79.92  ?  270 GLU A CG    1 
ATOM   1986 C CD    . GLU A 1 270 ? 40.029 6.387   -1.079  1.00 87.33  ?  270 GLU A CD    1 
ATOM   1987 O OE1   . GLU A 1 270 ? 38.852 5.949   -1.106  1.00 87.30  ?  270 GLU A OE1   1 
ATOM   1988 O OE2   . GLU A 1 270 ? 40.506 7.097   -1.995  1.00 91.05  -1 270 GLU A OE2   1 
ATOM   1989 N N     . PHE A 1 271 ? 38.926 2.060   1.692   1.00 75.70  ?  271 PHE A N     1 
ATOM   1990 C CA    . PHE A 1 271 ? 38.328 1.206   2.717   1.00 75.13  ?  271 PHE A CA    1 
ATOM   1991 C C     . PHE A 1 271 ? 39.132 -0.082  2.860   1.00 75.27  ?  271 PHE A C     1 
ATOM   1992 O O     . PHE A 1 271 ? 39.369 -0.795  1.874   1.00 71.04  ?  271 PHE A O     1 
ATOM   1993 C CB    . PHE A 1 271 ? 36.875 0.881   2.384   1.00 68.70  ?  271 PHE A CB    1 
ATOM   1994 C CG    . PHE A 1 271 ? 36.178 0.086   3.460   1.00 73.20  ?  271 PHE A CG    1 
ATOM   1995 C CD1   . PHE A 1 271 ? 35.914 0.652   4.703   1.00 77.27  ?  271 PHE A CD1   1 
ATOM   1996 C CD2   . PHE A 1 271 ? 35.779 -1.223  3.233   1.00 71.53  ?  271 PHE A CD2   1 
ATOM   1997 C CE1   . PHE A 1 271 ? 35.266 -0.076  5.705   1.00 74.79  ?  271 PHE A CE1   1 
ATOM   1998 C CE2   . PHE A 1 271 ? 35.128 -1.956  4.228   1.00 67.21  ?  271 PHE A CE2   1 
ATOM   1999 C CZ    . PHE A 1 271 ? 34.876 -1.378  5.468   1.00 68.49  ?  271 PHE A CZ    1 
ATOM   2000 N N     . GLY A 1 272 ? 39.532 -0.386  4.091   1.00 72.59  ?  272 GLY A N     1 
ATOM   2001 C CA    . GLY A 1 272 ? 40.616 -1.315  4.332   1.00 74.25  ?  272 GLY A CA    1 
ATOM   2002 C C     . GLY A 1 272 ? 40.244 -2.505  5.193   1.00 73.21  ?  272 GLY A C     1 
ATOM   2003 O O     . GLY A 1 272 ? 39.418 -2.405  6.098   1.00 73.85  ?  272 GLY A O     1 
ATOM   2004 N N     . TYR A 1 273 ? 40.893 -3.628  4.915   1.00 70.30  ?  273 TYR A N     1 
ATOM   2005 C CA    . TYR A 1 273 ? 40.754 -4.858  5.678   1.00 67.36  ?  273 TYR A CA    1 
ATOM   2006 C C     . TYR A 1 273 ? 42.128 -5.215  6.239   1.00 67.38  ?  273 TYR A C     1 
ATOM   2007 O O     . TYR A 1 273 ? 43.083 -5.364  5.471   1.00 69.18  ?  273 TYR A O     1 
ATOM   2008 C CB    . TYR A 1 273 ? 40.220 -5.966  4.766   1.00 67.31  ?  273 TYR A CB    1 
ATOM   2009 C CG    . TYR A 1 273 ? 39.703 -7.174  5.502   1.00 67.00  ?  273 TYR A CG    1 
ATOM   2010 C CD1   . TYR A 1 273 ? 39.183 -7.050  6.775   1.00 66.75  ?  273 TYR A CD1   1 
ATOM   2011 C CD2   . TYR A 1 273 ? 39.748 -8.438  4.939   1.00 66.47  ?  273 TYR A CD2   1 
ATOM   2012 C CE1   . TYR A 1 273 ? 38.708 -8.156  7.469   1.00 67.86  ?  273 TYR A CE1   1 
ATOM   2013 C CE2   . TYR A 1 273 ? 39.270 -9.552  5.635   1.00 65.79  ?  273 TYR A CE2   1 
ATOM   2014 C CZ    . TYR A 1 273 ? 38.752 -9.400  6.904   1.00 67.29  ?  273 TYR A CZ    1 
ATOM   2015 O OH    . TYR A 1 273 ? 38.264 -10.465 7.638   1.00 63.30  ?  273 TYR A OH    1 
ATOM   2016 N N     . LEU A 1 274 ? 42.244 -5.369  7.562   1.00 63.31  ?  274 LEU A N     1 
ATOM   2017 C CA    . LEU A 1 274 ? 43.544 -5.643  8.177   1.00 64.83  ?  274 LEU A CA    1 
ATOM   2018 C C     . LEU A 1 274 ? 43.562 -7.011  8.850   1.00 66.22  ?  274 LEU A C     1 
ATOM   2019 O O     . LEU A 1 274 ? 42.543 -7.474  9.366   1.00 66.83  ?  274 LEU A O     1 
ATOM   2020 C CB    . LEU A 1 274 ? 43.938 -4.562  9.220   1.00 67.93  ?  274 LEU A CB    1 
ATOM   2021 C CG    . LEU A 1 274 ? 43.445 -4.567  10.680  1.00 66.87  ?  274 LEU A CG    1 
ATOM   2022 C CD1   . LEU A 1 274 ? 44.377 -5.325  11.642  1.00 67.13  ?  274 LEU A CD1   1 
ATOM   2023 C CD2   . LEU A 1 274 ? 43.268 -3.142  11.178  1.00 71.51  ?  274 LEU A CD2   1 
ATOM   2024 N N     . LEU A 1 275 ? 44.734 -7.648  8.851   1.00 62.33  ?  275 LEU A N     1 
ATOM   2025 C CA    . LEU A 1 275 ? 44.979 -8.895  9.563   1.00 61.40  ?  275 LEU A CA    1 
ATOM   2026 C C     . LEU A 1 275 ? 46.061 -8.614  10.586  1.00 62.22  ?  275 LEU A C     1 
ATOM   2027 O O     . LEU A 1 275 ? 47.061 -7.973  10.258  1.00 65.13  ?  275 LEU A O     1 
ATOM   2028 C CB    . LEU A 1 275 ? 45.426 -9.997  8.602   1.00 61.32  ?  275 LEU A CB    1 
ATOM   2029 C CG    . LEU A 1 275 ? 45.420 -11.471 9.015   1.00 61.55  ?  275 LEU A CG    1 
ATOM   2030 C CD1   . LEU A 1 275 ? 45.409 -12.276 7.760   1.00 56.09  ?  275 LEU A CD1   1 
ATOM   2031 C CD2   . LEU A 1 275 ? 46.607 -11.897 9.871   1.00 55.25  ?  275 LEU A CD2   1 
ATOM   2032 N N     . LEU A 1 276 ? 45.869 -9.062  11.822  1.00 62.80  ?  276 LEU A N     1 
ATOM   2033 C CA    . LEU A 1 276 ? 46.745 -8.627  12.900  1.00 62.28  ?  276 LEU A CA    1 
ATOM   2034 C C     . LEU A 1 276 ? 47.180 -9.803  13.742  1.00 61.93  ?  276 LEU A C     1 
ATOM   2035 O O     . LEU A 1 276 ? 46.364 -10.670 14.064  1.00 63.30  ?  276 LEU A O     1 
ATOM   2036 C CB    . LEU A 1 276 ? 46.034 -7.621  13.779  1.00 65.32  ?  276 LEU A CB    1 
ATOM   2037 C CG    . LEU A 1 276 ? 46.858 -6.926  14.841  1.00 66.11  ?  276 LEU A CG    1 
ATOM   2038 C CD1   . LEU A 1 276 ? 46.224 -5.555  14.928  1.00 67.32  ?  276 LEU A CD1   1 
ATOM   2039 C CD2   . LEU A 1 276 ? 46.848 -7.670  16.196  1.00 61.27  ?  276 LEU A CD2   1 
ATOM   2040 N N     . VAL A 1 277 ? 48.447 -9.823  14.137  1.00 56.95  ?  277 VAL A N     1 
ATOM   2041 C CA    . VAL A 1 277 ? 48.910 -10.853 15.054  1.00 62.37  ?  277 VAL A CA    1 
ATOM   2042 C C     . VAL A 1 277 ? 49.649 -10.184 16.190  1.00 63.15  ?  277 VAL A C     1 
ATOM   2043 O O     . VAL A 1 277 ? 50.711 -9.589  15.984  1.00 61.14  ?  277 VAL A O     1 
ATOM   2044 C CB    . VAL A 1 277 ? 49.802 -11.894 14.381  1.00 63.54  ?  277 VAL A CB    1 
ATOM   2045 C CG1   . VAL A 1 277 ? 49.835 -13.128 15.249  1.00 62.52  ?  277 VAL A CG1   1 
ATOM   2046 C CG2   . VAL A 1 277 ? 49.288 -12.212 13.019  1.00 59.18  ?  277 VAL A CG2   1 
ATOM   2047 N N     . ALA A 1 278 ? 49.112 -10.310 17.388  1.00 64.31  ?  278 ALA A N     1 
ATOM   2048 C CA    . ALA A 1 278 ? 49.718 -9.763  18.586  1.00 64.49  ?  278 ALA A CA    1 
ATOM   2049 C C     . ALA A 1 278 ? 50.049 -10.915 19.516  1.00 61.81  ?  278 ALA A C     1 
ATOM   2050 O O     . ALA A 1 278 ? 49.366 -11.942 19.525  1.00 62.03  ?  278 ALA A O     1 
ATOM   2051 C CB    . ALA A 1 278 ? 48.784 -8.765  19.291  1.00 60.78  ?  278 ALA A CB    1 
ATOM   2052 N N     . GLN A 1 279 ? 51.109 -10.754 20.288  1.00 65.80  ?  279 GLN A N     1 
ATOM   2053 C CA    . GLN A 1 279 ? 51.504 -11.777 21.233  1.00 69.35  ?  279 GLN A CA    1 
ATOM   2054 C C     . GLN A 1 279 ? 51.528 -11.245 22.667  1.00 75.62  ?  279 GLN A C     1 
ATOM   2055 O O     . GLN A 1 279 ? 51.649 -10.038 22.917  1.00 77.27  ?  279 GLN A O     1 
ATOM   2056 C CB    . GLN A 1 279 ? 52.858 -12.349 20.866  1.00 68.36  ?  279 GLN A CB    1 
ATOM   2057 C CG    . GLN A 1 279 ? 53.164 -13.609 21.613  1.00 73.40  ?  279 GLN A CG    1 
ATOM   2058 C CD    . GLN A 1 279 ? 54.539 -14.090 21.305  1.00 75.76  ?  279 GLN A CD    1 
ATOM   2059 O OE1   . GLN A 1 279 ? 55.312 -13.371 20.673  1.00 80.06  ?  279 GLN A OE1   1 
ATOM   2060 N NE2   . GLN A 1 279 ? 54.866 -15.307 21.732  1.00 72.51  ?  279 GLN A NE2   1 
ATOM   2061 N N     . ARG A 1 280 ? 51.353 -12.164 23.613  1.00 77.77  ?  280 ARG A N     1 
ATOM   2062 C CA    . ARG A 1 280 ? 51.597 -11.884 25.010  1.00 80.32  ?  280 ARG A CA    1 
ATOM   2063 C C     . ARG A 1 280 ? 52.968 -12.418 25.374  1.00 81.81  ?  280 ARG A C     1 
ATOM   2064 O O     . ARG A 1 280 ? 53.221 -13.615 25.184  1.00 86.13  ?  280 ARG A O     1 
ATOM   2065 C CB    . ARG A 1 280 ? 50.532 -12.523 25.878  1.00 76.84  ?  280 ARG A CB    1 
ATOM   2066 C CG    . ARG A 1 280 ? 50.956 -12.516 27.292  1.00 82.79  ?  280 ARG A CG    1 
ATOM   2067 C CD    . ARG A 1 280 ? 49.871 -12.982 28.171  1.00 76.50  ?  280 ARG A CD    1 
ATOM   2068 N NE    . ARG A 1 280 ? 50.250 -12.757 29.552  1.00 77.71  ?  280 ARG A NE    1 
ATOM   2069 C CZ    . ARG A 1 280 ? 49.379 -12.768 30.541  1.00 80.90  ?  280 ARG A CZ    1 
ATOM   2070 N NH1   . ARG A 1 280 ? 48.091 -12.993 30.318  1.00 80.13  ?  280 ARG A NH1   1 
ATOM   2071 N NH2   . ARG A 1 280 ? 49.802 -12.539 31.779  1.00 83.33  ?  280 ARG A NH2   1 
ATOM   2072 N N     . PRO A 1 281 ? 53.886 -11.593 25.851  1.00 80.56  ?  281 PRO A N     1 
ATOM   2073 C CA    . PRO A 1 281 ? 55.259 -12.066 26.062  1.00 84.09  ?  281 PRO A CA    1 
ATOM   2074 C C     . PRO A 1 281 ? 55.297 -13.124 27.145  1.00 76.54  ?  281 PRO A C     1 
ATOM   2075 O O     . PRO A 1 281 ? 54.377 -13.243 27.953  1.00 82.58  ?  281 PRO A O     1 
ATOM   2076 C CB    . PRO A 1 281 ? 56.019 -10.800 26.474  1.00 87.77  ?  281 PRO A CB    1 
ATOM   2077 C CG    . PRO A 1 281 ? 55.133 -9.643  26.008  1.00 85.15  ?  281 PRO A CG    1 
ATOM   2078 C CD    . PRO A 1 281 ? 53.723 -10.164 26.160  1.00 82.30  ?  281 PRO A CD    1 
ATOM   2079 N N     . GLY A 1 282 ? 56.369 -13.916 27.130  1.00 81.94  ?  282 GLY A N     1 
ATOM   2080 C CA    . GLY A 1 282 ? 56.437 -15.121 27.929  1.00 82.71  ?  282 GLY A CA    1 
ATOM   2081 C C     . GLY A 1 282 ? 56.413 -16.369 27.033  1.00 93.91  ?  282 GLY A C     1 
ATOM   2082 O O     . GLY A 1 282 ? 56.823 -16.329 25.883  1.00 94.78  ?  282 GLY A O     1 
ATOM   2083 N N     . LYS A 1 283 ? 55.861 -17.462 27.603  1.00 99.40  ?  283 LYS A N     1 
ATOM   2084 C CA    . LYS A 1 283 ? 56.087 -18.853 27.140  1.00 95.08  ?  283 LYS A CA    1 
ATOM   2085 C C     . LYS A 1 283 ? 57.559 -19.074 26.904  1.00 99.20  ?  283 LYS A C     1 
ATOM   2086 O O     . LYS A 1 283 ? 57.943 -20.179 26.517  1.00 100.34 ?  283 LYS A O     1 
ATOM   2087 C CB    . LYS A 1 283 ? 55.331 -19.221 25.856  1.00 88.32  ?  283 LYS A CB    1 
ATOM   2088 C CG    . LYS A 1 283 ? 54.122 -20.163 26.023  1.00 86.58  ?  283 LYS A CG    1 
ATOM   2089 C CD    . LYS A 1 283 ? 54.437 -21.635 26.292  1.00 85.79  ?  283 LYS A CD    1 
ATOM   2090 C CE    . LYS A 1 283 ? 53.162 -22.419 26.038  1.00 85.22  ?  283 LYS A CE    1 
ATOM   2091 N NZ    . LYS A 1 283 ? 52.354 -21.705 24.966  1.00 71.25  ?  283 LYS A NZ    1 
ATOM   2092 O OXT   . LYS A 1 283 ? 58.368 -18.158 27.066  1.00 104.84 -1 283 LYS A OXT   1 
ATOM   2093 N N     . LEU B 1 6   ? 57.748 6.170   23.942  1.00 104.08 ?  6   LEU B N     1 
ATOM   2094 C CA    . LEU B 1 6   ? 57.901 7.160   22.873  1.00 102.74 ?  6   LEU B CA    1 
ATOM   2095 C C     . LEU B 1 6   ? 59.051 8.112   23.183  1.00 108.81 ?  6   LEU B C     1 
ATOM   2096 O O     . LEU B 1 6   ? 58.802 9.298   23.388  1.00 118.84 ?  6   LEU B O     1 
ATOM   2097 C CB    . LEU B 1 6   ? 56.604 7.959   22.683  1.00 101.31 ?  6   LEU B CB    1 
ATOM   2098 C CG    . LEU B 1 6   ? 56.252 8.594   21.333  1.00 106.00 ?  6   LEU B CG    1 
ATOM   2099 C CD1   . LEU B 1 6   ? 54.978 9.426   21.446  1.00 108.64 ?  6   LEU B CD1   1 
ATOM   2100 C CD2   . LEU B 1 6   ? 57.377 9.436   20.759  1.00 100.69 ?  6   LEU B CD2   1 
ATOM   2101 N N     . SER B 1 7   ? 60.294 7.603   23.175  1.00 109.51 ?  7   SER B N     1 
ATOM   2102 C CA    . SER B 1 7   ? 61.503 8.357   23.561  1.00 109.78 ?  7   SER B CA    1 
ATOM   2103 C C     . SER B 1 7   ? 61.585 8.546   25.077  1.00 115.45 ?  7   SER B C     1 
ATOM   2104 O O     . SER B 1 7   ? 62.068 9.576   25.560  1.00 116.14 ?  7   SER B O     1 
ATOM   2105 C CB    . SER B 1 7   ? 61.589 9.718   22.840  1.00 107.32 ?  7   SER B CB    1 
ATOM   2106 O OG    . SER B 1 7   ? 62.546 10.609  23.415  1.00 105.86 ?  7   SER B OG    1 
ATOM   2107 N N     . GLU B 1 8   ? 61.125 7.543   25.838  1.00 115.94 ?  8   GLU B N     1 
ATOM   2108 C CA    . GLU B 1 8   ? 61.198 7.639   27.293  1.00 114.19 ?  8   GLU B CA    1 
ATOM   2109 C C     . GLU B 1 8   ? 62.621 7.913   27.740  1.00 110.71 ?  8   GLU B C     1 
ATOM   2110 O O     . GLU B 1 8   ? 62.831 8.513   28.800  1.00 98.76  ?  8   GLU B O     1 
ATOM   2111 C CB    . GLU B 1 8   ? 60.680 6.347   27.934  1.00 112.53 ?  8   GLU B CB    1 
ATOM   2112 C CG    . GLU B 1 8   ? 59.176 6.128   27.768  1.00 110.92 ?  8   GLU B CG    1 
ATOM   2113 C CD    . GLU B 1 8   ? 58.835 5.067   26.744  1.00 104.05 ?  8   GLU B CD    1 
ATOM   2114 O OE1   . GLU B 1 8   ? 59.555 4.046   26.737  1.00 100.58 ?  8   GLU B OE1   1 
ATOM   2115 O OE2   . GLU B 1 8   ? 57.862 5.256   25.962  1.00 106.52 -1 8   GLU B OE2   1 
ATOM   2116 N N     . LEU B 1 9   ? 63.646 7.427   26.912  1.00 113.80 ?  9   LEU B N     1 
ATOM   2117 C CA    . LEU B 1 9   ? 65.088 7.655   26.837  1.00 113.50 ?  9   LEU B CA    1 
ATOM   2118 C C     . LEU B 1 9   ? 65.368 8.736   25.807  1.00 114.71 ?  9   LEU B C     1 
ATOM   2119 O O     . LEU B 1 9   ? 64.791 8.699   24.713  1.00 114.14 ?  9   LEU B O     1 
ATOM   2120 C CB    . LEU B 1 9   ? 65.820 6.382   26.444  1.00 113.56 ?  9   LEU B CB    1 
ATOM   2121 C CG    . LEU B 1 9   ? 67.265 6.089   26.845  1.00 116.08 ?  9   LEU B CG    1 
ATOM   2122 C CD1   . LEU B 1 9   ? 67.576 4.824   26.141  1.00 110.70 ?  9   LEU B CD1   1 
ATOM   2123 C CD2   . LEU B 1 9   ? 68.291 7.156   26.497  1.00 116.38 ?  9   LEU B CD2   1 
ATOM   2124 N N     . PRO B 1 10  ? 66.216 9.716   26.113  1.00 115.94 ?  10  PRO B N     1 
ATOM   2125 C CA    . PRO B 1 10  ? 66.510 10.760  25.123  1.00 117.96 ?  10  PRO B CA    1 
ATOM   2126 C C     . PRO B 1 10  ? 67.285 10.202  23.926  1.00 109.47 ?  10  PRO B C     1 
ATOM   2127 O O     . PRO B 1 10  ? 67.903 9.127   23.977  1.00 104.75 ?  10  PRO B O     1 
ATOM   2128 C CB    . PRO B 1 10  ? 67.346 11.779  25.916  1.00 115.07 ?  10  PRO B CB    1 
ATOM   2129 C CG    . PRO B 1 10  ? 67.038 11.484  27.376  1.00 104.24 ?  10  PRO B CG    1 
ATOM   2130 C CD    . PRO B 1 10  ? 66.834 10.010  27.422  1.00 104.67 ?  10  PRO B CD    1 
ATOM   2131 N N     . MET B 1 11  ? 67.236 10.941  22.820  1.00 106.96 ?  11  MET B N     1 
ATOM   2132 C CA    . MET B 1 11  ? 67.782 10.342  21.615  1.00 107.29 ?  11  MET B CA    1 
ATOM   2133 C C     . MET B 1 11  ? 68.666 11.294  20.801  1.00 107.75 ?  11  MET B C     1 
ATOM   2134 O O     . MET B 1 11  ? 68.384 12.495  20.720  1.00 109.19 ?  11  MET B O     1 
ATOM   2135 C CB    . MET B 1 11  ? 66.658 9.808   20.728  1.00 108.11 ?  11  MET B CB    1 
ATOM   2136 C CG    . MET B 1 11  ? 66.181 8.472   21.232  1.00 103.91 ?  11  MET B CG    1 
ATOM   2137 S SD    . MET B 1 11  ? 64.792 7.830   20.309  1.00 96.46  ?  11  MET B SD    1 
ATOM   2138 C CE    . MET B 1 11  ? 63.830 9.313   20.021  1.00 97.79  ?  11  MET B CE    1 
ATOM   2139 N N     . PRO B 1 12  ? 69.675 10.715  20.122  1.00 105.14 ?  12  PRO B N     1 
ATOM   2140 C CA    . PRO B 1 12  ? 70.804 11.511  19.581  1.00 105.11 ?  12  PRO B CA    1 
ATOM   2141 C C     . PRO B 1 12  ? 70.454 12.525  18.531  1.00 96.97  ?  12  PRO B C     1 
ATOM   2142 O O     . PRO B 1 12  ? 71.266 13.429  18.296  1.00 97.78  ?  12  PRO B O     1 
ATOM   2143 C CB    . PRO B 1 12  ? 71.723 10.437  18.977  1.00 99.63  ?  12  PRO B CB    1 
ATOM   2144 C CG    . PRO B 1 12  ? 71.431 9.262   19.737  1.00 100.34 ?  12  PRO B CG    1 
ATOM   2145 C CD    . PRO B 1 12  ? 70.008 9.291   20.173  1.00 99.33  ?  12  PRO B CD    1 
ATOM   2146 N N     . SER B 1 13  ? 69.332 12.380  17.850  1.00 92.55  ?  13  SER B N     1 
ATOM   2147 C CA    . SER B 1 13  ? 68.916 13.393  16.887  1.00 96.67  ?  13  SER B CA    1 
ATOM   2148 C C     . SER B 1 13  ? 69.954 13.632  15.776  1.00 94.93  ?  13  SER B C     1 
ATOM   2149 O O     . SER B 1 13  ? 70.433 14.764  15.625  1.00 89.68  ?  13  SER B O     1 
ATOM   2150 C CB    . SER B 1 13  ? 68.611 14.686  17.660  1.00 96.82  ?  13  SER B CB    1 
ATOM   2151 O OG    . SER B 1 13  ? 68.710 15.836  16.848  1.00 95.44  ?  13  SER B OG    1 
ATOM   2152 N N     . PRO B 1 14  ? 70.301 12.627  14.961  1.00 90.78  ?  14  PRO B N     1 
ATOM   2153 C CA    . PRO B 1 14  ? 71.577 12.672  14.239  1.00 90.63  ?  14  PRO B CA    1 
ATOM   2154 C C     . PRO B 1 14  ? 71.518 13.472  12.950  1.00 88.64  ?  14  PRO B C     1 
ATOM   2155 O O     . PRO B 1 14  ? 70.455 13.798  12.421  1.00 88.98  ?  14  PRO B O     1 
ATOM   2156 C CB    . PRO B 1 14  ? 71.877 11.200  13.947  1.00 86.13  ?  14  PRO B CB    1 
ATOM   2157 C CG    . PRO B 1 14  ? 70.538 10.577  13.846  1.00 85.37  ?  14  PRO B CG    1 
ATOM   2158 C CD    . PRO B 1 14  ? 69.578 11.368  14.705  1.00 84.13  ?  14  PRO B CD    1 
ATOM   2159 N N     . ALA B 1 15  ? 72.718 13.772  12.458  1.00 85.99  ?  15  ALA B N     1 
ATOM   2160 C CA    . ALA B 1 15  ? 72.950 14.601  11.283  1.00 86.19  ?  15  ALA B CA    1 
ATOM   2161 C C     . ALA B 1 15  ? 73.602 13.759  10.200  1.00 83.56  ?  15  ALA B C     1 
ATOM   2162 O O     . ALA B 1 15  ? 74.704 13.224  10.403  1.00 84.58  ?  15  ALA B O     1 
ATOM   2163 C CB    . ALA B 1 15  ? 73.859 15.784  11.620  1.00 85.23  ?  15  ALA B CB    1 
ATOM   2164 N N     . SER B 1 16  ? 72.948 13.704  9.033   1.00 82.70  ?  16  SER B N     1 
ATOM   2165 C CA    . SER B 1 16  ? 73.335 12.741  8.006   1.00 83.54  ?  16  SER B CA    1 
ATOM   2166 C C     . SER B 1 16  ? 74.794 12.904  7.610   1.00 79.56  ?  16  SER B C     1 
ATOM   2167 O O     . SER B 1 16  ? 75.524 11.914  7.502   1.00 81.94  ?  16  SER B O     1 
ATOM   2168 C CB    . SER B 1 16  ? 72.434 12.890  6.791   1.00 74.80  ?  16  SER B CB    1 
ATOM   2169 O OG    . SER B 1 16  ? 72.138 14.250  6.586   1.00 75.51  ?  16  SER B OG    1 
ATOM   2170 N N     . GLU B 1 17  ? 75.261 14.138  7.437   1.00 80.12  ?  17  GLU B N     1 
ATOM   2171 C CA    . GLU B 1 17  ? 76.667 14.308  7.089   1.00 85.89  ?  17  GLU B CA    1 
ATOM   2172 C C     . GLU B 1 17  ? 77.615 13.906  8.225   1.00 81.26  ?  17  GLU B C     1 
ATOM   2173 O O     . GLU B 1 17  ? 78.741 13.463  7.952   1.00 77.44  ?  17  GLU B O     1 
ATOM   2174 C CB    . GLU B 1 17  ? 76.920 15.746  6.642   1.00 83.54  ?  17  GLU B CB    1 
ATOM   2175 C CG    . GLU B 1 17  ? 76.053 16.177  5.458   1.00 87.26  ?  17  GLU B CG    1 
ATOM   2176 C CD    . GLU B 1 17  ? 76.523 15.631  4.094   1.00 92.69  ?  17  GLU B CD    1 
ATOM   2177 O OE1   . GLU B 1 17  ? 77.745 15.346  3.949   1.00 89.58  ?  17  GLU B OE1   1 
ATOM   2178 O OE2   . GLU B 1 17  ? 75.658 15.508  3.171   1.00 86.42  -1 17  GLU B OE2   1 
ATOM   2179 N N     . GLU B 1 18  ? 77.194 14.029  9.485   1.00 83.92  ?  18  GLU B N     1 
ATOM   2180 C CA    . GLU B 1 18  ? 78.026 13.496  10.558  1.00 86.13  ?  18  GLU B CA    1 
ATOM   2181 C C     . GLU B 1 18  ? 78.042 11.978  10.526  1.00 86.32  ?  18  GLU B C     1 
ATOM   2182 O O     . GLU B 1 18  ? 79.063 11.357  10.866  1.00 88.71  ?  18  GLU B O     1 
ATOM   2183 C CB    . GLU B 1 18  ? 77.526 13.977  11.915  1.00 85.41  ?  18  GLU B CB    1 
ATOM   2184 C CG    . GLU B 1 18  ? 77.523 15.474  12.098  1.00 91.44  ?  18  GLU B CG    1 
ATOM   2185 C CD    . GLU B 1 18  ? 77.357 15.845  13.558  1.00 103.56 ?  18  GLU B CD    1 
ATOM   2186 O OE1   . GLU B 1 18  ? 77.158 14.916  14.383  1.00 97.05  ?  18  GLU B OE1   1 
ATOM   2187 O OE2   . GLU B 1 18  ? 77.438 17.051  13.882  1.00 109.09 -1 18  GLU B OE2   1 
ATOM   2188 N N     . VAL B 1 19  ? 76.910 11.381  10.128  1.00 82.91  ?  19  VAL B N     1 
ATOM   2189 C CA    . VAL B 1 19  ? 76.824 9.940   9.922   1.00 83.46  ?  19  VAL B CA    1 
ATOM   2190 C C     . VAL B 1 19  ? 77.888 9.486   8.936   1.00 83.82  ?  19  VAL B C     1 
ATOM   2191 O O     . VAL B 1 19  ? 78.576 8.484   9.157   1.00 81.84  ?  19  VAL B O     1 
ATOM   2192 C CB    . VAL B 1 19  ? 75.413 9.565   9.437   1.00 74.98  ?  19  VAL B CB    1 
ATOM   2193 C CG1   . VAL B 1 19  ? 75.300 8.080   9.296   1.00 71.38  ?  19  VAL B CG1   1 
ATOM   2194 C CG2   . VAL B 1 19  ? 74.364 10.113  10.367  1.00 77.85  ?  19  VAL B CG2   1 
ATOM   2195 N N     . GLY B 1 20  ? 78.042 10.226  7.837   1.00 81.63  ?  20  GLY B N     1 
ATOM   2196 C CA    . GLY B 1 20  ? 79.096 9.920   6.887   1.00 76.61  ?  20  GLY B CA    1 
ATOM   2197 C C     . GLY B 1 20  ? 80.478 9.995   7.505   1.00 85.04  ?  20  GLY B C     1 
ATOM   2198 O O     . GLY B 1 20  ? 81.332 9.142   7.247   1.00 83.65  ?  20  GLY B O     1 
ATOM   2199 N N     . ALA B 1 21  ? 80.714 11.011  8.341   1.00 83.22  ?  21  ALA B N     1 
ATOM   2200 C CA    . ALA B 1 21  ? 81.983 11.075  9.049   1.00 82.14  ?  21  ALA B CA    1 
ATOM   2201 C C     . ALA B 1 21  ? 82.215 9.794   9.839   1.00 85.04  ?  21  ALA B C     1 
ATOM   2202 O O     . ALA B 1 21  ? 83.320 9.237   9.826   1.00 86.89  ?  21  ALA B O     1 
ATOM   2203 C CB    . ALA B 1 21  ? 82.007 12.294  9.973   1.00 96.69  ?  21  ALA B CB    1 
ATOM   2204 N N     . LEU B 1 22  ? 81.162 9.286   10.488  1.00 85.62  ?  22  LEU B N     1 
ATOM   2205 C CA    . LEU B 1 22  ? 81.283 8.094   11.324  1.00 86.67  ?  22  LEU B CA    1 
ATOM   2206 C C     . LEU B 1 22  ? 81.669 6.858   10.503  1.00 88.38  ?  22  LEU B C     1 
ATOM   2207 O O     . LEU B 1 22  ? 82.625 6.149   10.851  1.00 95.13  ?  22  LEU B O     1 
ATOM   2208 C CB    . LEU B 1 22  ? 79.969 7.872   12.089  1.00 82.40  ?  22  LEU B CB    1 
ATOM   2209 C CG    . LEU B 1 22  ? 79.947 6.985   13.337  1.00 84.00  ?  22  LEU B CG    1 
ATOM   2210 C CD1   . LEU B 1 22  ? 78.686 7.255   14.141  1.00 84.24  ?  22  LEU B CD1   1 
ATOM   2211 C CD2   . LEU B 1 22  ? 80.076 5.487   13.009  1.00 91.83  ?  22  LEU B CD2   1 
ATOM   2212 N N     . TYR B 1 23  ? 80.932 6.571   9.417   1.00 82.43  ?  23  TYR B N     1 
ATOM   2213 C CA    . TYR B 1 23  ? 81.220 5.372   8.626   1.00 83.64  ?  23  TYR B CA    1 
ATOM   2214 C C     . TYR B 1 23  ? 82.564 5.476   7.936   1.00 88.09  ?  23  TYR B C     1 
ATOM   2215 O O     . TYR B 1 23  ? 83.288 4.476   7.817   1.00 96.01  ?  23  TYR B O     1 
ATOM   2216 C CB    . TYR B 1 23  ? 80.128 5.111   7.589   1.00 76.31  ?  23  TYR B CB    1 
ATOM   2217 C CG    . TYR B 1 23  ? 78.870 4.541   8.178   1.00 73.48  ?  23  TYR B CG    1 
ATOM   2218 C CD1   . TYR B 1 23  ? 78.758 3.178   8.472   1.00 75.40  ?  23  TYR B CD1   1 
ATOM   2219 C CD2   . TYR B 1 23  ? 77.795 5.369   8.457   1.00 73.38  ?  23  TYR B CD2   1 
ATOM   2220 C CE1   . TYR B 1 23  ? 77.600 2.671   9.028   1.00 80.78  ?  23  TYR B CE1   1 
ATOM   2221 C CE2   . TYR B 1 23  ? 76.648 4.876   9.007   1.00 71.26  ?  23  TYR B CE2   1 
ATOM   2222 C CZ    . TYR B 1 23  ? 76.545 3.538   9.296   1.00 78.53  ?  23  TYR B CZ    1 
ATOM   2223 O OH    . TYR B 1 23  ? 75.369 3.108   9.852   1.00 85.19  ?  23  TYR B OH    1 
ATOM   2224 N N     . ASP B 1 24  ? 82.900 6.674   7.466   1.00 86.80  ?  24  ASP B N     1 
ATOM   2225 C CA    . ASP B 1 24  ? 84.251 6.938   7.002   1.00 88.89  ?  24  ASP B CA    1 
ATOM   2226 C C     . ASP B 1 24  ? 85.285 6.468   8.036   1.00 99.19  ?  24  ASP B C     1 
ATOM   2227 O O     . ASP B 1 24  ? 86.265 5.781   7.701   1.00 100.71 ?  24  ASP B O     1 
ATOM   2228 C CB    . ASP B 1 24  ? 84.365 8.436   6.714   1.00 86.58  ?  24  ASP B CB    1 
ATOM   2229 C CG    . ASP B 1 24  ? 83.699 8.838   5.373   1.00 83.40  ?  24  ASP B CG    1 
ATOM   2230 O OD1   . ASP B 1 24  ? 83.723 8.003   4.461   1.00 83.05  ?  24  ASP B OD1   1 
ATOM   2231 O OD2   . ASP B 1 24  ? 83.190 9.974   5.202   1.00 83.19  -1 24  ASP B OD2   1 
ATOM   2232 N N     . ARG B 1 25  ? 85.046 6.796   9.314   1.00 99.76  ?  25  ARG B N     1 
ATOM   2233 C CA    . ARG B 1 25  ? 85.927 6.342   10.389  1.00 110.91 ?  25  ARG B CA    1 
ATOM   2234 C C     . ARG B 1 25  ? 85.899 4.820   10.523  1.00 104.88 ?  25  ARG B C     1 
ATOM   2235 O O     . ARG B 1 25  ? 86.953 4.173   10.538  1.00 106.94 ?  25  ARG B O     1 
ATOM   2236 C CB    . ARG B 1 25  ? 85.542 7.017   11.720  1.00 112.53 ?  25  ARG B CB    1 
ATOM   2237 N N     . PHE B 1 26  ? 84.697 4.223   10.584  1.00 103.40 ?  26  PHE B N     1 
ATOM   2238 C CA    . PHE B 1 26  ? 84.550 2.866   11.110  1.00 110.30 ?  26  PHE B CA    1 
ATOM   2239 C C     . PHE B 1 26  ? 84.091 1.846   10.065  1.00 105.57 ?  26  PHE B C     1 
ATOM   2240 O O     . PHE B 1 26  ? 83.722 0.716   10.426  1.00 108.51 ?  26  PHE B O     1 
ATOM   2241 C CB    . PHE B 1 26  ? 83.636 2.879   12.356  1.00 110.60 ?  26  PHE B CB    1 
ATOM   2242 C CG    . PHE B 1 26  ? 84.259 3.601   13.564  1.00 117.18 ?  26  PHE B CG    1 
ATOM   2243 C CD1   . PHE B 1 26  ? 85.652 3.650   13.735  1.00 116.12 ?  26  PHE B CD1   1 
ATOM   2244 C CD2   . PHE B 1 26  ? 83.461 4.245   14.511  1.00 115.27 ?  26  PHE B CD2   1 
ATOM   2245 C CE1   . PHE B 1 26  ? 86.228 4.316   14.831  1.00 112.31 ?  26  PHE B CE1   1 
ATOM   2246 C CE2   . PHE B 1 26  ? 84.037 4.917   15.609  1.00 118.71 ?  26  PHE B CE2   1 
ATOM   2247 C CZ    . PHE B 1 26  ? 85.414 4.968   15.744  1.00 112.93 ?  26  PHE B CZ    1 
ATOM   2248 N N     . THR B 1 27  ? 84.122 2.193   8.784   1.00 99.94  ?  27  THR B N     1 
ATOM   2249 C CA    . THR B 1 27  ? 84.161 1.152   7.758   1.00 107.21 ?  27  THR B CA    1 
ATOM   2250 C C     . THR B 1 27  ? 85.598 0.880   7.357   1.00 110.33 ?  27  THR B C     1 
ATOM   2251 O O     . THR B 1 27  ? 85.924 0.767   6.181   1.00 106.93 ?  27  THR B O     1 
ATOM   2252 C CB    . THR B 1 27  ? 83.346 1.564   6.537   1.00 95.88  ?  27  THR B CB    1 
ATOM   2253 O OG1   . THR B 1 27  ? 83.873 2.797   6.018   1.00 90.92  ?  27  THR B OG1   1 
ATOM   2254 C CG2   . THR B 1 27  ? 81.871 1.737   6.873   1.00 88.66  ?  27  THR B CG2   1 
ATOM   2255 N N     . ALA B 1 28  ? 86.475 0.758   8.343   1.00 112.65 ?  28  ALA B N     1 
ATOM   2256 C CA    . ALA B 1 28  ? 87.893 0.567   8.054   1.00 116.82 ?  28  ALA B CA    1 
ATOM   2257 C C     . ALA B 1 28  ? 88.458 -0.139  9.283   1.00 123.98 ?  28  ALA B C     1 
ATOM   2258 O O     . ALA B 1 28  ? 88.775 0.519   10.276  1.00 129.05 ?  28  ALA B O     1 
ATOM   2259 C CB    . ALA B 1 28  ? 88.595 1.890   7.777   1.00 110.15 ?  28  ALA B CB    1 
ATOM   2260 N N     . LEU B 1 29  ? 88.617 -1.459  9.184   1.00 124.65 ?  29  LEU B N     1 
ATOM   2261 C CA    . LEU B 1 29  ? 88.553 -2.386  10.314  1.00 128.06 ?  29  LEU B CA    1 
ATOM   2262 C C     . LEU B 1 29  ? 87.137 -2.441  10.896  1.00 121.69 ?  29  LEU B C     1 
ATOM   2263 O O     . LEU B 1 29  ? 86.928 -3.051  11.953  1.00 123.21 ?  29  LEU B O     1 
ATOM   2264 C CB    . LEU B 1 29  ? 89.585 -2.070  11.417  1.00 130.23 ?  29  LEU B CB    1 
ATOM   2265 N N     . GLY B 1 30  ? 86.152 -1.808  10.240  1.00 120.10 ?  30  GLY B N     1 
ATOM   2266 C CA    . GLY B 1 30  ? 84.762 -2.124  10.522  1.00 117.37 ?  30  GLY B CA    1 
ATOM   2267 C C     . GLY B 1 30  ? 84.289 -3.320  9.729   1.00 121.48 ?  30  GLY B C     1 
ATOM   2268 O O     . GLY B 1 30  ? 83.412 -4.066  10.181  1.00 117.82 ?  30  GLY B O     1 
ATOM   2269 N N     . ALA B 1 31  ? 84.884 -3.541  8.557   1.00 122.09 ?  31  ALA B N     1 
ATOM   2270 C CA    . ALA B 1 31  ? 84.622 -4.758  7.799   1.00 118.22 ?  31  ALA B CA    1 
ATOM   2271 C C     . ALA B 1 31  ? 85.233 -5.997  8.458   1.00 118.95 ?  31  ALA B C     1 
ATOM   2272 O O     . ALA B 1 31  ? 84.716 -7.102  8.264   1.00 115.40 ?  31  ALA B O     1 
ATOM   2273 C CB    . ALA B 1 31  ? 85.149 -4.605  6.370   1.00 114.41 ?  31  ALA B CB    1 
ATOM   2274 N N     . ALA B 1 32  ? 86.322 -5.852  9.228   1.00 121.03 ?  32  ALA B N     1 
ATOM   2275 C CA    . ALA B 1 32  ? 87.042 -7.011  9.774   1.00 123.07 ?  32  ALA B CA    1 
ATOM   2276 C C     . ALA B 1 32  ? 86.382 -7.609  11.014  1.00 120.15 ?  32  ALA B C     1 
ATOM   2277 O O     . ALA B 1 32  ? 86.866 -8.638  11.514  1.00 114.43 ?  32  ALA B O     1 
ATOM   2278 C CB    . ALA B 1 32  ? 88.491 -6.645  10.114  1.00 117.74 ?  32  ALA B CB    1 
ATOM   2279 N N     . SER B 1 33  ? 85.311 -6.978  11.513  1.00 118.75 ?  33  SER B N     1 
ATOM   2280 C CA    . SER B 1 33  ? 84.585 -7.405  12.706  1.00 116.34 ?  33  SER B CA    1 
ATOM   2281 C C     . SER B 1 33  ? 83.271 -8.109  12.378  1.00 116.05 ?  33  SER B C     1 
ATOM   2282 O O     . SER B 1 33  ? 83.063 -9.270  12.747  1.00 114.01 ?  33  SER B O     1 
ATOM   2283 C CB    . SER B 1 33  ? 84.320 -6.178  13.578  1.00 117.73 ?  33  SER B CB    1 
ATOM   2284 O OG    . SER B 1 33  ? 83.880 -5.107  12.761  1.00 121.44 ?  33  SER B OG    1 
ATOM   2285 N N     . LEU B 1 34  ? 82.361 -7.414  11.698  1.00 115.27 ?  34  LEU B N     1 
ATOM   2286 C CA    . LEU B 1 34  ? 81.131 -8.025  11.219  1.00 112.52 ?  34  LEU B CA    1 
ATOM   2287 C C     . LEU B 1 34  ? 81.305 -8.645  9.839   1.00 112.83 ?  34  LEU B C     1 
ATOM   2288 O O     . LEU B 1 34  ? 80.920 -9.797  9.614   1.00 112.63 ?  34  LEU B O     1 
ATOM   2289 C CB    . LEU B 1 34  ? 80.032 -6.978  11.182  1.00 110.07 ?  34  LEU B CB    1 
ATOM   2290 C CG    . LEU B 1 34  ? 78.889 -7.462  10.317  1.00 107.92 ?  34  LEU B CG    1 
ATOM   2291 C CD1   . LEU B 1 34  ? 78.155 -8.627  10.956  1.00 102.48 ?  34  LEU B CD1   1 
ATOM   2292 C CD2   . LEU B 1 34  ? 77.983 -6.296  10.176  1.00 103.60 ?  34  LEU B CD2   1 
ATOM   2293 N N     . GLY B 1 35  ? 81.897 -7.887  8.917   1.00 113.66 ?  35  GLY B N     1 
ATOM   2294 C CA    . GLY B 1 35  ? 82.063 -8.327  7.553   1.00 106.63 ?  35  GLY B CA    1 
ATOM   2295 C C     . GLY B 1 35  ? 81.417 -7.354  6.577   1.00 94.71  ?  35  GLY B C     1 
ATOM   2296 O O     . GLY B 1 35  ? 81.416 -6.147  6.781   1.00 96.00  ?  35  GLY B O     1 
ATOM   2297 N N     . GLU B 1 36  ? 80.864 -7.943  5.511   1.00 90.92  ?  36  GLU B N     1 
ATOM   2298 C CA    . GLU B 1 36  ? 80.432 -7.184  4.347   1.00 85.14  ?  36  GLU B CA    1 
ATOM   2299 C C     . GLU B 1 36  ? 79.000 -6.653  4.488   1.00 78.55  ?  36  GLU B C     1 
ATOM   2300 O O     . GLU B 1 36  ? 78.697 -5.551  4.022   1.00 77.22  ?  36  GLU B O     1 
ATOM   2301 C CB    . GLU B 1 36  ? 80.584 -8.059  3.093   1.00 89.68  ?  36  GLU B CB    1 
ATOM   2302 C CG    . GLU B 1 36  ? 81.990 -8.620  2.800   1.00 95.27  ?  36  GLU B CG    1 
ATOM   2303 C CD    . GLU B 1 36  ? 83.071 -7.546  2.603   1.00 102.91 ?  36  GLU B CD    1 
ATOM   2304 O OE1   . GLU B 1 36  ? 82.740 -6.397  2.226   1.00 103.93 ?  36  GLU B OE1   1 
ATOM   2305 O OE2   . GLU B 1 36  ? 84.262 -7.858  2.827   1.00 103.87 -1 36  GLU B OE2   1 
ATOM   2306 N N     . ASN B 1 37  ? 78.098 -7.404  5.109   1.00 74.87  ?  37  ASN B N     1 
ATOM   2307 C CA    . ASN B 1 37  ? 76.715 -6.963  5.288   1.00 71.99  ?  37  ASN B CA    1 
ATOM   2308 C C     . ASN B 1 37  ? 76.622 -6.160  6.578   1.00 78.62  ?  37  ASN B C     1 
ATOM   2309 O O     . ASN B 1 37  ? 76.689 -6.737  7.662   1.00 83.04  ?  37  ASN B O     1 
ATOM   2310 C CB    . ASN B 1 37  ? 75.765 -8.157  5.361   1.00 72.15  ?  37  ASN B CB    1 
ATOM   2311 C CG    . ASN B 1 37  ? 75.131 -8.506  4.030   1.00 71.19  ?  37  ASN B CG    1 
ATOM   2312 O OD1   . ASN B 1 37  ? 75.015 -7.686  3.131   1.00 76.41  ?  37  ASN B OD1   1 
ATOM   2313 N ND2   . ASN B 1 37  ? 74.667 -9.733  3.925   1.00 72.50  ?  37  ASN B ND2   1 
ATOM   2314 N N     . LEU B 1 38  ? 76.429 -4.842  6.476   1.00 78.71  ?  38  LEU B N     1 
ATOM   2315 C CA    . LEU B 1 38  ? 76.268 -4.004  7.672   1.00 74.33  ?  38  LEU B CA    1 
ATOM   2316 C C     . LEU B 1 38  ? 74.800 -3.954  8.095   1.00 75.66  ?  38  LEU B C     1 
ATOM   2317 O O     . LEU B 1 38  ? 74.162 -2.902  8.109   1.00 73.00  ?  38  LEU B O     1 
ATOM   2318 C CB    . LEU B 1 38  ? 76.814 -2.600  7.436   1.00 69.38  ?  38  LEU B CB    1 
ATOM   2319 C CG    . LEU B 1 38  ? 78.213 -2.504  6.823   1.00 71.11  ?  38  LEU B CG    1 
ATOM   2320 C CD1   . LEU B 1 38  ? 78.744 -1.070  6.857   1.00 75.94  ?  38  LEU B CD1   1 
ATOM   2321 C CD2   . LEU B 1 38  ? 79.196 -3.477  7.471   1.00 76.77  ?  38  LEU B CD2   1 
ATOM   2322 N N     . HIS B 1 39  ? 74.276 -5.129  8.442   1.00 73.88  ?  39  HIS B N     1 
ATOM   2323 C CA    . HIS B 1 39  ? 72.920 -5.264  8.967   1.00 74.66  ?  39  HIS B CA    1 
ATOM   2324 C C     . HIS B 1 39  ? 72.809 -6.574  9.755   1.00 76.20  ?  39  HIS B C     1 
ATOM   2325 O O     . HIS B 1 39  ? 73.719 -7.413  9.745   1.00 78.29  ?  39  HIS B O     1 
ATOM   2326 C CB    . HIS B 1 39  ? 71.860 -5.174  7.848   1.00 73.40  ?  39  HIS B CB    1 
ATOM   2327 C CG    . HIS B 1 39  ? 71.927 -6.269  6.816   1.00 73.50  ?  39  HIS B CG    1 
ATOM   2328 N ND1   . HIS B 1 39  ? 72.604 -6.127  5.620   1.00 73.87  ?  39  HIS B ND1   1 
ATOM   2329 C CD2   . HIS B 1 39  ? 71.354 -7.498  6.778   1.00 69.32  ?  39  HIS B CD2   1 
ATOM   2330 C CE1   . HIS B 1 39  ? 72.464 -7.232  4.907   1.00 69.79  ?  39  HIS B CE1   1 
ATOM   2331 N NE2   . HIS B 1 39  ? 71.716 -8.081  5.589   1.00 66.39  ?  39  HIS B NE2   1 
ATOM   2332 N N     . PHE B 1 40  ? 71.677 -6.727  10.457  1.00 76.50  ?  40  PHE B N     1 
ATOM   2333 C CA    . PHE B 1 40  ? 71.435 -7.876  11.325  1.00 72.08  ?  40  PHE B CA    1 
ATOM   2334 C C     . PHE B 1 40  ? 71.361 -9.173  10.529  1.00 72.02  ?  40  PHE B C     1 
ATOM   2335 O O     . PHE B 1 40  ? 71.142 -9.177  9.319   1.00 77.71  ?  40  PHE B O     1 
ATOM   2336 C CB    . PHE B 1 40  ? 70.124 -7.711  12.093  1.00 74.39  ?  40  PHE B CB    1 
ATOM   2337 C CG    . PHE B 1 40  ? 70.226 -6.839  13.323  1.00 80.81  ?  40  PHE B CG    1 
ATOM   2338 C CD1   . PHE B 1 40  ? 70.639 -7.373  14.550  1.00 84.42  ?  40  PHE B CD1   1 
ATOM   2339 C CD2   . PHE B 1 40  ? 69.866 -5.487  13.265  1.00 81.53  ?  40  PHE B CD2   1 
ATOM   2340 C CE1   . PHE B 1 40  ? 70.702 -6.560  15.685  1.00 84.11  ?  40  PHE B CE1   1 
ATOM   2341 C CE2   . PHE B 1 40  ? 69.928 -4.664  14.399  1.00 81.99  ?  40  PHE B CE2   1 
ATOM   2342 C CZ    . PHE B 1 40  ? 70.343 -5.193  15.601  1.00 85.66  ?  40  PHE B CZ    1 
ATOM   2343 N N     . GLY B 1 41  ? 71.564 -10.297 11.230  1.00 73.26  ?  41  GLY B N     1 
ATOM   2344 C CA    . GLY B 1 41  ? 71.266 -11.605 10.678  1.00 72.37  ?  41  GLY B CA    1 
ATOM   2345 C C     . GLY B 1 41  ? 69.835 -12.041 10.988  1.00 73.02  ?  41  GLY B C     1 
ATOM   2346 O O     . GLY B 1 41  ? 69.139 -11.420 11.790  1.00 73.03  ?  41  GLY B O     1 
ATOM   2347 N N     . TYR B 1 42  ? 69.401 -13.125 10.336  1.00 71.21  ?  42  TYR B N     1 
ATOM   2348 C CA    . TYR B 1 42  ? 68.074 -13.681 10.594  1.00 73.80  ?  42  TYR B CA    1 
ATOM   2349 C C     . TYR B 1 42  ? 68.107 -15.194 10.579  1.00 80.41  ?  42  TYR B C     1 
ATOM   2350 O O     . TYR B 1 42  ? 68.604 -15.792 9.620   1.00 80.70  ?  42  TYR B O     1 
ATOM   2351 C CB    . TYR B 1 42  ? 67.081 -13.213 9.560   1.00 66.95  ?  42  TYR B CB    1 
ATOM   2352 C CG    . TYR B 1 42  ? 65.663 -13.657 9.776   1.00 66.43  ?  42  TYR B CG    1 
ATOM   2353 C CD1   . TYR B 1 42  ? 65.253 -14.941 9.495   1.00 66.99  ?  42  TYR B CD1   1 
ATOM   2354 C CD2   . TYR B 1 42  ? 64.712 -12.753 10.175  1.00 63.39  ?  42  TYR B CD2   1 
ATOM   2355 C CE1   . TYR B 1 42  ? 63.938 -15.306 9.652   1.00 66.40  ?  42  TYR B CE1   1 
ATOM   2356 C CE2   . TYR B 1 42  ? 63.408 -13.103 10.322  1.00 62.70  ?  42  TYR B CE2   1 
ATOM   2357 C CZ    . TYR B 1 42  ? 63.023 -14.369 10.063  1.00 62.26  ?  42  TYR B CZ    1 
ATOM   2358 O OH    . TYR B 1 42  ? 61.700 -14.665 10.237  1.00 56.38  ?  42  TYR B OH    1 
ATOM   2359 N N     . TRP B 1 43  ? 67.520 -15.805 11.610  1.00 78.77  ?  43  TRP B N     1 
ATOM   2360 C CA    . TRP B 1 43  ? 67.489 -17.250 11.760  1.00 81.85  ?  43  TRP B CA    1 
ATOM   2361 C C     . TRP B 1 43  ? 66.077 -17.708 12.069  1.00 86.17  ?  43  TRP B C     1 
ATOM   2362 O O     . TRP B 1 43  ? 65.252 -16.944 12.577  1.00 80.44  ?  43  TRP B O     1 
ATOM   2363 C CB    . TRP B 1 43  ? 68.408 -17.710 12.866  1.00 84.48  ?  43  TRP B CB    1 
ATOM   2364 C CG    . TRP B 1 43  ? 69.826 -17.403 12.617  1.00 80.98  ?  43  TRP B CG    1 
ATOM   2365 C CD1   . TRP B 1 43  ? 70.771 -18.256 12.114  1.00 82.42  ?  43  TRP B CD1   1 
ATOM   2366 C CD2   . TRP B 1 43  ? 70.493 -16.155 12.866  1.00 79.88  ?  43  TRP B CD2   1 
ATOM   2367 N NE1   . TRP B 1 43  ? 71.986 -17.614 12.039  1.00 81.75  ?  43  TRP B NE1   1 
ATOM   2368 C CE2   . TRP B 1 43  ? 71.840 -16.323 12.492  1.00 81.10  ?  43  TRP B CE2   1 
ATOM   2369 C CE3   . TRP B 1 43  ? 70.083 -14.912 13.359  1.00 76.35  ?  43  TRP B CE3   1 
ATOM   2370 C CZ2   . TRP B 1 43  ? 72.780 -15.281 12.592  1.00 76.95  ?  43  TRP B CZ2   1 
ATOM   2371 C CZ3   . TRP B 1 43  ? 71.023 -13.890 13.462  1.00 75.14  ?  43  TRP B CZ3   1 
ATOM   2372 C CH2   . TRP B 1 43  ? 72.347 -14.083 13.079  1.00 73.73  ?  43  TRP B CH2   1 
ATOM   2373 N N     . ASP B 1 44  ? 65.809 -18.975 11.767  1.00 86.36  ?  44  ASP B N     1 
ATOM   2374 C CA    . ASP B 1 44  ? 64.447 -19.475 11.887  1.00 93.37  ?  44  ASP B CA    1 
ATOM   2375 C C     . ASP B 1 44  ? 64.028 -19.665 13.337  1.00 95.91  ?  44  ASP B C     1 
ATOM   2376 O O     . ASP B 1 44  ? 62.841 -19.518 13.672  1.00 95.51  ?  44  ASP B O     1 
ATOM   2377 C CB    . ASP B 1 44  ? 64.340 -20.762 11.103  1.00 95.71  ?  44  ASP B CB    1 
ATOM   2378 C CG    . ASP B 1 44  ? 64.605 -20.530 9.652   1.00 93.46  ?  44  ASP B CG    1 
ATOM   2379 O OD1   . ASP B 1 44  ? 63.819 -19.759 9.049   1.00 89.86  ?  44  ASP B OD1   1 
ATOM   2380 O OD2   . ASP B 1 44  ? 65.621 -21.058 9.143   1.00 96.63  -1 44  ASP B OD2   1 
ATOM   2381 N N     . SER B 1 45  ? 64.975 -20.009 14.197  1.00 95.27  ?  45  SER B N     1 
ATOM   2382 C CA    . SER B 1 45  ? 64.747 -20.082 15.631  1.00 98.35  ?  45  SER B CA    1 
ATOM   2383 C C     . SER B 1 45  ? 66.098 -19.962 16.324  1.00 98.37  ?  45  SER B C     1 
ATOM   2384 O O     . SER B 1 45  ? 67.129 -20.314 15.728  1.00 98.00  ?  45  SER B O     1 
ATOM   2385 C CB    . SER B 1 45  ? 64.026 -21.388 16.019  1.00 104.50 ?  45  SER B CB    1 
ATOM   2386 O OG    . SER B 1 45  ? 64.720 -22.536 15.548  1.00 107.70 ?  45  SER B OG    1 
ATOM   2387 N N     . PRO B 1 46  ? 66.129 -19.476 17.580  1.00 99.33  ?  46  PRO B N     1 
ATOM   2388 C CA    . PRO B 1 46  ? 67.394 -18.950 18.131  1.00 98.48  ?  46  PRO B CA    1 
ATOM   2389 C C     . PRO B 1 46  ? 68.535 -19.956 18.116  1.00 101.92 ?  46  PRO B C     1 
ATOM   2390 O O     . PRO B 1 46  ? 69.702 -19.559 18.122  1.00 99.25  ?  46  PRO B O     1 
ATOM   2391 C CB    . PRO B 1 46  ? 67.009 -18.548 19.561  1.00 90.31  ?  46  PRO B CB    1 
ATOM   2392 C CG    . PRO B 1 46  ? 65.534 -18.344 19.520  1.00 87.56  ?  46  PRO B CG    1 
ATOM   2393 C CD    . PRO B 1 46  ? 65.019 -19.345 18.548  1.00 94.32  ?  46  PRO B CD    1 
ATOM   2394 N N     . ASP B 1 47  ? 68.222 -21.244 18.054  1.00 101.10 ?  47  ASP B N     1 
ATOM   2395 C CA    . ASP B 1 47  ? 69.160 -22.361 18.097  1.00 102.79 ?  47  ASP B CA    1 
ATOM   2396 C C     . ASP B 1 47  ? 69.924 -22.594 16.793  1.00 103.33 ?  47  ASP B C     1 
ATOM   2397 O O     . ASP B 1 47  ? 70.841 -23.432 16.788  1.00 102.23 ?  47  ASP B O     1 
ATOM   2398 C CB    . ASP B 1 47  ? 68.369 -23.621 18.407  1.00 105.90 ?  47  ASP B CB    1 
ATOM   2399 C CG    . ASP B 1 47  ? 67.063 -23.675 17.607  1.00 110.97 ?  47  ASP B CG    1 
ATOM   2400 O OD1   . ASP B 1 47  ? 67.101 -23.293 16.407  1.00 108.23 ?  47  ASP B OD1   1 
ATOM   2401 O OD2   . ASP B 1 47  ? 66.012 -24.098 18.165  1.00 116.36 -1 47  ASP B OD2   1 
ATOM   2402 N N     . SER B 1 48  ? 69.540 -21.920 15.696  1.00 103.97 ?  48  SER B N     1 
ATOM   2403 C CA    . SER B 1 48  ? 70.052 -22.238 14.361  1.00 100.00 ?  48  SER B CA    1 
ATOM   2404 C C     . SER B 1 48  ? 71.581 -22.241 14.358  1.00 92.20  ?  48  SER B C     1 
ATOM   2405 O O     . SER B 1 48  ? 72.235 -21.544 15.134  1.00 94.82  ?  48  SER B O     1 
ATOM   2406 C CB    . SER B 1 48  ? 69.500 -21.227 13.342  1.00 93.77  ?  48  SER B CB    1 
ATOM   2407 O OG    . SER B 1 48  ? 69.777 -21.540 11.984  1.00 92.10  ?  48  SER B OG    1 
ATOM   2408 N N     . GLN B 1 49  ? 72.161 -23.086 13.526  1.00 90.35  ?  49  GLN B N     1 
ATOM   2409 C CA    . GLN B 1 49  ? 73.604 -23.157 13.465  1.00 90.01  ?  49  GLN B CA    1 
ATOM   2410 C C     . GLN B 1 49  ? 74.151 -22.455 12.237  1.00 88.75  ?  49  GLN B C     1 
ATOM   2411 O O     . GLN B 1 49  ? 75.302 -22.684 11.871  1.00 90.33  ?  49  GLN B O     1 
ATOM   2412 C CB    . GLN B 1 49  ? 74.055 -24.618 13.503  1.00 88.68  ?  49  GLN B CB    1 
ATOM   2413 N N     . VAL B 1 50  ? 73.343 -21.644 11.567  1.00 87.67  ?  50  VAL B N     1 
ATOM   2414 C CA    . VAL B 1 50  ? 73.713 -21.121 10.249  1.00 87.16  ?  50  VAL B CA    1 
ATOM   2415 C C     . VAL B 1 50  ? 74.691 -19.951 10.430  1.00 82.06  ?  50  VAL B C     1 
ATOM   2416 O O     . VAL B 1 50  ? 74.438 -19.087 11.270  1.00 80.67  ?  50  VAL B O     1 
ATOM   2417 C CB    . VAL B 1 50  ? 72.468 -20.682 9.490   1.00 88.09  ?  50  VAL B CB    1 
ATOM   2418 C CG1   . VAL B 1 50  ? 72.797 -20.218 8.064   1.00 85.30  ?  50  VAL B CG1   1 
ATOM   2419 C CG2   . VAL B 1 50  ? 71.427 -21.781 9.497   1.00 87.60  ?  50  VAL B CG2   1 
ATOM   2420 N N     . PRO B 1 51  ? 75.792 -19.895 9.674   1.00 81.82  ?  51  PRO B N     1 
ATOM   2421 C CA    . PRO B 1 51  ? 76.782 -18.840 9.924   1.00 83.57  ?  51  PRO B CA    1 
ATOM   2422 C C     . PRO B 1 51  ? 76.149 -17.483 9.739   1.00 85.26  ?  51  PRO B C     1 
ATOM   2423 O O     . PRO B 1 51  ? 75.207 -17.311 8.961   1.00 87.47  ?  51  PRO B O     1 
ATOM   2424 C CB    . PRO B 1 51  ? 77.859 -19.079 8.855   1.00 83.99  ?  51  PRO B CB    1 
ATOM   2425 C CG    . PRO B 1 51  ? 77.618 -20.427 8.318   1.00 88.01  ?  51  PRO B CG    1 
ATOM   2426 C CD    . PRO B 1 51  ? 76.142 -20.697 8.488   1.00 86.05  ?  51  PRO B CD    1 
ATOM   2427 N N     . LEU B 1 52  ? 76.679 -16.517 10.478  1.00 88.39  ?  52  LEU B N     1 
ATOM   2428 C CA    . LEU B 1 52  ? 76.187 -15.153 10.353  1.00 87.99  ?  52  LEU B CA    1 
ATOM   2429 C C     . LEU B 1 52  ? 76.353 -14.648 8.929   1.00 84.55  ?  52  LEU B C     1 
ATOM   2430 O O     . LEU B 1 52  ? 75.454 -13.991 8.378   1.00 81.53  ?  52  LEU B O     1 
ATOM   2431 C CB    . LEU B 1 52  ? 76.925 -14.250 11.325  1.00 86.65  ?  52  LEU B CB    1 
ATOM   2432 C CG    . LEU B 1 52  ? 76.431 -12.858 11.017  1.00 85.26  ?  52  LEU B CG    1 
ATOM   2433 C CD1   . LEU B 1 52  ? 75.049 -12.688 11.625  1.00 85.41  ?  52  LEU B CD1   1 
ATOM   2434 C CD2   . LEU B 1 52  ? 77.416 -11.864 11.519  1.00 86.61  ?  52  LEU B CD2   1 
ATOM   2435 N N     . ALA B 1 53  ? 77.499 -14.954 8.320   1.00 85.33  ?  53  ALA B N     1 
ATOM   2436 C CA    . ALA B 1 53  ? 77.701 -14.667 6.914   1.00 82.83  ?  53  ALA B CA    1 
ATOM   2437 C C     . ALA B 1 53  ? 76.419 -14.960 6.145   1.00 82.52  ?  53  ALA B C     1 
ATOM   2438 O O     . ALA B 1 53  ? 75.779 -14.057 5.585   1.00 77.62  ?  53  ALA B O     1 
ATOM   2439 C CB    . ALA B 1 53  ? 78.873 -15.505 6.394   1.00 80.80  ?  53  ALA B CB    1 
ATOM   2440 N N     . GLU B 1 54  ? 75.982 -16.218 6.214   1.00 86.40  ?  54  GLU B N     1 
ATOM   2441 C CA    . GLU B 1 54  ? 74.818 -16.643 5.453   1.00 79.03  ?  54  GLU B CA    1 
ATOM   2442 C C     . GLU B 1 54  ? 73.546 -15.954 5.937   1.00 78.02  ?  54  GLU B C     1 
ATOM   2443 O O     . GLU B 1 54  ? 72.729 -15.517 5.118   1.00 77.69  ?  54  GLU B O     1 
ATOM   2444 C CB    . GLU B 1 54  ? 74.696 -18.159 5.522   1.00 81.58  ?  54  GLU B CB    1 
ATOM   2445 C CG    . GLU B 1 54  ? 73.572 -18.719 4.695   1.00 88.54  ?  54  GLU B CG    1 
ATOM   2446 C CD    . GLU B 1 54  ? 73.504 -20.238 4.768   1.00 94.61  ?  54  GLU B CD    1 
ATOM   2447 O OE1   . GLU B 1 54  ? 74.558 -20.869 5.057   1.00 89.19  ?  54  GLU B OE1   1 
ATOM   2448 O OE2   . GLU B 1 54  ? 72.393 -20.787 4.552   1.00 96.63  -1 54  GLU B OE2   1 
ATOM   2449 N N     . ALA B 1 55  ? 73.377 -15.809 7.258   1.00 80.61  ?  55  ALA B N     1 
ATOM   2450 C CA    . ALA B 1 55  ? 72.097 -15.330 7.788   1.00 77.96  ?  55  ALA B CA    1 
ATOM   2451 C C     . ALA B 1 55  ? 71.835 -13.855 7.491   1.00 74.46  ?  55  ALA B C     1 
ATOM   2452 O O     . ALA B 1 55  ? 70.665 -13.447 7.420   1.00 69.61  ?  55  ALA B O     1 
ATOM   2453 C CB    . ALA B 1 55  ? 72.021 -15.553 9.287   1.00 79.71  ?  55  ALA B CB    1 
ATOM   2454 N N     . THR B 1 56  ? 72.890 -13.038 7.363   1.00 73.79  ?  56  THR B N     1 
ATOM   2455 C CA    . THR B 1 56  ? 72.703 -11.654 6.936   1.00 68.29  ?  56  THR B CA    1 
ATOM   2456 C C     . THR B 1 56  ? 72.212 -11.586 5.498   1.00 71.71  ?  56  THR B C     1 
ATOM   2457 O O     . THR B 1 56  ? 71.304 -10.803 5.185   1.00 67.42  ?  56  THR B O     1 
ATOM   2458 C CB    . THR B 1 56  ? 73.995 -10.859 7.084   1.00 69.54  ?  56  THR B CB    1 
ATOM   2459 O OG1   . THR B 1 56  ? 75.098 -11.668 6.667   1.00 71.82  ?  56  THR B OG1   1 
ATOM   2460 C CG2   . THR B 1 56  ? 74.183 -10.434 8.528   1.00 76.49  ?  56  THR B CG2   1 
ATOM   2461 N N     . ASP B 1 57  ? 72.798 -12.403 4.609   1.00 73.25  ?  57  ASP B N     1 
ATOM   2462 C CA    . ASP B 1 57  ? 72.301 -12.458 3.238   1.00 68.57  ?  57  ASP B CA    1 
ATOM   2463 C C     . ASP B 1 57  ? 70.826 -12.799 3.223   1.00 66.52  ?  57  ASP B C     1 
ATOM   2464 O O     . ASP B 1 57  ? 70.081 -12.292 2.379   1.00 65.83  ?  57  ASP B O     1 
ATOM   2465 C CB    . ASP B 1 57  ? 73.097 -13.473 2.413   1.00 68.01  ?  57  ASP B CB    1 
ATOM   2466 C CG    . ASP B 1 57  ? 74.397 -12.897 1.877   1.00 70.73  ?  57  ASP B CG    1 
ATOM   2467 O OD1   . ASP B 1 57  ? 74.457 -11.660 1.676   1.00 71.65  ?  57  ASP B OD1   1 
ATOM   2468 O OD2   . ASP B 1 57  ? 75.360 -13.670 1.658   1.00 73.66  -1 57  ASP B OD2   1 
ATOM   2469 N N     . ARG B 1 58  ? 70.402 -13.625 4.172   1.00 63.37  ?  58  ARG B N     1 
ATOM   2470 C CA    . ARG B 1 58  ? 68.970 -14.005 4.264   1.00 65.73  ?  58  ARG B CA    1 
ATOM   2471 C C     . ARG B 1 58  ? 68.126 -12.741 4.446   1.00 68.29  ?  58  ARG B C     1 
ATOM   2472 O O     . ARG B 1 58  ? 67.129 -12.600 3.726   1.00 66.14  ?  58  ARG B O     1 
ATOM   2473 C CB    . ARG B 1 58  ? 68.754 -14.987 5.417   1.00 69.95  ?  58  ARG B CB    1 
ATOM   2474 C CG    . ARG B 1 58  ? 67.304 -15.143 5.850   1.00 71.63  ?  58  ARG B CG    1 
ATOM   2475 C CD    . ARG B 1 58  ? 66.749 -16.484 5.417   1.00 71.54  ?  58  ARG B CD    1 
ATOM   2476 N NE    . ARG B 1 58  ? 65.409 -16.717 5.933   1.00 79.13  ?  58  ARG B NE    1 
ATOM   2477 C CZ    . ARG B 1 58  ? 65.103 -17.642 6.834   1.00 78.12  ?  58  ARG B CZ    1 
ATOM   2478 N NH1   . ARG B 1 58  ? 66.056 -18.369 7.387   1.00 77.09  ?  58  ARG B NH1   1 
ATOM   2479 N NH2   . ARG B 1 58  ? 63.843 -17.836 7.179   1.00 80.28  ?  58  ARG B NH2   1 
ATOM   2480 N N     . LEU B 1 59  ? 68.500 -11.859 5.372   1.00 67.05  ?  59  LEU B N     1 
ATOM   2481 C CA    . LEU B 1 59  ? 67.662 -10.680 5.539   1.00 61.93  ?  59  LEU B CA    1 
ATOM   2482 C C     . LEU B 1 59  ? 67.629 -9.846  4.261   1.00 62.91  ?  59  LEU B C     1 
ATOM   2483 O O     . LEU B 1 59  ? 66.560 -9.339  3.892   1.00 60.68  ?  59  LEU B O     1 
ATOM   2484 C CB    . LEU B 1 59  ? 68.113 -9.821  6.721   1.00 63.87  ?  59  LEU B CB    1 
ATOM   2485 C CG    . LEU B 1 59  ? 67.138 -8.650  6.996   1.00 61.08  ?  59  LEU B CG    1 
ATOM   2486 C CD1   . LEU B 1 59  ? 65.891 -9.125  7.704   1.00 61.49  ?  59  LEU B CD1   1 
ATOM   2487 C CD2   . LEU B 1 59  ? 67.751 -7.483  7.753   1.00 61.97  ?  59  LEU B CD2   1 
ATOM   2488 N N     . THR B 1 60  ? 68.779 -9.693  3.569   1.00 62.68  ?  60  THR B N     1 
ATOM   2489 C CA    . THR B 1 60  ? 68.767 -9.003  2.276   1.00 57.08  ?  60  THR B CA    1 
ATOM   2490 C C     . THR B 1 60  ? 67.667 -9.569  1.435   1.00 60.18  ?  60  THR B C     1 
ATOM   2491 O O     . THR B 1 60  ? 66.868 -8.839  0.841   1.00 58.12  ?  60  THR B O     1 
ATOM   2492 C CB    . THR B 1 60  ? 70.045 -9.196  1.461   1.00 60.19  ?  60  THR B CB    1 
ATOM   2493 O OG1   . THR B 1 60  ? 71.210 -8.800  2.182   1.00 66.66  ?  60  THR B OG1   1 
ATOM   2494 C CG2   . THR B 1 60  ? 69.927 -8.372  0.191   1.00 58.44  ?  60  THR B CG2   1 
ATOM   2495 N N     . ASP B 1 61  ? 67.619 -10.898 1.401   1.00 61.70  ?  61  ASP B N     1 
ATOM   2496 C CA    . ASP B 1 61  ? 66.778 -11.605 0.452   1.00 61.53  ?  61  ASP B CA    1 
ATOM   2497 C C     . ASP B 1 61  ? 65.306 -11.413 0.792   1.00 60.29  ?  61  ASP B C     1 
ATOM   2498 O O     . ASP B 1 61  ? 64.517 -11.010 -0.072  1.00 62.00  ?  61  ASP B O     1 
ATOM   2499 C CB    . ASP B 1 61  ? 67.193 -13.085 0.392   1.00 58.07  ?  61  ASP B CB    1 
ATOM   2500 C CG    . ASP B 1 61  ? 68.518 -13.312 -0.425  1.00 62.36  ?  61  ASP B CG    1 
ATOM   2501 O OD1   . ASP B 1 61  ? 68.950 -12.424 -1.204  1.00 62.32  ?  61  ASP B OD1   1 
ATOM   2502 O OD2   . ASP B 1 61  ? 69.136 -14.391 -0.314  1.00 60.58  -1 61  ASP B OD2   1 
ATOM   2503 N N     . MET B 1 62  ? 64.919 -11.606 2.056   1.00 63.91  ?  62  MET B N     1 
ATOM   2504 C CA    . MET B 1 62  ? 63.510 -11.379 2.355   1.00 62.55  ?  62  MET B CA    1 
ATOM   2505 C C     . MET B 1 62  ? 63.118 -9.916  2.211   1.00 61.71  ?  62  MET B C     1 
ATOM   2506 O O     . MET B 1 62  ? 61.935 -9.621  2.010   1.00 63.43  ?  62  MET B O     1 
ATOM   2507 C CB    . MET B 1 62  ? 63.139 -11.890 3.741   1.00 60.68  ?  62  MET B CB    1 
ATOM   2508 C CG    . MET B 1 62  ? 64.116 -11.607 4.846   1.00 65.33  ?  62  MET B CG    1 
ATOM   2509 S SD    . MET B 1 62  ? 63.468 -12.353 6.382   1.00 68.78  ?  62  MET B SD    1 
ATOM   2510 C CE    . MET B 1 62  ? 62.054 -11.290 6.749   1.00 61.66  ?  62  MET B CE    1 
ATOM   2511 N N     . MET B 1 63  ? 64.066 -8.988  2.285   1.00 58.53  ?  63  MET B N     1 
ATOM   2512 C CA    . MET B 1 63  ? 63.673 -7.620  1.986   1.00 60.27  ?  63  MET B CA    1 
ATOM   2513 C C     . MET B 1 63  ? 63.619 -7.399  0.487   1.00 57.73  ?  63  MET B C     1 
ATOM   2514 O O     . MET B 1 63  ? 62.688 -6.760  -0.014  1.00 56.44  ?  63  MET B O     1 
ATOM   2515 C CB    . MET B 1 63  ? 64.615 -6.636  2.669   1.00 60.92  ?  63  MET B CB    1 
ATOM   2516 C CG    . MET B 1 63  ? 64.636 -6.784  4.180   1.00 60.06  ?  63  MET B CG    1 
ATOM   2517 S SD    . MET B 1 63  ? 65.615 -5.488  4.907   1.00 62.28  ?  63  MET B SD    1 
ATOM   2518 C CE    . MET B 1 63  ? 64.767 -4.016  4.343   1.00 58.01  ?  63  MET B CE    1 
ATOM   2519 N N     . ALA B 1 64  ? 64.570 -7.982  -0.244  1.00 56.10  ?  64  ALA B N     1 
ATOM   2520 C CA    . ALA B 1 64  ? 64.536 -7.921  -1.705  1.00 61.65  ?  64  ALA B CA    1 
ATOM   2521 C C     . ALA B 1 64  ? 63.212 -8.463  -2.259  1.00 59.26  ?  64  ALA B C     1 
ATOM   2522 O O     . ALA B 1 64  ? 62.570 -7.843  -3.119  1.00 55.19  ?  64  ALA B O     1 
ATOM   2523 C CB    . ALA B 1 64  ? 65.729 -8.702  -2.274  1.00 51.58  ?  64  ALA B CB    1 
ATOM   2524 N N     . GLU B 1 65  ? 62.774 -9.605  -1.740  1.00 56.77  ?  65  GLU B N     1 
ATOM   2525 C CA    . GLU B 1 65  ? 61.584 -10.249 -2.261  1.00 53.13  ?  65  GLU B CA    1 
ATOM   2526 C C     . GLU B 1 65  ? 60.356 -9.358  -2.136  1.00 54.89  ?  65  GLU B C     1 
ATOM   2527 O O     . GLU B 1 65  ? 59.538 -9.302  -3.063  1.00 57.59  ?  65  GLU B O     1 
ATOM   2528 C CB    . GLU B 1 65  ? 61.422 -11.578 -1.532  1.00 58.75  ?  65  GLU B CB    1 
ATOM   2529 C CG    . GLU B 1 65  ? 60.018 -12.042 -1.188  1.00 68.11  ?  65  GLU B CG    1 
ATOM   2530 C CD    . GLU B 1 65  ? 60.015 -13.399 -0.433  1.00 86.83  ?  65  GLU B CD    1 
ATOM   2531 O OE1   . GLU B 1 65  ? 60.948 -14.221 -0.658  1.00 94.63  ?  65  GLU B OE1   1 
ATOM   2532 O OE2   . GLU B 1 65  ? 59.091 -13.647 0.391   1.00 93.75  -1 65  GLU B OE2   1 
ATOM   2533 N N     . ARG B 1 66  ? 60.237 -8.610  -1.037  1.00 57.11  ?  66  ARG B N     1 
ATOM   2534 C CA    . ARG B 1 66  ? 59.098 -7.729  -0.874  1.00 53.24  ?  66  ARG B CA    1 
ATOM   2535 C C     . ARG B 1 66  ? 59.161 -6.511  -1.781  1.00 56.53  ?  66  ARG B C     1 
ATOM   2536 O O     . ARG B 1 66  ? 58.139 -5.847  -1.951  1.00 61.64  ?  66  ARG B O     1 
ATOM   2537 C CB    . ARG B 1 66  ? 58.995 -7.323  0.572   1.00 57.39  ?  66  ARG B CB    1 
ATOM   2538 C CG    . ARG B 1 66  ? 58.746 -8.513  1.460   1.00 57.39  ?  66  ARG B CG    1 
ATOM   2539 C CD    . ARG B 1 66  ? 59.090 -8.238  2.914   1.00 57.94  ?  66  ARG B CD    1 
ATOM   2540 N NE    . ARG B 1 66  ? 58.244 -8.985  3.837   1.00 54.54  ?  66  ARG B NE    1 
ATOM   2541 C CZ    . ARG B 1 66  ? 58.587 -10.140 4.378   1.00 57.58  ?  66  ARG B CZ    1 
ATOM   2542 N NH1   . ARG B 1 66  ? 59.734 -10.725 4.083   1.00 55.93  ?  66  ARG B NH1   1 
ATOM   2543 N NH2   . ARG B 1 66  ? 57.770 -10.715 5.258   1.00 63.00  ?  66  ARG B NH2   1 
ATOM   2544 N N     . LEU B 1 67  ? 60.320 -6.207  -2.373  1.00 55.26  ?  67  LEU B N     1 
ATOM   2545 C CA    . LEU B 1 67  ? 60.377 -5.160  -3.393  1.00 54.30  ?  67  LEU B CA    1 
ATOM   2546 C C     . LEU B 1 67  ? 59.569 -5.524  -4.630  1.00 51.90  ?  67  LEU B C     1 
ATOM   2547 O O     . LEU B 1 67  ? 59.062 -4.632  -5.326  1.00 50.01  ?  67  LEU B O     1 
ATOM   2548 C CB    . LEU B 1 67  ? 61.817 -4.894  -3.812  1.00 51.25  ?  67  LEU B CB    1 
ATOM   2549 C CG    . LEU B 1 67  ? 62.784 -4.432  -2.733  1.00 54.49  ?  67  LEU B CG    1 
ATOM   2550 C CD1   . LEU B 1 67  ? 64.178 -4.355  -3.308  1.00 48.64  ?  67  LEU B CD1   1 
ATOM   2551 C CD2   . LEU B 1 67  ? 62.354 -3.080  -2.221  1.00 55.00  ?  67  LEU B CD2   1 
ATOM   2552 N N     . ARG B 1 68  ? 59.470 -6.820  -4.938  1.00 55.68  ?  68  ARG B N     1 
ATOM   2553 C CA    . ARG B 1 68  ? 58.730 -7.317  -6.095  1.00 49.77  ?  68  ARG B CA    1 
ATOM   2554 C C     . ARG B 1 68  ? 59.270 -6.726  -7.398  1.00 49.73  ?  68  ARG B C     1 
ATOM   2555 O O     . ARG B 1 68  ? 58.633 -5.925  -8.066  1.00 52.54  ?  68  ARG B O     1 
ATOM   2556 C CB    . ARG B 1 68  ? 57.243 -7.024  -5.949  1.00 53.50  ?  68  ARG B CB    1 
ATOM   2557 C CG    . ARG B 1 68  ? 56.602 -7.817  -4.855  1.00 65.63  ?  68  ARG B CG    1 
ATOM   2558 C CD    . ARG B 1 68  ? 55.113 -7.515  -4.791  1.00 76.86  ?  68  ARG B CD    1 
ATOM   2559 N NE    . ARG B 1 68  ? 54.564 -7.839  -3.475  1.00 85.02  ?  68  ARG B NE    1 
ATOM   2560 C CZ    . ARG B 1 68  ? 53.580 -8.704  -3.262  1.00 91.08  ?  68  ARG B CZ    1 
ATOM   2561 N NH1   . ARG B 1 68  ? 53.003 -9.360  -4.268  1.00 91.70  ?  68  ARG B NH1   1 
ATOM   2562 N NH2   . ARG B 1 68  ? 53.154 -8.905  -2.013  1.00 91.12  ?  68  ARG B NH2   1 
ATOM   2563 N N     . ILE B 1 69  ? 60.480 -7.134  -7.736  1.00 50.53  ?  69  ILE B N     1 
ATOM   2564 C CA    . ILE B 1 69  ? 61.143 -6.614  -8.925  1.00 49.49  ?  69  ILE B CA    1 
ATOM   2565 C C     . ILE B 1 69  ? 61.525 -7.767  -9.852  1.00 56.89  ?  69  ILE B C     1 
ATOM   2566 O O     . ILE B 1 69  ? 61.313 -8.937  -9.512  1.00 54.07  ?  69  ILE B O     1 
ATOM   2567 C CB    . ILE B 1 69  ? 62.368 -5.787  -8.514  1.00 55.97  ?  69  ILE B CB    1 
ATOM   2568 C CG1   . ILE B 1 69  ? 63.279 -6.621  -7.623  1.00 52.46  ?  69  ILE B CG1   1 
ATOM   2569 C CG2   . ILE B 1 69  ? 61.920 -4.588  -7.724  1.00 49.95  ?  69  ILE B CG2   1 
ATOM   2570 C CD1   . ILE B 1 69  ? 64.665 -6.108  -7.554  1.00 53.53  ?  69  ILE B CD1   1 
ATOM   2571 N N     . GLY B 1 70  ? 62.071 -7.458  -11.031 1.00 56.07  ?  70  GLY B N     1 
ATOM   2572 C CA    . GLY B 1 70  ? 62.515 -8.496  -11.944 1.00 50.35  ?  70  GLY B CA    1 
ATOM   2573 C C     . GLY B 1 70  ? 63.703 -7.987  -12.721 1.00 56.55  ?  70  GLY B C     1 
ATOM   2574 O O     . GLY B 1 70  ? 64.236 -6.938  -12.354 1.00 55.09  ?  70  GLY B O     1 
ATOM   2575 N N     . ALA B 1 71  ? 64.144 -8.674  -13.777 1.00 56.38  ?  71  ALA B N     1 
ATOM   2576 C CA    . ALA B 1 71  ? 65.152 -8.058  -14.627 1.00 56.15  ?  71  ALA B CA    1 
ATOM   2577 C C     . ALA B 1 71  ? 64.587 -6.761  -15.196 1.00 58.11  ?  71  ALA B C     1 
ATOM   2578 O O     . ALA B 1 71  ? 63.379 -6.652  -15.446 1.00 58.25  ?  71  ALA B O     1 
ATOM   2579 C CB    . ALA B 1 71  ? 65.579 -9.000  -15.750 1.00 55.32  ?  71  ALA B CB    1 
ATOM   2580 N N     . GLY B 1 72  ? 65.453 -5.756  -15.333 1.00 64.85  ?  72  GLY B N     1 
ATOM   2581 C CA    . GLY B 1 72  ? 65.023 -4.449  -15.829 1.00 66.05  ?  72  GLY B CA    1 
ATOM   2582 C C     . GLY B 1 72  ? 64.019 -3.738  -14.948 1.00 65.64  ?  72  GLY B C     1 
ATOM   2583 O O     . GLY B 1 72  ? 63.043 -3.163  -15.456 1.00 68.82  ?  72  GLY B O     1 
ATOM   2584 N N     . SER B 1 73  ? 64.194 -3.831  -13.630 1.00 61.36  ?  73  SER B N     1 
ATOM   2585 C CA    . SER B 1 73  ? 63.526 -2.973  -12.664 1.00 57.76  ?  73  SER B CA    1 
ATOM   2586 C C     . SER B 1 73  ? 64.542 -1.979  -12.162 1.00 56.43  ?  73  SER B C     1 
ATOM   2587 O O     . SER B 1 73  ? 65.636 -2.370  -11.766 1.00 55.15  ?  73  SER B O     1 
ATOM   2588 C CB    . SER B 1 73  ? 62.992 -3.738  -11.453 1.00 53.17  ?  73  SER B CB    1 
ATOM   2589 O OG    . SER B 1 73  ? 61.860 -4.535  -11.728 1.00 57.20  ?  73  SER B OG    1 
ATOM   2590 N N     . ARG B 1 74  ? 64.179 -0.705  -12.147 1.00 55.41  ?  74  ARG B N     1 
ATOM   2591 C CA    . ARG B 1 74  ? 65.008 0.284   -11.469 1.00 54.34  ?  74  ARG B CA    1 
ATOM   2592 C C     . ARG B 1 74  ? 64.740 0.180   -9.966  1.00 53.68  ?  74  ARG B C     1 
ATOM   2593 O O     . ARG B 1 74  ? 63.587 0.269   -9.543  1.00 57.16  ?  74  ARG B O     1 
ATOM   2594 C CB    . ARG B 1 74  ? 64.700 1.694   -11.983 1.00 58.04  ?  74  ARG B CB    1 
ATOM   2595 C CG    . ARG B 1 74  ? 64.666 1.924   -13.523 1.00 56.58  ?  74  ARG B CG    1 
ATOM   2596 C CD    . ARG B 1 74  ? 65.981 1.646   -14.246 1.00 55.81  ?  74  ARG B CD    1 
ATOM   2597 N NE    . ARG B 1 74  ? 67.027 2.604   -13.936 1.00 54.69  ?  74  ARG B NE    1 
ATOM   2598 C CZ    . ARG B 1 74  ? 68.220 2.606   -14.510 1.00 60.01  ?  74  ARG B CZ    1 
ATOM   2599 N NH1   . ARG B 1 74  ? 68.528 1.741   -15.466 1.00 74.96  ?  74  ARG B NH1   1 
ATOM   2600 N NH2   . ARG B 1 74  ? 69.130 3.491   -14.112 1.00 60.41  ?  74  ARG B NH2   1 
ATOM   2601 N N     . VAL B 1 75  ? 65.785 -0.033  -9.159  1.00 51.46  ?  75  VAL B N     1 
ATOM   2602 C CA    . VAL B 1 75  ? 65.657 -0.150  -7.704  1.00 52.73  ?  75  VAL B CA    1 
ATOM   2603 C C     . VAL B 1 75  ? 66.563 0.873   -7.020  1.00 53.47  ?  75  VAL B C     1 
ATOM   2604 O O     . VAL B 1 75  ? 67.702 1.089   -7.448  1.00 52.30  ?  75  VAL B O     1 
ATOM   2605 C CB    . VAL B 1 75  ? 65.974 -1.578  -7.217  1.00 48.24  ?  75  VAL B CB    1 
ATOM   2606 C CG1   . VAL B 1 75  ? 66.377 -1.578  -5.765  1.00 54.33  ?  75  VAL B CG1   1 
ATOM   2607 C CG2   . VAL B 1 75  ? 64.760 -2.452  -7.403  1.00 51.36  ?  75  VAL B CG2   1 
ATOM   2608 N N     . LEU B 1 76  ? 66.047 1.515   -5.960  1.00 56.66  ?  76  LEU B N     1 
ATOM   2609 C CA    . LEU B 1 76  ? 66.791 2.504   -5.177  1.00 54.67  ?  76  LEU B CA    1 
ATOM   2610 C C     . LEU B 1 76  ? 67.227 1.903   -3.848  1.00 52.33  ?  76  LEU B C     1 
ATOM   2611 O O     . LEU B 1 76  ? 66.392 1.445   -3.060  1.00 49.55  ?  76  LEU B O     1 
ATOM   2612 C CB    . LEU B 1 76  ? 65.965 3.761   -4.925  1.00 54.85  ?  76  LEU B CB    1 
ATOM   2613 C CG    . LEU B 1 76  ? 66.664 4.786   -4.037  1.00 56.23  ?  76  LEU B CG    1 
ATOM   2614 C CD1   . LEU B 1 76  ? 68.060 5.068   -4.555  1.00 53.31  ?  76  LEU B CD1   1 
ATOM   2615 C CD2   . LEU B 1 76  ? 65.839 6.059   -3.965  1.00 56.18  ?  76  LEU B CD2   1 
ATOM   2616 N N     . ASP B 1 77  ? 68.535 1.941   -3.602  1.00 50.06  ?  77  ASP B N     1 
ATOM   2617 C CA    . ASP B 1 77  ? 69.159 1.360   -2.418  1.00 54.26  ?  77  ASP B CA    1 
ATOM   2618 C C     . ASP B 1 77  ? 69.523 2.497   -1.467  1.00 59.49  ?  77  ASP B C     1 
ATOM   2619 O O     . ASP B 1 77  ? 70.634 3.024   -1.511  1.00 57.28  ?  77  ASP B O     1 
ATOM   2620 C CB    . ASP B 1 77  ? 70.385 0.552   -2.827  1.00 56.54  ?  77  ASP B CB    1 
ATOM   2621 C CG    . ASP B 1 77  ? 71.096 -0.090  -1.645  1.00 65.21  ?  77  ASP B CG    1 
ATOM   2622 O OD1   . ASP B 1 77  ? 70.549 -0.037  -0.510  1.00 67.19  ?  77  ASP B OD1   1 
ATOM   2623 O OD2   . ASP B 1 77  ? 72.209 -0.654  -1.851  1.00 65.87  -1 77  ASP B OD2   1 
ATOM   2624 N N     . LEU B 1 78  ? 68.578 2.887   -0.605  1.00 56.61  ?  78  LEU B N     1 
ATOM   2625 C CA    . LEU B 1 78  ? 68.889 3.844   0.452   1.00 58.49  ?  78  LEU B CA    1 
ATOM   2626 C C     . LEU B 1 78  ? 69.950 3.263   1.378   1.00 59.91  ?  78  LEU B C     1 
ATOM   2627 O O     . LEU B 1 78  ? 69.785 2.158   1.909   1.00 67.18  ?  78  LEU B O     1 
ATOM   2628 C CB    . LEU B 1 78  ? 67.629 4.198   1.256   1.00 58.54  ?  78  LEU B CB    1 
ATOM   2629 C CG    . LEU B 1 78  ? 67.156 5.648   1.161   1.00 57.59  ?  78  LEU B CG    1 
ATOM   2630 C CD1   . LEU B 1 78  ? 66.979 6.039   -0.307  1.00 60.22  ?  78  LEU B CD1   1 
ATOM   2631 C CD2   . LEU B 1 78  ? 65.881 5.838   1.928   1.00 54.03  ?  78  LEU B CD2   1 
ATOM   2632 N N     . GLY B 1 79  ? 71.043 4.002   1.568   1.00 53.92  ?  79  GLY B N     1 
ATOM   2633 C CA    . GLY B 1 79  ? 72.011 3.607   2.561   1.00 56.26  ?  79  GLY B CA    1 
ATOM   2634 C C     . GLY B 1 79  ? 72.755 2.384   2.107   1.00 66.20  ?  79  GLY B C     1 
ATOM   2635 O O     . GLY B 1 79  ? 72.511 1.283   2.601   1.00 71.83  ?  79  GLY B O     1 
ATOM   2636 N N     . CYS B 1 80  ? 73.618 2.535   1.124   1.00 62.20  ?  80  CYS B N     1 
ATOM   2637 C CA    . CYS B 1 80  ? 74.007 1.341   0.396   1.00 62.37  ?  80  CYS B CA    1 
ATOM   2638 C C     . CYS B 1 80  ? 74.973 0.446   1.146   1.00 68.42  ?  80  CYS B C     1 
ATOM   2639 O O     . CYS B 1 80  ? 75.189 -0.692  0.703   1.00 76.76  ?  80  CYS B O     1 
ATOM   2640 C CB    . CYS B 1 80  ? 74.633 1.736   -0.921  1.00 64.84  ?  80  CYS B CB    1 
ATOM   2641 S SG    . CYS B 1 80  ? 76.116 2.566   -0.570  1.00 71.40  ?  80  CYS B SG    1 
ATOM   2642 N N     . GLY B 1 81  ? 75.561 0.929   2.244   1.00 68.65  ?  81  GLY B N     1 
ATOM   2643 C CA    . GLY B 1 81  ? 76.628 0.198   2.888   1.00 68.38  ?  81  GLY B CA    1 
ATOM   2644 C C     . GLY B 1 81  ? 77.847 0.089   1.992   1.00 70.67  ?  81  GLY B C     1 
ATOM   2645 O O     . GLY B 1 81  ? 78.124 0.945   1.152   1.00 67.93  ?  81  GLY B O     1 
ATOM   2646 N N     . VAL B 1 82  ? 78.572 -1.009  2.164   1.00 75.74  ?  82  VAL B N     1 
ATOM   2647 C CA    . VAL B 1 82  ? 79.838 -1.222  1.476   1.00 71.40  ?  82  VAL B CA    1 
ATOM   2648 C C     . VAL B 1 82  ? 79.546 -1.981  0.178   1.00 69.64  ?  82  VAL B C     1 
ATOM   2649 O O     . VAL B 1 82  ? 80.446 -2.481  -0.509  1.00 69.44  ?  82  VAL B O     1 
ATOM   2650 C CB    . VAL B 1 82  ? 80.819 -1.921  2.443   1.00 70.40  ?  82  VAL B CB    1 
ATOM   2651 C CG1   . VAL B 1 82  ? 80.134 -3.077  3.132   1.00 75.94  ?  82  VAL B CG1   1 
ATOM   2652 C CG2   . VAL B 1 82  ? 82.127 -2.343  1.797   1.00 76.41  ?  82  VAL B CG2   1 
ATOM   2653 N N     . GLY B 1 83  ? 78.264 -2.037  -0.180  1.00 67.00  ?  83  GLY B N     1 
ATOM   2654 C CA    . GLY B 1 83  ? 77.815 -2.501  -1.478  1.00 66.56  ?  83  GLY B CA    1 
ATOM   2655 C C     . GLY B 1 83  ? 77.189 -3.884  -1.516  1.00 64.45  ?  83  GLY B C     1 
ATOM   2656 O O     . GLY B 1 83  ? 76.466 -4.196  -2.476  1.00 60.72  ?  83  GLY B O     1 
ATOM   2657 N N     . THR B 1 84  ? 77.427 -4.718  -0.508  1.00 69.26  ?  84  THR B N     1 
ATOM   2658 C CA    . THR B 1 84  ? 77.102 -6.132  -0.675  1.00 68.85  ?  84  THR B CA    1 
ATOM   2659 C C     . THR B 1 84  ? 75.606 -6.397  -0.846  1.00 65.96  ?  84  THR B C     1 
ATOM   2660 O O     . THR B 1 84  ? 75.247 -7.106  -1.805  1.00 64.68  ?  84  THR B O     1 
ATOM   2661 C CB    . THR B 1 84  ? 77.731 -6.929  0.463   1.00 63.07  ?  84  THR B CB    1 
ATOM   2662 O OG1   . THR B 1 84  ? 76.910 -6.808  1.616   1.00 72.69  ?  84  THR B OG1   1 
ATOM   2663 C CG2   . THR B 1 84  ? 79.097 -6.351  0.770   1.00 62.90  ?  84  THR B CG2   1 
ATOM   2664 N N     . PRO B 1 85  ? 74.686 -5.868  -0.018  1.00 64.04  ?  85  PRO B N     1 
ATOM   2665 C CA    . PRO B 1 85  ? 73.276 -6.209  -0.255  1.00 61.01  ?  85  PRO B CA    1 
ATOM   2666 C C     . PRO B 1 85  ? 72.769 -5.717  -1.607  1.00 59.76  ?  85  PRO B C     1 
ATOM   2667 O O     . PRO B 1 85  ? 71.917 -6.367  -2.231  1.00 59.27  ?  85  PRO B O     1 
ATOM   2668 C CB    . PRO B 1 85  ? 72.562 -5.531  0.913   1.00 62.04  ?  85  PRO B CB    1 
ATOM   2669 C CG    . PRO B 1 85  ? 73.375 -4.325  1.169   1.00 64.66  ?  85  PRO B CG    1 
ATOM   2670 C CD    . PRO B 1 85  ? 74.795 -4.777  0.969   1.00 62.77  ?  85  PRO B CD    1 
ATOM   2671 N N     . GLY B 1 86  ? 73.290 -4.584  -2.083  1.00 62.32  ?  86  GLY B N     1 
ATOM   2672 C CA    . GLY B 1 86  ? 72.838 -3.999  -3.328  1.00 56.59  ?  86  GLY B CA    1 
ATOM   2673 C C     . GLY B 1 86  ? 73.381 -4.731  -4.523  1.00 57.73  ?  86  GLY B C     1 
ATOM   2674 O O     . GLY B 1 86  ? 72.632 -5.033  -5.449  1.00 57.91  ?  86  GLY B O     1 
ATOM   2675 N N     . VAL B 1 87  ? 74.684 -5.032  -4.518  1.00 60.94  ?  87  VAL B N     1 
ATOM   2676 C CA    . VAL B 1 87  ? 75.258 -5.795  -5.625  1.00 57.54  ?  87  VAL B CA    1 
ATOM   2677 C C     . VAL B 1 87  ? 74.560 -7.133  -5.707  1.00 57.54  ?  87  VAL B C     1 
ATOM   2678 O O     . VAL B 1 87  ? 74.275 -7.632  -6.803  1.00 62.12  ?  87  VAL B O     1 
ATOM   2679 C CB    . VAL B 1 87  ? 76.792 -5.954  -5.490  1.00 53.93  ?  87  VAL B CB    1 
ATOM   2680 C CG1   . VAL B 1 87  ? 77.311 -7.000  -6.448  1.00 56.25  ?  87  VAL B CG1   1 
ATOM   2681 C CG2   . VAL B 1 87  ? 77.505 -4.658  -5.793  1.00 55.18  ?  87  VAL B CG2   1 
ATOM   2682 N N     . ARG B 1 88  ? 74.197 -7.689  -4.547  1.00 56.21  ?  88  ARG B N     1 
ATOM   2683 C CA    . ARG B 1 88  ? 73.480 -8.964  -4.482  1.00 60.99  ?  88  ARG B CA    1 
ATOM   2684 C C     . ARG B 1 88  ? 72.154 -8.911  -5.241  1.00 57.91  ?  88  ARG B C     1 
ATOM   2685 O O     . ARG B 1 88  ? 71.890 -9.742  -6.120  1.00 58.58  ?  88  ARG B O     1 
ATOM   2686 C CB    . ARG B 1 88  ? 73.233 -9.334  -3.023  1.00 55.58  ?  88  ARG B CB    1 
ATOM   2687 C CG    . ARG B 1 88  ? 72.571 -10.643 -2.853  1.00 55.14  ?  88  ARG B CG    1 
ATOM   2688 C CD    . ARG B 1 88  ? 72.402 -10.906 -1.396  1.00 57.85  ?  88  ARG B CD    1 
ATOM   2689 N NE    . ARG B 1 88  ? 71.851 -12.229 -1.138  1.00 60.45  ?  88  ARG B NE    1 
ATOM   2690 C CZ    . ARG B 1 88  ? 72.515 -13.365 -1.318  1.00 57.53  ?  88  ARG B CZ    1 
ATOM   2691 N NH1   . ARG B 1 88  ? 73.760 -13.377 -1.784  1.00 56.66  ?  88  ARG B NH1   1 
ATOM   2692 N NH2   . ARG B 1 88  ? 71.912 -14.515 -1.039  1.00 49.98  ?  88  ARG B NH2   1 
ATOM   2693 N N     . ILE B 1 89  ? 71.322 -7.920  -4.932  1.00 54.72  ?  89  ILE B N     1 
ATOM   2694 C CA    . ILE B 1 89  ? 70.039 -7.766  -5.603  1.00 53.49  ?  89  ILE B CA    1 
ATOM   2695 C C     . ILE B 1 89  ? 70.221 -7.588  -7.102  1.00 55.49  ?  89  ILE B C     1 
ATOM   2696 O O     . ILE B 1 89  ? 69.406 -8.060  -7.897  1.00 51.89  ?  89  ILE B O     1 
ATOM   2697 C CB    . ILE B 1 89  ? 69.275 -6.599  -4.971  1.00 51.95  ?  89  ILE B CB    1 
ATOM   2698 C CG1   . ILE B 1 89  ? 69.028 -6.951  -3.517  1.00 47.76  ?  89  ILE B CG1   1 
ATOM   2699 C CG2   . ILE B 1 89  ? 68.016 -6.293  -5.750  1.00 47.21  ?  89  ILE B CG2   1 
ATOM   2700 C CD1   . ILE B 1 89  ? 68.387 -5.902  -2.779  1.00 47.82  ?  89  ILE B CD1   1 
ATOM   2701 N N     . ALA B 1 90  ? 71.282 -6.906  -7.524  1.00 55.44  ?  90  ALA B N     1 
ATOM   2702 C CA    . ALA B 1 90  ? 71.512 -6.752  -8.958  1.00 55.58  ?  90  ALA B CA    1 
ATOM   2703 C C     . ALA B 1 90  ? 71.926 -8.077  -9.612  1.00 57.87  ?  90  ALA B C     1 
ATOM   2704 O O     . ALA B 1 90  ? 71.402 -8.451  -10.673 1.00 58.01  ?  90  ALA B O     1 
ATOM   2705 C CB    . ALA B 1 90  ? 72.562 -5.671  -9.199  1.00 56.81  ?  90  ALA B CB    1 
ATOM   2706 N N     . ARG B 1 91  ? 72.874 -8.796  -8.993  1.00 57.16  ?  91  ARG B N     1 
ATOM   2707 C CA    . ARG B 1 91  ? 73.355 -10.066 -9.543  1.00 56.34  ?  91  ARG B CA    1 
ATOM   2708 C C     . ARG B 1 91  ? 72.261 -11.119 -9.568  1.00 58.46  ?  91  ARG B C     1 
ATOM   2709 O O     . ARG B 1 91  ? 72.136 -11.883 -10.540 1.00 63.07  ?  91  ARG B O     1 
ATOM   2710 C CB    . ARG B 1 91  ? 74.536 -10.593 -8.722  1.00 59.70  ?  91  ARG B CB    1 
ATOM   2711 C CG    . ARG B 1 91  ? 74.866 -12.045 -9.017  1.00 57.79  ?  91  ARG B CG    1 
ATOM   2712 C CD    . ARG B 1 91  ? 76.038 -12.480 -8.203  1.00 59.58  ?  91  ARG B CD    1 
ATOM   2713 N NE    . ARG B 1 91  ? 75.869 -12.118 -6.803  1.00 55.94  ?  91  ARG B NE    1 
ATOM   2714 C CZ    . ARG B 1 91  ? 75.220 -12.865 -5.925  1.00 55.65  ?  91  ARG B CZ    1 
ATOM   2715 N NH1   . ARG B 1 91  ? 74.575 -13.956 -6.297  1.00 56.10  ?  91  ARG B NH1   1 
ATOM   2716 N NH2   . ARG B 1 91  ? 75.243 -12.528 -4.636  1.00 67.20  ?  91  ARG B NH2   1 
ATOM   2717 N N     . LEU B 1 92  ? 71.483 -11.196 -8.499  1.00 54.67  ?  92  LEU B N     1 
ATOM   2718 C CA    . LEU B 1 92  ? 70.495 -12.252 -8.422  1.00 55.50  ?  92  LEU B CA    1 
ATOM   2719 C C     . LEU B 1 92  ? 69.242 -11.902 -9.199  1.00 58.08  ?  92  LEU B C     1 
ATOM   2720 O O     . LEU B 1 92  ? 68.738 -12.742 -9.949  1.00 71.31  ?  92  LEU B O     1 
ATOM   2721 C CB    . LEU B 1 92  ? 70.170 -12.568 -6.969  1.00 48.16  ?  92  LEU B CB    1 
ATOM   2722 C CG    . LEU B 1 92  ? 71.303 -13.354 -6.333  1.00 55.74  ?  92  LEU B CG    1 
ATOM   2723 C CD1   . LEU B 1 92  ? 71.066 -13.467 -4.858  1.00 54.21  ?  92  LEU B CD1   1 
ATOM   2724 C CD2   . LEU B 1 92  ? 71.416 -14.718 -6.973  1.00 52.29  ?  92  LEU B CD2   1 
ATOM   2725 N N     . SER B 1 93  ? 68.729 -10.678 -9.064  1.00 55.26  ?  93  SER B N     1 
ATOM   2726 C CA    . SER B 1 93  ? 67.452 -10.343 -9.694  1.00 52.19  ?  93  SER B CA    1 
ATOM   2727 C C     . SER B 1 93  ? 67.585 -9.748  -11.087 1.00 54.44  ?  93  SER B C     1 
ATOM   2728 O O     . SER B 1 93  ? 66.571 -9.628  -11.791 1.00 55.34  ?  93  SER B O     1 
ATOM   2729 C CB    . SER B 1 93  ? 66.661 -9.357  -8.836  1.00 53.81  ?  93  SER B CB    1 
ATOM   2730 O OG    . SER B 1 93  ? 67.055 -8.019  -9.089  1.00 51.31  ?  93  SER B OG    1 
ATOM   2731 N N     . GLY B 1 94  ? 68.790 -9.350  -11.498 1.00 54.16  ?  94  GLY B N     1 
ATOM   2732 C CA    . GLY B 1 94  ? 68.943 -8.651  -12.754 1.00 55.63  ?  94  GLY B CA    1 
ATOM   2733 C C     . GLY B 1 94  ? 68.290 -7.296  -12.787 1.00 54.95  ?  94  GLY B C     1 
ATOM   2734 O O     . GLY B 1 94  ? 68.328 -6.633  -13.824 1.00 61.02  ?  94  GLY B O     1 
ATOM   2735 N N     . ALA B 1 95  ? 67.682 -6.868  -11.697 1.00 50.26  ?  95  ALA B N     1 
ATOM   2736 C CA    . ALA B 1 95  ? 67.278 -5.490  -11.590 1.00 49.81  ?  95  ALA B CA    1 
ATOM   2737 C C     . ALA B 1 95  ? 68.502 -4.592  -11.595 1.00 51.23  ?  95  ALA B C     1 
ATOM   2738 O O     . ALA B 1 95  ? 69.623 -5.027  -11.299 1.00 57.92  ?  95  ALA B O     1 
ATOM   2739 C CB    . ALA B 1 95  ? 66.504 -5.245  -10.306 1.00 53.91  ?  95  ALA B CB    1 
ATOM   2740 N N     . HIS B 1 96  ? 68.266 -3.324  -11.961 1.00 53.26  ?  96  HIS B N     1 
ATOM   2741 C CA    . HIS B 1 96  ? 69.254 -2.253  -11.882 1.00 49.43  ?  96  HIS B CA    1 
ATOM   2742 C C     . HIS B 1 96  ? 69.132 -1.549  -10.542 1.00 50.96  ?  96  HIS B C     1 
ATOM   2743 O O     . HIS B 1 96  ? 68.030 -1.171  -10.127 1.00 48.17  ?  96  HIS B O     1 
ATOM   2744 C CB    . HIS B 1 96  ? 69.068 -1.223  -12.991 1.00 49.78  ?  96  HIS B CB    1 
ATOM   2745 C CG    . HIS B 1 96  ? 70.037 -0.086  -12.909 1.00 56.14  ?  96  HIS B CG    1 
ATOM   2746 N ND1   . HIS B 1 96  ? 71.069 0.081   -13.808 1.00 62.74  ?  96  HIS B ND1   1 
ATOM   2747 C CD2   . HIS B 1 96  ? 70.141 0.936   -12.028 1.00 55.01  ?  96  HIS B CD2   1 
ATOM   2748 C CE1   . HIS B 1 96  ? 71.764 1.159   -13.488 1.00 64.86  ?  96  HIS B CE1   1 
ATOM   2749 N NE2   . HIS B 1 96  ? 71.224 1.693   -12.406 1.00 56.64  ?  96  HIS B NE2   1 
ATOM   2750 N N     . VAL B 1 97  ? 70.270 -1.337  -9.895  1.00 56.84  ?  97  VAL B N     1 
ATOM   2751 C CA    . VAL B 1 97  ? 70.342 -0.809  -8.537  1.00 57.52  ?  97  VAL B CA    1 
ATOM   2752 C C     . VAL B 1 97  ? 71.189 0.462   -8.591  1.00 56.27  ?  97  VAL B C     1 
ATOM   2753 O O     . VAL B 1 97  ? 72.380 0.409   -8.932  1.00 51.09  ?  97  VAL B O     1 
ATOM   2754 C CB    . VAL B 1 97  ? 70.925 -1.849  -7.567  1.00 52.73  ?  97  VAL B CB    1 
ATOM   2755 C CG1   . VAL B 1 97  ? 71.307 -1.221  -6.237  1.00 55.43  ?  97  VAL B CG1   1 
ATOM   2756 C CG2   . VAL B 1 97  ? 69.934 -2.978  -7.354  1.00 55.00  ?  97  VAL B CG2   1 
ATOM   2757 N N     . THR B 1 98  ? 70.555 1.612   -8.312  1.00 55.33  ?  98  THR B N     1 
ATOM   2758 C CA    . THR B 1 98  ? 71.241 2.864   -7.995  1.00 56.75  ?  98  THR B CA    1 
ATOM   2759 C C     . THR B 1 98  ? 71.214 2.992   -6.468  1.00 58.62  ?  98  THR B C     1 
ATOM   2760 O O     . THR B 1 98  ? 70.139 2.987   -5.851  1.00 56.75  ?  98  THR B O     1 
ATOM   2761 C CB    . THR B 1 98  ? 70.585 4.088   -8.667  1.00 56.74  ?  98  THR B CB    1 
ATOM   2762 O OG1   . THR B 1 98  ? 69.324 4.337   -8.066  1.00 66.29  ?  98  THR B OG1   1 
ATOM   2763 C CG2   . THR B 1 98  ? 70.286 3.898   -10.157 1.00 61.15  ?  98  THR B CG2   1 
ATOM   2764 N N     . GLY B 1 99  ? 72.390 3.054   -5.853  1.00 58.14  ?  99  GLY B N     1 
ATOM   2765 C CA    . GLY B 1 99  ? 72.498 3.101   -4.404  1.00 60.53  ?  99  GLY B CA    1 
ATOM   2766 C C     . GLY B 1 99  ? 73.168 4.383   -3.944  1.00 62.75  ?  99  GLY B C     1 
ATOM   2767 O O     . GLY B 1 99  ? 73.998 4.950   -4.659  1.00 64.21  ?  99  GLY B O     1 
ATOM   2768 N N     . ILE B 1 100 ? 72.798 4.842   -2.733  1.00 61.84  ?  100 ILE B N     1 
ATOM   2769 C CA    . ILE B 1 100 ? 73.277 6.106   -2.168  1.00 67.13  ?  100 ILE B CA    1 
ATOM   2770 C C     . ILE B 1 100 ? 73.798 5.881   -0.747  1.00 66.21  ?  100 ILE B C     1 
ATOM   2771 O O     . ILE B 1 100 ? 73.260 5.060   0.011   1.00 63.03  ?  100 ILE B O     1 
ATOM   2772 C CB    . ILE B 1 100 ? 72.184 7.205   -2.182  1.00 64.36  ?  100 ILE B CB    1 
ATOM   2773 C CG1   . ILE B 1 100 ? 71.116 6.946   -1.118  1.00 60.84  ?  100 ILE B CG1   1 
ATOM   2774 C CG2   . ILE B 1 100 ? 71.545 7.319   -3.562  1.00 53.76  ?  100 ILE B CG2   1 
ATOM   2775 C CD1   . ILE B 1 100 ? 69.972 7.911   -1.199  1.00 59.26  ?  100 ILE B CD1   1 
ATOM   2776 N N     . SER B 1 101 ? 74.883 6.584   -0.410  1.00 61.09  ?  101 SER B N     1 
ATOM   2777 C CA    . SER B 1 101 ? 75.434 6.635   0.939   1.00 63.88  ?  101 SER B CA    1 
ATOM   2778 C C     . SER B 1 101 ? 76.010 8.022   1.151   1.00 66.23  ?  101 SER B C     1 
ATOM   2779 O O     . SER B 1 101 ? 76.325 8.720   0.184   1.00 71.67  ?  101 SER B O     1 
ATOM   2780 C CB    . SER B 1 101 ? 76.521 5.581   1.155   1.00 67.34  ?  101 SER B CB    1 
ATOM   2781 O OG    . SER B 1 101 ? 77.026 5.628   2.475   1.00 70.97  ?  101 SER B OG    1 
ATOM   2782 N N     . VAL B 1 102 ? 76.222 8.398   2.412   1.00 66.67  ?  102 VAL B N     1 
ATOM   2783 C CA    . VAL B 1 102 ? 76.768 9.749   2.737   1.00 69.60  ?  102 VAL B CA    1 
ATOM   2784 C C     . VAL B 1 102 ? 78.258 9.628   3.076   1.00 72.14  ?  102 VAL B C     1 
ATOM   2785 O O     . VAL B 1 102 ? 78.899 10.674  3.243   1.00 75.77  ?  102 VAL B O     1 
ATOM   2786 C CB    . VAL B 1 102 ? 75.971 10.419  3.874   1.00 68.88  ?  102 VAL B CB    1 
ATOM   2787 C CG1   . VAL B 1 102 ? 74.531 10.689  3.470   1.00 72.40  ?  102 VAL B CG1   1 
ATOM   2788 C CG2   . VAL B 1 102 ? 76.022 9.605   5.156   1.00 75.07  ?  102 VAL B CG2   1 
ATOM   2789 N N     . SER B 1 103 ? 78.785 8.407   3.160   1.00 68.33  ?  103 SER B N     1 
ATOM   2790 C CA    . SER B 1 103 ? 80.204 8.202   3.422   1.00 74.37  ?  103 SER B CA    1 
ATOM   2791 C C     . SER B 1 103 ? 80.967 7.928   2.129   1.00 74.66  ?  103 SER B C     1 
ATOM   2792 O O     . SER B 1 103 ? 80.625 7.005   1.380   1.00 69.84  ?  103 SER B O     1 
ATOM   2793 C CB    . SER B 1 103 ? 80.420 7.039   4.381   1.00 72.59  ?  103 SER B CB    1 
ATOM   2794 O OG    . SER B 1 103 ? 81.701 6.464   4.181   1.00 74.52  ?  103 SER B OG    1 
ATOM   2795 N N     . HIS B 1 104 ? 82.029 8.704   1.901   1.00 79.84  ?  104 HIS B N     1 
ATOM   2796 C CA    . HIS B 1 104 ? 82.851 8.511   0.713   1.00 72.11  ?  104 HIS B CA    1 
ATOM   2797 C C     . HIS B 1 104 ? 83.501 7.133   0.709   1.00 70.41  ?  104 HIS B C     1 
ATOM   2798 O O     . HIS B 1 104 ? 83.497 6.440   -0.309  1.00 72.22  ?  104 HIS B O     1 
ATOM   2799 C CB    . HIS B 1 104 ? 83.901 9.617   0.628   1.00 74.37  ?  104 HIS B CB    1 
ATOM   2800 C CG    . HIS B 1 104 ? 84.770 9.533   -0.588  1.00 69.23  ?  104 HIS B CG    1 
ATOM   2801 N ND1   . HIS B 1 104 ? 85.934 8.795   -0.622  1.00 71.78  ?  104 HIS B ND1   1 
ATOM   2802 C CD2   . HIS B 1 104 ? 84.648 10.095  -1.814  1.00 70.31  ?  104 HIS B CD2   1 
ATOM   2803 C CE1   . HIS B 1 104 ? 86.490 8.904   -1.816  1.00 75.88  ?  104 HIS B CE1   1 
ATOM   2804 N NE2   . HIS B 1 104 ? 85.732 9.689   -2.558  1.00 71.77  ?  104 HIS B NE2   1 
ATOM   2805 N N     . GLU B 1 105 ? 84.059 6.703   1.842   1.00 77.24  ?  105 GLU B N     1 
ATOM   2806 C CA    . GLU B 1 105 ? 84.743 5.411   1.843   1.00 77.70  ?  105 GLU B CA    1 
ATOM   2807 C C     . GLU B 1 105 ? 83.784 4.273   1.502   1.00 75.20  ?  105 GLU B C     1 
ATOM   2808 O O     . GLU B 1 105 ? 84.205 3.278   0.900   1.00 74.97  ?  105 GLU B O     1 
ATOM   2809 C CB    . GLU B 1 105 ? 85.435 5.155   3.191   1.00 79.36  ?  105 GLU B CB    1 
ATOM   2810 C CG    . GLU B 1 105 ? 86.647 6.035   3.439   1.00 81.07  ?  105 GLU B CG    1 
ATOM   2811 C CD    . GLU B 1 105 ? 87.715 5.802   2.398   1.00 87.78  ?  105 GLU B CD    1 
ATOM   2812 O OE1   . GLU B 1 105 ? 87.883 4.628   2.001   1.00 94.60  ?  105 GLU B OE1   1 
ATOM   2813 O OE2   . GLU B 1 105 ? 88.358 6.784   1.960   1.00 82.42  -1 105 GLU B OE2   1 
ATOM   2814 N N     . GLN B 1 106 ? 82.497 4.410   1.844   1.00 72.50  ?  106 GLN B N     1 
ATOM   2815 C CA    . GLN B 1 106 ? 81.521 3.402   1.444   1.00 69.93  ?  106 GLN B CA    1 
ATOM   2816 C C     . GLN B 1 106 ? 81.297 3.430   -0.070  1.00 70.72  ?  106 GLN B C     1 
ATOM   2817 O O     . GLN B 1 106 ? 81.643 2.467   -0.771  1.00 71.44  ?  106 GLN B O     1 
ATOM   2818 C CB    . GLN B 1 106 ? 80.212 3.594   2.214   1.00 71.10  ?  106 GLN B CB    1 
ATOM   2819 C CG    . GLN B 1 106 ? 80.247 2.928   3.595   1.00 72.48  ?  106 GLN B CG    1 
ATOM   2820 C CD    . GLN B 1 106 ? 78.927 2.980   4.344   1.00 68.24  ?  106 GLN B CD    1 
ATOM   2821 O OE1   . GLN B 1 106 ? 78.005 3.688   3.958   1.00 72.48  ?  106 GLN B OE1   1 
ATOM   2822 N NE2   . GLN B 1 106 ? 78.840 2.223   5.425   1.00 64.06  ?  106 GLN B NE2   1 
ATOM   2823 N N     . VAL B 1 107 ? 80.792 4.552   -0.612  1.00 65.31  ?  107 VAL B N     1 
ATOM   2824 C CA    . VAL B 1 107 ? 80.486 4.670   -2.045  1.00 62.57  ?  107 VAL B CA    1 
ATOM   2825 C C     . VAL B 1 107 ? 81.653 4.239   -2.938  1.00 67.13  ?  107 VAL B C     1 
ATOM   2826 O O     . VAL B 1 107 ? 81.472 3.908   -4.112  1.00 68.35  ?  107 VAL B O     1 
ATOM   2827 C CB    . VAL B 1 107 ? 80.044 6.104   -2.396  1.00 63.20  ?  107 VAL B CB    1 
ATOM   2828 C CG1   . VAL B 1 107 ? 81.167 7.054   -2.205  1.00 74.14  ?  107 VAL B CG1   1 
ATOM   2829 C CG2   . VAL B 1 107 ? 79.542 6.207   -3.853  1.00 61.79  ?  107 VAL B CG2   1 
ATOM   2830 N N     . VAL B 1 108 ? 82.864 4.228   -2.409  1.00 62.75  ?  108 VAL B N     1 
ATOM   2831 C CA    . VAL B 1 108 ? 83.964 3.680   -3.185  1.00 62.49  ?  108 VAL B CA    1 
ATOM   2832 C C     . VAL B 1 108 ? 83.998 2.158   -3.071  1.00 65.74  ?  108 VAL B C     1 
ATOM   2833 O O     . VAL B 1 108 ? 84.051 1.455   -4.082  1.00 64.45  ?  108 VAL B O     1 
ATOM   2834 C CB    . VAL B 1 108 ? 85.292 4.332   -2.767  1.00 61.29  ?  108 VAL B CB    1 
ATOM   2835 C CG1   . VAL B 1 108 ? 86.428 3.761   -3.580  1.00 59.15  ?  108 VAL B CG1   1 
ATOM   2836 C CG2   . VAL B 1 108 ? 85.203 5.827   -2.977  1.00 61.64  ?  108 VAL B CG2   1 
ATOM   2837 N N     . ARG B 1 109 ? 83.938 1.612   -1.857  1.00 64.79  ?  109 ARG B N     1 
ATOM   2838 C CA    . ARG B 1 109 ? 84.033 0.162   -1.750  1.00 61.27  ?  109 ARG B CA    1 
ATOM   2839 C C     . ARG B 1 109 ? 82.927 -0.516  -2.540  1.00 66.87  ?  109 ARG B C     1 
ATOM   2840 O O     . ARG B 1 109 ? 83.131 -1.619  -3.062  1.00 69.60  ?  109 ARG B O     1 
ATOM   2841 C CB    . ARG B 1 109 ? 84.013 -0.297  -0.288  1.00 66.23  ?  109 ARG B CB    1 
ATOM   2842 C CG    . ARG B 1 109 ? 85.120 0.285   0.546   1.00 67.15  ?  109 ARG B CG    1 
ATOM   2843 C CD    . ARG B 1 109 ? 85.854 -0.698  1.461   1.00 82.20  ?  109 ARG B CD    1 
ATOM   2844 N NE    . ARG B 1 109 ? 86.381 0.042   2.615   1.00 98.48  ?  109 ARG B NE    1 
ATOM   2845 C CZ    . ARG B 1 109 ? 87.522 -0.194  3.266   1.00 101.92 ?  109 ARG B CZ    1 
ATOM   2846 N NH1   . ARG B 1 109 ? 88.347 -1.172  2.902   1.00 105.17 ?  109 ARG B NH1   1 
ATOM   2847 N NH2   . ARG B 1 109 ? 87.851 0.582   4.304   1.00 98.09  ?  109 ARG B NH2   1 
ATOM   2848 N N     . ALA B 1 110 ? 81.775 0.147   -2.693  1.00 63.14  ?  110 ALA B N     1 
ATOM   2849 C CA    . ALA B 1 110 ? 80.607 -0.486  -3.306  1.00 62.06  ?  110 ALA B CA    1 
ATOM   2850 C C     . ALA B 1 110 ? 80.650 -0.448  -4.833  1.00 64.15  ?  110 ALA B C     1 
ATOM   2851 O O     . ALA B 1 110 ? 80.304 -1.436  -5.493  1.00 64.39  ?  110 ALA B O     1 
ATOM   2852 C CB    . ALA B 1 110 ? 79.331 0.177   -2.786  1.00 63.13  ?  110 ALA B CB    1 
ATOM   2853 N N     . ASN B 1 111 ? 81.058 0.672   -5.417  1.00 63.11  ?  111 ASN B N     1 
ATOM   2854 C CA    . ASN B 1 111 ? 81.338 0.661   -6.841  1.00 58.31  ?  111 ASN B CA    1 
ATOM   2855 C C     . ASN B 1 111 ? 82.354 -0.421  -7.173  1.00 61.34  ?  111 ASN B C     1 
ATOM   2856 O O     . ASN B 1 111 ? 82.317 -1.010  -8.261  1.00 66.18  ?  111 ASN B O     1 
ATOM   2857 C CB    . ASN B 1 111 ? 81.871 2.027   -7.282  1.00 61.02  ?  111 ASN B CB    1 
ATOM   2858 C CG    . ASN B 1 111 ? 80.785 3.085   -7.444  1.00 61.30  ?  111 ASN B CG    1 
ATOM   2859 O OD1   . ASN B 1 111 ? 79.590 2.775   -7.549  1.00 54.74  ?  111 ASN B OD1   1 
ATOM   2860 N ND2   . ASN B 1 111 ? 81.212 4.353   -7.504  1.00 70.24  ?  111 ASN B ND2   1 
ATOM   2861 N N     . ALA B 1 112 ? 83.259 -0.696  -6.239  1.00 61.80  ?  112 ALA B N     1 
ATOM   2862 C CA    . ALA B 1 112 ? 84.281 -1.712  -6.429  1.00 60.08  ?  112 ALA B CA    1 
ATOM   2863 C C     . ALA B 1 112 ? 83.677 -3.099  -6.419  1.00 65.65  ?  112 ALA B C     1 
ATOM   2864 O O     . ALA B 1 112 ? 83.995 -3.937  -7.274  1.00 66.43  ?  112 ALA B O     1 
ATOM   2865 C CB    . ALA B 1 112 ? 85.327 -1.606  -5.325  1.00 56.48  ?  112 ALA B CB    1 
ATOM   2866 N N     . LEU B 1 113 ? 82.830 -3.368  -5.428  1.00 58.97  ?  113 LEU B N     1 
ATOM   2867 C CA    . LEU B 1 113 ? 82.137 -4.641  -5.401  1.00 63.05  ?  113 LEU B CA    1 
ATOM   2868 C C     . LEU B 1 113 ? 81.370 -4.857  -6.701  1.00 67.73  ?  113 LEU B C     1 
ATOM   2869 O O     . LEU B 1 113 ? 81.552 -5.878  -7.373  1.00 66.36  ?  113 LEU B O     1 
ATOM   2870 C CB    . LEU B 1 113 ? 81.215 -4.697  -4.195  1.00 57.87  ?  113 LEU B CB    1 
ATOM   2871 C CG    . LEU B 1 113 ? 80.638 -6.090  -4.024  1.00 60.02  ?  113 LEU B CG    1 
ATOM   2872 C CD1   . LEU B 1 113 ? 81.725 -7.127  -4.248  1.00 64.24  ?  113 LEU B CD1   1 
ATOM   2873 C CD2   . LEU B 1 113 ? 80.042 -6.231  -2.658  1.00 56.66  ?  113 LEU B CD2   1 
ATOM   2874 N N     . ALA B 1 114 ? 80.555 -3.869  -7.101  1.00 62.60  ?  114 ALA B N     1 
ATOM   2875 C CA    . ALA B 1 114 ? 79.895 -3.906  -8.404  1.00 56.50  ?  114 ALA B CA    1 
ATOM   2876 C C     . ALA B 1 114 ? 80.895 -4.183  -9.512  1.00 63.28  ?  114 ALA B C     1 
ATOM   2877 O O     . ALA B 1 114 ? 80.686 -5.072  -10.343 1.00 66.17  ?  114 ALA B O     1 
ATOM   2878 C CB    . ALA B 1 114 ? 79.171 -2.587  -8.666  1.00 54.51  ?  114 ALA B CB    1 
ATOM   2879 N N     . GLU B 1 115 ? 82.015 -3.453  -9.515  1.00 66.35  ?  115 GLU B N     1 
ATOM   2880 C CA    . GLU B 1 115 ? 83.001 -3.585  -10.587 1.00 64.63  ?  115 GLU B CA    1 
ATOM   2881 C C     . GLU B 1 115 ? 83.624 -4.972  -10.600 1.00 67.24  ?  115 GLU B C     1 
ATOM   2882 O O     . GLU B 1 115 ? 83.889 -5.538  -11.670 1.00 65.69  ?  115 GLU B O     1 
ATOM   2883 C CB    . GLU B 1 115 ? 84.080 -2.514  -10.447 1.00 63.36  ?  115 GLU B CB    1 
ATOM   2884 C CG    . GLU B 1 115 ? 84.515 -1.883  -11.763 1.00 67.21  ?  115 GLU B CG    1 
ATOM   2885 C CD    . GLU B 1 115 ? 85.380 -2.814  -12.580 1.00 77.27  ?  115 GLU B CD    1 
ATOM   2886 O OE1   . GLU B 1 115 ? 85.959 -3.734  -11.967 1.00 79.95  ?  115 GLU B OE1   1 
ATOM   2887 O OE2   . GLU B 1 115 ? 85.485 -2.641  -13.822 1.00 79.93  -1 115 GLU B OE2   1 
ATOM   2888 N N     . GLU B 1 116 ? 83.864 -5.543  -9.420  1.00 71.98  ?  116 GLU B N     1 
ATOM   2889 C CA    . GLU B 1 116 ? 84.465 -6.866  -9.384  1.00 74.40  ?  116 GLU B CA    1 
ATOM   2890 C C     . GLU B 1 116 ? 83.452 -7.967  -9.662  1.00 73.77  ?  116 GLU B C     1 
ATOM   2891 O O     . GLU B 1 116 ? 83.842 -9.085  -10.028 1.00 76.48  ?  116 GLU B O     1 
ATOM   2892 C CB    . GLU B 1 116 ? 85.165 -7.092  -8.044  1.00 74.12  ?  116 GLU B CB    1 
ATOM   2893 C CG    . GLU B 1 116 ? 86.429 -7.911  -8.217  1.00 81.52  ?  116 GLU B CG    1 
ATOM   2894 C CD    . GLU B 1 116 ? 86.146 -9.393  -8.128  1.00 89.59  ?  116 GLU B CD    1 
ATOM   2895 O OE1   . GLU B 1 116 ? 85.299 -9.763  -7.275  1.00 88.30  ?  116 GLU B OE1   1 
ATOM   2896 O OE2   . GLU B 1 116 ? 86.752 -10.176 -8.909  1.00 90.74  -1 116 GLU B OE2   1 
ATOM   2897 N N     . ALA B 1 117 ? 82.166 -7.670  -9.550  1.00 67.77  ?  117 ALA B N     1 
ATOM   2898 C CA    . ALA B 1 117 ? 81.153 -8.625  -9.952  1.00 65.75  ?  117 ALA B CA    1 
ATOM   2899 C C     . ALA B 1 117 ? 80.819 -8.502  -11.423 1.00 59.69  ?  117 ALA B C     1 
ATOM   2900 O O     . ALA B 1 117 ? 79.933 -9.207  -11.910 1.00 56.46  ?  117 ALA B O     1 
ATOM   2901 C CB    . ALA B 1 117 ? 79.890 -8.456  -9.102  1.00 56.62  ?  117 ALA B CB    1 
ATOM   2902 N N     . GLY B 1 118 ? 81.518 -7.635  -12.142 1.00 63.09  ?  118 GLY B N     1 
ATOM   2903 C CA    . GLY B 1 118 ? 81.200 -7.411  -13.536 1.00 62.49  ?  118 GLY B CA    1 
ATOM   2904 C C     . GLY B 1 118 ? 79.839 -6.798  -13.726 1.00 61.78  ?  118 GLY B C     1 
ATOM   2905 O O     . GLY B 1 118 ? 79.220 -6.975  -14.786 1.00 67.35  ?  118 GLY B O     1 
ATOM   2906 N N     . LEU B 1 119 ? 79.362 -6.057  -12.729 1.00 57.11  ?  119 LEU B N     1 
ATOM   2907 C CA    . LEU B 1 119 ? 78.016 -5.512  -12.754 1.00 56.62  ?  119 LEU B CA    1 
ATOM   2908 C C     . LEU B 1 119 ? 78.042 -3.995  -12.559 1.00 59.49  ?  119 LEU B C     1 
ATOM   2909 O O     . LEU B 1 119 ? 77.097 -3.412  -12.014 1.00 60.72  ?  119 LEU B O     1 
ATOM   2910 C CB    . LEU B 1 119 ? 77.147 -6.205  -11.705 1.00 50.54  ?  119 LEU B CB    1 
ATOM   2911 C CG    . LEU B 1 119 ? 76.991 -7.706  -11.899 1.00 50.62  ?  119 LEU B CG    1 
ATOM   2912 C CD1   . LEU B 1 119 ? 76.279 -8.274  -10.728 1.00 54.66  ?  119 LEU B CD1   1 
ATOM   2913 C CD2   . LEU B 1 119 ? 76.217 -8.000  -13.157 1.00 53.59  ?  119 LEU B CD2   1 
ATOM   2914 N N     . ALA B 1 120 ? 79.106 -3.331  -13.035 1.00 57.12  ?  120 ALA B N     1 
ATOM   2915 C CA    . ALA B 1 120 ? 79.205 -1.879  -12.862 1.00 56.77  ?  120 ALA B CA    1 
ATOM   2916 C C     . ALA B 1 120 ? 78.153 -1.103  -13.655 1.00 64.09  ?  120 ALA B C     1 
ATOM   2917 O O     . ALA B 1 120 ? 77.868 0.055   -13.333 1.00 63.64  ?  120 ALA B O     1 
ATOM   2918 C CB    . ALA B 1 120 ? 80.596 -1.399  -13.257 1.00 56.69  ?  120 ALA B CB    1 
ATOM   2919 N N     . ASP B 1 121 ? 77.524 -1.760  -14.636 1.00 70.73  ?  121 ASP B N     1 
ATOM   2920 C CA    . ASP B 1 121 ? 76.529 -1.044  -15.466 1.00 70.51  ?  121 ASP B CA    1 
ATOM   2921 C C     . ASP B 1 121 ? 75.155 -1.276  -14.852 1.00 66.89  ?  121 ASP B C     1 
ATOM   2922 O O     . ASP B 1 121 ? 74.263 -0.455  -15.085 1.00 67.93  ?  121 ASP B O     1 
ATOM   2923 C CB    . ASP B 1 121 ? 76.625 -1.511  -16.915 1.00 74.43  ?  121 ASP B CB    1 
ATOM   2924 C CG    . ASP B 1 121 ? 78.047 -1.861  -17.312 1.00 81.11  ?  121 ASP B CG    1 
ATOM   2925 O OD1   . ASP B 1 121 ? 78.510 -2.952  -16.923 1.00 81.29  -1 121 ASP B OD1   1 
ATOM   2926 O OD2   . ASP B 1 121 ? 78.685 -1.032  -17.990 1.00 81.40  ?  121 ASP B OD2   1 
ATOM   2927 N N     . ARG B 1 122 ? 75.018 -2.325  -14.063 1.00 63.93  ?  122 ARG B N     1 
ATOM   2928 C CA    . ARG B 1 122 ? 73.751 -2.708  -13.482 1.00 61.69  ?  122 ARG B CA    1 
ATOM   2929 C C     . ARG B 1 122 ? 73.587 -2.222  -12.054 1.00 57.04  ?  122 ARG B C     1 
ATOM   2930 O O     . ARG B 1 122 ? 72.462 -2.224  -11.547 1.00 53.52  ?  122 ARG B O     1 
ATOM   2931 C CB    . ARG B 1 122 ? 73.608 -4.239  -13.527 1.00 55.86  ?  122 ARG B CB    1 
ATOM   2932 C CG    . ARG B 1 122 ? 72.252 -4.771  -13.127 1.00 54.25  ?  122 ARG B CG    1 
ATOM   2933 C CD    . ARG B 1 122 ? 72.278 -6.260  -12.944 1.00 54.14  ?  122 ARG B CD    1 
ATOM   2934 N NE    . ARG B 1 122 ? 72.898 -6.938  -14.078 1.00 62.57  ?  122 ARG B NE    1 
ATOM   2935 C CZ    . ARG B 1 122 ? 72.921 -8.259  -14.221 1.00 63.16  ?  122 ARG B CZ    1 
ATOM   2936 N NH1   . ARG B 1 122 ? 72.358 -9.057  -13.323 1.00 59.48  ?  122 ARG B NH1   1 
ATOM   2937 N NH2   . ARG B 1 122 ? 73.518 -8.794  -15.292 1.00 57.70  ?  122 ARG B NH2   1 
ATOM   2938 N N     . ALA B 1 123 ? 74.684 -1.833  -11.391 1.00 61.21  ?  123 ALA B N     1 
ATOM   2939 C CA    . ALA B 1 123 ? 74.675 -1.433  -9.977  1.00 55.71  ?  123 ALA B CA    1 
ATOM   2940 C C     . ALA B 1 123 ? 75.675 -0.301  -9.797  1.00 58.63  ?  123 ALA B C     1 
ATOM   2941 O O     . ALA B 1 123 ? 76.876 -0.545  -9.645  1.00 59.64  ?  123 ALA B O     1 
ATOM   2942 C CB    . ALA B 1 123 ? 75.015 -2.589  -9.051  1.00 54.06  ?  123 ALA B CB    1 
ATOM   2943 N N     . ARG B 1 124 ? 75.169 0.930   -9.794  1.00 60.38  ?  124 ARG B N     1 
ATOM   2944 C CA    . ARG B 1 124 ? 75.961 2.138   -9.589  1.00 62.97  ?  124 ARG B CA    1 
ATOM   2945 C C     . ARG B 1 124 ? 75.656 2.755   -8.222  1.00 61.75  ?  124 ARG B C     1 
ATOM   2946 O O     . ARG B 1 124 ? 74.490 2.863   -7.820  1.00 60.56  ?  124 ARG B O     1 
ATOM   2947 C CB    . ARG B 1 124 ? 75.694 3.140   -10.707 1.00 56.52  ?  124 ARG B CB    1 
ATOM   2948 C CG    . ARG B 1 124 ? 76.198 2.649   -12.036 1.00 61.90  ?  124 ARG B CG    1 
ATOM   2949 C CD    . ARG B 1 124 ? 75.490 3.328   -13.168 1.00 58.90  ?  124 ARG B CD    1 
ATOM   2950 N NE    . ARG B 1 124 ? 76.116 3.034   -14.445 1.00 60.08  ?  124 ARG B NE    1 
ATOM   2951 C CZ    . ARG B 1 124 ? 75.695 3.546   -15.586 1.00 66.88  ?  124 ARG B CZ    1 
ATOM   2952 N NH1   . ARG B 1 124 ? 74.637 4.342   -15.637 1.00 58.00  ?  124 ARG B NH1   1 
ATOM   2953 N NH2   . ARG B 1 124 ? 76.356 3.267   -16.699 1.00 69.96  ?  124 ARG B NH2   1 
ATOM   2954 N N     . PHE B 1 125 ? 76.708 3.146   -7.494  1.00 63.76  ?  125 PHE B N     1 
ATOM   2955 C CA    . PHE B 1 125 ? 76.585 3.712   -6.155  1.00 57.90  ?  125 PHE B CA    1 
ATOM   2956 C C     . PHE B 1 125 ? 77.153 5.128   -6.128  1.00 59.78  ?  125 PHE B C     1 
ATOM   2957 O O     . PHE B 1 125 ? 78.252 5.370   -6.632  1.00 64.84  ?  125 PHE B O     1 
ATOM   2958 C CB    . PHE B 1 125 ? 77.284 2.806   -5.153  1.00 53.57  ?  125 PHE B CB    1 
ATOM   2959 C CG    . PHE B 1 125 ? 76.685 1.451   -5.085  1.00 59.80  ?  125 PHE B CG    1 
ATOM   2960 C CD1   . PHE B 1 125 ? 75.536 1.242   -4.345  1.00 61.54  ?  125 PHE B CD1   1 
ATOM   2961 C CD2   . PHE B 1 125 ? 77.232 0.395   -5.789  1.00 61.54  ?  125 PHE B CD2   1 
ATOM   2962 C CE1   . PHE B 1 125 ? 74.937 -0.001  -4.279  1.00 62.23  ?  125 PHE B CE1   1 
ATOM   2963 C CE2   . PHE B 1 125 ? 76.645 -0.862  -5.739  1.00 64.64  ?  125 PHE B CE2   1 
ATOM   2964 C CZ    . PHE B 1 125 ? 75.488 -1.061  -4.979  1.00 66.05  ?  125 PHE B CZ    1 
ATOM   2965 N N     . GLN B 1 126 ? 76.398 6.062   -5.547  1.00 59.55  ?  126 GLN B N     1 
ATOM   2966 C CA    . GLN B 1 126 ? 76.713 7.483   -5.621  1.00 64.80  ?  126 GLN B CA    1 
ATOM   2967 C C     . GLN B 1 126 ? 76.459 8.146   -4.274  1.00 65.22  ?  126 GLN B C     1 
ATOM   2968 O O     . GLN B 1 126 ? 75.735 7.612   -3.435  1.00 67.30  ?  126 GLN B O     1 
ATOM   2969 C CB    . GLN B 1 126 ? 75.881 8.190   -6.692  1.00 62.77  ?  126 GLN B CB    1 
ATOM   2970 C CG    . GLN B 1 126 ? 74.566 8.746   -6.203  1.00 56.07  ?  126 GLN B CG    1 
ATOM   2971 C CD    . GLN B 1 126 ? 73.795 9.453   -7.309  1.00 60.87  ?  126 GLN B CD    1 
ATOM   2972 O OE1   . GLN B 1 126 ? 73.548 8.876   -8.361  1.00 62.36  ?  126 GLN B OE1   1 
ATOM   2973 N NE2   . GLN B 1 126 ? 73.417 10.711  -7.083  1.00 67.86  ?  126 GLN B NE2   1 
ATOM   2974 N N     . ARG B 1 127 ? 77.054 9.319   -4.064  1.00 63.85  ?  127 ARG B N     1 
ATOM   2975 C CA    . ARG B 1 127 ? 76.906 10.035  -2.802  1.00 63.50  ?  127 ARG B CA    1 
ATOM   2976 C C     . ARG B 1 127 ? 75.687 10.946  -2.896  1.00 63.76  ?  127 ARG B C     1 
ATOM   2977 O O     . ARG B 1 127 ? 75.590 11.760  -3.823  1.00 66.37  ?  127 ARG B O     1 
ATOM   2978 C CB    . ARG B 1 127 ? 78.163 10.840  -2.486  1.00 62.07  ?  127 ARG B CB    1 
ATOM   2979 C CG    . ARG B 1 127 ? 78.344 11.102  -1.013  1.00 65.04  ?  127 ARG B CG    1 
ATOM   2980 C CD    . ARG B 1 127 ? 79.569 11.957  -0.760  1.00 73.51  ?  127 ARG B CD    1 
ATOM   2981 N NE    . ARG B 1 127 ? 79.978 11.905  0.642   1.00 77.85  ?  127 ARG B NE    1 
ATOM   2982 C CZ    . ARG B 1 127 ? 81.133 12.371  1.112   1.00 88.49  ?  127 ARG B CZ    1 
ATOM   2983 N NH1   . ARG B 1 127 ? 82.000 12.996  0.323   1.00 85.99  ?  127 ARG B NH1   1 
ATOM   2984 N NH2   . ARG B 1 127 ? 81.432 12.196  2.406   1.00 89.82  ?  127 ARG B NH2   1 
ATOM   2985 N N     . ALA B 1 128 ? 74.746 10.788  -1.961  1.00 59.47  ?  128 ALA B N     1 
ATOM   2986 C CA    . ALA B 1 128 ? 73.545 11.626  -1.888  1.00 64.16  ?  128 ALA B CA    1 
ATOM   2987 C C     . ALA B 1 128 ? 72.882 11.488  -0.520  1.00 70.87  ?  128 ALA B C     1 
ATOM   2988 O O     . ALA B 1 128 ? 73.121 10.520  0.219   1.00 68.67  ?  128 ALA B O     1 
ATOM   2989 C CB    . ALA B 1 128 ? 72.538 11.289  -2.986  1.00 61.42  ?  128 ALA B CB    1 
ATOM   2990 N N     . ASP B 1 129 ? 72.044 12.479  -0.183  1.00 70.20  ?  129 ASP B N     1 
ATOM   2991 C CA    . ASP B 1 129 ? 71.436 12.561  1.142   1.00 71.91  ?  129 ASP B CA    1 
ATOM   2992 C C     . ASP B 1 129 ? 69.987 12.128  1.035   1.00 75.07  ?  129 ASP B C     1 
ATOM   2993 O O     . ASP B 1 129 ? 69.213 12.750  0.305   1.00 75.46  ?  129 ASP B O     1 
ATOM   2994 C CB    . ASP B 1 129 ? 71.526 13.980  1.708   1.00 79.06  ?  129 ASP B CB    1 
ATOM   2995 C CG    . ASP B 1 129 ? 71.386 14.026  3.233   1.00 74.23  ?  129 ASP B CG    1 
ATOM   2996 O OD1   . ASP B 1 129 ? 70.506 13.327  3.780   1.00 75.24  -1 129 ASP B OD1   1 
ATOM   2997 O OD2   . ASP B 1 129 ? 72.165 14.766  3.874   1.00 80.55  ?  129 ASP B OD2   1 
ATOM   2998 N N     . ALA B 1 130 ? 69.611 11.096  1.801   1.00 74.30  ?  130 ALA B N     1 
ATOM   2999 C CA    . ALA B 1 130 ? 68.246 10.597  1.714   1.00 69.02  ?  130 ALA B CA    1 
ATOM   3000 C C     . ALA B 1 130 ? 67.231 11.698  2.005   1.00 73.07  ?  130 ALA B C     1 
ATOM   3001 O O     . ALA B 1 130 ? 66.086 11.628  1.542   1.00 74.15  ?  130 ALA B O     1 
ATOM   3002 C CB    . ALA B 1 130 ? 68.073 9.408   2.655   1.00 64.55  ?  130 ALA B CB    1 
ATOM   3003 N N     . MET B 1 131 ? 67.635 12.734  2.742   1.00 68.57  ?  131 MET B N     1 
ATOM   3004 C CA    . MET B 1 131 ? 66.782 13.893  2.990   1.00 77.05  ?  131 MET B CA    1 
ATOM   3005 C C     . MET B 1 131 ? 66.655 14.801  1.778   1.00 73.80  ?  131 MET B C     1 
ATOM   3006 O O     . MET B 1 131 ? 65.888 15.769  1.813   1.00 71.68  ?  131 MET B O     1 
ATOM   3007 C CB    . MET B 1 131 ? 67.328 14.675  4.172   1.00 76.39  ?  131 MET B CB    1 
ATOM   3008 C CG    . MET B 1 131 ? 67.571 13.780  5.363   1.00 76.72  ?  131 MET B CG    1 
ATOM   3009 S SD    . MET B 1 131 ? 66.440 14.206  6.674   1.00 77.40  ?  131 MET B SD    1 
ATOM   3010 C CE    . MET B 1 131 ? 67.112 15.801  7.080   1.00 75.66  ?  131 MET B CE    1 
ATOM   3011 N N     . ASP B 1 132 ? 67.418 14.526  0.727   1.00 74.31  ?  132 ASP B N     1 
ATOM   3012 C CA    . ASP B 1 132 ? 67.340 15.284  -0.516  1.00 74.08  ?  132 ASP B CA    1 
ATOM   3013 C C     . ASP B 1 132 ? 67.812 14.336  -1.615  1.00 74.99  ?  132 ASP B C     1 
ATOM   3014 O O     . ASP B 1 132 ? 69.024 14.187  -1.817  1.00 73.88  ?  132 ASP B O     1 
ATOM   3015 C CB    . ASP B 1 132 ? 68.200 16.537  -0.436  1.00 77.73  ?  132 ASP B CB    1 
ATOM   3016 C CG    . ASP B 1 132 ? 67.981 17.492  -1.603  1.00 82.99  ?  132 ASP B CG    1 
ATOM   3017 O OD1   . ASP B 1 132 ? 67.158 17.182  -2.508  1.00 80.24  ?  132 ASP B OD1   1 
ATOM   3018 O OD2   . ASP B 1 132 ? 68.643 18.563  -1.602  1.00 78.44  -1 132 ASP B OD2   1 
ATOM   3019 N N     . LEU B 1 133 ? 66.849 13.709  -2.317  1.00 75.30  ?  133 LEU B N     1 
ATOM   3020 C CA    . LEU B 1 133 ? 67.126 12.668  -3.307  1.00 63.63  ?  133 LEU B CA    1 
ATOM   3021 C C     . LEU B 1 133 ? 67.286 13.297  -4.687  1.00 64.90  ?  133 LEU B C     1 
ATOM   3022 O O     . LEU B 1 133 ? 66.305 13.837  -5.225  1.00 65.38  ?  133 LEU B O     1 
ATOM   3023 C CB    . LEU B 1 133 ? 65.993 11.633  -3.322  1.00 63.91  ?  133 LEU B CB    1 
ATOM   3024 C CG    . LEU B 1 133 ? 65.819 10.586  -2.215  1.00 61.60  ?  133 LEU B CG    1 
ATOM   3025 C CD1   . LEU B 1 133 ? 64.980 9.408   -2.692  1.00 57.98  ?  133 LEU B CD1   1 
ATOM   3026 C CD2   . LEU B 1 133 ? 67.165 10.098  -1.719  1.00 62.56  ?  133 LEU B CD2   1 
ATOM   3027 N N     . PRO B 1 134 ? 68.477 13.233  -5.313  1.00 62.39  ?  134 PRO B N     1 
ATOM   3028 C CA    . PRO B 1 134 ? 68.700 13.953  -6.584  1.00 61.75  ?  134 PRO B CA    1 
ATOM   3029 C C     . PRO B 1 134 ? 68.261 13.165  -7.821  1.00 61.49  ?  134 PRO B C     1 
ATOM   3030 O O     . PRO B 1 134 ? 69.062 12.855  -8.716  1.00 62.69  ?  134 PRO B O     1 
ATOM   3031 C CB    . PRO B 1 134 ? 70.214 14.201  -6.551  1.00 57.80  ?  134 PRO B CB    1 
ATOM   3032 C CG    . PRO B 1 134 ? 70.770 13.074  -5.752  1.00 58.00  ?  134 PRO B CG    1 
ATOM   3033 C CD    . PRO B 1 134 ? 69.722 12.669  -4.763  1.00 59.58  ?  134 PRO B CD    1 
ATOM   3034 N N     . PHE B 1 135 ? 66.958 12.885  -7.915  1.00 57.82  ?  135 PHE B N     1 
ATOM   3035 C CA    . PHE B 1 135 ? 66.415 11.975  -8.913  1.00 61.68  ?  135 PHE B CA    1 
ATOM   3036 C C     . PHE B 1 135 ? 65.044 12.445  -9.369  1.00 65.06  ?  135 PHE B C     1 
ATOM   3037 O O     . PHE B 1 135 ? 64.216 12.819  -8.533  1.00 65.99  ?  135 PHE B O     1 
ATOM   3038 C CB    . PHE B 1 135 ? 66.264 10.571  -8.336  1.00 60.76  ?  135 PHE B CB    1 
ATOM   3039 C CG    . PHE B 1 135 ? 67.536 9.985   -7.788  1.00 58.82  ?  135 PHE B CG    1 
ATOM   3040 C CD1   . PHE B 1 135 ? 68.697 9.978   -8.542  1.00 62.38  ?  135 PHE B CD1   1 
ATOM   3041 C CD2   . PHE B 1 135 ? 67.561 9.411   -6.530  1.00 61.11  ?  135 PHE B CD2   1 
ATOM   3042 C CE1   . PHE B 1 135 ? 69.863 9.431   -8.044  1.00 64.46  ?  135 PHE B CE1   1 
ATOM   3043 C CE2   . PHE B 1 135 ? 68.725 8.851   -6.022  1.00 59.96  ?  135 PHE B CE2   1 
ATOM   3044 C CZ    . PHE B 1 135 ? 69.875 8.862   -6.778  1.00 60.46  ?  135 PHE B CZ    1 
ATOM   3045 N N     . GLU B 1 136 ? 64.782 12.373  -10.680 1.00 65.17  ?  136 GLU B N     1 
ATOM   3046 C CA    . GLU B 1 136 ? 63.476 12.769  -11.203 1.00 63.75  ?  136 GLU B CA    1 
ATOM   3047 C C     . GLU B 1 136 ? 62.371 12.102  -10.387 1.00 62.36  ?  136 GLU B C     1 
ATOM   3048 O O     . GLU B 1 136 ? 62.578 11.048  -9.781  1.00 62.67  ?  136 GLU B O     1 
ATOM   3049 C CB    . GLU B 1 136 ? 63.347 12.376  -12.687 1.00 68.28  ?  136 GLU B CB    1 
ATOM   3050 C CG    . GLU B 1 136 ? 63.962 13.362  -13.699 1.00 65.65  ?  136 GLU B CG    1 
ATOM   3051 C CD    . GLU B 1 136 ? 63.407 14.756  -13.513 1.00 69.39  ?  136 GLU B CD    1 
ATOM   3052 O OE1   . GLU B 1 136 ? 62.226 14.861  -13.104 1.00 78.32  ?  136 GLU B OE1   1 
ATOM   3053 O OE2   . GLU B 1 136 ? 64.140 15.743  -13.749 1.00 70.10  -1 136 GLU B OE2   1 
ATOM   3054 N N     . ASP B 1 137 ? 61.197 12.732  -10.324 1.00 64.33  ?  137 ASP B N     1 
ATOM   3055 C CA    . ASP B 1 137 ? 60.071 12.056  -9.679  1.00 58.38  ?  137 ASP B CA    1 
ATOM   3056 C C     . ASP B 1 137 ? 59.783 10.774  -10.447 1.00 65.65  ?  137 ASP B C     1 
ATOM   3057 O O     . ASP B 1 137 ? 60.066 10.677  -11.649 1.00 70.36  ?  137 ASP B O     1 
ATOM   3058 C CB    . ASP B 1 137 ? 58.810 12.934  -9.646  1.00 56.79  ?  137 ASP B CB    1 
ATOM   3059 C CG    . ASP B 1 137 ? 58.941 14.153  -8.727  1.00 67.64  ?  137 ASP B CG    1 
ATOM   3060 O OD1   . ASP B 1 137 ? 59.957 14.272  -8.016  1.00 67.19  ?  137 ASP B OD1   1 
ATOM   3061 O OD2   . ASP B 1 137 ? 58.023 15.017  -8.711  1.00 79.73  -1 137 ASP B OD2   1 
ATOM   3062 N N     . GLU B 1 138 ? 59.255 9.774   -9.745  1.00 61.61  ?  138 GLU B N     1 
ATOM   3063 C CA    . GLU B 1 138 ? 58.791 8.531   -10.378 1.00 60.99  ?  138 GLU B CA    1 
ATOM   3064 C C     . GLU B 1 138 ? 59.868 7.915   -11.275 1.00 64.46  ?  138 GLU B C     1 
ATOM   3065 O O     . GLU B 1 138 ? 59.691 7.759   -12.494 1.00 77.96  ?  138 GLU B O     1 
ATOM   3066 C CB    . GLU B 1 138 ? 57.493 8.759   -11.173 1.00 61.77  ?  138 GLU B CB    1 
ATOM   3067 C CG    . GLU B 1 138 ? 56.219 8.822   -10.323 1.00 63.49  ?  138 GLU B CG    1 
ATOM   3068 C CD    . GLU B 1 138 ? 54.966 9.134   -11.115 1.00 66.05  ?  138 GLU B CD    1 
ATOM   3069 O OE1   . GLU B 1 138 ? 54.886 8.789   -12.313 1.00 67.23  ?  138 GLU B OE1   1 
ATOM   3070 O OE2   . GLU B 1 138 ? 54.050 9.731   -10.519 1.00 70.04  -1 138 GLU B OE2   1 
ATOM   3071 N N     . SER B 1 139 ? 61.007 7.574   -10.665 1.00 62.94  ?  139 SER B N     1 
ATOM   3072 C CA    . SER B 1 139 ? 62.090 6.950   -11.420 1.00 62.04  ?  139 SER B CA    1 
ATOM   3073 C C     . SER B 1 139 ? 62.547 5.624   -10.812 1.00 58.42  ?  139 SER B C     1 
ATOM   3074 O O     . SER B 1 139 ? 63.604 5.106   -11.199 1.00 57.55  ?  139 SER B O     1 
ATOM   3075 C CB    . SER B 1 139 ? 63.262 7.926   -11.570 1.00 64.37  ?  139 SER B CB    1 
ATOM   3076 O OG    . SER B 1 139 ? 63.690 8.410   -10.302 1.00 62.03  ?  139 SER B OG    1 
ATOM   3077 N N     . PHE B 1 140 ? 61.760 5.048   -9.898  1.00 54.20  ?  140 PHE B N     1 
ATOM   3078 C CA    . PHE B 1 140 ? 62.081 3.773   -9.259  1.00 55.22  ?  140 PHE B CA    1 
ATOM   3079 C C     . PHE B 1 140 ? 60.850 2.882   -9.067  1.00 59.24  ?  140 PHE B C     1 
ATOM   3080 O O     . PHE B 1 140 ? 59.794 3.336   -8.618  1.00 61.63  ?  140 PHE B O     1 
ATOM   3081 C CB    . PHE B 1 140 ? 62.755 4.002   -7.899  1.00 60.59  ?  140 PHE B CB    1 
ATOM   3082 C CG    . PHE B 1 140 ? 64.074 4.653   -8.014  1.00 55.55  ?  140 PHE B CG    1 
ATOM   3083 C CD1   . PHE B 1 140 ? 65.190 3.905   -8.336  1.00 53.76  ?  140 PHE B CD1   1 
ATOM   3084 C CD2   . PHE B 1 140 ? 64.191 6.021   -7.864  1.00 53.67  ?  140 PHE B CD2   1 
ATOM   3085 C CE1   . PHE B 1 140 ? 66.404 4.503   -8.484  1.00 56.38  ?  140 PHE B CE1   1 
ATOM   3086 C CE2   . PHE B 1 140 ? 65.399 6.635   -8.003  1.00 54.27  ?  140 PHE B CE2   1 
ATOM   3087 C CZ    . PHE B 1 140 ? 66.515 5.879   -8.314  1.00 58.82  ?  140 PHE B CZ    1 
ATOM   3088 N N     . ASP B 1 141 ? 61.003 1.594   -9.389  1.00 55.51  ?  141 ASP B N     1 
ATOM   3089 C CA    . ASP B 1 141 ? 59.963 0.618   -9.106  1.00 53.86  ?  141 ASP B CA    1 
ATOM   3090 C C     . ASP B 1 141 ? 59.940 0.201   -7.632  1.00 58.65  ?  141 ASP B C     1 
ATOM   3091 O O     . ASP B 1 141 ? 58.891 -0.228  -7.136  1.00 58.00  ?  141 ASP B O     1 
ATOM   3092 C CB    . ASP B 1 141 ? 60.152 -0.614  -9.999  1.00 52.67  ?  141 ASP B CB    1 
ATOM   3093 C CG    . ASP B 1 141 ? 60.212 -0.269  -11.486 1.00 58.68  ?  141 ASP B CG    1 
ATOM   3094 O OD1   . ASP B 1 141 ? 59.349 0.506   -11.950 1.00 60.78  ?  141 ASP B OD1   1 
ATOM   3095 O OD2   . ASP B 1 141 ? 61.115 -0.784  -12.191 1.00 56.99  -1 141 ASP B OD2   1 
ATOM   3096 N N     . ALA B 1 142 ? 61.052 0.304   -6.913  1.00 51.74  ?  142 ALA B N     1 
ATOM   3097 C CA    . ALA B 1 142 ? 61.054 -0.160  -5.534  1.00 52.44  ?  142 ALA B CA    1 
ATOM   3098 C C     . ALA B 1 142 ? 62.193 0.524   -4.795  1.00 57.56  ?  142 ALA B C     1 
ATOM   3099 O O     . ALA B 1 142 ? 63.168 0.944   -5.419  1.00 56.81  ?  142 ALA B O     1 
ATOM   3100 C CB    . ALA B 1 142 ? 61.197 -1.685  -5.451  1.00 48.67  ?  142 ALA B CB    1 
ATOM   3101 N N     . VAL B 1 143 ? 62.058 0.664   -3.470  1.00 57.86  ?  143 VAL B N     1 
ATOM   3102 C CA    . VAL B 1 143 ? 63.134 1.177   -2.628  1.00 54.90  ?  143 VAL B CA    1 
ATOM   3103 C C     . VAL B 1 143 ? 63.328 0.248   -1.439  1.00 54.94  ?  143 VAL B C     1 
ATOM   3104 O O     . VAL B 1 143 ? 62.360 -0.123  -0.769  1.00 58.44  ?  143 VAL B O     1 
ATOM   3105 C CB    . VAL B 1 143 ? 62.869 2.605   -2.137  1.00 50.42  ?  143 VAL B CB    1 
ATOM   3106 C CG1   . VAL B 1 143 ? 64.107 3.122   -1.443  1.00 54.08  ?  143 VAL B CG1   1 
ATOM   3107 C CG2   . VAL B 1 143 ? 62.503 3.497   -3.285  1.00 50.16  ?  143 VAL B CG2   1 
ATOM   3108 N N     . ILE B 1 144 ? 64.576 -0.134  -1.189  1.00 59.14  ?  144 ILE B N     1 
ATOM   3109 C CA    . ILE B 1 144 ? 64.946 -0.944  -0.041  1.00 55.81  ?  144 ILE B CA    1 
ATOM   3110 C C     . ILE B 1 144 ? 65.830 -0.079  0.825   1.00 55.40  ?  144 ILE B C     1 
ATOM   3111 O O     . ILE B 1 144 ? 66.833 0.461   0.348   1.00 55.59  ?  144 ILE B O     1 
ATOM   3112 C CB    . ILE B 1 144 ? 65.671 -2.241  -0.453  1.00 49.95  ?  144 ILE B CB    1 
ATOM   3113 C CG1   . ILE B 1 144 ? 66.279 -2.955  0.758   1.00 57.73  ?  144 ILE B CG1   1 
ATOM   3114 C CG2   . ILE B 1 144 ? 66.751 -1.944  -1.462  1.00 52.59  ?  144 ILE B CG2   1 
ATOM   3115 C CD1   . ILE B 1 144 ? 66.837 -4.333  0.452   1.00 56.94  ?  144 ILE B CD1   1 
ATOM   3116 N N     . ALA B 1 145 ? 65.458 0.068   2.085   1.00 58.59  ?  145 ALA B N     1 
ATOM   3117 C CA    . ALA B 1 145 ? 66.268 0.822   3.031   1.00 58.74  ?  145 ALA B CA    1 
ATOM   3118 C C     . ALA B 1 145 ? 66.720 -0.116  4.152   1.00 62.67  ?  145 ALA B C     1 
ATOM   3119 O O     . ALA B 1 145 ? 66.141 -0.166  5.247   1.00 66.44  ?  145 ALA B O     1 
ATOM   3120 C CB    . ALA B 1 145 ? 65.483 1.965   3.523   1.00 60.99  ?  145 ALA B CB    1 
ATOM   3121 N N     . LEU B 1 146 ? 67.819 -0.816  3.890   1.00 60.77  ?  146 LEU B N     1 
ATOM   3122 C CA    . LEU B 1 146 ? 68.247 -1.956  4.699   1.00 63.64  ?  146 LEU B CA    1 
ATOM   3123 C C     . LEU B 1 146 ? 69.128 -1.471  5.849   1.00 63.56  ?  146 LEU B C     1 
ATOM   3124 O O     . LEU B 1 146 ? 70.346 -1.328  5.698   1.00 65.46  ?  146 LEU B O     1 
ATOM   3125 C CB    . LEU B 1 146 ? 68.951 -2.957  3.792   1.00 60.88  ?  146 LEU B CB    1 
ATOM   3126 C CG    . LEU B 1 146 ? 69.583 -4.254  4.256   1.00 59.81  ?  146 LEU B CG    1 
ATOM   3127 C CD1   . LEU B 1 146 ? 68.849 -4.841  5.412   1.00 62.02  ?  146 LEU B CD1   1 
ATOM   3128 C CD2   . LEU B 1 146 ? 69.511 -5.185  3.087   1.00 62.83  ?  146 LEU B CD2   1 
ATOM   3129 N N     . GLU B 1 147 ? 68.498 -1.238  7.010   1.00 60.83  ?  147 GLU B N     1 
ATOM   3130 C CA    . GLU B 1 147 ? 69.150 -0.703  8.213   1.00 66.44  ?  147 GLU B CA    1 
ATOM   3131 C C     . GLU B 1 147 ? 69.705 0.694   7.981   1.00 66.02  ?  147 GLU B C     1 
ATOM   3132 O O     . GLU B 1 147 ? 70.825 1.032   8.360   1.00 63.91  ?  147 GLU B O     1 
ATOM   3133 C CB    . GLU B 1 147 ? 70.235 -1.624  8.720   1.00 70.32  ?  147 GLU B CB    1 
ATOM   3134 C CG    . GLU B 1 147 ? 69.777 -2.365  9.900   1.00 71.44  ?  147 GLU B CG    1 
ATOM   3135 C CD    . GLU B 1 147 ? 70.900 -3.023  10.588  1.00 78.23  ?  147 GLU B CD    1 
ATOM   3136 O OE1   . GLU B 1 147 ? 71.880 -2.328  10.915  1.00 89.42  ?  147 GLU B OE1   1 
ATOM   3137 O OE2   . GLU B 1 147 ? 70.810 -4.240  10.784  1.00 82.49  -1 147 GLU B OE2   1 
ATOM   3138 N N     . SER B 1 148 ? 68.912 1.512   7.368   1.00 67.56  ?  148 SER B N     1 
ATOM   3139 C CA    . SER B 1 148 ? 69.386 2.815   6.979   1.00 68.75  ?  148 SER B CA    1 
ATOM   3140 C C     . SER B 1 148 ? 68.568 3.924   7.582   1.00 67.34  ?  148 SER B C     1 
ATOM   3141 O O     . SER B 1 148 ? 69.125 4.934   7.995   1.00 63.63  ?  148 SER B O     1 
ATOM   3142 C CB    . SER B 1 148 ? 69.336 2.942   5.460   1.00 60.74  ?  148 SER B CB    1 
ATOM   3143 O OG    . SER B 1 148 ? 68.007 2.753   5.003   1.00 61.79  ?  148 SER B OG    1 
ATOM   3144 N N     . ILE B 1 149 ? 67.246 3.767   7.613   1.00 69.48  ?  149 ILE B N     1 
ATOM   3145 C CA    . ILE B 1 149 ? 66.419 4.860   8.079   1.00 62.87  ?  149 ILE B CA    1 
ATOM   3146 C C     . ILE B 1 149 ? 66.790 5.248   9.498   1.00 70.69  ?  149 ILE B C     1 
ATOM   3147 O O     . ILE B 1 149 ? 66.575 6.395   9.890   1.00 72.80  ?  149 ILE B O     1 
ATOM   3148 C CB    . ILE B 1 149 ? 64.933 4.478   7.927   1.00 67.14  ?  149 ILE B CB    1 
ATOM   3149 C CG1   . ILE B 1 149 ? 64.068 5.708   7.661   1.00 64.53  ?  149 ILE B CG1   1 
ATOM   3150 C CG2   . ILE B 1 149 ? 64.448 3.814   9.163   1.00 73.15  ?  149 ILE B CG2   1 
ATOM   3151 C CD1   . ILE B 1 149 ? 62.568 5.443   7.637   1.00 68.82  ?  149 ILE B CD1   1 
ATOM   3152 N N     . ILE B 1 150 ? 67.435 4.334   10.238  1.00 71.61  ?  150 ILE B N     1 
ATOM   3153 C CA    . ILE B 1 150 ? 67.716 4.515   11.665  1.00 72.53  ?  150 ILE B CA    1 
ATOM   3154 C C     . ILE B 1 150 ? 68.657 5.692   11.917  1.00 74.91  ?  150 ILE B C     1 
ATOM   3155 O O     . ILE B 1 150 ? 68.521 6.409   12.920  1.00 83.33  ?  150 ILE B O     1 
ATOM   3156 C CB    . ILE B 1 150 ? 68.290 3.221   12.275  1.00 72.12  ?  150 ILE B CB    1 
ATOM   3157 C CG1   . ILE B 1 150 ? 69.467 2.681   11.443  1.00 75.24  ?  150 ILE B CG1   1 
ATOM   3158 C CG2   . ILE B 1 150 ? 67.194 2.201   12.457  1.00 70.28  ?  150 ILE B CG2   1 
ATOM   3159 C CD1   . ILE B 1 150 ? 70.117 1.466   12.030  1.00 77.72  ?  150 ILE B CD1   1 
ATOM   3160 N N     . HIS B 1 151 ? 69.636 5.899   11.045  1.00 67.40  ?  151 HIS B N     1 
ATOM   3161 C CA    . HIS B 1 151 ? 70.582 6.995   11.179  1.00 70.62  ?  151 HIS B CA    1 
ATOM   3162 C C     . HIS B 1 151 ? 70.048 8.329   10.669  1.00 73.66  ?  151 HIS B C     1 
ATOM   3163 O O     . HIS B 1 151 ? 70.859 9.193   10.308  1.00 77.67  ?  151 HIS B O     1 
ATOM   3164 C CB    . HIS B 1 151 ? 71.857 6.691   10.407  1.00 73.15  ?  151 HIS B CB    1 
ATOM   3165 C CG    . HIS B 1 151 ? 72.562 5.457   10.843  1.00 73.12  ?  151 HIS B CG    1 
ATOM   3166 N ND1   . HIS B 1 151 ? 73.173 5.344   12.070  1.00 85.64  ?  151 HIS B ND1   1 
ATOM   3167 C CD2   . HIS B 1 151 ? 72.820 4.305   10.185  1.00 77.70  ?  151 HIS B CD2   1 
ATOM   3168 C CE1   . HIS B 1 151 ? 73.755 4.161   12.161  1.00 91.54  ?  151 HIS B CE1   1 
ATOM   3169 N NE2   . HIS B 1 151 ? 73.566 3.517   11.024  1.00 82.49  ?  151 HIS B NE2   1 
ATOM   3170 N N     . MET B 1 152 ? 68.745 8.541   10.554  1.00 77.01  ?  152 MET B N     1 
ATOM   3171 C CA    . MET B 1 152 ? 68.497 9.681   9.686   1.00 77.64  ?  152 MET B CA    1 
ATOM   3172 C C     . MET B 1 152 ? 67.747 10.797  10.393  1.00 80.01  ?  152 MET B C     1 
ATOM   3173 O O     . MET B 1 152 ? 66.996 10.557  11.345  1.00 77.99  ?  152 MET B O     1 
ATOM   3174 C CB    . MET B 1 152 ? 67.726 9.261   8.434   1.00 70.96  ?  152 MET B CB    1 
ATOM   3175 C CG    . MET B 1 152 ? 68.488 8.244   7.633   1.00 77.61  ?  152 MET B CG    1 
ATOM   3176 S SD    . MET B 1 152 ? 68.012 8.234   5.925   1.00 73.31  ?  152 MET B SD    1 
ATOM   3177 C CE    . MET B 1 152 ? 66.365 7.663   6.180   1.00 75.19  ?  152 MET B CE    1 
ATOM   3178 N N     . PRO B 1 153 ? 67.949 12.030  9.957   1.00 80.10  ?  153 PRO B N     1 
ATOM   3179 C CA    . PRO B 1 153 ? 67.446 13.167  10.740  1.00 79.95  ?  153 PRO B CA    1 
ATOM   3180 C C     . PRO B 1 153 ? 65.924 13.274  10.807  1.00 80.11  ?  153 PRO B C     1 
ATOM   3181 O O     . PRO B 1 153 ? 65.377 13.271  11.913  1.00 85.38  ?  153 PRO B O     1 
ATOM   3182 C CB    . PRO B 1 153 ? 68.085 14.376  10.045  1.00 80.75  ?  153 PRO B CB    1 
ATOM   3183 C CG    . PRO B 1 153 ? 69.346 13.810  9.395   1.00 84.36  ?  153 PRO B CG    1 
ATOM   3184 C CD    . PRO B 1 153 ? 68.960 12.425  8.954   1.00 80.61  ?  153 PRO B CD    1 
ATOM   3185 N N     . ASP B 1 154 ? 65.204 13.334  9.687   1.00 80.00  ?  154 ASP B N     1 
ATOM   3186 C CA    . ASP B 1 154 ? 63.752 13.488  9.758   1.00 76.85  ?  154 ASP B CA    1 
ATOM   3187 C C     . ASP B 1 154 ? 63.035 12.407  8.953   1.00 76.17  ?  154 ASP B C     1 
ATOM   3188 O O     . ASP B 1 154 ? 62.831 12.557  7.742   1.00 76.62  ?  154 ASP B O     1 
ATOM   3189 C CB    . ASP B 1 154 ? 63.316 14.864  9.301   1.00 73.42  ?  154 ASP B CB    1 
ATOM   3190 C CG    . ASP B 1 154 ? 61.843 15.090  9.539   1.00 79.05  ?  154 ASP B CG    1 
ATOM   3191 O OD1   . ASP B 1 154 ? 61.364 14.690  10.615  1.00 86.90  ?  154 ASP B OD1   1 
ATOM   3192 O OD2   . ASP B 1 154 ? 61.153 15.645  8.667   1.00 82.93  -1 154 ASP B OD2   1 
ATOM   3193 N N     . ARG B 1 155 ? 62.586 11.358  9.658   1.00 76.86  ?  155 ARG B N     1 
ATOM   3194 C CA    . ARG B 1 155 ? 61.894 10.250  9.009   1.00 75.02  ?  155 ARG B CA    1 
ATOM   3195 C C     . ARG B 1 155 ? 60.743 10.748  8.142   1.00 76.09  ?  155 ARG B C     1 
ATOM   3196 O O     . ARG B 1 155 ? 60.642 10.375  6.972   1.00 77.45  ?  155 ARG B O     1 
ATOM   3197 C CB    . ARG B 1 155 ? 61.405 9.236   10.054  1.00 69.55  ?  155 ARG B CB    1 
ATOM   3198 C CG    . ARG B 1 155 ? 62.505 8.322   10.620  1.00 69.41  ?  155 ARG B CG    1 
ATOM   3199 C CD    . ARG B 1 155 ? 61.945 7.327   11.625  1.00 72.96  ?  155 ARG B CD    1 
ATOM   3200 N NE    . ARG B 1 155 ? 62.931 6.329   12.034  1.00 74.05  ?  155 ARG B NE    1 
ATOM   3201 C CZ    . ARG B 1 155 ? 63.697 6.417   13.117  1.00 78.17  ?  155 ARG B CZ    1 
ATOM   3202 N NH1   . ARG B 1 155 ? 63.623 7.460   13.937  1.00 76.79  ?  155 ARG B NH1   1 
ATOM   3203 N NH2   . ARG B 1 155 ? 64.541 5.425   13.399  1.00 78.08  ?  155 ARG B NH2   1 
ATOM   3204 N N     . ALA B 1 156 ? 59.905 11.643  8.672   1.00 77.06  ?  156 ALA B N     1 
ATOM   3205 C CA    . ALA B 1 156 ? 58.737 12.085  7.909   1.00 77.84  ?  156 ALA B CA    1 
ATOM   3206 C C     . ALA B 1 156 ? 59.137 12.689  6.567   1.00 77.75  ?  156 ALA B C     1 
ATOM   3207 O O     . ALA B 1 156 ? 58.366 12.621  5.597   1.00 76.39  ?  156 ALA B O     1 
ATOM   3208 C CB    . ALA B 1 156 ? 57.911 13.096  8.703   1.00 73.66  ?  156 ALA B CB    1 
ATOM   3209 N N     . GLN B 1 157 ? 60.363 13.202  6.473   1.00 76.96  ?  157 GLN B N     1 
ATOM   3210 C CA    . GLN B 1 157 ? 60.798 13.872  5.219   1.00 78.00  ?  157 GLN B CA    1 
ATOM   3211 C C     . GLN B 1 157 ? 61.431 12.837  4.297   1.00 79.43  ?  157 GLN B C     1 
ATOM   3212 O O     . GLN B 1 157 ? 61.104 12.818  3.106   1.00 76.97  ?  157 GLN B O     1 
ATOM   3213 C CB    . GLN B 1 157 ? 61.822 14.962  5.515   1.00 75.83  ?  157 GLN B CB    1 
ATOM   3214 C CG    . GLN B 1 157 ? 62.103 15.865  4.327   1.00 80.16  ?  157 GLN B CG    1 
ATOM   3215 C CD    . GLN B 1 157 ? 63.513 16.395  4.381   1.00 85.37  ?  157 GLN B CD    1 
ATOM   3216 O OE1   . GLN B 1 157 ? 63.886 17.304  3.646   1.00 93.80  ?  157 GLN B OE1   1 
ATOM   3217 N NE2   . GLN B 1 157 ? 64.308 15.824  5.270   1.00 82.58  ?  157 GLN B NE2   1 
ATOM   3218 N N     . VAL B 1 158 ? 62.323 12.024  4.845   1.00 78.58  ?  158 VAL B N     1 
ATOM   3219 C CA    . VAL B 1 158 ? 62.936 10.959  4.057   1.00 73.79  ?  158 VAL B CA    1 
ATOM   3220 C C     . VAL B 1 158 ? 61.863 10.118  3.374   1.00 71.88  ?  158 VAL B C     1 
ATOM   3221 O O     . VAL B 1 158 ? 61.885 9.949   2.148   1.00 68.38  ?  158 VAL B O     1 
ATOM   3222 C CB    . VAL B 1 158 ? 63.834 10.085  4.943   1.00 72.85  ?  158 VAL B CB    1 
ATOM   3223 C CG1   . VAL B 1 158 ? 64.181 8.905   4.146   1.00 63.00  ?  158 VAL B CG1   1 
ATOM   3224 C CG2   . VAL B 1 158 ? 65.073 10.845  5.368   1.00 69.09  ?  158 VAL B CG2   1 
ATOM   3225 N N     . LEU B 1 159 ? 60.874 9.627   4.154   1.00 75.25  ?  159 LEU B N     1 
ATOM   3226 C CA    . LEU B 1 159 ? 59.718 8.922   3.582   1.00 73.26  ?  159 LEU B CA    1 
ATOM   3227 C C     . LEU B 1 159 ? 58.994 9.779   2.538   1.00 70.59  ?  159 LEU B C     1 
ATOM   3228 O O     . LEU B 1 159 ? 58.578 9.273   1.491   1.00 69.93  ?  159 LEU B O     1 
ATOM   3229 C CB    . LEU B 1 159 ? 58.740 8.484   4.683   1.00 68.31  ?  159 LEU B CB    1 
ATOM   3230 C CG    . LEU B 1 159 ? 59.215 7.611   5.859   1.00 71.45  ?  159 LEU B CG    1 
ATOM   3231 C CD1   . LEU B 1 159 ? 58.066 7.363   6.837   1.00 66.89  ?  159 LEU B CD1   1 
ATOM   3232 C CD2   . LEU B 1 159 ? 59.835 6.296   5.411   1.00 65.50  ?  159 LEU B CD2   1 
ATOM   3233 N N     . ALA B 1 160 ? 58.811 11.074  2.803   1.00 73.22  ?  160 ALA B N     1 
ATOM   3234 C CA    . ALA B 1 160 ? 58.206 11.936  1.786   1.00 70.53  ?  160 ALA B CA    1 
ATOM   3235 C C     . ALA B 1 160 ? 59.088 12.047  0.550   1.00 67.73  ?  160 ALA B C     1 
ATOM   3236 O O     . ALA B 1 160 ? 58.575 12.226  -0.562  1.00 63.25  ?  160 ALA B O     1 
ATOM   3237 C CB    . ALA B 1 160 ? 57.914 13.321  2.364   1.00 74.37  ?  160 ALA B CB    1 
ATOM   3238 N N     . GLN B 1 161 ? 60.411 11.958  0.720   1.00 69.71  ?  161 GLN B N     1 
ATOM   3239 C CA    . GLN B 1 161 ? 61.301 11.927  -0.442  1.00 68.89  ?  161 GLN B CA    1 
ATOM   3240 C C     . GLN B 1 161 ? 61.096 10.647  -1.262  1.00 66.16  ?  161 GLN B C     1 
ATOM   3241 O O     . GLN B 1 161 ? 60.907 10.703  -2.483  1.00 66.04  ?  161 GLN B O     1 
ATOM   3242 C CB    . GLN B 1 161 ? 62.767 12.071  0.004   1.00 69.68  ?  161 GLN B CB    1 
ATOM   3243 C CG    . GLN B 1 161 ? 63.285 13.519  -0.006  1.00 70.28  ?  161 GLN B CG    1 
ATOM   3244 C CD    . GLN B 1 161 ? 63.250 14.162  -1.403  1.00 70.30  ?  161 GLN B CD    1 
ATOM   3245 O OE1   . GLN B 1 161 ? 64.175 13.961  -2.186  1.00 75.29  ?  161 GLN B OE1   1 
ATOM   3246 N NE2   . GLN B 1 161 ? 62.181 14.921  -1.722  1.00 69.23  ?  161 GLN B NE2   1 
ATOM   3247 N N     . VAL B 1 162 ? 61.084 9.488   -0.587  1.00 64.60  ?  162 VAL B N     1 
ATOM   3248 C CA    . VAL B 1 162 ? 60.878 8.192   -1.240  1.00 59.19  ?  162 VAL B CA    1 
ATOM   3249 C C     . VAL B 1 162 ? 59.514 8.137   -1.926  1.00 60.65  ?  162 VAL B C     1 
ATOM   3250 O O     . VAL B 1 162 ? 59.388 7.637   -3.046  1.00 64.40  ?  162 VAL B O     1 
ATOM   3251 C CB    . VAL B 1 162 ? 61.047 7.050   -0.214  1.00 59.82  ?  162 VAL B CB    1 
ATOM   3252 C CG1   . VAL B 1 162 ? 60.596 5.731   -0.793  1.00 53.05  ?  162 VAL B CG1   1 
ATOM   3253 C CG2   . VAL B 1 162 ? 62.483 6.934   0.241   1.00 57.20  ?  162 VAL B CG2   1 
ATOM   3254 N N     . GLY B 1 163 ? 58.470 8.649   -1.277  1.00 56.30  ?  163 GLY B N     1 
ATOM   3255 C CA    . GLY B 1 163 ? 57.164 8.628   -1.900  1.00 60.01  ?  163 GLY B CA    1 
ATOM   3256 C C     . GLY B 1 163 ? 57.117 9.394   -3.197  1.00 64.48  ?  163 GLY B C     1 
ATOM   3257 O O     . GLY B 1 163 ? 56.218 9.164   -4.012  1.00 67.42  ?  163 GLY B O     1 
ATOM   3258 N N     . ARG B 1 164 ? 58.093 10.274  -3.417  1.00 61.16  ?  164 ARG B N     1 
ATOM   3259 C CA    . ARG B 1 164 ? 58.179 11.108  -4.612  1.00 57.96  ?  164 ARG B CA    1 
ATOM   3260 C C     . ARG B 1 164 ? 58.836 10.372  -5.777  1.00 64.95  ?  164 ARG B C     1 
ATOM   3261 O O     . ARG B 1 164 ? 58.363 10.445  -6.923  1.00 59.72  ?  164 ARG B O     1 
ATOM   3262 C CB    . ARG B 1 164 ? 58.968 12.367  -4.268  1.00 58.69  ?  164 ARG B CB    1 
ATOM   3263 C CG    . ARG B 1 164 ? 59.063 13.362  -5.376  1.00 59.85  ?  164 ARG B CG    1 
ATOM   3264 C CD    . ARG B 1 164 ? 59.829 14.565  -4.889  1.00 65.59  ?  164 ARG B CD    1 
ATOM   3265 N NE    . ARG B 1 164 ? 61.178 14.189  -4.499  1.00 61.40  ?  164 ARG B NE    1 
ATOM   3266 C CZ    . ARG B 1 164 ? 62.170 14.027  -5.362  1.00 65.74  ?  164 ARG B CZ    1 
ATOM   3267 N NH1   . ARG B 1 164 ? 61.983 14.174  -6.667  1.00 58.56  ?  164 ARG B NH1   1 
ATOM   3268 N NH2   . ARG B 1 164 ? 63.381 13.717  -4.903  1.00 63.95  ?  164 ARG B NH2   1 
ATOM   3269 N N     . VAL B 1 165 ? 59.954 9.697   -5.496  1.00 64.25  ?  165 VAL B N     1 
ATOM   3270 C CA    . VAL B 1 165 ? 60.673 8.936   -6.507  1.00 60.29  ?  165 VAL B CA    1 
ATOM   3271 C C     . VAL B 1 165 ? 59.981 7.611   -6.818  1.00 61.89  ?  165 VAL B C     1 
ATOM   3272 O O     . VAL B 1 165 ? 60.127 7.086   -7.932  1.00 67.64  ?  165 VAL B O     1 
ATOM   3273 C CB    . VAL B 1 165 ? 62.133 8.685   -6.086  1.00 58.43  ?  165 VAL B CB    1 
ATOM   3274 C CG1   . VAL B 1 165 ? 62.929 9.941   -6.197  1.00 59.16  ?  165 VAL B CG1   1 
ATOM   3275 C CG2   . VAL B 1 165 ? 62.204 8.171   -4.687  1.00 59.35  ?  165 VAL B CG2   1 
ATOM   3276 N N     . LEU B 1 166 ? 59.250 7.030   -5.859  1.00 62.54  ?  166 LEU B N     1 
ATOM   3277 C CA    . LEU B 1 166 ? 58.546 5.776   -6.107  1.00 58.91  ?  166 LEU B CA    1 
ATOM   3278 C C     . LEU B 1 166 ? 57.474 5.959   -7.179  1.00 60.72  ?  166 LEU B C     1 
ATOM   3279 O O     . LEU B 1 166 ? 56.583 6.808   -7.045  1.00 63.65  ?  166 LEU B O     1 
ATOM   3280 C CB    . LEU B 1 166 ? 57.912 5.269   -4.817  1.00 57.87  ?  166 LEU B CB    1 
ATOM   3281 C CG    . LEU B 1 166 ? 58.663 4.069   -4.281  1.00 54.54  ?  166 LEU B CG    1 
ATOM   3282 C CD1   . LEU B 1 166 ? 58.030 3.553   -3.037  1.00 55.42  ?  166 LEU B CD1   1 
ATOM   3283 C CD2   . LEU B 1 166 ? 58.638 3.013   -5.331  1.00 63.12  ?  166 LEU B CD2   1 
ATOM   3284 N N     . ARG B 1 167 ? 57.555 5.149   -8.243  1.00 58.33  ?  167 ARG B N     1 
ATOM   3285 C CA    . ARG B 1 167 ? 56.492 5.148   -9.235  1.00 60.69  ?  167 ARG B CA    1 
ATOM   3286 C C     . ARG B 1 167 ? 55.216 4.648   -8.547  1.00 58.28  ?  167 ARG B C     1 
ATOM   3287 O O     . ARG B 1 167 ? 55.277 4.032   -7.482  1.00 53.82  ?  167 ARG B O     1 
ATOM   3288 C CB    . ARG B 1 167 ? 56.879 4.276   -10.460 1.00 58.83  ?  167 ARG B CB    1 
ATOM   3289 C CG    . ARG B 1 167 ? 58.150 4.729   -11.279 1.00 57.76  ?  167 ARG B CG    1 
ATOM   3290 C CD    . ARG B 1 167 ? 58.534 3.828   -12.503 1.00 59.19  ?  167 ARG B CD    1 
ATOM   3291 N NE    . ARG B 1 167 ? 59.550 4.451   -13.353 1.00 67.33  ?  167 ARG B NE    1 
ATOM   3292 C CZ    . ARG B 1 167 ? 60.638 3.855   -13.825 1.00 62.10  ?  167 ARG B CZ    1 
ATOM   3293 N NH1   . ARG B 1 167 ? 60.833 2.553   -13.693 1.00 58.98  ?  167 ARG B NH1   1 
ATOM   3294 N NH2   . ARG B 1 167 ? 61.556 4.590   -14.443 1.00 62.74  ?  167 ARG B NH2   1 
ATOM   3295 N N     . PRO B 1 168 ? 54.045 4.965   -9.085  1.00 57.89  ?  168 PRO B N     1 
ATOM   3296 C CA    . PRO B 1 168 ? 52.820 4.373   -8.537  1.00 62.08  ?  168 PRO B CA    1 
ATOM   3297 C C     . PRO B 1 168 ? 52.905 2.855   -8.545  1.00 62.09  ?  168 PRO B C     1 
ATOM   3298 O O     . PRO B 1 168 ? 53.379 2.245   -9.501  1.00 69.79  ?  168 PRO B O     1 
ATOM   3299 C CB    . PRO B 1 168 ? 51.732 4.879   -9.484  1.00 65.35  ?  168 PRO B CB    1 
ATOM   3300 C CG    . PRO B 1 168 ? 52.281 6.173   -9.977  1.00 59.86  ?  168 PRO B CG    1 
ATOM   3301 C CD    . PRO B 1 168 ? 53.762 5.997   -10.090 1.00 61.98  ?  168 PRO B CD    1 
ATOM   3302 N N     . GLY B 1 169 ? 52.455 2.241   -7.463  1.00 62.82  ?  169 GLY B N     1 
ATOM   3303 C CA    . GLY B 1 169 ? 52.546 0.814   -7.308  1.00 64.79  ?  169 GLY B CA    1 
ATOM   3304 C C     . GLY B 1 169 ? 53.847 0.328   -6.713  1.00 55.86  ?  169 GLY B C     1 
ATOM   3305 O O     . GLY B 1 169 ? 53.907 -0.803  -6.227  1.00 58.16  ?  169 GLY B O     1 
ATOM   3306 N N     . GLY B 1 170 ? 54.881 1.150   -6.714  1.00 55.21  ?  170 GLY B N     1 
ATOM   3307 C CA    . GLY B 1 170 ? 56.134 0.732   -6.141  1.00 56.74  ?  170 GLY B CA    1 
ATOM   3308 C C     . GLY B 1 170 ? 56.019 0.563   -4.649  1.00 58.08  ?  170 GLY B C     1 
ATOM   3309 O O     . GLY B 1 170 ? 55.126 1.107   -4.012  1.00 65.21  ?  170 GLY B O     1 
ATOM   3310 N N     . ARG B 1 171 ? 56.961 -0.194  -4.123  1.00 54.77  ?  171 ARG B N     1 
ATOM   3311 C CA    . ARG B 1 171 ? 56.905 -0.527  -2.693  1.00 50.83  ?  171 ARG B CA    1 
ATOM   3312 C C     . ARG B 1 171 ? 58.197 -0.142  -1.998  1.00 54.96  ?  171 ARG B C     1 
ATOM   3313 O O     . ARG B 1 171 ? 59.259 -0.266  -2.611  1.00 57.69  ?  171 ARG B O     1 
ATOM   3314 C CB    . ARG B 1 171 ? 56.713 -2.032  -2.521  1.00 55.31  ?  171 ARG B CB    1 
ATOM   3315 C CG    . ARG B 1 171 ? 55.270 -2.470  -2.326  1.00 60.00  ?  171 ARG B CG    1 
ATOM   3316 C CD    . ARG B 1 171 ? 55.176 -3.982  -2.324  1.00 63.46  ?  171 ARG B CD    1 
ATOM   3317 N NE    . ARG B 1 171 ? 53.817 -4.452  -2.529  1.00 69.57  ?  171 ARG B NE    1 
ATOM   3318 C CZ    . ARG B 1 171 ? 53.254 -4.608  -3.719  1.00 72.61  ?  171 ARG B CZ    1 
ATOM   3319 N NH1   . ARG B 1 171 ? 53.901 -4.243  -4.810  1.00 73.19  ?  171 ARG B NH1   1 
ATOM   3320 N NH2   . ARG B 1 171 ? 52.046 -5.134  -3.812  1.00 79.69  ?  171 ARG B NH2   1 
ATOM   3321 N N     . LEU B 1 172 ? 58.086 0.312   -0.771  1.00 58.92  ?  172 LEU B N     1 
ATOM   3322 C CA    . LEU B 1 172 ? 59.211 0.643   0.091   1.00 55.32  ?  172 LEU B CA    1 
ATOM   3323 C C     . LEU B 1 172 ? 59.386 -0.462  1.130   1.00 58.76  ?  172 LEU B C     1 
ATOM   3324 O O     . LEU B 1 172 ? 58.427 -0.805  1.837   1.00 58.41  ?  172 LEU B O     1 
ATOM   3325 C CB    . LEU B 1 172 ? 58.954 1.994   0.761   1.00 56.33  ?  172 LEU B CB    1 
ATOM   3326 C CG    . LEU B 1 172 ? 59.680 2.346   2.051   1.00 53.31  ?  172 LEU B CG    1 
ATOM   3327 C CD1   . LEU B 1 172 ? 61.170 2.426   1.824   1.00 51.12  ?  172 LEU B CD1   1 
ATOM   3328 C CD2   . LEU B 1 172 ? 59.128 3.649   2.542   1.00 52.17  ?  172 LEU B CD2   1 
ATOM   3329 N N     . VAL B 1 173 ? 60.595 -1.029  1.215   1.00 54.92  ?  173 VAL B N     1 
ATOM   3330 C CA    . VAL B 1 173 ? 60.918 -2.031  2.231   1.00 57.16  ?  173 VAL B CA    1 
ATOM   3331 C C     . VAL B 1 173 ? 62.064 -1.505  3.080   1.00 61.84  ?  173 VAL B C     1 
ATOM   3332 O O     . VAL B 1 173 ? 63.158 -1.227  2.560   1.00 56.62  ?  173 VAL B O     1 
ATOM   3333 C CB    . VAL B 1 173 ? 61.284 -3.398  1.626   1.00 59.82  ?  173 VAL B CB    1 
ATOM   3334 C CG1   . VAL B 1 173 ? 61.498 -4.455  2.730   1.00 57.20  ?  173 VAL B CG1   1 
ATOM   3335 C CG2   . VAL B 1 173 ? 60.217 -3.853  0.642   1.00 65.52  ?  173 VAL B CG2   1 
ATOM   3336 N N     . LEU B 1 174 ? 61.816 -1.402  4.394   1.00 61.00  ?  174 LEU B N     1 
ATOM   3337 C CA    . LEU B 1 174 ? 62.788 -0.876  5.342   1.00 62.32  ?  174 LEU B CA    1 
ATOM   3338 C C     . LEU B 1 174 ? 62.848 -1.746  6.585   1.00 65.08  ?  174 LEU B C     1 
ATOM   3339 O O     . LEU B 1 174 ? 61.907 -2.457  6.931   1.00 66.32  ?  174 LEU B O     1 
ATOM   3340 C CB    . LEU B 1 174 ? 62.464 0.554   5.778   1.00 57.80  ?  174 LEU B CB    1 
ATOM   3341 C CG    . LEU B 1 174 ? 61.091 0.753   6.392   1.00 61.24  ?  174 LEU B CG    1 
ATOM   3342 C CD1   . LEU B 1 174 ? 61.213 0.748   7.875   1.00 65.01  ?  174 LEU B CD1   1 
ATOM   3343 C CD2   . LEU B 1 174 ? 60.502 2.068   5.889   1.00 59.58  ?  174 LEU B CD2   1 
ATOM   3344 N N     . THR B 1 175 ? 63.985 -1.678  7.244   1.00 65.45  ?  175 THR B N     1 
ATOM   3345 C CA    . THR B 1 175 ? 64.064 -2.011  8.648   1.00 64.70  ?  175 THR B CA    1 
ATOM   3346 C C     . THR B 1 175 ? 64.096 -0.704  9.438   1.00 70.96  ?  175 THR B C     1 
ATOM   3347 O O     . THR B 1 175 ? 64.297 0.368   8.846   1.00 71.47  ?  175 THR B O     1 
ATOM   3348 C CB    . THR B 1 175 ? 65.289 -2.883  8.923   1.00 65.33  ?  175 THR B CB    1 
ATOM   3349 O OG1   . THR B 1 175 ? 66.461 -2.326  8.320   1.00 63.86  ?  175 THR B OG1   1 
ATOM   3350 C CG2   . THR B 1 175 ? 65.051 -4.274  8.404   1.00 62.65  ?  175 THR B CG2   1 
ATOM   3351 N N     . ASP B 1 176 ? 63.831 -0.805  10.769  1.00 72.30  ?  176 ASP B N     1 
ATOM   3352 C CA    . ASP B 1 176 ? 63.882 0.256   11.802  1.00 69.46  ?  176 ASP B CA    1 
ATOM   3353 C C     . ASP B 1 176 ? 63.952 -0.364  13.208  1.00 69.57  ?  176 ASP B C     1 
ATOM   3354 O O     . ASP B 1 176 ? 63.568 -1.520  13.415  1.00 70.31  ?  176 ASP B O     1 
ATOM   3355 C CB    . ASP B 1 176 ? 62.664 1.201   11.722  1.00 68.38  ?  176 ASP B CB    1 
ATOM   3356 C CG    . ASP B 1 176 ? 63.030 2.678   11.943  1.00 72.23  ?  176 ASP B CG    1 
ATOM   3357 O OD1   . ASP B 1 176 ? 64.110 2.969   12.527  1.00 74.88  ?  176 ASP B OD1   1 
ATOM   3358 O OD2   . ASP B 1 176 ? 62.220 3.545   11.517  1.00 70.19  -1 176 ASP B OD2   1 
ATOM   3359 N N     . PHE B 1 177 ? 64.449 0.423   14.182  1.00 74.76  ?  177 PHE B N     1 
ATOM   3360 C CA    . PHE B 1 177 ? 64.426 0.074   15.608  1.00 70.81  ?  177 PHE B CA    1 
ATOM   3361 C C     . PHE B 1 177 ? 63.188 0.679   16.262  1.00 77.38  ?  177 PHE B C     1 
ATOM   3362 O O     . PHE B 1 177 ? 62.715 1.744   15.847  1.00 80.29  ?  177 PHE B O     1 
ATOM   3363 C CB    . PHE B 1 177 ? 65.651 0.606   16.349  1.00 70.44  ?  177 PHE B CB    1 
ATOM   3364 C CG    . PHE B 1 177 ? 66.900 -0.183  16.138  1.00 73.02  ?  177 PHE B CG    1 
ATOM   3365 C CD1   . PHE B 1 177 ? 66.953 -1.527  16.465  1.00 75.27  ?  177 PHE B CD1   1 
ATOM   3366 C CD2   . PHE B 1 177 ? 68.048 0.439   15.659  1.00 72.58  ?  177 PHE B CD2   1 
ATOM   3367 C CE1   . PHE B 1 177 ? 68.139 -2.250  16.293  1.00 74.55  ?  177 PHE B CE1   1 
ATOM   3368 C CE2   . PHE B 1 177 ? 69.231 -0.272  15.495  1.00 78.37  ?  177 PHE B CE2   1 
ATOM   3369 C CZ    . PHE B 1 177 ? 69.281 -1.618  15.810  1.00 75.08  ?  177 PHE B CZ    1 
ATOM   3370 N N     . PHE B 1 178 ? 62.679 -0.029  17.284  1.00 82.57  ?  178 PHE B N     1 
ATOM   3371 C CA    . PHE B 1 178 ? 61.461 0.477   17.954  1.00 76.14  ?  178 PHE B CA    1 
ATOM   3372 C C     . PHE B 1 178 ? 61.285 -0.070  19.364  1.00 81.43  ?  178 PHE B C     1 
ATOM   3373 O O     . PHE B 1 178 ? 61.967 -1.034  19.734  1.00 80.84  ?  178 PHE B O     1 
ATOM   3374 C CB    . PHE B 1 178 ? 60.211 0.172   17.125  1.00 76.14  ?  178 PHE B CB    1 
ATOM   3375 C CG    . PHE B 1 178 ? 59.633 -1.215  17.239  1.00 80.58  ?  178 PHE B CG    1 
ATOM   3376 C CD1   . PHE B 1 178 ? 60.352 -2.325  16.832  1.00 77.80  ?  178 PHE B CD1   1 
ATOM   3377 C CD2   . PHE B 1 178 ? 58.344 -1.403  17.705  1.00 75.48  ?  178 PHE B CD2   1 
ATOM   3378 C CE1   . PHE B 1 178 ? 59.809 -3.596  16.923  1.00 78.67  ?  178 PHE B CE1   1 
ATOM   3379 C CE2   . PHE B 1 178 ? 57.801 -2.673  17.793  1.00 83.12  ?  178 PHE B CE2   1 
ATOM   3380 C CZ    . PHE B 1 178 ? 58.533 -3.767  17.402  1.00 82.81  ?  178 PHE B CZ    1 
ATOM   3381 N N     . GLU B 1 179 ? 60.431 0.602   20.142  1.00 91.12  ?  179 GLU B N     1 
ATOM   3382 C CA    . GLU B 1 179 ? 60.051 0.160   21.479  1.00 85.42  ?  179 GLU B CA    1 
ATOM   3383 C C     . GLU B 1 179 ? 58.849 -0.771  21.332  1.00 84.75  ?  179 GLU B C     1 
ATOM   3384 O O     . GLU B 1 179 ? 57.746 -0.325  20.982  1.00 78.06  ?  179 GLU B O     1 
ATOM   3385 C CB    . GLU B 1 179 ? 59.737 1.365   22.372  1.00 87.75  ?  179 GLU B CB    1 
ATOM   3386 C CG    . GLU B 1 179 ? 60.875 2.434   22.463  1.00 88.06  ?  179 GLU B CG    1 
ATOM   3387 C CD    . GLU B 1 179 ? 60.771 3.397   23.677  1.00 101.13 ?  179 GLU B CD    1 
ATOM   3388 O OE1   . GLU B 1 179 ? 59.855 4.264   23.711  1.00 104.86 ?  179 GLU B OE1   1 
ATOM   3389 O OE2   . GLU B 1 179 ? 61.631 3.289   24.592  1.00 104.40 -1 179 GLU B OE2   1 
ATOM   3390 N N     . ARG B 1 180 ? 59.075 -2.072  21.570  1.00 88.02  ?  180 ARG B N     1 
ATOM   3391 C CA    . ARG B 1 180 ? 57.983 -3.042  21.527  1.00 89.19  ?  180 ARG B CA    1 
ATOM   3392 C C     . ARG B 1 180 ? 56.930 -2.706  22.569  1.00 94.02  ?  180 ARG B C     1 
ATOM   3393 O O     . ARG B 1 180 ? 55.725 -2.864  22.335  1.00 95.19  ?  180 ARG B O     1 
ATOM   3394 C CB    . ARG B 1 180 ? 58.540 -4.447  21.743  1.00 88.81  ?  180 ARG B CB    1 
ATOM   3395 C CG    . ARG B 1 180 ? 59.707 -4.750  20.827  1.00 83.79  ?  180 ARG B CG    1 
ATOM   3396 C CD    . ARG B 1 180 ? 60.434 -6.019  21.203  1.00 82.69  ?  180 ARG B CD    1 
ATOM   3397 N NE    . ARG B 1 180 ? 59.756 -7.218  20.731  1.00 75.50  ?  180 ARG B NE    1 
ATOM   3398 C CZ    . ARG B 1 180 ? 60.335 -8.405  20.624  1.00 77.53  ?  180 ARG B CZ    1 
ATOM   3399 N NH1   . ARG B 1 180 ? 61.607 -8.588  20.946  1.00 79.26  ?  180 ARG B NH1   1 
ATOM   3400 N NH2   . ARG B 1 180 ? 59.620 -9.435  20.187  1.00 81.24  ?  180 ARG B NH2   1 
ATOM   3401 N N     . ALA B 1 181 ? 57.376 -2.242  23.712  1.00 90.74  ?  181 ALA B N     1 
ATOM   3402 C CA    . ALA B 1 181 ? 56.554 -1.593  24.711  1.00 94.24  ?  181 ALA B CA    1 
ATOM   3403 C C     . ALA B 1 181 ? 57.550 -0.897  25.632  1.00 104.10 ?  181 ALA B C     1 
ATOM   3404 O O     . ALA B 1 181 ? 58.761 -0.996  25.381  1.00 97.85  ?  181 ALA B O     1 
ATOM   3405 C CB    . ALA B 1 181 ? 55.667 -2.608  25.435  1.00 97.06  ?  181 ALA B CB    1 
ATOM   3406 N N     . PRO B 1 182 ? 57.084 -0.183  26.710  1.00 110.60 ?  182 PRO B N     1 
ATOM   3407 C CA    . PRO B 1 182 ? 58.004 0.396   27.705  1.00 103.76 ?  182 PRO B CA    1 
ATOM   3408 C C     . PRO B 1 182 ? 59.236 -0.442  28.042  1.00 102.00 ?  182 PRO B C     1 
ATOM   3409 O O     . PRO B 1 182 ? 59.156 -1.614  28.435  1.00 103.68 ?  182 PRO B O     1 
ATOM   3410 C CB    . PRO B 1 182 ? 57.099 0.546   28.936  1.00 101.03 ?  182 PRO B CB    1 
ATOM   3411 C CG    . PRO B 1 182 ? 55.677 0.715   28.359  1.00 103.79 ?  182 PRO B CG    1 
ATOM   3412 C CD    . PRO B 1 182 ? 55.742 0.407   26.872  1.00 109.65 ?  182 PRO B CD    1 
ATOM   3413 N N     . LEU B 1 183 ? 60.384 0.549   27.996  1.00 105.26 ?  183 LEU B N     1 
ATOM   3414 C CA    . LEU B 1 183 ? 61.753 0.024   28.206  1.00 103.84 ?  183 LEU B CA    1 
ATOM   3415 C C     . LEU B 1 183 ? 61.939 -0.539  29.605  1.00 105.06 ?  183 LEU B C     1 
ATOM   3416 O O     . LEU B 1 183 ? 61.455 0.084   30.557  1.00 107.45 ?  183 LEU B O     1 
ATOM   3417 C CB    . LEU B 1 183 ? 62.732 1.178   27.976  1.00 107.44 ?  183 LEU B CB    1 
ATOM   3418 C CG    . LEU B 1 183 ? 62.782 1.732   26.553  1.00 103.62 ?  183 LEU B CG    1 
ATOM   3419 C CD1   . LEU B 1 183 ? 63.674 2.960   26.492  1.00 105.34 ?  183 LEU B CD1   1 
ATOM   3420 C CD2   . LEU B 1 183 ? 63.268 0.673   25.578  1.00 93.11  ?  183 LEU B CD2   1 
ATOM   3421 N N     . ALA B 1 184 ? 62.571 -1.931  29.626  1.00 106.78 ?  184 ALA B N     1 
ATOM   3422 C CA    . ALA B 1 184 ? 62.977 -2.257  30.986  1.00 109.40 ?  184 ALA B CA    1 
ATOM   3423 C C     . ALA B 1 184 ? 64.023 -1.252  31.453  1.00 107.59 ?  184 ALA B C     1 
ATOM   3424 O O     . ALA B 1 184 ? 65.017 -1.020  30.736  1.00 106.97 ?  184 ALA B O     1 
ATOM   3425 C CB    . ALA B 1 184 ? 63.544 -3.675  31.082  1.00 107.63 ?  184 ALA B CB    1 
ATOM   3426 N N     . PRO B 1 185 ? 63.827 -0.609  32.617  1.00 114.30 ?  185 PRO B N     1 
ATOM   3427 C CA    . PRO B 1 185 ? 64.840 0.345   33.103  1.00 111.85 ?  185 PRO B CA    1 
ATOM   3428 C C     . PRO B 1 185 ? 66.219 -0.284  33.300  1.00 116.93 ?  185 PRO B C     1 
ATOM   3429 O O     . PRO B 1 185 ? 67.226 0.402   33.062  1.00 114.03 ?  185 PRO B O     1 
ATOM   3430 C CB    . PRO B 1 185 ? 64.242 0.879   34.417  1.00 93.31  ?  185 PRO B CB    1 
ATOM   3431 C CG    . PRO B 1 185 ? 62.978 0.144   34.642  1.00 87.63  ?  185 PRO B CG    1 
ATOM   3432 C CD    . PRO B 1 185 ? 62.585 -0.567  33.413  1.00 106.29 ?  185 PRO B CD    1 
ATOM   3433 N N     . GLU B 1 186 ? 66.291 -1.588  33.632  1.00 112.95 ?  186 GLU B N     1 
ATOM   3434 C CA    . GLU B 1 186 ? 67.579 -2.250  33.837  1.00 116.07 ?  186 GLU B CA    1 
ATOM   3435 C C     . GLU B 1 186 ? 68.509 -2.078  32.636  1.00 120.97 ?  186 GLU B C     1 
ATOM   3436 O O     . GLU B 1 186 ? 69.742 -2.101  32.796  1.00 121.11 ?  186 GLU B O     1 
ATOM   3437 C CB    . GLU B 1 186 ? 67.355 -3.734  34.131  1.00 115.08 ?  186 GLU B CB    1 
ATOM   3438 N N     . GLY B 1 187 ? 67.946 -1.904  31.432  1.00 118.44 ?  187 GLY B N     1 
ATOM   3439 C CA    . GLY B 1 187 ? 68.754 -1.807  30.227  1.00 118.07 ?  187 GLY B CA    1 
ATOM   3440 C C     . GLY B 1 187 ? 68.715 -0.514  29.430  1.00 120.08 ?  187 GLY B C     1 
ATOM   3441 O O     . GLY B 1 187 ? 69.399 -0.449  28.402  1.00 118.04 ?  187 GLY B O     1 
ATOM   3442 N N     . ARG B 1 188 ? 67.970 0.522   29.859  1.00 121.94 ?  188 ARG B N     1 
ATOM   3443 C CA    . ARG B 1 188 ? 67.966 1.797   29.127  1.00 115.90 ?  188 ARG B CA    1 
ATOM   3444 C C     . ARG B 1 188 ? 69.364 2.334   28.906  1.00 115.67 ?  188 ARG B C     1 
ATOM   3445 O O     . ARG B 1 188 ? 69.565 3.224   28.070  1.00 109.79 ?  188 ARG B O     1 
ATOM   3446 C CB    . ARG B 1 188 ? 67.191 2.867   29.878  1.00 114.12 ?  188 ARG B CB    1 
ATOM   3447 C CG    . ARG B 1 188 ? 66.044 2.335   30.635  1.00 109.80 ?  188 ARG B CG    1 
ATOM   3448 C CD    . ARG B 1 188 ? 65.445 3.403   31.494  1.00 104.16 ?  188 ARG B CD    1 
ATOM   3449 N NE    . ARG B 1 188 ? 64.482 4.207   30.758  1.00 101.27 ?  188 ARG B NE    1 
ATOM   3450 C CZ    . ARG B 1 188 ? 64.682 5.467   30.421  1.00 99.34  ?  188 ARG B CZ    1 
ATOM   3451 N NH1   . ARG B 1 188 ? 65.819 6.084   30.715  1.00 97.54  ?  188 ARG B NH1   1 
ATOM   3452 N NH2   . ARG B 1 188 ? 63.710 6.128   29.796  1.00 102.47 ?  188 ARG B NH2   1 
ATOM   3453 N N     . ALA B 1 189 ? 70.314 1.834   29.681  1.00 116.80 ?  189 ALA B N     1 
ATOM   3454 C CA    . ALA B 1 189 ? 71.713 2.168   29.549  1.00 117.61 ?  189 ALA B CA    1 
ATOM   3455 C C     . ALA B 1 189 ? 72.245 1.766   28.193  1.00 112.76 ?  189 ALA B C     1 
ATOM   3456 O O     . ALA B 1 189 ? 72.546 2.630   27.361  1.00 112.67 ?  189 ALA B O     1 
ATOM   3457 C CB    . ALA B 1 189 ? 72.510 1.455   30.637  1.00 119.30 ?  189 ALA B CB    1 
ATOM   3458 N N     . ALA B 1 190 ? 72.319 0.450   27.960  1.00 114.59 ?  190 ALA B N     1 
ATOM   3459 C CA    . ALA B 1 190 ? 72.987 -0.067  26.766  1.00 112.20 ?  190 ALA B CA    1 
ATOM   3460 C C     . ALA B 1 190 ? 72.341 0.453   25.488  1.00 110.06 ?  190 ALA B C     1 
ATOM   3461 O O     . ALA B 1 190 ? 73.023 0.652   24.474  1.00 102.29 ?  190 ALA B O     1 
ATOM   3462 C CB    . ALA B 1 190 ? 72.988 -1.594  26.777  1.00 112.40 ?  190 ALA B CB    1 
ATOM   3463 N N     . VAL B 1 191 ? 71.023 0.671   25.513  1.00 111.16 ?  191 VAL B N     1 
ATOM   3464 C CA    . VAL B 1 191 ? 70.363 1.276   24.362  1.00 103.24 ?  191 VAL B CA    1 
ATOM   3465 C C     . VAL B 1 191 ? 70.706 2.766   24.258  1.00 102.40 ?  191 VAL B C     1 
ATOM   3466 O O     . VAL B 1 191 ? 70.954 3.273   23.156  1.00 105.54 ?  191 VAL B O     1 
ATOM   3467 C CB    . VAL B 1 191 ? 68.841 1.010   24.397  1.00 102.19 ?  191 VAL B CB    1 
ATOM   3468 C CG1   . VAL B 1 191 ? 68.563 -0.479  24.479  1.00 97.14  ?  191 VAL B CG1   1 
ATOM   3469 C CG2   . VAL B 1 191 ? 68.201 1.662   25.554  1.00 113.51 ?  191 VAL B CG2   1 
ATOM   3470 N N     . GLN B 1 192 ? 70.749 3.490   25.391  1.00 109.19 ?  192 GLN B N     1 
ATOM   3471 C CA    . GLN B 1 192 ? 71.195 4.888   25.356  1.00 105.85 ?  192 GLN B CA    1 
ATOM   3472 C C     . GLN B 1 192 ? 72.593 5.014   24.762  1.00 102.53 ?  192 GLN B C     1 
ATOM   3473 O O     . GLN B 1 192 ? 72.914 6.057   24.179  1.00 99.43  ?  192 GLN B O     1 
ATOM   3474 C CB    . GLN B 1 192 ? 71.178 5.507   26.760  1.00 109.10 ?  192 GLN B CB    1 
ATOM   3475 N N     . ARG B 1 193 ? 73.426 3.961   24.912  1.00 104.85 ?  193 ARG B N     1 
ATOM   3476 C CA    . ARG B 1 193 ? 74.827 3.932   24.467  1.00 100.57 ?  193 ARG B CA    1 
ATOM   3477 C C     . ARG B 1 193 ? 74.954 3.573   22.990  1.00 101.22 ?  193 ARG B C     1 
ATOM   3478 O O     . ARG B 1 193 ? 75.719 4.207   22.258  1.00 96.36  ?  193 ARG B O     1 
ATOM   3479 C CB    . ARG B 1 193 ? 75.643 2.935   25.303  1.00 87.96  ?  193 ARG B CB    1 
ATOM   3480 N N     . TYR B 1 194 ? 74.261 2.514   22.560  1.00 103.08 ?  194 TYR B N     1 
ATOM   3481 C CA    . TYR B 1 194 ? 74.171 2.163   21.143  1.00 97.41  ?  194 TYR B CA    1 
ATOM   3482 C C     . TYR B 1 194 ? 73.570 3.298   20.336  1.00 98.98  ?  194 TYR B C     1 
ATOM   3483 O O     . TYR B 1 194 ? 74.162 3.776   19.363  1.00 94.14  ?  194 TYR B O     1 
ATOM   3484 C CB    . TYR B 1 194 ? 73.308 0.917   20.994  1.00 93.21  ?  194 TYR B CB    1 
ATOM   3485 C CG    . TYR B 1 194 ? 73.493 0.094   19.735  1.00 94.92  ?  194 TYR B CG    1 
ATOM   3486 C CD1   . TYR B 1 194 ? 74.756 -0.311  19.321  1.00 100.05 ?  194 TYR B CD1   1 
ATOM   3487 C CD2   . TYR B 1 194 ? 72.390 -0.353  19.001  1.00 91.45  ?  194 TYR B CD2   1 
ATOM   3488 C CE1   . TYR B 1 194 ? 74.919 -1.111  18.202  1.00 95.40  ?  194 TYR B CE1   1 
ATOM   3489 C CE2   . TYR B 1 194 ? 72.544 -1.155  17.883  1.00 88.22  ?  194 TYR B CE2   1 
ATOM   3490 C CZ    . TYR B 1 194 ? 73.807 -1.524  17.505  1.00 94.12  ?  194 TYR B CZ    1 
ATOM   3491 O OH    . TYR B 1 194 ? 73.983 -2.313  16.419  1.00 99.50  ?  194 TYR B OH    1 
ATOM   3492 N N     . LEU B 1 195 ? 72.383 3.739   20.757  1.00 97.98  ?  195 LEU B N     1 
ATOM   3493 C CA    . LEU B 1 195 ? 71.649 4.779   20.045  1.00 95.80  ?  195 LEU B CA    1 
ATOM   3494 C C     . LEU B 1 195 ? 72.488 6.040   19.880  1.00 97.56  ?  195 LEU B C     1 
ATOM   3495 O O     . LEU B 1 195 ? 72.530 6.636   18.796  1.00 99.54  ?  195 LEU B O     1 
ATOM   3496 C CB    . LEU B 1 195 ? 70.346 5.105   20.789  1.00 94.97  ?  195 LEU B CB    1 
ATOM   3497 C CG    . LEU B 1 195 ? 68.997 4.484   20.427  1.00 92.87  ?  195 LEU B CG    1 
ATOM   3498 C CD1   . LEU B 1 195 ? 67.869 5.235   21.129  1.00 86.31  ?  195 LEU B CD1   1 
ATOM   3499 C CD2   . LEU B 1 195 ? 68.773 4.511   18.925  1.00 92.06  ?  195 LEU B CD2   1 
ATOM   3500 N N     . HIS B 1 196 ? 73.165 6.457   20.949  1.00 101.80 ?  196 HIS B N     1 
ATOM   3501 C CA    . HIS B 1 196 ? 74.029 7.626   20.860  1.00 103.11 ?  196 HIS B CA    1 
ATOM   3502 C C     . HIS B 1 196 ? 75.271 7.308   20.054  1.00 100.92 ?  196 HIS B C     1 
ATOM   3503 O O     . HIS B 1 196 ? 75.547 7.965   19.045  1.00 100.77 ?  196 HIS B O     1 
ATOM   3504 C CB    . HIS B 1 196 ? 74.396 8.150   22.260  1.00 107.44 ?  196 HIS B CB    1 
ATOM   3505 C CG    . HIS B 1 196 ? 75.346 9.319   22.247  1.00 112.80 ?  196 HIS B CG    1 
ATOM   3506 N ND1   . HIS B 1 196 ? 76.707 9.178   22.438  1.00 111.90 ?  196 HIS B ND1   1 
ATOM   3507 C CD2   . HIS B 1 196 ? 75.126 10.649  22.080  1.00 114.11 ?  196 HIS B CD2   1 
ATOM   3508 C CE1   . HIS B 1 196 ? 77.283 10.367  22.381  1.00 114.22 ?  196 HIS B CE1   1 
ATOM   3509 N NE2   . HIS B 1 196 ? 76.348 11.277  22.164  1.00 119.92 ?  196 HIS B NE2   1 
ATOM   3510 N N     . ASP B 1 197 ? 76.002 6.265   20.446  1.00 104.02 ?  197 ASP B N     1 
ATOM   3511 C CA    . ASP B 1 197 ? 77.320 6.071   19.862  1.00 104.41 ?  197 ASP B CA    1 
ATOM   3512 C C     . ASP B 1 197 ? 77.274 5.784   18.381  1.00 99.33  ?  197 ASP B C     1 
ATOM   3513 O O     . ASP B 1 197 ? 78.325 5.840   17.738  1.00 100.01 ?  197 ASP B O     1 
ATOM   3514 C CB    . ASP B 1 197 ? 78.086 4.937   20.527  1.00 107.63 ?  197 ASP B CB    1 
ATOM   3515 C CG    . ASP B 1 197 ? 78.516 5.286   21.893  1.00 107.58 ?  197 ASP B CG    1 
ATOM   3516 O OD1   . ASP B 1 197 ? 77.863 6.169   22.489  1.00 106.48 ?  197 ASP B OD1   1 
ATOM   3517 O OD2   . ASP B 1 197 ? 79.510 4.695   22.353  1.00 114.63 -1 197 ASP B OD2   1 
ATOM   3518 N N     . PHE B 1 198 ? 76.110 5.465   17.818  1.00 97.38  ?  198 PHE B N     1 
ATOM   3519 C CA    . PHE B 1 198 ? 76.070 5.332   16.370  1.00 96.61  ?  198 PHE B CA    1 
ATOM   3520 C C     . PHE B 1 198 ? 75.016 6.218   15.744  1.00 94.38  ?  198 PHE B C     1 
ATOM   3521 O O     . PHE B 1 198 ? 74.558 5.928   14.642  1.00 88.25  ?  198 PHE B O     1 
ATOM   3522 C CB    . PHE B 1 198 ? 75.868 3.891   15.950  1.00 93.56  ?  198 PHE B CB    1 
ATOM   3523 C CG    . PHE B 1 198 ? 76.945 2.980   16.420  1.00 100.18 ?  198 PHE B CG    1 
ATOM   3524 C CD1   . PHE B 1 198 ? 78.153 2.939   15.751  1.00 100.16 ?  198 PHE B CD1   1 
ATOM   3525 C CD2   . PHE B 1 198 ? 76.764 2.174   17.537  1.00 104.81 ?  198 PHE B CD2   1 
ATOM   3526 C CE1   . PHE B 1 198 ? 79.161 2.107   16.158  1.00 111.93 ?  198 PHE B CE1   1 
ATOM   3527 C CE2   . PHE B 1 198 ? 77.777 1.328   17.956  1.00 110.99 ?  198 PHE B CE2   1 
ATOM   3528 C CZ    . PHE B 1 198 ? 78.978 1.298   17.261  1.00 116.26 ?  198 PHE B CZ    1 
ATOM   3529 N N     . MET B 1 199 ? 74.628 7.286   16.431  1.00 93.19  ?  199 MET B N     1 
ATOM   3530 C CA    . MET B 1 199 ? 73.818 8.338   15.843  1.00 92.67  ?  199 MET B CA    1 
ATOM   3531 C C     . MET B 1 199 ? 72.511 7.773   15.288  1.00 91.35  ?  199 MET B C     1 
ATOM   3532 O O     . MET B 1 199 ? 72.266 7.816   14.086  1.00 82.38  ?  199 MET B O     1 
ATOM   3533 C CB    . MET B 1 199 ? 74.602 9.072   14.741  1.00 84.99  ?  199 MET B CB    1 
ATOM   3534 C CG    . MET B 1 199 ? 76.101 9.306   15.016  1.00 80.00  ?  199 MET B CG    1 
ATOM   3535 S SD    . MET B 1 199 ? 76.702 10.739  14.056  1.00 80.65  ?  199 MET B SD    1 
ATOM   3536 C CE    . MET B 1 199 ? 78.472 10.710  14.353  1.00 84.44  ?  199 MET B CE    1 
ATOM   3537 N N     . MET B 1 200 ? 71.673 7.224   16.178  1.00 92.57  ?  200 MET B N     1 
ATOM   3538 C CA    . MET B 1 200 ? 70.437 6.563   15.751  1.00 85.99  ?  200 MET B CA    1 
ATOM   3539 C C     . MET B 1 200 ? 69.226 7.056   16.543  1.00 89.78  ?  200 MET B C     1 
ATOM   3540 O O     . MET B 1 200 ? 69.330 7.903   17.430  1.00 98.51  ?  200 MET B O     1 
ATOM   3541 C CB    . MET B 1 200 ? 70.550 5.048   15.897  1.00 84.02  ?  200 MET B CB    1 
ATOM   3542 C CG    . MET B 1 200 ? 71.775 4.443   15.276  1.00 83.98  ?  200 MET B CG    1 
ATOM   3543 S SD    . MET B 1 200 ? 71.604 2.698   15.577  1.00 92.26  ?  200 MET B SD    1 
ATOM   3544 C CE    . MET B 1 200 ? 73.224 2.171   16.011  1.00 95.30  ?  200 MET B CE    1 
ATOM   3545 N N     . THR B 1 201 ? 68.063 6.485   16.234  1.00 89.92  ?  201 THR B N     1 
ATOM   3546 C CA    . THR B 1 201 ? 66.800 6.927   16.821  1.00 89.77  ?  201 THR B CA    1 
ATOM   3547 C C     . THR B 1 201 ? 65.768 5.804   16.690  1.00 88.33  ?  201 THR B C     1 
ATOM   3548 O O     . THR B 1 201 ? 65.581 5.264   15.595  1.00 88.36  ?  201 THR B O     1 
ATOM   3549 C CB    . THR B 1 201 ? 66.318 8.253   16.153  1.00 89.58  ?  201 THR B CB    1 
ATOM   3550 O OG1   . THR B 1 201 ? 64.942 8.521   16.462  1.00 90.07  ?  201 THR B OG1   1 
ATOM   3551 C CG2   . THR B 1 201 ? 66.505 8.248   14.623  1.00 89.58  ?  201 THR B CG2   1 
ATOM   3552 N N     . MET B 1 202 ? 65.125 5.435   17.808  1.00 88.56  ?  202 MET B N     1 
ATOM   3553 C CA    . MET B 1 202 ? 64.015 4.481   17.818  1.00 84.45  ?  202 MET B CA    1 
ATOM   3554 C C     . MET B 1 202 ? 62.709 5.173   17.463  1.00 84.33  ?  202 MET B C     1 
ATOM   3555 O O     . MET B 1 202 ? 62.611 6.398   17.466  1.00 89.48  ?  202 MET B O     1 
ATOM   3556 C CB    . MET B 1 202 ? 63.865 3.819   19.185  1.00 87.69  ?  202 MET B CB    1 
ATOM   3557 C CG    . MET B 1 202 ? 65.110 3.133   19.672  1.00 88.34  ?  202 MET B CG    1 
ATOM   3558 S SD    . MET B 1 202 ? 64.776 2.357   21.249  1.00 102.77 ?  202 MET B SD    1 
ATOM   3559 C CE    . MET B 1 202 ? 66.425 2.114   21.942  1.00 96.19  ?  202 MET B CE    1 
ATOM   3560 N N     . VAL B 1 203 ? 61.691 4.435   17.230  1.00 76.47  ?  203 VAL B N     1 
ATOM   3561 C CA    . VAL B 1 203 ? 60.397 5.039   16.823  1.00 82.00  ?  203 VAL B CA    1 
ATOM   3562 C C     . VAL B 1 203 ? 59.249 4.231   17.430  1.00 83.57  ?  203 VAL B C     1 
ATOM   3563 O O     . VAL B 1 203 ? 59.507 3.131   17.927  1.00 85.41  ?  203 VAL B O     1 
ATOM   3564 C CB    . VAL B 1 203 ? 60.322 5.097   15.286  1.00 77.28  ?  203 VAL B CB    1 
ATOM   3565 C CG1   . VAL B 1 203 ? 59.974 3.751   14.673  1.00 76.74  ?  203 VAL B CG1   1 
ATOM   3566 C CG2   . VAL B 1 203 ? 59.384 6.184   14.789  1.00 77.64  ?  203 VAL B CG2   1 
ATOM   3567 N N     . SER B 1 204 ? 58.059 4.746   17.421  1.00 82.86  ?  204 SER B N     1 
ATOM   3568 C CA    . SER B 1 204 ? 56.867 4.107   17.939  1.00 84.28  ?  204 SER B CA    1 
ATOM   3569 C C     . SER B 1 204 ? 56.171 3.380   16.801  1.00 80.86  ?  204 SER B C     1 
ATOM   3570 O O     . SER B 1 204 ? 56.035 3.908   15.698  1.00 77.98  ?  204 SER B O     1 
ATOM   3571 C CB    . SER B 1 204 ? 55.918 5.132   18.564  1.00 87.39  ?  204 SER B CB    1 
ATOM   3572 O OG    . SER B 1 204 ? 55.058 5.696   17.574  1.00 88.25  ?  204 SER B OG    1 
ATOM   3573 N N     . ALA B 1 205 ? 55.740 2.149   17.057  1.00 80.94  ?  205 ALA B N     1 
ATOM   3574 C CA    . ALA B 1 205 ? 55.093 1.355   15.995  1.00 73.10  ?  205 ALA B CA    1 
ATOM   3575 C C     . ALA B 1 205 ? 53.886 2.123   15.476  1.00 75.11  ?  205 ALA B C     1 
ATOM   3576 O O     . ALA B 1 205 ? 53.547 1.958   14.299  1.00 81.79  ?  205 ALA B O     1 
ATOM   3577 C CB    . ALA B 1 205 ? 54.687 0.026   16.555  1.00 58.55  ?  205 ALA B CB    1 
ATOM   3578 N N     . GLU B 1 206 ? 53.284 2.950   16.324  1.00 72.92  ?  206 GLU B N     1 
ATOM   3579 C CA    . GLU B 1 206 ? 52.048 3.674   15.936  1.00 72.93  ?  206 GLU B CA    1 
ATOM   3580 C C     . GLU B 1 206 ? 52.416 4.960   15.200  1.00 75.17  ?  206 GLU B C     1 
ATOM   3581 O O     . GLU B 1 206 ? 51.511 5.735   14.876  1.00 76.70  ?  206 GLU B O     1 
ATOM   3582 C CB    . GLU B 1 206 ? 51.218 3.967   17.185  1.00 76.80  ?  206 GLU B CB    1 
ATOM   3583 C CG    . GLU B 1 206 ? 52.003 4.645   18.289  1.00 82.52  ?  206 GLU B CG    1 
ATOM   3584 C CD    . GLU B 1 206 ? 52.646 3.706   19.293  1.00 85.42  ?  206 GLU B CD    1 
ATOM   3585 O OE1   . GLU B 1 206 ? 52.808 2.517   18.971  1.00 80.50  ?  206 GLU B OE1   1 
ATOM   3586 O OE2   . GLU B 1 206 ? 52.987 4.169   20.395  1.00 93.94  -1 206 GLU B OE2   1 
ATOM   3587 N N     . ALA B 1 207 ? 53.702 5.166   14.945  1.00 72.33  ?  207 ALA B N     1 
ATOM   3588 C CA    . ALA B 1 207 ? 54.131 6.366   14.204  1.00 70.46  ?  207 ALA B CA    1 
ATOM   3589 C C     . ALA B 1 207 ? 54.054 6.099   12.709  1.00 75.29  ?  207 ALA B C     1 
ATOM   3590 O O     . ALA B 1 207 ? 53.516 6.955   12.000  1.00 74.04  ?  207 ALA B O     1 
ATOM   3591 C CB    . ALA B 1 207 ? 55.540 6.707   14.578  1.00 65.84  ?  207 ALA B CB    1 
ATOM   3592 N N     . TYR B 1 208 ? 54.552 4.948   12.269  1.00 70.22  ?  208 TYR B N     1 
ATOM   3593 C CA    . TYR B 1 208 ? 54.643 4.663   10.814  1.00 67.98  ?  208 TYR B CA    1 
ATOM   3594 C C     . TYR B 1 208 ? 53.322 4.893   10.075  1.00 68.79  ?  208 TYR B C     1 
ATOM   3595 O O     . TYR B 1 208 ? 53.371 5.512   9.016   1.00 67.29  ?  208 TYR B O     1 
ATOM   3596 C CB    . TYR B 1 208 ? 55.250 3.279   10.597  1.00 69.12  ?  208 TYR B CB    1 
ATOM   3597 C CG    . TYR B 1 208 ? 56.727 3.333   10.318  1.00 74.53  ?  208 TYR B CG    1 
ATOM   3598 C CD1   . TYR B 1 208 ? 57.212 4.038   9.233   1.00 71.54  ?  208 TYR B CD1   1 
ATOM   3599 C CD2   . TYR B 1 208 ? 57.637 2.709   11.152  1.00 71.76  ?  208 TYR B CD2   1 
ATOM   3600 C CE1   . TYR B 1 208 ? 58.567 4.107   8.966   1.00 71.69  ?  208 TYR B CE1   1 
ATOM   3601 C CE2   . TYR B 1 208 ? 58.996 2.767   10.901  1.00 73.54  ?  208 TYR B CE2   1 
ATOM   3602 C CZ    . TYR B 1 208 ? 59.461 3.470   9.805   1.00 77.08  ?  208 TYR B CZ    1 
ATOM   3603 O OH    . TYR B 1 208 ? 60.800 3.539   9.543   1.00 80.42  ?  208 TYR B OH    1 
ATOM   3604 N N     . PRO B 1 209 ? 52.149 4.400   10.508  1.00 69.64  ?  209 PRO B N     1 
ATOM   3605 C CA    . PRO B 1 209 ? 50.939 4.617   9.710   1.00 69.17  ?  209 PRO B CA    1 
ATOM   3606 C C     . PRO B 1 209 ? 50.740 6.097   9.328   1.00 69.31  ?  209 PRO B C     1 
ATOM   3607 O O     . PRO B 1 209 ? 50.713 6.355   8.147   1.00 71.34  ?  209 PRO B O     1 
ATOM   3608 C CB    . PRO B 1 209 ? 49.830 3.988   10.568  1.00 71.42  ?  209 PRO B CB    1 
ATOM   3609 C CG    . PRO B 1 209 ? 50.549 2.947   11.393  1.00 72.27  ?  209 PRO B CG    1 
ATOM   3610 C CD    . PRO B 1 209 ? 51.907 3.550   11.677  1.00 72.27  ?  209 PRO B CD    1 
ATOM   3611 N N     . PRO B 1 210 ? 50.597 7.076   10.253  1.00 72.14  ?  210 PRO B N     1 
ATOM   3612 C CA    . PRO B 1 210 ? 50.487 8.483   9.863   1.00 67.97  ?  210 PRO B CA    1 
ATOM   3613 C C     . PRO B 1 210 ? 51.759 8.914   9.137   1.00 70.17  ?  210 PRO B C     1 
ATOM   3614 O O     . PRO B 1 210 ? 51.687 9.699   8.221   1.00 68.17  ?  210 PRO B O     1 
ATOM   3615 C CB    . PRO B 1 210 ? 50.409 9.219   11.198  1.00 63.37  ?  210 PRO B CB    1 
ATOM   3616 C CG    . PRO B 1 210 ? 49.861 8.208   12.161  1.00 69.09  ?  210 PRO B CG    1 
ATOM   3617 C CD    . PRO B 1 210 ? 50.488 6.913   11.706  1.00 74.29  ?  210 PRO B CD    1 
ATOM   3618 N N     . LEU B 1 211 ? 52.886 8.378   9.577   1.00 67.84  ?  211 LEU B N     1 
ATOM   3619 C CA    . LEU B 1 211 ? 54.170 8.690   8.965   1.00 65.65  ?  211 LEU B CA    1 
ATOM   3620 C C     . LEU B 1 211 ? 54.185 8.375   7.487   1.00 69.12  ?  211 LEU B C     1 
ATOM   3621 O O     . LEU B 1 211 ? 54.620 9.193   6.673   1.00 72.37  ?  211 LEU B O     1 
ATOM   3622 C CB    . LEU B 1 211 ? 55.254 7.898   9.656   1.00 68.19  ?  211 LEU B CB    1 
ATOM   3623 C CG    . LEU B 1 211 ? 56.048 8.840   10.501  1.00 65.44  ?  211 LEU B CG    1 
ATOM   3624 C CD1   . LEU B 1 211 ? 57.095 8.078   11.254  1.00 65.15  ?  211 LEU B CD1   1 
ATOM   3625 C CD2   . LEU B 1 211 ? 56.644 9.816   9.543   1.00 69.15  ?  211 LEU B CD2   1 
ATOM   3626 N N     . LEU B 1 212 ? 53.763 7.170   7.120   1.00 67.19  ?  212 LEU B N     1 
ATOM   3627 C CA    . LEU B 1 212 ? 53.742 6.837   5.705   1.00 66.06  ?  212 LEU B CA    1 
ATOM   3628 C C     . LEU B 1 212 ? 52.624 7.578   4.992   1.00 69.00  ?  212 LEU B C     1 
ATOM   3629 O O     . LEU B 1 212 ? 52.818 8.056   3.876   1.00 72.17  ?  212 LEU B O     1 
ATOM   3630 C CB    . LEU B 1 212 ? 53.625 5.325   5.520   1.00 66.83  ?  212 LEU B CB    1 
ATOM   3631 C CG    . LEU B 1 212 ? 54.831 4.589   6.124   1.00 67.03  ?  212 LEU B CG    1 
ATOM   3632 C CD1   . LEU B 1 212 ? 54.474 3.198   6.607   1.00 65.20  ?  212 LEU B CD1   1 
ATOM   3633 C CD2   . LEU B 1 212 ? 55.959 4.510   5.125   1.00 63.05  ?  212 LEU B CD2   1 
ATOM   3634 N N     . ARG B 1 213 ? 51.491 7.701   5.463   1.00 67.83  ?  213 ARG B N     1 
ATOM   3635 C CA    . ARG B 1 213 ? 50.414 8.435   4.758   1.00 68.23  ?  213 ARG B CA    1 
ATOM   3636 C C     . ARG B 1 213 ? 50.919 9.842   4.452   1.00 71.52  ?  213 ARG B C     1 
ATOM   3637 O O     . ARG B 1 213 ? 50.586 10.365  3.380   1.00 76.18  ?  213 ARG B O     1 
ATOM   3638 C CB    . ARG B 1 213 ? 49.145 8.453   5.611   1.00 67.05  ?  213 ARG B CB    1 
ATOM   3639 C CG    . ARG B 1 213 ? 48.436 7.110   5.695   1.00 72.71  ?  213 ARG B CG    1 
ATOM   3640 C CD    . ARG B 1 213 ? 47.124 7.209   6.446   1.00 72.58  ?  213 ARG B CD    1 
ATOM   3641 N NE    . ARG B 1 213 ? 47.221 8.065   7.617   1.00 67.62  ?  213 ARG B NE    1 
ATOM   3642 C CZ    . ARG B 1 213 ? 47.140 7.636   8.869   1.00 68.98  ?  213 ARG B CZ    1 
ATOM   3643 N NH1   . ARG B 1 213 ? 47.352 6.363   9.147   1.00 76.86  ?  213 ARG B NH1   1 
ATOM   3644 N NH2   . ARG B 1 213 ? 46.847 8.482   9.841   1.00 76.21  ?  213 ARG B NH2   1 
ATOM   3645 N N     . GLY B 1 214 ? 51.683 10.454  5.478   1.00 68.68  ?  214 GLY B N     1 
ATOM   3646 C CA    . GLY B 1 214 ? 52.251 11.749  5.139   1.00 65.76  ?  214 GLY B CA    1 
ATOM   3647 C C     . GLY B 1 214 ? 53.104 11.715  3.881   1.00 75.34  ?  214 GLY B C     1 
ATOM   3648 O O     . GLY B 1 214 ? 52.951 12.556  2.990   1.00 79.92  ?  214 GLY B O     1 
ATOM   3649 N N     . ALA B 1 215 ? 53.989 10.726  3.773   1.00 76.66  ?  215 ALA B N     1 
ATOM   3650 C CA    . ALA B 1 215 ? 54.840 10.546  2.597   1.00 72.05  ?  215 ALA B CA    1 
ATOM   3651 C C     . ALA B 1 215 ? 54.074 10.152  1.332   1.00 69.26  ?  215 ALA B C     1 
ATOM   3652 O O     . ALA B 1 215 ? 54.690 10.052  0.263   1.00 69.11  ?  215 ALA B O     1 
ATOM   3653 C CB    . ALA B 1 215 ? 55.874 9.473   2.902   1.00 71.99  ?  215 ALA B CB    1 
ATOM   3654 N N     . GLY B 1 216 ? 52.768 9.901   1.419   1.00 69.13  ?  216 GLY B N     1 
ATOM   3655 C CA    . GLY B 1 216 ? 52.025 9.440   0.261   1.00 73.71  ?  216 GLY B CA    1 
ATOM   3656 C C     . GLY B 1 216 ? 52.070 7.943   0.002   1.00 72.78  ?  216 GLY B C     1 
ATOM   3657 O O     . GLY B 1 216 ? 51.885 7.527   -1.155  1.00 71.47  ?  216 GLY B O     1 
ATOM   3658 N N     . LEU B 1 217 ? 52.314 7.122   1.049   1.00 67.92  ?  217 LEU B N     1 
ATOM   3659 C CA    . LEU B 1 217 ? 52.392 5.661   0.987   1.00 64.61  ?  217 LEU B CA    1 
ATOM   3660 C C     . LEU B 1 217 ? 51.463 5.027   2.013   1.00 68.30  ?  217 LEU B C     1 
ATOM   3661 O O     . LEU B 1 217 ? 51.301 5.548   3.117   1.00 72.02  ?  217 LEU B O     1 
ATOM   3662 C CB    . LEU B 1 217 ? 53.791 5.152   1.287   1.00 65.60  ?  217 LEU B CB    1 
ATOM   3663 C CG    . LEU B 1 217 ? 54.925 5.973   0.714   1.00 70.00  ?  217 LEU B CG    1 
ATOM   3664 C CD1   . LEU B 1 217 ? 56.181 5.473   1.363   1.00 70.74  ?  217 LEU B CD1   1 
ATOM   3665 C CD2   . LEU B 1 217 ? 54.983 5.838   -0.798  1.00 67.11  ?  217 LEU B CD2   1 
ATOM   3666 N N     . TRP B 1 218 ? 50.896 3.865   1.666   1.00 70.55  ?  218 TRP B N     1 
ATOM   3667 C CA    . TRP B 1 218 ? 50.060 3.075   2.572   1.00 68.67  ?  218 TRP B CA    1 
ATOM   3668 C C     . TRP B 1 218 ? 50.879 1.965   3.218   1.00 66.10  ?  218 TRP B C     1 
ATOM   3669 O O     . TRP B 1 218 ? 51.584 1.232   2.519   1.00 65.30  ?  218 TRP B O     1 
ATOM   3670 C CB    . TRP B 1 218 ? 48.876 2.464   1.819   1.00 67.88  ?  218 TRP B CB    1 
ATOM   3671 C CG    . TRP B 1 218 ? 47.880 3.491   1.362   1.00 77.15  ?  218 TRP B CG    1 
ATOM   3672 C CD1   . TRP B 1 218 ? 47.922 4.830   1.611   1.00 78.28  ?  218 TRP B CD1   1 
ATOM   3673 C CD2   . TRP B 1 218 ? 46.689 3.269   0.586   1.00 75.52  ?  218 TRP B CD2   1 
ATOM   3674 N NE1   . TRP B 1 218 ? 46.842 5.454   1.039   1.00 77.91  ?  218 TRP B NE1   1 
ATOM   3675 C CE2   . TRP B 1 218 ? 46.072 4.521   0.401   1.00 75.52  ?  218 TRP B CE2   1 
ATOM   3676 C CE3   . TRP B 1 218 ? 46.095 2.137   0.025   1.00 71.01  ?  218 TRP B CE3   1 
ATOM   3677 C CZ2   . TRP B 1 218 ? 44.887 4.675   -0.318  1.00 76.86  ?  218 TRP B CZ2   1 
ATOM   3678 C CZ3   . TRP B 1 218 ? 44.916 2.296   -0.694  1.00 74.30  ?  218 TRP B CZ3   1 
ATOM   3679 C CH2   . TRP B 1 218 ? 44.327 3.555   -0.856  1.00 77.45  ?  218 TRP B CH2   1 
ATOM   3680 N N     . LEU B 1 219 ? 50.788 1.832   4.543   1.00 64.87  ?  219 LEU B N     1 
ATOM   3681 C CA    . LEU B 1 219 ? 51.412 0.677   5.173   1.00 65.81  ?  219 LEU B CA    1 
ATOM   3682 C C     . LEU B 1 219 ? 50.840 -0.593  4.562   1.00 65.31  ?  219 LEU B C     1 
ATOM   3683 O O     . LEU B 1 219 ? 49.661 -0.662  4.198   1.00 64.66  ?  219 LEU B O     1 
ATOM   3684 C CB    . LEU B 1 219 ? 51.192 0.663   6.682   1.00 60.86  ?  219 LEU B CB    1 
ATOM   3685 C CG    . LEU B 1 219 ? 51.741 -0.607  7.347   1.00 58.94  ?  219 LEU B CG    1 
ATOM   3686 C CD1   . LEU B 1 219 ? 53.221 -0.701  7.099   1.00 65.18  ?  219 LEU B CD1   1 
ATOM   3687 C CD2   . LEU B 1 219 ? 51.436 -0.656  8.826   1.00 59.22  ?  219 LEU B CD2   1 
ATOM   3688 N N     . GLU B 1 220 ? 51.692 -1.576  4.390   1.00 62.98  ?  220 GLU B N     1 
ATOM   3689 C CA    . GLU B 1 220 ? 51.255 -2.862  3.892   1.00 68.65  ?  220 GLU B CA    1 
ATOM   3690 C C     . GLU B 1 220 ? 51.541 -3.986  4.858   1.00 63.81  ?  220 GLU B C     1 
ATOM   3691 O O     . GLU B 1 220 ? 50.751 -4.923  4.945   1.00 59.91  ?  220 GLU B O     1 
ATOM   3692 C CB    . GLU B 1 220 ? 51.951 -3.166  2.566   1.00 65.44  ?  220 GLU B CB    1 
ATOM   3693 C CG    . GLU B 1 220 ? 51.338 -4.298  1.809   1.00 63.98  ?  220 GLU B CG    1 
ATOM   3694 C CD    . GLU B 1 220 ? 52.191 -4.695  0.617   1.00 76.92  ?  220 GLU B CD    1 
ATOM   3695 O OE1   . GLU B 1 220 ? 53.281 -5.285  0.820   1.00 83.92  ?  220 GLU B OE1   1 
ATOM   3696 O OE2   . GLU B 1 220 ? 51.777 -4.397  -0.530  1.00 73.76  -1 220 GLU B OE2   1 
ATOM   3697 N N     . GLU B 1 221 ? 52.633 -3.900  5.600   1.00 65.17  ?  221 GLU B N     1 
ATOM   3698 C CA    . GLU B 1 221 ? 53.098 -5.026  6.398   1.00 65.93  ?  221 GLU B CA    1 
ATOM   3699 C C     . GLU B 1 221 ? 54.048 -4.464  7.447   1.00 65.09  ?  221 GLU B C     1 
ATOM   3700 O O     . GLU B 1 221 ? 55.101 -3.914  7.099   1.00 65.10  ?  221 GLU B O     1 
ATOM   3701 C CB    . GLU B 1 221 ? 53.793 -6.077  5.517   1.00 67.06  ?  221 GLU B CB    1 
ATOM   3702 C CG    . GLU B 1 221 ? 54.145 -7.409  6.243   1.00 68.05  ?  221 GLU B CG    1 
ATOM   3703 C CD    . GLU B 1 221 ? 55.397 -8.157  5.706   1.00 67.11  ?  221 GLU B CD    1 
ATOM   3704 O OE1   . GLU B 1 221 ? 56.002 -7.716  4.699   1.00 65.82  ?  221 GLU B OE1   1 
ATOM   3705 O OE2   . GLU B 1 221 ? 55.773 -9.202  6.307   1.00 73.10  -1 221 GLU B OE2   1 
ATOM   3706 N N     . PHE B 1 222 ? 53.668 -4.568  8.708   1.00 65.42  ?  222 PHE B N     1 
ATOM   3707 C CA    . PHE B 1 222 ? 54.615 -4.387  9.789   1.00 64.25  ?  222 PHE B CA    1 
ATOM   3708 C C     . PHE B 1 222 ? 54.929 -5.753  10.371  1.00 69.88  ?  222 PHE B C     1 
ATOM   3709 O O     . PHE B 1 222 ? 54.022 -6.562  10.604  1.00 64.56  ?  222 PHE B O     1 
ATOM   3710 C CB    . PHE B 1 222 ? 54.056 -3.472  10.875  1.00 65.68  ?  222 PHE B CB    1 
ATOM   3711 C CG    . PHE B 1 222 ? 54.968 -3.317  12.059  1.00 66.50  ?  222 PHE B CG    1 
ATOM   3712 C CD1   . PHE B 1 222 ? 54.975 -4.255  13.079  1.00 65.05  ?  222 PHE B CD1   1 
ATOM   3713 C CD2   . PHE B 1 222 ? 55.813 -2.227  12.152  1.00 70.02  ?  222 PHE B CD2   1 
ATOM   3714 C CE1   . PHE B 1 222 ? 55.817 -4.121  14.165  1.00 70.59  ?  222 PHE B CE1   1 
ATOM   3715 C CE2   . PHE B 1 222 ? 56.651 -2.077  13.236  1.00 69.09  ?  222 PHE B CE2   1 
ATOM   3716 C CZ    . PHE B 1 222 ? 56.658 -3.029  14.250  1.00 70.07  ?  222 PHE B CZ    1 
ATOM   3717 N N     . LEU B 1 223 ? 56.209 -5.999  10.637  1.00 68.43  ?  223 LEU B N     1 
ATOM   3718 C CA    . LEU B 1 223 ? 56.641 -7.304  11.125  1.00 69.34  ?  223 LEU B CA    1 
ATOM   3719 C C     . LEU B 1 223 ? 57.718 -7.129  12.193  1.00 73.47  ?  223 LEU B C     1 
ATOM   3720 O O     . LEU B 1 223 ? 58.815 -6.642  11.890  1.00 74.85  ?  223 LEU B O     1 
ATOM   3721 C CB    . LEU B 1 223 ? 57.152 -8.158  9.966   1.00 65.43  ?  223 LEU B CB    1 
ATOM   3722 C CG    . LEU B 1 223 ? 56.998 -9.674  10.050  1.00 67.24  ?  223 LEU B CG    1 
ATOM   3723 C CD1   . LEU B 1 223 ? 55.589 -10.019 10.526  1.00 67.31  ?  223 LEU B CD1   1 
ATOM   3724 C CD2   . LEU B 1 223 ? 57.277 -10.286 8.690   1.00 70.22  ?  223 LEU B CD2   1 
ATOM   3725 N N     . ASP B 1 224 ? 57.410 -7.540  13.436  1.00 72.98  ?  224 ASP B N     1 
ATOM   3726 C CA    . ASP B 1 224 ? 58.389 -7.575  14.525  1.00 65.12  ?  224 ASP B CA    1 
ATOM   3727 C C     . ASP B 1 224 ? 59.324 -8.761  14.314  1.00 66.61  ?  224 ASP B C     1 
ATOM   3728 O O     . ASP B 1 224 ? 58.959 -9.917  14.543  1.00 71.86  ?  224 ASP B O     1 
ATOM   3729 C CB    . ASP B 1 224 ? 57.666 -7.658  15.871  1.00 70.06  ?  224 ASP B CB    1 
ATOM   3730 C CG    . ASP B 1 224 ? 58.613 -7.567  17.078  1.00 73.01  ?  224 ASP B CG    1 
ATOM   3731 O OD1   . ASP B 1 224 ? 59.784 -8.009  16.998  1.00 68.83  ?  224 ASP B OD1   1 
ATOM   3732 O OD2   . ASP B 1 224 ? 58.162 -7.067  18.137  1.00 76.36  -1 224 ASP B OD2   1 
ATOM   3733 N N     . ILE B 1 225 ? 60.534 -8.494  13.865  1.00 65.89  ?  225 ILE B N     1 
ATOM   3734 C CA    . ILE B 1 225 ? 61.477 -9.568  13.653  1.00 72.11  ?  225 ILE B CA    1 
ATOM   3735 C C     . ILE B 1 225 ? 62.534 -9.583  14.752  1.00 73.89  ?  225 ILE B C     1 
ATOM   3736 O O     . ILE B 1 225 ? 63.633 -10.088 14.546  1.00 75.56  ?  225 ILE B O     1 
ATOM   3737 C CB    . ILE B 1 225 ? 62.107 -9.495  12.251  1.00 66.90  ?  225 ILE B CB    1 
ATOM   3738 C CG1   . ILE B 1 225 ? 62.956 -8.246  12.090  1.00 68.15  ?  225 ILE B CG1   1 
ATOM   3739 C CG2   . ILE B 1 225 ? 61.034 -9.444  11.196  1.00 64.71  ?  225 ILE B CG2   1 
ATOM   3740 C CD1   . ILE B 1 225 ? 63.733 -8.240  10.827  1.00 66.06  ?  225 ILE B CD1   1 
ATOM   3741 N N     . SER B 1 226 ? 62.210 -9.018  15.908  1.00 74.99  ?  226 SER B N     1 
ATOM   3742 C CA    . SER B 1 226 ? 63.238 -8.898  16.969  1.00 75.22  ?  226 SER B CA    1 
ATOM   3743 C C     . SER B 1 226 ? 63.658 -10.276 17.488  1.00 78.45  ?  226 SER B C     1 
ATOM   3744 O O     . SER B 1 226 ? 64.866 -10.487 17.670  1.00 78.49  ?  226 SER B O     1 
ATOM   3745 C CB    . SER B 1 226 ? 62.738 -8.013  18.061  1.00 73.58  ?  226 SER B CB    1 
ATOM   3746 O OG    . SER B 1 226 ? 61.969 -6.950  17.526  1.00 72.50  ?  226 SER B OG    1 
ATOM   3747 N N     . ASP B 1 227 ? 62.703 -11.178 17.708  1.00 77.09  ?  227 ASP B N     1 
ATOM   3748 C CA    . ASP B 1 227 ? 63.038 -12.479 18.285  1.00 78.73  ?  227 ASP B CA    1 
ATOM   3749 C C     . ASP B 1 227 ? 63.883 -13.334 17.348  1.00 78.67  ?  227 ASP B C     1 
ATOM   3750 O O     . ASP B 1 227 ? 64.410 -14.372 17.767  1.00 77.92  ?  227 ASP B O     1 
ATOM   3751 C CB    . ASP B 1 227 ? 61.760 -13.229 18.664  1.00 85.97  ?  227 ASP B CB    1 
ATOM   3752 C CG    . ASP B 1 227 ? 60.863 -12.422 19.579  1.00 88.22  ?  227 ASP B CG    1 
ATOM   3753 O OD1   . ASP B 1 227 ? 61.394 -11.822 20.546  1.00 80.93  ?  227 ASP B OD1   1 
ATOM   3754 O OD2   . ASP B 1 227 ? 59.633 -12.382 19.318  1.00 90.28  -1 227 ASP B OD2   1 
ATOM   3755 N N     . GLN B 1 228 ? 64.004 -12.938 16.087  1.00 77.51  ?  228 GLN B N     1 
ATOM   3756 C CA    . GLN B 1 228 ? 64.786 -13.674 15.117  1.00 75.45  ?  228 GLN B CA    1 
ATOM   3757 C C     . GLN B 1 228 ? 66.072 -12.959 14.737  1.00 74.02  ?  228 GLN B C     1 
ATOM   3758 O O     . GLN B 1 228 ? 66.865 -13.523 13.979  1.00 78.01  ?  228 GLN B O     1 
ATOM   3759 C CB    . GLN B 1 228 ? 63.956 -13.921 13.844  1.00 72.87  ?  228 GLN B CB    1 
ATOM   3760 C CG    . GLN B 1 228 ? 62.717 -14.775 14.040  1.00 70.50  ?  228 GLN B CG    1 
ATOM   3761 C CD    . GLN B 1 228 ? 61.601 -14.062 14.787  1.00 78.09  ?  228 GLN B CD    1 
ATOM   3762 O OE1   . GLN B 1 228 ? 61.023 -14.615 15.728  1.00 89.81  ?  228 GLN B OE1   1 
ATOM   3763 N NE2   . GLN B 1 228 ? 61.289 -12.833 14.377  1.00 73.57  ?  228 GLN B NE2   1 
ATOM   3764 N N     . THR B 1 229 ? 66.288 -11.729 15.215  1.00 72.45  ?  229 THR B N     1 
ATOM   3765 C CA    . THR B 1 229 ? 67.369 -10.879 14.724  1.00 75.69  ?  229 THR B CA    1 
ATOM   3766 C C     . THR B 1 229 ? 68.336 -10.423 15.802  1.00 79.43  ?  229 THR B C     1 
ATOM   3767 O O     . THR B 1 229 ? 69.555 -10.578 15.636  1.00 78.49  ?  229 THR B O     1 
ATOM   3768 C CB    . THR B 1 229 ? 66.781 -9.636  14.044  1.00 73.46  ?  229 THR B CB    1 
ATOM   3769 O OG1   . THR B 1 229 ? 65.614 -9.235  14.773  1.00 75.80  ?  229 THR B OG1   1 
ATOM   3770 C CG2   . THR B 1 229 ? 66.417 -9.910  12.603  1.00 70.71  ?  229 THR B CG2   1 
ATOM   3771 N N     . LEU B 1 230 ? 67.825 -9.839  16.893  1.00 81.19  ?  230 LEU B N     1 
ATOM   3772 C CA    . LEU B 1 230 ? 68.677 -9.034  17.766  1.00 79.19  ?  230 LEU B CA    1 
ATOM   3773 C C     . LEU B 1 230 ? 69.692 -9.893  18.527  1.00 82.94  ?  230 LEU B C     1 
ATOM   3774 O O     . LEU B 1 230 ? 70.902 -9.751  18.305  1.00 81.14  ?  230 LEU B O     1 
ATOM   3775 C CB    . LEU B 1 230 ? 67.813 -8.194  18.724  1.00 73.11  ?  230 LEU B CB    1 
ATOM   3776 C CG    . LEU B 1 230 ? 66.907 -7.089  18.139  1.00 72.19  ?  230 LEU B CG    1 
ATOM   3777 C CD1   . LEU B 1 230 ? 66.043 -6.449  19.199  1.00 76.95  ?  230 LEU B CD1   1 
ATOM   3778 C CD2   . LEU B 1 230 ? 67.680 -6.021  17.432  1.00 70.07  ?  230 LEU B CD2   1 
ATOM   3779 N N     . GLU B 1 231 ? 69.225 -10.819 19.380  1.00 89.03  ?  231 GLU B N     1 
ATOM   3780 C CA    . GLU B 1 231 ? 70.140 -11.508 20.290  1.00 90.47  ?  231 GLU B CA    1 
ATOM   3781 C C     . GLU B 1 231 ? 71.257 -12.218 19.531  1.00 88.58  ?  231 GLU B C     1 
ATOM   3782 O O     . GLU B 1 231 ? 72.432 -11.886 19.691  1.00 90.53  ?  231 GLU B O     1 
ATOM   3783 C CB    . GLU B 1 231 ? 69.388 -12.495 21.199  1.00 91.22  ?  231 GLU B CB    1 
ATOM   3784 C CG    . GLU B 1 231 ? 70.383 -13.362 22.020  1.00 97.12  ?  231 GLU B CG    1 
ATOM   3785 C CD    . GLU B 1 231 ? 69.784 -14.135 23.198  1.00 109.99 ?  231 GLU B CD    1 
ATOM   3786 O OE1   . GLU B 1 231 ? 68.593 -13.902 23.549  1.00 114.66 ?  231 GLU B OE1   1 
ATOM   3787 O OE2   . GLU B 1 231 ? 70.535 -14.976 23.770  1.00 112.75 -1 231 GLU B OE2   1 
ATOM   3788 N N     . LYS B 1 232 ? 70.906 -13.179 18.671  1.00 87.64  ?  232 LYS B N     1 
ATOM   3789 C CA    . LYS B 1 232 ? 71.910 -14.133 18.205  1.00 85.72  ?  232 LYS B CA    1 
ATOM   3790 C C     . LYS B 1 232 ? 73.033 -13.445 17.445  1.00 89.84  ?  232 LYS B C     1 
ATOM   3791 O O     . LYS B 1 232 ? 74.185 -13.906 17.477  1.00 91.50  ?  232 LYS B O     1 
ATOM   3792 C CB    . LYS B 1 232 ? 71.252 -15.216 17.342  1.00 82.75  ?  232 LYS B CB    1 
ATOM   3793 C CG    . LYS B 1 232 ? 72.185 -16.379 16.995  1.00 84.57  ?  232 LYS B CG    1 
ATOM   3794 C CD    . LYS B 1 232 ? 71.437 -17.584 16.461  1.00 83.40  ?  232 LYS B CD    1 
ATOM   3795 C CE    . LYS B 1 232 ? 72.263 -18.826 16.702  1.00 91.92  ?  232 LYS B CE    1 
ATOM   3796 N NZ    . LYS B 1 232 ? 73.678 -18.650 16.285  1.00 86.22  ?  232 LYS B NZ    1 
ATOM   3797 N N     . THR B 1 233 ? 72.712 -12.350 16.753  1.00 89.57  ?  233 THR B N     1 
ATOM   3798 C CA    . THR B 1 233 ? 73.749 -11.489 16.194  1.00 88.73  ?  233 THR B CA    1 
ATOM   3799 C C     . THR B 1 233 ? 74.624 -10.926 17.299  1.00 91.78  ?  233 THR B C     1 
ATOM   3800 O O     . THR B 1 233 ? 75.859 -11.026 17.252  1.00 95.61  ?  233 THR B O     1 
ATOM   3801 C CB    . THR B 1 233 ? 73.113 -10.328 15.429  1.00 89.20  ?  233 THR B CB    1 
ATOM   3802 O OG1   . THR B 1 233 ? 71.904 -10.762 14.793  1.00 82.37  ?  233 THR B OG1   1 
ATOM   3803 C CG2   . THR B 1 233 ? 74.080 -9.758  14.410  1.00 86.30  ?  233 THR B CG2   1 
ATOM   3804 N N     . PHE B 1 234 ? 73.980 -10.326 18.306  1.00 94.00  ?  234 PHE B N     1 
ATOM   3805 C CA    . PHE B 1 234 ? 74.693 -9.641  19.374  1.00 92.30  ?  234 PHE B CA    1 
ATOM   3806 C C     . PHE B 1 234 ? 75.670 -10.592 20.059  1.00 97.88  ?  234 PHE B C     1 
ATOM   3807 O O     . PHE B 1 234 ? 76.866 -10.290 20.174  1.00 104.48 ?  234 PHE B O     1 
ATOM   3808 C CB    . PHE B 1 234 ? 73.677 -9.050  20.362  1.00 90.84  ?  234 PHE B CB    1 
ATOM   3809 C CG    . PHE B 1 234 ? 72.944 -7.795  19.860  1.00 86.78  ?  234 PHE B CG    1 
ATOM   3810 C CD1   . PHE B 1 234 ? 73.567 -6.868  19.040  1.00 87.80  ?  234 PHE B CD1   1 
ATOM   3811 C CD2   . PHE B 1 234 ? 71.639 -7.534  20.246  1.00 89.31  ?  234 PHE B CD2   1 
ATOM   3812 C CE1   . PHE B 1 234 ? 72.903 -5.705  18.604  1.00 83.23  ?  234 PHE B CE1   1 
ATOM   3813 C CE2   . PHE B 1 234 ? 70.968 -6.370  19.809  1.00 84.50  ?  234 PHE B CE2   1 
ATOM   3814 C CZ    . PHE B 1 234 ? 71.608 -5.460  18.994  1.00 76.41  ?  234 PHE B CZ    1 
ATOM   3815 N N     . ARG B 1 235 ? 75.188 -11.786 20.451  1.00 96.71  ?  235 ARG B N     1 
ATOM   3816 C CA    . ARG B 1 235 ? 76.053 -12.801 21.061  1.00 97.83  ?  235 ARG B CA    1 
ATOM   3817 C C     . ARG B 1 235 ? 77.273 -13.085 20.189  1.00 104.83 ?  235 ARG B C     1 
ATOM   3818 O O     . ARG B 1 235 ? 78.381 -13.258 20.703  1.00 109.59 ?  235 ARG B O     1 
ATOM   3819 C CB    . ARG B 1 235 ? 75.272 -14.103 21.332  1.00 89.57  ?  235 ARG B CB    1 
ATOM   3820 N N     . LEU B 1 236 ? 77.101 -13.090 18.865  1.00 105.83 ?  236 LEU B N     1 
ATOM   3821 C CA    . LEU B 1 236 ? 78.214 -13.467 17.998  1.00 104.53 ?  236 LEU B CA    1 
ATOM   3822 C C     . LEU B 1 236 ? 79.161 -12.306 17.715  1.00 105.27 ?  236 LEU B C     1 
ATOM   3823 O O     . LEU B 1 236 ? 80.376 -12.517 17.628  1.00 106.34 ?  236 LEU B O     1 
ATOM   3824 C CB    . LEU B 1 236 ? 77.690 -14.053 16.684  1.00 102.43 ?  236 LEU B CB    1 
ATOM   3825 C CG    . LEU B 1 236 ? 78.126 -15.498 16.408  1.00 105.91 ?  236 LEU B CG    1 
ATOM   3826 C CD1   . LEU B 1 236 ? 77.683 -15.936 15.017  1.00 104.07 ?  236 LEU B CD1   1 
ATOM   3827 C CD2   . LEU B 1 236 ? 79.650 -15.701 16.594  1.00 102.80 ?  236 LEU B CD2   1 
ATOM   3828 N N     . LEU B 1 237 ? 78.643 -11.084 17.550  1.00 105.05 ?  237 LEU B N     1 
ATOM   3829 C CA    . LEU B 1 237 ? 79.532 -9.971  17.219  1.00 112.60 ?  237 LEU B CA    1 
ATOM   3830 C C     . LEU B 1 237 ? 80.403 -9.584  18.408  1.00 115.71 ?  237 LEU B C     1 
ATOM   3831 O O     . LEU B 1 237 ? 81.618 -9.367  18.264  1.00 115.47 ?  237 LEU B O     1 
ATOM   3832 C CB    . LEU B 1 237 ? 78.749 -8.756  16.729  1.00 111.84 ?  237 LEU B CB    1 
ATOM   3833 C CG    . LEU B 1 237 ? 79.790 -7.666  16.442  1.00 116.63 ?  237 LEU B CG    1 
ATOM   3834 C CD1   . LEU B 1 237 ? 80.623 -8.000  15.189  1.00 114.26 ?  237 LEU B CD1   1 
ATOM   3835 C CD2   . LEU B 1 237 ? 79.193 -6.271  16.395  1.00 116.64 ?  237 LEU B CD2   1 
ATOM   3836 N N     . SER B 1 238 ? 79.797 -9.475  19.592  1.00 114.62 ?  238 SER B N     1 
ATOM   3837 C CA    . SER B 1 238 ? 80.609 -9.291  20.782  1.00 117.03 ?  238 SER B CA    1 
ATOM   3838 C C     . SER B 1 238 ? 81.588 -10.446 20.956  1.00 118.58 ?  238 SER B C     1 
ATOM   3839 O O     . SER B 1 238 ? 82.722 -10.229 21.385  1.00 122.11 ?  238 SER B O     1 
ATOM   3840 C CB    . SER B 1 238 ? 79.719 -9.133  22.012  1.00 117.32 ?  238 SER B CB    1 
ATOM   3841 O OG    . SER B 1 238 ? 79.440 -10.390 22.585  1.00 112.71 ?  238 SER B OG    1 
ATOM   3842 N N     . GLU B 1 239 ? 81.198 -11.668 20.574  1.00 117.80 ?  239 GLU B N     1 
ATOM   3843 C CA    . GLU B 1 239 ? 82.125 -12.798 20.671  1.00 116.57 ?  239 GLU B CA    1 
ATOM   3844 C C     . GLU B 1 239 ? 83.205 -12.737 19.595  1.00 115.09 ?  239 GLU B C     1 
ATOM   3845 O O     . GLU B 1 239 ? 84.372 -13.054 19.858  1.00 115.03 ?  239 GLU B O     1 
ATOM   3846 C CB    . GLU B 1 239 ? 81.362 -14.119 20.586  1.00 108.87 ?  239 GLU B CB    1 
ATOM   3847 N N     . ARG B 1 240 ? 82.835 -12.360 18.370  1.00 117.29 ?  240 ARG B N     1 
ATOM   3848 C CA    . ARG B 1 240 ? 83.859 -12.113 17.364  1.00 116.45 ?  240 ARG B CA    1 
ATOM   3849 C C     . ARG B 1 240 ? 84.846 -11.071 17.870  1.00 120.30 ?  240 ARG B C     1 
ATOM   3850 O O     . ARG B 1 240 ? 86.061 -11.298 17.846  1.00 121.85 ?  240 ARG B O     1 
ATOM   3851 C CB    . ARG B 1 240 ? 83.225 -11.667 16.043  1.00 106.64 ?  240 ARG B CB    1 
ATOM   3852 N N     . ILE B 1 241 ? 84.335 -9.953  18.402  1.00 120.23 ?  241 ILE B N     1 
ATOM   3853 C CA    . ILE B 1 241 ? 85.202 -8.856  18.832  1.00 122.88 ?  241 ILE B CA    1 
ATOM   3854 C C     . ILE B 1 241 ? 86.104 -9.299  19.985  1.00 128.25 ?  241 ILE B C     1 
ATOM   3855 O O     . ILE B 1 241 ? 87.336 -9.204  19.904  1.00 125.37 ?  241 ILE B O     1 
ATOM   3856 C CB    . ILE B 1 241 ? 84.353 -7.626  19.208  1.00 117.64 ?  241 ILE B CB    1 
ATOM   3857 N N     . ASN B 1 242 ? 85.514 -9.846  21.050  1.00 129.22 ?  242 ASN B N     1 
ATOM   3858 C CA    . ASN B 1 242 ? 86.276 -10.148 22.261  1.00 129.91 ?  242 ASN B CA    1 
ATOM   3859 C C     . ASN B 1 242 ? 87.210 -11.325 22.083  1.00 130.99 ?  242 ASN B C     1 
ATOM   3860 O O     . ASN B 1 242 ? 87.955 -11.646 23.013  1.00 133.89 ?  242 ASN B O     1 
ATOM   3861 C CB    . ASN B 1 242 ? 85.340 -10.410 23.441  1.00 127.73 ?  242 ASN B CB    1 
ATOM   3862 C CG    . ASN B 1 242 ? 84.722 -9.138  23.972  1.00 130.15 ?  242 ASN B CG    1 
ATOM   3863 O OD1   . ASN B 1 242 ? 83.566 -8.790  23.655  1.00 127.95 ?  242 ASN B OD1   1 
ATOM   3864 N ND2   . ASN B 1 242 ? 85.507 -8.406  24.753  1.00 130.82 ?  242 ASN B ND2   1 
ATOM   3865 N N     . SER B 1 243 ? 87.173 -11.988 20.935  1.00 130.88 ?  243 SER B N     1 
ATOM   3866 C CA    . SER B 1 243 ? 88.166 -13.001 20.652  1.00 126.65 ?  243 SER B CA    1 
ATOM   3867 C C     . SER B 1 243 ? 89.488 -12.417 20.175  1.00 128.64 ?  243 SER B C     1 
ATOM   3868 O O     . SER B 1 243 ? 90.471 -13.159 20.109  1.00 129.39 ?  243 SER B O     1 
ATOM   3869 C CB    . SER B 1 243 ? 87.638 -13.972 19.608  1.00 120.57 ?  243 SER B CB    1 
ATOM   3870 O OG    . SER B 1 243 ? 88.649 -14.898 19.266  1.00 113.06 ?  243 SER B OG    1 
ATOM   3871 N N     . SER B 1 244 ? 89.536 -11.133 19.804  1.00 130.64 ?  244 SER B N     1 
ATOM   3872 C CA    . SER B 1 244 ? 90.798 -10.493 19.406  1.00 138.22 ?  244 SER B CA    1 
ATOM   3873 C C     . SER B 1 244 ? 90.901 -9.060  19.939  1.00 142.00 ?  244 SER B C     1 
ATOM   3874 O O     . SER B 1 244 ? 91.425 -8.170  19.259  1.00 143.53 ?  244 SER B O     1 
ATOM   3875 C CB    . SER B 1 244 ? 90.980 -10.502 17.882  1.00 135.33 ?  244 SER B CB    1 
ATOM   3876 O OG    . SER B 1 244 ? 91.284 -11.799 17.385  1.00 132.46 ?  244 SER B OG    1 
ATOM   3877 N N     . LYS B 1 245 ? 90.442 -8.817  21.176  1.00 141.76 ?  245 LYS B N     1 
ATOM   3878 C CA    . LYS B 1 245 ? 90.465 -7.460  21.728  1.00 140.49 ?  245 LYS B CA    1 
ATOM   3879 C C     . LYS B 1 245 ? 91.886 -6.927  21.914  1.00 152.94 ?  245 LYS B C     1 
ATOM   3880 O O     . LYS B 1 245 ? 92.053 -5.719  22.120  1.00 156.68 ?  245 LYS B O     1 
ATOM   3881 C CB    . LYS B 1 245 ? 89.690 -7.405  23.050  1.00 133.38 ?  245 LYS B CB    1 
ATOM   3882 N N     . GLN B 1 246 ? 92.907 -7.790  21.823  1.00 151.25 ?  246 GLN B N     1 
ATOM   3883 C CA    . GLN B 1 246 ? 94.295 -7.360  21.693  1.00 152.32 ?  246 GLN B CA    1 
ATOM   3884 C C     . GLN B 1 246 ? 94.641 -6.886  20.281  1.00 158.83 ?  246 GLN B C     1 
ATOM   3885 O O     . GLN B 1 246 ? 95.778 -6.459  20.063  1.00 160.55 ?  246 GLN B O     1 
ATOM   3886 C CB    . GLN B 1 246 ? 95.241 -8.496  22.114  1.00 149.48 ?  246 GLN B CB    1 
ATOM   3887 N N     . ARG B 1 247 ? 93.712 -6.994  19.312  1.00 155.29 ?  247 ARG B N     1 
ATOM   3888 C CA    . ARG B 1 247 ? 93.855 -6.352  17.999  1.00 157.33 ?  247 ARG B CA    1 
ATOM   3889 C C     . ARG B 1 247 ? 93.402 -4.893  17.985  1.00 166.39 ?  247 ARG B C     1 
ATOM   3890 O O     . ARG B 1 247 ? 93.652 -4.192  17.001  1.00 167.92 ?  247 ARG B O     1 
ATOM   3891 C CB    . ARG B 1 247 ? 93.085 -7.111  16.908  1.00 143.72 ?  247 ARG B CB    1 
ATOM   3892 N N     . LEU B 1 248 ? 92.760 -4.416  19.048  1.00 161.50 ?  248 LEU B N     1 
ATOM   3893 C CA    . LEU B 1 248 ? 92.580 -2.982  19.242  1.00 166.49 ?  248 LEU B CA    1 
ATOM   3894 C C     . LEU B 1 248 ? 93.915 -2.272  19.370  1.00 169.79 ?  248 LEU B C     1 
ATOM   3895 O O     . LEU B 1 248 ? 93.977 -1.050  19.199  1.00 170.22 ?  248 LEU B O     1 
ATOM   3896 C CB    . LEU B 1 248 ? 91.718 -2.729  20.491  1.00 167.44 ?  248 LEU B CB    1 
ATOM   3897 N N     . GLU B 1 249 ? 94.978 -3.022  19.659  1.00 171.28 ?  249 GLU B N     1 
ATOM   3898 C CA    . GLU B 1 249 ? 96.319 -2.461  19.732  1.00 173.36 ?  249 GLU B CA    1 
ATOM   3899 C C     . GLU B 1 249 ? 96.762 -1.821  18.399  1.00 175.07 ?  249 GLU B C     1 
ATOM   3900 O O     . GLU B 1 249 ? 97.837 -1.205  18.372  1.00 179.44 ?  249 GLU B O     1 
ATOM   3901 C CB    . GLU B 1 249 ? 97.297 -3.561  20.236  1.00 171.21 ?  249 GLU B CB    1 
ATOM   3902 N N     . THR B 1 250 ? 96.010 -2.039  17.293  1.00 173.26 ?  250 THR B N     1 
ATOM   3903 C CA    . THR B 1 250 ? 96.116 -1.305  16.038  1.00 170.00 ?  250 THR B CA    1 
ATOM   3904 C C     . THR B 1 250 ? 94.785 -0.688  15.594  1.00 168.16 ?  250 THR B C     1 
ATOM   3905 O O     . THR B 1 250 ? 94.768 0.112   14.637  1.00 167.47 ?  250 THR B O     1 
ATOM   3906 C CB    . THR B 1 250 ? 96.683 -2.181  14.936  1.00 168.18 ?  250 THR B CB    1 
ATOM   3907 N N     . GLN B 1 251 ? 93.627 -1.025  16.206  1.00 168.95 ?  251 GLN B N     1 
ATOM   3908 C CA    . GLN B 1 251 ? 92.399 -0.584  15.537  1.00 164.00 ?  251 GLN B CA    1 
ATOM   3909 C C     . GLN B 1 251 ? 91.752 0.664   16.149  1.00 164.79 ?  251 GLN B C     1 
ATOM   3910 O O     . GLN B 1 251 ? 90.749 1.148   15.611  1.00 164.96 ?  251 GLN B O     1 
ATOM   3911 C CB    . GLN B 1 251 ? 91.334 -1.691  15.495  1.00 164.52 ?  251 GLN B CB    1 
ATOM   3912 C CG    . GLN B 1 251 ? 91.576 -3.099  14.982  1.00 165.01 ?  251 GLN B CG    1 
ATOM   3913 C CD    . GLN B 1 251 ? 92.582 -3.290  13.897  1.00 166.25 ?  251 GLN B CD    1 
ATOM   3914 O OE1   . GLN B 1 251 ? 92.858 -2.439  13.069  1.00 167.20 ?  251 GLN B OE1   1 
ATOM   3915 N NE2   . GLN B 1 251 ? 93.093 -4.477  13.865  1.00 161.83 ?  251 GLN B NE2   1 
ATOM   3916 N N     . PHE B 1 252 ? 92.320 1.237   17.211  1.00 167.09 ?  252 PHE B N     1 
ATOM   3917 C CA    . PHE B 1 252 ? 91.637 2.229   18.040  1.00 164.10 ?  252 PHE B CA    1 
ATOM   3918 C C     . PHE B 1 252 ? 90.439 1.607   18.711  1.00 164.13 ?  252 PHE B C     1 
ATOM   3919 O O     . PHE B 1 252 ? 89.508 2.330   19.114  1.00 158.54 ?  252 PHE B O     1 
ATOM   3920 C CB    . PHE B 1 252 ? 91.201 3.477   17.252  1.00 157.27 ?  252 PHE B CB    1 
ATOM   3921 N N     . GLY B 1 253 ? 90.427 0.270   18.772  1.00 164.44 ?  253 GLY B N     1 
ATOM   3922 C CA    . GLY B 1 253 ? 89.357 -0.422  19.453  1.00 162.02 ?  253 GLY B CA    1 
ATOM   3923 C C     . GLY B 1 253 ? 89.282 -0.167  20.938  1.00 160.52 ?  253 GLY B C     1 
ATOM   3924 O O     . GLY B 1 253 ? 88.196 -0.218  21.514  1.00 158.02 ?  253 GLY B O     1 
ATOM   3925 N N     . GLU B 1 254 ? 90.414 0.135   21.573  1.00 164.80 ?  254 GLU B N     1 
ATOM   3926 C CA    . GLU B 1 254 ? 90.349 0.544   22.968  1.00 164.59 ?  254 GLU B CA    1 
ATOM   3927 C C     . GLU B 1 254 ? 89.458 1.773   23.140  1.00 164.97 ?  254 GLU B C     1 
ATOM   3928 O O     . GLU B 1 254 ? 89.008 2.040   24.253  1.00 165.87 ?  254 GLU B O     1 
ATOM   3929 C CB    . GLU B 1 254 ? 91.752 0.806   23.540  1.00 165.16 ?  254 GLU B CB    1 
ATOM   3930 N N     . GLU B 1 255 ? 89.169 2.508   22.049  1.00 165.00 ?  255 GLU B N     1 
ATOM   3931 C CA    . GLU B 1 255 ? 88.288 3.680   22.024  1.00 160.74 ?  255 GLU B CA    1 
ATOM   3932 C C     . GLU B 1 255 ? 87.019 3.521   21.207  1.00 153.46 ?  255 GLU B C     1 
ATOM   3933 O O     . GLU B 1 255 ? 86.069 4.283   21.431  1.00 152.76 ?  255 GLU B O     1 
ATOM   3934 C CB    . GLU B 1 255 ? 89.061 4.912   21.496  1.00 160.92 ?  255 GLU B CB    1 
ATOM   3935 N N     . MET B 1 256 ? 86.986 2.603   20.279  1.00 157.66 ?  256 MET B N     1 
ATOM   3936 C CA    . MET B 1 256 ? 85.866 2.534   19.350  1.00 146.45 ?  256 MET B CA    1 
ATOM   3937 C C     . MET B 1 256 ? 85.198 1.169   19.251  1.00 141.03 ?  256 MET B C     1 
ATOM   3938 O O     . MET B 1 256 ? 83.996 1.123   18.966  1.00 138.56 ?  256 MET B O     1 
ATOM   3939 C CB    . MET B 1 256 ? 86.313 2.951   17.942  1.00 138.66 ?  256 MET B CB    1 
ATOM   3940 N N     . VAL B 1 257 ? 85.905 0.057   19.483  1.00 144.60 ?  257 VAL B N     1 
ATOM   3941 C CA    . VAL B 1 257 ? 85.211 -1.228  19.440  1.00 141.57 ?  257 VAL B CA    1 
ATOM   3942 C C     . VAL B 1 257 ? 84.394 -1.456  20.717  1.00 138.63 ?  257 VAL B C     1 
ATOM   3943 O O     . VAL B 1 257 ? 83.421 -2.223  20.713  1.00 139.97 ?  257 VAL B O     1 
ATOM   3944 C CB    . VAL B 1 257 ? 86.188 -2.390  19.147  1.00 136.93 ?  257 VAL B CB    1 
ATOM   3945 C CG1   . VAL B 1 257 ? 87.026 -2.097  17.898  1.00 136.31 ?  257 VAL B CG1   1 
ATOM   3946 C CG2   . VAL B 1 257 ? 87.040 -2.754  20.349  1.00 132.10 ?  257 VAL B CG2   1 
ATOM   3947 N N     . ASN B 1 258 ? 84.767 -0.819  21.828  1.00 138.19 ?  258 ASN B N     1 
ATOM   3948 C CA    . ASN B 1 258 ? 83.920 -0.872  23.018  1.00 138.65 ?  258 ASN B CA    1 
ATOM   3949 C C     . ASN B 1 258 ? 82.554 -0.241  22.757  1.00 139.17 ?  258 ASN B C     1 
ATOM   3950 O O     . ASN B 1 258 ? 81.528 -0.715  23.269  1.00 135.95 ?  258 ASN B O     1 
ATOM   3951 C CB    . ASN B 1 258 ? 84.633 -0.193  24.192  1.00 140.25 ?  258 ASN B CB    1 
ATOM   3952 C CG    . ASN B 1 258 ? 85.330 1.105   23.785  1.00 148.08 ?  258 ASN B CG    1 
ATOM   3953 O OD1   . ASN B 1 258 ? 85.729 1.283   22.625  1.00 151.18 ?  258 ASN B OD1   1 
ATOM   3954 N ND2   . ASN B 1 258 ? 85.485 2.009   24.741  1.00 148.12 ?  258 ASN B ND2   1 
ATOM   3955 N N     . GLN B 1 259 ? 82.524 0.840   21.973  1.00 137.32 ?  259 GLN B N     1 
ATOM   3956 C CA    . GLN B 1 259 ? 81.247 1.377   21.523  1.00 133.82 ?  259 GLN B CA    1 
ATOM   3957 C C     . GLN B 1 259 ? 80.526 0.383   20.612  1.00 132.23 ?  259 GLN B C     1 
ATOM   3958 O O     . GLN B 1 259 ? 79.294 0.269   20.672  1.00 131.98 ?  259 GLN B O     1 
ATOM   3959 C CB    . GLN B 1 259 ? 81.460 2.729   20.826  1.00 130.04 ?  259 GLN B CB    1 
ATOM   3960 N N     . PHE B 1 260 ? 81.277 -0.365  19.790  1.00 130.52 ?  260 PHE B N     1 
ATOM   3961 C CA    . PHE B 1 260 ? 80.683 -1.348  18.885  1.00 129.42 ?  260 PHE B CA    1 
ATOM   3962 C C     . PHE B 1 260 ? 80.289 -2.649  19.584  1.00 130.63 ?  260 PHE B C     1 
ATOM   3963 O O     . PHE B 1 260 ? 79.376 -3.331  19.104  1.00 128.58 ?  260 PHE B O     1 
ATOM   3964 C CB    . PHE B 1 260 ? 81.642 -1.654  17.730  1.00 127.27 ?  260 PHE B CB    1 
ATOM   3965 N N     . ASP B 1 261 ? 80.980 -3.031  20.695  1.00 129.03 ?  261 ASP B N     1 
ATOM   3966 C CA    . ASP B 1 261 ? 80.690 -4.279  21.410  1.00 123.94 ?  261 ASP B CA    1 
ATOM   3967 C C     . ASP B 1 261 ? 79.246 -4.359  21.879  1.00 126.90 ?  261 ASP B C     1 
ATOM   3968 O O     . ASP B 1 261 ? 78.824 -3.641  22.800  1.00 128.85 ?  261 ASP B O     1 
ATOM   3969 C CB    . ASP B 1 261 ? 81.554 -4.493  22.642  1.00 123.16 ?  261 ASP B CB    1 
ATOM   3970 C CG    . ASP B 1 261 ? 80.978 -5.575  23.541  1.00 126.00 ?  261 ASP B CG    1 
ATOM   3971 O OD1   . ASP B 1 261 ? 81.138 -6.756  23.186  1.00 122.59 ?  261 ASP B OD1   1 
ATOM   3972 O OD2   . ASP B 1 261 ? 80.325 -5.252  24.560  1.00 128.19 -1 261 ASP B OD2   1 
ATOM   3973 N N     . PRO B 1 262 ? 78.480 -5.277  21.301  1.00 122.07 ?  262 PRO B N     1 
ATOM   3974 C CA    . PRO B 1 262 ? 77.037 -5.311  21.532  1.00 119.16 ?  262 PRO B CA    1 
ATOM   3975 C C     . PRO B 1 262 ? 76.617 -6.162  22.710  1.00 116.91 ?  262 PRO B C     1 
ATOM   3976 O O     . PRO B 1 262 ? 75.422 -6.194  23.013  1.00 116.48 ?  262 PRO B O     1 
ATOM   3977 C CB    . PRO B 1 262 ? 76.532 -5.922  20.228  1.00 115.81 ?  262 PRO B CB    1 
ATOM   3978 C CG    . PRO B 1 262 ? 77.628 -6.889  19.849  1.00 117.02 ?  262 PRO B CG    1 
ATOM   3979 C CD    . PRO B 1 262 ? 78.908 -6.243  20.275  1.00 121.09 ?  262 PRO B CD    1 
ATOM   3980 N N     . GLY B 1 263 ? 77.567 -6.828  23.375  1.00 117.54 ?  263 GLY B N     1 
ATOM   3981 C CA    . GLY B 1 263 ? 77.202 -7.780  24.409  1.00 115.56 ?  263 GLY B CA    1 
ATOM   3982 C C     . GLY B 1 263 ? 76.302 -7.187  25.473  1.00 115.86 ?  263 GLY B C     1 
ATOM   3983 O O     . GLY B 1 263 ? 75.430 -7.878  26.010  1.00 110.82 ?  263 GLY B O     1 
ATOM   3984 N N     . ASP B 1 264 ? 76.470 -5.890  25.763  1.00 118.71 ?  264 ASP B N     1 
ATOM   3985 C CA    . ASP B 1 264 ? 75.604 -5.209  26.726  1.00 118.93 ?  264 ASP B CA    1 
ATOM   3986 C C     . ASP B 1 264 ? 74.134 -5.150  26.284  1.00 116.82 ?  264 ASP B C     1 
ATOM   3987 O O     . ASP B 1 264 ? 73.286 -4.683  27.062  1.00 114.01 ?  264 ASP B O     1 
ATOM   3988 C CB    . ASP B 1 264 ? 76.142 -3.782  27.045  1.00 119.20 ?  264 ASP B CB    1 
ATOM   3989 C CG    . ASP B 1 264 ? 76.411 -2.905  25.787  1.00 125.45 ?  264 ASP B CG    1 
ATOM   3990 O OD1   . ASP B 1 264 ? 77.196 -3.342  24.906  1.00 124.53 ?  264 ASP B OD1   1 
ATOM   3991 O OD2   . ASP B 1 264 ? 75.866 -1.761  25.707  1.00 125.60 -1 264 ASP B OD2   1 
ATOM   3992 N N     . LEU B 1 265 ? 73.803 -5.613  25.069  1.00 118.65 ?  265 LEU B N     1 
ATOM   3993 C CA    . LEU B 1 265 ? 72.454 -5.458  24.540  1.00 109.05 ?  265 LEU B CA    1 
ATOM   3994 C C     . LEU B 1 265 ? 71.674 -6.765  24.460  1.00 99.98  ?  265 LEU B C     1 
ATOM   3995 O O     . LEU B 1 265 ? 70.447 -6.717  24.352  1.00 99.02  ?  265 LEU B O     1 
ATOM   3996 C CB    . LEU B 1 265 ? 72.504 -4.767  23.170  1.00 100.32 ?  265 LEU B CB    1 
ATOM   3997 C CG    . LEU B 1 265 ? 72.686 -3.249  23.272  1.00 103.30 ?  265 LEU B CG    1 
ATOM   3998 C CD1   . LEU B 1 265 ? 73.324 -2.686  22.027  1.00 98.34  ?  265 LEU B CD1   1 
ATOM   3999 C CD2   . LEU B 1 265 ? 71.364 -2.547  23.567  1.00 95.42  ?  265 LEU B CD2   1 
ATOM   4000 N N     . VAL B 1 266 ? 72.330 -7.923  24.568  1.00 100.96 ?  266 VAL B N     1 
ATOM   4001 C CA    . VAL B 1 266 ? 71.576 -9.151  24.776  1.00 98.81  ?  266 VAL B CA    1 
ATOM   4002 C C     . VAL B 1 266 ? 70.598 -8.941  25.932  1.00 101.21 ?  266 VAL B C     1 
ATOM   4003 O O     . VAL B 1 266 ? 70.869 -8.210  26.891  1.00 105.12 ?  266 VAL B O     1 
ATOM   4004 C CB    . VAL B 1 266 ? 72.521 -10.340 25.029  1.00 94.06  ?  266 VAL B CB    1 
ATOM   4005 C CG1   . VAL B 1 266 ? 73.642 -10.336 24.032  1.00 89.88  ?  266 VAL B CG1   1 
ATOM   4006 C CG2   . VAL B 1 266 ? 73.081 -10.292 26.421  1.00 101.33 ?  266 VAL B CG2   1 
ATOM   4007 N N     . GLY B 1 267 ? 69.418 -9.506  25.799  1.00 97.48  ?  267 GLY B N     1 
ATOM   4008 C CA    . GLY B 1 267 ? 68.466 -9.455  26.865  1.00 99.78  ?  267 GLY B CA    1 
ATOM   4009 C C     . GLY B 1 267 ? 67.565 -8.242  26.876  1.00 100.10 ?  267 GLY B C     1 
ATOM   4010 O O     . GLY B 1 267 ? 66.477 -8.309  27.463  1.00 102.63 ?  267 GLY B O     1 
ATOM   4011 N N     . VAL B 1 268 ? 67.954 -7.134  26.248  1.00 92.96  ?  268 VAL B N     1 
ATOM   4012 C CA    . VAL B 1 268 ? 67.075 -5.972  26.377  1.00 98.80  ?  268 VAL B CA    1 
ATOM   4013 C C     . VAL B 1 268 ? 65.792 -6.287  25.609  1.00 96.94  ?  268 VAL B C     1 
ATOM   4014 O O     . VAL B 1 268 ? 65.730 -6.185  24.379  1.00 93.47  ?  268 VAL B O     1 
ATOM   4015 C CB    . VAL B 1 268 ? 67.739 -4.677  25.890  1.00 97.39  ?  268 VAL B CB    1 
ATOM   4016 C CG1   . VAL B 1 268 ? 67.015 -3.442  26.471  1.00 94.39  ?  268 VAL B CG1   1 
ATOM   4017 C CG2   . VAL B 1 268 ? 69.203 -4.665  26.292  1.00 98.30  ?  268 VAL B CG2   1 
ATOM   4018 N N     . LYS B 1 269 ? 64.755 -6.680  26.342  1.00 100.39 ?  269 LYS B N     1 
ATOM   4019 C CA    . LYS B 1 269 ? 63.678 -7.422  25.717  1.00 96.33  ?  269 LYS B CA    1 
ATOM   4020 C C     . LYS B 1 269 ? 62.603 -6.548  25.088  1.00 92.40  ?  269 LYS B C     1 
ATOM   4021 O O     . LYS B 1 269 ? 61.897 -7.030  24.204  1.00 90.79  ?  269 LYS B O     1 
ATOM   4022 C CB    . LYS B 1 269 ? 63.037 -8.372  26.734  1.00 97.83  ?  269 LYS B CB    1 
ATOM   4023 N N     . GLU B 1 270 ? 62.438 -5.296  25.505  1.00 92.43  ?  270 GLU B N     1 
ATOM   4024 C CA    . GLU B 1 270 ? 61.514 -4.422  24.791  1.00 91.67  ?  270 GLU B CA    1 
ATOM   4025 C C     . GLU B 1 270 ? 62.214 -3.651  23.672  1.00 88.79  ?  270 GLU B C     1 
ATOM   4026 O O     . GLU B 1 270 ? 61.562 -2.839  22.992  1.00 82.50  ?  270 GLU B O     1 
ATOM   4027 C CB    . GLU B 1 270 ? 60.805 -3.462  25.763  1.00 89.01  ?  270 GLU B CB    1 
ATOM   4028 N N     . PHE B 1 271 ? 63.526 -3.891  23.476  1.00 85.87  ?  271 PHE B N     1 
ATOM   4029 C CA    . PHE B 1 271 ? 64.258 -3.365  22.324  1.00 85.68  ?  271 PHE B CA    1 
ATOM   4030 C C     . PHE B 1 271 ? 63.859 -4.123  21.060  1.00 86.36  ?  271 PHE B C     1 
ATOM   4031 O O     . PHE B 1 271 ? 63.957 -5.358  21.013  1.00 87.72  ?  271 PHE B O     1 
ATOM   4032 C CB    . PHE B 1 271 ? 65.763 -3.488  22.543  1.00 83.00  ?  271 PHE B CB    1 
ATOM   4033 C CG    . PHE B 1 271 ? 66.597 -2.793  21.481  1.00 84.24  ?  271 PHE B CG    1 
ATOM   4034 C CD1   . PHE B 1 271 ? 66.256 -1.526  21.018  1.00 84.14  ?  271 PHE B CD1   1 
ATOM   4035 C CD2   . PHE B 1 271 ? 67.737 -3.390  20.969  1.00 83.28  ?  271 PHE B CD2   1 
ATOM   4036 C CE1   . PHE B 1 271 ? 67.025 -0.894  20.055  1.00 80.28  ?  271 PHE B CE1   1 
ATOM   4037 C CE2   . PHE B 1 271 ? 68.503 -2.752  20.010  1.00 74.03  ?  271 PHE B CE2   1 
ATOM   4038 C CZ    . PHE B 1 271 ? 68.143 -1.506  19.559  1.00 72.62  ?  271 PHE B CZ    1 
ATOM   4039 N N     . GLY B 1 272 ? 63.465 -3.389  20.025  1.00 80.95  ?  272 GLY B N     1 
ATOM   4040 C CA    . GLY B 1 272 ? 62.762 -3.980  18.895  1.00 84.55  ?  272 GLY B CA    1 
ATOM   4041 C C     . GLY B 1 272 ? 63.315 -3.627  17.532  1.00 79.05  ?  272 GLY B C     1 
ATOM   4042 O O     . GLY B 1 272 ? 63.679 -2.474  17.270  1.00 75.40  ?  272 GLY B O     1 
ATOM   4043 N N     . TYR B 1 273 ? 63.381 -4.641  16.665  1.00 74.85  ?  273 TYR B N     1 
ATOM   4044 C CA    . TYR B 1 273 ? 63.769 -4.519  15.263  1.00 73.37  ?  273 TYR B CA    1 
ATOM   4045 C C     . TYR B 1 273 ? 62.581 -4.911  14.402  1.00 67.99  ?  273 TYR B C     1 
ATOM   4046 O O     . TYR B 1 273 ? 61.949 -5.939  14.663  1.00 73.30  ?  273 TYR B O     1 
ATOM   4047 C CB    . TYR B 1 273 ? 64.937 -5.439  14.949  1.00 72.45  ?  273 TYR B CB    1 
ATOM   4048 C CG    . TYR B 1 273 ? 65.630 -5.174  13.628  1.00 72.60  ?  273 TYR B CG    1 
ATOM   4049 C CD1   . TYR B 1 273 ? 65.681 -3.902  13.081  1.00 68.91  ?  273 TYR B CD1   1 
ATOM   4050 C CD2   . TYR B 1 273 ? 66.263 -6.212  12.922  1.00 74.63  ?  273 TYR B CD2   1 
ATOM   4051 C CE1   . TYR B 1 273 ? 66.359 -3.663  11.860  1.00 71.42  ?  273 TYR B CE1   1 
ATOM   4052 C CE2   . TYR B 1 273 ? 66.930 -5.979  11.692  1.00 76.10  ?  273 TYR B CE2   1 
ATOM   4053 C CZ    . TYR B 1 273 ? 66.974 -4.706  11.170  1.00 73.09  ?  273 TYR B CZ    1 
ATOM   4054 O OH    . TYR B 1 273 ? 67.626 -4.486  9.976   1.00 62.43  ?  273 TYR B OH    1 
ATOM   4055 N N     . LEU B 1 274 ? 62.282 -4.117  13.369  1.00 64.48  ?  274 LEU B N     1 
ATOM   4056 C CA    . LEU B 1 274 ? 61.069 -4.336  12.584  1.00 67.28  ?  274 LEU B CA    1 
ATOM   4057 C C     . LEU B 1 274 ? 61.340 -4.304  11.088  1.00 64.05  ?  274 LEU B C     1 
ATOM   4058 O O     . LEU B 1 274 ? 62.120 -3.487  10.602  1.00 64.37  ?  274 LEU B O     1 
ATOM   4059 C CB    . LEU B 1 274 ? 59.984 -3.291  12.906  1.00 66.82  ?  274 LEU B CB    1 
ATOM   4060 C CG    . LEU B 1 274 ? 60.162 -1.847  12.417  1.00 69.28  ?  274 LEU B CG    1 
ATOM   4061 C CD1   . LEU B 1 274 ? 59.256 -1.475  11.250  1.00 61.59  ?  274 LEU B CD1   1 
ATOM   4062 C CD2   . LEU B 1 274 ? 59.949 -0.888  13.566  1.00 70.15  ?  274 LEU B CD2   1 
ATOM   4063 N N     . LEU B 1 275 ? 60.663 -5.182  10.361  1.00 64.51  ?  275 LEU B N     1 
ATOM   4064 C CA    . LEU B 1 275 ? 60.592 -5.130  8.906   1.00 61.55  ?  275 LEU B CA    1 
ATOM   4065 C C     . LEU B 1 275 ? 59.290 -4.458  8.491   1.00 58.18  ?  275 LEU B C     1 
ATOM   4066 O O     . LEU B 1 275 ? 58.239 -4.692  9.094   1.00 63.64  ?  275 LEU B O     1 
ATOM   4067 C CB    . LEU B 1 275 ? 60.666 -6.542  8.328   1.00 60.34  ?  275 LEU B CB    1 
ATOM   4068 C CG    . LEU B 1 275 ? 60.637 -6.806  6.829   1.00 58.82  ?  275 LEU B CG    1 
ATOM   4069 C CD1   . LEU B 1 275 ? 61.972 -6.488  6.229   1.00 59.07  ?  275 LEU B CD1   1 
ATOM   4070 C CD2   . LEU B 1 275 ? 60.317 -8.260  6.624   1.00 56.72  ?  275 LEU B CD2   1 
ATOM   4071 N N     . LEU B 1 276 ? 59.354 -3.592  7.489   1.00 56.94  ?  276 LEU B N     1 
ATOM   4072 C CA    . LEU B 1 276 ? 58.161 -2.866  7.076   1.00 61.74  ?  276 LEU B CA    1 
ATOM   4073 C C     . LEU B 1 276 ? 58.125 -2.765  5.556   1.00 61.96  ?  276 LEU B C     1 
ATOM   4074 O O     . LEU B 1 276 ? 59.167 -2.642  4.898   1.00 60.24  ?  276 LEU B O     1 
ATOM   4075 C CB    . LEU B 1 276 ? 58.096 -1.464  7.723   1.00 57.02  ?  276 LEU B CB    1 
ATOM   4076 C CG    . LEU B 1 276 ? 56.972 -0.522  7.275   1.00 58.42  ?  276 LEU B CG    1 
ATOM   4077 C CD1   . LEU B 1 276 ? 56.521 0.347   8.403   1.00 63.58  ?  276 LEU B CD1   1 
ATOM   4078 C CD2   . LEU B 1 276 ? 57.396 0.361   6.129   1.00 60.00  ?  276 LEU B CD2   1 
ATOM   4079 N N     . VAL B 1 277 ? 56.909 -2.810  5.008   1.00 58.06  ?  277 VAL B N     1 
ATOM   4080 C CA    . VAL B 1 277 ? 56.676 -2.655  3.577   1.00 60.09  ?  277 VAL B CA    1 
ATOM   4081 C C     . VAL B 1 277 ? 55.474 -1.740  3.406   1.00 62.60  ?  277 VAL B C     1 
ATOM   4082 O O     . VAL B 1 277 ? 54.466 -1.929  4.097   1.00 65.94  ?  277 VAL B O     1 
ATOM   4083 C CB    . VAL B 1 277 ? 56.432 -4.014  2.890   1.00 58.28  ?  277 VAL B CB    1 
ATOM   4084 C CG1   . VAL B 1 277 ? 56.009 -3.816  1.484   1.00 58.30  ?  277 VAL B CG1   1 
ATOM   4085 C CG2   . VAL B 1 277 ? 57.671 -4.882  2.937   1.00 57.24  ?  277 VAL B CG2   1 
ATOM   4086 N N     . ALA B 1 278 ? 55.589 -0.734  2.512   1.00 63.10  ?  278 ALA B N     1 
ATOM   4087 C CA    . ALA B 1 278 ? 54.505 0.199   2.164   1.00 60.10  ?  278 ALA B CA    1 
ATOM   4088 C C     . ALA B 1 278 ? 54.443 0.354   0.655   1.00 62.58  ?  278 ALA B C     1 
ATOM   4089 O O     . ALA B 1 278 ? 55.420 0.077   -0.035  1.00 62.91  ?  278 ALA B O     1 
ATOM   4090 C CB    . ALA B 1 278 ? 54.689 1.590   2.777   1.00 62.81  ?  278 ALA B CB    1 
ATOM   4091 N N     . GLN B 1 279 ? 53.301 0.815   0.137   1.00 62.36  ?  279 GLN B N     1 
ATOM   4092 C CA    . GLN B 1 279 ? 53.061 0.840   -1.309  1.00 59.66  ?  279 GLN B CA    1 
ATOM   4093 C C     . GLN B 1 279 ? 52.412 2.154   -1.752  1.00 68.70  ?  279 GLN B C     1 
ATOM   4094 O O     . GLN B 1 279 ? 51.386 2.560   -1.200  1.00 73.81  ?  279 GLN B O     1 
ATOM   4095 C CB    . GLN B 1 279 ? 52.174 -0.356  -1.722  1.00 64.87  ?  279 GLN B CB    1 
ATOM   4096 C CG    . GLN B 1 279 ? 51.746 -0.382  -3.212  1.00 69.37  ?  279 GLN B CG    1 
ATOM   4097 C CD    . GLN B 1 279 ? 50.882 -1.604  -3.614  1.00 71.36  ?  279 GLN B CD    1 
ATOM   4098 O OE1   . GLN B 1 279 ? 50.081 -2.109  -2.815  1.00 74.35  ?  279 GLN B OE1   1 
ATOM   4099 N NE2   . GLN B 1 279 ? 51.037 -2.067  -4.867  1.00 65.62  ?  279 GLN B NE2   1 
ATOM   4100 N N     . ARG B 1 280 ? 52.989 2.817   -2.762  1.00 67.55  ?  280 ARG B N     1 
ATOM   4101 C CA    . ARG B 1 280 ? 52.336 3.995   -3.337  1.00 71.28  ?  280 ARG B CA    1 
ATOM   4102 C C     . ARG B 1 280 ? 51.240 3.565   -4.322  1.00 71.90  ?  280 ARG B C     1 
ATOM   4103 O O     . ARG B 1 280 ? 51.530 2.838   -5.273  1.00 69.80  ?  280 ARG B O     1 
ATOM   4104 C CB    . ARG B 1 280 ? 53.371 4.903   -4.027  1.00 66.31  ?  280 ARG B CB    1 
ATOM   4105 C CG    . ARG B 1 280 ? 52.741 5.875   -5.048  1.00 65.20  ?  280 ARG B CG    1 
ATOM   4106 C CD    . ARG B 1 280 ? 53.639 7.036   -5.490  1.00 59.30  ?  280 ARG B CD    1 
ATOM   4107 N NE    . ARG B 1 280 ? 52.884 7.920   -6.373  1.00 61.81  ?  280 ARG B NE    1 
ATOM   4108 C CZ    . ARG B 1 280 ? 53.390 8.949   -7.044  1.00 63.05  ?  280 ARG B CZ    1 
ATOM   4109 N NH1   . ARG B 1 280 ? 54.670 9.283   -6.954  1.00 62.22  ?  280 ARG B NH1   1 
ATOM   4110 N NH2   . ARG B 1 280 ? 52.592 9.663   -7.834  1.00 75.88  ?  280 ARG B NH2   1 
ATOM   4111 N N     . PRO B 1 281 ? 49.987 4.008   -4.145  1.00 72.33  ?  281 PRO B N     1 
ATOM   4112 C CA    . PRO B 1 281 ? 48.872 3.429   -4.926  1.00 73.67  ?  281 PRO B CA    1 
ATOM   4113 C C     . PRO B 1 281 ? 49.006 3.654   -6.423  1.00 75.99  ?  281 PRO B C     1 
ATOM   4114 O O     . PRO B 1 281 ? 49.590 4.644   -6.868  1.00 76.90  ?  281 PRO B O     1 
ATOM   4115 C CB    . PRO B 1 281 ? 47.636 4.148   -4.375  1.00 77.97  ?  281 PRO B CB    1 
ATOM   4116 C CG    . PRO B 1 281 ? 48.047 4.553   -2.984  1.00 78.00  ?  281 PRO B CG    1 
ATOM   4117 C CD    . PRO B 1 281 ? 49.513 4.889   -3.072  1.00 73.39  ?  281 PRO B CD    1 
ATOM   4118 N N     . GLY B 1 282 ? 48.460 2.710   -7.205  1.00 71.16  ?  282 GLY B N     1 
ATOM   4119 C CA    . GLY B 1 282 ? 48.619 2.723   -8.661  1.00 76.26  ?  282 GLY B CA    1 
ATOM   4120 C C     . GLY B 1 282 ? 49.289 1.478   -9.242  1.00 84.52  ?  282 GLY B C     1 
ATOM   4121 O O     . GLY B 1 282 ? 49.350 0.453   -8.550  1.00 82.46  ?  282 GLY B O     1 
ATOM   4122 N N     . LYS B 1 283 ? 49.660 1.535   -10.529 1.00 86.55  ?  283 LYS B N     1 
ATOM   4123 C CA    . LYS B 1 283 ? 50.235 0.372   -11.268 1.00 89.97  ?  283 LYS B CA    1 
ATOM   4124 C C     . LYS B 1 283 ? 49.316 -0.845  -11.124 1.00 102.21 ?  283 LYS B C     1 
ATOM   4125 O O     . LYS B 1 283 ? 48.113 -0.677  -10.944 1.00 106.03 ?  283 LYS B O     1 
ATOM   4126 C CB    . LYS B 1 283 ? 51.666 0.037   -10.840 1.00 85.06  ?  283 LYS B CB    1 
ATOM   4127 C CG    . LYS B 1 283 ? 52.347 -1.049  -11.663 1.00 87.60  ?  283 LYS B CG    1 
ATOM   4128 C CD    . LYS B 1 283 ? 53.524 -1.691  -10.961 1.00 88.78  ?  283 LYS B CD    1 
ATOM   4129 C CE    . LYS B 1 283 ? 54.555 -0.691  -10.485 1.00 77.06  ?  283 LYS B CE    1 
ATOM   4130 N NZ    . LYS B 1 283 ? 55.758 -1.355  -9.931  1.00 68.31  ?  283 LYS B NZ    1 
ATOM   4131 O OXT   . LYS B 1 283 ? 49.843 -1.960  -11.221 1.00 107.70 -1 283 LYS B OXT   1 
HETATM 4132 N N     . SAH C 2 .   ? 34.287 -15.773 12.241  1.00 62.11  ?  301 SAH A N     1 
HETATM 4133 C CA    . SAH C 2 .   ? 32.928 -16.360 12.148  1.00 66.24  ?  301 SAH A CA    1 
HETATM 4134 C CB    . SAH C 2 .   ? 31.831 -15.304 12.299  1.00 62.72  ?  301 SAH A CB    1 
HETATM 4135 C CG    . SAH C 2 .   ? 32.250 -13.898 11.959  1.00 62.65  ?  301 SAH A CG    1 
HETATM 4136 S SD    . SAH C 2 .   ? 30.825 -12.793 11.957  1.00 61.75  ?  301 SAH A SD    1 
HETATM 4137 C C     . SAH C 2 .   ? 32.784 -17.004 10.777  1.00 62.97  ?  301 SAH A C     1 
HETATM 4138 O O     . SAH C 2 .   ? 31.886 -17.840 10.620  1.00 73.09  ?  301 SAH A O     1 
HETATM 4139 O OXT   . SAH C 2 .   ? 33.562 -16.634 9.936   1.00 56.71  ?  301 SAH A OXT   1 
HETATM 4140 C "C5'" . SAH C 2 .   ? 30.994 -11.954 13.549  1.00 68.69  ?  301 SAH A "C5'" 1 
HETATM 4141 C "C4'" . SAH C 2 .   ? 30.888 -12.871 14.741  1.00 71.24  ?  301 SAH A "C4'" 1 
HETATM 4142 O "O4'" . SAH C 2 .   ? 31.228 -12.139 15.939  1.00 69.32  ?  301 SAH A "O4'" 1 
HETATM 4143 C "C3'" . SAH C 2 .   ? 29.495 -13.449 14.983  1.00 70.61  ?  301 SAH A "C3'" 1 
HETATM 4144 O "O3'" . SAH C 2 .   ? 29.586 -14.802 15.400  1.00 70.19  ?  301 SAH A "O3'" 1 
HETATM 4145 C "C2'" . SAH C 2 .   ? 28.969 -12.605 16.142  1.00 66.41  ?  301 SAH A "C2'" 1 
HETATM 4146 O "O2'" . SAH C 2 .   ? 28.000 -13.282 16.909  1.00 74.07  ?  301 SAH A "O2'" 1 
HETATM 4147 C "C1'" . SAH C 2 .   ? 30.258 -12.411 16.919  1.00 68.43  ?  301 SAH A "C1'" 1 
HETATM 4148 N N9    . SAH C 2 .   ? 30.226 -11.300 17.857  1.00 71.09  ?  301 SAH A N9    1 
HETATM 4149 C C8    . SAH C 2 .   ? 29.865 -10.005 17.593  1.00 75.19  ?  301 SAH A C8    1 
HETATM 4150 N N7    . SAH C 2 .   ? 29.949 -9.223  18.639  1.00 78.96  ?  301 SAH A N7    1 
HETATM 4151 C C5    . SAH C 2 .   ? 30.392 -10.056 19.655  1.00 74.36  ?  301 SAH A C5    1 
HETATM 4152 C C6    . SAH C 2 .   ? 30.681 -9.824  21.010  1.00 74.68  ?  301 SAH A C6    1 
HETATM 4153 N N6    . SAH C 2 .   ? 30.554 -8.639  21.596  1.00 79.21  ?  301 SAH A N6    1 
HETATM 4154 N N1    . SAH C 2 .   ? 31.108 -10.876 21.744  1.00 75.17  ?  301 SAH A N1    1 
HETATM 4155 C C2    . SAH C 2 .   ? 31.232 -12.066 21.148  1.00 70.38  ?  301 SAH A C2    1 
HETATM 4156 N N3    . SAH C 2 .   ? 30.989 -12.402 19.886  1.00 69.71  ?  301 SAH A N3    1 
HETATM 4157 C C4    . SAH C 2 .   ? 30.571 -11.340 19.183  1.00 70.47  ?  301 SAH A C4    1 
HETATM 4158 N N     . SAH D 2 .   ? 71.960 -1.436  4.015   1.00 65.80  ?  301 SAH B N     1 
HETATM 4159 C CA    . SAH D 2 .   ? 73.417 -1.493  3.894   1.00 68.93  ?  301 SAH B CA    1 
HETATM 4160 C CB    . SAH D 2 .   ? 74.104 -0.482  4.832   1.00 68.42  ?  301 SAH B CB    1 
HETATM 4161 C CG    . SAH D 2 .   ? 73.370 -0.187  6.138   1.00 79.63  ?  301 SAH B CG    1 
HETATM 4162 S SD    . SAH D 2 .   ? 74.460 0.726   7.301   1.00 72.85  ?  301 SAH B SD    1 
HETATM 4163 C C     . SAH D 2 .   ? 73.882 -2.875  4.224   1.00 71.66  ?  301 SAH B C     1 
HETATM 4164 O O     . SAH D 2 .   ? 75.042 -3.234  3.982   1.00 73.06  ?  301 SAH B O     1 
HETATM 4165 O OXT   . SAH D 2 .   ? 72.954 -3.539  4.731   1.00 66.87  ?  301 SAH B OXT   1 
HETATM 4166 C "C5'" . SAH D 2 .   ? 73.673 2.348   7.277   1.00 72.36  ?  301 SAH B "C5'" 1 
HETATM 4167 C "C4'" . SAH D 2 .   ? 73.891 3.025   5.953   1.00 67.23  ?  301 SAH B "C4'" 1 
HETATM 4168 O "O4'" . SAH D 2 .   ? 72.950 4.079   5.912   1.00 67.74  ?  301 SAH B "O4'" 1 
HETATM 4169 C "C3'" . SAH D 2 .   ? 75.256 3.670   5.755   1.00 69.55  ?  301 SAH B "C3'" 1 
HETATM 4170 O "O3'" . SAH D 2 .   ? 75.751 3.197   4.529   1.00 75.09  ?  301 SAH B "O3'" 1 
HETATM 4171 C "C2'" . SAH D 2 .   ? 74.949 5.164   5.693   1.00 67.63  ?  301 SAH B "C2'" 1 
HETATM 4172 O "O2'" . SAH D 2 .   ? 75.673 5.863   4.744   1.00 66.41  ?  301 SAH B "O2'" 1 
HETATM 4173 C "C1'" . SAH D 2 .   ? 73.508 5.164   5.232   1.00 67.73  ?  301 SAH B "C1'" 1 
HETATM 4174 N N9    . SAH D 2 .   ? 72.865 6.399   5.557   1.00 67.34  ?  301 SAH B N9    1 
HETATM 4175 C C8    . SAH D 2 .   ? 72.576 6.872   6.825   1.00 73.43  ?  301 SAH B C8    1 
HETATM 4176 N N7    . SAH D 2 .   ? 71.984 8.039   6.846   1.00 79.48  ?  301 SAH B N7    1 
HETATM 4177 C C5    . SAH D 2 .   ? 71.864 8.375   5.507   1.00 72.77  ?  301 SAH B C5    1 
HETATM 4178 C C6    . SAH D 2 .   ? 71.318 9.503   4.847   1.00 72.44  ?  301 SAH B C6    1 
HETATM 4179 N N6    . SAH D 2 .   ? 70.773 10.522  5.508   1.00 74.35  ?  301 SAH B N6    1 
HETATM 4180 N N1    . SAH D 2 .   ? 71.334 9.553   3.509   1.00 74.88  ?  301 SAH B N1    1 
HETATM 4181 C C2    . SAH D 2 .   ? 71.885 8.509   2.880   1.00 70.37  ?  301 SAH B C2    1 
HETATM 4182 N N3    . SAH D 2 .   ? 72.446 7.389   3.377   1.00 67.20  ?  301 SAH B N3    1 
HETATM 4183 C C4    . SAH D 2 .   ? 72.409 7.364   4.697   1.00 67.93  ?  301 SAH B C4    1 
HETATM 4184 C C1    . MQA E 3 .   ? 74.712 0.645   11.107  1.00 102.88 ?  302 MQA B C1    1 
HETATM 4185 C C2    . MQA E 3 .   ? 73.352 0.745   11.708  1.00 98.78  ?  302 MQA B C2    1 
HETATM 4186 C C3    . MQA E 3 .   ? 73.610 0.469   13.227  1.00 100.39 ?  302 MQA B C3    1 
HETATM 4187 C C5    . MQA E 3 .   ? 73.768 -2.647  13.593  1.00 103.87 ?  302 MQA B C5    1 
HETATM 4188 C C6    . MQA E 3 .   ? 74.180 -4.152  13.422  1.00 99.90  ?  302 MQA B C6    1 
HETATM 4189 C C7    . MQA E 3 .   ? 75.544 -4.560  12.719  1.00 105.11 ?  302 MQA B C7    1 
HETATM 4190 C C8    . MQA E 3 .   ? 76.498 -3.447  12.168  1.00 109.36 ?  302 MQA B C8    1 
HETATM 4191 C C9    . MQA E 3 .   ? 76.782 -0.502  11.965  1.00 106.00 ?  302 MQA B C9    1 
HETATM 4192 C C10   . MQA E 3 .   ? 77.442 -0.455  10.631  1.00 102.88 ?  302 MQA B C10   1 
HETATM 4193 C C11   . MQA E 3 .   ? 79.602 0.079   11.791  1.00 112.95 ?  302 MQA B C11   1 
HETATM 4194 O O5    . MQA E 3 .   ? 72.751 -2.303  14.133  1.00 102.81 ?  302 MQA B O5    1 
HETATM 4195 C CM6   . MQA E 3 .   ? 73.249 -5.258  13.952  1.00 94.97  ?  302 MQA B CM6   1 
HETATM 4196 O O7    . MQA E 3 .   ? 75.971 -5.921  12.580  1.00 106.65 ?  302 MQA B O7    1 
HETATM 4197 C C24   . MQA E 3 .   ? 76.490 -6.510  13.771  1.00 106.75 ?  302 MQA B C24   1 
HETATM 4198 O O8    . MQA E 3 .   ? 77.517 -3.798  11.635  1.00 111.42 ?  302 MQA B O8    1 
HETATM 4199 C C4A   . MQA E 3 .   ? 74.712 -1.601  13.103  1.00 104.28 ?  302 MQA B C4A   1 
HETATM 4200 C C8A   . MQA E 3 .   ? 76.128 -1.975  12.313  1.00 106.52 ?  302 MQA B C8A   1 
HETATM 4201 N N4    . MQA E 3 .   ? 74.696 -0.355  12.991  1.00 104.65 ?  302 MQA B N4    1 
HETATM 4202 C C9A   . MQA E 3 .   ? 75.641 0.456   12.206  1.00 106.34 ?  302 MQA B C9A   1 
HETATM 4203 O O24   . MQA E 3 .   ? 76.016 1.658   12.935  1.00 102.03 ?  302 MQA B O24   1 
HETATM 4204 C C25   . MQA E 3 .   ? 77.104 2.439   12.482  1.00 98.26  ?  302 MQA B C25   1 
HETATM 4205 N N2    . MQA E 3 .   ? 73.536 0.066   10.409  1.00 94.10  ?  302 MQA B N2    1 
HETATM 4206 O O10   . MQA E 3 .   ? 78.778 0.098   10.616  1.00 104.63 ?  302 MQA B O10   1 
HETATM 4207 O O11   . MQA E 3 .   ? 79.666 -0.894  12.491  1.00 114.43 ?  302 MQA B O11   1 
HETATM 4208 N N12   . MQA E 3 .   ? 80.394 1.278   12.138  1.00 115.06 ?  302 MQA B N12   1 
HETATM 4209 O O     . HOH F 4 .   ? 34.528 -24.524 4.294   1.00 60.80  ?  401 HOH A O     1 
HETATM 4210 O O     . HOH F 4 .   ? 39.289 -30.421 28.095  1.00 56.77  ?  402 HOH A O     1 
HETATM 4211 O O     . HOH G 4 .   ? 62.429 6.534   23.965  1.00 98.81  ?  401 HOH B O     1 
HETATM 4212 O O     . HOH G 4 .   ? 62.333 -5.812  28.356  1.00 76.42  ?  402 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     . LEU A 6   ? 1.3058 0.7063 1.3193 0.0040  0.3967  -0.0939 6   LEU A N     
2    C CA    . LEU A 6   ? 1.4414 0.8424 1.4283 -0.0006 0.3923  -0.1050 6   LEU A CA    
3    C C     . LEU A 6   ? 1.5008 0.8916 1.5027 0.0100  0.4142  -0.0974 6   LEU A C     
4    O O     . LEU A 6   ? 1.6685 1.0278 1.6618 0.0069  0.4392  -0.1101 6   LEU A O     
5    C CB    . LEU A 6   ? 1.4283 0.8061 1.3752 -0.0178 0.3954  -0.1321 6   LEU A CB    
6    C CG    . LEU A 6   ? 1.4937 0.8829 1.4061 -0.0280 0.3771  -0.1447 6   LEU A CG    
7    C CD1   . LEU A 6   ? 1.4636 0.8293 1.3400 -0.0462 0.3828  -0.1695 6   LEU A CD1   
8    C CD2   . LEU A 6   ? 1.4442 0.8372 1.3564 -0.0213 0.3825  -0.1403 6   LEU A CD2   
9    N N     . SER A 7   ? 1.4192 0.8361 1.4410 0.0212  0.4049  -0.0782 7   SER A N     
10   C CA    . SER A 7   ? 1.4978 0.9107 1.5450 0.0342  0.4253  -0.0639 7   SER A CA    
11   C C     . SER A 7   ? 1.6654 1.0687 1.7514 0.0451  0.4464  -0.0476 7   SER A C     
12   O O     . SER A 7   ? 1.7379 1.1225 1.8408 0.0533  0.4734  -0.0428 7   SER A O     
13   C CB    . SER A 7   ? 1.5515 0.9378 1.5749 0.0297  0.4450  -0.0814 7   SER A CB    
14   O OG    . SER A 7   ? 1.4764 0.8538 1.5264 0.0426  0.4698  -0.0684 7   SER A OG    
15   N N     . GLU A 8   ? 1.6312 1.0477 1.7325 0.0453  0.4349  -0.0382 8   GLU A N     
16   C CA    . GLU A 8   ? 1.5244 0.9375 1.6662 0.0559  0.4516  -0.0188 8   GLU A CA    
17   C C     . GLU A 8   ? 1.5783 1.0104 1.7577 0.0715  0.4587  0.0087  8   GLU A C     
18   O O     . GLU A 8   ? 1.4931 0.9142 1.7064 0.0819  0.4824  0.0236  8   GLU A O     
19   C CB    . GLU A 8   ? 1.3881 0.8215 1.5398 0.0534  0.4323  -0.0102 8   GLU A CB    
20   C CG    . GLU A 8   ? 1.3984 0.8141 1.5196 0.0389  0.4268  -0.0337 8   GLU A CG    
21   C CD    . GLU A 8   ? 1.3944 0.8369 1.4927 0.0302  0.3938  -0.0393 8   GLU A CD    
22   O OE1   . GLU A 8   ? 1.3801 0.8560 1.4959 0.0363  0.3759  -0.0204 8   GLU A OE1   
23   O OE2   . GLU A 8   ? 1.3810 0.8115 1.4441 0.0169  0.3865  -0.0621 8   GLU A OE2   
24   N N     . LEU A 9   ? 1.5554 1.0184 1.7315 0.0730  0.4375  0.0175  9   LEU A N     
25   C CA    . LEU A 9   ? 1.4999 0.9810 1.7030 0.0850  0.4423  0.0396  9   LEU A CA    
26   C C     . LEU A 9   ? 1.5085 0.9686 1.6929 0.0847  0.4580  0.0257  9   LEU A C     
27   O O     . LEU A 9   ? 1.5521 0.9949 1.6970 0.0732  0.4545  -0.0002 9   LEU A O     
28   C CB    . LEU A 9   ? 1.4550 0.9778 1.6604 0.0845  0.4118  0.0535  9   LEU A CB    
29   C CG    . LEU A 9   ? 1.4742 1.0253 1.7145 0.0900  0.4028  0.0795  9   LEU A CG    
30   C CD1   . LEU A 9   ? 1.3881 0.9771 1.6222 0.0854  0.3711  0.0870  9   LEU A CD1   
31   C CD2   . LEU A 9   ? 1.4794 1.0362 1.7657 0.1045  0.4238  0.1078  9   LEU A CD2   
32   N N     . PRO A 10  ? 1.5274 0.9898 1.7402 0.0970  0.4756  0.0435  10  PRO A N     
33   C CA    . PRO A 10  ? 1.5429 0.9891 1.7391 0.0973  0.4896  0.0323  10  PRO A CA    
34   C C     . PRO A 10  ? 1.5480 1.0163 1.7162 0.0899  0.4622  0.0254  10  PRO A C     
35   O O     . PRO A 10  ? 1.4892 0.9920 1.6692 0.0920  0.4391  0.0420  10  PRO A O     
36   C CB    . PRO A 10  ? 1.5092 0.9626 1.7494 0.1136  0.5099  0.0594  10  PRO A CB    
37   C CG    . PRO A 10  ? 1.4455 0.9109 1.7250 0.1212  0.5121  0.0823  10  PRO A CG    
38   C CD    . PRO A 10  ? 1.4697 0.9531 1.7317 0.1109  0.4822  0.0764  10  PRO A CD    
39   N N     . MET A 11  ? 1.5986 1.0472 1.7293 0.0806  0.4649  0.0009  11  MET A N     
40   C CA    . MET A 11  ? 1.5483 1.0188 1.6579 0.0754  0.4410  -0.0021 11  MET A CA    
41   C C     . MET A 11  ? 1.5908 1.0525 1.6951 0.0790  0.4564  -0.0040 11  MET A C     
42   O O     . MET A 11  ? 1.6358 1.0658 1.7239 0.0758  0.4798  -0.0211 11  MET A O     
43   C CB    . MET A 11  ? 1.4909 0.9569 1.5593 0.0600  0.4217  -0.0261 11  MET A CB    
44   C CG    . MET A 11  ? 1.3901 0.8719 1.4638 0.0567  0.4017  -0.0221 11  MET A CG    
45   S SD    . MET A 11  ? 1.2710 0.7493 1.2991 0.0394  0.3799  -0.0483 11  MET A SD    
46   C CE    . MET A 11  ? 1.3690 0.8099 1.3649 0.0309  0.4036  -0.0735 11  MET A CE    
47   N N     . PRO A 12  ? 1.5447 1.0334 1.6634 0.0854  0.4456  0.0135  12  PRO A N     
48   C CA    . PRO A 12  ? 1.5081 0.9910 1.6201 0.0881  0.4580  0.0118  12  PRO A CA    
49   C C     . PRO A 12  ? 1.4229 0.8963 1.4891 0.0746  0.4479  -0.0135 12  PRO A C     
50   O O     . PRO A 12  ? 1.4150 0.8931 1.4574 0.0640  0.4268  -0.0260 12  PRO A O     
51   C CB    . PRO A 12  ? 1.4450 0.9640 1.5834 0.0963  0.4430  0.0378  12  PRO A CB    
52   C CG    . PRO A 12  ? 1.4096 0.9533 1.5515 0.0923  0.4154  0.0445  12  PRO A CG    
53   C CD    . PRO A 12  ? 1.4570 0.9830 1.5998 0.0899  0.4227  0.0366  12  PRO A CD    
54   N N     . SER A 13  ? 1.4206 0.8798 1.4753 0.0750  0.4650  -0.0206 13  SER A N     
55   C CA    . SER A 13  ? 1.4278 0.8799 1.4395 0.0619  0.4565  -0.0427 13  SER A CA    
56   C C     . SER A 13  ? 1.3834 0.8573 1.3977 0.0657  0.4469  -0.0314 13  SER A C     
57   O O     . SER A 13  ? 1.3804 0.8464 1.4047 0.0727  0.4681  -0.0261 13  SER A O     
58   C CB    . SER A 13  ? 1.4577 0.8738 1.4470 0.0557  0.4840  -0.0639 13  SER A CB    
59   O OG    . SER A 13  ? 1.5973 0.9965 1.5646 0.0440  0.4816  -0.0828 13  SER A OG    
60   N N     . PRO A 14  ? 1.3265 0.8267 1.3329 0.0614  0.4167  -0.0275 14  PRO A N     
61   C CA    . PRO A 14  ? 1.2819 0.8032 1.2917 0.0644  0.4064  -0.0163 14  PRO A CA    
62   C C     . PRO A 14  ? 1.2836 0.7892 1.2656 0.0587  0.4188  -0.0312 14  PRO A C     
63   O O     . PRO A 14  ? 1.3050 0.7906 1.2552 0.0477  0.4236  -0.0531 14  PRO A O     
64   C CB    . PRO A 14  ? 1.2235 0.7684 1.2227 0.0575  0.3730  -0.0161 14  PRO A CB    
65   C CG    . PRO A 14  ? 1.2070 0.7466 1.2051 0.0537  0.3668  -0.0226 14  PRO A CG    
66   C CD    . PRO A 14  ? 1.2373 0.7453 1.2262 0.0517  0.3923  -0.0370 14  PRO A CD    
67   N N     . ALA A 15  ? 1.2549 0.7704 1.2496 0.0658  0.4250  -0.0185 15  ALA A N     
68   C CA    . ALA A 15  ? 1.3043 0.8151 1.2723 0.0596  0.4281  -0.0291 15  ALA A CA    
69   C C     . ALA A 15  ? 1.2666 0.8045 1.2273 0.0553  0.3977  -0.0234 15  ALA A C     
70   O O     . ALA A 15  ? 1.2984 0.8597 1.2851 0.0622  0.3839  -0.0042 15  ALA A O     
71   C CB    . ALA A 15  ? 1.3906 0.8964 1.3761 0.0695  0.4531  -0.0187 15  ALA A CB    
72   N N     . SER A 16  ? 1.2283 0.7636 1.1541 0.0433  0.3871  -0.0396 16  SER A N     
73   C CA    . SER A 16  ? 1.2767 0.8365 1.1976 0.0397  0.3591  -0.0338 16  SER A CA    
74   C C     . SER A 16  ? 1.3008 0.8778 1.2414 0.0478  0.3590  -0.0155 16  SER A C     
75   O O     . SER A 16  ? 1.2903 0.8899 1.2401 0.0484  0.3374  -0.0043 16  SER A O     
76   C CB    . SER A 16  ? 1.2198 0.7758 1.1025 0.0259  0.3480  -0.0518 16  SER A CB    
77   O OG    . SER A 16  ? 1.4237 0.9607 1.2844 0.0205  0.3684  -0.0649 16  SER A OG    
78   N N     . GLU A 17  ? 1.3089 0.8756 1.2578 0.0541  0.3837  -0.0116 17  GLU A N     
79   C CA    . GLU A 17  ? 1.2720 0.8562 1.2444 0.0630  0.3851  0.0083  17  GLU A CA    
80   C C     . GLU A 17  ? 1.3295 0.9310 1.3410 0.0732  0.3807  0.0303  17  GLU A C     
81   O O     . GLU A 17  ? 1.3117 0.9372 1.3405 0.0764  0.3669  0.0473  17  GLU A O     
82   C CB    . GLU A 17  ? 1.3943 0.9627 1.3657 0.0673  0.4144  0.0066  17  GLU A CB    
83   C CG    . GLU A 17  ? 1.3779 0.9642 1.3690 0.0749  0.4166  0.0257  17  GLU A CG    
84   C CD    . GLU A 17  ? 1.4928 1.0946 1.4641 0.0670  0.3957  0.0242  17  GLU A CD    
85   O OE1   . GLU A 17  ? 1.4855 1.0826 1.4261 0.0556  0.3826  0.0075  17  GLU A OE1   
86   O OE2   . GLU A 17  ? 1.5853 1.2050 1.5733 0.0721  0.3923  0.0407  17  GLU A OE2   
87   N N     . GLU A 18  ? 1.3241 0.9148 1.3501 0.0777  0.3922  0.0308  18  GLU A N     
88   C CA    . GLU A 18  ? 1.3068 0.9154 1.3714 0.0873  0.3898  0.0536  18  GLU A CA    
89   C C     . GLU A 18  ? 1.2895 0.9204 1.3559 0.0823  0.3595  0.0585  18  GLU A C     
90   O O     . GLU A 18  ? 1.2704 0.9254 1.3642 0.0871  0.3501  0.0794  18  GLU A O     
91   C CB    . GLU A 18  ? 1.2946 0.8851 1.3758 0.0938  0.4118  0.0540  18  GLU A CB    
92   C CG    . GLU A 18  ? 1.3359 0.9057 1.4252 0.1015  0.4453  0.0541  18  GLU A CG    
93   C CD    . GLU A 18  ? 1.3840 0.9311 1.4858 0.1063  0.4677  0.0506  18  GLU A CD    
94   O OE1   . GLU A 18  ? 1.3968 0.9459 1.5017 0.1038  0.4562  0.0493  18  GLU A OE1   
95   O OE2   . GLU A 18  ? 1.3702 0.8969 1.4788 0.1125  0.4976  0.0491  18  GLU A OE2   
96   N N     . VAL A 19  ? 1.2900 0.9137 1.3278 0.0721  0.3447  0.0398  19  VAL A N     
97   C CA    . VAL A 19  ? 1.2315 0.8744 1.2692 0.0670  0.3172  0.0424  19  VAL A CA    
98   C C     . VAL A 19  ? 1.1951 0.8578 1.2296 0.0640  0.2992  0.0491  19  VAL A C     
99   O O     . VAL A 19  ? 1.1760 0.8605 1.2247 0.0634  0.2813  0.0611  19  VAL A O     
100  C CB    . VAL A 19  ? 1.1697 0.7990 1.1800 0.0578  0.3085  0.0214  19  VAL A CB    
101  C CG1   . VAL A 19  ? 1.1674 0.7784 1.1839 0.0606  0.3255  0.0164  19  VAL A CG1   
102  C CG2   . VAL A 19  ? 1.2491 0.8647 1.2256 0.0496  0.3097  0.0031  19  VAL A CG2   
103  N N     . GLY A 20  ? 1.1742 0.8299 1.1906 0.0614  0.3044  0.0419  20  GLY A N     
104  C CA    . GLY A 20  ? 1.2105 0.8844 1.2287 0.0600  0.2909  0.0511  20  GLY A CA    
105  C C     . GLY A 20  ? 1.1616 0.8537 1.2133 0.0685  0.2953  0.0749  20  GLY A C     
106  O O     . GLY A 20  ? 1.0701 0.7841 1.1341 0.0669  0.2777  0.0871  20  GLY A O     
107  N N     . ALA A 21  ? 1.1997 0.8832 1.2671 0.0771  0.3197  0.0820  21  ALA A N     
108  C CA    . ALA A 21  ? 1.1858 0.8881 1.2890 0.0858  0.3254  0.1070  21  ALA A CA    
109  C C     . ALA A 21  ? 1.1806 0.9014 1.3052 0.0860  0.3114  0.1197  21  ALA A C     
110  O O     . ALA A 21  ? 1.1502 0.8959 1.2993 0.0881  0.3035  0.1406  21  ALA A O     
111  C CB    . ALA A 21  ? 1.2909 0.9779 1.4093 0.0959  0.3564  0.1117  21  ALA A CB    
112  N N     . LEU A 22  ? 1.1784 0.8885 1.2936 0.0830  0.3080  0.1076  22  LEU A N     
113  C CA    . LEU A 22  ? 1.1545 0.8819 1.2869 0.0820  0.2942  0.1180  22  LEU A CA    
114  C C     . LEU A 22  ? 1.1289 0.8752 1.2515 0.0728  0.2663  0.1173  22  LEU A C     
115  O O     . LEU A 22  ? 1.0674 0.8383 1.2103 0.0718  0.2544  0.1342  22  LEU A O     
116  C CB    . LEU A 22  ? 1.1135 0.8230 1.2372 0.0811  0.2991  0.1044  22  LEU A CB    
117  C CG    . LEU A 22  ? 1.0247 0.7519 1.1639 0.0793  0.2846  0.1139  22  LEU A CG    
118  C CD1   . LEU A 22  ? 1.0054 0.7515 1.1838 0.0878  0.2935  0.1409  22  LEU A CD1   
119  C CD2   . LEU A 22  ? 1.0403 0.7487 1.1659 0.0769  0.2873  0.0977  22  LEU A CD2   
120  N N     . TYR A 23  ? 1.1179 0.8533 1.2100 0.0653  0.2558  0.0979  23  TYR A N     
121  C CA    . TYR A 23  ? 1.1109 0.8619 1.1949 0.0571  0.2313  0.0969  23  TYR A CA    
122  C C     . TYR A 23  ? 1.1060 0.8721 1.1973 0.0565  0.2264  0.1089  23  TYR A C     
123  O O     . TYR A 23  ? 1.1135 0.8982 1.2102 0.0510  0.2087  0.1161  23  TYR A O     
124  C CB    . TYR A 23  ? 1.0997 0.8357 1.1520 0.0497  0.2215  0.0743  23  TYR A CB    
125  C CG    . TYR A 23  ? 1.0661 0.7964 1.1139 0.0474  0.2172  0.0653  23  TYR A CG    
126  C CD1   . TYR A 23  ? 1.0723 0.8203 1.1348 0.0455  0.2044  0.0743  23  TYR A CD1   
127  C CD2   . TYR A 23  ? 1.0591 0.7676 1.0873 0.0461  0.2256  0.0480  23  TYR A CD2   
128  C CE1   . TYR A 23  ? 1.0339 0.7777 1.0928 0.0435  0.2006  0.0668  23  TYR A CE1   
129  C CE2   . TYR A 23  ? 1.0863 0.7902 1.1110 0.0438  0.2215  0.0403  23  TYR A CE2   
130  C CZ    . TYR A 23  ? 1.0562 0.7778 1.0968 0.0430  0.2091  0.0500  23  TYR A CZ    
131  O OH    . TYR A 23  ? 1.0587 0.7767 1.0962 0.0407  0.2051  0.0430  23  TYR A OH    
132  N N     . ASP A 24  ? 1.1329 0.8914 1.2247 0.0616  0.2423  0.1115  24  ASP A N     
133  C CA    . ASP A 24  ? 1.1181 0.8930 1.2220 0.0621  0.2394  0.1265  24  ASP A CA    
134  C C     . ASP A 24  ? 1.0997 0.9002 1.2346 0.0637  0.2341  0.1492  24  ASP A C     
135  O O     . ASP A 24  ? 1.1058 0.9254 1.2452 0.0573  0.2169  0.1571  24  ASP A O     
136  C CB    . ASP A 24  ? 1.0811 0.8453 1.1865 0.0692  0.2613  0.1288  24  ASP A CB    
137  C CG    . ASP A 24  ? 1.0079 0.7573 1.0833 0.0645  0.2607  0.1118  24  ASP A CG    
138  O OD1   . ASP A 24  ? 1.0327 0.7870 1.0934 0.0566  0.2411  0.1050  24  ASP A OD1   
139  O OD2   . ASP A 24  ? 1.0715 0.8047 1.1382 0.0682  0.2799  0.1055  24  ASP A OD2   
140  N N     . ARG A 25  ? 1.0802 0.8815 1.2365 0.0713  0.2485  0.1598  25  ARG A N     
141  C CA    . ARG A 25  ? 1.1097 0.9381 1.2967 0.0723  0.2433  0.1833  25  ARG A CA    
142  C C     . ARG A 25  ? 1.1082 0.9505 1.2898 0.0622  0.2200  0.1806  25  ARG A C     
143  O O     . ARG A 25  ? 1.0764 0.9447 1.2738 0.0572  0.2076  0.1969  25  ARG A O     
144  C CB    . ARG A 25  ? 1.1055 0.9307 1.3169 0.0827  0.2639  0.1949  25  ARG A CB    
145  C CG    . ARG A 25  ? 1.1349 0.9823 1.3820 0.0898  0.2736  0.2236  25  ARG A CG    
146  C CD    . ARG A 25  ? 1.1903 1.0275 1.4605 0.1025  0.3000  0.2329  25  ARG A CD    
147  N NE    . ARG A 25  ? 1.3171 1.1193 1.5649 0.1066  0.3183  0.2107  25  ARG A NE    
148  C CZ    . ARG A 25  ? 1.2996 1.0800 1.5413 0.1093  0.3296  0.1981  25  ARG A CZ    
149  N NH1   . ARG A 25  ? 1.2765 1.0660 1.5345 0.1099  0.3255  0.2065  25  ARG A NH1   
150  N NH2   . ARG A 25  ? 1.2883 1.0376 1.5067 0.1108  0.3457  0.1771  25  ARG A NH2   
151  N N     . PHE A 26  ? 1.0977 0.9240 1.2571 0.0583  0.2140  0.1605  26  PHE A N     
152  C CA    . PHE A 26  ? 1.0620 0.9009 1.2166 0.0491  0.1935  0.1575  26  PHE A CA    
153  C C     . PHE A 26  ? 1.1421 0.9890 1.2832 0.0395  0.1753  0.1529  26  PHE A C     
154  O O     . PHE A 26  ? 1.1518 1.0206 1.3021 0.0322  0.1610  0.1630  26  PHE A O     
155  C CB    . PHE A 26  ? 1.0484 0.8683 1.1836 0.0477  0.1924  0.1376  26  PHE A CB    
156  C CG    . PHE A 26  ? 1.0822 0.9003 1.2338 0.0539  0.2044  0.1442  26  PHE A CG    
157  C CD1   . PHE A 26  ? 1.1018 0.9433 1.2841 0.0566  0.2061  0.1679  26  PHE A CD1   
158  C CD2   . PHE A 26  ? 1.0931 0.8871 1.2305 0.0566  0.2141  0.1277  26  PHE A CD2   
159  C CE1   . PHE A 26  ? 1.0737 0.9139 1.2733 0.0628  0.2177  0.1755  26  PHE A CE1   
160  C CE2   . PHE A 26  ? 1.1074 0.8983 1.2610 0.0623  0.2259  0.1339  26  PHE A CE2   
161  C CZ    . PHE A 26  ? 1.1015 0.9153 1.2869 0.0659  0.2280  0.1581  26  PHE A CZ    
162  N N     . THR A 27  ? 1.1191 0.9486 1.2385 0.0390  0.1761  0.1380  27  THR A N     
163  C CA    . THR A 27  ? 1.1119 0.9440 1.2157 0.0301  0.1590  0.1300  27  THR A CA    
164  C C     . THR A 27  ? 1.0966 0.9496 1.2159 0.0265  0.1529  0.1471  27  THR A C     
165  O O     . THR A 27  ? 1.1229 0.9870 1.2392 0.0170  0.1365  0.1469  27  THR A O     
166  C CB    . THR A 27  ? 1.0672 0.8778 1.1470 0.0310  0.1629  0.1132  27  THR A CB    
167  O OG1   . THR A 27  ? 1.0830 0.8761 1.1471 0.0320  0.1662  0.0969  27  THR A OG1   
168  C CG2   . THR A 27  ? 1.1349 0.9481 1.2019 0.0228  0.1466  0.1070  27  THR A CG2   
169  N N     . ALA A 28  ? 1.0945 0.9525 1.2302 0.0336  0.1665  0.1618  28  ALA A N     
170  C CA    . ALA A 28  ? 1.1592 1.0386 1.3118 0.0306  0.1619  0.1801  28  ALA A CA    
171  C C     . ALA A 28  ? 1.1684 1.0744 1.3469 0.0282  0.1579  0.2007  28  ALA A C     
172  O O     . ALA A 28  ? 1.1754 1.1029 1.3669 0.0223  0.1499  0.2159  28  ALA A O     
173  C CB    . ALA A 28  ? 1.1140 0.9886 1.2737 0.0393  0.1788  0.1879  28  ALA A CB    
174  N N     . LEU A 29  ? 1.1491 1.0553 1.3354 0.0319  0.1628  0.2022  29  LEU A N     
175  C CA    . LEU A 29  ? 1.1401 1.0735 1.3484 0.0275  0.1559  0.2207  29  LEU A CA    
176  C C     . LEU A 29  ? 1.1683 1.1125 1.3639 0.0129  0.1341  0.2136  29  LEU A C     
177  O O     . LEU A 29  ? 1.1763 1.1447 1.3863 0.0062  0.1258  0.2274  29  LEU A O     
178  C CB    . LEU A 29  ? 1.0993 1.0287 1.3191 0.0355  0.1675  0.2239  29  LEU A CB    
179  N N     . GLY A 30  ? 1.1534 1.0808 1.3232 0.0075  0.1252  0.1930  30  GLY A N     
180  C CA    . GLY A 30  ? 1.0759 1.0082 1.2317 -0.0056 0.1069  0.1828  30  GLY A CA    
181  C C     . GLY A 30  ? 1.0584 0.9828 1.2038 -0.0066 0.1037  0.1698  30  GLY A C     
182  O O     . GLY A 30  ? 1.0431 0.9672 1.1740 -0.0165 0.0902  0.1578  30  GLY A O     
183  N N     . ALA A 31  ? 1.0739 0.9912 1.2267 0.0034  0.1166  0.1717  31  ALA A N     
184  C CA    . ALA A 31  ? 1.0596 0.9693 1.2042 0.0034  0.1150  0.1605  31  ALA A CA    
185  C C     . ALA A 31  ? 1.0664 0.9533 1.1828 0.0007  0.1088  0.1354  31  ALA A C     
186  O O     . ALA A 31  ? 1.0800 0.9705 1.1853 -0.0087 0.0953  0.1264  31  ALA A O     
187  C CB    . ALA A 31  ? 1.0822 0.9832 1.2391 0.0156  0.1327  0.1658  31  ALA A CB    
188  N N     . ALA A 32  ? 1.0121 0.8766 1.1169 0.0083  0.1189  0.1247  32  ALA A N     
189  C CA    . ALA A 32  ? 1.0295 0.8742 1.1091 0.0060  0.1135  0.1033  32  ALA A CA    
190  C C     . ALA A 32  ? 1.0553 0.9033 1.1287 -0.0006 0.1036  0.1023  32  ALA A C     
191  O O     . ALA A 32  ? 1.0525 0.8906 1.1197 0.0026  0.1083  0.0999  32  ALA A O     
192  C CB    . ALA A 32  ? 1.0284 0.8508 1.0979 0.0147  0.1277  0.0938  32  ALA A CB    
193  N N     . SER A 33  ? 0.9929 0.8552 1.0681 -0.0106 0.0901  0.1042  33  SER A N     
194  C CA    . SER A 33  ? 0.9793 0.8452 1.0507 -0.0181 0.0809  0.1042  33  SER A CA    
195  C C     . SER A 33  ? 0.9303 0.7780 0.9810 -0.0206 0.0745  0.0851  33  SER A C     
196  O O     . SER A 33  ? 0.9148 0.7508 0.9544 -0.0183 0.0750  0.0724  33  SER A O     
197  C CB    . SER A 33  ? 0.8849 0.7733 0.9664 -0.0293 0.0703  0.1144  33  SER A CB    
198  O OG    . SER A 33  ? 0.9597 0.8595 1.0516 -0.0324 0.0693  0.1276  33  SER A OG    
199  N N     . LEU A 34  ? 0.9268 0.7732 0.9741 -0.0253 0.0690  0.0845  34  LEU A N     
200  C CA    . LEU A 34  ? 0.9306 0.7612 0.9620 -0.0272 0.0636  0.0695  34  LEU A CA    
201  C C     . LEU A 34  ? 0.8874 0.7139 0.9094 -0.0323 0.0560  0.0563  34  LEU A C     
202  O O     . LEU A 34  ? 0.7917 0.6294 0.8173 -0.0411 0.0487  0.0576  34  LEU A O     
203  C CB    . LEU A 34  ? 0.9112 0.7452 0.9452 -0.0337 0.0577  0.0740  34  LEU A CB    
204  C CG    . LEU A 34  ? 0.9958 0.8258 1.0321 -0.0268 0.0658  0.0811  34  LEU A CG    
205  C CD1   . LEU A 34  ? 1.0245 0.8680 1.0734 -0.0319 0.0635  0.0954  34  LEU A CD1   
206  C CD2   . LEU A 34  ? 0.8754 0.6875 0.8967 -0.0239 0.0657  0.0689  34  LEU A CD2   
207  N N     . GLY A 35  ? 0.9401 0.7513 0.9497 -0.0274 0.0580  0.0437  35  GLY A N     
208  C CA    . GLY A 35  ? 0.9014 0.7073 0.9019 -0.0316 0.0511  0.0307  35  GLY A CA    
209  C C     . GLY A 35  ? 0.8728 0.6839 0.8743 -0.0312 0.0519  0.0288  35  GLY A C     
210  O O     . GLY A 35  ? 0.8631 0.6739 0.8592 -0.0363 0.0456  0.0199  35  GLY A O     
211  N N     . GLU A 36  ? 0.8576 0.6730 0.8665 -0.0251 0.0601  0.0370  36  GLU A N     
212  C CA    . GLU A 36  ? 0.8893 0.7101 0.9015 -0.0242 0.0618  0.0373  36  GLU A CA    
213  C C     . GLU A 36  ? 0.8473 0.6532 0.8516 -0.0160 0.0702  0.0296  36  GLU A C     
214  O O     . GLU A 36  ? 0.8132 0.6091 0.8138 -0.0104 0.0777  0.0295  36  GLU A O     
215  C CB    . GLU A 36  ? 0.8580 0.6970 0.8882 -0.0244 0.0653  0.0548  36  GLU A CB    
216  C CG    . GLU A 36  ? 0.9291 0.7840 0.9656 -0.0345 0.0564  0.0624  36  GLU A CG    
217  C CD    . GLU A 36  ? 0.9244 0.8011 0.9804 -0.0356 0.0587  0.0824  36  GLU A CD    
218  O OE1   . GLU A 36  ? 0.9540 0.8297 1.0199 -0.0269 0.0691  0.0924  36  GLU A OE1   
219  O OE2   . GLU A 36  ? 0.8938 0.7891 0.9552 -0.0455 0.0508  0.0884  36  GLU A OE2   
220  N N     . ASN A 37  ? 0.8448 0.6493 0.8450 -0.0165 0.0687  0.0226  37  ASN A N     
221  C CA    . ASN A 37  ? 0.8176 0.6089 0.8102 -0.0104 0.0761  0.0150  37  ASN A CA    
222  C C     . ASN A 37  ? 0.8461 0.6414 0.8515 -0.0052 0.0868  0.0255  37  ASN A C     
223  O O     . ASN A 37  ? 0.8341 0.6448 0.8530 -0.0073 0.0851  0.0358  37  ASN A O     
224  C CB    . ASN A 37  ? 0.8262 0.6141 0.8093 -0.0134 0.0696  0.0029  37  ASN A CB    
225  C CG    . ASN A 37  ? 0.8227 0.6021 0.7930 -0.0161 0.0624  -0.0084 37  ASN A CG    
226  O OD1   . ASN A 37  ? 0.8865 0.6557 0.8492 -0.0133 0.0650  -0.0118 37  ASN A OD1   
227  N ND2   . ASN A 37  ? 0.8508 0.6348 0.8193 -0.0217 0.0539  -0.0140 37  ASN A ND2   
228  N N     . LEU A 38  ? 0.8252 0.6072 0.8270 0.0012  0.0986  0.0238  38  LEU A N     
229  C CA    . LEU A 38  ? 0.8406 0.6210 0.8534 0.0072  0.1115  0.0310  38  LEU A CA    
230  C C     . LEU A 38  ? 0.8221 0.5897 0.8245 0.0082  0.1149  0.0191  38  LEU A C     
231  O O     . LEU A 38  ? 0.8546 0.6062 0.8486 0.0117  0.1257  0.0125  38  LEU A O     
232  C CB    . LEU A 38  ? 0.8475 0.6207 0.8640 0.0131  0.1248  0.0369  38  LEU A CB    
233  C CG    . LEU A 38  ? 0.8229 0.6089 0.8505 0.0124  0.1224  0.0497  38  LEU A CG    
234  C CD1   . LEU A 38  ? 0.8729 0.6471 0.8932 0.0162  0.1317  0.0478  38  LEU A CD1   
235  C CD2   . LEU A 38  ? 0.8522 0.6543 0.9038 0.0152  0.1277  0.0680  38  LEU A CD2   
236  N N     . HIS A 39  ? 0.7779 0.5528 0.7802 0.0041  0.1058  0.0159  39  HIS A N     
237  C CA    . HIS A 39  ? 0.8240 0.5891 0.8186 0.0046  0.1083  0.0061  39  HIS A CA    
238  C C     . HIS A 39  ? 0.8338 0.6120 0.8326 0.0000  0.0982  0.0066  39  HIS A C     
239  O O     . HIS A 39  ? 0.8602 0.6534 0.8643 -0.0046 0.0888  0.0118  39  HIS A O     
240  C CB    . HIS A 39  ? 0.8753 0.6245 0.8486 0.0031  0.1068  -0.0096 39  HIS A CB    
241  C CG    . HIS A 39  ? 0.8601 0.6131 0.8240 -0.0017 0.0934  -0.0160 39  HIS A CG    
242  N ND1   . HIS A 39  ? 0.9152 0.6641 0.8718 -0.0021 0.0917  -0.0177 39  HIS A ND1   
243  C CD2   . HIS A 39  ? 0.8321 0.5911 0.7927 -0.0061 0.0824  -0.0216 39  HIS A CD2   
244  C CE1   . HIS A 39  ? 0.8020 0.5540 0.7529 -0.0061 0.0804  -0.0232 39  HIS A CE1   
245  N NE2   . HIS A 39  ? 0.7957 0.5534 0.7486 -0.0086 0.0750  -0.0262 39  HIS A NE2   
246  N N     . PHE A 40  ? 0.8339 0.6062 0.8297 0.0006  0.1008  0.0007  40  PHE A N     
247  C CA    . PHE A 40  ? 0.8331 0.6188 0.8351 -0.0030 0.0937  0.0032  40  PHE A CA    
248  C C     . PHE A 40  ? 0.8451 0.6359 0.8360 -0.0094 0.0801  -0.0060 40  PHE A C     
249  O O     . PHE A 40  ? 0.8371 0.6171 0.8137 -0.0101 0.0769  -0.0171 40  PHE A O     
250  C CB    . PHE A 40  ? 0.8619 0.6389 0.8627 -0.0011 0.0997  -0.0016 40  PHE A CB    
251  C CG    . PHE A 40  ? 0.8675 0.6423 0.8845 0.0048  0.1138  0.0097  40  PHE A CG    
252  C CD1   . PHE A 40  ? 0.8841 0.6771 0.9217 0.0054  0.1141  0.0260  40  PHE A CD1   
253  C CD2   . PHE A 40  ? 0.8825 0.6370 0.8944 0.0094  0.1274  0.0045  40  PHE A CD2   
254  C CE1   . PHE A 40  ? 0.9150 0.7059 0.9708 0.0118  0.1282  0.0382  40  PHE A CE1   
255  C CE2   . PHE A 40  ? 0.8714 0.6214 0.8996 0.0153  0.1426  0.0146  40  PHE A CE2   
256  C CZ    . PHE A 40  ? 0.9084 0.6764 0.9599 0.0173  0.1433  0.0321  40  PHE A CZ    
257  N N     . GLY A 41  ? 0.8900 0.6979 0.8880 -0.0144 0.0726  -0.0007 41  GLY A N     
258  C CA    . GLY A 41  ? 0.8334 0.6448 0.8211 -0.0206 0.0619  -0.0109 41  GLY A CA    
259  C C     . GLY A 41  ? 0.8057 0.6112 0.7866 -0.0201 0.0618  -0.0200 41  GLY A C     
260  O O     . GLY A 41  ? 0.8081 0.6114 0.7950 -0.0167 0.0687  -0.0162 41  GLY A O     
261  N N     . TYR A 42  ? 0.7691 0.5718 0.7386 -0.0235 0.0545  -0.0317 42  TYR A N     
262  C CA    . TYR A 42  ? 0.8271 0.6259 0.7903 -0.0236 0.0535  -0.0402 42  TYR A CA    
263  C C     . TYR A 42  ? 0.8750 0.6848 0.8356 -0.0297 0.0449  -0.0450 42  TYR A C     
264  O O     . TYR A 42  ? 0.8757 0.6850 0.8308 -0.0329 0.0397  -0.0505 42  TYR A O     
265  C CB    . TYR A 42  ? 0.8165 0.5987 0.7673 -0.0207 0.0551  -0.0505 42  TYR A CB    
266  C CG    . TYR A 42  ? 0.8848 0.6623 0.8286 -0.0210 0.0543  -0.0589 42  TYR A CG    
267  C CD1   . TYR A 42  ? 0.9021 0.6859 0.8425 -0.0244 0.0470  -0.0652 42  TYR A CD1   
268  C CD2   . TYR A 42  ? 0.9315 0.6976 0.8714 -0.0184 0.0614  -0.0612 42  TYR A CD2   
269  C CE1   . TYR A 42  ? 0.8837 0.6644 0.8186 -0.0246 0.0461  -0.0721 42  TYR A CE1   
270  C CE2   . TYR A 42  ? 0.9484 0.7107 0.8815 -0.0197 0.0601  -0.0687 42  TYR A CE2   
271  C CZ    . TYR A 42  ? 0.8486 0.6190 0.7798 -0.0225 0.0521  -0.0735 42  TYR A CZ    
272  O OH    . TYR A 42  ? 0.8402 0.6083 0.7658 -0.0238 0.0508  -0.0800 42  TYR A OH    
273  N N     . TRP A 43  ? 0.8874 0.7063 0.8520 -0.0316 0.0443  -0.0429 43  TRP A N     
274  C CA    . TRP A 43  ? 0.8735 0.7032 0.8349 -0.0378 0.0375  -0.0478 43  TRP A CA    
275  C C     . TRP A 43  ? 0.9349 0.7603 0.8917 -0.0362 0.0379  -0.0550 43  TRP A C     
276  O O     . TRP A 43  ? 0.9247 0.7419 0.8830 -0.0317 0.0435  -0.0537 43  TRP A O     
277  C CB    . TRP A 43  ? 0.8570 0.7071 0.8284 -0.0434 0.0355  -0.0363 43  TRP A CB    
278  C CG    . TRP A 43  ? 0.8855 0.7442 0.8636 -0.0463 0.0347  -0.0265 43  TRP A CG    
279  C CD1   . TRP A 43  ? 0.9398 0.8088 0.9150 -0.0548 0.0285  -0.0275 43  TRP A CD1   
280  C CD2   . TRP A 43  ? 0.8400 0.6993 0.8297 -0.0416 0.0405  -0.0136 43  TRP A CD2   
281  N NE1   . TRP A 43  ? 0.9218 0.7987 0.9056 -0.0562 0.0291  -0.0156 43  TRP A NE1   
282  C CE2   . TRP A 43  ? 0.8434 0.7150 0.8370 -0.0476 0.0366  -0.0064 43  TRP A CE2   
283  C CE3   . TRP A 43  ? 0.8270 0.6769 0.8240 -0.0333 0.0496  -0.0078 43  TRP A CE3   
284  C CZ2   . TRP A 43  ? 0.8500 0.7265 0.8560 -0.0448 0.0408  0.0077  43  TRP A CZ2   
285  C CZ3   . TRP A 43  ? 0.8214 0.6746 0.8306 -0.0301 0.0552  0.0055  43  TRP A CZ3   
286  C CH2   . TRP A 43  ? 0.8622 0.7294 0.8763 -0.0355 0.0504  0.0136  43  TRP A CH2   
287  N N     . ASP A 44  ? 1.0321 0.8627 0.9831 -0.0405 0.0326  -0.0630 44  ASP A N     
288  C CA    . ASP A 44  ? 1.0500 0.8784 0.9971 -0.0396 0.0323  -0.0697 44  ASP A CA    
289  C C     . ASP A 44  ? 1.0504 0.8929 1.0042 -0.0424 0.0323  -0.0632 44  ASP A C     
290  O O     . ASP A 44  ? 1.0764 0.9158 1.0305 -0.0402 0.0344  -0.0644 44  ASP A O     
291  C CB    . ASP A 44  ? 1.1099 0.9371 1.0489 -0.0420 0.0279  -0.0810 44  ASP A CB    
292  C CG    . ASP A 44  ? 1.1568 0.9738 1.0915 -0.0406 0.0271  -0.0857 44  ASP A CG    
293  O OD1   . ASP A 44  ? 1.1107 0.9156 1.0421 -0.0356 0.0288  -0.0882 44  ASP A OD1   
294  O OD2   . ASP A 44  ? 1.1628 0.9846 1.0974 -0.0452 0.0249  -0.0866 44  ASP A OD2   
295  N N     . SER A 45  ? 1.0048 0.8637 0.9635 -0.0484 0.0295  -0.0564 45  SER A N     
296  C CA    . SER A 45  ? 1.1017 0.9779 1.0673 -0.0523 0.0285  -0.0486 45  SER A CA    
297  C C     . SER A 45  ? 1.1517 1.0417 1.1300 -0.0541 0.0297  -0.0325 45  SER A C     
298  O O     . SER A 45  ? 1.1165 1.0087 1.0947 -0.0566 0.0281  -0.0301 45  SER A O     
299  C CB    . SER A 45  ? 1.1512 1.0387 1.1095 -0.0600 0.0232  -0.0559 45  SER A CB    
300  O OG    . SER A 45  ? 1.2678 1.1619 1.2229 -0.0667 0.0199  -0.0564 45  SER A OG    
301  N N     . PRO A 46  ? 1.1273 1.0271 1.1180 -0.0529 0.0328  -0.0202 46  PRO A N     
302  C CA    . PRO A 46  ? 1.1525 1.0666 1.1584 -0.0536 0.0347  -0.0022 46  PRO A CA    
303  C C     . PRO A 46  ? 1.2120 1.1490 1.2174 -0.0643 0.0273  0.0031  46  PRO A C     
304  O O     . PRO A 46  ? 1.1803 1.1287 1.1961 -0.0660 0.0275  0.0167  46  PRO A O     
305  C CB    . PRO A 46  ? 1.0921 1.0124 1.1116 -0.0505 0.0395  0.0088  46  PRO A CB    
306  C CG    . PRO A 46  ? 1.0865 0.9891 1.0960 -0.0466 0.0414  -0.0053 46  PRO A CG    
307  C CD    . PRO A 46  ? 1.0458 0.9456 1.0382 -0.0512 0.0345  -0.0211 46  PRO A CD    
308  N N     . ASP A 47  ? 1.2291 1.1710 1.2213 -0.0719 0.0214  -0.0085 47  ASP A N     
309  C CA    . ASP A 47  ? 1.2096 1.1729 1.1980 -0.0847 0.0147  -0.0057 47  ASP A CA    
310  C C     . ASP A 47  ? 1.2032 1.1548 1.1792 -0.0878 0.0126  -0.0182 47  ASP A C     
311  O O     . ASP A 47  ? 1.2045 1.1699 1.1746 -0.0995 0.0076  -0.0190 47  ASP A O     
312  C CB    . ASP A 47  ? 1.2190 1.1963 1.2006 -0.0925 0.0109  -0.0104 47  ASP A CB    
313  C CG    . ASP A 47  ? 1.3168 1.2760 1.2842 -0.0899 0.0116  -0.0303 47  ASP A CG    
314  O OD1   . ASP A 47  ? 1.3151 1.2519 1.2788 -0.0818 0.0145  -0.0391 47  ASP A OD1   
315  O OD2   . ASP A 47  ? 1.3499 1.3187 1.3106 -0.0959 0.0093  -0.0360 47  ASP A OD2   
316  N N     . SER A 48  ? 1.2631 1.1906 1.2353 -0.0786 0.0163  -0.0273 48  SER A N     
317  C CA    . SER A 48  ? 1.1586 1.0736 1.1202 -0.0807 0.0148  -0.0393 48  SER A CA    
318  C C     . SER A 48  ? 1.0529 0.9753 1.0196 -0.0851 0.0133  -0.0297 48  SER A C     
319  O O     . SER A 48  ? 1.0650 0.9872 1.0431 -0.0789 0.0166  -0.0175 48  SER A O     
320  C CB    . SER A 48  ? 1.0793 0.9691 1.0369 -0.0699 0.0188  -0.0488 48  SER A CB    
321  O OG    . SER A 48  ? 0.8842 0.7635 0.8379 -0.0698 0.0185  -0.0531 48  SER A OG    
322  N N     . GLN A 49  ? 1.0233 0.9511 0.9814 -0.0959 0.0090  -0.0359 49  GLN A N     
323  C CA    . GLN A 49  ? 1.0501 0.9900 1.0126 -0.1033 0.0062  -0.0258 49  GLN A CA    
324  C C     . GLN A 49  ? 1.0199 0.9413 0.9786 -0.1002 0.0076  -0.0324 49  GLN A C     
325  O O     . GLN A 49  ? 1.0309 0.9589 0.9879 -0.1093 0.0045  -0.0305 49  GLN A O     
326  C CB    . GLN A 49  ? 1.1506 1.1119 1.1062 -0.1202 0.0005  -0.0262 49  GLN A CB    
327  C CG    . GLN A 49  ? 1.1888 1.1772 1.1532 -0.1252 -0.0020 -0.0109 49  GLN A CG    
328  C CD    . GLN A 49  ? 1.2220 1.2182 1.2066 -0.1161 0.0008  0.0100  49  GLN A CD    
329  O OE1   . GLN A 49  ? 1.2056 1.1915 1.1977 -0.1038 0.0061  0.0123  49  GLN A OE1   
330  N NE2   . GLN A 49  ? 1.2311 1.2450 1.2248 -0.1225 -0.0020 0.0254  49  GLN A NE2   
331  N N     . VAL A 50  ? 1.0047 0.9042 0.9622 -0.0882 0.0119  -0.0394 50  VAL A N     
332  C CA    . VAL A 50  ? 0.9029 0.7872 0.8591 -0.0847 0.0133  -0.0424 50  VAL A CA    
333  C C     . VAL A 50  ? 0.9541 0.8480 0.9224 -0.0835 0.0141  -0.0257 50  VAL A C     
334  O O     . VAL A 50  ? 0.9097 0.8115 0.8888 -0.0782 0.0171  -0.0135 50  VAL A O     
335  C CB    . VAL A 50  ? 0.8703 0.7325 0.8232 -0.0726 0.0175  -0.0511 50  VAL A CB    
336  C CG1   . VAL A 50  ? 0.8844 0.7321 0.8354 -0.0696 0.0185  -0.0543 50  VAL A CG1   
337  C CG2   . VAL A 50  ? 0.8794 0.7354 0.8233 -0.0734 0.0168  -0.0651 50  VAL A CG2   
338  N N     . PRO A 51  ? 0.9778 0.8722 0.9462 -0.0885 0.0122  -0.0234 51  PRO A N     
339  C CA    . PRO A 51  ? 0.8758 0.7820 0.8574 -0.0878 0.0131  -0.0059 51  PRO A CA    
340  C C     . PRO A 51  ? 0.8425 0.7328 0.8298 -0.0738 0.0201  -0.0027 51  PRO A C     
341  O O     . PRO A 51  ? 0.7975 0.6679 0.7771 -0.0664 0.0229  -0.0143 51  PRO A O     
342  C CB    . PRO A 51  ? 0.9279 0.8375 0.9055 -0.0985 0.0087  -0.0071 51  PRO A CB    
343  C CG    . PRO A 51  ? 0.8842 0.7732 0.8484 -0.0985 0.0087  -0.0261 51  PRO A CG    
344  C CD    . PRO A 51  ? 0.9155 0.8006 0.8734 -0.0958 0.0096  -0.0360 51  PRO A CD    
345  N N     . LEU A 52  ? 0.9177 0.8182 0.9189 -0.0709 0.0232  0.0140  52  LEU A N     
346  C CA    . LEU A 52  ? 0.8844 0.7715 0.8919 -0.0580 0.0317  0.0181  52  LEU A CA    
347  C C     . LEU A 52  ? 0.8454 0.7111 0.8428 -0.0536 0.0331  0.0068  52  LEU A C     
348  O O     . LEU A 52  ? 0.8407 0.6893 0.8321 -0.0454 0.0377  -0.0014 52  LEU A O     
349  C CB    . LEU A 52  ? 0.8678 0.7695 0.8932 -0.0561 0.0356  0.0383  52  LEU A CB    
350  C CG    . LEU A 52  ? 0.7751 0.6602 0.8053 -0.0430 0.0464  0.0404  52  LEU A CG    
351  C CD1   . LEU A 52  ? 0.7223 0.5945 0.7474 -0.0365 0.0512  0.0317  52  LEU A CD1   
352  C CD2   . LEU A 52  ? 0.8616 0.7604 0.9121 -0.0393 0.0527  0.0612  52  LEU A CD2   
353  N N     . ALA A 53  ? 0.8921 0.7594 0.8873 -0.0599 0.0288  0.0063  53  ALA A N     
354  C CA    . ALA A 53  ? 0.8919 0.7411 0.8806 -0.0553 0.0305  -0.0009 53  ALA A CA    
355  C C     . ALA A 53  ? 0.8742 0.7059 0.8502 -0.0519 0.0302  -0.0174 53  ALA A C     
356  O O     . ALA A 53  ? 0.8354 0.6523 0.8076 -0.0441 0.0341  -0.0213 53  ALA A O     
357  C CB    . ALA A 53  ? 0.8155 0.6700 0.8043 -0.0644 0.0253  0.0008  53  ALA A CB    
358  N N     . GLU A 54  ? 0.9021 0.7366 0.8719 -0.0578 0.0258  -0.0264 54  GLU A N     
359  C CA    . GLU A 54  ? 0.8538 0.6734 0.8136 -0.0546 0.0256  -0.0407 54  GLU A CA    
360  C C     . GLU A 54  ? 0.8593 0.6736 0.8181 -0.0464 0.0297  -0.0420 54  GLU A C     
361  O O     . GLU A 54  ? 0.8655 0.6663 0.8179 -0.0411 0.0311  -0.0499 54  GLU A O     
362  C CB    . GLU A 54  ? 0.9268 0.7507 0.8807 -0.0633 0.0211  -0.0502 54  GLU A CB    
363  C CG    . GLU A 54  ? 0.9712 0.7971 0.9230 -0.0735 0.0175  -0.0530 54  GLU A CG    
364  C CD    . GLU A 54  ? 1.0883 0.9162 1.0323 -0.0826 0.0151  -0.0647 54  GLU A CD    
365  O OE1   . GLU A 54  ? 1.0695 0.8912 1.0090 -0.0786 0.0164  -0.0736 54  GLU A OE1   
366  O OE2   . GLU A 54  ? 1.1053 0.9416 1.0473 -0.0946 0.0122  -0.0650 54  GLU A OE2   
367  N N     . ALA A 55  ? 0.8432 0.6686 0.8088 -0.0461 0.0317  -0.0338 55  ALA A N     
368  C CA    . ALA A 55  ? 0.8699 0.6886 0.8348 -0.0390 0.0366  -0.0352 55  ALA A CA    
369  C C     . ALA A 55  ? 0.8210 0.6263 0.7851 -0.0314 0.0429  -0.0337 55  ALA A C     
370  O O     . ALA A 55  ? 0.7992 0.5922 0.7555 -0.0271 0.0451  -0.0414 55  ALA A O     
371  C CB    . ALA A 55  ? 0.8500 0.6830 0.8249 -0.0399 0.0385  -0.0249 55  ALA A CB    
372  N N     . THR A 56  ? 0.8435 0.6521 0.8150 -0.0304 0.0457  -0.0236 56  THR A N     
373  C CA    . THR A 56  ? 0.8571 0.6539 0.8277 -0.0237 0.0528  -0.0215 56  THR A CA    
374  C C     . THR A 56  ? 0.8344 0.6183 0.7935 -0.0229 0.0503  -0.0314 56  THR A C     
375  O O     . THR A 56  ? 0.7907 0.5630 0.7426 -0.0185 0.0547  -0.0358 56  THR A O     
376  C CB    . THR A 56  ? 0.8194 0.6240 0.8013 -0.0232 0.0562  -0.0080 56  THR A CB    
377  O OG1   . THR A 56  ? 0.8755 0.6854 0.8570 -0.0292 0.0492  -0.0077 56  THR A OG1   
378  C CG2   . THR A 56  ? 0.7790 0.5991 0.7757 -0.0237 0.0590  0.0053  56  THR A CG2   
379  N N     . ASP A 57  ? 0.7937 0.5799 0.7511 -0.0279 0.0435  -0.0347 57  ASP A N     
380  C CA    . ASP A 57  ? 0.7980 0.5731 0.7471 -0.0268 0.0410  -0.0432 57  ASP A CA    
381  C C     . ASP A 57  ? 0.7977 0.5666 0.7390 -0.0248 0.0404  -0.0525 57  ASP A C     
382  O O     . ASP A 57  ? 0.8048 0.5646 0.7394 -0.0216 0.0415  -0.0563 57  ASP A O     
383  C CB    . ASP A 57  ? 0.8517 0.6289 0.8017 -0.0328 0.0350  -0.0460 57  ASP A CB    
384  C CG    . ASP A 57  ? 0.8568 0.6344 0.8113 -0.0339 0.0352  -0.0388 57  ASP A CG    
385  O OD1   . ASP A 57  ? 0.8794 0.6542 0.8352 -0.0291 0.0400  -0.0323 57  ASP A OD1   
386  O OD2   . ASP A 57  ? 0.9207 0.7008 0.8770 -0.0402 0.0310  -0.0400 57  ASP A OD2   
387  N N     . ARG A 58  ? 0.8256 0.6009 0.7679 -0.0272 0.0387  -0.0552 58  ARG A N     
388  C CA    . ARG A 58  ? 0.8362 0.6068 0.7719 -0.0257 0.0378  -0.0637 58  ARG A CA    
389  C C     . ARG A 58  ? 0.8304 0.5935 0.7614 -0.0212 0.0433  -0.0636 58  ARG A C     
390  O O     . ARG A 58  ? 0.8526 0.6092 0.7760 -0.0199 0.0424  -0.0697 58  ARG A O     
391  C CB    . ARG A 58  ? 0.8448 0.6245 0.7826 -0.0292 0.0353  -0.0659 58  ARG A CB    
392  C CG    . ARG A 58  ? 0.9127 0.6878 0.8443 -0.0274 0.0345  -0.0741 58  ARG A CG    
393  C CD    . ARG A 58  ? 1.0192 0.8020 0.9514 -0.0313 0.0310  -0.0789 58  ARG A CD    
394  N NE    . ARG A 58  ? 1.1016 0.8818 1.0295 -0.0293 0.0309  -0.0846 58  ARG A NE    
395  C CZ    . ARG A 58  ? 1.1542 0.9419 1.0828 -0.0317 0.0295  -0.0871 58  ARG A CZ    
396  N NH1   . ARG A 58  ? 1.1174 0.9163 1.0501 -0.0366 0.0282  -0.0844 58  ARG A NH1   
397  N NH2   . ARG A 58  ? 1.1884 0.9739 1.1136 -0.0300 0.0293  -0.0919 58  ARG A NH2   
398  N N     . LEU A 59  ? 0.7903 0.5545 0.7259 -0.0193 0.0496  -0.0567 59  LEU A N     
399  C CA    . LEU A 59  ? 0.8033 0.5575 0.7328 -0.0160 0.0566  -0.0581 59  LEU A CA    
400  C C     . LEU A 59  ? 0.8470 0.5927 0.7683 -0.0149 0.0572  -0.0602 59  LEU A C     
401  O O     . LEU A 59  ? 0.8123 0.5511 0.7234 -0.0150 0.0580  -0.0661 59  LEU A O     
402  C CB    . LEU A 59  ? 0.8251 0.5803 0.7632 -0.0134 0.0653  -0.0495 59  LEU A CB    
403  C CG    . LEU A 59  ? 0.8248 0.5676 0.7572 -0.0106 0.0755  -0.0513 59  LEU A CG    
404  C CD1   . LEU A 59  ? 0.8656 0.6011 0.7865 -0.0124 0.0747  -0.0614 59  LEU A CD1   
405  C CD2   . LEU A 59  ? 0.8081 0.5536 0.7531 -0.0078 0.0840  -0.0423 59  LEU A CD2   
406  N N     . THR A 60  ? 0.8365 0.5843 0.7621 -0.0146 0.0563  -0.0547 60  THR A N     
407  C CA    . THR A 60  ? 0.7605 0.5020 0.6792 -0.0138 0.0565  -0.0553 60  THR A CA    
408  C C     . THR A 60  ? 0.8199 0.5592 0.7314 -0.0151 0.0502  -0.0623 60  THR A C     
409  O O     . THR A 60  ? 0.7912 0.5255 0.6933 -0.0151 0.0514  -0.0648 60  THR A O     
410  C CB    . THR A 60  ? 0.7983 0.5437 0.7243 -0.0141 0.0547  -0.0485 60  THR A CB    
411  O OG1   . THR A 60  ? 0.9133 0.6633 0.8482 -0.0129 0.0603  -0.0400 60  THR A OG1   
412  C CG2   . THR A 60  ? 0.7936 0.5332 0.7133 -0.0131 0.0555  -0.0476 60  THR A CG2   
413  N N     . ASP A 61  ? 0.8035 0.5477 0.7197 -0.0167 0.0439  -0.0651 61  ASP A N     
414  C CA    . ASP A 61  ? 0.8118 0.5548 0.7247 -0.0171 0.0387  -0.0702 61  ASP A CA    
415  C C     . ASP A 61  ? 0.8391 0.5810 0.7446 -0.0173 0.0391  -0.0753 61  ASP A C     
416  O O     . ASP A 61  ? 0.8586 0.5995 0.7590 -0.0175 0.0365  -0.0772 61  ASP A O     
417  C CB    . ASP A 61  ? 0.8155 0.5624 0.7354 -0.0189 0.0340  -0.0729 61  ASP A CB    
418  C CG    . ASP A 61  ? 0.7581 0.5051 0.6842 -0.0202 0.0329  -0.0690 61  ASP A CG    
419  O OD1   . ASP A 61  ? 0.7522 0.4975 0.6783 -0.0191 0.0354  -0.0632 61  ASP A OD1   
420  O OD2   . ASP A 61  ? 0.7194 0.4677 0.6500 -0.0228 0.0300  -0.0722 61  ASP A OD2   
421  N N     . MET A 62  ? 0.8586 0.6017 0.7646 -0.0178 0.0422  -0.0765 62  MET A N     
422  C CA    . MET A 62  ? 0.8649 0.6066 0.7644 -0.0189 0.0429  -0.0814 62  MET A CA    
423  C C     . MET A 62  ? 0.8678 0.6028 0.7563 -0.0198 0.0470  -0.0822 62  MET A C     
424  O O     . MET A 62  ? 0.8688 0.6036 0.7496 -0.0221 0.0448  -0.0862 62  MET A O     
425  C CB    . MET A 62  ? 0.8658 0.6100 0.7702 -0.0190 0.0465  -0.0806 62  MET A CB    
426  C CG    . MET A 62  ? 0.9055 0.6498 0.8065 -0.0204 0.0468  -0.0853 62  MET A CG    
427  S SD    . MET A 62  ? 1.0794 0.8285 0.9905 -0.0199 0.0514  -0.0806 62  MET A SD    
428  C CE    . MET A 62  ? 0.9512 0.7101 0.8723 -0.0203 0.0471  -0.0750 62  MET A CE    
429  N N     . MET A 63  ? 0.8497 0.5798 0.7370 -0.0188 0.0535  -0.0785 63  MET A N     
430  C CA    . MET A 63  ? 0.8739 0.5970 0.7489 -0.0208 0.0588  -0.0803 63  MET A CA    
431  C C     . MET A 63  ? 0.8307 0.5560 0.7003 -0.0221 0.0537  -0.0788 63  MET A C     
432  O O     . MET A 63  ? 0.8652 0.5892 0.7228 -0.0260 0.0536  -0.0816 63  MET A O     
433  C CB    . MET A 63  ? 0.9034 0.6202 0.7799 -0.0188 0.0692  -0.0766 63  MET A CB    
434  C CG    . MET A 63  ? 0.8212 0.5383 0.7082 -0.0164 0.0744  -0.0745 63  MET A CG    
435  S SD    . MET A 63  ? 0.9554 0.6658 0.8480 -0.0130 0.0881  -0.0685 63  MET A SD    
436  C CE    . MET A 63  ? 0.9126 0.6101 0.7856 -0.0167 0.0958  -0.0756 63  MET A CE    
437  N N     . ALA A 64  ? 0.8009 0.5307 0.6798 -0.0196 0.0488  -0.0743 64  ALA A N     
438  C CA    . ALA A 64  ? 0.8702 0.6021 0.7468 -0.0201 0.0447  -0.0708 64  ALA A CA    
439  C C     . ALA A 64  ? 0.8763 0.6131 0.7495 -0.0222 0.0383  -0.0728 64  ALA A C     
440  O O     . ALA A 64  ? 1.0001 0.7390 0.8651 -0.0251 0.0370  -0.0707 64  ALA A O     
441  C CB    . ALA A 64  ? 0.8439 0.5780 0.7326 -0.0173 0.0417  -0.0659 64  ALA A CB    
442  N N     . GLU A 65  ? 0.8635 0.6035 0.7433 -0.0213 0.0344  -0.0759 65  GLU A N     
443  C CA    . GLU A 65  ? 0.8989 0.6450 0.7779 -0.0227 0.0286  -0.0761 65  GLU A CA    
444  C C     . GLU A 65  ? 0.9060 0.6526 0.7711 -0.0280 0.0298  -0.0792 65  GLU A C     
445  O O     . GLU A 65  ? 0.9346 0.6878 0.7953 -0.0311 0.0254  -0.0766 65  GLU A O     
446  C CB    . GLU A 65  ? 0.9344 0.6838 0.8238 -0.0203 0.0253  -0.0789 65  GLU A CB    
447  C CG    . GLU A 65  ? 1.0085 0.7577 0.8955 -0.0217 0.0269  -0.0848 65  GLU A CG    
448  C CD    . GLU A 65  ? 1.1616 0.9139 1.0591 -0.0195 0.0248  -0.0875 65  GLU A CD    
449  O OE1   . GLU A 65  ? 1.1194 0.8702 1.0242 -0.0178 0.0254  -0.0868 65  GLU A OE1   
450  O OE2   . GLU A 65  ? 1.3021 1.0587 1.1999 -0.0203 0.0226  -0.0906 65  GLU A OE2   
451  N N     . ARG A 66  ? 0.8751 0.6151 0.7333 -0.0298 0.0361  -0.0839 66  ARG A N     
452  C CA    . ARG A 66  ? 0.9108 0.6487 0.7541 -0.0362 0.0387  -0.0881 66  ARG A CA    
453  C C     . ARG A 66  ? 0.9383 0.6769 0.7700 -0.0406 0.0395  -0.0853 66  ARG A C     
454  O O     . ARG A 66  ? 0.9749 0.7183 0.7953 -0.0475 0.0368  -0.0863 66  ARG A O     
455  C CB    . ARG A 66  ? 0.9122 0.6404 0.7523 -0.0366 0.0474  -0.0931 66  ARG A CB    
456  C CG    . ARG A 66  ? 0.8337 0.5641 0.6846 -0.0335 0.0456  -0.0949 66  ARG A CG    
457  C CD    . ARG A 66  ? 0.9394 0.6616 0.7888 -0.0340 0.0540  -0.0984 66  ARG A CD    
458  N NE    . ARG A 66  ? 0.9631 0.6890 0.8165 -0.0347 0.0511  -0.1015 66  ARG A NE    
459  C CZ    . ARG A 66  ? 0.9214 0.6535 0.7875 -0.0307 0.0476  -0.0996 66  ARG A CZ    
460  N NH1   . ARG A 66  ? 0.8096 0.5445 0.6850 -0.0265 0.0463  -0.0952 66  ARG A NH1   
461  N NH2   . ARG A 66  ? 0.8522 0.5879 0.7208 -0.0319 0.0455  -0.1024 66  ARG A NH2   
462  N N     . LEU A 67  ? 0.9585 0.6943 0.7930 -0.0374 0.0425  -0.0809 67  LEU A N     
463  C CA    . LEU A 67  ? 0.9370 0.6751 0.7612 -0.0415 0.0429  -0.0772 67  LEU A CA    
464  C C     . LEU A 67  ? 0.9456 0.6964 0.7712 -0.0439 0.0333  -0.0713 67  LEU A C     
465  O O     . LEU A 67  ? 1.0722 0.8286 0.8859 -0.0504 0.0322  -0.0685 67  LEU A O     
466  C CB    . LEU A 67  ? 0.9028 0.6377 0.7335 -0.0367 0.0462  -0.0719 67  LEU A CB    
467  C CG    . LEU A 67  ? 0.9168 0.6412 0.7473 -0.0343 0.0565  -0.0747 67  LEU A CG    
468  C CD1   . LEU A 67  ? 0.8887 0.6139 0.7313 -0.0287 0.0565  -0.0677 67  LEU A CD1   
469  C CD2   . LEU A 67  ? 0.9081 0.6258 0.7205 -0.0403 0.0654  -0.0789 67  LEU A CD2   
470  N N     . ARG A 68  ? 0.9318 0.6881 0.7724 -0.0391 0.0270  -0.0688 68  ARG A N     
471  C CA    . ARG A 68  ? 0.9395 0.7084 0.7863 -0.0397 0.0188  -0.0618 68  ARG A CA    
472  C C     . ARG A 68  ? 0.9660 0.7405 0.8147 -0.0396 0.0167  -0.0521 68  ARG A C     
473  O O     . ARG A 68  ? 0.9119 0.6967 0.7528 -0.0456 0.0129  -0.0463 68  ARG A O     
474  C CB    . ARG A 68  ? 0.8994 0.6759 0.7346 -0.0477 0.0157  -0.0638 68  ARG A CB    
475  C CG    . ARG A 68  ? 0.9769 0.7510 0.8143 -0.0473 0.0157  -0.0710 68  ARG A CG    
476  C CD    . ARG A 68  ? 1.0817 0.8644 0.9065 -0.0568 0.0123  -0.0719 68  ARG A CD    
477  N NE    . ARG A 68  ? 1.2160 1.0001 1.0434 -0.0575 0.0107  -0.0769 68  ARG A NE    
478  C CZ    . ARG A 68  ? 1.2491 1.0227 1.0708 -0.0587 0.0163  -0.0861 68  ARG A CZ    
479  N NH1   . ARG A 68  ? 1.1394 0.8992 0.9557 -0.0574 0.0248  -0.0911 68  ARG A NH1   
480  N NH2   . ARG A 68  ? 1.2786 1.0561 1.1017 -0.0609 0.0138  -0.0892 68  ARG A NH2   
481  N N     . ILE A 69  ? 1.0237 0.7924 0.8835 -0.0332 0.0186  -0.0494 69  ILE A N     
482  C CA    . ILE A 69  ? 0.9833 0.7552 0.8460 -0.0325 0.0179  -0.0404 69  ILE A CA    
483  C C     . ILE A 69  ? 1.0128 0.7869 0.8962 -0.0258 0.0139  -0.0336 69  ILE A C     
484  O O     . ILE A 69  ? 0.9725 0.7418 0.8669 -0.0213 0.0140  -0.0379 69  ILE A O     
485  C CB    . ILE A 69  ? 0.8964 0.6586 0.7534 -0.0318 0.0251  -0.0428 69  ILE A CB    
486  C CG1   . ILE A 69  ? 0.8642 0.6176 0.7330 -0.0257 0.0277  -0.0469 69  ILE A CG1   
487  C CG2   . ILE A 69  ? 0.8838 0.6416 0.7210 -0.0381 0.0313  -0.0499 69  ILE A CG2   
488  C CD1   . ILE A 69  ? 0.8573 0.6029 0.7225 -0.0248 0.0350  -0.0485 69  ILE A CD1   
489  N N     . GLY A 70  ? 1.0076 0.7889 0.8960 -0.0258 0.0111  -0.0227 70  GLY A N     
490  C CA    . GLY A 70  ? 1.0046 0.7856 0.9133 -0.0196 0.0092  -0.0155 70  GLY A CA    
491  C C     . GLY A 70  ? 0.9806 0.7580 0.8914 -0.0185 0.0115  -0.0097 70  GLY A C     
492  O O     . GLY A 70  ? 0.9812 0.7541 0.8789 -0.0213 0.0156  -0.0135 70  GLY A O     
493  N N     . ALA A 71  ? 0.9737 0.7521 0.9015 -0.0144 0.0098  -0.0005 71  ALA A N     
494  C CA    . ALA A 71  ? 0.9191 0.6972 0.8489 -0.0143 0.0110  0.0075  71  ALA A CA    
495  C C     . ALA A 71  ? 0.9008 0.6924 0.8192 -0.0199 0.0083  0.0165  71  ALA A C     
496  O O     . ALA A 71  ? 0.9030 0.7068 0.8215 -0.0223 0.0037  0.0221  71  ALA A O     
497  C CB    . ALA A 71  ? 0.8280 0.6028 0.7799 -0.0090 0.0104  0.0150  71  ALA A CB    
498  N N     . GLY A 72  ? 0.9032 0.6940 0.8116 -0.0226 0.0112  0.0184  72  GLY A N     
499  C CA    . GLY A 72  ? 0.8902 0.6935 0.7835 -0.0297 0.0098  0.0249  72  GLY A CA    
500  C C     . GLY A 72  ? 0.8750 0.6777 0.7447 -0.0367 0.0128  0.0142  72  GLY A C     
501  O O     . GLY A 72  ? 1.0073 0.8213 0.8617 -0.0447 0.0113  0.0179  72  GLY A O     
502  N N     . SER A 73  ? 0.9097 0.6999 0.7759 -0.0346 0.0173  0.0015  73  SER A N     
503  C CA    . SER A 73  ? 0.9340 0.7201 0.7794 -0.0405 0.0224  -0.0092 73  SER A CA    
504  C C     . SER A 73  ? 0.9207 0.6979 0.7576 -0.0405 0.0310  -0.0124 73  SER A C     
505  O O     . SER A 73  ? 0.9077 0.6776 0.7569 -0.0342 0.0334  -0.0114 73  SER A O     
506  C CB    . SER A 73  ? 0.8987 0.6769 0.7467 -0.0380 0.0232  -0.0199 73  SER A CB    
507  O OG    . SER A 73  ? 0.9127 0.7002 0.7663 -0.0388 0.0161  -0.0173 73  SER A OG    
508  N N     . ARG A 74  ? 0.9122 0.6897 0.7298 -0.0474 0.0361  -0.0159 74  ARG A N     
509  C CA    . ARG A 74  ? 0.9265 0.6946 0.7358 -0.0471 0.0464  -0.0195 74  ARG A CA    
510  C C     . ARG A 74  ? 0.8802 0.6360 0.6829 -0.0469 0.0538  -0.0322 74  ARG A C     
511  O O     . ARG A 74  ? 0.8929 0.6489 0.6803 -0.0539 0.0548  -0.0392 74  ARG A O     
512  C CB    . ARG A 74  ? 0.9576 0.7329 0.7476 -0.0559 0.0494  -0.0167 74  ARG A CB    
513  C CG    . ARG A 74  ? 0.9647 0.7541 0.7618 -0.0565 0.0422  -0.0021 74  ARG A CG    
514  C CD    . ARG A 74  ? 1.0295 0.8215 0.8118 -0.0618 0.0488  0.0008  74  ARG A CD    
515  N NE    . ARG A 74  ? 1.1954 1.0024 0.9845 -0.0630 0.0418  0.0159  74  ARG A NE    
516  C CZ    . ARG A 74  ? 1.2050 1.0132 1.0167 -0.0549 0.0372  0.0260  74  ARG A CZ    
517  N NH1   . ARG A 74  ? 1.1704 0.9673 0.9922 -0.0478 0.0427  0.0246  74  ARG A NH1   
518  N NH2   . ARG A 74  ? 1.1312 0.9520 0.9561 -0.0543 0.0275  0.0380  74  ARG A NH2   
519  N N     . VAL A 75  ? 0.8591 0.6058 0.6723 -0.0402 0.0584  -0.0346 75  VAL A N     
520  C CA    . VAL A 75  ? 0.9721 0.7080 0.7844 -0.0383 0.0652  -0.0441 75  VAL A CA    
521  C C     . VAL A 75  ? 0.9668 0.6939 0.7757 -0.0365 0.0777  -0.0454 75  VAL A C     
522  O O     . VAL A 75  ? 0.9325 0.6609 0.7512 -0.0322 0.0790  -0.0380 75  VAL A O     
523  C CB    . VAL A 75  ? 0.9217 0.6567 0.7532 -0.0316 0.0598  -0.0438 75  VAL A CB    
524  C CG1   . VAL A 75  ? 0.8986 0.6245 0.7302 -0.0297 0.0669  -0.0515 75  VAL A CG1   
525  C CG2   . VAL A 75  ? 0.8265 0.5691 0.6621 -0.0327 0.0493  -0.0430 75  VAL A CG2   
526  N N     . LEU A 76  ? 0.9272 0.6450 0.7234 -0.0398 0.0878  -0.0544 76  LEU A N     
527  C CA    . LEU A 76  ? 0.9154 0.6232 0.7112 -0.0369 0.1018  -0.0558 76  LEU A CA    
528  C C     . LEU A 76  ? 0.9434 0.6457 0.7558 -0.0296 0.1046  -0.0564 76  LEU A C     
529  O O     . LEU A 76  ? 0.9151 0.6145 0.7277 -0.0304 0.1027  -0.0625 76  LEU A O     
530  C CB    . LEU A 76  ? 0.9781 0.6769 0.7517 -0.0445 0.1136  -0.0653 76  LEU A CB    
531  C CG    . LEU A 76  ? 0.9556 0.6420 0.7306 -0.0405 0.1309  -0.0672 76  LEU A CG    
532  C CD1   . LEU A 76  ? 0.9291 0.6197 0.7125 -0.0357 0.1339  -0.0573 76  LEU A CD1   
533  C CD2   . LEU A 76  ? 0.9992 0.6740 0.7512 -0.0490 0.1442  -0.0786 76  LEU A CD2   
534  N N     . ASP A 77  ? 0.9330 0.6355 0.7597 -0.0233 0.1087  -0.0492 77  ASP A N     
535  C CA    . ASP A 77  ? 0.9472 0.6475 0.7906 -0.0172 0.1113  -0.0473 77  ASP A CA    
536  C C     . ASP A 77  ? 1.0043 0.6942 0.8449 -0.0154 0.1284  -0.0492 77  ASP A C     
537  O O     . ASP A 77  ? 0.9594 0.6493 0.8073 -0.0115 0.1362  -0.0422 77  ASP A O     
538  C CB    . ASP A 77  ? 0.9232 0.6321 0.7849 -0.0125 0.1044  -0.0371 77  ASP A CB    
539  C CG    . ASP A 77  ? 0.8908 0.6009 0.7692 -0.0079 0.1057  -0.0340 77  ASP A CG    
540  O OD1   . ASP A 77  ? 0.9721 0.6766 0.8487 -0.0078 0.1107  -0.0397 77  ASP A OD1   
541  O OD2   . ASP A 77  ? 0.9135 0.6307 0.8068 -0.0052 0.1018  -0.0254 77  ASP A OD2   
542  N N     . LEU A 78  ? 1.0099 0.6902 0.8403 -0.0186 0.1350  -0.0588 78  LEU A N     
543  C CA    . LEU A 78  ? 1.0051 0.6720 0.8303 -0.0181 0.1532  -0.0632 78  LEU A CA    
544  C C     . LEU A 78  ? 1.0142 0.6799 0.8615 -0.0097 0.1605  -0.0560 78  LEU A C     
545  O O     . LEU A 78  ? 1.0959 0.7587 0.9496 -0.0085 0.1608  -0.0586 78  LEU A O     
546  C CB    . LEU A 78  ? 1.0142 0.6708 0.8218 -0.0253 0.1575  -0.0761 78  LEU A CB    
547  C CG    . LEU A 78  ? 1.0496 0.6893 0.8464 -0.0274 0.1779  -0.0833 78  LEU A CG    
548  C CD1   . LEU A 78  ? 1.0571 0.6953 0.8330 -0.0344 0.1828  -0.0870 78  LEU A CD1   
549  C CD2   . LEU A 78  ? 1.0116 0.6402 0.7985 -0.0328 0.1823  -0.0947 78  LEU A CD2   
550  N N     . GLY A 79  ? 0.9352 0.6053 0.7953 -0.0041 0.1652  -0.0456 79  GLY A N     
551  C CA    . GLY A 79  ? 0.9240 0.5963 0.8069 0.0036  0.1723  -0.0358 79  GLY A CA    
552  C C     . GLY A 79  ? 1.0021 0.6900 0.9001 0.0052  0.1559  -0.0274 79  GLY A C     
553  O O     . GLY A 79  ? 1.0057 0.6969 0.9080 0.0044  0.1476  -0.0297 79  GLY A O     
554  N N     . CYS A 80  ? 0.9709 0.6682 0.8755 0.0064  0.1509  -0.0184 80  CYS A N     
555  C CA    . CYS A 80  ? 0.8820 0.5925 0.7960 0.0053  0.1343  -0.0131 80  CYS A CA    
556  C C     . CYS A 80  ? 0.8768 0.5995 0.8130 0.0087  0.1319  0.0000  80  CYS A C     
557  O O     . CYS A 80  ? 0.9225 0.6543 0.8636 0.0061  0.1187  0.0024  80  CYS A O     
558  C CB    . CYS A 80  ? 0.9035 0.6170 0.8096 0.0027  0.1286  -0.0116 80  CYS A CB    
559  S SG    . CYS A 80  ? 0.9414 0.6578 0.8557 0.0066  0.1393  0.0001  80  CYS A SG    
560  N N     . GLY A 81  ? 0.9041 0.6275 0.8533 0.0137  0.1441  0.0088  81  GLY A N     
561  C CA    . GLY A 81  ? 0.8850 0.6234 0.8562 0.0156  0.1405  0.0228  81  GLY A CA    
562  C C     . GLY A 81  ? 0.8725 0.6220 0.8492 0.0133  0.1312  0.0307  81  GLY A C     
563  O O     . GLY A 81  ? 0.9575 0.7056 0.9328 0.0150  0.1373  0.0350  81  GLY A O     
564  N N     . VAL A 82  ? 0.8409 0.6014 0.8253 0.0095  0.1187  0.0340  82  VAL A N     
565  C CA    . VAL A 82  ? 0.7631 0.5334 0.7533 0.0059  0.1099  0.0414  82  VAL A CA    
566  C C     . VAL A 82  ? 0.7756 0.5404 0.7519 0.0012  0.0986  0.0305  82  VAL A C     
567  O O     . VAL A 82  ? 0.8420 0.6133 0.8227 -0.0032 0.0889  0.0335  82  VAL A O     
568  C CB    . VAL A 82  ? 0.8240 0.6111 0.8321 0.0030  0.1039  0.0527  82  VAL A CB    
569  C CG1   . VAL A 82  ? 0.8125 0.6074 0.8378 0.0085  0.1157  0.0666  82  VAL A CG1   
570  C CG2   . VAL A 82  ? 0.8998 0.6896 0.9060 -0.0013 0.0948  0.0457  82  VAL A CG2   
571  N N     . GLY A 83  ? 0.8314 0.5849 0.7925 0.0016  0.0997  0.0186  83  GLY A N     
572  C CA    . GLY A 83  ? 0.8548 0.6034 0.8037 -0.0018 0.0908  0.0104  83  GLY A CA    
573  C C     . GLY A 83  ? 0.8217 0.5737 0.7729 -0.0058 0.0790  0.0056  83  GLY A C     
574  O O     . GLY A 83  ? 0.8822 0.6317 0.8281 -0.0082 0.0717  0.0014  83  GLY A O     
575  N N     . THR A 84  ? 0.8279 0.5862 0.7878 -0.0067 0.0777  0.0072  84  THR A N     
576  C CA    . THR A 84  ? 0.8761 0.6380 0.8375 -0.0116 0.0671  0.0022  84  THR A CA    
577  C C     . THR A 84  ? 0.8367 0.5901 0.7858 -0.0114 0.0642  -0.0099 84  THR A C     
578  O O     . THR A 84  ? 0.8139 0.5647 0.7598 -0.0138 0.0573  -0.0143 84  THR A O     
579  C CB    . THR A 84  ? 0.8508 0.6240 0.8236 -0.0138 0.0661  0.0077  84  THR A CB    
580  O OG1   . THR A 84  ? 0.8662 0.6488 0.8509 -0.0140 0.0689  0.0206  84  THR A OG1   
581  C CG2   . THR A 84  ? 0.8226 0.5999 0.7954 -0.0202 0.0562  0.0019  84  THR A CG2   
582  N N     . PRO A 85  ? 0.7886 0.5374 0.7317 -0.0089 0.0696  -0.0148 85  PRO A N     
583  C CA    . PRO A 85  ? 0.7840 0.5263 0.7157 -0.0096 0.0664  -0.0252 85  PRO A CA    
584  C C     . PRO A 85  ? 0.7820 0.5192 0.7043 -0.0099 0.0646  -0.0272 85  PRO A C     
585  O O     . PRO A 85  ? 0.7516 0.4881 0.6712 -0.0115 0.0577  -0.0319 85  PRO A O     
586  C CB    . PRO A 85  ? 0.7616 0.4991 0.6886 -0.0072 0.0752  -0.0279 85  PRO A CB    
587  C CG    . PRO A 85  ? 0.7444 0.4886 0.6849 -0.0056 0.0799  -0.0194 85  PRO A CG    
588  C CD    . PRO A 85  ? 0.8423 0.5919 0.7903 -0.0056 0.0794  -0.0102 85  PRO A CD    
589  N N     . GLY A 86  ? 0.8477 0.5825 0.7663 -0.0083 0.0714  -0.0228 86  GLY A N     
590  C CA    . GLY A 86  ? 0.7634 0.4954 0.6725 -0.0093 0.0697  -0.0235 86  GLY A CA    
591  C C     . GLY A 86  ? 0.7372 0.4727 0.6533 -0.0106 0.0611  -0.0198 86  GLY A C     
592  O O     . GLY A 86  ? 0.7375 0.4722 0.6492 -0.0117 0.0557  -0.0223 86  GLY A O     
593  N N     . VAL A 87  ? 0.7472 0.4869 0.6751 -0.0108 0.0601  -0.0133 87  VAL A N     
594  C CA    . VAL A 87  ? 0.7375 0.4785 0.6724 -0.0128 0.0531  -0.0102 87  VAL A CA    
595  C C     . VAL A 87  ? 0.7753 0.5146 0.7117 -0.0146 0.0463  -0.0175 87  VAL A C     
596  O O     . VAL A 87  ? 0.8341 0.5710 0.7714 -0.0149 0.0419  -0.0183 87  VAL A O     
597  C CB    . VAL A 87  ? 0.7271 0.4733 0.6736 -0.0144 0.0533  -0.0024 87  VAL A CB    
598  C CG1   . VAL A 87  ? 0.7625 0.5082 0.7162 -0.0181 0.0461  -0.0025 87  VAL A CG1   
599  C CG2   . VAL A 87  ? 0.7336 0.4813 0.6801 -0.0125 0.0592  0.0062  87  VAL A CG2   
600  N N     . ARG A 88  ? 0.7573 0.4983 0.6949 -0.0154 0.0462  -0.0222 88  ARG A N     
601  C CA    . ARG A 88  ? 0.8005 0.5401 0.7386 -0.0170 0.0410  -0.0300 88  ARG A CA    
602  C C     . ARG A 88  ? 0.7945 0.5307 0.7245 -0.0150 0.0398  -0.0348 88  ARG A C     
603  O O     . ARG A 88  ? 0.8046 0.5391 0.7371 -0.0154 0.0355  -0.0383 88  ARG A O     
604  C CB    . ARG A 88  ? 0.8091 0.5529 0.7490 -0.0185 0.0416  -0.0332 88  ARG A CB    
605  C CG    . ARG A 88  ? 0.7725 0.5150 0.7100 -0.0193 0.0379  -0.0420 88  ARG A CG    
606  C CD    . ARG A 88  ? 0.8321 0.5803 0.7716 -0.0214 0.0382  -0.0442 88  ARG A CD    
607  N NE    . ARG A 88  ? 0.7396 0.4871 0.6778 -0.0231 0.0344  -0.0526 88  ARG A NE    
608  C CZ    . ARG A 88  ? 0.7777 0.5283 0.7200 -0.0279 0.0313  -0.0559 88  ARG A CZ    
609  N NH1   . ARG A 88  ? 0.8352 0.5910 0.7828 -0.0326 0.0305  -0.0513 88  ARG A NH1   
610  N NH2   . ARG A 88  ? 0.7451 0.4940 0.6858 -0.0286 0.0292  -0.0639 88  ARG A NH2   
611  N N     . ILE A 89  ? 0.7894 0.5248 0.7098 -0.0135 0.0442  -0.0350 89  ILE A N     
612  C CA    . ILE A 89  ? 0.7381 0.4724 0.6502 -0.0135 0.0421  -0.0387 89  ILE A CA    
613  C C     . ILE A 89  ? 0.7706 0.5058 0.6845 -0.0133 0.0387  -0.0333 89  ILE A C     
614  O O     . ILE A 89  ? 0.7904 0.5268 0.7056 -0.0132 0.0342  -0.0343 89  ILE A O     
615  C CB    . ILE A 89  ? 0.7640 0.4967 0.6634 -0.0139 0.0479  -0.0415 89  ILE A CB    
616  C CG1   . ILE A 89  ? 0.7277 0.4593 0.6279 -0.0136 0.0511  -0.0462 89  ILE A CG1   
617  C CG2   . ILE A 89  ? 0.7379 0.4718 0.6276 -0.0158 0.0447  -0.0441 89  ILE A CG2   
618  C CD1   . ILE A 89  ? 0.7329 0.4615 0.6216 -0.0149 0.0545  -0.0523 89  ILE A CD1   
619  N N     . ALA A 90  ? 0.7832 0.5187 0.6984 -0.0132 0.0411  -0.0262 90  ALA A N     
620  C CA    . ALA A 90  ? 0.7987 0.5359 0.7173 -0.0131 0.0378  -0.0196 90  ALA A CA    
621  C C     . ALA A 90  ? 0.8021 0.5371 0.7343 -0.0126 0.0331  -0.0193 90  ALA A C     
622  O O     . ALA A 90  ? 0.7768 0.5125 0.7139 -0.0117 0.0296  -0.0166 90  ALA A O     
623  C CB    . ALA A 90  ? 0.7447 0.4831 0.6622 -0.0132 0.0417  -0.0119 90  ALA A CB    
624  N N     . ARG A 91  ? 0.7533 0.4860 0.6921 -0.0138 0.0336  -0.0219 91  ARG A N     
625  C CA    . ARG A 91  ? 0.7815 0.5104 0.7319 -0.0150 0.0307  -0.0231 91  ARG A CA    
626  C C     . ARG A 91  ? 0.7978 0.5245 0.7501 -0.0141 0.0283  -0.0298 91  ARG A C     
627  O O     . ARG A 91  ? 0.8036 0.5266 0.7651 -0.0132 0.0269  -0.0287 91  ARG A O     
628  C CB    . ARG A 91  ? 0.7820 0.5110 0.7362 -0.0186 0.0315  -0.0251 91  ARG A CB    
629  C CG    . ARG A 91  ? 0.7313 0.4558 0.6931 -0.0218 0.0293  -0.0308 91  ARG A CG    
630  C CD    . ARG A 91  ? 0.7578 0.4839 0.7236 -0.0273 0.0293  -0.0298 91  ARG A CD    
631  N NE    . ARG A 91  ? 0.8435 0.5768 0.8047 -0.0286 0.0302  -0.0314 91  ARG A NE    
632  C CZ    . ARG A 91  ? 0.9282 0.6631 0.8878 -0.0313 0.0291  -0.0390 91  ARG A CZ    
633  N NH1   . ARG A 91  ? 0.8240 0.5530 0.7851 -0.0328 0.0278  -0.0468 91  ARG A NH1   
634  N NH2   . ARG A 91  ? 0.9403 0.6831 0.8975 -0.0324 0.0301  -0.0380 91  ARG A NH2   
635  N N     . LEU A 92  ? 0.8082 0.5371 0.7535 -0.0140 0.0286  -0.0363 92  LEU A N     
636  C CA    . LEU A 92  ? 0.7432 0.4712 0.6908 -0.0131 0.0268  -0.0426 92  LEU A CA    
637  C C     . LEU A 92  ? 0.7878 0.5194 0.7322 -0.0106 0.0250  -0.0400 92  LEU A C     
638  O O     . LEU A 92  ? 0.8233 0.5547 0.7733 -0.0090 0.0235  -0.0426 92  LEU A O     
639  C CB    . LEU A 92  ? 0.7816 0.5114 0.7240 -0.0147 0.0275  -0.0503 92  LEU A CB    
640  C CG    . LEU A 92  ? 0.8161 0.5457 0.7619 -0.0185 0.0283  -0.0520 92  LEU A CG    
641  C CD1   . LEU A 92  ? 0.7101 0.4436 0.6522 -0.0203 0.0286  -0.0582 92  LEU A CD1   
642  C CD2   . LEU A 92  ? 0.7204 0.4446 0.6752 -0.0208 0.0275  -0.0535 92  LEU A CD2   
643  N N     . SER A 93  ? 0.7998 0.5355 0.7354 -0.0107 0.0255  -0.0349 93  SER A N     
644  C CA    . SER A 93  ? 0.7730 0.5145 0.7038 -0.0104 0.0231  -0.0317 93  SER A CA    
645  C C     . SER A 93  ? 0.8759 0.6212 0.8107 -0.0099 0.0216  -0.0210 93  SER A C     
646  O O     . SER A 93  ? 0.8786 0.6307 0.8151 -0.0096 0.0184  -0.0159 93  SER A O     
647  C CB    . SER A 93  ? 0.7646 0.5089 0.6792 -0.0131 0.0251  -0.0352 93  SER A CB    
648  O OG    . SER A 93  ? 0.8306 0.5747 0.7370 -0.0146 0.0288  -0.0315 93  SER A OG    
649  N N     . GLY A 94  ? 0.8783 0.6208 0.8156 -0.0100 0.0235  -0.0163 94  GLY A N     
650  C CA    . GLY A 94  ? 0.9076 0.6549 0.8471 -0.0101 0.0223  -0.0054 94  GLY A CA    
651  C C     . GLY A 94  ? 0.9293 0.6842 0.8527 -0.0133 0.0228  -0.0027 94  GLY A C     
652  O O     . GLY A 94  ? 0.9665 0.7291 0.8899 -0.0144 0.0206  0.0069  94  GLY A O     
653  N N     . ALA A 95  ? 0.8977 0.6509 0.8074 -0.0154 0.0260  -0.0110 95  ALA A N     
654  C CA    . ALA A 95  ? 0.8959 0.6535 0.7881 -0.0198 0.0286  -0.0108 95  ALA A CA    
655  C C     . ALA A 95  ? 0.8443 0.5994 0.7328 -0.0200 0.0341  -0.0073 95  ALA A C     
656  O O     . ALA A 95  ? 0.8590 0.6079 0.7546 -0.0173 0.0371  -0.0088 95  ALA A O     
657  C CB    . ALA A 95  ? 0.8822 0.6367 0.7623 -0.0220 0.0314  -0.0214 95  ALA A CB    
658  N N     . HIS A 96  ? 0.8787 0.6401 0.7564 -0.0238 0.0352  -0.0018 96  HIS A N     
659  C CA    . HIS A 96  ? 0.8887 0.6479 0.7609 -0.0243 0.0418  0.0009  96  HIS A CA    
660  C C     . HIS A 96  ? 0.8299 0.5818 0.6899 -0.0253 0.0502  -0.0091 96  HIS A C     
661  O O     . HIS A 96  ? 0.8600 0.6123 0.7045 -0.0300 0.0523  -0.0151 96  HIS A O     
662  C CB    . HIS A 96  ? 0.9300 0.6987 0.7931 -0.0287 0.0412  0.0095  96  HIS A CB    
663  C CG    . HIS A 96  ? 0.9719 0.7497 0.8476 -0.0280 0.0327  0.0203  96  HIS A CG    
664  N ND1   . HIS A 96  ? 1.0310 0.8052 0.9274 -0.0226 0.0290  0.0243  96  HIS A ND1   
665  C CD2   . HIS A 96  ? 1.0233 0.8139 0.8945 -0.0324 0.0278  0.0285  96  HIS A CD2   
666  C CE1   . HIS A 96  ? 1.0247 0.8075 0.9306 -0.0225 0.0230  0.0346  96  HIS A CE1   
667  N NE2   . HIS A 96  ? 1.0997 0.8939 0.9912 -0.0282 0.0217  0.0384  96  HIS A NE2   
668  N N     . VAL A 97  ? 0.7937 0.5392 0.6617 -0.0214 0.0550  -0.0105 97  VAL A N     
669  C CA    . VAL A 97  ? 0.8750 0.6135 0.7356 -0.0211 0.0640  -0.0178 97  VAL A CA    
670  C C     . VAL A 97  ? 0.8926 0.6295 0.7489 -0.0208 0.0735  -0.0138 97  VAL A C     
671  O O     . VAL A 97  ? 0.8612 0.6005 0.7287 -0.0181 0.0730  -0.0057 97  VAL A O     
672  C CB    . VAL A 97  ? 0.8315 0.5661 0.7050 -0.0172 0.0634  -0.0211 97  VAL A CB    
673  C CG1   . VAL A 97  ? 0.7983 0.5267 0.6675 -0.0161 0.0738  -0.0256 97  VAL A CG1   
674  C CG2   . VAL A 97  ? 0.7628 0.4984 0.6382 -0.0178 0.0559  -0.0263 97  VAL A CG2   
675  N N     . THR A 98  ? 0.9069 0.6388 0.7467 -0.0240 0.0829  -0.0205 98  THR A N     
676  C CA    . THR A 98  ? 0.8994 0.6276 0.7338 -0.0235 0.0951  -0.0186 98  THR A CA    
677  C C     . THR A 98  ? 0.8782 0.5968 0.7141 -0.0205 0.1057  -0.0251 98  THR A C     
678  O O     . THR A 98  ? 0.9068 0.6192 0.7291 -0.0243 0.1103  -0.0344 98  THR A O     
679  C CB    . THR A 98  ? 0.9148 0.6453 0.7285 -0.0306 0.0989  -0.0200 98  THR A CB    
680  O OG1   . THR A 98  ? 0.9897 0.7312 0.8062 -0.0325 0.0884  -0.0113 98  THR A OG1   
681  C CG2   . THR A 98  ? 0.9932 0.7188 0.8001 -0.0303 0.1133  -0.0195 98  THR A CG2   
682  N N     . GLY A 99  ? 0.8791 0.5975 0.7324 -0.0144 0.1086  -0.0192 99  GLY A N     
683  C CA    . GLY A 99  ? 0.9123 0.6237 0.7708 -0.0108 0.1191  -0.0220 99  GLY A CA    
684  C C     . GLY A 99  ? 0.9171 0.6225 0.7702 -0.0095 0.1352  -0.0208 99  GLY A C     
685  O O     . GLY A 99  ? 0.8904 0.5996 0.7411 -0.0100 0.1372  -0.0150 99  GLY A O     
686  N N     . ILE A 100 ? 0.9440 0.6394 0.7951 -0.0080 0.1477  -0.0267 100 ILE A N     
687  C CA    . ILE A 100 ? 0.9508 0.6385 0.8007 -0.0053 0.1659  -0.0255 100 ILE A CA    
688  C C     . ILE A 100 ? 0.9733 0.6580 0.8421 0.0016  0.1737  -0.0217 100 ILE A C     
689  O O     . ILE A 100 ? 0.9893 0.6728 0.8622 0.0016  0.1688  -0.0256 100 ILE A O     
690  C CB    . ILE A 100 ? 0.9643 0.6399 0.7892 -0.0119 0.1777  -0.0377 100 ILE A CB    
691  C CG1   . ILE A 100 ? 1.0269 0.6898 0.8494 -0.0121 0.1863  -0.0473 100 ILE A CG1   
692  C CG2   . ILE A 100 ? 0.9467 0.6283 0.7522 -0.0208 0.1660  -0.0421 100 ILE A CG2   
693  C CD1   . ILE A 100 ? 1.0465 0.6965 0.8430 -0.0207 0.1973  -0.0610 100 ILE A CD1   
694  N N     . SER A 101 ? 0.9955 0.6807 0.8772 0.0074  0.1856  -0.0125 101 SER A N     
695  C CA    . SER A 101 ? 1.0416 0.7253 0.9434 0.0145  0.1959  -0.0060 101 SER A CA    
696  C C     . SER A 101 ? 1.0279 0.7018 0.9293 0.0183  0.2177  -0.0045 101 SER A C     
697  O O     . SER A 101 ? 1.0127 0.6840 0.8997 0.0152  0.2226  -0.0072 101 SER A O     
698  C CB    . SER A 101 ? 1.0286 0.7286 0.9549 0.0188  0.1860  0.0090  101 SER A CB    
699  O OG    . SER A 101 ? 0.9688 0.6698 0.9156 0.0253  0.1964  0.0175  101 SER A OG    
700  N N     . VAL A 102 ? 1.0317 0.7002 0.9494 0.0248  0.2317  -0.0001 102 VAL A N     
701  C CA    . VAL A 102 ? 1.0396 0.6990 0.9616 0.0299  0.2544  0.0031  102 VAL A CA    
702  C C     . VAL A 102 ? 1.0910 0.7657 1.0414 0.0379  0.2555  0.0229  102 VAL A C     
703  O O     . VAL A 102 ? 1.1834 0.8567 1.1393 0.0422  0.2703  0.0294  102 VAL A O     
704  C CB    . VAL A 102 ? 1.0404 0.6810 0.9621 0.0322  0.2735  -0.0048 102 VAL A CB    
705  C CG1   . VAL A 102 ? 1.1023 0.7274 0.9930 0.0225  0.2746  -0.0248 102 VAL A CG1   
706  C CG2   . VAL A 102 ? 1.1014 0.7477 1.0454 0.0370  0.2691  0.0027  102 VAL A CG2   
707  N N     . SER A 103 ? 1.1028 0.7933 1.0710 0.0391  0.2400  0.0329  103 SER A N     
708  C CA    . SER A 103 ? 1.0763 0.7847 1.0701 0.0442  0.2376  0.0523  103 SER A CA    
709  C C     . SER A 103 ? 1.0210 0.7399 1.0083 0.0401  0.2251  0.0557  103 SER A C     
710  O O     . SER A 103 ? 0.9699 0.6934 0.9467 0.0337  0.2069  0.0500  103 SER A O     
711  C CB    . SER A 103 ? 1.0399 0.7621 1.0532 0.0450  0.2258  0.0611  103 SER A CB    
712  O OG    . SER A 103 ? 1.0761 0.8184 1.1122 0.0473  0.2206  0.0799  103 SER A OG    
713  N N     . HIS A 104 ? 1.0193 0.7417 1.0140 0.0439  0.2358  0.0654  104 HIS A N     
714  C CA    . HIS A 104 ? 1.0103 0.7432 1.0011 0.0402  0.2248  0.0702  104 HIS A CA    
715  C C     . HIS A 104 ? 0.9752 0.7268 0.9828 0.0381  0.2061  0.0816  104 HIS A C     
716  O O     . HIS A 104 ? 0.9499 0.7059 0.9485 0.0319  0.1897  0.0781  104 HIS A O     
717  C CB    . HIS A 104 ? 1.0211 0.7551 1.0181 0.0451  0.2408  0.0795  104 HIS A CB    
718  C CG    . HIS A 104 ? 1.0347 0.7811 1.0315 0.0418  0.2302  0.0872  104 HIS A CG    
719  N ND1   . HIS A 104 ? 0.9775 0.7425 0.9965 0.0426  0.2206  0.1039  104 HIS A ND1   
720  C CD2   . HIS A 104 ? 1.0321 0.7754 1.0092 0.0370  0.2275  0.0811  104 HIS A CD2   
721  C CE1   . HIS A 104 ? 0.9612 0.7325 0.9747 0.0388  0.2131  0.1071  104 HIS A CE1   
722  N NE2   . HIS A 104 ? 0.9809 0.7397 0.9697 0.0358  0.2170  0.0941  104 HIS A NE2   
723  N N     . GLU A 105 ? 1.0183 0.7809 1.0504 0.0424  0.2086  0.0951  105 GLU A N     
724  C CA    . GLU A 105 ? 0.9964 0.7779 1.0434 0.0385  0.1914  0.1058  105 GLU A CA    
725  C C     . GLU A 105 ? 1.0000 0.7796 1.0355 0.0319  0.1746  0.0940  105 GLU A C     
726  O O     . GLU A 105 ? 0.9801 0.7724 1.0216 0.0263  0.1591  0.0987  105 GLU A O     
727  C CB    . GLU A 105 ? 1.0403 0.8361 1.1157 0.0436  0.1977  0.1236  105 GLU A CB    
728  C CG    . GLU A 105 ? 1.1578 0.9581 1.2490 0.0508  0.2146  0.1381  105 GLU A CG    
729  C CD    . GLU A 105 ? 1.2026 1.0239 1.3089 0.0478  0.2050  0.1547  105 GLU A CD    
730  O OE1   . GLU A 105 ? 1.2156 1.0533 1.3330 0.0423  0.1903  0.1624  105 GLU A OE1   
731  O OE2   . GLU A 105 ? 1.2446 1.0661 1.3506 0.0500  0.2123  0.1597  105 GLU A OE2   
732  N N     . GLN A 106 ? 0.9993 0.7633 1.0183 0.0318  0.1781  0.0787  106 GLN A N     
733  C CA    . GLN A 106 ? 0.9329 0.6943 0.9392 0.0257  0.1628  0.0667  106 GLN A CA    
734  C C     . GLN A 106 ? 0.9362 0.6929 0.9241 0.0206  0.1537  0.0581  106 GLN A C     
735  O O     . GLN A 106 ? 0.8914 0.6548 0.8791 0.0155  0.1384  0.0577  106 GLN A O     
736  C CB    . GLN A 106 ? 0.9369 0.6847 0.9336 0.0270  0.1694  0.0547  106 GLN A CB    
737  C CG    . GLN A 106 ? 0.9875 0.7408 1.0030 0.0310  0.1747  0.0626  106 GLN A CG    
738  C CD    . GLN A 106 ? 0.9319 0.6742 0.9377 0.0300  0.1751  0.0501  106 GLN A CD    
739  O OE1   . GLN A 106 ? 1.0140 0.7394 1.0034 0.0302  0.1843  0.0378  106 GLN A OE1   
740  N NE2   . GLN A 106 ? 0.8959 0.6484 0.9112 0.0279  0.1648  0.0530  106 GLN A NE2   
741  N N     . VAL A 107 ? 0.9167 0.6621 0.8890 0.0215  0.1636  0.0515  107 VAL A N     
742  C CA    . VAL A 107 ? 0.9673 0.7099 0.9222 0.0163  0.1546  0.0443  107 VAL A CA    
743  C C     . VAL A 107 ? 0.9694 0.7244 0.9347 0.0142  0.1441  0.0550  107 VAL A C     
744  O O     . VAL A 107 ? 0.9086 0.6647 0.8673 0.0095  0.1310  0.0513  107 VAL A O     
745  C CB    . VAL A 107 ? 0.9231 0.6546 0.8595 0.0163  0.1674  0.0373  107 VAL A CB    
746  C CG1   . VAL A 107 ? 0.9317 0.6637 0.8778 0.0218  0.1838  0.0465  107 VAL A CG1   
747  C CG2   . VAL A 107 ? 0.8827 0.6165 0.8057 0.0111  0.1580  0.0354  107 VAL A CG2   
748  N N     . VAL A 108 ? 0.9278 0.6925 0.9111 0.0175  0.1494  0.0690  108 VAL A N     
749  C CA    . VAL A 108 ? 0.9084 0.6853 0.9025 0.0145  0.1396  0.0798  108 VAL A CA    
750  C C     . VAL A 108 ? 0.9283 0.7108 0.9270 0.0088  0.1232  0.0778  108 VAL A C     
751  O O     . VAL A 108 ? 0.9481 0.7303 0.9416 0.0040  0.1120  0.0749  108 VAL A O     
752  C CB    . VAL A 108 ? 0.9049 0.6934 0.9194 0.0186  0.1483  0.0963  108 VAL A CB    
753  C CG1   . VAL A 108 ? 0.8448 0.6466 0.8705 0.0136  0.1363  0.1068  108 VAL A CG1   
754  C CG2   . VAL A 108 ? 0.8678 0.6504 0.8774 0.0238  0.1652  0.0982  108 VAL A CG2   
755  N N     . ARG A 109 ? 1.0027 0.7907 1.0121 0.0092  0.1222  0.0800  109 ARG A N     
756  C CA    . ARG A 109 ? 0.9993 0.7935 1.0125 0.0027  0.1076  0.0781  109 ARG A CA    
757  C C     . ARG A 109 ? 0.9716 0.7545 0.9684 0.0002  0.1004  0.0624  109 ARG A C     
758  O O     . ARG A 109 ? 0.9926 0.7775 0.9894 -0.0055 0.0886  0.0589  109 ARG A O     
759  C CB    . ARG A 109 ? 1.0022 0.8081 1.0312 0.0028  0.1082  0.0860  109 ARG A CB    
760  C CG    . ARG A 109 ? 1.0789 0.9004 1.1267 0.0032  0.1116  0.1042  109 ARG A CG    
761  C CD    . ARG A 109 ? 1.0961 0.9280 1.1615 0.0079  0.1207  0.1162  109 ARG A CD    
762  N NE    . ARG A 109 ? 1.0577 0.8992 1.1286 0.0025  0.1113  0.1163  109 ARG A NE    
763  C CZ    . ARG A 109 ? 1.0844 0.9403 1.1617 -0.0067 0.0986  0.1217  109 ARG A CZ    
764  N NH1   . ARG A 109 ? 1.0589 0.9218 1.1401 -0.0115 0.0936  0.1288  109 ARG A NH1   
765  N NH2   . ARG A 109 ? 1.0032 0.8665 1.0819 -0.0122 0.0908  0.1195  109 ARG A NH2   
766  N N     . ALA A 110 ? 0.9298 0.7009 0.9127 0.0037  0.1077  0.0531  110 ALA A N     
767  C CA    . ALA A 110 ? 0.8772 0.6395 0.8451 0.0009  0.1004  0.0399  110 ALA A CA    
768  C C     . ALA A 110 ? 0.8862 0.6481 0.8497 -0.0024 0.0923  0.0403  110 ALA A C     
769  O O     . ALA A 110 ? 0.8638 0.6257 0.8275 -0.0064 0.0816  0.0362  110 ALA A O     
770  C CB    . ALA A 110 ? 0.8123 0.5634 0.7653 0.0038  0.1099  0.0308  110 ALA A CB    
771  N N     . ASN A 111 ? 0.8326 0.5948 0.7939 -0.0009 0.0982  0.0461  111 ASN A N     
772  C CA    . ASN A 111 ? 0.8133 0.5760 0.7719 -0.0037 0.0913  0.0483  111 ASN A CA    
773  C C     . ASN A 111 ? 0.8630 0.6324 0.8355 -0.0077 0.0818  0.0546  111 ASN A C     
774  O O     . ASN A 111 ? 0.8243 0.5914 0.7960 -0.0110 0.0734  0.0527  111 ASN A O     
775  C CB    . ASN A 111 ? 0.8213 0.5847 0.7755 -0.0016 0.1003  0.0546  111 ASN A CB    
776  C CG    . ASN A 111 ? 0.8361 0.5927 0.7718 -0.0021 0.1031  0.0467  111 ASN A CG    
777  O OD1   . ASN A 111 ? 0.9101 0.6648 0.8395 -0.0051 0.0941  0.0419  111 ASN A OD1   
778  N ND2   . ASN A 111 ? 0.7903 0.5431 0.7170 0.0002  0.1160  0.0451  111 ASN A ND2   
779  N N     . ALA A 112 ? 0.8643 0.6424 0.8504 -0.0080 0.0835  0.0629  112 ALA A N     
780  C CA    . ALA A 112 ? 0.7704 0.5555 0.7682 -0.0140 0.0744  0.0682  112 ALA A CA    
781  C C     . ALA A 112 ? 0.8203 0.6012 0.8154 -0.0186 0.0650  0.0578  112 ALA A C     
782  O O     . ALA A 112 ? 0.8268 0.6063 0.8249 -0.0241 0.0572  0.0568  112 ALA A O     
783  C CB    . ALA A 112 ? 0.7367 0.5347 0.7493 -0.0144 0.0779  0.0798  112 ALA A CB    
784  N N     . LEU A 113 ? 0.7707 0.5488 0.7605 -0.0166 0.0666  0.0499  113 LEU A N     
785  C CA    . LEU A 113 ? 0.8053 0.5795 0.7918 -0.0204 0.0589  0.0397  113 LEU A CA    
786  C C     . LEU A 113 ? 0.8303 0.5944 0.8082 -0.0204 0.0546  0.0321  113 LEU A C     
787  O O     . LEU A 113 ? 0.8367 0.5976 0.8169 -0.0248 0.0477  0.0278  113 LEU A O     
788  C CB    . LEU A 113 ? 0.8531 0.6268 0.8356 -0.0176 0.0624  0.0340  113 LEU A CB    
789  C CG    . LEU A 113 ? 0.7938 0.5668 0.7747 -0.0215 0.0557  0.0249  113 LEU A CG    
790  C CD1   . LEU A 113 ? 0.8263 0.6117 0.8180 -0.0268 0.0530  0.0310  113 LEU A CD1   
791  C CD2   . LEU A 113 ? 0.7185 0.4858 0.6905 -0.0171 0.0597  0.0168  113 LEU A CD2   
792  N N     . ALA A 114 ? 0.8165 0.5757 0.7849 -0.0158 0.0593  0.0308  114 ALA A N     
793  C CA    . ALA A 114 ? 0.8468 0.5997 0.8091 -0.0159 0.0550  0.0269  114 ALA A CA    
794  C C     . ALA A 114 ? 0.8191 0.5727 0.7900 -0.0189 0.0508  0.0338  114 ALA A C     
795  O O     . ALA A 114 ? 0.7954 0.5440 0.7687 -0.0209 0.0451  0.0305  114 ALA A O     
796  C CB    . ALA A 114 ? 0.8081 0.5587 0.7578 -0.0124 0.0606  0.0259  114 ALA A CB    
797  N N     . GLU A 115 ? 0.8339 0.5934 0.8109 -0.0192 0.0541  0.0438  115 GLU A N     
798  C CA    . GLU A 115 ? 0.8566 0.6171 0.8430 -0.0228 0.0502  0.0511  115 GLU A CA    
799  C C     . GLU A 115 ? 0.8439 0.6021 0.8381 -0.0292 0.0435  0.0469  115 GLU A C     
800  O O     . GLU A 115 ? 0.8755 0.6272 0.8735 -0.0319 0.0392  0.0454  115 GLU A O     
801  C CB    . GLU A 115 ? 0.8464 0.6154 0.8390 -0.0224 0.0552  0.0631  115 GLU A CB    
802  C CG    . GLU A 115 ? 0.8726 0.6424 0.8576 -0.0176 0.0620  0.0681  115 GLU A CG    
803  C CD    . GLU A 115 ? 0.8918 0.6700 0.8840 -0.0168 0.0679  0.0804  115 GLU A CD    
804  O OE1   . GLU A 115 ? 0.9037 0.6882 0.9083 -0.0205 0.0653  0.0868  115 GLU A OE1   
805  O OE2   . GLU A 115 ? 0.9136 0.6928 0.8985 -0.0131 0.0753  0.0837  115 GLU A OE2   
806  N N     . GLU A 116 ? 0.8130 0.5765 0.8098 -0.0322 0.0431  0.0450  116 GLU A N     
807  C CA    . GLU A 116 ? 0.8393 0.6018 0.8417 -0.0403 0.0372  0.0409  116 GLU A CA    
808  C C     . GLU A 116 ? 0.8391 0.5909 0.8368 -0.0405 0.0340  0.0288  116 GLU A C     
809  O O     . GLU A 116 ? 0.8938 0.6404 0.8954 -0.0470 0.0304  0.0242  116 GLU A O     
810  C CB    . GLU A 116 ? 0.7884 0.5619 0.7945 -0.0446 0.0368  0.0429  116 GLU A CB    
811  C CG    . GLU A 116 ? 0.8039 0.5889 0.8160 -0.0420 0.0418  0.0560  116 GLU A CG    
812  C CD    . GLU A 116 ? 0.8699 0.6592 0.8908 -0.0464 0.0403  0.0664  116 GLU A CD    
813  O OE1   . GLU A 116 ? 0.8236 0.6218 0.8522 -0.0551 0.0364  0.0710  116 GLU A OE1   
814  O OE2   . GLU A 116 ? 0.9458 0.7313 0.9661 -0.0420 0.0432  0.0710  116 GLU A OE2   
815  N N     . ALA A 117 ? 0.8157 0.5638 0.8052 -0.0341 0.0360  0.0237  117 ALA A N     
816  C CA    . ALA A 117 ? 0.7809 0.5206 0.7673 -0.0336 0.0334  0.0134  117 ALA A CA    
817  C C     . ALA A 117 ? 0.8750 0.6068 0.8642 -0.0314 0.0323  0.0148  117 ALA A C     
818  O O     . ALA A 117 ? 0.8567 0.5814 0.8464 -0.0308 0.0306  0.0078  117 ALA A O     
819  C CB    . ALA A 117 ? 0.7371 0.4780 0.7140 -0.0286 0.0355  0.0077  117 ALA A CB    
820  N N     . GLY A 118 ? 0.8312 0.5648 0.8237 -0.0301 0.0333  0.0247  118 GLY A N     
821  C CA    . GLY A 118 ? 0.8573 0.5861 0.8525 -0.0271 0.0325  0.0281  118 GLY A CA    
822  C C     . GLY A 118 ? 0.8626 0.5945 0.8479 -0.0215 0.0337  0.0279  118 GLY A C     
823  O O     . GLY A 118 ? 0.8768 0.6068 0.8641 -0.0192 0.0322  0.0303  118 GLY A O     
824  N N     . LEU A 119 ? 0.7911 0.5282 0.7663 -0.0199 0.0369  0.0257  119 LEU A N     
825  C CA    . LEU A 119 ? 0.8168 0.5559 0.7800 -0.0165 0.0386  0.0228  119 LEU A CA    
826  C C     . LEU A 119 ? 0.8813 0.6258 0.8359 -0.0151 0.0439  0.0287  119 LEU A C     
827  O O     . LEU A 119 ? 0.8287 0.5744 0.7709 -0.0138 0.0467  0.0251  119 LEU A O     
828  C CB    . LEU A 119 ? 0.7501 0.4881 0.7076 -0.0163 0.0392  0.0127  119 LEU A CB    
829  C CG    . LEU A 119 ? 0.7427 0.4755 0.7048 -0.0171 0.0348  0.0054  119 LEU A CG    
830  C CD1   . LEU A 119 ? 0.7369 0.4701 0.6932 -0.0171 0.0355  -0.0035 119 LEU A CD1   
831  C CD2   . LEU A 119 ? 0.7467 0.4789 0.7087 -0.0147 0.0324  0.0072  119 LEU A CD2   
832  N N     . ALA A 120 ? 0.8938 0.6413 0.8541 -0.0159 0.0460  0.0374  120 ALA A N     
833  C CA    . ALA A 120 ? 0.8783 0.6306 0.8305 -0.0144 0.0527  0.0426  120 ALA A CA    
834  C C     . ALA A 120 ? 0.8822 0.6366 0.8230 -0.0140 0.0531  0.0440  120 ALA A C     
835  O O     . ALA A 120 ? 0.8943 0.6512 0.8228 -0.0137 0.0596  0.0438  120 ALA A O     
836  C CB    . ALA A 120 ? 0.8558 0.6120 0.8178 -0.0154 0.0542  0.0531  120 ALA A CB    
837  N N     . ASP A 121 ? 0.8504 0.6044 0.7950 -0.0146 0.0467  0.0453  121 ASP A N     
838  C CA    . ASP A 121 ? 0.8650 0.6242 0.7996 -0.0153 0.0458  0.0479  121 ASP A CA    
839  C C     . ASP A 121 ? 0.8966 0.6548 0.8192 -0.0157 0.0455  0.0382  121 ASP A C     
840  O O     . ASP A 121 ? 0.9851 0.7483 0.8934 -0.0180 0.0474  0.0383  121 ASP A O     
841  C CB    . ASP A 121 ? 0.8607 0.6219 0.8071 -0.0154 0.0395  0.0565  121 ASP A CB    
842  C CG    . ASP A 121 ? 0.8971 0.6508 0.8574 -0.0142 0.0349  0.0521  121 ASP A CG    
843  O OD1   . ASP A 121 ? 0.9564 0.7039 0.9217 -0.0145 0.0358  0.0460  121 ASP A OD1   
844  O OD2   . ASP A 121 ? 0.8862 0.6410 0.8526 -0.0134 0.0307  0.0554  121 ASP A OD2   
845  N N     . ARG A 122 ? 0.8766 0.6292 0.8037 -0.0146 0.0434  0.0297  122 ARG A N     
846  C CA    . ARG A 122 ? 0.8528 0.6050 0.7698 -0.0152 0.0425  0.0212  122 ARG A CA    
847  C C     . ARG A 122 ? 0.8017 0.5498 0.7102 -0.0149 0.0486  0.0123  122 ARG A C     
848  O O     . ARG A 122 ? 0.7697 0.5171 0.6673 -0.0161 0.0494  0.0051  122 ARG A O     
849  C CB    . ARG A 122 ? 0.9042 0.6541 0.8322 -0.0140 0.0359  0.0185  122 ARG A CB    
850  C CG    . ARG A 122 ? 0.9874 0.7433 0.9212 -0.0139 0.0303  0.0270  122 ARG A CG    
851  C CD    . ARG A 122 ? 1.0580 0.8089 1.0109 -0.0114 0.0262  0.0285  122 ARG A CD    
852  N NE    . ARG A 122 ? 1.2606 1.0079 1.2273 -0.0108 0.0263  0.0361  122 ARG A NE    
853  C CZ    . ARG A 122 ? 1.2140 0.9524 1.1949 -0.0103 0.0260  0.0337  122 ARG A CZ    
854  N NH1   . ARG A 122 ? 1.1897 0.9219 1.1734 -0.0098 0.0256  0.0239  122 ARG A NH1   
855  N NH2   . ARG A 122 ? 0.9617 0.6970 0.9535 -0.0110 0.0265  0.0410  122 ARG A NH2   
856  N N     . ALA A 123 ? 0.8315 0.5777 0.7452 -0.0136 0.0533  0.0138  123 ALA A N     
857  C CA    . ALA A 123 ? 0.8089 0.5520 0.7181 -0.0126 0.0602  0.0081  123 ALA A CA    
858  C C     . ALA A 123 ? 0.8662 0.6107 0.7733 -0.0117 0.0689  0.0141  123 ALA A C     
859  O O     . ALA A 123 ? 0.8663 0.6129 0.7852 -0.0105 0.0696  0.0207  123 ALA A O     
860  C CB    . ALA A 123 ? 0.7523 0.4940 0.6737 -0.0117 0.0577  0.0057  123 ALA A CB    
861  N N     . ARG A 124 ? 0.8862 0.6293 0.7757 -0.0133 0.0759  0.0102  124 ARG A N     
862  C CA    . ARG A 124 ? 0.8796 0.6231 0.7642 -0.0127 0.0862  0.0149  124 ARG A CA    
863  C C     . ARG A 124 ? 0.8923 0.6294 0.7724 -0.0107 0.0979  0.0090  124 ARG A C     
864  O O     . ARG A 124 ? 0.9170 0.6492 0.7890 -0.0120 0.0984  -0.0002 124 ARG A O     
865  C CB    . ARG A 124 ? 0.9149 0.6623 0.7850 -0.0169 0.0864  0.0169  124 ARG A CB    
866  C CG    . ARG A 124 ? 0.9223 0.6770 0.8010 -0.0177 0.0769  0.0265  124 ARG A CG    
867  C CD    . ARG A 124 ? 1.0119 0.7730 0.8771 -0.0219 0.0789  0.0312  124 ARG A CD    
868  N NE    . ARG A 124 ? 1.0343 0.7966 0.8819 -0.0271 0.0779  0.0242  124 ARG A NE    
869  C CZ    . ARG A 124 ? 1.0574 0.8256 0.9060 -0.0295 0.0678  0.0259  124 ARG A CZ    
870  N NH1   . ARG A 124 ? 1.0005 0.7701 0.8676 -0.0260 0.0591  0.0316  124 ARG A NH1   
871  N NH2   . ARG A 124 ? 1.1304 0.9033 0.9618 -0.0359 0.0669  0.0222  124 ARG A NH2   
872  N N     . PHE A 125 ? 0.8598 0.5977 0.7488 -0.0071 0.1071  0.0159  125 PHE A N     
873  C CA    . PHE A 125 ? 0.9011 0.6325 0.7886 -0.0043 0.1200  0.0120  125 PHE A CA    
874  C C     . PHE A 125 ? 0.8936 0.6232 0.7749 -0.0033 0.1338  0.0154  125 PHE A C     
875  O O     . PHE A 125 ? 1.0211 0.7568 0.9044 -0.0037 0.1326  0.0235  125 PHE A O     
876  C CB    . PHE A 125 ? 0.8716 0.6061 0.7786 -0.0002 0.1194  0.0172  125 PHE A CB    
877  C CG    . PHE A 125 ? 0.8708 0.6069 0.7830 -0.0017 0.1073  0.0131  125 PHE A CG    
878  C CD1   . PHE A 125 ? 0.9068 0.6373 0.8127 -0.0022 0.1079  0.0036  125 PHE A CD1   
879  C CD2   . PHE A 125 ? 0.8489 0.5914 0.7715 -0.0032 0.0959  0.0182  125 PHE A CD2   
880  C CE1   . PHE A 125 ? 0.9079 0.6402 0.8181 -0.0036 0.0973  -0.0003 125 PHE A CE1   
881  C CE2   . PHE A 125 ? 0.8521 0.5952 0.7786 -0.0051 0.0860  0.0133  125 PHE A CE2   
882  C CZ    . PHE A 125 ? 0.8676 0.6061 0.7879 -0.0050 0.0867  0.0042  125 PHE A CZ    
883  N N     . GLN A 126 ? 0.8739 0.5941 0.7471 -0.0023 0.1476  0.0085  126 GLN A N     
884  C CA    . GLN A 126 ? 0.9467 0.6624 0.8121 -0.0015 0.1641  0.0094  126 GLN A CA    
885  C C     . GLN A 126 ? 0.9285 0.6334 0.7970 0.0027  0.1804  0.0050  126 GLN A C     
886  O O     . GLN A 126 ? 0.9340 0.6337 0.8028 0.0026  0.1781  -0.0019 126 GLN A O     
887  C CB    . GLN A 126 ? 0.8659 0.5788 0.7057 -0.0092 0.1655  0.0015  126 GLN A CB    
888  C CG    . GLN A 126 ? 0.9333 0.6362 0.7553 -0.0143 0.1684  -0.0128 126 GLN A CG    
889  C CD    . GLN A 126 ? 1.0071 0.7128 0.8052 -0.0239 0.1645  -0.0182 126 GLN A CD    
890  O OE1   . GLN A 126 ? 1.1284 0.8261 0.9060 -0.0298 0.1761  -0.0276 126 GLN A OE1   
891  N NE2   . GLN A 126 ? 0.9812 0.6988 0.7822 -0.0260 0.1485  -0.0118 126 GLN A NE2   
892  N N     . ARG A 127 ? 0.9460 0.6481 0.8192 0.0069  0.1966  0.0101  127 ARG A N     
893  C CA    . ARG A 127 ? 0.9745 0.6646 0.8511 0.0113  0.2153  0.0064  127 ARG A CA    
894  C C     . ARG A 127 ? 1.0038 0.6788 0.8532 0.0048  0.2268  -0.0093 127 ARG A C     
895  O O     . ARG A 127 ? 1.0125 0.6874 0.8442 -0.0006 0.2304  -0.0122 127 ARG A O     
896  C CB    . ARG A 127 ? 1.0303 0.7237 0.9242 0.0187  0.2292  0.0190  127 ARG A CB    
897  C CG    . ARG A 127 ? 1.0615 0.7417 0.9612 0.0243  0.2515  0.0168  127 ARG A CG    
898  C CD    . ARG A 127 ? 1.2174 0.8904 1.1078 0.0249  0.2712  0.0159  127 ARG A CD    
899  N NE    . ARG A 127 ? 1.2753 0.9604 1.1880 0.0321  0.2754  0.0333  127 ARG A NE    
900  C CZ    . ARG A 127 ? 1.3230 1.0079 1.2596 0.0414  0.2902  0.0438  127 ARG A CZ    
901  N NH1   . ARG A 127 ? 1.3071 0.9791 1.2491 0.0452  0.3031  0.0388  127 ARG A NH1   
902  N NH2   . ARG A 127 ? 1.3341 1.0326 1.2907 0.0469  0.2923  0.0607  127 ARG A NH2   
903  N N     . ALA A 128 ? 0.9683 0.6315 0.8136 0.0040  0.2319  -0.0194 128 ALA A N     
904  C CA    . ALA A 128 ? 0.9340 0.5822 0.7525 -0.0041 0.2422  -0.0357 128 ALA A CA    
905  C C     . ALA A 128 ? 1.0676 0.7028 0.8894 -0.0027 0.2492  -0.0437 128 ALA A C     
906  O O     . ALA A 128 ? 1.0838 0.7249 0.9235 0.0019  0.2391  -0.0385 128 ALA A O     
907  C CB    . ALA A 128 ? 0.9349 0.5893 0.7304 -0.0149 0.2264  -0.0429 128 ALA A CB    
908  N N     . ASP A 129 ? 1.1217 0.7392 0.9245 -0.0080 0.2662  -0.0572 129 ASP A N     
909  C CA    . ASP A 129 ? 1.1274 0.7291 0.9311 -0.0077 0.2766  -0.0663 129 ASP A CA    
910  C C     . ASP A 129 ? 1.1782 0.7763 0.9572 -0.0197 0.2663  -0.0806 129 ASP A C     
911  O O     . ASP A 129 ? 1.2102 0.8054 0.9621 -0.0305 0.2680  -0.0903 129 ASP A O     
912  C CB    . ASP A 129 ? 1.1597 0.7410 0.9594 -0.0061 0.3053  -0.0725 129 ASP A CB    
913  C CG    . ASP A 129 ? 1.2292 0.7939 1.0388 -0.0026 0.3183  -0.0778 129 ASP A CG    
914  O OD1   . ASP A 129 ? 1.2495 0.8168 1.0617 -0.0043 0.3052  -0.0802 129 ASP A OD1   
915  O OD2   . ASP A 129 ? 1.3010 0.8495 1.1168 0.0022  0.3427  -0.0791 129 ASP A OD2   
916  N N     . ALA A 130 ? 1.1628 0.7622 0.9511 -0.0183 0.2564  -0.0815 130 ALA A N     
917  C CA    . ALA A 130 ? 1.1767 0.7741 0.9443 -0.0292 0.2463  -0.0938 130 ALA A CA    
918  C C     . ALA A 130 ? 1.1911 0.7690 0.9327 -0.0394 0.2638  -0.1100 130 ALA A C     
919  O O     . ALA A 130 ? 1.2191 0.7980 0.9355 -0.0521 0.2568  -0.1203 130 ALA A O     
920  C CB    . ALA A 130 ? 1.1532 0.7519 0.9370 -0.0250 0.2377  -0.0923 130 ALA A CB    
921  N N     . MET A 131 ? 1.1744 0.7350 0.9220 -0.0344 0.2874  -0.1122 131 MET A N     
922  C CA    . MET A 131 ? 1.2417 0.7808 0.9647 -0.0444 0.3072  -0.1289 131 MET A CA    
923  C C     . MET A 131 ? 1.3069 0.8497 1.0004 -0.0565 0.3070  -0.1356 131 MET A C     
924  O O     . MET A 131 ? 1.3769 0.9082 1.0413 -0.0707 0.3143  -0.1515 131 MET A O     
925  C CB    . MET A 131 ? 1.2787 0.7991 1.0170 -0.0351 0.3344  -0.1277 131 MET A CB    
926  C CG    . MET A 131 ? 1.4350 0.9286 1.1577 -0.0428 0.3546  -0.1452 131 MET A CG    
927  S SD    . MET A 131 ? 1.3234 0.8103 1.0720 -0.0348 0.3539  -0.1420 131 MET A SD    
928  C CE    . MET A 131 ? 1.3057 0.8014 1.0957 -0.0146 0.3613  -0.1194 131 MET A CE    
929  N N     . ASP A 132 ? 1.2884 0.8478 0.9879 -0.0522 0.2985  -0.1237 132 ASP A N     
930  C CA    . ASP A 132 ? 1.2391 0.8050 0.9121 -0.0635 0.2973  -0.1279 132 ASP A CA    
931  C C     . ASP A 132 ? 1.2423 0.8340 0.9247 -0.0608 0.2725  -0.1136 132 ASP A C     
932  O O     . ASP A 132 ? 1.2200 0.8210 0.9216 -0.0506 0.2711  -0.0999 132 ASP A O     
933  C CB    . ASP A 132 ? 1.3314 0.8857 1.0013 -0.0609 0.3215  -0.1289 132 ASP A CB    
934  C CG    . ASP A 132 ? 1.4113 0.9636 1.0451 -0.0770 0.3279  -0.1407 132 ASP A CG    
935  O OD1   . ASP A 132 ? 1.3797 0.9415 0.9916 -0.0905 0.3123  -0.1466 132 ASP A OD1   
936  O OD2   . ASP A 132 ? 1.4413 0.9838 1.0693 -0.0762 0.3486  -0.1431 132 ASP A OD2   
937  N N     . LEU A 133 ? 1.2291 0.8320 0.8996 -0.0697 0.2532  -0.1162 133 LEU A N     
938  C CA    . LEU A 133 ? 1.1843 0.8097 0.8665 -0.0665 0.2301  -0.1029 133 LEU A CA    
939  C C     . LEU A 133 ? 1.1854 0.8226 0.8523 -0.0732 0.2278  -0.0987 133 LEU A C     
940  O O     . LEU A 133 ? 1.2213 0.8595 0.8599 -0.0876 0.2287  -0.1075 133 LEU A O     
941  C CB    . LEU A 133 ? 1.1398 0.7733 0.8177 -0.0725 0.2115  -0.1058 133 LEU A CB    
942  C CG    . LEU A 133 ? 1.1693 0.7986 0.8668 -0.0650 0.2064  -0.1058 133 LEU A CG    
943  C CD1   . LEU A 133 ? 1.1367 0.7765 0.8261 -0.0728 0.1880  -0.1085 133 LEU A CD1   
944  C CD2   . LEU A 133 ? 1.1366 0.7725 0.8659 -0.0499 0.2016  -0.0918 133 LEU A CD2   
945  N N     . PRO A 134 ? 1.1635 0.8107 0.8473 -0.0644 0.2247  -0.0852 134 PRO A N     
946  C CA    . PRO A 134 ? 1.1075 0.7681 0.7785 -0.0706 0.2207  -0.0793 134 PRO A CA    
947  C C     . PRO A 134 ? 1.1204 0.8003 0.7876 -0.0768 0.1977  -0.0732 134 PRO A C     
948  O O     . PRO A 134 ? 1.2127 0.9068 0.8957 -0.0711 0.1857  -0.0595 134 PRO A O     
949  C CB    . PRO A 134 ? 1.0882 0.7532 0.7839 -0.0576 0.2237  -0.0653 134 PRO A CB    
950  C CG    . PRO A 134 ? 1.1403 0.8037 0.8638 -0.0461 0.2171  -0.0602 134 PRO A CG    
951  C CD    . PRO A 134 ? 1.1023 0.7495 0.8178 -0.0490 0.2258  -0.0739 134 PRO A CD    
952  N N     . PHE A 135 ? 1.1644 0.8457 0.8128 -0.0883 0.1914  -0.0821 135 PHE A N     
953  C CA    . PHE A 135 ? 1.2045 0.9045 0.8560 -0.0917 0.1693  -0.0743 135 PHE A CA    
954  C C     . PHE A 135 ? 1.1439 0.8496 0.7651 -0.1093 0.1668  -0.0825 135 PHE A C     
955  O O     . PHE A 135 ? 1.1300 0.8216 0.7317 -0.1178 0.1790  -0.0973 135 PHE A O     
956  C CB    . PHE A 135 ? 1.1312 0.8304 0.8045 -0.0831 0.1579  -0.0727 135 PHE A CB    
957  C CG    . PHE A 135 ? 1.0950 0.7934 0.7990 -0.0675 0.1560  -0.0626 135 PHE A CG    
958  C CD1   . PHE A 135 ? 1.0788 0.7916 0.7987 -0.0624 0.1432  -0.0487 135 PHE A CD1   
959  C CD2   . PHE A 135 ? 1.1176 0.8015 0.8349 -0.0589 0.1669  -0.0665 135 PHE A CD2   
960  C CE1   . PHE A 135 ? 1.0284 0.7408 0.7745 -0.0503 0.1413  -0.0402 135 PHE A CE1   
961  C CE2   . PHE A 135 ? 1.0614 0.7474 0.8058 -0.0465 0.1644  -0.0564 135 PHE A CE2   
962  C CZ    . PHE A 135 ? 0.9813 0.6813 0.7388 -0.0429 0.1515  -0.0439 135 PHE A CZ    
963  N N     . GLU A 136 ? 1.1625 0.8895 0.7807 -0.1153 0.1510  -0.0723 136 GLU A N     
964  C CA    . GLU A 136 ? 1.2041 0.9411 0.7941 -0.1333 0.1469  -0.0775 136 GLU A CA    
965  C C     . GLU A 136 ? 1.1777 0.9104 0.7643 -0.1379 0.1414  -0.0865 136 GLU A C     
966  O O     . GLU A 136 ? 1.2505 0.9807 0.8600 -0.1268 0.1338  -0.0835 136 GLU A O     
967  C CB    . GLU A 136 ? 1.2727 1.0362 0.8644 -0.1378 0.1301  -0.0613 136 GLU A CB    
968  C CG    . GLU A 136 ? 1.4879 1.2625 1.0472 -0.1563 0.1340  -0.0637 136 GLU A CG    
969  C CD    . GLU A 136 ? 1.6623 1.4583 1.2263 -0.1566 0.1259  -0.0462 136 GLU A CD    
970  O OE1   . GLU A 136 ? 1.6982 1.4886 1.2633 -0.1516 0.1370  -0.0444 136 GLU A OE1   
971  O OE2   . GLU A 136 ? 1.7615 1.5804 1.3292 -0.1616 0.1088  -0.0333 136 GLU A OE2   
972  N N     . ASP A 137 ? 1.1834 0.9154 0.7401 -0.1554 0.1457  -0.0979 137 ASP A N     
973  C CA    . ASP A 137 ? 1.2150 0.9465 0.7660 -0.1625 0.1388  -0.1052 137 ASP A CA    
974  C C     . ASP A 137 ? 1.1745 0.9284 0.7443 -0.1587 0.1164  -0.0901 137 ASP A C     
975  O O     . ASP A 137 ? 1.1703 0.9449 0.7435 -0.1601 0.1058  -0.0759 137 ASP A O     
976  C CB    . ASP A 137 ? 1.2597 0.9929 0.7735 -0.1853 0.1440  -0.1171 137 ASP A CB    
977  C CG    . ASP A 137 ? 1.3134 1.0208 0.8064 -0.1906 0.1687  -0.1349 137 ASP A CG    
978  O OD1   . ASP A 137 ? 1.3142 1.0047 0.8236 -0.1757 0.1817  -0.1356 137 ASP A OD1   
979  O OD2   . ASP A 137 ? 1.3713 1.0759 0.8320 -0.2104 0.1754  -0.1478 137 ASP A OD2   
980  N N     . GLU A 138 ? 1.1925 0.9420 0.7761 -0.1531 0.1103  -0.0927 138 GLU A N     
981  C CA    . GLU A 138 ? 1.1950 0.9640 0.7950 -0.1506 0.0908  -0.0807 138 GLU A CA    
982  C C     . GLU A 138 ? 1.1900 0.9691 0.8178 -0.1360 0.0818  -0.0641 138 GLU A C     
983  O O     . GLU A 138 ? 1.1968 0.9973 0.8324 -0.1375 0.0678  -0.0501 138 GLU A O     
984  C CB    . GLU A 138 ? 1.1919 0.9827 0.7708 -0.1691 0.0809  -0.0771 138 GLU A CB    
985  C CG    . GLU A 138 ? 1.2041 0.9859 0.7550 -0.1857 0.0881  -0.0937 138 GLU A CG    
986  C CD    . GLU A 138 ? 1.2484 1.0547 0.7854 -0.2026 0.0741  -0.0882 138 GLU A CD    
987  O OE1   . GLU A 138 ? 1.2127 1.0441 0.7627 -0.2011 0.0589  -0.0701 138 GLU A OE1   
988  O OE2   . GLU A 138 ? 1.2794 1.0796 0.7931 -0.2177 0.0788  -0.1016 138 GLU A OE2   
989  N N     . SER A 139 ? 1.1256 0.8897 0.7696 -0.1221 0.0901  -0.0650 139 SER A N     
990  C CA    . SER A 139 ? 1.0853 0.8567 0.7530 -0.1100 0.0839  -0.0507 139 SER A CA    
991  C C     . SER A 139 ? 1.1092 0.8781 0.8049 -0.0965 0.0760  -0.0468 139 SER A C     
992  O O     . SER A 139 ? 1.1559 0.9326 0.8715 -0.0882 0.0684  -0.0346 139 SER A O     
993  C CB    . SER A 139 ? 1.1128 0.8723 0.7807 -0.1043 0.0977  -0.0521 139 SER A CB    
994  O OG    . SER A 139 ? 1.1856 0.9248 0.8593 -0.0969 0.1092  -0.0625 139 SER A OG    
995  N N     . PHE A 140 ? 1.1241 0.8819 0.8215 -0.0948 0.0783  -0.0569 140 PHE A N     
996  C CA    . PHE A 140 ? 1.0539 0.8069 0.7758 -0.0824 0.0736  -0.0552 140 PHE A CA    
997  C C     . PHE A 140 ? 1.0174 0.7769 0.7415 -0.0853 0.0637  -0.0571 140 PHE A C     
998  O O     . PHE A 140 ? 1.0294 0.7862 0.7358 -0.0950 0.0665  -0.0663 140 PHE A O     
999  C CB    . PHE A 140 ? 1.0306 0.7646 0.7568 -0.0756 0.0864  -0.0640 140 PHE A CB    
1000 C CG    . PHE A 140 ? 1.0529 0.7829 0.7892 -0.0678 0.0929  -0.0583 140 PHE A CG    
1001 C CD1   . PHE A 140 ? 1.0109 0.7462 0.7703 -0.0581 0.0850  -0.0483 140 PHE A CD1   
1002 C CD2   . PHE A 140 ? 1.0410 0.7618 0.7639 -0.0706 0.1074  -0.0629 140 PHE A CD2   
1003 C CE1   . PHE A 140 ? 0.9996 0.7323 0.7688 -0.0516 0.0905  -0.0422 140 PHE A CE1   
1004 C CE2   . PHE A 140 ? 0.9956 0.7140 0.7292 -0.0631 0.1136  -0.0564 140 PHE A CE2   
1005 C CZ    . PHE A 140 ? 1.0244 0.7494 0.7812 -0.0538 0.1046  -0.0456 140 PHE A CZ    
1006 N N     . ASP A 141 ? 1.0139 0.7810 0.7599 -0.0771 0.0531  -0.0486 141 ASP A N     
1007 C CA    . ASP A 141 ? 0.9840 0.7564 0.7359 -0.0777 0.0448  -0.0500 141 ASP A CA    
1008 C C     . ASP A 141 ? 0.9491 0.7065 0.7046 -0.0733 0.0508  -0.0612 141 ASP A C     
1009 O O     . ASP A 141 ? 1.0220 0.7818 0.7779 -0.0755 0.0461  -0.0649 141 ASP A O     
1010 C CB    . ASP A 141 ? 0.9086 0.6922 0.6837 -0.0699 0.0337  -0.0380 141 ASP A CB    
1011 C CG    . ASP A 141 ? 0.9452 0.7449 0.7210 -0.0732 0.0274  -0.0243 141 ASP A CG    
1012 O OD1   . ASP A 141 ? 1.0079 0.8214 0.7704 -0.0837 0.0228  -0.0208 141 ASP A OD1   
1013 O OD2   . ASP A 141 ? 0.9781 0.7779 0.7689 -0.0657 0.0266  -0.0161 141 ASP A OD2   
1014 N N     . ALA A 142 ? 0.9726 0.7158 0.7317 -0.0671 0.0609  -0.0654 142 ALA A N     
1015 C CA    . ALA A 142 ? 0.9656 0.6967 0.7315 -0.0621 0.0662  -0.0733 142 ALA A CA    
1016 C C     . ALA A 142 ? 0.9613 0.6797 0.7313 -0.0561 0.0783  -0.0750 142 ALA A C     
1017 O O     . ALA A 142 ? 0.9865 0.7065 0.7612 -0.0526 0.0801  -0.0683 142 ALA A O     
1018 C CB    . ALA A 142 ? 0.9640 0.7002 0.7505 -0.0544 0.0567  -0.0695 142 ALA A CB    
1019 N N     . VAL A 143 ? 0.9255 0.6320 0.6953 -0.0548 0.0869  -0.0828 143 VAL A N     
1020 C CA    . VAL A 143 ? 0.9021 0.5973 0.6779 -0.0489 0.0995  -0.0832 143 VAL A CA    
1021 C C     . VAL A 143 ? 0.9417 0.6329 0.7332 -0.0423 0.0996  -0.0844 143 VAL A C     
1022 O O     . VAL A 143 ? 1.0307 0.7205 0.8188 -0.0455 0.0972  -0.0904 143 VAL A O     
1023 C CB    . VAL A 143 ? 0.9287 0.6112 0.6852 -0.0556 0.1144  -0.0918 143 VAL A CB    
1024 C CG1   . VAL A 143 ? 1.0013 0.6737 0.7668 -0.0483 0.1283  -0.0896 143 VAL A CG1   
1025 C CG2   . VAL A 143 ? 0.9583 0.6470 0.6948 -0.0654 0.1128  -0.0922 143 VAL A CG2   
1026 N N     . ILE A 144 ? 0.8767 0.5676 0.6853 -0.0340 0.1019  -0.0780 144 ILE A N     
1027 C CA    . ILE A 144 ? 0.9404 0.6296 0.7642 -0.0286 0.1025  -0.0777 144 ILE A CA    
1028 C C     . ILE A 144 ? 1.0254 0.7061 0.8563 -0.0238 0.1167  -0.0752 144 ILE A C     
1029 O O     . ILE A 144 ? 1.0217 0.7026 0.8546 -0.0214 0.1217  -0.0696 144 ILE A O     
1030 C CB    . ILE A 144 ? 0.9480 0.6483 0.7881 -0.0240 0.0900  -0.0711 144 ILE A CB    
1031 C CG1   . ILE A 144 ? 0.9511 0.6522 0.8081 -0.0186 0.0914  -0.0682 144 ILE A CG1   
1032 C CG2   . ILE A 144 ? 0.9027 0.6085 0.7470 -0.0222 0.0868  -0.0634 144 ILE A CG2   
1033 C CD1   . ILE A 144 ? 0.8298 0.5408 0.6993 -0.0165 0.0797  -0.0644 144 ILE A CD1   
1034 N N     . ALA A 145 ? 1.0303 0.7036 0.8656 -0.0224 0.1241  -0.0786 145 ALA A N     
1035 C CA    . ALA A 145 ? 1.0345 0.6994 0.8795 -0.0172 0.1391  -0.0752 145 ALA A CA    
1036 C C     . ALA A 145 ? 0.9984 0.6696 0.8641 -0.0115 0.1360  -0.0688 145 ALA A C     
1037 O O     . ALA A 145 ? 0.9946 0.6601 0.8640 -0.0111 0.1413  -0.0716 145 ALA A O     
1038 C CB    . ALA A 145 ? 1.0012 0.6497 0.8315 -0.0217 0.1538  -0.0851 145 ALA A CB    
1039 N N     . LEU A 146 ? 0.8772 0.5605 0.7554 -0.0083 0.1266  -0.0607 146 LEU A N     
1040 C CA    . LEU A 146 ? 0.9408 0.6332 0.8375 -0.0047 0.1220  -0.0540 146 LEU A CA    
1041 C C     . LEU A 146 ? 0.9514 0.6417 0.8632 0.0010  0.1353  -0.0452 146 LEU A C     
1042 O O     . LEU A 146 ? 0.9230 0.6164 0.8415 0.0040  0.1391  -0.0372 146 LEU A O     
1043 C CB    . LEU A 146 ? 0.8913 0.5969 0.7952 -0.0044 0.1090  -0.0482 146 LEU A CB    
1044 C CG    . LEU A 146 ? 0.8821 0.5999 0.8030 -0.0028 0.1026  -0.0410 146 LEU A CG    
1045 C CD1   . LEU A 146 ? 0.8355 0.5551 0.7553 -0.0050 0.0970  -0.0469 146 LEU A CD1   
1046 C CD2   . LEU A 146 ? 0.8706 0.5983 0.7961 -0.0040 0.0922  -0.0365 146 LEU A CD2   
1047 N N     . GLU A 147 ? 0.9715 0.6576 0.8898 0.0025  0.1423  -0.0452 147 GLU A N     
1048 C CA    . GLU A 147 ? 0.9718 0.6562 0.9078 0.0085  0.1558  -0.0355 147 GLU A CA    
1049 C C     . GLU A 147 ? 0.9726 0.6469 0.9066 0.0114  0.1707  -0.0337 147 GLU A C     
1050 O O     . GLU A 147 ? 0.9796 0.6587 0.9312 0.0173  0.1786  -0.0213 147 GLU A O     
1051 C CB    . GLU A 147 ? 0.8865 0.5896 0.8439 0.0115  0.1483  -0.0215 147 GLU A CB    
1052 C CG    . GLU A 147 ? 0.8866 0.5958 0.8528 0.0110  0.1442  -0.0200 147 GLU A CG    
1053 C CD    . GLU A 147 ? 0.9192 0.6480 0.9078 0.0132  0.1397  -0.0042 147 GLU A CD    
1054 O OE1   . GLU A 147 ? 1.0000 0.7351 1.0033 0.0173  0.1462  0.0087  147 GLU A OE1   
1055 O OE2   . GLU A 147 ? 0.8805 0.6196 0.8718 0.0100  0.1296  -0.0044 147 GLU A OE2   
1056 N N     . SER A 148 ? 0.9658 0.6273 0.8782 0.0068  0.1747  -0.0455 148 SER A N     
1057 C CA    . SER A 148 ? 1.0244 0.6763 0.9328 0.0088  0.1895  -0.0449 148 SER A CA    
1058 C C     . SER A 148 ? 1.0624 0.6935 0.9617 0.0075  0.2081  -0.0543 148 SER A C     
1059 O O     . SER A 148 ? 1.0450 0.6685 0.9565 0.0134  0.2254  -0.0485 148 SER A O     
1060 C CB    . SER A 148 ? 1.0216 0.6760 0.9121 0.0038  0.1814  -0.0496 148 SER A CB    
1061 O OG    . SER A 148 ? 1.0586 0.7123 0.9312 -0.0037 0.1702  -0.0607 148 SER A OG    
1062 N N     . ILE A 149 ? 1.0630 0.6851 0.9432 -0.0002 0.2054  -0.0681 149 ILE A N     
1063 C CA    . ILE A 149 ? 1.0683 0.6687 0.9344 -0.0044 0.2231  -0.0799 149 ILE A CA    
1064 C C     . ILE A 149 ? 1.0708 0.6614 0.9575 0.0031  0.2408  -0.0739 149 ILE A C     
1065 O O     . ILE A 149 ? 1.1053 0.6759 0.9856 0.0021  0.2607  -0.0810 149 ILE A O     
1066 C CB    . ILE A 149 ? 1.1213 0.7165 0.9669 -0.0145 0.2155  -0.0939 149 ILE A CB    
1067 C CG1   . ILE A 149 ? 1.0422 0.6188 0.8617 -0.0237 0.2290  -0.1085 149 ILE A CG1   
1068 C CG2   . ILE A 149 ? 1.0276 0.6193 0.8864 -0.0122 0.2177  -0.0933 149 ILE A CG2   
1069 C CD1   . ILE A 149 ? 1.0005 0.5747 0.7970 -0.0359 0.2202  -0.1218 149 ILE A CD1   
1070 N N     . ILE A 150 ? 1.0333 0.6379 0.9453 0.0102  0.2345  -0.0602 150 ILE A N     
1071 C CA    . ILE A 150 ? 1.0643 0.6631 0.9996 0.0177  0.2495  -0.0514 150 ILE A CA    
1072 C C     . ILE A 150 ? 1.0810 0.6731 1.0292 0.0252  0.2690  -0.0429 150 ILE A C     
1073 O O     . ILE A 150 ? 1.1337 0.7099 1.0923 0.0295  0.2898  -0.0420 150 ILE A O     
1074 C CB    . ILE A 150 ? 1.0410 0.6614 0.9989 0.0219  0.2352  -0.0374 150 ILE A CB    
1075 C CG1   . ILE A 150 ? 0.9908 0.6319 0.9568 0.0244  0.2222  -0.0260 150 ILE A CG1   
1076 C CG2   . ILE A 150 ? 0.9747 0.5989 0.9199 0.0148  0.2193  -0.0470 150 ILE A CG2   
1077 C CD1   . ILE A 150 ? 0.9836 0.6464 0.9686 0.0263  0.2082  -0.0135 150 ILE A CD1   
1078 N N     . HIS A 151 ? 1.1014 0.7054 1.0508 0.0272  0.2635  -0.0359 151 HIS A N     
1079 C CA    . HIS A 151 ? 1.1152 0.7147 1.0762 0.0342  0.2812  -0.0273 151 HIS A CA    
1080 C C     . HIS A 151 ? 1.1543 0.7309 1.0916 0.0295  0.2983  -0.0427 151 HIS A C     
1081 O O     . HIS A 151 ? 1.2637 0.8324 1.2090 0.0352  0.3170  -0.0378 151 HIS A O     
1082 C CB    . HIS A 151 ? 1.0706 0.6909 1.0391 0.0366  0.2688  -0.0152 151 HIS A CB    
1083 C CG    . HIS A 151 ? 1.1000 0.7444 1.0914 0.0400  0.2529  0.0007  151 HIS A CG    
1084 N ND1   . HIS A 151 ? 1.0618 0.7148 1.0835 0.0481  0.2608  0.0181  151 HIS A ND1   
1085 C CD2   . HIS A 151 ? 1.0795 0.7418 1.0678 0.0358  0.2304  0.0026  151 HIS A CD2   
1086 C CE1   . HIS A 151 ? 0.9868 0.6632 1.0213 0.0475  0.2428  0.0295  151 HIS A CE1   
1087 N NE2   . HIS A 151 ? 1.0264 0.7075 1.0406 0.0401  0.2249  0.0195  151 HIS A NE2   
1088 N N     . MET A 152 ? 1.1333 0.7006 1.0412 0.0187  0.2921  -0.0604 152 MET A N     
1089 C CA    . MET A 152 ? 1.2023 0.7532 1.0857 0.0125  0.3055  -0.0734 152 MET A CA    
1090 C C     . MET A 152 ? 1.2777 0.8015 1.1570 0.0114  0.3308  -0.0839 152 MET A C     
1091 O O     . MET A 152 ? 1.2987 0.8155 1.1870 0.0121  0.3335  -0.0852 152 MET A O     
1092 C CB    . MET A 152 ? 1.1870 0.7420 1.0396 0.0002  0.2885  -0.0864 152 MET A CB    
1093 C CG    . MET A 152 ? 1.1729 0.7517 1.0301 0.0018  0.2670  -0.0762 152 MET A CG    
1094 S SD    . MET A 152 ? 1.1355 0.7236 0.9647 -0.0106 0.2445  -0.0868 152 MET A SD    
1095 C CE    . MET A 152 ? 1.0956 0.7085 0.9424 -0.0042 0.2255  -0.0705 152 MET A CE    
1096 N N     . PRO A 153 ? 1.3029 0.8106 1.1699 0.0097  0.3508  -0.0910 153 PRO A N     
1097 C CA    . PRO A 153 ? 1.2860 0.7649 1.1506 0.0091  0.3787  -0.1012 153 PRO A CA    
1098 C C     . PRO A 153 ? 1.3353 0.7965 1.1702 -0.0053 0.3797  -0.1225 153 PRO A C     
1099 O O     . PRO A 153 ? 1.3817 0.8197 1.2192 -0.0056 0.3999  -0.1300 153 PRO A O     
1100 C CB    . PRO A 153 ? 1.2843 0.7538 1.1420 0.0106  0.3981  -0.1028 153 PRO A CB    
1101 C CG    . PRO A 153 ? 1.2875 0.7837 1.1628 0.0190  0.3833  -0.0841 153 PRO A CG    
1102 C CD    . PRO A 153 ? 1.3168 0.8345 1.1860 0.0139  0.3520  -0.0825 153 PRO A CD    
1103 N N     . ASP A 154 ? 1.3524 0.8235 1.1604 -0.0174 0.3595  -0.1321 154 ASP A N     
1104 C CA    . ASP A 154 ? 1.3405 0.7963 1.1205 -0.0322 0.3607  -0.1514 154 ASP A CA    
1105 C C     . ASP A 154 ? 1.2951 0.7716 1.0604 -0.0407 0.3314  -0.1532 154 ASP A C     
1106 O O     . ASP A 154 ? 1.2818 0.7724 1.0322 -0.0455 0.3188  -0.1528 154 ASP A O     
1107 C CB    . ASP A 154 ? 1.3475 0.7825 1.0974 -0.0434 0.3805  -0.1684 154 ASP A CB    
1108 C CG    . ASP A 154 ? 1.3581 0.7800 1.0751 -0.0619 0.3797  -0.1889 154 ASP A CG    
1109 O OD1   . ASP A 154 ? 1.3807 0.7819 1.1007 -0.0637 0.3938  -0.1967 154 ASP A OD1   
1110 O OD2   . ASP A 154 ? 1.3699 0.8027 1.0589 -0.0750 0.3651  -0.1962 154 ASP A OD2   
1111 N N     . ARG A 155 ? 1.2108 0.6893 0.9812 -0.0425 0.3212  -0.1545 155 ARG A N     
1112 C CA    . ARG A 155 ? 1.1868 0.6846 0.9449 -0.0501 0.2948  -0.1558 155 ARG A CA    
1113 C C     . ARG A 155 ? 1.2493 0.7416 0.9701 -0.0679 0.2932  -0.1724 155 ARG A C     
1114 O O     . ARG A 155 ? 1.2524 0.7626 0.9601 -0.0735 0.2754  -0.1710 155 ARG A O     
1115 C CB    . ARG A 155 ? 1.1485 0.6503 0.9219 -0.0473 0.2854  -0.1526 155 ARG A CB    
1116 C CG    . ARG A 155 ? 1.1573 0.6715 0.9662 -0.0314 0.2826  -0.1341 155 ARG A CG    
1117 C CD    . ARG A 155 ? 1.1265 0.6461 0.9500 -0.0293 0.2735  -0.1305 155 ARG A CD    
1118 N NE    . ARG A 155 ? 1.0878 0.6210 0.9440 -0.0158 0.2704  -0.1124 155 ARG A NE    
1119 C CZ    . ARG A 155 ? 1.1415 0.6671 1.0207 -0.0058 0.2883  -0.1027 155 ARG A CZ    
1120 N NH1   . ARG A 155 ? 1.1447 0.6482 1.0186 -0.0060 0.3119  -0.1091 155 ARG A NH1   
1121 N NH2   . ARG A 155 ? 1.1540 0.6951 1.0625 0.0042  0.2828  -0.0858 155 ARG A NH2   
1122 N N     . ALA A 156 ? 1.2510 0.7187 0.9545 -0.0775 0.3124  -0.1878 156 ALA A N     
1123 C CA    . ALA A 156 ? 1.2324 0.6962 0.8990 -0.0970 0.3101  -0.2039 156 ALA A CA    
1124 C C     . ALA A 156 ? 1.2446 0.7164 0.8918 -0.1026 0.3094  -0.2048 156 ALA A C     
1125 O O     . ALA A 156 ? 1.2851 0.7639 0.9034 -0.1185 0.3002  -0.2133 156 ALA A O     
1126 C CB    . ALA A 156 ? 1.2325 0.6660 0.8849 -0.1067 0.3335  -0.2209 156 ALA A CB    
1127 N N     . GLN A 157 ? 1.2516 0.7237 0.9142 -0.0904 0.3189  -0.1952 157 GLN A N     
1128 C CA    . GLN A 157 ? 1.2700 0.7523 0.9175 -0.0941 0.3169  -0.1936 157 GLN A CA    
1129 C C     . GLN A 157 ? 1.2900 0.8016 0.9519 -0.0865 0.2915  -0.1772 157 GLN A C     
1130 O O     . GLN A 157 ? 1.2974 0.8248 0.9411 -0.0957 0.2771  -0.1772 157 GLN A O     
1131 C CB    . GLN A 157 ? 1.2974 0.7641 0.9526 -0.0859 0.3422  -0.1924 157 GLN A CB    
1132 C CG    . GLN A 157 ? 1.3652 0.8398 1.0011 -0.0916 0.3435  -0.1926 157 GLN A CG    
1133 C CD    . GLN A 157 ? 1.4006 0.8604 1.0450 -0.0830 0.3694  -0.1909 157 GLN A CD    
1134 O OE1   . GLN A 157 ? 1.5029 0.9415 1.1617 -0.0758 0.3907  -0.1934 157 GLN A OE1   
1135 N NE2   . GLN A 157 ? 1.3579 0.8294 0.9945 -0.0835 0.3678  -0.1858 157 GLN A NE2   
1136 N N     . VAL A 158 ? 1.2343 0.7537 0.9291 -0.0703 0.2863  -0.1626 158 VAL A N     
1137 C CA    . VAL A 158 ? 1.1942 0.7393 0.9026 -0.0641 0.2624  -0.1487 158 VAL A CA    
1138 C C     . VAL A 158 ? 1.1884 0.7459 0.8812 -0.0752 0.2421  -0.1534 158 VAL A C     
1139 O O     . VAL A 158 ? 1.1585 0.7337 0.8433 -0.0791 0.2263  -0.1488 158 VAL A O     
1140 C CB    . VAL A 158 ? 1.2334 0.7843 0.9773 -0.0480 0.2594  -0.1344 158 VAL A CB    
1141 C CG1   . VAL A 158 ? 1.1762 0.7516 0.9326 -0.0432 0.2358  -0.1221 158 VAL A CG1   
1142 C CG2   . VAL A 158 ? 1.2045 0.7469 0.9661 -0.0370 0.2788  -0.1268 158 VAL A CG2   
1143 N N     . LEU A 159 ? 1.1948 0.7429 0.8826 -0.0810 0.2432  -0.1625 159 LEU A N     
1144 C CA    . LEU A 159 ? 1.2196 0.7801 0.8933 -0.0918 0.2246  -0.1664 159 LEU A CA    
1145 C C     . LEU A 159 ? 1.1715 0.7357 0.8132 -0.1079 0.2230  -0.1745 159 LEU A C     
1146 O O     . LEU A 159 ? 1.1814 0.7663 0.8172 -0.1126 0.2043  -0.1690 159 LEU A O     
1147 C CB    . LEU A 159 ? 1.1675 0.7161 0.8414 -0.0957 0.2280  -0.1749 159 LEU A CB    
1148 C CG    . LEU A 159 ? 1.1078 0.6592 0.8136 -0.0808 0.2245  -0.1647 159 LEU A CG    
1149 C CD1   . LEU A 159 ? 1.1654 0.7008 0.8717 -0.0842 0.2335  -0.1732 159 LEU A CD1   
1150 C CD2   . LEU A 159 ? 1.0286 0.6038 0.7470 -0.0761 0.2007  -0.1541 159 LEU A CD2   
1151 N N     . ALA A 160 ? 1.2346 0.7799 0.8561 -0.1168 0.2430  -0.1868 160 ALA A N     
1152 C CA    . ALA A 160 ? 1.3054 0.8562 0.8952 -0.1333 0.2417  -0.1938 160 ALA A CA    
1153 C C     . ALA A 160 ? 1.2203 0.7912 0.8148 -0.1282 0.2311  -0.1807 160 ALA A C     
1154 O O     . ALA A 160 ? 1.2186 0.8080 0.7977 -0.1384 0.2164  -0.1781 160 ALA A O     
1155 C CB    . ALA A 160 ? 1.2127 0.7376 0.7803 -0.1433 0.2678  -0.2101 160 ALA A CB    
1156 N N     . GLN A 161 ? 1.1679 0.7370 0.7856 -0.1122 0.2374  -0.1707 161 GLN A N     
1157 C CA    . GLN A 161 ? 1.1710 0.7575 0.7934 -0.1075 0.2288  -0.1585 161 GLN A CA    
1158 C C     . GLN A 161 ? 1.2129 0.8235 0.8481 -0.1041 0.2031  -0.1464 161 GLN A C     
1159 O O     . GLN A 161 ? 1.2193 0.8471 0.8444 -0.1104 0.1912  -0.1409 161 GLN A O     
1160 C CB    . GLN A 161 ? 1.2150 0.7947 0.8607 -0.0916 0.2414  -0.1500 161 GLN A CB    
1161 C CG    . GLN A 161 ? 1.2992 0.8604 0.9313 -0.0946 0.2669  -0.1583 161 GLN A CG    
1162 C CD    . GLN A 161 ? 1.2975 0.8671 0.9023 -0.1072 0.2667  -0.1612 161 GLN A CD    
1163 O OE1   . GLN A 161 ? 1.2482 0.8302 0.8605 -0.1013 0.2628  -0.1498 161 GLN A OE1   
1164 N NE2   . GLN A 161 ? 1.3005 0.8637 0.8729 -0.1255 0.2711  -0.1760 161 GLN A NE2   
1165 N N     . VAL A 162 ? 1.1909 0.8030 0.8491 -0.0941 0.1951  -0.1416 162 VAL A N     
1166 C CA    . VAL A 162 ? 1.1078 0.7401 0.7778 -0.0914 0.1726  -0.1320 162 VAL A CA    
1167 C C     . VAL A 162 ? 1.1327 0.7751 0.7805 -0.1066 0.1617  -0.1372 162 VAL A C     
1168 O O     . VAL A 162 ? 1.1416 0.8032 0.7883 -0.1093 0.1467  -0.1287 162 VAL A O     
1169 C CB    . VAL A 162 ? 1.0753 0.7055 0.7693 -0.0807 0.1682  -0.1290 162 VAL A CB    
1170 C CG1   . VAL A 162 ? 0.9974 0.6450 0.6970 -0.0819 0.1473  -0.1241 162 VAL A CG1   
1171 C CG2   . VAL A 162 ? 1.0977 0.7275 0.8174 -0.0657 0.1721  -0.1186 162 VAL A CG2   
1172 N N     . GLY A 163 ? 1.1137 0.7435 0.7443 -0.1173 0.1696  -0.1505 163 GLY A N     
1173 C CA    . GLY A 163 ? 1.1055 0.7461 0.7146 -0.1335 0.1592  -0.1552 163 GLY A CA    
1174 C C     . GLY A 163 ? 1.1656 0.8187 0.7529 -0.1453 0.1565  -0.1533 163 GLY A C     
1175 O O     . GLY A 163 ? 1.1726 0.8446 0.7495 -0.1559 0.1419  -0.1496 163 GLY A O     
1176 N N     . ARG A 164 ? 1.2082 0.8525 0.7896 -0.1437 0.1706  -0.1547 164 ARG A N     
1177 C CA    . ARG A 164 ? 1.1896 0.8468 0.7514 -0.1541 0.1686  -0.1516 164 ARG A CA    
1178 C C     . ARG A 164 ? 1.2062 0.8877 0.7857 -0.1463 0.1499  -0.1335 164 ARG A C     
1179 O O     . ARG A 164 ? 1.1884 0.8905 0.7572 -0.1566 0.1365  -0.1273 164 ARG A O     
1180 C CB    . ARG A 164 ? 1.2134 0.8536 0.7666 -0.1529 0.1902  -0.1577 164 ARG A CB    
1181 C CG    . ARG A 164 ? 1.1939 0.8455 0.7242 -0.1647 0.1913  -0.1561 164 ARG A CG    
1182 C CD    . ARG A 164 ? 1.2099 0.8408 0.7279 -0.1655 0.2161  -0.1660 164 ARG A CD    
1183 N NE    . ARG A 164 ? 1.2884 0.9083 0.8354 -0.1454 0.2252  -0.1595 164 ARG A NE    
1184 C CZ    . ARG A 164 ? 1.2609 0.8934 0.8278 -0.1331 0.2184  -0.1443 164 ARG A CZ    
1185 N NH1   . ARG A 164 ? 1.1730 0.8290 0.7365 -0.1373 0.2021  -0.1332 164 ARG A NH1   
1186 N NH2   . ARG A 164 ? 1.2336 0.8556 0.8254 -0.1166 0.2280  -0.1391 164 ARG A NH2   
1187 N N     . VAL A 165 ? 1.2186 0.8982 0.8263 -0.1284 0.1490  -0.1243 165 VAL A N     
1188 C CA    . VAL A 165 ? 1.1946 0.8930 0.8198 -0.1203 0.1348  -0.1079 165 VAL A CA    
1189 C C     . VAL A 165 ? 1.1473 0.8607 0.7870 -0.1178 0.1159  -0.1004 165 VAL A C     
1190 O O     . VAL A 165 ? 1.1530 0.8850 0.8011 -0.1164 0.1024  -0.0877 165 VAL A O     
1191 C CB    . VAL A 165 ? 1.1532 0.8440 0.8019 -0.1039 0.1415  -0.1013 165 VAL A CB    
1192 C CG1   . VAL A 165 ? 1.2024 0.8777 0.8392 -0.1052 0.1621  -0.1084 165 VAL A CG1   
1193 C CG2   . VAL A 165 ? 1.0601 0.7426 0.7320 -0.0920 0.1402  -0.1018 165 VAL A CG2   
1194 N N     . LEU A 166 ? 1.1381 0.8436 0.7823 -0.1167 0.1153  -0.1075 166 LEU A N     
1195 C CA    . LEU A 166 ? 1.1468 0.8660 0.8042 -0.1146 0.0986  -0.1013 166 LEU A CA    
1196 C C     . LEU A 166 ? 1.1489 0.8868 0.7892 -0.1292 0.0879  -0.0981 166 LEU A C     
1197 O O     . LEU A 166 ? 1.2268 0.9616 0.8416 -0.1441 0.0935  -0.1080 166 LEU A O     
1198 C CB    . LEU A 166 ? 1.1359 0.8428 0.7988 -0.1121 0.1016  -0.1103 166 LEU A CB    
1199 C CG    . LEU A 166 ? 1.0589 0.7647 0.7507 -0.0962 0.0970  -0.1040 166 LEU A CG    
1200 C CD1   . LEU A 166 ? 1.0525 0.7439 0.7469 -0.0946 0.1040  -0.1136 166 LEU A CD1   
1201 C CD2   . LEU A 166 ? 1.0393 0.7639 0.7437 -0.0940 0.0796  -0.0938 166 LEU A CD2   
1202 N N     . ARG A 167 ? 1.0752 0.8326 0.7299 -0.1254 0.0730  -0.0840 167 ARG A N     
1203 C CA    . ARG A 167 ? 1.1338 0.9126 0.7765 -0.1385 0.0616  -0.0778 167 ARG A CA    
1204 C C     . ARG A 167 ? 1.2227 1.0030 0.8617 -0.1449 0.0564  -0.0840 167 ARG A C     
1205 O O     . ARG A 167 ? 1.1979 0.9681 0.8526 -0.1351 0.0568  -0.0879 167 ARG A O     
1206 C CB    . ARG A 167 ? 1.1271 0.9257 0.7903 -0.1313 0.0480  -0.0596 167 ARG A CB    
1207 C CG    . ARG A 167 ? 1.1386 0.9349 0.8113 -0.1224 0.0521  -0.0523 167 ARG A CG    
1208 C CD    . ARG A 167 ? 1.0746 0.8914 0.7658 -0.1177 0.0388  -0.0338 167 ARG A CD    
1209 N NE    . ARG A 167 ? 1.1152 0.9296 0.8185 -0.1086 0.0418  -0.0261 167 ARG A NE    
1210 C CZ    . ARG A 167 ? 1.1314 0.9586 0.8548 -0.1020 0.0327  -0.0106 167 ARG A CZ    
1211 N NH1   . ARG A 167 ? 1.2187 1.0623 0.9539 -0.1025 0.0207  -0.0003 167 ARG A NH1   
1212 N NH2   . ARG A 167 ? 1.1688 0.9921 0.9021 -0.0945 0.0363  -0.0046 167 ARG A NH2   
1213 N N     . PRO A 168 ? 1.2223 1.0158 0.8398 -0.1623 0.0517  -0.0850 168 PRO A N     
1214 C CA    . PRO A 168 ? 1.2331 1.0321 0.8487 -0.1691 0.0448  -0.0885 168 PRO A CA    
1215 C C     . PRO A 168 ? 1.2098 1.0198 0.8553 -0.1559 0.0322  -0.0769 168 PRO A C     
1216 O O     . PRO A 168 ? 1.2534 1.0810 0.9143 -0.1506 0.0223  -0.0614 168 PRO A O     
1217 C CB    . PRO A 168 ? 1.2354 1.0552 0.8267 -0.1898 0.0382  -0.0850 168 PRO A CB    
1218 C CG    . PRO A 168 ? 1.2338 1.0426 0.8019 -0.1976 0.0512  -0.0931 168 PRO A CG    
1219 C CD    . PRO A 168 ? 1.2195 1.0184 0.8081 -0.1789 0.0565  -0.0878 168 PRO A CD    
1220 N N     . GLY A 169 ? 1.1802 0.9793 0.8338 -0.1510 0.0336  -0.0847 169 GLY A N     
1221 C CA    . GLY A 169 ? 1.1616 0.9654 0.8430 -0.1373 0.0255  -0.0775 169 GLY A CA    
1222 C C     . GLY A 169 ? 1.1369 0.9234 0.8371 -0.1204 0.0322  -0.0799 169 GLY A C     
1223 O O     . GLY A 169 ? 1.1215 0.9054 0.8394 -0.1111 0.0293  -0.0802 169 GLY A O     
1224 N N     . GLY A 170 ? 1.0891 0.8648 0.7857 -0.1168 0.0413  -0.0817 170 GLY A N     
1225 C CA    . GLY A 170 ? 1.0886 0.8506 0.8035 -0.1019 0.0470  -0.0823 170 GLY A CA    
1226 C C     . GLY A 170 ? 1.0804 0.8243 0.7951 -0.0993 0.0562  -0.0944 170 GLY A C     
1227 O O     . GLY A 170 ? 1.0768 0.8148 0.7744 -0.1096 0.0608  -0.1040 170 GLY A O     
1228 N N     . ARG A 171 ? 0.9884 0.7238 0.7225 -0.0862 0.0589  -0.0934 171 ARG A N     
1229 C CA    . ARG A 171 ? 1.0020 0.7239 0.7411 -0.0824 0.0656  -0.1017 171 ARG A CA    
1230 C C     . ARG A 171 ? 0.9721 0.6794 0.7180 -0.0742 0.0777  -0.1034 171 ARG A C     
1231 O O     . ARG A 171 ? 0.9720 0.6811 0.7251 -0.0685 0.0783  -0.0967 171 ARG A O     
1232 C CB    . ARG A 171 ? 1.0300 0.7589 0.7884 -0.0751 0.0562  -0.0983 171 ARG A CB    
1233 C CG    . ARG A 171 ? 1.0706 0.8120 0.8246 -0.0824 0.0464  -0.0979 171 ARG A CG    
1234 C CD    . ARG A 171 ? 1.0796 0.8272 0.8540 -0.0739 0.0387  -0.0943 171 ARG A CD    
1235 N NE    . ARG A 171 ? 1.0783 0.8367 0.8509 -0.0797 0.0309  -0.0943 171 ARG A NE    
1236 C CZ    . ARG A 171 ? 1.0548 0.8303 0.8296 -0.0829 0.0211  -0.0859 171 ARG A CZ    
1237 N NH1   . ARG A 171 ? 1.0907 0.8745 0.8673 -0.0822 0.0177  -0.0769 171 ARG A NH1   
1238 N NH2   . ARG A 171 ? 1.1482 0.9338 0.9251 -0.0867 0.0145  -0.0851 171 ARG A NH2   
1239 N N     . LEU A 172 ? 0.8839 0.5773 0.6288 -0.0738 0.0875  -0.1113 172 LEU A N     
1240 C CA    . LEU A 172 ? 0.9045 0.5855 0.6588 -0.0658 0.0994  -0.1113 172 LEU A CA    
1241 C C     . LEU A 172 ? 0.9736 0.6539 0.7469 -0.0577 0.0972  -0.1099 172 LEU A C     
1242 O O     . LEU A 172 ? 0.9801 0.6596 0.7515 -0.0612 0.0950  -0.1150 172 LEU A O     
1243 C CB    . LEU A 172 ? 0.8945 0.5589 0.6321 -0.0723 0.1156  -0.1208 172 LEU A CB    
1244 C CG    . LEU A 172 ? 0.9252 0.5745 0.6745 -0.0648 0.1297  -0.1225 172 LEU A CG    
1245 C CD1   . LEU A 172 ? 0.9440 0.5944 0.7096 -0.0541 0.1334  -0.1132 172 LEU A CD1   
1246 C CD2   . LEU A 172 ? 0.9065 0.5382 0.6379 -0.0729 0.1459  -0.1336 172 LEU A CD2   
1247 N N     . VAL A 173 ? 0.8976 0.5800 0.6890 -0.0479 0.0969  -0.1026 173 VAL A N     
1248 C CA    . VAL A 173 ? 0.9112 0.5943 0.7204 -0.0410 0.0956  -0.1003 173 VAL A CA    
1249 C C     . VAL A 173 ? 0.9699 0.6446 0.7891 -0.0347 0.1079  -0.0968 173 VAL A C     
1250 O O     . VAL A 173 ? 1.0062 0.6820 0.8286 -0.0314 0.1106  -0.0912 173 VAL A O     
1251 C CB    . VAL A 173 ? 0.8757 0.5724 0.6988 -0.0362 0.0822  -0.0938 173 VAL A CB    
1252 C CG1   . VAL A 173 ? 0.8450 0.5436 0.6832 -0.0314 0.0807  -0.0927 173 VAL A CG1   
1253 C CG2   . VAL A 173 ? 0.8731 0.5787 0.6882 -0.0416 0.0714  -0.0952 173 VAL A CG2   
1254 N N     . LEU A 174 ? 0.9277 0.5949 0.7531 -0.0329 0.1158  -0.0990 174 LEU A N     
1255 C CA    . LEU A 174 ? 0.9632 0.6235 0.8014 -0.0264 0.1284  -0.0939 174 LEU A CA    
1256 C C     . LEU A 174 ? 0.9557 0.6189 0.8102 -0.0223 0.1276  -0.0906 174 LEU A C     
1257 O O     . LEU A 174 ? 0.9853 0.6499 0.8366 -0.0258 0.1221  -0.0957 174 LEU A O     
1258 C CB    . LEU A 174 ? 0.9673 0.6102 0.7935 -0.0297 0.1457  -0.1005 174 LEU A CB    
1259 C CG    . LEU A 174 ? 0.9830 0.6148 0.7971 -0.0369 0.1507  -0.1113 174 LEU A CG    
1260 C CD1   . LEU A 174 ? 0.9948 0.6156 0.8229 -0.0318 0.1646  -0.1096 174 LEU A CD1   
1261 C CD2   . LEU A 174 ? 0.9430 0.5648 0.7315 -0.0473 0.1569  -0.1219 174 LEU A CD2   
1262 N N     . THR A 175 ? 0.9158 0.5817 0.7884 -0.0152 0.1330  -0.0811 175 THR A N     
1263 C CA    . THR A 175 ? 0.9406 0.6055 0.8276 -0.0120 0.1383  -0.0775 175 THR A CA    
1264 C C     . THR A 175 ? 0.9656 0.6147 0.8547 -0.0097 0.1577  -0.0774 175 THR A C     
1265 O O     . THR A 175 ? 0.9913 0.6329 0.8733 -0.0095 0.1661  -0.0785 175 THR A O     
1266 C CB    . THR A 175 ? 0.8619 0.5429 0.7697 -0.0066 0.1313  -0.0654 175 THR A CB    
1267 O OG1   . THR A 175 ? 0.9181 0.6025 0.8346 -0.0023 0.1353  -0.0563 175 THR A OG1   
1268 C CG2   . THR A 175 ? 0.9062 0.6001 0.8116 -0.0094 0.1145  -0.0672 175 THR A CG2   
1269 N N     . ASP A 176 ? 0.9803 0.6238 0.8793 -0.0080 0.1654  -0.0764 176 ASP A N     
1270 C CA    . ASP A 176 ? 0.9636 0.5902 0.8679 -0.0052 0.1857  -0.0762 176 ASP A CA    
1271 C C     . ASP A 176 ? 1.0005 0.6309 0.9270 -0.0003 0.1894  -0.0671 176 ASP A C     
1272 O O     . ASP A 176 ? 1.0241 0.6673 0.9554 -0.0015 0.1766  -0.0651 176 ASP A O     
1273 C CB    . ASP A 176 ? 1.0355 0.6422 0.9168 -0.0135 0.1947  -0.0919 176 ASP A CB    
1274 C CG    . ASP A 176 ? 1.0884 0.6750 0.9689 -0.0117 0.2174  -0.0942 176 ASP A CG    
1275 O OD1   . ASP A 176 ? 1.0432 0.6305 0.9454 -0.0026 0.2279  -0.0821 176 ASP A OD1   
1276 O OD2   . ASP A 176 ? 1.1249 0.6957 0.9826 -0.0201 0.2249  -0.1080 176 ASP A OD2   
1277 N N     . PHE A 177 ? 0.9820 0.6015 0.9227 0.0053  0.2078  -0.0610 177 PHE A N     
1278 C CA    . PHE A 177 ? 1.0239 0.6438 0.9857 0.0097  0.2147  -0.0523 177 PHE A CA    
1279 C C     . PHE A 177 ? 1.0799 0.6776 1.0313 0.0048  0.2267  -0.0648 177 PHE A C     
1280 O O     . PHE A 177 ? 1.1203 0.6990 1.0510 -0.0008 0.2360  -0.0786 177 PHE A O     
1281 C CB    . PHE A 177 ? 1.0455 0.6674 1.0331 0.0193  0.2288  -0.0360 177 PHE A CB    
1282 C CG    . PHE A 177 ? 1.0428 0.6907 1.0475 0.0236  0.2161  -0.0199 177 PHE A CG    
1283 C CD1   . PHE A 177 ? 1.0013 0.6691 1.0118 0.0214  0.1990  -0.0148 177 PHE A CD1   
1284 C CD2   . PHE A 177 ? 1.0532 0.7059 1.0679 0.0290  0.2219  -0.0097 177 PHE A CD2   
1285 C CE1   . PHE A 177 ? 0.9912 0.6829 1.0159 0.0234  0.1878  -0.0007 177 PHE A CE1   
1286 C CE2   . PHE A 177 ? 0.9977 0.6749 1.0279 0.0315  0.2103  0.0055  177 PHE A CE2   
1287 C CZ    . PHE A 177 ? 0.9658 0.6623 1.0005 0.0281  0.1932  0.0097  177 PHE A CZ    
1288 N N     . PHE A 178 ? 1.0727 0.6733 1.0379 0.0058  0.2264  -0.0601 178 PHE A N     
1289 C CA    . PHE A 178 ? 1.1253 0.7051 1.0824 0.0007  0.2375  -0.0713 178 PHE A CA    
1290 C C     . PHE A 178 ? 1.1119 0.6965 1.0944 0.0055  0.2414  -0.0593 178 PHE A C     
1291 O O     . PHE A 178 ? 1.0730 0.6805 1.0749 0.0107  0.2311  -0.0440 178 PHE A O     
1292 C CB    . PHE A 178 ? 1.1027 0.6809 1.0320 -0.0107 0.2242  -0.0878 178 PHE A CB    
1293 C CG    . PHE A 178 ? 1.1226 0.7212 1.0566 -0.0121 0.2051  -0.0840 178 PHE A CG    
1294 C CD1   . PHE A 178 ? 1.0639 0.6866 1.0089 -0.0076 0.1901  -0.0728 178 PHE A CD1   
1295 C CD2   . PHE A 178 ? 1.1038 0.6971 1.0301 -0.0188 0.2024  -0.0922 178 PHE A CD2   
1296 C CE1   . PHE A 178 ? 0.9882 0.6284 0.9360 -0.0095 0.1741  -0.0706 178 PHE A CE1   
1297 C CE2   . PHE A 178 ? 1.0763 0.6884 1.0068 -0.0200 0.1859  -0.0888 178 PHE A CE2   
1298 C CZ    . PHE A 178 ? 1.0536 0.6889 0.9945 -0.0152 0.1721  -0.0784 178 PHE A CZ    
1299 N N     . GLU A 179 ? 1.1665 0.7293 1.1481 0.0029  0.2565  -0.0664 179 GLU A N     
1300 C CA    . GLU A 179 ? 1.0974 0.6618 1.1026 0.0068  0.2619  -0.0558 179 GLU A CA    
1301 C C     . GLU A 179 ? 1.1232 0.6948 1.1161 -0.0014 0.2460  -0.0638 179 GLU A C     
1302 O O     . GLU A 179 ? 1.1199 0.6754 1.0897 -0.0110 0.2472  -0.0810 179 GLU A O     
1303 C CB    . GLU A 179 ? 1.1996 0.7350 1.2132 0.0090  0.2888  -0.0583 179 GLU A CB    
1304 C CG    . GLU A 179 ? 1.2992 0.8240 1.3221 0.0167  0.3072  -0.0529 179 GLU A CG    
1305 C CD    . GLU A 179 ? 1.3548 0.8451 1.3773 0.0163  0.3354  -0.0618 179 GLU A CD    
1306 O OE1   . GLU A 179 ? 1.3755 0.8452 1.3679 0.0069  0.3412  -0.0822 179 GLU A OE1   
1307 O OE2   . GLU A 179 ? 1.3339 0.8186 1.3863 0.0250  0.3517  -0.0480 179 GLU A OE2   
1308 N N     . ARG A 180 ? 1.0826 0.6800 1.0904 0.0014  0.2309  -0.0512 180 ARG A N     
1309 C CA    . ARG A 180 ? 1.1180 0.7233 1.1177 -0.0053 0.2173  -0.0569 180 ARG A CA    
1310 C C     . ARG A 180 ? 1.1716 0.7588 1.1779 -0.0074 0.2310  -0.0594 180 ARG A C     
1311 O O     . ARG A 180 ? 1.1921 0.7716 1.1813 -0.0162 0.2267  -0.0724 180 ARG A O     
1312 C CB    . ARG A 180 ? 1.0366 0.6730 1.0518 -0.0019 0.2006  -0.0424 180 ARG A CB    
1313 C CG    . ARG A 180 ? 1.0317 0.6844 1.0406 -0.0006 0.1879  -0.0404 180 ARG A CG    
1314 C CD    . ARG A 180 ? 1.0099 0.6926 1.0326 0.0012  0.1724  -0.0270 180 ARG A CD    
1315 N NE    . ARG A 180 ? 0.9811 0.6747 0.9868 -0.0053 0.1548  -0.0368 180 ARG A NE    
1316 C CZ    . ARG A 180 ? 0.9406 0.6580 0.9520 -0.0062 0.1406  -0.0300 180 ARG A CZ    
1317 N NH1   . ARG A 180 ? 0.8744 0.6099 0.9065 -0.0022 0.1399  -0.0130 180 ARG A NH1   
1318 N NH2   . ARG A 180 ? 0.9969 0.7206 0.9929 -0.0117 0.1273  -0.0402 180 ARG A NH2   
1319 N N     . ALA A 181 ? 1.1680 0.7476 1.1995 0.0004  0.2484  -0.0467 181 ALA A N     
1320 C CA    . ALA A 181 ? 1.2104 0.7733 1.2549 0.0003  0.2635  -0.0452 181 ALA A CA    
1321 C C     . ALA A 181 ? 1.2606 0.8176 1.3355 0.0115  0.2835  -0.0284 181 ALA A C     
1322 O O     . ALA A 181 ? 1.1766 0.7516 1.2651 0.0189  0.2798  -0.0143 181 ALA A O     
1323 C CB    . ALA A 181 ? 1.1906 0.7732 1.2448 -0.0016 0.2496  -0.0377 181 ALA A CB    
1324 N N     . PRO A 182 ? 1.3072 0.8398 1.3946 0.0131  0.3051  -0.0284 182 PRO A N     
1325 C CA    . PRO A 182 ? 1.3061 0.8298 1.4231 0.0245  0.3274  -0.0127 182 PRO A CA    
1326 C C     . PRO A 182 ? 1.2496 0.8070 1.3971 0.0345  0.3185  0.0141  182 PRO A C     
1327 O O     . PRO A 182 ? 1.1975 0.7817 1.3510 0.0328  0.2999  0.0233  182 PRO A O     
1328 C CB    . PRO A 182 ? 1.3005 0.8009 1.4312 0.0241  0.3461  -0.0131 182 PRO A CB    
1329 C CG    . PRO A 182 ? 1.3367 0.8194 1.4317 0.0096  0.3404  -0.0390 182 PRO A CG    
1330 C CD    . PRO A 182 ? 1.2865 0.7970 1.3612 0.0040  0.3113  -0.0432 182 PRO A CD    
1331 N N     . LEU A 183 ? 1.2693 0.8267 1.4352 0.0439  0.3315  0.0267  183 LEU A N     
1332 C CA    . LEU A 183 ? 1.2307 0.8229 1.4210 0.0513  0.3205  0.0511  183 LEU A CA    
1333 C C     . LEU A 183 ? 1.2609 0.8652 1.4918 0.0593  0.3294  0.0770  183 LEU A C     
1334 O O     . LEU A 183 ? 1.2864 0.8679 1.5363 0.0651  0.3534  0.0813  183 LEU A O     
1335 C CB    . LEU A 183 ? 1.2736 0.8656 1.4668 0.0575  0.3280  0.0555  183 LEU A CB    
1336 C CG    . LEU A 183 ? 1.2345 0.8651 1.4373 0.0596  0.3078  0.0728  183 LEU A CG    
1337 C CD1   . LEU A 183 ? 1.0868 0.7290 1.2567 0.0495  0.2827  0.0565  183 LEU A CD1   
1338 C CD2   . LEU A 183 ? 1.2149 0.8494 1.4319 0.0677  0.3175  0.0849  183 LEU A CD2   
1339 N N     . ALA A 184 ? 1.2502 0.8910 1.4944 0.0593  0.3104  0.0946  184 ALA A N     
1340 C CA    . ALA A 184 ? 1.2701 0.9324 1.5513 0.0649  0.3123  0.1216  184 ALA A CA    
1341 C C     . ALA A 184 ? 1.2977 0.9688 1.6146 0.0767  0.3275  0.1470  184 ALA A C     
1342 O O     . ALA A 184 ? 1.2647 0.9472 1.5786 0.0787  0.3228  0.1504  184 ALA A O     
1343 C CB    . ALA A 184 ? 1.2912 0.9920 1.5694 0.0588  0.2852  0.1300  184 ALA A CB    
1344 N N     . PRO A 185 ? 1.2747 0.9429 1.6276 0.0846  0.3452  0.1668  185 PRO A N     
1345 C CA    . PRO A 185 ? 1.2686 0.9422 1.6582 0.0970  0.3632  0.1916  185 PRO A CA    
1346 C C     . PRO A 185 ? 1.2606 0.9776 1.6650 0.0983  0.3461  0.2149  185 PRO A C     
1347 O O     . PRO A 185 ? 1.3159 1.0351 1.7269 0.1040  0.3526  0.2212  185 PRO A O     
1348 C CB    . PRO A 185 ? 1.1600 0.8291 1.5865 0.1037  0.3803  0.2107  185 PRO A CB    
1349 C CG    . PRO A 185 ? 1.2531 0.9393 1.6682 0.0941  0.3594  0.2075  185 PRO A CG    
1350 C CD    . PRO A 185 ? 1.2252 0.8934 1.5911 0.0829  0.3464  0.1725  185 PRO A CD    
1351 N N     . GLU A 186 ? 1.2489 1.0012 1.6575 0.0924  0.3244  0.2274  186 GLU A N     
1352 C CA    . GLU A 186 ? 1.2463 1.0417 1.6701 0.0919  0.3086  0.2509  186 GLU A CA    
1353 C C     . GLU A 186 ? 1.2709 1.0684 1.6651 0.0871  0.2960  0.2352  186 GLU A C     
1354 O O     . GLU A 186 ? 1.3032 1.1333 1.7076 0.0861  0.2842  0.2526  186 GLU A O     
1355 C CB    . GLU A 186 ? 1.2595 1.0912 1.6870 0.0837  0.2868  0.2631  186 GLU A CB    
1356 N N     . GLY A 187 ? 1.2451 1.0094 1.6037 0.0836  0.2984  0.2037  187 GLY A N     
1357 C CA    . GLY A 187 ? 1.2353 0.9987 1.5643 0.0788  0.2868  0.1870  187 GLY A CA    
1358 C C     . GLY A 187 ? 1.2682 0.9943 1.5811 0.0826  0.3048  0.1677  187 GLY A C     
1359 O O     . GLY A 187 ? 1.1529 0.8757 1.4401 0.0786  0.2962  0.1528  187 GLY A O     
1360 N N     . ARG A 188 ? 1.3293 1.0264 1.6566 0.0898  0.3303  0.1673  188 ARG A N     
1361 C CA    . ARG A 188 ? 1.3152 0.9793 1.6321 0.0940  0.3507  0.1528  188 ARG A CA    
1362 C C     . ARG A 188 ? 1.2911 0.9704 1.6270 0.1018  0.3557  0.1709  188 ARG A C     
1363 O O     . ARG A 188 ? 1.2870 0.9448 1.6105 0.1042  0.3684  0.1589  188 ARG A O     
1364 C CB    . ARG A 188 ? 1.3489 0.9784 1.6801 0.0999  0.3794  0.1500  188 ARG A CB    
1365 C CG    . ARG A 188 ? 1.3785 0.9828 1.6819 0.0906  0.3780  0.1246  188 ARG A CG    
1366 C CD    . ARG A 188 ? 1.4103 0.9799 1.7293 0.0957  0.4075  0.1224  188 ARG A CD    
1367 N NE    . ARG A 188 ? 1.4224 0.9603 1.7350 0.0998  0.4317  0.1107  188 ARG A NE    
1368 C CZ    . ARG A 188 ? 1.4549 0.9584 1.7319 0.0916  0.4398  0.0805  188 ARG A CZ    
1369 N NH1   . ARG A 188 ? 1.4762 0.9736 1.7206 0.0790  0.4244  0.0589  188 ARG A NH1   
1370 N NH2   . ARG A 188 ? 1.4556 0.9312 1.7299 0.0957  0.4643  0.0721  188 ARG A NH2   
1371 N N     . ALA A 189 ? 1.3124 1.0295 1.6787 0.1052  0.3465  0.2003  189 ALA A N     
1372 C CA    . ALA A 189 ? 1.2723 1.0076 1.6626 0.1128  0.3519  0.2220  189 ALA A CA    
1373 C C     . ALA A 189 ? 1.2394 0.9859 1.6019 0.1059  0.3334  0.2107  189 ALA A C     
1374 O O     . ALA A 189 ? 1.2301 0.9622 1.5859 0.1098  0.3441  0.2043  189 ALA A O     
1375 C CB    . ALA A 189 ? 1.2491 1.0246 1.6805 0.1166  0.3462  0.2584  189 ALA A CB    
1376 N N     . ALA A 190 ? 1.2227 0.9949 1.5693 0.0957  0.3062  0.2084  190 ALA A N     
1377 C CA    . ALA A 190 ? 1.1996 0.9848 1.5230 0.0889  0.2880  0.2001  190 ALA A CA    
1378 C C     . ALA A 190 ? 1.1845 0.9368 1.4697 0.0853  0.2905  0.1684  190 ALA A C     
1379 O O     . ALA A 190 ? 1.2363 0.9896 1.5092 0.0845  0.2868  0.1636  190 ALA A O     
1380 C CB    . ALA A 190 ? 1.1289 0.9457 1.4431 0.0781  0.2604  0.2027  190 ALA A CB    
1381 N N     . VAL A 191 ? 1.1646 0.8889 1.4306 0.0825  0.2963  0.1473  191 VAL A N     
1382 C CA    . VAL A 191 ? 1.1173 0.8131 1.3467 0.0777  0.2979  0.1184  191 VAL A CA    
1383 C C     . VAL A 191 ? 1.2548 0.9279 1.4886 0.0853  0.3215  0.1168  191 VAL A C     
1384 O O     . VAL A 191 ? 1.2166 0.8833 1.4293 0.0829  0.3189  0.1050  191 VAL A O     
1385 C CB    . VAL A 191 ? 1.0700 0.7429 1.2789 0.0718  0.2989  0.0975  191 VAL A CB    
1386 C CG1   . VAL A 191 ? 1.1076 0.7507 1.2812 0.0667  0.3039  0.0700  191 VAL A CG1   
1387 C CG2   . VAL A 191 ? 1.0699 0.7645 1.2687 0.0634  0.2743  0.0956  191 VAL A CG2   
1388 N N     . GLN A 192 ? 1.2936 0.9534 1.5551 0.0946  0.3458  0.1287  192 GLN A N     
1389 C CA    . GLN A 192 ? 1.2442 0.8803 1.5114 0.1024  0.3715  0.1270  192 GLN A CA    
1390 C C     . GLN A 192 ? 1.2331 0.8900 1.5099 0.1064  0.3674  0.1413  192 GLN A C     
1391 O O     . GLN A 192 ? 1.2750 0.9148 1.5384 0.1079  0.3786  0.1308  192 GLN A O     
1392 C CB    . GLN A 192 ? 1.2825 0.9058 1.5853 0.1129  0.3980  0.1426  192 GLN A CB    
1393 C CG    . GLN A 192 ? 1.3080 0.9024 1.6201 0.1219  0.4298  0.1407  192 GLN A CG    
1394 C CD    . GLN A 192 ? 1.4286 1.0121 1.7816 0.1335  0.4568  0.1593  192 GLN A CD    
1395 O OE1   . GLN A 192 ? 1.4993 1.0551 1.8481 0.1319  0.4704  0.1468  192 GLN A OE1   
1396 N NE2   . GLN A 192 ? 1.3709 0.9763 1.7644 0.1449  0.4650  0.1899  192 GLN A NE2   
1397 N N     . ARG A 193 ? 1.2038 0.8987 1.5032 0.1073  0.3512  0.1655  193 ARG A N     
1398 C CA    . ARG A 193 ? 1.2281 0.9469 1.5391 0.1100  0.3454  0.1817  193 ARG A CA    
1399 C C     . ARG A 193 ? 1.2692 0.9894 1.5433 0.1004  0.3261  0.1622  193 ARG A C     
1400 O O     . ARG A 193 ? 1.2764 0.9924 1.5450 0.1027  0.3316  0.1605  193 ARG A O     
1401 C CB    . ARG A 193 ? 1.2251 0.9854 1.5689 0.1110  0.3325  0.2126  193 ARG A CB    
1402 C CG    . ARG A 193 ? 1.2932 1.0832 1.6542 0.1130  0.3261  0.2340  193 ARG A CG    
1403 C CD    . ARG A 193 ? 1.2829 1.0745 1.6841 0.1269  0.3514  0.2593  193 ARG A CD    
1404 N NE    . ARG A 193 ? 1.3926 1.1763 1.7876 0.1305  0.3598  0.2558  193 ARG A NE    
1405 C CZ    . ARG A 193 ? 1.4065 1.1878 1.8304 0.1423  0.3825  0.2732  193 ARG A CZ    
1406 N NH1   . ARG A 193 ? 1.3768 1.1645 1.8419 0.1528  0.3999  0.2980  193 ARG A NH1   
1407 N NH2   . ARG A 193 ? 1.3115 1.0842 1.7240 0.1440  0.3886  0.2664  193 ARG A NH2   
1408 N N     . TYR A 194 ? 1.2657 0.9909 1.5150 0.0900  0.3045  0.1476  194 TYR A N     
1409 C CA    . TYR A 194 ? 1.1962 0.9226 1.4119 0.0810  0.2858  0.1294  194 TYR A CA    
1410 C C     . TYR A 194 ? 1.1828 0.8770 1.3719 0.0806  0.2985  0.1068  194 TYR A C     
1411 O O     . TYR A 194 ? 1.1541 0.8501 1.3316 0.0795  0.2950  0.1033  194 TYR A O     
1412 C CB    . TYR A 194 ? 1.1618 0.8956 1.3592 0.0713  0.2648  0.1180  194 TYR A CB    
1413 C CG    . TYR A 194 ? 1.1663 0.9098 1.3356 0.0615  0.2414  0.1044  194 TYR A CG    
1414 C CD1   . TYR A 194 ? 1.1435 0.9156 1.3199 0.0584  0.2256  0.1174  194 TYR A CD1   
1415 C CD2   . TYR A 194 ? 1.1303 0.8551 1.2672 0.0547  0.2349  0.0792  194 TYR A CD2   
1416 C CE1   . TYR A 194 ? 1.0607 0.8392 1.2130 0.0496  0.2060  0.1047  194 TYR A CE1   
1417 C CE2   . TYR A 194 ? 1.0654 0.7985 1.1797 0.0467  0.2149  0.0681  194 TYR A CE2   
1418 C CZ    . TYR A 194 ? 1.0002 0.7590 1.1228 0.0446  0.2013  0.0806  194 TYR A CZ    
1419 O OH    . TYR A 194 ? 1.0780 0.8429 1.1795 0.0369  0.1833  0.0694  194 TYR A OH    
1420 N N     . LEU A 195 ? 1.1711 0.8361 1.3503 0.0808  0.3138  0.0917  195 LEU A N     
1421 C CA    . LEU A 195 ? 1.1950 0.8304 1.3461 0.0781  0.3253  0.0692  195 LEU A CA    
1422 C C     . LEU A 195 ? 1.2500 0.8760 1.4130 0.0864  0.3467  0.0764  195 LEU A C     
1423 O O     . LEU A 195 ? 1.2191 0.8298 1.3573 0.0829  0.3508  0.0606  195 LEU A O     
1424 C CB    . LEU A 195 ? 1.1991 0.8058 1.3382 0.0753  0.3382  0.0524  195 LEU A CB    
1425 C CG    . LEU A 195 ? 1.2170 0.8204 1.3273 0.0641  0.3203  0.0332  195 LEU A CG    
1426 C CD1   . LEU A 195 ? 1.1648 0.7941 1.2907 0.0633  0.3024  0.0463  195 LEU A CD1   
1427 C CD2   . LEU A 195 ? 1.2406 0.8101 1.3351 0.0602  0.3378  0.0139  195 LEU A CD2   
1428 N N     . HIS A 196 ? 1.2418 0.8772 1.4428 0.0971  0.3610  0.1004  196 HIS A N     
1429 C CA    . HIS A 196 ? 1.2820 0.9125 1.4987 0.1061  0.3812  0.1106  196 HIS A CA    
1430 C C     . HIS A 196 ? 1.2364 0.8951 1.4566 0.1056  0.3650  0.1232  196 HIS A C     
1431 O O     . HIS A 196 ? 1.2584 0.9095 1.4649 0.1056  0.3701  0.1161  196 HIS A O     
1432 C CB    . HIS A 196 ? 1.2789 0.9099 1.5384 0.1185  0.4036  0.1337  196 HIS A CB    
1433 C CG    . HIS A 196 ? 1.3378 0.9572 1.6137 0.1287  0.4299  0.1418  196 HIS A CG    
1434 N ND1   . HIS A 196 ? 1.2713 0.9168 1.5816 0.1376  0.4324  0.1703  196 HIS A ND1   
1435 C CD2   . HIS A 196 ? 1.4554 1.0403 1.7184 0.1309  0.4557  0.1254  196 HIS A CD2   
1436 C CE1   . HIS A 196 ? 1.4085 1.0360 1.7275 0.1460  0.4588  0.1715  196 HIS A CE1   
1437 N NE2   . HIS A 196 ? 1.4811 1.0711 1.7711 0.1420  0.4737  0.1439  196 HIS A NE2   
1438 N N     . ASP A 197 ? 1.1936 0.8852 1.4312 0.1042  0.3453  0.1415  197 ASP A N     
1439 C CA    . ASP A 197 ? 1.1568 0.8770 1.4018 0.1032  0.3307  0.1561  197 ASP A CA    
1440 C C     . ASP A 197 ? 1.1394 0.8583 1.3488 0.0935  0.3124  0.1370  197 ASP A C     
1441 O O     . ASP A 197 ? 1.1198 0.8570 1.3322 0.0925  0.3030  0.1463  197 ASP A O     
1442 C CB    . ASP A 197 ? 1.1432 0.8982 1.4118 0.1015  0.3137  0.1782  197 ASP A CB    
1443 C CG    . ASP A 197 ? 1.2509 1.0151 1.5609 0.1119  0.3307  0.2041  197 ASP A CG    
1444 O OD1   . ASP A 197 ? 1.3097 1.0479 1.6281 0.1208  0.3571  0.2015  197 ASP A OD1   
1445 O OD2   . ASP A 197 ? 1.2815 1.0787 1.6154 0.1109  0.3184  0.2271  197 ASP A OD2   
1446 N N     . PHE A 198 ? 1.1762 0.8756 1.3537 0.0861  0.3065  0.1121  198 PHE A N     
1447 C CA    . PHE A 198 ? 1.1367 0.8352 1.2828 0.0776  0.2904  0.0956  198 PHE A CA    
1448 C C     . PHE A 198 ? 1.1472 0.8142 1.2640 0.0749  0.3025  0.0716  198 PHE A C     
1449 O O     . PHE A 198 ? 1.1648 0.8284 1.2531 0.0670  0.2895  0.0559  198 PHE A O     
1450 C CB    . PHE A 198 ? 1.1001 0.8136 1.2340 0.0686  0.2648  0.0901  198 PHE A CB    
1451 C CG    . PHE A 198 ? 1.1108 0.8576 1.2664 0.0677  0.2495  0.1111  198 PHE A CG    
1452 C CD1   . PHE A 198 ? 1.0420 0.8046 1.2240 0.0707  0.2503  0.1286  198 PHE A CD1   
1453 C CD2   . PHE A 198 ? 1.1885 0.9513 1.3374 0.0630  0.2343  0.1136  198 PHE A CD2   
1454 C CE1   . PHE A 198 ? 1.0409 0.8362 1.2409 0.0678  0.2357  0.1480  198 PHE A CE1   
1455 C CE2   . PHE A 198 ? 1.1674 0.9608 1.3342 0.0600  0.2202  0.1319  198 PHE A CE2   
1456 C CZ    . PHE A 198 ? 1.1264 0.9368 1.3180 0.0619  0.2206  0.1490  198 PHE A CZ    
1457 N N     . MET A 199 ? 1.1340 0.7783 1.2573 0.0807  0.3275  0.0690  199 MET A N     
1458 C CA    . MET A 199 ? 1.1541 0.7683 1.2494 0.0770  0.3418  0.0468  199 MET A CA    
1459 C C     . MET A 199 ? 1.1646 0.7695 1.2270 0.0656  0.3271  0.0245  199 MET A C     
1460 O O     . MET A 199 ? 1.1992 0.8019 1.2340 0.0581  0.3169  0.0108  199 MET A O     
1461 C CB    . MET A 199 ? 1.0747 0.6898 1.1605 0.0775  0.3450  0.0462  199 MET A CB    
1462 C CG    . MET A 199 ? 1.0678 0.7017 1.1864 0.0875  0.3516  0.0713  199 MET A CG    
1463 S SD    . MET A 199 ? 1.2078 0.8333 1.3158 0.0895  0.3655  0.0683  199 MET A SD    
1464 C CE    . MET A 199 ? 1.1821 0.8341 1.3339 0.1013  0.3709  0.1012  199 MET A CE    
1465 N N     . MET A 200 ? 1.1377 0.7386 1.2050 0.0643  0.3258  0.0223  200 MET A N     
1466 C CA    . MET A 200 ? 1.1390 0.7341 1.1790 0.0538  0.3112  0.0036  200 MET A CA    
1467 C C     . MET A 200 ? 1.1985 0.7705 1.2359 0.0523  0.3257  -0.0066 200 MET A C     
1468 O O     . MET A 200 ? 1.2240 0.7909 1.2875 0.0601  0.3421  0.0049  200 MET A O     
1469 C CB    . MET A 200 ? 1.1541 0.7756 1.1994 0.0510  0.2852  0.0111  200 MET A CB    
1470 C CG    . MET A 200 ? 1.1254 0.7706 1.1761 0.0518  0.2702  0.0225  200 MET A CG    
1471 S SD    . MET A 200 ? 1.0684 0.7425 1.1309 0.0489  0.2456  0.0331  200 MET A SD    
1472 C CE    . MET A 200 ? 1.1153 0.7960 1.2149 0.0577  0.2596  0.0540  200 MET A CE    
1473 N N     . THR A 201 ? 1.2051 0.7647 1.2116 0.0416  0.3186  -0.0275 201 THR A N     
1474 C CA    . THR A 201 ? 1.1970 0.7332 1.1941 0.0369  0.3304  -0.0411 201 THR A CA    
1475 C C     . THR A 201 ? 1.1939 0.7380 1.1752 0.0279  0.3091  -0.0504 201 THR A C     
1476 O O     . THR A 201 ? 1.1646 0.7237 1.1301 0.0225  0.2884  -0.0543 201 THR A O     
1477 C CB    . THR A 201 ? 1.1675 0.6757 1.1381 0.0305  0.3485  -0.0603 201 THR A CB    
1478 O OG1   . THR A 201 ? 1.0936 0.6028 1.0300 0.0180  0.3320  -0.0773 201 THR A OG1   
1479 C CG2   . THR A 201 ? 1.2538 0.7615 1.2313 0.0373  0.3615  -0.0529 201 THR A CG2   
1480 N N     . MET A 202 ? 1.1884 0.7219 1.1754 0.0266  0.3151  -0.0533 202 MET A N     
1481 C CA    . MET A 202 ? 1.1194 0.6576 1.0925 0.0181  0.2983  -0.0625 202 MET A CA    
1482 C C     . MET A 202 ? 1.1598 0.6725 1.1029 0.0067  0.3065  -0.0851 202 MET A C     
1483 O O     . MET A 202 ? 1.2346 0.7235 1.1700 0.0054  0.3279  -0.0936 202 MET A O     
1484 C CB    . MET A 202 ? 1.1694 0.7154 1.1695 0.0234  0.2983  -0.0495 202 MET A CB    
1485 C CG    . MET A 202 ? 1.2211 0.7903 1.2539 0.0345  0.2958  -0.0251 202 MET A CG    
1486 S SD    . MET A 202 ? 1.1974 0.7758 1.2662 0.0414  0.3006  -0.0062 202 MET A SD    
1487 C CE    . MET A 202 ? 1.0325 0.6158 1.0808 0.0307  0.2803  -0.0197 202 MET A CE    
1488 N N     . VAL A 203 ? 1.1483 0.6665 1.0741 -0.0025 0.2897  -0.0948 203 VAL A N     
1489 C CA    . VAL A 203 ? 1.2134 0.7105 1.1115 -0.0150 0.2956  -0.1150 203 VAL A CA    
1490 C C     . VAL A 203 ? 1.2827 0.7803 1.1843 -0.0190 0.2891  -0.1170 203 VAL A C     
1491 O O     . VAL A 203 ? 1.1984 0.7160 1.1190 -0.0135 0.2759  -0.1045 203 VAL A O     
1492 C CB    . VAL A 203 ? 1.1640 0.6666 1.0304 -0.0255 0.2817  -0.1273 203 VAL A CB    
1493 C CG1   . VAL A 203 ? 1.1113 0.6139 0.9753 -0.0216 0.2883  -0.1245 203 VAL A CG1   
1494 C CG2   . VAL A 203 ? 1.1847 0.7136 1.0514 -0.0262 0.2552  -0.1221 203 VAL A CG2   
1495 N N     . SER A 204 ? 1.3243 0.7994 1.2072 -0.0295 0.2996  -0.1332 204 SER A N     
1496 C CA    . SER A 204 ? 1.3255 0.8027 1.2020 -0.0373 0.2891  -0.1391 204 SER A CA    
1497 C C     . SER A 204 ? 1.3163 0.8119 1.1700 -0.0461 0.2651  -0.1457 204 SER A C     
1498 O O     . SER A 204 ? 1.2822 0.7768 1.1142 -0.0521 0.2630  -0.1538 204 SER A O     
1499 C CB    . SER A 204 ? 1.3029 0.7494 1.1657 -0.0473 0.3084  -0.1548 204 SER A CB    
1500 O OG    . SER A 204 ? 1.3615 0.7882 1.2022 -0.0538 0.3236  -0.1680 204 SER A OG    
1501 N N     . ALA A 205 ? 1.2622 0.7760 1.1224 -0.0462 0.2472  -0.1408 205 ALA A N     
1502 C CA    . ALA A 205 ? 1.1845 0.7156 1.0258 -0.0539 0.2255  -0.1461 205 ALA A CA    
1503 C C     . ALA A 205 ? 1.2565 0.7740 1.0671 -0.0697 0.2274  -0.1637 205 ALA A C     
1504 O O     . ALA A 205 ? 1.2509 0.7792 1.0422 -0.0768 0.2143  -0.1687 205 ALA A O     
1505 C CB    . ALA A 205 ? 1.1569 0.7082 1.0120 -0.0511 0.2087  -0.1380 205 ALA A CB    
1506 N N     . GLU A 206 ? 1.2530 0.7478 1.0594 -0.0761 0.2434  -0.1727 206 GLU A N     
1507 C CA    . GLU A 206 ? 1.2306 0.7103 1.0062 -0.0931 0.2479  -0.1904 206 GLU A CA    
1508 C C     . GLU A 206 ? 1.3105 0.7770 1.0679 -0.0971 0.2604  -0.1984 206 GLU A C     
1509 O O     . GLU A 206 ? 1.2931 0.7527 1.0210 -0.1127 0.2607  -0.2124 206 GLU A O     
1510 C CB    . GLU A 206 ? 1.2323 0.6893 1.0085 -0.0997 0.2627  -0.1985 206 GLU A CB    
1511 C CG    . GLU A 206 ? 1.2749 0.7099 1.0729 -0.0897 0.2872  -0.1941 206 GLU A CG    
1512 C CD    . GLU A 206 ? 1.2011 0.6516 1.0351 -0.0733 0.2825  -0.1745 206 GLU A CD    
1513 O OE1   . GLU A 206 ? 1.0882 0.5659 0.9283 -0.0692 0.2609  -0.1654 206 GLU A OE1   
1514 O OE2   . GLU A 206 ? 1.2615 0.6979 1.1184 -0.0647 0.3006  -0.1674 206 GLU A OE2   
1515 N N     . ALA A 207 ? 1.3325 0.7974 1.1064 -0.0842 0.2700  -0.1891 207 ALA A N     
1516 C CA    . ALA A 207 ? 1.2805 0.7357 1.0380 -0.0871 0.2809  -0.1954 207 ALA A CA    
1517 C C     . ALA A 207 ? 1.2629 0.7384 0.9998 -0.0942 0.2613  -0.1970 207 ALA A C     
1518 O O     . ALA A 207 ? 1.2899 0.7578 0.9994 -0.1067 0.2659  -0.2090 207 ALA A O     
1519 C CB    . ALA A 207 ? 1.2871 0.7406 1.0699 -0.0708 0.2932  -0.1824 207 ALA A CB    
1520 N N     . TYR A 208 ? 1.2462 0.7482 0.9962 -0.0869 0.2398  -0.1849 208 TYR A N     
1521 C CA    . TYR A 208 ? 1.2482 0.7696 0.9862 -0.0892 0.2235  -0.1824 208 TYR A CA    
1522 C C     . TYR A 208 ? 1.2616 0.7862 0.9692 -0.1067 0.2148  -0.1941 208 TYR A C     
1523 O O     . TYR A 208 ? 1.2816 0.8086 0.9706 -0.1131 0.2146  -0.1976 208 TYR A O     
1524 C CB    . TYR A 208 ? 1.0739 0.6206 0.8329 -0.0782 0.2038  -0.1679 208 TYR A CB    
1525 C CG    . TYR A 208 ? 1.0710 0.6246 0.8466 -0.0655 0.2054  -0.1561 208 TYR A CG    
1526 C CD1   . TYR A 208 ? 0.9891 0.5479 0.7524 -0.0673 0.2029  -0.1562 208 TYR A CD1   
1527 C CD2   . TYR A 208 ? 1.1175 0.6740 0.9216 -0.0523 0.2091  -0.1440 208 TYR A CD2   
1528 C CE1   . TYR A 208 ? 1.0577 0.6229 0.8363 -0.0563 0.2044  -0.1452 208 TYR A CE1   
1529 C CE2   . TYR A 208 ? 1.1105 0.6747 0.9298 -0.0420 0.2102  -0.1327 208 TYR A CE2   
1530 C CZ    . TYR A 208 ? 1.0860 0.6539 0.8924 -0.0440 0.2079  -0.1337 208 TYR A CZ    
1531 O OH    . TYR A 208 ? 1.0764 0.6522 0.8981 -0.0343 0.2088  -0.1222 208 TYR A OH    
1532 N N     . PRO A 209 ? 1.2361 0.7632 0.9374 -0.1155 0.2069  -0.1991 209 PRO A N     
1533 C CA    . PRO A 209 ? 1.2635 0.7995 0.9376 -0.1324 0.1957  -0.2071 209 PRO A CA    
1534 C C     . PRO A 209 ? 1.3136 0.8313 0.9590 -0.1472 0.2112  -0.2214 209 PRO A C     
1535 O O     . PRO A 209 ? 1.3579 0.8866 0.9805 -0.1594 0.2026  -0.2248 209 PRO A O     
1536 C CB    . PRO A 209 ? 1.2387 0.7770 0.9150 -0.1381 0.1886  -0.2098 209 PRO A CB    
1537 C CG    . PRO A 209 ? 1.1561 0.6963 0.8633 -0.1218 0.1886  -0.1992 209 PRO A CG    
1538 C CD    . PRO A 209 ? 1.1870 0.7127 0.9071 -0.1105 0.2059  -0.1957 209 PRO A CD    
1539 N N     . PRO A 210 ? 1.3513 0.8403 0.9963 -0.1475 0.2350  -0.2303 210 PRO A N     
1540 C CA    . PRO A 210 ? 1.3280 0.7985 0.9476 -0.1590 0.2525  -0.2432 210 PRO A CA    
1541 C C     . PRO A 210 ? 1.3334 0.8120 0.9532 -0.1516 0.2528  -0.2365 210 PRO A C     
1542 O O     . PRO A 210 ? 1.3422 0.8295 0.9375 -0.1636 0.2474  -0.2409 210 PRO A O     
1543 C CB    . PRO A 210 ? 1.2399 0.6790 0.8690 -0.1553 0.2782  -0.2502 210 PRO A CB    
1544 C CG    . PRO A 210 ? 1.2948 0.7355 0.9373 -0.1545 0.2713  -0.2482 210 PRO A CG    
1545 C CD    . PRO A 210 ? 1.3381 0.8096 0.9997 -0.1430 0.2467  -0.2319 210 PRO A CD    
1546 N N     . LEU A 211 ? 1.3111 0.7890 0.9590 -0.1325 0.2585  -0.2247 211 LEU A N     
1547 C CA    . LEU A 211 ? 1.2949 0.7790 0.9447 -0.1251 0.2607  -0.2180 211 LEU A CA    
1548 C C     . LEU A 211 ? 1.2624 0.7732 0.9005 -0.1303 0.2382  -0.2127 211 LEU A C     
1549 O O     . LEU A 211 ? 1.2623 0.7756 0.8808 -0.1379 0.2401  -0.2161 211 LEU A O     
1550 C CB    . LEU A 211 ? 1.2143 0.7016 0.8992 -0.1042 0.2633  -0.2027 211 LEU A CB    
1551 C CG    . LEU A 211 ? 1.2792 0.7426 0.9804 -0.0950 0.2889  -0.2028 211 LEU A CG    
1552 C CD1   . LEU A 211 ? 1.3611 0.8021 1.0600 -0.1016 0.3025  -0.2137 211 LEU A CD1   
1553 C CD2   . LEU A 211 ? 1.2217 0.6985 0.9585 -0.0758 0.2839  -0.1840 211 LEU A CD2   
1554 N N     . LEU A 212 ? 1.2626 0.7938 0.9126 -0.1269 0.2173  -0.2043 212 LEU A N     
1555 C CA    . LEU A 212 ? 1.3035 0.8603 0.9460 -0.1309 0.1961  -0.1978 212 LEU A CA    
1556 C C     . LEU A 212 ? 1.2804 0.8391 0.8897 -0.1519 0.1937  -0.2087 212 LEU A C     
1557 O O     . LEU A 212 ? 1.2903 0.8624 0.8860 -0.1577 0.1868  -0.2059 212 LEU A O     
1558 C CB    . LEU A 212 ? 1.2261 0.8019 0.8885 -0.1235 0.1765  -0.1878 212 LEU A CB    
1559 C CG    . LEU A 212 ? 1.1425 0.7231 0.8371 -0.1049 0.1735  -0.1757 212 LEU A CG    
1560 C CD1   . LEU A 212 ? 1.0945 0.6926 0.7989 -0.1036 0.1551  -0.1704 212 LEU A CD1   
1561 C CD2   . LEU A 212 ? 1.0693 0.6589 0.7760 -0.0938 0.1712  -0.1649 212 LEU A CD2   
1562 N N     . ARG A 213 ? 1.2865 0.8331 0.8824 -0.1644 0.1991  -0.2204 213 ARG A N     
1563 C CA    . ARG A 213 ? 1.3604 0.9080 0.9224 -0.1867 0.1985  -0.2318 213 ARG A CA    
1564 C C     . ARG A 213 ? 1.4673 0.9996 1.0084 -0.1937 0.2167  -0.2408 213 ARG A C     
1565 O O     . ARG A 213 ? 1.4038 0.9479 0.9205 -0.2077 0.2113  -0.2430 213 ARG A O     
1566 C CB    . ARG A 213 ? 1.3450 0.8799 0.8971 -0.1992 0.2027  -0.2434 213 ARG A CB    
1567 C CG    . ARG A 213 ? 1.3727 0.9300 0.9320 -0.2014 0.1807  -0.2362 213 ARG A CG    
1568 C CD    . ARG A 213 ? 1.4533 1.0016 0.9935 -0.2203 0.1834  -0.2491 213 ARG A CD    
1569 N NE    . ARG A 213 ? 1.4222 0.9391 0.9675 -0.2174 0.2051  -0.2594 213 ARG A NE    
1570 C CZ    . ARG A 213 ? 1.4369 0.9473 1.0070 -0.2054 0.2065  -0.2554 213 ARG A CZ    
1571 N NH1   . ARG A 213 ? 1.3830 0.9152 0.9714 -0.1978 0.1874  -0.2438 213 ARG A NH1   
1572 N NH2   . ARG A 213 ? 1.3894 0.8711 0.9668 -0.2008 0.2283  -0.2625 213 ARG A NH2   
1573 N N     . GLY A 214 ? 1.4328 0.9405 0.9847 -0.1835 0.2383  -0.2447 214 GLY A N     
1574 C CA    . GLY A 214 ? 1.4024 0.8939 0.9394 -0.1867 0.2582  -0.2523 214 GLY A CA    
1575 C C     . GLY A 214 ? 1.4123 0.9225 0.9518 -0.1800 0.2499  -0.2408 214 GLY A C     
1576 O O     . GLY A 214 ? 1.4507 0.9509 0.9769 -0.1830 0.2649  -0.2459 214 GLY A O     
1577 N N     . ALA A 215 ? 1.4049 0.9410 0.9624 -0.1706 0.2275  -0.2254 215 ALA A N     
1578 C CA    . ALA A 215 ? 1.3421 0.8988 0.9022 -0.1657 0.2163  -0.2135 215 ALA A CA    
1579 C C     . ALA A 215 ? 1.3306 0.9144 0.8783 -0.1771 0.1936  -0.2082 215 ALA A C     
1580 O O     . ALA A 215 ? 1.2863 0.8911 0.8431 -0.1708 0.1796  -0.1949 215 ALA A O     
1581 C CB    . ALA A 215 ? 1.2840 0.8470 0.8795 -0.1432 0.2114  -0.1983 215 ALA A CB    
1582 N N     . GLY A 216 ? 1.3267 0.9111 0.8555 -0.1936 0.1896  -0.2173 216 GLY A N     
1583 C CA    . GLY A 216 ? 1.3143 0.9271 0.8366 -0.2029 0.1672  -0.2094 216 GLY A CA    
1584 C C     . GLY A 216 ? 1.2979 0.9299 0.8508 -0.1866 0.1486  -0.1932 216 GLY A C     
1585 O O     . GLY A 216 ? 1.3811 1.0370 0.9374 -0.1860 0.1329  -0.1810 216 GLY A O     
1586 N N     . LEU A 217 ? 1.2763 0.8983 0.8523 -0.1733 0.1507  -0.1924 217 LEU A N     
1587 C CA    . LEU A 217 ? 1.2555 0.8937 0.8588 -0.1598 0.1343  -0.1797 217 LEU A CA    
1588 C C     . LEU A 217 ? 1.2880 0.9213 0.8970 -0.1614 0.1323  -0.1845 217 LEU A C     
1589 O O     . LEU A 217 ? 1.3350 0.9464 0.9467 -0.1591 0.1470  -0.1930 217 LEU A O     
1590 C CB    . LEU A 217 ? 1.1905 0.8240 0.8201 -0.1397 0.1385  -0.1713 217 LEU A CB    
1591 C CG    . LEU A 217 ? 1.2387 0.8744 0.8660 -0.1359 0.1427  -0.1661 217 LEU A CG    
1592 C CD1   . LEU A 217 ? 1.1601 0.7864 0.8117 -0.1180 0.1511  -0.1603 217 LEU A CD1   
1593 C CD2   . LEU A 217 ? 1.1771 0.8386 0.8056 -0.1372 0.1242  -0.1544 217 LEU A CD2   
1594 N N     . TRP A 218 ? 1.1976 0.8515 0.8104 -0.1648 0.1146  -0.1782 218 TRP A N     
1595 C CA    . TRP A 218 ? 1.2026 0.8556 0.8260 -0.1635 0.1103  -0.1798 218 TRP A CA    
1596 C C     . TRP A 218 ? 1.1496 0.8040 0.8039 -0.1435 0.1070  -0.1708 218 TRP A C     
1597 O O     . TRP A 218 ? 1.1344 0.8039 0.8028 -0.1338 0.0969  -0.1597 218 TRP A O     
1598 C CB    . TRP A 218 ? 1.1844 0.8606 0.8021 -0.1739 0.0928  -0.1750 218 TRP A CB    
1599 C CG    . TRP A 218 ? 1.3211 1.0020 0.9086 -0.1957 0.0924  -0.1817 218 TRP A CG    
1600 C CD1   . TRP A 218 ? 1.3467 1.0100 0.9090 -0.2086 0.1074  -0.1946 218 TRP A CD1   
1601 C CD2   . TRP A 218 ? 1.3332 1.0392 0.9124 -0.2084 0.0763  -0.1755 218 TRP A CD2   
1602 N NE1   . TRP A 218 ? 1.3657 1.0420 0.9022 -0.2298 0.1010  -0.1976 218 TRP A NE1   
1603 C CE2   . TRP A 218 ? 1.3303 1.0340 0.8775 -0.2300 0.0815  -0.1850 218 TRP A CE2   
1604 C CE3   . TRP A 218 ? 1.2898 1.0203 0.8859 -0.2037 0.0588  -0.1624 218 TRP A CE3   
1605 C CZ2   . TRP A 218 ? 1.3613 1.0887 0.8933 -0.2477 0.0683  -0.1806 218 TRP A CZ2   
1606 C CZ3   . TRP A 218 ? 1.3576 1.1110 0.9406 -0.2199 0.0466  -0.1574 218 TRP A CZ3   
1607 C CH2   . TRP A 218 ? 1.3622 1.1151 0.9136 -0.2418 0.0506  -0.1658 218 TRP A CH2   
1608 N N     . LEU A 219 ? 1.1054 0.7453 0.7705 -0.1381 0.1153  -0.1752 219 LEU A N     
1609 C CA    . LEU A 219 ? 1.1118 0.7568 0.8048 -0.1215 0.1103  -0.1662 219 LEU A CA    
1610 C C     . LEU A 219 ? 1.1506 0.8182 0.8530 -0.1202 0.0917  -0.1584 219 LEU A C     
1611 O O     . LEU A 219 ? 1.1698 0.8460 0.8604 -0.1319 0.0844  -0.1608 219 LEU A O     
1612 C CB    . LEU A 219 ? 1.0580 0.6859 0.7612 -0.1171 0.1218  -0.1708 219 LEU A CB    
1613 C CG    . LEU A 219 ? 1.0293 0.6646 0.7599 -0.1017 0.1164  -0.1612 219 LEU A CG    
1614 C CD1   . LEU A 219 ? 1.0642 0.7004 0.8053 -0.0907 0.1193  -0.1539 219 LEU A CD1   
1615 C CD2   . LEU A 219 ? 0.9873 0.6085 0.7278 -0.0989 0.1268  -0.1643 219 LEU A CD2   
1616 N N     . GLU A 220 ? 1.0518 0.7292 0.7758 -0.1064 0.0846  -0.1486 220 GLU A N     
1617 C CA    . GLU A 220 ? 1.0150 0.7114 0.7515 -0.1028 0.0694  -0.1413 220 GLU A CA    
1618 C C     . GLU A 220 ? 1.0090 0.7046 0.7657 -0.0926 0.0689  -0.1392 220 GLU A C     
1619 O O     . GLU A 220 ? 0.9928 0.6989 0.7552 -0.0935 0.0603  -0.1376 220 GLU A O     
1620 C CB    . GLU A 220 ? 0.9834 0.6939 0.7267 -0.0969 0.0605  -0.1316 220 GLU A CB    
1621 C CG    . GLU A 220 ? 1.0853 0.8124 0.8466 -0.0896 0.0478  -0.1234 220 GLU A CG    
1622 C CD    . GLU A 220 ? 1.1418 0.8847 0.9045 -0.0897 0.0381  -0.1146 220 GLU A CD    
1623 O OE1   . GLU A 220 ? 1.0206 0.7638 0.7697 -0.0959 0.0399  -0.1140 220 GLU A OE1   
1624 O OE2   . GLU A 220 ? 1.2473 1.0026 1.0254 -0.0835 0.0292  -0.1078 220 GLU A OE2   
1625 N N     . GLU A 221 ? 0.9490 0.6332 0.7163 -0.0837 0.0783  -0.1386 221 GLU A N     
1626 C CA    . GLU A 221 ? 0.9671 0.6541 0.7547 -0.0739 0.0767  -0.1343 221 GLU A CA    
1627 C C     . GLU A 221 ? 0.9612 0.6338 0.7570 -0.0677 0.0900  -0.1342 221 GLU A C     
1628 O O     . GLU A 221 ? 0.9985 0.6668 0.7955 -0.0634 0.0955  -0.1314 221 GLU A O     
1629 C CB    . GLU A 221 ? 1.0194 0.7214 0.8201 -0.0658 0.0658  -0.1261 221 GLU A CB    
1630 C CG    . GLU A 221 ? 0.9410 0.6481 0.7609 -0.0569 0.0633  -0.1218 221 GLU A CG    
1631 C CD    . GLU A 221 ? 0.9790 0.6980 0.8095 -0.0504 0.0545  -0.1153 221 GLU A CD    
1632 O OE1   . GLU A 221 ? 1.0781 0.8022 0.9028 -0.0523 0.0496  -0.1134 221 GLU A OE1   
1633 O OE2   . GLU A 221 ? 0.9251 0.6484 0.7698 -0.0440 0.0530  -0.1121 221 GLU A OE2   
1634 N N     . PHE A 222 ? 0.9660 0.6321 0.7686 -0.0672 0.0955  -0.1361 222 PHE A N     
1635 C CA    . PHE A 222 ? 0.9720 0.6277 0.7879 -0.0601 0.1076  -0.1331 222 PHE A CA    
1636 C C     . PHE A 222 ? 0.9922 0.6601 0.8278 -0.0527 0.1008  -0.1257 222 PHE A C     
1637 O O     . PHE A 222 ? 1.0156 0.6907 0.8519 -0.0557 0.0936  -0.1273 222 PHE A O     
1638 C CB    . PHE A 222 ? 0.9246 0.5614 0.7345 -0.0656 0.1220  -0.1402 222 PHE A CB    
1639 C CG    . PHE A 222 ? 0.9603 0.5874 0.7876 -0.0570 0.1352  -0.1345 222 PHE A CG    
1640 C CD1   . PHE A 222 ? 0.9325 0.5652 0.7783 -0.0517 0.1342  -0.1281 222 PHE A CD1   
1641 C CD2   . PHE A 222 ? 0.9858 0.6002 0.8121 -0.0543 0.1487  -0.1343 222 PHE A CD2   
1642 C CE1   . PHE A 222 ? 0.9319 0.5588 0.7957 -0.0439 0.1457  -0.1203 222 PHE A CE1   
1643 C CE2   . PHE A 222 ? 1.0435 0.6510 0.8884 -0.0459 0.1610  -0.1270 222 PHE A CE2   
1644 C CZ    . PHE A 222 ? 1.0285 0.6431 0.8930 -0.0407 0.1591  -0.1193 222 PHE A CZ    
1645 N N     . LEU A 223 ? 0.9619 0.6325 0.8129 -0.0440 0.1037  -0.1175 223 LEU A N     
1646 C CA    . LEU A 223 ? 0.9362 0.6218 0.8039 -0.0382 0.0955  -0.1100 223 LEU A CA    
1647 C C     . LEU A 223 ? 0.9890 0.6726 0.8739 -0.0315 0.1047  -0.1013 223 LEU A C     
1648 O O     . LEU A 223 ? 0.9711 0.6551 0.8612 -0.0270 0.1078  -0.0958 223 LEU A O     
1649 C CB    . LEU A 223 ? 0.9107 0.6092 0.7789 -0.0360 0.0840  -0.1073 223 LEU A CB    
1650 C CG    . LEU A 223 ? 0.9610 0.6754 0.8395 -0.0334 0.0730  -0.1037 223 LEU A CG    
1651 C CD1   . LEU A 223 ? 0.9130 0.6303 0.7928 -0.0364 0.0711  -0.1065 223 LEU A CD1   
1652 C CD2   . LEU A 223 ? 0.8936 0.6158 0.7667 -0.0340 0.0629  -0.1052 223 LEU A CD2   
1653 N N     . ASP A 224 ? 0.9875 0.6704 0.8823 -0.0310 0.1088  -0.0989 224 ASP A N     
1654 C CA    . ASP A 224 ? 0.9515 0.6371 0.8659 -0.0246 0.1161  -0.0879 224 ASP A CA    
1655 C C     . ASP A 224 ? 0.9604 0.6662 0.8852 -0.0215 0.1044  -0.0801 224 ASP A C     
1656 O O     . ASP A 224 ? 1.0070 0.7243 0.9329 -0.0235 0.0950  -0.0809 224 ASP A O     
1657 C CB    . ASP A 224 ? 0.9818 0.6621 0.9044 -0.0255 0.1231  -0.0866 224 ASP A CB    
1658 C CG    . ASP A 224 ? 1.0238 0.7071 0.9691 -0.0187 0.1322  -0.0731 224 ASP A CG    
1659 O OD1   . ASP A 224 ? 1.0095 0.7010 0.9640 -0.0139 0.1318  -0.0643 224 ASP A OD1   
1660 O OD2   . ASP A 224 ? 1.1006 0.7788 1.0555 -0.0185 0.1398  -0.0701 224 ASP A OD2   
1661 N N     . ILE A 225 ? 0.9134 0.6235 0.8443 -0.0175 0.1050  -0.0734 225 ILE A N     
1662 C CA    . ILE A 225 ? 0.9388 0.6672 0.8780 -0.0161 0.0945  -0.0667 225 ILE A CA    
1663 C C     . ILE A 225 ? 1.0149 0.7534 0.9743 -0.0123 0.0989  -0.0527 225 ILE A C     
1664 O O     . ILE A 225 ? 0.9926 0.7468 0.9594 -0.0122 0.0916  -0.0457 225 ILE A O     
1665 C CB    . ILE A 225 ? 0.8884 0.6176 0.8200 -0.0159 0.0894  -0.0688 225 ILE A CB    
1666 C CG1   . ILE A 225 ? 0.8931 0.6140 0.8285 -0.0121 0.0999  -0.0634 225 ILE A CG1   
1667 C CG2   . ILE A 225 ? 0.8760 0.5990 0.7902 -0.0198 0.0841  -0.0801 225 ILE A CG2   
1668 C CD1   . ILE A 225 ? 0.9176 0.6389 0.8461 -0.0119 0.0957  -0.0645 225 ILE A CD1   
1669 N N     . SER A 226 ? 0.9916 0.7222 0.9605 -0.0099 0.1107  -0.0479 226 SER A N     
1670 C CA    . SER A 226 ? 0.9392 0.6791 0.9298 -0.0054 0.1169  -0.0319 226 SER A CA    
1671 C C     . SER A 226 ? 0.9625 0.7263 0.9631 -0.0075 0.1057  -0.0234 226 SER A C     
1672 O O     . SER A 226 ? 0.9397 0.7182 0.9523 -0.0064 0.1035  -0.0116 226 SER A O     
1673 C CB    . SER A 226 ? 0.9477 0.6751 0.9485 -0.0026 0.1314  -0.0283 226 SER A CB    
1674 O OG    . SER A 226 ? 1.0285 0.7326 1.0185 -0.0020 0.1434  -0.0374 226 SER A OG    
1675 N N     . ASP A 227 ? 0.9848 0.7538 0.9798 -0.0116 0.0982  -0.0294 227 ASP A N     
1676 C CA    . ASP A 227 ? 0.9876 0.7793 0.9920 -0.0144 0.0894  -0.0212 227 ASP A CA    
1677 C C     . ASP A 227 ? 0.9671 0.7716 0.9651 -0.0179 0.0780  -0.0233 227 ASP A C     
1678 O O     . ASP A 227 ? 0.9821 0.8062 0.9867 -0.0216 0.0711  -0.0164 227 ASP A O     
1679 C CB    . ASP A 227 ? 1.0140 0.8074 1.0143 -0.0177 0.0857  -0.0271 227 ASP A CB    
1680 C CG    . ASP A 227 ? 1.0684 0.8519 1.0790 -0.0151 0.0970  -0.0224 227 ASP A CG    
1681 O OD1   . ASP A 227 ? 1.0261 0.8113 1.0545 -0.0109 0.1062  -0.0088 227 ASP A OD1   
1682 O OD2   . ASP A 227 ? 1.1186 0.8931 1.1203 -0.0176 0.0970  -0.0320 227 ASP A OD2   
1683 N N     . GLN A 228 ? 0.9698 0.7635 0.9550 -0.0175 0.0763  -0.0324 228 GLN A N     
1684 C CA    . GLN A 228 ? 0.9511 0.7533 0.9307 -0.0205 0.0672  -0.0348 228 GLN A CA    
1685 C C     . GLN A 228 ? 0.9266 0.7317 0.9138 -0.0185 0.0700  -0.0255 228 GLN A C     
1686 O O     . GLN A 228 ? 0.8880 0.7031 0.8739 -0.0221 0.0627  -0.0246 228 GLN A O     
1687 C CB    . GLN A 228 ? 0.9588 0.7486 0.9213 -0.0212 0.0631  -0.0493 228 GLN A CB    
1688 C CG    . GLN A 228 ? 0.9476 0.7377 0.9021 -0.0239 0.0580  -0.0586 228 GLN A CG    
1689 C CD    . GLN A 228 ? 1.0282 0.8088 0.9821 -0.0228 0.0644  -0.0605 228 GLN A CD    
1690 O OE1   . GLN A 228 ? 0.9876 0.7530 0.9318 -0.0222 0.0685  -0.0677 228 GLN A OE1   
1691 N NE2   . GLN A 228 ? 1.0607 0.8509 1.0249 -0.0236 0.0654  -0.0539 228 GLN A NE2   
1692 N N     . THR A 229 ? 0.9630 0.7588 0.9577 -0.0133 0.0809  -0.0191 229 THR A N     
1693 C CA    . THR A 229 ? 0.8708 0.6653 0.8700 -0.0106 0.0847  -0.0125 229 THR A CA    
1694 C C     . THR A 229 ? 0.8855 0.6921 0.9061 -0.0077 0.0913  0.0058  229 THR A C     
1695 O O     . THR A 229 ? 0.8704 0.6933 0.8989 -0.0102 0.0861  0.0155  229 THR A O     
1696 C CB    . THR A 229 ? 0.9339 0.7062 0.9225 -0.0068 0.0934  -0.0211 229 THR A CB    
1697 O OG1   . THR A 229 ? 0.9147 0.6752 0.9017 -0.0055 0.1011  -0.0256 229 THR A OG1   
1698 C CG2   . THR A 229 ? 0.8803 0.6459 0.8505 -0.0097 0.0855  -0.0344 229 THR A CG2   
1699 N N     . LEU A 230 ? 0.9302 0.7298 0.9614 -0.0030 0.1026  0.0113  230 LEU A N     
1700 C CA    . LEU A 230 ? 0.8616 0.6667 0.9145 0.0023  0.1132  0.0290  230 LEU A CA    
1701 C C     . LEU A 230 ? 0.9121 0.7456 0.9825 -0.0011 0.1062  0.0461  230 LEU A C     
1702 O O     . LEU A 230 ? 0.9018 0.7484 0.9855 -0.0002 0.1070  0.0603  230 LEU A O     
1703 C CB    . LEU A 230 ? 0.7997 0.5879 0.8596 0.0079  0.1283  0.0294  230 LEU A CB    
1704 C CG    . LEU A 230 ? 0.8495 0.6097 0.8916 0.0097  0.1370  0.0131  230 LEU A CG    
1705 C CD1   . LEU A 230 ? 0.8040 0.5470 0.8442 0.0106  0.1470  0.0064  230 LEU A CD1   
1706 C CD2   . LEU A 230 ? 0.8680 0.6200 0.9164 0.0152  0.1488  0.0190  230 LEU A CD2   
1707 N N     . GLU A 231 ? 0.9478 0.7928 1.0175 -0.0059 0.0987  0.0454  231 GLU A N     
1708 C CA    . GLU A 231 ? 0.8930 0.7655 0.9816 -0.0091 0.0947  0.0639  231 GLU A CA    
1709 C C     . GLU A 231 ? 0.8909 0.7850 0.9780 -0.0168 0.0828  0.0692  231 GLU A C     
1710 O O     . GLU A 231 ? 0.9190 0.8317 1.0239 -0.0172 0.0837  0.0879  231 GLU A O     
1711 C CB    . GLU A 231 ? 1.0219 0.9011 1.1086 -0.0130 0.0899  0.0610  231 GLU A CB    
1712 C CG    . GLU A 231 ? 1.0150 0.9260 1.1126 -0.0204 0.0806  0.0758  231 GLU A CG    
1713 C CD    . GLU A 231 ? 1.1136 1.0349 1.2236 -0.0205 0.0824  0.0850  231 GLU A CD    
1714 O OE1   . GLU A 231 ? 1.1825 1.0843 1.2881 -0.0162 0.0889  0.0754  231 GLU A OE1   
1715 O OE2   . GLU A 231 ? 1.1794 1.1291 1.3036 -0.0257 0.0773  0.1023  231 GLU A OE2   
1716 N N     . LYS A 232 ? 0.8887 0.7812 0.9553 -0.0235 0.0720  0.0533  232 LYS A N     
1717 C CA    . LYS A 232 ? 0.9207 0.8309 0.9836 -0.0323 0.0614  0.0557  232 LYS A CA    
1718 C C     . LYS A 232 ? 0.9324 0.8409 1.0014 -0.0294 0.0649  0.0630  232 LYS A C     
1719 O O     . LYS A 232 ? 0.9134 0.8430 0.9915 -0.0352 0.0600  0.0761  232 LYS A O     
1720 C CB    . LYS A 232 ? 0.8471 0.7491 0.8872 -0.0381 0.0524  0.0353  232 LYS A CB    
1721 C CG    . LYS A 232 ? 0.9830 0.9067 1.0184 -0.0500 0.0413  0.0355  232 LYS A CG    
1722 C CD    . LYS A 232 ? 0.9952 0.9089 1.0115 -0.0534 0.0360  0.0157  232 LYS A CD    
1723 C CE    . LYS A 232 ? 1.0606 0.9953 1.0720 -0.0656 0.0271  0.0152  232 LYS A CE    
1724 N NZ    . LYS A 232 ? 1.0430 0.9894 1.0531 -0.0743 0.0218  0.0191  232 LYS A NZ    
1725 N N     . THR A 233 ? 0.9096 0.7941 0.9731 -0.0214 0.0733  0.0549  233 THR A N     
1726 C CA    . THR A 233 ? 0.9103 0.7917 0.9794 -0.0178 0.0780  0.0615  233 THR A CA    
1727 C C     . THR A 233 ? 0.9454 0.8434 1.0404 -0.0143 0.0852  0.0851  233 THR A C     
1728 O O     . THR A 233 ? 0.9836 0.8982 1.0880 -0.0176 0.0818  0.0977  233 THR A O     
1729 C CB    . THR A 233 ? 0.9160 0.7692 0.9747 -0.0100 0.0875  0.0492  233 THR A CB    
1730 O OG1   . THR A 233 ? 0.9238 0.7639 0.9602 -0.0132 0.0804  0.0295  233 THR A OG1   
1731 C CG2   . THR A 233 ? 0.9083 0.7591 0.9732 -0.0062 0.0931  0.0568  233 THR A CG2   
1732 N N     . PHE A 234 ? 0.9238 0.8175 1.0322 -0.0075 0.0957  0.0922  234 PHE A N     
1733 C CA    . PHE A 234 ? 0.9933 0.9016 1.1295 -0.0025 0.1045  0.1162  234 PHE A CA    
1734 C C     . PHE A 234 ? 0.9687 0.9118 1.1179 -0.0114 0.0937  0.1337  234 PHE A C     
1735 O O     . PHE A 234 ? 1.0235 0.9855 1.1907 -0.0117 0.0944  0.1530  234 PHE A O     
1736 C CB    . PHE A 234 ? 1.0042 0.8988 1.1527 0.0065  0.1191  0.1196  234 PHE A CB    
1737 C CG    . PHE A 234 ? 0.9667 0.8290 1.1039 0.0140  0.1315  0.1048  234 PHE A CG    
1738 C CD1   . PHE A 234 ? 0.9722 0.8262 1.1058 0.0169  0.1356  0.1033  234 PHE A CD1   
1739 C CD2   . PHE A 234 ? 0.9743 0.8151 1.1026 0.0167  0.1384  0.0917  234 PHE A CD2   
1740 C CE1   . PHE A 234 ? 0.9908 0.8164 1.1120 0.0223  0.1469  0.0894  234 PHE A CE1   
1741 C CE2   . PHE A 234 ? 0.9675 0.7796 1.0829 0.0215  0.1494  0.0774  234 PHE A CE2   
1742 C CZ    . PHE A 234 ? 0.9892 0.7939 1.1008 0.0242  0.1539  0.0763  234 PHE A CZ    
1743 N N     . ARG A 235 ? 0.9249 0.8783 1.0652 -0.0193 0.0835  0.1279  235 ARG A N     
1744 C CA    . ARG A 235 ? 0.9667 0.9539 1.1139 -0.0307 0.0717  0.1417  235 ARG A CA    
1745 C C     . ARG A 235 ? 1.0067 1.0035 1.1473 -0.0383 0.0635  0.1421  235 ARG A C     
1746 O O     . ARG A 235 ? 1.0175 1.0375 1.1761 -0.0410 0.0627  0.1629  235 ARG A O     
1747 C CB    . ARG A 235 ? 0.9884 0.9805 1.1196 -0.0394 0.0617  0.1293  235 ARG A CB    
1748 C CG    . ARG A 235 ? 0.9804 0.9679 1.1197 -0.0338 0.0682  0.1314  235 ARG A CG    
1749 C CD    . ARG A 235 ? 1.0221 1.0354 1.1608 -0.0445 0.0578  0.1364  235 ARG A CD    
1750 N NE    . ARG A 235 ? 1.0325 1.0457 1.1841 -0.0391 0.0643  0.1434  235 ARG A NE    
1751 C CZ    . ARG A 235 ? 1.0197 1.0613 1.1893 -0.0434 0.0619  0.1637  235 ARG A CZ    
1752 N NH1   . ARG A 235 ? 0.9534 1.0279 1.1310 -0.0535 0.0531  0.1804  235 ARG A NH1   
1753 N NH2   . ARG A 235 ? 1.1024 1.1403 1.2824 -0.0381 0.0682  0.1680  235 ARG A NH2   
1754 N N     . LEU A 236 ? 1.0109 0.9892 1.1272 -0.0412 0.0585  0.1199  236 LEU A N     
1755 C CA    . LEU A 236 ? 0.9712 0.9562 1.0794 -0.0493 0.0505  0.1179  236 LEU A CA    
1756 C C     . LEU A 236 ? 0.9982 0.9849 1.1228 -0.0430 0.0578  0.1330  236 LEU A C     
1757 O O     . LEU A 236 ? 1.0948 1.1029 1.2267 -0.0508 0.0518  0.1457  236 LEU A O     
1758 C CB    . LEU A 236 ? 0.8984 0.8593 0.9806 -0.0508 0.0465  0.0922  236 LEU A CB    
1759 C CG    . LEU A 236 ? 0.8993 0.8679 0.9642 -0.0636 0.0347  0.0795  236 LEU A CG    
1760 C CD1   . LEU A 236 ? 0.9560 0.9410 1.0256 -0.0675 0.0323  0.0848  236 LEU A CD1   
1761 C CD2   . LEU A 236 ? 0.8739 0.8158 0.9170 -0.0616 0.0337  0.0552  236 LEU A CD2   
1762 N N     . LEU A 237 ? 1.0436 1.0088 1.1742 -0.0296 0.0713  0.1321  237 LEU A N     
1763 C CA    . LEU A 237 ? 1.0769 1.0426 1.2236 -0.0226 0.0803  0.1462  237 LEU A CA    
1764 C C     . LEU A 237 ? 1.0882 1.0839 1.2645 -0.0228 0.0826  0.1753  237 LEU A C     
1765 O O     . LEU A 237 ? 1.1118 1.1236 1.3006 -0.0248 0.0817  0.1906  237 LEU A O     
1766 C CB    . LEU A 237 ? 1.0848 1.0202 1.2303 -0.0090 0.0958  0.1378  237 LEU A CB    
1767 C CG    . LEU A 237 ? 1.1760 1.0888 1.3009 -0.0078 0.0957  0.1199  237 LEU A CG    
1768 C CD1   . LEU A 237 ? 1.1539 1.0661 1.2557 -0.0183 0.0807  0.1025  237 LEU A CD1   
1769 C CD2   . LEU A 237 ? 1.2013 1.0834 1.3179 0.0025  0.1091  0.1069  237 LEU A CD2   
1770 N N     . SER A 238 ? 1.0526 1.0579 1.2416 -0.0211 0.0853  0.1845  238 SER A N     
1771 C CA    . SER A 238 ? 1.0329 1.0648 1.2541 -0.0186 0.0904  0.2144  238 SER A CA    
1772 C C     . SER A 238 ? 1.0745 1.1447 1.3017 -0.0333 0.0757  0.2305  238 SER A C     
1773 O O     . SER A 238 ? 1.0961 1.1906 1.3486 -0.0329 0.0780  0.2563  238 SER A O     
1774 C CB    . SER A 238 ? 1.0563 1.0874 1.2895 -0.0131 0.0973  0.2197  238 SER A CB    
1775 O OG    . SER A 238 ? 1.0849 1.1436 1.3517 -0.0105 0.1022  0.2507  238 SER A OG    
1776 N N     . GLU A 239 ? 1.1182 1.1949 1.3227 -0.0471 0.0610  0.2160  239 GLU A N     
1777 C CA    . GLU A 239 ? 1.1334 1.2465 1.3403 -0.0637 0.0470  0.2294  239 GLU A CA    
1778 C C     . GLU A 239 ? 1.1352 1.2556 1.3435 -0.0683 0.0437  0.2353  239 GLU A C     
1779 O O     . GLU A 239 ? 1.1653 1.3192 1.3902 -0.0769 0.0381  0.2584  239 GLU A O     
1780 C CB    . GLU A 239 ? 1.1500 1.2641 1.3296 -0.0776 0.0340  0.2094  239 GLU A CB    
1781 C CG    . GLU A 239 ? 1.1635 1.2574 1.3346 -0.0704 0.0387  0.1946  239 GLU A CG    
1782 C CD    . GLU A 239 ? 1.2490 1.3581 1.4063 -0.0836 0.0278  0.1877  239 GLU A CD    
1783 O OE1   . GLU A 239 ? 1.3059 1.4226 1.4441 -0.0981 0.0167  0.1769  239 GLU A OE1   
1784 O OE2   . GLU A 239 ? 1.2692 1.3816 1.4348 -0.0795 0.0312  0.1927  239 GLU A OE2   
1785 N N     . ARG A 240 ? 1.1508 1.2413 1.3424 -0.0629 0.0470  0.2157  240 ARG A N     
1786 C CA    . ARG A 240 ? 1.1768 1.2699 1.3709 -0.0648 0.0461  0.2208  240 ARG A CA    
1787 C C     . ARG A 240 ? 1.1437 1.2486 1.3695 -0.0541 0.0576  0.2476  240 ARG A C     
1788 O O     . ARG A 240 ? 1.1836 1.3159 1.4246 -0.0609 0.0531  0.2680  240 ARG A O     
1789 C CB    . ARG A 240 ? 1.1497 1.2064 1.3213 -0.0589 0.0494  0.1952  240 ARG A CB    
1790 C CG    . ARG A 240 ? 1.1805 1.2306 1.3603 -0.0523 0.0561  0.2018  240 ARG A CG    
1791 C CD    . ARG A 240 ? 1.2527 1.2689 1.4084 -0.0481 0.0578  0.1760  240 ARG A CD    
1792 N NE    . ARG A 240 ? 1.2701 1.2793 1.4018 -0.0577 0.0472  0.1551  240 ARG A NE    
1793 C CZ    . ARG A 240 ? 1.2783 1.2589 1.3899 -0.0530 0.0490  0.1320  240 ARG A CZ    
1794 N NH1   . ARG A 240 ? 1.3097 1.2662 1.4201 -0.0400 0.0601  0.1258  240 ARG A NH1   
1795 N NH2   . ARG A 240 ? 1.2459 1.2228 1.3383 -0.0622 0.0396  0.1152  240 ARG A NH2   
1796 N N     . ILE A 241 ? 1.1156 1.1999 1.3521 -0.0375 0.0733  0.2478  241 ILE A N     
1797 C CA    . ILE A 241 ? 1.1052 1.1984 1.3737 -0.0259 0.0869  0.2730  241 ILE A CA    
1798 C C     . ILE A 241 ? 1.1528 1.2871 1.4491 -0.0318 0.0826  0.3036  241 ILE A C     
1799 O O     . ILE A 241 ? 1.1738 1.3327 1.4942 -0.0320 0.0842  0.3288  241 ILE A O     
1800 C CB    . ILE A 241 ? 1.0954 1.1569 1.3686 -0.0084 0.1057  0.2655  241 ILE A CB    
1801 C CG1   . ILE A 241 ? 1.0655 1.0898 1.3061 -0.0064 0.1060  0.2330  241 ILE A CG1   
1802 C CG2   . ILE A 241 ? 1.0294 1.0906 1.3292 0.0042  0.1219  0.2846  241 ILE A CG2   
1803 C CD1   . ILE A 241 ? 1.0237 1.0160 1.2652 0.0086  0.1243  0.2238  241 ILE A CD1   
1804 N N     . ASN A 242 ? 1.0870 1.2314 1.3810 -0.0372 0.0769  0.3031  242 ASN A N     
1805 C CA    . ASN A 242 ? 1.1365 1.3241 1.4537 -0.0461 0.0698  0.3320  242 ASN A CA    
1806 C C     . ASN A 242 ? 1.2527 1.4707 1.5616 -0.0656 0.0524  0.3380  242 ASN A C     
1807 O O     . ASN A 242 ? 1.3013 1.5555 1.6353 -0.0708 0.0495  0.3676  242 ASN A O     
1808 C CB    . ASN A 242 ? 1.0872 1.2788 1.4005 -0.0490 0.0665  0.3283  242 ASN A CB    
1809 N N     . SER A 243 ? 1.2238 1.4275 1.4983 -0.0770 0.0412  0.3106  243 SER A N     
1810 C CA    . SER A 243 ? 1.2321 1.4605 1.4955 -0.0971 0.0255  0.3128  243 SER A CA    
1811 C C     . SER A 243 ? 1.2842 1.5197 1.5610 -0.0956 0.0278  0.3266  243 SER A C     
1812 O O     . SER A 243 ? 1.3448 1.6122 1.6254 -0.1116 0.0166  0.3411  243 SER A O     
1813 C CB    . SER A 243 ? 1.2604 1.4668 1.4851 -0.1080 0.0159  0.2790  243 SER A CB    
1814 O OG    . SER A 243 ? 1.2461 1.4475 1.4563 -0.1113 0.0125  0.2652  243 SER A OG    
1815 N N     . SER A 244 ? 1.3014 1.5077 1.5832 -0.0781 0.0419  0.3211  244 SER A N     
1816 C CA    . SER A 244 ? 1.3509 1.5637 1.6475 -0.0750 0.0458  0.3355  244 SER A CA    
1817 C C     . SER A 244 ? 1.3753 1.6233 1.7122 -0.0708 0.0515  0.3739  244 SER A C     
1818 O O     . SER A 244 ? 1.3876 1.6665 1.7378 -0.0806 0.0445  0.3944  244 SER A O     
1819 C CB    . SER A 244 ? 1.2963 1.4680 1.5857 -0.0579 0.0601  0.3182  244 SER A CB    
1820 O OG    . SER A 244 ? 1.3014 1.4589 1.6094 -0.0394 0.0776  0.3248  244 SER A OG    
1821 N N     . LYS A 245 ? 1.3142 1.5592 1.6722 -0.0566 0.0643  0.3850  245 LYS A N     
1822 C CA    . LYS A 245 ? 1.2917 1.5674 1.6917 -0.0497 0.0726  0.4227  245 LYS A CA    
1823 C C     . LYS A 245 ? 1.4062 1.7335 1.8179 -0.0693 0.0558  0.4481  245 LYS A C     
1824 O O     . LYS A 245 ? 1.3922 1.7508 1.8331 -0.0701 0.0567  0.4788  245 LYS A O     
1825 C CB    . LYS A 245 ? 1.2271 1.4906 1.6457 -0.0335 0.0880  0.4285  245 LYS A CB    
1826 N N     . GLN A 246 ? 1.3896 1.7273 1.7783 -0.0862 0.0404  0.4360  246 GLN A N     
1827 C CA    . GLN A 246 ? 1.3969 1.7831 1.7902 -0.1084 0.0231  0.4563  246 GLN A CA    
1828 C C     . GLN A 246 ? 1.4534 1.8465 1.8239 -0.1272 0.0090  0.4459  246 GLN A C     
1829 O O     . GLN A 246 ? 1.4697 1.9056 1.8497 -0.1450 -0.0033 0.4682  246 GLN A O     
1830 C CB    . GLN A 246 ? 1.3456 1.7412 1.7244 -0.1190 0.0140  0.4486  246 GLN A CB    
1831 C CG    . GLN A 246 ? 1.4189 1.8126 1.8232 -0.1023 0.0270  0.4625  246 GLN A CG    
1832 C CD    . GLN A 246 ? 1.4604 1.8853 1.9130 -0.0925 0.0365  0.5049  246 GLN A CD    
1833 O OE1   . GLN A 246 ? 1.4286 1.8358 1.9006 -0.0746 0.0524  0.5116  246 GLN A OE1   
1834 N NE2   . GLN A 246 ? 1.4385 1.9103 1.9112 -0.1041 0.0276  0.5343  246 GLN A NE2   
1835 N N     . ARG A 247 ? 1.4213 1.7866 1.7697 -0.1269 0.0088  0.4226  247 ARG A N     
1836 C CA    . ARG A 247 ? 1.4352 1.8109 1.7691 -0.1443 -0.0031 0.4190  247 ARG A CA    
1837 C C     . ARG A 247 ? 1.4673 1.8544 1.8328 -0.1334 0.0060  0.4451  247 ARG A C     
1838 O O     . ARG A 247 ? 1.4905 1.9119 1.8658 -0.1482 -0.0036 0.4650  247 ARG A O     
1839 C CB    . ARG A 247 ? 1.3953 1.7264 1.6929 -0.1437 -0.0035 0.3800  247 ARG A CB    
1840 C CG    . ARG A 247 ? 1.3862 1.7019 1.6522 -0.1530 -0.0109 0.3519  247 ARG A CG    
1841 C CD    . ARG A 247 ? 1.3166 1.5907 1.5504 -0.1522 -0.0109 0.3166  247 ARG A CD    
1842 N NE    . ARG A 247 ? 1.3326 1.5916 1.5381 -0.1599 -0.0166 0.2905  247 ARG A NE    
1843 C CZ    . ARG A 247 ? 1.3787 1.6527 1.5639 -0.1825 -0.0299 0.2816  247 ARG A CZ    
1844 N NH1   . ARG A 247 ? 1.4167 1.6809 1.5824 -0.1949 -0.0361 0.2663  247 ARG A NH1   
1845 N NH2   . ARG A 247 ? 1.3041 1.6025 1.4885 -0.1932 -0.0363 0.2881  247 ARG A NH2   
1846 N N     . LEU A 248 ? 1.5000 1.8589 1.8798 -0.1091 0.0244  0.4442  248 LEU A N     
1847 C CA    . LEU A 248 ? 1.4661 1.8310 1.8761 -0.0960 0.0364  0.4672  248 LEU A CA    
1848 C C     . LEU A 248 ? 1.4788 1.8893 1.9311 -0.0950 0.0386  0.5095  248 LEU A C     
1849 O O     . LEU A 248 ? 1.4838 1.8909 1.9677 -0.0752 0.0563  0.5282  248 LEU A O     
1850 C CB    . LEU A 248 ? 1.4329 1.7525 1.8432 -0.0712 0.0568  0.4514  248 LEU A CB    
1851 C CG    . LEU A 248 ? 1.4752 1.7594 1.8598 -0.0684 0.0586  0.4245  248 LEU A CG    
1852 C CD1   . LEU A 248 ? 1.4224 1.6874 1.7657 -0.0825 0.0447  0.3909  248 LEU A CD1   
1853 C CD2   . LEU A 248 ? 1.4858 1.7315 1.8749 -0.0447 0.0800  0.4145  248 LEU A CD2   
1854 N N     . GLU A 249 ? 1.5103 1.9613 1.9630 -0.1157 0.0221  0.5239  249 GLU A N     
1855 C CA    . GLU A 249 ? 1.3985 1.8996 1.8918 -0.1180 0.0213  0.5674  249 GLU A CA    
1856 C C     . GLU A 249 ? 1.4617 1.9873 1.9645 -0.1281 0.0149  0.5843  249 GLU A C     
1857 O O     . GLU A 249 ? 1.3822 1.9519 1.9217 -0.1301 0.0144  0.6236  249 GLU A O     
1858 C CB    . GLU A 249 ? 1.3240 1.8584 1.8089 -0.1386 0.0048  0.5732  249 GLU A CB    
1859 C CG    . GLU A 249 ? 1.3972 1.9406 1.8446 -0.1666 -0.0158 0.5538  249 GLU A CG    
1860 C CD    . GLU A 249 ? 1.4160 1.9748 1.8426 -0.1847 -0.0292 0.5452  249 GLU A CD    
1861 O OE1   . GLU A 249 ? 1.4079 1.9608 1.8434 -0.1732 -0.0219 0.5469  249 GLU A OE1   
1862 O OE2   . GLU A 249 ? 1.5048 2.0813 1.9061 -0.2106 -0.0461 0.5364  249 GLU A OE2   
1863 N N     . THR A 250 ? 1.4493 1.9479 1.9206 -0.1344 0.0099  0.5561  250 THR A N     
1864 C CA    . THR A 250 ? 1.4232 1.9400 1.9027 -0.1425 0.0052  0.5699  250 THR A CA    
1865 C C     . THR A 250 ? 1.3529 1.9311 1.8529 -0.1640 -0.0099 0.6055  250 THR A C     
1866 O O     . THR A 250 ? 1.3454 1.9510 1.8777 -0.1607 -0.0062 0.6367  250 THR A O     
1870 N N     . GLU A 255 ? 1.4060 1.7787 2.0036 0.0025  0.1324  0.5812  255 GLU A N     
1871 C CA    . GLU A 255 ? 1.4664 1.8363 2.0977 0.0200  0.1528  0.6016  255 GLU A CA    
1872 C C     . GLU A 255 ? 1.5797 1.8958 2.2045 0.0409  0.1768  0.5782  255 GLU A C     
1873 O O     . GLU A 255 ? 1.6169 1.9246 2.2690 0.0562  0.1956  0.5906  255 GLU A O     
1874 C CB    . GLU A 255 ? 1.4458 1.8270 2.0699 0.0118  0.1445  0.6033  255 GLU A CB    
1875 C CG    . GLU A 255 ? 1.3977 1.8223 2.0111 -0.0141 0.1172  0.6129  255 GLU A CG    
1876 C CD    . GLU A 255 ? 1.3869 1.8684 2.0451 -0.0188 0.1139  0.6608  255 GLU A CD    
1877 O OE1   . GLU A 255 ? 1.3292 1.8208 2.0232 -0.0056 0.1276  0.6851  255 GLU A OE1   
1878 O OE2   . GLU A 255 ? 1.3459 1.8625 2.0042 -0.0361 0.0977  0.6748  255 GLU A OE2   
1879 N N     . MET A 256 ? 1.5444 1.8253 2.1346 0.0411  0.1769  0.5459  256 MET A N     
1880 C CA    . MET A 256 ? 1.6075 1.8359 2.1833 0.0574  0.1972  0.5186  256 MET A CA    
1881 C C     . MET A 256 ? 1.7064 1.9194 2.2569 0.0516  0.1889  0.4960  256 MET A C     
1882 O O     . MET A 256 ? 1.7260 1.9430 2.2436 0.0351  0.1674  0.4772  256 MET A O     
1883 C CB    . MET A 256 ? 1.5915 1.7905 2.1348 0.0565  0.1965  0.4907  256 MET A CB    
1884 C CG    . MET A 256 ? 1.6609 1.8086 2.1876 0.0712  0.2167  0.4631  256 MET A CG    
1885 S SD    . MET A 256 ? 1.7828 1.9047 2.2894 0.0752  0.2234  0.4451  256 MET A SD    
1886 C CE    . MET A 256 ? 1.6852 1.7779 2.2180 0.0989  0.2597  0.4512  256 MET A CE    
1887 N N     . VAL A 257 ? 1.7028 1.8990 2.2682 0.0641  0.2052  0.4977  257 VAL A N     
1888 C CA    . VAL A 257 ? 1.7087 1.8966 2.2557 0.0583  0.1970  0.4817  257 VAL A CA    
1889 C C     . VAL A 257 ? 1.7365 1.8783 2.2772 0.0730  0.2178  0.4611  257 VAL A C     
1890 O O     . VAL A 257 ? 1.7396 1.8769 2.2798 0.0729  0.2177  0.4575  257 VAL A O     
1891 C CB    . VAL A 257 ? 1.6643 1.8984 2.2407 0.0511  0.1874  0.5146  257 VAL A CB    
1892 C CG1   . VAL A 257 ? 1.6402 1.8789 2.2640 0.0685  0.2104  0.5442  257 VAL A CG1   
1893 C CG2   . VAL A 257 ? 1.6926 1.9303 2.2409 0.0368  0.1687  0.4971  257 VAL A CG2   
1894 N N     . ASN A 258 ? 1.7070 1.8142 2.2408 0.0845  0.2355  0.4464  258 ASN A N     
1895 C CA    . ASN A 258 ? 1.6845 1.7448 2.2052 0.0958  0.2546  0.4220  258 ASN A CA    
1896 C C     . ASN A 258 ? 1.6496 1.6766 2.1267 0.0922  0.2509  0.3859  258 ASN A C     
1897 O O     . ASN A 258 ? 1.6507 1.6607 2.1272 0.0998  0.2642  0.3818  258 ASN A O     
1898 C CB    . ASN A 258 ? 1.7063 1.7539 2.2647 0.1147  0.2853  0.4406  258 ASN A CB    
1899 C CG    . ASN A 258 ? 1.7085 1.7266 2.2717 0.1238  0.3029  0.4316  258 ASN A CG    
1900 O OD1   . ASN A 258 ? 1.6701 1.7053 2.2480 0.1213  0.2974  0.4446  258 ASN A OD1   
1901 N ND2   . ASN A 258 ? 1.6806 1.6546 2.2313 0.1336  0.3246  0.4099  258 ASN A ND2   
1902 N N     . GLN A 259 ? 1.5997 1.6184 2.0410 0.0805  0.2329  0.3605  259 GLN A N     
1903 C CA    . GLN A 259 ? 1.5900 1.5765 1.9906 0.0773  0.2294  0.3263  259 GLN A CA    
1904 C C     . GLN A 259 ? 1.5876 1.5491 1.9604 0.0740  0.2256  0.2993  259 GLN A C     
1905 O O     . GLN A 259 ? 1.5908 1.5369 1.9282 0.0664  0.2140  0.2732  259 GLN A O     
1906 C CB    . GLN A 259 ? 1.5772 1.5818 1.9581 0.0640  0.2074  0.3214  259 GLN A CB    
1907 C CG    . GLN A 259 ? 1.5980 1.5986 1.9809 0.0683  0.2144  0.3244  259 GLN A CG    
1908 C CD    . GLN A 259 ? 1.6522 1.6856 2.0757 0.0727  0.2204  0.3605  259 GLN A CD    
1909 O OE1   . GLN A 259 ? 1.6666 1.7294 2.1165 0.0709  0.2167  0.3848  259 GLN A OE1   
1910 N NE2   . GLN A 259 ? 1.6040 1.6343 2.0335 0.0781  0.2292  0.3656  259 GLN A NE2   
1911 N N     . PHE A 260 ? 1.4129 1.3712 1.8021 0.0792  0.2349  0.3062  260 PHE A N     
1912 C CA    . PHE A 260 ? 1.3583 1.2913 1.7235 0.0770  0.2338  0.2817  260 PHE A CA    
1913 C C     . PHE A 260 ? 1.3428 1.2871 1.6782 0.0621  0.2079  0.2658  260 PHE A C     
1914 O O     . PHE A 260 ? 1.3635 1.2882 1.6656 0.0572  0.2006  0.2398  260 PHE A O     
1915 C CB    . PHE A 260 ? 1.4057 1.2947 1.7502 0.0841  0.2509  0.2561  260 PHE A CB    
1916 C CG    . PHE A 260 ? 1.3973 1.2612 1.7130 0.0797  0.2474  0.2291  260 PHE A CG    
1917 C CD1   . PHE A 260 ? 1.3462 1.2075 1.6747 0.0820  0.2532  0.2336  260 PHE A CD1   
1918 C CD2   . PHE A 260 ? 1.3541 1.1986 1.6318 0.0731  0.2382  0.2007  260 PHE A CD2   
1919 C CE1   . PHE A 260 ? 1.3115 1.1511 1.6142 0.0775  0.2496  0.2095  260 PHE A CE1   
1920 C CE2   . PHE A 260 ? 1.3074 1.1316 1.5604 0.0689  0.2346  0.1779  260 PHE A CE2   
1921 C CZ    . PHE A 260 ? 1.3042 1.1256 1.5691 0.0709  0.2402  0.1818  260 PHE A CZ    
1922 N N     . ASP A 261 ? 1.3812 1.3606 1.7309 0.0544  0.1939  0.2844  261 ASP A N     
1923 C CA    . ASP A 261 ? 1.2322 1.2234 1.5569 0.0402  0.1716  0.2711  261 ASP A CA    
1924 C C     . ASP A 261 ? 1.1814 1.1392 1.4788 0.0409  0.1736  0.2420  261 ASP A C     
1925 O O     . ASP A 261 ? 1.1775 1.1238 1.4851 0.0471  0.1848  0.2434  261 ASP A O     
1926 C CB    . ASP A 261 ? 1.1275 1.1573 1.4735 0.0332  0.1613  0.2952  261 ASP A CB    
1927 C CG    . ASP A 261 ? 1.1206 1.1746 1.4466 0.0161  0.1374  0.2902  261 ASP A CG    
1928 O OD1   . ASP A 261 ? 1.1316 1.1654 1.4242 0.0108  0.1293  0.2622  261 ASP A OD1   
1929 O OD2   . ASP A 261 ? 1.0538 1.1464 1.3969 0.0077  0.1273  0.3137  261 ASP A OD2   
1930 N N     . PRO A 262 ? 1.1792 1.1201 1.4429 0.0350  0.1642  0.2161  262 PRO A N     
1931 C CA    . PRO A 262 ? 1.1168 1.0273 1.3549 0.0354  0.1660  0.1894  262 PRO A CA    
1932 C C     . PRO A 262 ? 1.1040 1.0244 1.3397 0.0295  0.1568  0.1877  262 PRO A C     
1933 O O     . PRO A 262 ? 1.1205 1.0179 1.3427 0.0313  0.1613  0.1708  262 PRO A O     
1934 C CB    . PRO A 262 ? 1.0578 0.9567 1.2646 0.0291  0.1550  0.1673  262 PRO A CB    
1935 C CG    . PRO A 262 ? 1.1105 1.0382 1.3241 0.0219  0.1426  0.1814  262 PRO A CG    
1936 C CD    . PRO A 262 ? 1.1583 1.1066 1.4077 0.0281  0.1525  0.2112  262 PRO A CD    
1937 N N     . GLY A 263 ? 1.1176 1.0724 1.3653 0.0216  0.1441  0.2048  263 GLY A N     
1938 C CA    . GLY A 263 ? 1.1037 1.0723 1.3536 0.0162  0.1367  0.2077  263 GLY A CA    
1939 C C     . GLY A 263 ? 1.0746 1.0388 1.3502 0.0257  0.1523  0.2219  263 GLY A C     
1940 O O     . GLY A 263 ? 1.1033 1.0770 1.3819 0.0222  0.1478  0.2245  263 GLY A O     
1941 N N     . ASP A 264 ? 1.0677 1.0184 1.3631 0.0376  0.1712  0.2317  264 ASP A N     
1942 C CA    . ASP A 264 ? 1.0469 0.9813 1.3615 0.0477  0.1897  0.2378  264 ASP A CA    
1943 C C     . ASP A 264 ? 1.0606 0.9594 1.3489 0.0482  0.1941  0.2091  264 ASP A C     
1944 O O     . ASP A 264 ? 1.0730 0.9535 1.3732 0.0554  0.2100  0.2100  264 ASP A O     
1945 C CB    . ASP A 264 ? 1.1488 1.0732 1.4894 0.0604  0.2112  0.2527  264 ASP A CB    
1946 C CG    . ASP A 264 ? 1.2679 1.2299 1.6429 0.0615  0.2098  0.2867  264 ASP A CG    
1947 O OD1   . ASP A 264 ? 1.2843 1.2793 1.6562 0.0504  0.1900  0.2953  264 ASP A OD1   
1948 O OD2   . ASP A 264 ? 1.3272 1.2861 1.7333 0.0733  0.2293  0.3056  264 ASP A OD2   
1949 N N     . LEU A 265 ? 1.1141 1.0023 1.3682 0.0408  0.1816  0.1845  265 LEU A N     
1950 C CA    . LEU A 265 ? 1.0970 0.9540 1.3255 0.0403  0.1844  0.1580  265 LEU A CA    
1951 C C     . LEU A 265 ? 1.0792 0.9453 1.2902 0.0307  0.1676  0.1471  265 LEU A C     
1952 O O     . LEU A 265 ? 1.0959 0.9399 1.2900 0.0300  0.1699  0.1286  265 LEU A O     
1953 C CB    . LEU A 265 ? 1.0624 0.8965 1.2651 0.0402  0.1854  0.1372  265 LEU A CB    
1954 C CG    . LEU A 265 ? 1.0852 0.9021 1.3012 0.0502  0.2060  0.1430  265 LEU A CG    
1955 C CD1   . LEU A 265 ? 1.0857 0.8959 1.2831 0.0486  0.2022  0.1322  265 LEU A CD1   
1956 C CD2   . LEU A 265 ? 1.0854 0.8691 1.2965 0.0550  0.2236  0.1298  265 LEU A CD2   
1957 N N     . VAL A 266 ? 1.0439 0.9421 1.2579 0.0227  0.1512  0.1576  266 VAL A N     
1958 C CA    . VAL A 266 ? 1.0858 0.9932 1.2850 0.0139  0.1372  0.1481  266 VAL A CA    
1959 C C     . VAL A 266 ? 1.1571 1.0631 1.3732 0.0176  0.1456  0.1567  266 VAL A C     
1960 O O     . VAL A 266 ? 1.1501 1.0708 1.3966 0.0225  0.1539  0.1811  266 VAL A O     
1961 C CB    . VAL A 266 ? 1.0579 1.0003 1.2570 0.0033  0.1195  0.1581  266 VAL A CB    
1962 C CG1   . VAL A 266 ? 1.0490 0.9877 1.2242 -0.0025 0.1092  0.1424  266 VAL A CG1   
1963 C CG2   . VAL A 266 ? 1.1286 1.1003 1.3598 0.0047  0.1222  0.1889  266 VAL A CG2   
1964 N N     . GLY A 267 ? 1.1567 1.0456 1.3543 0.0153  0.1438  0.1378  267 GLY A N     
1965 C CA    . GLY A 267 ? 1.1427 1.0276 1.3528 0.0177  0.1510  0.1428  267 GLY A CA    
1966 C C     . GLY A 267 ? 1.1359 0.9848 1.3450 0.0253  0.1693  0.1321  267 GLY A C     
1967 O O     . GLY A 267 ? 1.1664 1.0061 1.3790 0.0257  0.1744  0.1297  267 GLY A O     
1968 N N     . VAL A 268 ? 1.1270 0.9549 1.3297 0.0302  0.1792  0.1241  268 VAL A N     
1969 C CA    . VAL A 268 ? 1.0396 0.8324 1.2393 0.0359  0.1979  0.1127  268 VAL A CA    
1970 C C     . VAL A 268 ? 1.0122 0.7862 1.1770 0.0291  0.1899  0.0847  268 VAL A C     
1971 O O     . VAL A 268 ? 1.0468 0.8062 1.1903 0.0278  0.1890  0.0691  268 VAL A O     
1972 C CB    . VAL A 268 ? 1.0240 0.8039 1.2320 0.0435  0.2128  0.1171  268 VAL A CB    
1973 C CG1   . VAL A 268 ? 1.0451 0.7893 1.2530 0.0490  0.2349  0.1071  268 VAL A CG1   
1974 C CG2   . VAL A 268 ? 1.0771 0.8847 1.3194 0.0487  0.2154  0.1471  268 VAL A CG2   
1975 N N     . LYS A 269 ? 1.0538 0.8296 1.2139 0.0245  0.1839  0.0796  269 LYS A N     
1976 C CA    . LYS A 269 ? 1.0393 0.8064 1.1686 0.0170  0.1721  0.0567  269 LYS A CA    
1977 C C     . LYS A 269 ? 1.0386 0.7715 1.1487 0.0171  0.1834  0.0367  269 LYS A C     
1978 O O     . LYS A 269 ? 1.0562 0.7821 1.1400 0.0114  0.1740  0.0185  269 LYS A O     
1979 C CB    . LYS A 269 ? 1.0136 0.7933 1.1443 0.0121  0.1632  0.0577  269 LYS A CB    
1980 N N     . GLU A 270 ? 1.0456 0.7573 1.1683 0.0228  0.2038  0.0400  270 GLU A N     
1981 C CA    . GLU A 270 ? 1.0564 0.7350 1.1596 0.0211  0.2160  0.0204  270 GLU A CA    
1982 C C     . GLU A 270 ? 1.0515 0.7206 1.1396 0.0219  0.2183  0.0119  270 GLU A C     
1983 O O     . GLU A 270 ? 1.0389 0.6848 1.1039 0.0176  0.2234  -0.0068 270 GLU A O     
1984 C CB    . GLU A 270 ? 1.0577 0.7146 1.1794 0.0263  0.2392  0.0258  270 GLU A CB    
1985 C CG    . GLU A 270 ? 1.0798 0.7408 1.2160 0.0253  0.2398  0.0328  270 GLU A CG    
1986 C CD    . GLU A 270 ? 1.1531 0.8403 1.3248 0.0322  0.2402  0.0608  270 GLU A CD    
1987 O OE1   . GLU A 270 ? 1.1435 0.8438 1.3299 0.0380  0.2420  0.0751  270 GLU A OE1   
1988 O OE2   . GLU A 270 ? 1.1926 0.8886 1.3781 0.0313  0.2387  0.0695  270 GLU A OE2   
1989 N N     . PHE A 271 ? 1.0296 0.7168 1.1301 0.0264  0.2145  0.0257  271 PHE A N     
1990 C CA    . PHE A 271 ? 1.0288 0.7094 1.1163 0.0273  0.2157  0.0194  271 PHE A CA    
1991 C C     . PHE A 271 ? 1.0371 0.7250 1.0978 0.0198  0.1962  0.0050  271 PHE A C     
1992 O O     . PHE A 271 ? 0.9753 0.6863 1.0375 0.0169  0.1795  0.0099  271 PHE A O     
1993 C CB    . PHE A 271 ? 0.9334 0.6320 1.0447 0.0343  0.2183  0.0402  271 PHE A CB    
1994 C CG    . PHE A 271 ? 0.9965 0.6879 1.0969 0.0358  0.2214  0.0351  271 PHE A CG    
1995 C CD1   . PHE A 271 ? 1.0592 0.7231 1.1535 0.0388  0.2406  0.0264  271 PHE A CD1   
1996 C CD2   . PHE A 271 ? 0.9701 0.6817 1.0660 0.0337  0.2058  0.0387  271 PHE A CD2   
1997 C CE1   . PHE A 271 ? 1.0331 0.6914 1.1171 0.0399  0.2437  0.0221  271 PHE A CE1   
1998 C CE2   . PHE A 271 ? 0.9205 0.6259 1.0072 0.0350  0.2086  0.0349  271 PHE A CE2   
1999 C CZ    . PHE A 271 ? 0.9473 0.6268 1.0281 0.0383  0.2273  0.0269  271 PHE A CZ    
2000 N N     . GLY A 272 ? 1.0176 0.6861 1.0542 0.0163  0.1990  -0.0123 272 GLY A N     
2001 C CA    . GLY A 272 ? 1.0466 0.7172 1.0576 0.0087  0.1831  -0.0276 272 GLY A CA    
2002 C C     . GLY A 272 ? 1.0381 0.7091 1.0346 0.0078  0.1779  -0.0330 272 GLY A C     
2003 O O     . GLY A 272 ? 1.0500 0.7093 1.0467 0.0112  0.1902  -0.0325 272 GLY A O     
2004 N N     . TYR A 273 ? 1.0010 0.6849 0.9851 0.0032  0.1602  -0.0384 273 TYR A N     
2005 C CA    . TYR A 273 ? 0.9682 0.6534 0.9378 0.0015  0.1530  -0.0441 273 TYR A CA    
2006 C C     . TYR A 273 ? 0.9787 0.6571 0.9244 -0.0057 0.1447  -0.0603 273 TYR A C     
2007 O O     . TYR A 273 ? 0.9991 0.6867 0.9427 -0.0090 0.1337  -0.0630 273 TYR A O     
2008 C CB    . TYR A 273 ? 0.9566 0.6648 0.9361 0.0026  0.1397  -0.0339 273 TYR A CB    
2009 C CG    . TYR A 273 ? 0.9550 0.6646 0.9259 0.0025  0.1352  -0.0355 273 TYR A CG    
2010 C CD1   . TYR A 273 ? 0.9592 0.6538 0.9231 0.0043  0.1464  -0.0389 273 TYR A CD1   
2011 C CD2   . TYR A 273 ? 0.9435 0.6689 0.9131 0.0001  0.1205  -0.0341 273 TYR A CD2   
2012 C CE1   . TYR A 273 ? 0.9751 0.6717 0.9317 0.0041  0.1423  -0.0395 273 TYR A CE1   
2013 C CE2   . TYR A 273 ? 0.9370 0.6629 0.8998 0.0000  0.1168  -0.0351 273 TYR A CE2   
2014 C CZ    . TYR A 273 ? 0.9626 0.6748 0.9194 0.0021  0.1274  -0.0372 273 TYR A CZ    
2015 O OH    . TYR A 273 ? 0.9138 0.6268 0.8643 0.0020  0.1242  -0.0373 273 TYR A OH    
2016 N N     . LEU A 274 ? 0.9379 0.6019 0.8659 -0.0086 0.1497  -0.0702 274 LEU A N     
2017 C CA    . LEU A 274 ? 0.9661 0.6253 0.8720 -0.0163 0.1422  -0.0838 274 LEU A CA    
2018 C C     . LEU A 274 ? 0.9855 0.6509 0.8796 -0.0180 0.1324  -0.0864 274 LEU A C     
2019 O O     . LEU A 274 ? 0.9926 0.6573 0.8893 -0.0145 0.1367  -0.0817 274 LEU A O     
2020 C CB    . LEU A 274 ? 1.0174 0.6548 0.9089 -0.0215 0.1557  -0.0947 274 LEU A CB    
2021 C CG    . LEU A 274 ? 1.0139 0.6363 0.8905 -0.0239 0.1666  -0.1012 274 LEU A CG    
2022 C CD1   . LEU A 274 ? 1.0250 0.6485 0.8772 -0.0326 0.1569  -0.1117 274 LEU A CD1   
2023 C CD2   . LEU A 274 ? 1.0807 0.6809 0.9554 -0.0255 0.1864  -0.1067 274 LEU A CD2   
2024 N N     . LEU A 275 ? 0.9379 0.6098 0.8205 -0.0231 0.1197  -0.0930 275 LEU A N     
2025 C CA    . LEU A 275 ? 0.9282 0.6052 0.7994 -0.0253 0.1105  -0.0957 275 LEU A CA    
2026 C C     . LEU A 275 ? 0.9481 0.6172 0.7989 -0.0336 0.1104  -0.1064 275 LEU A C     
2027 O O     . LEU A 275 ? 0.9864 0.6545 0.8336 -0.0378 0.1084  -0.1114 275 LEU A O     
2028 C CB    . LEU A 275 ? 0.9193 0.6130 0.7976 -0.0240 0.0957  -0.0923 275 LEU A CB    
2029 C CG    . LEU A 275 ? 0.9210 0.6222 0.7954 -0.0239 0.0864  -0.0912 275 LEU A CG    
2030 C CD1   . LEU A 275 ? 0.8433 0.5578 0.7301 -0.0212 0.0770  -0.0865 275 LEU A CD1   
2031 C CD2   . LEU A 275 ? 0.8464 0.5475 0.7052 -0.0296 0.0800  -0.0981 275 LEU A CD2   
2032 N N     . LEU A 276 ? 0.9614 0.6260 0.7986 -0.0368 0.1123  -0.1094 276 LEU A N     
2033 C CA    . LEU A 276 ? 0.9644 0.6213 0.7807 -0.0464 0.1143  -0.1191 276 LEU A CA    
2034 C C     . LEU A 276 ? 0.9607 0.6268 0.7656 -0.0503 0.1042  -0.1191 276 LEU A C     
2035 O O     . LEU A 276 ? 0.9756 0.6454 0.7842 -0.0461 0.1034  -0.1135 276 LEU A O     
2036 C CB    . LEU A 276 ? 1.0119 0.6503 0.8196 -0.0489 0.1317  -0.1241 276 LEU A CB    
2037 C CG    . LEU A 276 ? 1.0332 0.6611 0.8177 -0.0610 0.1366  -0.1358 276 LEU A CG    
2038 C CD1   . LEU A 276 ? 1.0548 0.6623 0.8407 -0.0606 0.1558  -0.1402 276 LEU A CD1   
2039 C CD2   . LEU A 276 ? 0.9774 0.6075 0.7431 -0.0675 0.1345  -0.1384 276 LEU A CD2   
2040 N N     . VAL A 277 ? 0.9004 0.5711 0.6925 -0.0586 0.0968  -0.1242 277 VAL A N     
2041 C CA    . VAL A 277 ? 0.9692 0.6498 0.7508 -0.0632 0.0880  -0.1227 277 VAL A CA    
2042 C C     . VAL A 277 ? 0.9882 0.6639 0.7471 -0.0761 0.0911  -0.1310 277 VAL A C     
2043 O O     . VAL A 277 ? 0.9642 0.6412 0.7177 -0.0826 0.0878  -0.1356 277 VAL A O     
2044 C CB    . VAL A 277 ? 0.9752 0.6725 0.7666 -0.0606 0.0729  -0.1174 277 VAL A CB    
2045 C CG1   . VAL A 277 ? 0.9604 0.6674 0.7478 -0.0616 0.0658  -0.1121 277 VAL A CG1   
2046 C CG2   . VAL A 277 ? 0.9121 0.6126 0.7238 -0.0506 0.0709  -0.1123 277 VAL A CG2   
2047 N N     . ALA A 278 ? 1.0091 0.6802 0.7540 -0.0808 0.0970  -0.1326 278 ALA A N     
2048 C CA    . ALA A 278 ? 1.0209 0.6883 0.7412 -0.0950 0.1002  -0.1406 278 ALA A CA    
2049 C C     . ALA A 278 ? 0.9844 0.6677 0.6964 -0.0997 0.0899  -0.1347 278 ALA A C     
2050 O O     . ALA A 278 ? 0.9815 0.6713 0.7040 -0.0917 0.0865  -0.1264 278 ALA A O     
2051 C CB    . ALA A 278 ? 0.9848 0.6316 0.6930 -0.0985 0.1189  -0.1490 278 ALA A CB    
2052 N N     . GLN A 279 ? 1.0383 0.7293 0.7325 -0.1132 0.0845  -0.1380 279 GLN A N     
2053 C CA    . GLN A 279 ? 1.0801 0.7886 0.7664 -0.1190 0.0745  -0.1308 279 GLN A CA    
2054 C C     . GLN A 279 ? 1.1703 0.8751 0.8279 -0.1351 0.0813  -0.1381 279 GLN A C     
2055 O O     . GLN A 279 ? 1.2014 0.8916 0.8429 -0.1447 0.0916  -0.1502 279 GLN A O     
2056 C CB    . GLN A 279 ? 1.0585 0.7867 0.7521 -0.1209 0.0588  -0.1239 279 GLN A CB    
2057 C CG    . GLN A 279 ? 1.1155 0.8637 0.8097 -0.1227 0.0479  -0.1123 279 GLN A CG    
2058 C CD    . GLN A 279 ? 1.1360 0.9039 0.8385 -0.1248 0.0339  -0.1047 279 GLN A CD    
2059 O OE1   . GLN A 279 ? 1.1908 0.9573 0.8940 -0.1275 0.0326  -0.1096 279 GLN A OE1   
2060 N NE2   . GLN A 279 ? 1.0860 0.8726 0.7964 -0.1233 0.0239  -0.0918 279 GLN A NE2   
2061 N N     . ARG A 280 ? 1.1953 0.9128 0.8466 -0.1383 0.0764  -0.1308 280 ARG A N     
2062 C CA    . ARG A 280 ? 1.2359 0.9570 0.8590 -0.1557 0.0791  -0.1354 280 ARG A CA    
2063 C C     . ARG A 280 ? 1.2477 0.9939 0.8666 -0.1659 0.0627  -0.1273 280 ARG A C     
2064 O O     . ARG A 280 ? 1.2906 1.0550 0.9268 -0.1581 0.0504  -0.1132 280 ARG A O     
2065 C CB    . ARG A 280 ? 1.1933 0.9146 0.8116 -0.1538 0.0843  -0.1313 280 ARG A CB    
2066 C CG    . ARG A 280 ? 1.2743 1.0065 0.8651 -0.1723 0.0829  -0.1326 280 ARG A CG    
2067 C CD    . ARG A 280 ? 1.1975 0.9280 0.7812 -0.1715 0.0902  -0.1302 280 ARG A CD    
2068 N NE    . ARG A 280 ? 1.2202 0.9593 0.7731 -0.1918 0.0912  -0.1341 280 ARG A NE    
2069 C CZ    . ARG A 280 ? 1.2677 1.0018 0.8043 -0.1969 0.1016  -0.1371 280 ARG A CZ    
2070 N NH1   . ARG A 280 ? 1.2581 0.9791 0.8075 -0.1827 0.1117  -0.1360 280 ARG A NH1   
2071 N NH2   . ARG A 280 ? 1.3054 1.0487 0.8119 -0.2175 0.1021  -0.1412 280 ARG A NH2   
2072 N N     . PRO A 281 ? 1.2381 0.9866 0.8363 -0.1829 0.0621  -0.1349 281 PRO A N     
2073 C CA    . PRO A 281 ? 1.2741 1.0490 0.8720 -0.1920 0.0457  -0.1252 281 PRO A CA    
2074 C C     . PRO A 281 ? 1.1729 0.9701 0.7652 -0.1978 0.0373  -0.1125 281 PRO A C     
2075 O O     . PRO A 281 ? 1.2554 1.0467 0.8355 -0.2001 0.0452  -0.1146 281 PRO A O     
2076 C CB    . PRO A 281 ? 1.3310 1.1003 0.9034 -0.2116 0.0497  -0.1382 281 PRO A CB    
2077 C CG    . PRO A 281 ? 1.3100 1.0466 0.8786 -0.2072 0.0681  -0.1545 281 PRO A CG    
2078 C CD    . PRO A 281 ? 1.2749 1.0013 0.8506 -0.1946 0.0770  -0.1525 281 PRO A CD    
2079 N N     . GLY A 282 ? 1.2286 1.0525 0.8322 -0.1993 0.0214  -0.0978 282 GLY A N     
2080 C CA    . GLY A 282 ? 1.2292 1.0768 0.8368 -0.2003 0.0118  -0.0812 282 GLY A CA    
2081 C C     . GLY A 282 ? 1.3566 1.2122 0.9993 -0.1800 0.0038  -0.0666 282 GLY A C     
2082 O O     . GLY A 282 ? 1.3628 1.2143 1.0243 -0.1696 0.0013  -0.0670 282 GLY A O     
2083 N N     . LYS A 283 ? 1.4203 1.2860 1.0704 -0.1751 0.0010  -0.0543 283 LYS A N     
2084 C CA    . LYS A 283 ? 1.3504 1.2309 1.0312 -0.1609 -0.0087 -0.0365 283 LYS A CA    
2085 C C     . LYS A 283 ? 1.3916 1.2944 1.0833 -0.1645 -0.0211 -0.0258 283 LYS A C     
2086 O O     . LYS A 283 ? 1.3927 1.3088 1.1108 -0.1535 -0.0287 -0.0107 283 LYS A O     
2087 C CB    . LYS A 283 ? 1.2631 1.1246 0.9680 -0.1405 -0.0037 -0.0396 283 LYS A CB    
2088 C CG    . LYS A 283 ? 1.2395 1.0954 0.9548 -0.1299 0.0000  -0.0338 283 LYS A CG    
2089 C CD    . LYS A 283 ? 1.2158 1.0920 0.9517 -0.1241 -0.0099 -0.0139 283 LYS A CD    
2090 C CE    . LYS A 283 ? 1.2082 1.0721 0.9576 -0.1111 -0.0045 -0.0118 283 LYS A CE    
2091 N NZ    . LYS A 283 ? 1.0393 0.8776 0.7904 -0.1025 0.0052  -0.0273 283 LYS A NZ    
2092 O OXT   . LYS A 283 ? 1.4669 1.3742 1.1425 -0.1780 -0.0228 -0.0321 283 LYS A OXT   
2093 N N     . LEU B 6   ? 1.6785 1.1388 1.1374 -0.3166 0.2222  -0.3241 6   LEU B N     
2094 C CA    . LEU B 6   ? 1.6606 1.1030 1.1401 -0.3094 0.2302  -0.3254 6   LEU B CA    
2095 C C     . LEU B 6   ? 1.7475 1.1825 1.2042 -0.3350 0.2308  -0.3385 6   LEU B C     
2096 O O     . LEU B 6   ? 1.8821 1.2942 1.3388 -0.3390 0.2502  -0.3467 6   LEU B O     
2097 C CB    . LEU B 6   ? 1.6503 1.0565 1.1427 -0.2966 0.2581  -0.3318 6   LEU B CB    
2098 C CG    . LEU B 6   ? 1.7020 1.0953 1.2302 -0.2770 0.2658  -0.3242 6   LEU B CG    
2099 C CD1   . LEU B 6   ? 1.7428 1.1034 1.2816 -0.2672 0.2947  -0.3294 6   LEU B CD1   
2100 C CD2   . LEU B 6   ? 1.6353 1.0261 1.1645 -0.2877 0.2615  -0.3278 6   LEU B CD2   
2101 N N     . SER B 7   ? 1.7481 1.2146 1.1981 -0.3461 0.2071  -0.3315 7   SER B N     
2102 C CA    . SER B 7   ? 1.7586 1.2264 1.1861 -0.3724 0.2033  -0.3411 7   SER B CA    
2103 C C     . SER B 7   ? 1.8398 1.3112 1.2354 -0.3942 0.2085  -0.3494 7   SER B C     
2104 O O     . SER B 7   ? 1.8556 1.3189 1.2383 -0.4111 0.2169  -0.3577 7   SER B O     
2105 C CB    . SER B 7   ? 1.7297 1.1741 1.1738 -0.3691 0.2179  -0.3453 7   SER B CB    
2106 O OG    . SER B 7   ? 1.7169 1.1628 1.1424 -0.3923 0.2186  -0.3526 7   SER B OG    
2107 N N     . GLU B 8   ? 1.8464 1.3304 1.2283 -0.3949 0.2034  -0.3471 8   GLU B N     
2108 C CA    . GLU B 8   ? 1.8325 1.3226 1.1835 -0.4164 0.2073  -0.3540 8   GLU B CA    
2109 C C     . GLU B 8   ? 1.7875 1.2997 1.1193 -0.4423 0.1928  -0.3542 8   GLU B C     
2110 O O     . GLU B 8   ? 1.6447 1.1551 0.9528 -0.4631 0.2008  -0.3624 8   GLU B O     
2111 C CB    . GLU B 8   ? 1.8094 1.3166 1.1496 -0.4139 0.1988  -0.3486 8   GLU B CB    
2112 C CG    . GLU B 8   ? 1.7918 1.2766 1.1462 -0.3915 0.2159  -0.3496 8   GLU B CG    
2113 C CD    . GLU B 8   ? 1.6897 1.1888 1.0748 -0.3654 0.2026  -0.3331 8   GLU B CD    
2114 O OE1   . GLU B 8   ? 1.6323 1.1679 1.0215 -0.3655 0.1786  -0.3181 8   GLU B OE1   
2115 O OE2   . GLU B 8   ? 1.7186 1.1984 1.1302 -0.3424 0.2153  -0.3305 8   GLU B OE2   
2116 N N     . LEU B 9   ? 1.8154 1.3507 1.1578 -0.4417 0.1705  -0.3441 9   LEU B N     
2117 C CA    . LEU B 9   ? 1.8064 1.3642 1.1420 -0.4602 0.1539  -0.3403 9   LEU B CA    
2118 C C     . LEU B 9   ? 1.8222 1.3596 1.1768 -0.4539 0.1621  -0.3440 9   LEU B C     
2119 O O     . LEU B 9   ? 1.8114 1.3335 1.1920 -0.4312 0.1670  -0.3414 9   LEU B O     
2120 C CB    . LEU B 9   ? 1.7934 1.3868 1.1344 -0.4585 0.1266  -0.3257 9   LEU B CB    
2121 C CG    . LEU B 9   ? 1.8171 1.4484 1.1449 -0.4809 0.1040  -0.3167 9   LEU B CG    
2122 C CD1   . LEU B 9   ? 1.7263 1.3933 1.0866 -0.4585 0.0828  -0.2919 9   LEU B CD1   
2123 C CD2   . LEU B 9   ? 1.8211 1.4510 1.1498 -0.4940 0.1034  -0.3198 9   LEU B CD2   
2124 N N     . PRO B 10  ? 1.8419 1.3787 1.1847 -0.4736 0.1644  -0.3496 10  PRO B N     
2125 C CA    . PRO B 10  ? 1.8678 1.3856 1.2288 -0.4681 0.1721  -0.3526 10  PRO B CA    
2126 C C     . PRO B 10  ? 1.7468 1.2841 1.1283 -0.4593 0.1516  -0.3409 10  PRO B C     
2127 O O     . PRO B 10  ? 1.6774 1.2470 1.0555 -0.4632 0.1295  -0.3305 10  PRO B O     
2128 C CB    . PRO B 10  ? 1.8387 1.3563 1.1771 -0.4952 0.1766  -0.3608 10  PRO B CB    
2129 C CG    . PRO B 10  ? 1.7089 1.2335 1.0184 -0.5111 0.1805  -0.3657 10  PRO B CG    
2130 C CD    . PRO B 10  ? 1.7051 1.2551 1.0167 -0.5020 0.1631  -0.3544 10  PRO B CD    
2131 N N     . MET B 11  ? 1.7139 1.2319 1.1183 -0.4470 0.1595  -0.3418 11  MET B N     
2132 C CA    . MET B 11  ? 1.7056 1.2396 1.1313 -0.4359 0.1422  -0.3309 11  MET B CA    
2133 C C     . MET B 11  ? 1.7089 1.2390 1.1459 -0.4411 0.1411  -0.3309 11  MET B C     
2134 O O     . MET B 11  ? 1.7352 1.2380 1.1756 -0.4416 0.1600  -0.3394 11  MET B O     
2135 C CB    . MET B 11  ? 1.7077 1.2347 1.1654 -0.4027 0.1475  -0.3214 11  MET B CB    
2136 C CG    . MET B 11  ? 1.6473 1.1968 1.1042 -0.3930 0.1373  -0.3114 11  MET B CG    
2137 S SD    . MET B 11  ? 1.5438 1.0857 1.0356 -0.3564 0.1440  -0.3007 11  MET B SD    
2138 C CE    . MET B 11  ? 1.5759 1.0679 1.0716 -0.3531 0.1747  -0.3166 11  MET B CE    
2139 N N     . PRO B 12  ? 1.6597 1.2233 1.1119 -0.4380 0.1189  -0.3156 12  PRO B N     
2140 C CA    . PRO B 12  ? 1.6569 1.2244 1.1123 -0.4506 0.1133  -0.3156 12  PRO B CA    
2141 C C     . PRO B 12  ? 1.5564 1.0945 1.0336 -0.4384 0.1287  -0.3196 12  PRO B C     
2142 O O     . PRO B 12  ? 1.5698 1.1020 1.0435 -0.4534 0.1294  -0.3245 12  PRO B O     
2143 C CB    . PRO B 12  ? 1.5654 1.1788 1.0414 -0.4405 0.0872  -0.2934 12  PRO B CB    
2144 C CG    . PRO B 12  ? 1.5700 1.2045 1.0378 -0.4379 0.0780  -0.2866 12  PRO B CG    
2145 C CD    . PRO B 12  ? 1.5694 1.1740 1.0305 -0.4288 0.0969  -0.2974 12  PRO B CD    
2146 N N     . SER B 13  ? 1.4976 1.0202 0.9987 -0.4118 0.1395  -0.3157 13  SER B N     
2147 C CA    . SER B 13  ? 1.5520 1.0463 1.0746 -0.4003 0.1556  -0.3183 13  SER B CA    
2148 C C     . SER B 13  ? 1.5167 1.0296 1.0606 -0.3975 0.1425  -0.3069 13  SER B C     
2149 O O     . SER B 13  ? 1.4576 0.9523 0.9976 -0.4113 0.1509  -0.3153 13  SER B O     
2150 C CB    . SER B 13  ? 1.5720 1.0311 1.0756 -0.4164 0.1787  -0.3361 13  SER B CB    
2151 O OG    . SER B 13  ? 1.5553 0.9941 1.0769 -0.4130 0.1905  -0.3373 13  SER B OG    
2152 N N     . PRO B 14  ? 1.4451 0.9922 1.0119 -0.3797 0.1234  -0.2882 14  PRO B N     
2153 C CA    . PRO B 14  ? 1.4308 1.0038 1.0090 -0.3838 0.1070  -0.2779 14  PRO B CA    
2154 C C     . PRO B 14  ? 1.4007 0.9611 1.0062 -0.3709 0.1144  -0.2736 14  PRO B C     
2155 O O     . PRO B 14  ? 1.4071 0.9447 1.0291 -0.3538 0.1296  -0.2742 14  PRO B O     
2156 C CB    . PRO B 14  ? 1.3560 0.9689 0.9477 -0.3691 0.0860  -0.2603 14  PRO B CB    
2157 C CG    . PRO B 14  ? 1.3463 0.9489 0.9484 -0.3474 0.0941  -0.2585 14  PRO B CG    
2158 C CD    . PRO B 14  ? 1.3500 0.9143 0.9323 -0.3564 0.1162  -0.2761 14  PRO B CD    
2159 N N     . ALA B 15  ? 1.3595 0.9376 0.9701 -0.3799 0.1028  -0.2678 15  ALA B N     
2160 C CA    . ALA B 15  ? 1.3567 0.9274 0.9907 -0.3726 0.1073  -0.2631 15  ALA B CA    
2161 C C     . ALA B 15  ? 1.3026 0.9108 0.9616 -0.3565 0.0881  -0.2440 15  ALA B C     
2162 O O     . ALA B 15  ? 1.3072 0.9460 0.9602 -0.3664 0.0704  -0.2375 15  ALA B O     
2163 C CB    . ALA B 15  ? 1.3542 0.9121 0.9721 -0.3991 0.1113  -0.2737 15  ALA B CB    
2164 N N     . SER B 16  ? 1.2830 0.8889 0.9705 -0.3328 0.0925  -0.2349 16  SER B N     
2165 C CA    . SER B 16  ? 1.2747 0.9143 0.9853 -0.3149 0.0764  -0.2178 16  SER B CA    
2166 C C     . SER B 16  ? 1.2149 0.8793 0.9289 -0.3257 0.0623  -0.2109 16  SER B C     
2167 O O     . SER B 16  ? 1.2326 0.9302 0.9506 -0.3227 0.0453  -0.2004 16  SER B O     
2168 C CB    . SER B 16  ? 1.1575 0.7885 0.8960 -0.2917 0.0850  -0.2104 16  SER B CB    
2169 O OG    . SER B 16  ? 1.1753 0.7762 0.9173 -0.2970 0.1017  -0.2173 16  SER B OG    
2170 N N     . GLU B 17  ? 1.2276 0.8763 0.9401 -0.3391 0.0694  -0.2165 17  GLU B N     
2171 C CA    . GLU B 17  ? 1.2915 0.9648 1.0070 -0.3504 0.0558  -0.2094 17  GLU B CA    
2172 C C     . GLU B 17  ? 1.2348 0.9272 0.9257 -0.3724 0.0430  -0.2120 17  GLU B C     
2173 O O     . GLU B 17  ? 1.1732 0.8986 0.8704 -0.3757 0.0266  -0.2007 17  GLU B O     
2174 C CB    . GLU B 17  ? 1.2676 0.9188 0.9878 -0.3602 0.0669  -0.2145 17  GLU B CB    
2175 C CG    . GLU B 17  ? 1.3106 0.9468 1.0580 -0.3389 0.0787  -0.2089 17  GLU B CG    
2176 C CD    . GLU B 17  ? 1.3598 1.0274 1.1345 -0.3213 0.0661  -0.1913 17  GLU B CD    
2177 O OE1   . GLU B 17  ? 1.3109 1.0070 1.0858 -0.3291 0.0509  -0.1844 17  GLU B OE1   
2178 O OE2   . GLU B 17  ? 1.2745 0.9386 1.0706 -0.3004 0.0721  -0.1843 17  GLU B OE2   
2179 N N     . GLU B 18  ? 1.2834 0.9580 0.9471 -0.3875 0.0499  -0.2255 18  GLU B N     
2180 C CA    . GLU B 18  ? 1.3113 1.0090 0.9524 -0.4074 0.0362  -0.2254 18  GLU B CA    
2181 C C     . GLU B 18  ? 1.2994 1.0299 0.9505 -0.3913 0.0215  -0.2113 18  GLU B C     
2182 O O     . GLU B 18  ? 1.3198 1.0836 0.9674 -0.4006 0.0048  -0.2017 18  GLU B O     
2183 C CB    . GLU B 18  ? 1.3221 0.9929 0.9301 -0.4281 0.0479  -0.2437 18  GLU B CB    
2184 C CG    . GLU B 18  ? 1.4146 1.0500 1.0097 -0.4468 0.0644  -0.2598 18  GLU B CG    
2185 C CD    . GLU B 18  ? 1.5869 1.2033 1.1445 -0.4731 0.0726  -0.2777 18  GLU B CD    
2186 O OE1   . GLU B 18  ? 1.5042 1.1357 1.0475 -0.4747 0.0654  -0.2765 18  GLU B OE1   
2187 O OE2   . GLU B 18  ? 1.6721 1.2588 1.2142 -0.4927 0.0865  -0.2930 18  GLU B OE2   
2188 N N     . VAL B 19  ? 1.2549 0.9762 0.9191 -0.3677 0.0279  -0.2094 19  VAL B N     
2189 C CA    . VAL B 19  ? 1.2483 0.9973 0.9257 -0.3496 0.0159  -0.1962 19  VAL B CA    
2190 C C     . VAL B 19  ? 1.2341 1.0162 0.9342 -0.3415 0.0014  -0.1801 19  VAL B C     
2191 O O     . VAL B 19  ? 1.1974 1.0113 0.9007 -0.3407 -0.0131 -0.1687 19  VAL B O     
2192 C CB    . VAL B 19  ? 1.1425 0.8734 0.8329 -0.3258 0.0268  -0.1972 19  VAL B CB    
2193 C CG1   . VAL B 19  ? 1.0844 0.8412 0.7864 -0.3090 0.0154  -0.1850 19  VAL B CG1   
2194 C CG2   . VAL B 19  ? 1.1971 0.8939 0.8668 -0.3334 0.0430  -0.2129 19  VAL B CG2   
2195 N N     . GLY B 20  ? 1.2030 0.9784 0.9202 -0.3352 0.0059  -0.1783 20  GLY B N     
2196 C CA    . GLY B 20  ? 1.1224 0.9281 0.8602 -0.3290 -0.0064 -0.1640 20  GLY B CA    
2197 C C     . GLY B 20  ? 1.2247 1.0549 0.9516 -0.3508 -0.0194 -0.1596 20  GLY B C     
2198 O O     . GLY B 20  ? 1.1916 1.0559 0.9310 -0.3459 -0.0332 -0.1453 20  GLY B O     
2199 N N     . ALA B 21  ? 1.2149 1.0284 0.9187 -0.3756 -0.0146 -0.1714 21  ALA B N     
2200 C CA    . ALA B 21  ? 1.1974 1.0355 0.8880 -0.3992 -0.0275 -0.1672 21  ALA B CA    
2201 C C     . ALA B 21  ? 1.2263 1.0931 0.9118 -0.3990 -0.0403 -0.1579 21  ALA B C     
2202 O O     . ALA B 21  ? 1.2348 1.1379 0.9287 -0.4029 -0.0553 -0.1432 21  ALA B O     
2203 C CB    . ALA B 21  ? 1.4001 1.2118 1.0618 -0.4275 -0.0186 -0.1842 21  ALA B CB    
2204 N N     . LEU B 22  ? 1.2423 1.0943 0.9167 -0.3930 -0.0340 -0.1647 22  LEU B N     
2205 C CA    . LEU B 22  ? 1.2492 1.1262 0.9178 -0.3935 -0.0449 -0.1561 22  LEU B CA    
2206 C C     . LEU B 22  ? 1.2504 1.1591 0.9487 -0.3705 -0.0559 -0.1371 22  LEU B C     
2207 O O     . LEU B 22  ? 1.3228 1.2663 1.0253 -0.3760 -0.0701 -0.1229 22  LEU B O     
2208 C CB    . LEU B 22  ? 1.2091 1.0605 0.8611 -0.3902 -0.0340 -0.1681 22  LEU B CB    
2209 C CG    . LEU B 22  ? 1.2294 1.0978 0.8645 -0.3993 -0.0419 -0.1647 22  LEU B CG    
2210 C CD1   . LEU B 22  ? 1.2511 1.0860 0.8638 -0.4028 -0.0273 -0.1816 22  LEU B CD1   
2211 C CD2   . LEU B 22  ? 1.3106 1.2097 0.9688 -0.3783 -0.0533 -0.1463 22  LEU B CD2   
2212 N N     . TYR B 23  ? 1.1717 1.0691 0.8910 -0.3450 -0.0489 -0.1362 23  TYR B N     
2213 C CA    . TYR B 23  ? 1.1693 1.0933 0.9153 -0.3233 -0.0571 -0.1202 23  TYR B CA    
2214 C C     . TYR B 23  ? 1.2109 1.1628 0.9734 -0.3258 -0.0670 -0.1076 23  TYR B C     
2215 O O     . TYR B 23  ? 1.2954 1.2791 1.0735 -0.3186 -0.0777 -0.0921 23  TYR B O     
2216 C CB    . TYR B 23  ? 1.0772 0.9827 0.8396 -0.2981 -0.0472 -0.1231 23  TYR B CB    
2217 C CG    . TYR B 23  ? 1.0502 0.9383 0.8035 -0.2901 -0.0405 -0.1297 23  TYR B CG    
2218 C CD1   . TYR B 23  ? 1.0662 0.9725 0.8263 -0.2791 -0.0474 -0.1204 23  TYR B CD1   
2219 C CD2   . TYR B 23  ? 1.0654 0.9186 0.8042 -0.2934 -0.0267 -0.1448 23  TYR B CD2   
2220 C CE1   . TYR B 23  ? 1.1424 1.0329 0.8940 -0.2724 -0.0413 -0.1262 23  TYR B CE1   
2221 C CE2   . TYR B 23  ? 1.0463 0.8841 0.7771 -0.2864 -0.0202 -0.1505 23  TYR B CE2   
2222 C CZ    . TYR B 23  ? 1.1302 0.9867 0.8667 -0.2763 -0.0279 -0.1414 23  TYR B CZ    
2223 O OH    . TYR B 23  ? 1.2228 1.0630 0.9509 -0.2700 -0.0209 -0.1473 23  TYR B OH    
2224 N N     . ASP B 24  ? 1.1990 1.1392 0.9599 -0.3354 -0.0627 -0.1135 24  ASP B N     
2225 C CA    . ASP B 24  ? 1.2128 1.1794 0.9853 -0.3430 -0.0723 -0.1024 24  ASP B CA    
2226 C C     . ASP B 24  ? 1.3354 1.3340 1.0994 -0.3608 -0.0864 -0.0919 24  ASP B C     
2227 O O     . ASP B 24  ? 1.3368 1.3698 1.1198 -0.3556 -0.0972 -0.0748 24  ASP B O     
2228 C CB    . ASP B 24  ? 1.1936 1.1380 0.9581 -0.3570 -0.0647 -0.1131 24  ASP B CB    
2229 C CG    . ASP B 24  ? 1.1536 1.0788 0.9363 -0.3373 -0.0540 -0.1161 24  ASP B CG    
2230 O OD1   . ASP B 24  ? 1.1364 1.0778 0.9414 -0.3164 -0.0569 -0.1058 24  ASP B OD1   
2231 O OD2   . ASP B 24  ? 1.1632 1.0585 0.9390 -0.3430 -0.0425 -0.1278 24  ASP B OD2   
2232 N N     . ARG B 25  ? 1.3554 1.3438 1.0912 -0.3817 -0.0858 -0.1013 25  ARG B N     
2233 C CA    . ARG B 25  ? 1.4896 1.5093 1.2151 -0.4003 -0.0994 -0.0909 25  ARG B CA    
2234 C C     . ARG B 25  ? 1.3993 1.4448 1.1409 -0.3830 -0.1070 -0.0754 25  ARG B C     
2235 O O     . ARG B 25  ? 1.4078 1.4909 1.1647 -0.3837 -0.1194 -0.0567 25  ARG B O     
2236 C CB    . ARG B 25  ? 1.5286 1.5293 1.2178 -0.4267 -0.0956 -0.1063 25  ARG B CB    
2237 N N     . PHE B 26  ? 1.3875 1.4131 1.1280 -0.3665 -0.0989 -0.0821 26  PHE B N     
2238 C CA    . PHE B 26  ? 1.4660 1.5116 1.2135 -0.3566 -0.1053 -0.0702 26  PHE B CA    
2239 C C     . PHE B 26  ? 1.3963 1.4428 1.1720 -0.3254 -0.1019 -0.0633 26  PHE B C     
2240 O O     . PHE B 26  ? 1.4284 1.4839 1.2104 -0.3142 -0.1041 -0.0561 26  PHE B O     
2241 C CB    . PHE B 26  ? 1.4853 1.5127 1.2043 -0.3683 -0.1009 -0.0820 26  PHE B CB    
2242 C CG    . PHE B 26  ? 1.5755 1.6110 1.2657 -0.4016 -0.1069 -0.0856 26  PHE B CG    
2243 C CD1   . PHE B 26  ? 1.5484 1.6200 1.2436 -0.4173 -0.1207 -0.0706 26  PHE B CD1   
2244 C CD2   . PHE B 26  ? 1.5714 1.5790 1.2294 -0.4182 -0.0983 -0.1039 26  PHE B CD2   
2245 C CE1   . PHE B 26  ? 1.5064 1.5869 1.1738 -0.4500 -0.1268 -0.0738 26  PHE B CE1   
2246 C CE2   . PHE B 26  ? 1.6222 1.6368 1.2515 -0.4508 -0.1031 -0.1086 26  PHE B CE2   
2247 C CZ    . PHE B 26  ? 1.5354 1.5863 1.1690 -0.4671 -0.1176 -0.0938 26  PHE B CZ    
2248 N N     . THR B 27  ? 1.3219 1.3604 1.1147 -0.3118 -0.0966 -0.0650 27  THR B N     
2249 C CA    . THR B 27  ? 1.4001 1.4514 1.2220 -0.2861 -0.0967 -0.0541 27  THR B CA    
2250 C C     . THR B 27  ? 1.4209 1.5083 1.2630 -0.2872 -0.1068 -0.0364 27  THR B C     
2251 O O     . THR B 27  ? 1.3688 1.4619 1.2323 -0.2726 -0.1047 -0.0317 27  THR B O     
2252 C CB    . THR B 27  ? 1.2626 1.2876 1.0927 -0.2698 -0.0852 -0.0647 27  THR B CB    
2253 O OG1   . THR B 27  ? 1.2023 1.2220 1.0303 -0.2805 -0.0837 -0.0690 27  THR B OG1   
2254 C CG2   . THR B 27  ? 1.1879 1.1788 1.0019 -0.2661 -0.0746 -0.0800 27  THR B CG2   
2255 N N     . ALA B 28  ? 1.4435 1.5572 1.2795 -0.3048 -0.1178 -0.0255 28  ALA B N     
2256 C CA    . ALA B 28  ? 1.4775 1.6280 1.3330 -0.3078 -0.1278 -0.0070 28  ALA B CA    
2257 C C     . ALA B 28  ? 1.5592 1.7398 1.4116 -0.3200 -0.1393 0.0081  28  ALA B C     
2258 O O     . ALA B 28  ? 1.6293 1.8149 1.4590 -0.3456 -0.1454 0.0058  28  ALA B O     
2259 C CB    . ALA B 28  ? 1.3961 1.5454 1.2439 -0.3255 -0.1293 -0.0116 28  ALA B CB    
2260 N N     . LEU B 29  ? 1.5530 1.7543 1.4290 -0.3023 -0.1418 0.0239  29  LEU B N     
2261 C CA    . LEU B 29  ? 1.5912 1.8099 1.4647 -0.3059 -0.1484 0.0351  29  LEU B CA    
2262 C C     . LEU B 29  ? 1.5290 1.7152 1.3796 -0.3047 -0.1408 0.0181  29  LEU B C     
2263 O O     . LEU B 29  ? 1.5476 1.7439 1.3901 -0.3108 -0.1456 0.0242  29  LEU B O     
2264 C CB    . LEU B 29  ? 1.6115 1.8625 1.4741 -0.3333 -0.1620 0.0481  29  LEU B CB    
2265 N N     . GLY B 30  ? 1.5246 1.6732 1.3656 -0.2971 -0.1291 -0.0022 30  GLY B N     
2266 C CA    . GLY B 30  ? 1.5037 1.6234 1.3325 -0.2882 -0.1205 -0.0153 30  GLY B CA    
2267 C C     . GLY B 30  ? 1.5477 1.6661 1.4017 -0.2601 -0.1155 -0.0097 30  GLY B C     
2268 O O     . GLY B 30  ? 1.5058 1.6145 1.3565 -0.2521 -0.1125 -0.0116 30  GLY B O     
2269 N N     . ALA B 31  ? 1.5437 1.6724 1.4228 -0.2458 -0.1145 -0.0026 31  ALA B N     
2270 C CA    . ALA B 31  ? 1.4855 1.6167 1.3898 -0.2207 -0.1099 0.0041  31  ALA B CA    
2271 C C     . ALA B 31  ? 1.4788 1.6406 1.4000 -0.2170 -0.1174 0.0246  31  ALA B C     
2272 O O     . ALA B 31  ? 1.4304 1.5888 1.3657 -0.1991 -0.1129 0.0280  31  ALA B O     
2273 C CB    . ALA B 31  ? 1.4292 1.5637 1.3541 -0.2082 -0.1059 0.0055  31  ALA B CB    
2274 N N     . ALA B 32  ? 1.4949 1.6873 1.4161 -0.2338 -0.1285 0.0394  32  ALA B N     
2275 C CA    . ALA B 32  ? 1.5025 1.7287 1.4449 -0.2297 -0.1358 0.0628  32  ALA B CA    
2276 C C     . ALA B 32  ? 1.4699 1.6959 1.3992 -0.2352 -0.1388 0.0652  32  ALA B C     
2277 O O     . ALA B 32  ? 1.3822 1.6355 1.3302 -0.2308 -0.1444 0.0857  32  ALA B O     
2278 C CB    . ALA B 32  ? 1.4203 1.6836 1.3699 -0.2461 -0.1474 0.0805  32  ALA B CB    
2279 N N     . SER B 33  ? 1.4720 1.6688 1.3711 -0.2444 -0.1348 0.0458  33  SER B N     
2280 C CA    . SER B 33  ? 1.4483 1.6417 1.3306 -0.2513 -0.1367 0.0453  33  SER B CA    
2281 C C     . SER B 33  ? 1.4532 1.6183 1.3380 -0.2312 -0.1262 0.0350  33  SER B C     
2282 O O     . SER B 33  ? 1.4195 1.5944 1.3178 -0.2208 -0.1272 0.0466  33  SER B O     
2283 C CB    . SER B 33  ? 1.4825 1.6631 1.3275 -0.2775 -0.1385 0.0304  33  SER B CB    
2284 O OG    . SER B 33  ? 1.5434 1.6933 1.3776 -0.2769 -0.1296 0.0103  33  SER B OG    
2285 N N     . LEU B 34  ? 1.4588 1.5894 1.3314 -0.2262 -0.1163 0.0140  34  LEU B N     
2286 C CA    . LEU B 34  ? 1.4313 1.5359 1.3080 -0.2070 -0.1063 0.0044  34  LEU B CA    
2287 C C     . LEU B 34  ? 1.4257 1.5302 1.3309 -0.1847 -0.1008 0.0078  34  LEU B C     
2288 O O     . LEU B 34  ? 1.4178 1.5218 1.3398 -0.1678 -0.0973 0.0133  34  LEU B O     
2289 C CB    . LEU B 34  ? 1.4206 1.4899 1.2715 -0.2128 -0.0979 -0.0182 34  LEU B CB    
2290 C CG    . LEU B 34  ? 1.3989 1.4432 1.2584 -0.1918 -0.0875 -0.0276 34  LEU B CG    
2291 C CD1   . LEU B 34  ? 1.3293 1.3728 1.1916 -0.1833 -0.0869 -0.0226 34  LEU B CD1   
2292 C CD2   . LEU B 34  ? 1.3617 1.3748 1.1996 -0.1979 -0.0794 -0.0472 34  LEU B CD2   
2293 N N     . GLY B 35  ? 1.4344 1.5394 1.3447 -0.1852 -0.0996 0.0044  35  GLY B N     
2294 C CA    . GLY B 35  ? 1.3379 1.4417 1.2718 -0.1662 -0.0936 0.0054  35  GLY B CA    
2295 C C     . GLY B 35  ? 1.1992 1.2762 1.1233 -0.1639 -0.0856 -0.0125 35  GLY B C     
2296 O O     . GLY B 35  ? 1.2247 1.2925 1.1303 -0.1787 -0.0864 -0.0215 35  GLY B O     
2297 N N     . GLU B 36  ? 1.1505 1.2156 1.0884 -0.1452 -0.0774 -0.0169 36  GLU B N     
2298 C CA    . GLU B 36  ? 1.0842 1.1308 1.0200 -0.1404 -0.0703 -0.0296 36  GLU B CA    
2299 C C     . GLU B 36  ? 1.0176 1.0334 0.9336 -0.1416 -0.0638 -0.0456 36  GLU B C     
2300 O O     . GLU B 36  ? 1.0090 1.0098 0.9153 -0.1466 -0.0600 -0.0557 36  GLU B O     
2301 C CB    . GLU B 36  ? 1.1323 1.1835 1.0917 -0.1215 -0.0646 -0.0262 36  GLU B CB    
2302 C CG    . GLU B 36  ? 1.1854 1.2663 1.1681 -0.1176 -0.0684 -0.0101 36  GLU B CG    
2303 C CD    . GLU B 36  ? 1.2774 1.3731 1.2594 -0.1298 -0.0737 -0.0064 36  GLU B CD    
2304 O OE1   . GLU B 36  ? 1.3001 1.3807 1.2680 -0.1370 -0.0718 -0.0179 36  GLU B OE1   
2305 O OE2   . GLU B 36  ? 1.2755 1.3987 1.2725 -0.1321 -0.0796 0.0091  36  GLU B OE2   
2306 N N     . ASN B 37  ? 0.9758 0.9819 0.8870 -0.1368 -0.0619 -0.0473 37  ASN B N     
2307 C CA    . ASN B 37  ? 0.9543 0.9324 0.8485 -0.1372 -0.0553 -0.0610 37  ASN B CA    
2308 C C     . ASN B 37  ? 1.0479 1.0207 0.9186 -0.1557 -0.0583 -0.0651 37  ASN B C     
2309 O O     . ASN B 37  ? 1.1025 1.0846 0.9679 -0.1610 -0.0631 -0.0590 37  ASN B O     
2310 C CB    . ASN B 37  ? 0.9572 0.9274 0.8570 -0.1239 -0.0516 -0.0609 37  ASN B CB    
2311 C CG    . ASN B 37  ? 0.9447 0.9038 0.8562 -0.1085 -0.0441 -0.0663 37  ASN B CG    
2312 O OD1   . ASN B 37  ? 1.0138 0.9649 0.9246 -0.1082 -0.0403 -0.0730 37  ASN B OD1   
2313 N ND2   . ASN B 37  ? 0.9581 0.9165 0.8800 -0.0965 -0.0418 -0.0635 37  ASN B ND2   
2314 N N     . LEU B 38  ? 1.0590 1.0162 0.9154 -0.1659 -0.0546 -0.0757 38  LEU B N     
2315 C CA    . LEU B 38  ? 1.0148 0.9628 0.8467 -0.1846 -0.0550 -0.0824 38  LEU B CA    
2316 C C     . LEU B 38  ? 1.0450 0.9664 0.8634 -0.1817 -0.0464 -0.0934 38  LEU B C     
2317 O O     . LEU B 38  ? 1.0233 0.9219 0.8284 -0.1876 -0.0387 -0.1052 38  LEU B O     
2318 C CB    . LEU B 38  ? 0.9567 0.8995 0.7799 -0.1982 -0.0540 -0.0885 38  LEU B CB    
2319 C CG    . LEU B 38  ? 0.9653 0.9329 0.8034 -0.2003 -0.0614 -0.0782 38  LEU B CG    
2320 C CD1   . LEU B 38  ? 1.0325 0.9943 0.8583 -0.2176 -0.0610 -0.0845 38  LEU B CD1   
2321 C CD2   . LEU B 38  ? 1.0239 1.0226 0.8704 -0.2029 -0.0722 -0.0625 38  LEU B CD2   
2322 N N     . HIS B 39  ? 1.0196 0.9444 0.8431 -0.1719 -0.0474 -0.0886 39  HIS B N     
2323 C CA    . HIS B 39  ? 1.0405 0.9439 0.8523 -0.1690 -0.0403 -0.0968 39  HIS B CA    
2324 C C     . HIS B 39  ? 1.0546 0.9709 0.8697 -0.1648 -0.0453 -0.0875 39  HIS B C     
2325 O O     . HIS B 39  ? 1.0682 1.0085 0.8978 -0.1617 -0.0532 -0.0745 39  HIS B O     
2326 C CB    . HIS B 39  ? 1.0281 0.9118 0.8489 -0.1540 -0.0310 -0.1038 39  HIS B CB    
2327 C CG    . HIS B 39  ? 1.0183 0.9126 0.8617 -0.1366 -0.0324 -0.0965 39  HIS B CG    
2328 N ND1   . HIS B 39  ? 1.0150 0.9182 0.8735 -0.1308 -0.0332 -0.0938 39  HIS B ND1   
2329 C CD2   . HIS B 39  ? 0.9618 0.8574 0.8145 -0.1244 -0.0320 -0.0926 39  HIS B CD2   
2330 C CE1   . HIS B 39  ? 0.9557 0.8650 0.8309 -0.1162 -0.0328 -0.0891 39  HIS B CE1   
2331 N NE2   . HIS B 39  ? 0.9153 0.8197 0.7876 -0.1122 -0.0322 -0.0883 39  HIS B NE2   
2332 N N     . PHE B 40  ? 1.0681 0.9681 0.8706 -0.1648 -0.0402 -0.0937 40  PHE B N     
2333 C CA    . PHE B 40  ? 1.0086 0.9185 0.8118 -0.1623 -0.0442 -0.0856 40  PHE B CA    
2334 C C     . PHE B 40  ? 0.9969 0.9148 0.8248 -0.1432 -0.0451 -0.0769 40  PHE B C     
2335 O O     . PHE B 40  ? 1.0670 0.9775 0.9079 -0.1314 -0.0407 -0.0802 40  PHE B O     
2336 C CB    . PHE B 40  ? 1.0509 0.9393 0.8363 -0.1647 -0.0367 -0.0951 40  PHE B CB    
2337 C CG    . PHE B 40  ? 1.1424 1.0269 0.9010 -0.1854 -0.0365 -0.1014 40  PHE B CG    
2338 C CD1   . PHE B 40  ? 1.1853 1.0879 0.9342 -0.1965 -0.0441 -0.0933 40  PHE B CD1   
2339 C CD2   . PHE B 40  ? 1.1642 1.0265 0.9072 -0.1943 -0.0277 -0.1156 40  PHE B CD2   
2340 C CE1   . PHE B 40  ? 1.1918 1.0907 0.9133 -0.2175 -0.0433 -0.1004 40  PHE B CE1   
2341 C CE2   . PHE B 40  ? 1.1810 1.0369 0.8974 -0.2146 -0.0257 -0.1235 40  PHE B CE2   
2342 C CZ    . PHE B 40  ? 1.2254 1.0995 0.9299 -0.2268 -0.0335 -0.1166 40  PHE B CZ    
2343 N N     . GLY B 41  ? 1.0051 0.9389 0.8397 -0.1410 -0.0507 -0.0652 41  GLY B N     
2344 C CA    . GLY B 41  ? 0.9858 0.9223 0.8415 -0.1237 -0.0495 -0.0584 41  GLY B CA    
2345 C C     . GLY B 41  ? 1.0025 0.9201 0.8517 -0.1175 -0.0434 -0.0646 41  GLY B C     
2346 O O     . GLY B 41  ? 1.0137 0.9187 0.8423 -0.1268 -0.0405 -0.0722 41  GLY B O     
2347 N N     . TYR B 42  ? 0.9746 0.8897 0.8414 -0.1020 -0.0406 -0.0613 42  TYR B N     
2348 C CA    . TYR B 42  ? 1.0137 0.9131 0.8771 -0.0956 -0.0355 -0.0653 42  TYR B CA    
2349 C C     . TYR B 42  ? 1.0881 0.9966 0.9707 -0.0842 -0.0371 -0.0545 42  TYR B C     
2350 O O     . TYR B 42  ? 1.0835 0.9975 0.9854 -0.0741 -0.0363 -0.0508 42  TYR B O     
2351 C CB    . TYR B 42  ? 0.9343 0.8125 0.7969 -0.0884 -0.0273 -0.0773 42  TYR B CB    
2352 C CG    . TYR B 42  ? 0.9343 0.7965 0.7930 -0.0826 -0.0217 -0.0815 42  TYR B CG    
2353 C CD1   . TYR B 42  ? 0.9363 0.7992 0.8096 -0.0713 -0.0210 -0.0765 42  TYR B CD1   
2354 C CD2   . TYR B 42  ? 0.9072 0.7524 0.7487 -0.0883 -0.0161 -0.0908 42  TYR B CD2   
2355 C CE1   . TYR B 42  ? 0.9349 0.7834 0.8047 -0.0667 -0.0162 -0.0803 42  TYR B CE1   
2356 C CE2   . TYR B 42  ? 0.9039 0.7352 0.7431 -0.0829 -0.0107 -0.0940 42  TYR B CE2   
2357 C CZ    . TYR B 42  ? 0.8930 0.7267 0.7459 -0.0725 -0.0113 -0.0886 42  TYR B CZ    
2358 O OH    . TYR B 42  ? 0.8240 0.6444 0.6740 -0.0682 -0.0061 -0.0915 42  TYR B OH    
2359 N N     . TRP B 43  ? 1.0691 0.9775 0.9464 -0.0857 -0.0381 -0.0500 43  TRP B N     
2360 C CA    . TRP B 43  ? 1.0995 1.0156 0.9949 -0.0758 -0.0391 -0.0388 43  TRP B CA    
2361 C C     . TRP B 43  ? 1.1618 1.0610 1.0513 -0.0713 -0.0341 -0.0436 43  TRP B C     
2362 O O     . TRP B 43  ? 1.1000 0.9866 0.9697 -0.0784 -0.0314 -0.0524 43  TRP B O     
2363 C CB    . TRP B 43  ? 1.1237 1.0639 1.0225 -0.0828 -0.0473 -0.0230 43  TRP B CB    
2364 C CG    . TRP B 43  ? 1.0696 1.0298 0.9773 -0.0868 -0.0528 -0.0153 43  TRP B CG    
2365 C CD1   . TRP B 43  ? 1.0739 1.0501 1.0075 -0.0777 -0.0544 -0.0028 43  TRP B CD1   
2366 C CD2   . TRP B 43  ? 1.0589 1.0257 0.9505 -0.1014 -0.0570 -0.0191 43  TRP B CD2   
2367 N NE1   . TRP B 43  ? 1.0590 1.0530 0.9941 -0.0854 -0.0598 0.0024  43  TRP B NE1   
2368 C CE2   . TRP B 43  ? 1.0613 1.0499 0.9703 -0.1005 -0.0620 -0.0077 43  TRP B CE2   
2369 C CE3   . TRP B 43  ? 1.0270 0.9823 0.8916 -0.1152 -0.0561 -0.0312 43  TRP B CE3   
2370 C CZ2   . TRP B 43  ? 1.0079 1.0082 0.9076 -0.1136 -0.0672 -0.0078 43  TRP B CZ2   
2371 C CZ3   . TRP B 43  ? 1.0115 0.9769 0.8666 -0.1285 -0.0605 -0.0321 43  TRP B CZ3   
2372 C CH2   . TRP B 43  ? 0.9803 0.9684 0.8526 -0.1279 -0.0665 -0.0204 43  TRP B CH2   
2373 N N     . ASP B 44  ? 1.1583 1.0570 1.0659 -0.0597 -0.0322 -0.0376 44  ASP B N     
2374 C CA    . ASP B 44  ? 1.2536 1.1360 1.1580 -0.0545 -0.0273 -0.0421 44  ASP B CA    
2375 C C     . ASP B 44  ? 1.2882 1.1750 1.1809 -0.0618 -0.0302 -0.0361 44  ASP B C     
2376 O O     . ASP B 44  ? 1.2920 1.1642 1.1726 -0.0626 -0.0261 -0.0427 44  ASP B O     
2377 C CB    . ASP B 44  ? 1.2766 1.1564 1.2035 -0.0412 -0.0239 -0.0383 44  ASP B CB    
2378 C CG    . ASP B 44  ? 1.2472 1.1213 1.1824 -0.0353 -0.0199 -0.0462 44  ASP B CG    
2379 O OD1   . ASP B 44  ? 1.2101 1.0700 1.1341 -0.0364 -0.0160 -0.0582 44  ASP B OD1   
2380 O OD2   . ASP B 44  ? 1.2779 1.1630 1.2306 -0.0302 -0.0204 -0.0398 44  ASP B OD2   
2381 N N     . SER B 45  ? 1.2718 1.1796 1.1684 -0.0673 -0.0372 -0.0226 45  SER B N     
2382 C CA    . SER B 45  ? 1.3125 1.2287 1.1956 -0.0770 -0.0412 -0.0158 45  SER B CA    
2383 C C     . SER B 45  ? 1.3036 1.2464 1.1878 -0.0870 -0.0501 -0.0029 45  SER B C     
2384 O O     . SER B 45  ? 1.2879 1.2438 1.1917 -0.0817 -0.0527 0.0054  45  SER B O     
2385 C CB    . SER B 45  ? 1.3869 1.3015 1.2820 -0.0685 -0.0398 -0.0073 45  SER B CB    
2386 O OG    . SER B 45  ? 1.4146 1.3398 1.3377 -0.0578 -0.0409 0.0051  45  SER B OG    
2387 N N     . PRO B 46  ? 1.3194 1.2717 1.1830 -0.1021 -0.0545 -0.0004 46  PRO B N     
2388 C CA    . PRO B 46  ? 1.3026 1.2786 1.1605 -0.1158 -0.0630 0.0078  46  PRO B CA    
2389 C C     . PRO B 46  ? 1.3281 1.3309 1.2136 -0.1102 -0.0698 0.0289  46  PRO B C     
2390 O O     . PRO B 46  ? 1.2868 1.3090 1.1752 -0.1176 -0.0760 0.0360  46  PRO B O     
2391 C CB    . PRO B 46  ? 1.2064 1.1873 1.0377 -0.1324 -0.0656 0.0076  46  PRO B CB    
2392 C CG    . PRO B 46  ? 1.1853 1.1383 1.0034 -0.1281 -0.0562 -0.0073 46  PRO B CG    
2393 C CD    . PRO B 46  ? 1.2662 1.2084 1.1093 -0.1085 -0.0517 -0.0056 46  PRO B CD    
2394 N N     . ASP B 47  ? 1.3101 1.3138 1.2173 -0.0970 -0.0679 0.0394  47  ASP B N     
2395 C CA    . ASP B 47  ? 1.3138 1.3408 1.2510 -0.0895 -0.0722 0.0611  47  ASP B CA    
2396 C C     . ASP B 47  ? 1.3127 1.3391 1.2743 -0.0770 -0.0687 0.0616  47  ASP B C     
2397 O O     . ASP B 47  ? 1.2831 1.3298 1.2714 -0.0707 -0.0713 0.0802  47  ASP B O     
2398 C CB    . ASP B 47  ? 1.3502 1.3720 1.3014 -0.0790 -0.0689 0.0692  47  ASP B CB    
2399 C CG    . ASP B 47  ? 1.4269 1.4159 1.3734 -0.0689 -0.0590 0.0507  47  ASP B CG    
2400 O OD1   . ASP B 47  ? 1.3960 1.3705 1.3459 -0.0623 -0.0539 0.0382  47  ASP B OD1   
2401 O OD2   . ASP B 47  ? 1.5007 1.4800 1.4405 -0.0680 -0.0567 0.0495  47  ASP B OD2   
2402 N N     . SER B 48  ? 1.3306 1.3347 1.2850 -0.0727 -0.0623 0.0426  48  SER B N     
2403 C CA    . SER B 48  ? 1.2746 1.2741 1.2509 -0.0597 -0.0571 0.0407  48  SER B CA    
2404 C C     . SER B 48  ? 1.1609 1.1882 1.1539 -0.0620 -0.0630 0.0563  48  SER B C     
2405 O O     . SER B 48  ? 1.1919 1.2381 1.1726 -0.0764 -0.0714 0.0625  48  SER B O     
2406 C CB    . SER B 48  ? 1.2086 1.1850 1.1694 -0.0596 -0.0515 0.0189  48  SER B CB    
2407 O OG    . SER B 48  ? 1.1838 1.1529 1.1626 -0.0474 -0.0453 0.0144  48  SER B OG    
2408 N N     . GLN B 49  ? 1.1268 1.1574 1.1486 -0.0481 -0.0582 0.0636  49  GLN B N     
2409 C CA    . GLN B 49  ? 1.1072 1.1645 1.1485 -0.0484 -0.0626 0.0798  49  GLN B CA    
2410 C C     . GLN B 49  ? 1.0925 1.1442 1.1352 -0.0457 -0.0590 0.0688  49  GLN B C     
2411 O O     . GLN B 49  ? 1.0991 1.1693 1.1635 -0.0416 -0.0596 0.0810  49  GLN B O     
2412 C CB    . GLN B 49  ? 1.0747 1.1437 1.1510 -0.0349 -0.0592 0.0996  49  GLN B CB    
2413 N N     . VAL B 50  ? 1.0938 1.1213 1.1160 -0.0473 -0.0548 0.0472  50  VAL B N     
2414 C CA    . VAL B 50  ? 1.0887 1.1086 1.1145 -0.0426 -0.0498 0.0362  50  VAL B CA    
2415 C C     . VAL B 50  ? 1.0218 1.0589 1.0374 -0.0558 -0.0576 0.0384  50  VAL B C     
2416 O O     . VAL B 50  ? 1.0119 1.0499 1.0033 -0.0703 -0.0636 0.0345  50  VAL B O     
2417 C CB    . VAL B 50  ? 1.1160 1.1061 1.1249 -0.0400 -0.0430 0.0146  50  VAL B CB    
2418 C CG1   . VAL B 50  ? 1.0816 1.0647 1.0949 -0.0349 -0.0375 0.0040  50  VAL B CG1   
2419 C CG2   . VAL B 50  ? 1.1129 1.0871 1.1284 -0.0302 -0.0368 0.0129  50  VAL B CG2   
2420 N N     . PRO B 51  ? 1.0085 1.0590 1.0414 -0.0517 -0.0569 0.0441  51  PRO B N     
2421 C CA    . PRO B 51  ? 1.0271 1.0965 1.0517 -0.0652 -0.0651 0.0482  51  PRO B CA    
2422 C C     . PRO B 51  ? 1.0645 1.1154 1.0595 -0.0759 -0.0652 0.0285  51  PRO B C     
2423 O O     . PRO B 51  ? 1.1033 1.1293 1.0909 -0.0696 -0.0578 0.0124  51  PRO B O     
2424 C CB    . PRO B 51  ? 1.0202 1.1011 1.0699 -0.0555 -0.0612 0.0544  51  PRO B CB    
2425 C CG    . PRO B 51  ? 1.0656 1.1387 1.1396 -0.0378 -0.0517 0.0581  51  PRO B CG    
2426 C CD    . PRO B 51  ? 1.0548 1.1016 1.1133 -0.0355 -0.0477 0.0448  51  PRO B CD    
2427 N N     . LEU B 52  ? 1.1052 1.1692 1.0838 -0.0928 -0.0736 0.0308  52  LEU B N     
2428 C CA    . LEU B 52  ? 1.1149 1.1615 1.0666 -0.1040 -0.0729 0.0130  52  LEU B CA    
2429 C C     . LEU B 52  ? 1.0728 1.1091 1.0307 -0.0966 -0.0670 0.0028  52  LEU B C     
2430 O O     . LEU B 52  ? 1.0471 1.0596 0.9910 -0.0959 -0.0612 -0.0137 52  LEU B O     
2431 C CB    . LEU B 52  ? 1.0977 1.1619 1.0328 -0.1243 -0.0824 0.0180  52  LEU B CB    
2432 C CG    . LEU B 52  ? 1.0953 1.1380 1.0061 -0.1337 -0.0791 -0.0013 52  LEU B CG    
2433 C CD1   . LEU B 52  ? 1.1124 1.1312 1.0016 -0.1366 -0.0745 -0.0139 52  LEU B CD1   
2434 C CD2   . LEU B 52  ? 1.1108 1.1701 1.0097 -0.1526 -0.0869 0.0019  52  LEU B CD2   
2435 N N     . ALA B 53  ? 1.0690 1.1243 1.0488 -0.0911 -0.0680 0.0137  53  ALA B N     
2436 C CA    . ALA B 53  ? 1.0369 1.0847 1.0255 -0.0826 -0.0617 0.0056  53  ALA B CA    
2437 C C     . ALA B 53  ? 1.0435 1.0636 1.0284 -0.0716 -0.0523 -0.0093 53  ALA B C     
2438 O O     . ALA B 53  ? 0.9923 0.9947 0.9623 -0.0745 -0.0490 -0.0238 53  ALA B O     
2439 C CB    . ALA B 53  ? 0.9939 1.0636 1.0126 -0.0725 -0.0609 0.0209  53  ALA B CB    
2440 N N     . GLU B 54  ? 1.0893 1.1059 1.0875 -0.0602 -0.0482 -0.0048 54  GLU B N     
2441 C CA    . GLU B 54  ? 1.0045 0.9972 1.0012 -0.0501 -0.0395 -0.0174 54  GLU B CA    
2442 C C     . GLU B 54  ? 1.0067 0.9794 0.9784 -0.0573 -0.0395 -0.0298 54  GLU B C     
2443 O O     . GLU B 54  ? 1.0112 0.9658 0.9750 -0.0547 -0.0340 -0.0430 54  GLU B O     
2444 C CB    . GLU B 54  ? 1.0298 1.0235 1.0465 -0.0377 -0.0351 -0.0091 54  GLU B CB    
2445 C CG    . GLU B 54  ? 1.1257 1.0963 1.1422 -0.0279 -0.0261 -0.0215 54  GLU B CG    
2446 C CD    . GLU B 54  ? 1.1958 1.1660 1.2329 -0.0163 -0.0208 -0.0135 54  GLU B CD    
2447 O OE1   . GLU B 54  ? 1.1141 1.1031 1.1718 -0.0125 -0.0219 0.0019  54  GLU B OE1   
2448 O OE2   . GLU B 54  ? 1.2289 1.1803 1.2623 -0.0113 -0.0154 -0.0219 54  GLU B OE2   
2449 N N     . ALA B 55  ? 1.0423 1.0192 1.0014 -0.0671 -0.0454 -0.0252 55  ALA B N     
2450 C CA    . ALA B 55  ? 1.0226 0.9796 0.9599 -0.0724 -0.0435 -0.0362 55  ALA B CA    
2451 C C     . ALA B 55  ? 0.9885 0.9336 0.9071 -0.0816 -0.0423 -0.0490 55  ALA B C     
2452 O O     . ALA B 55  ? 0.9382 0.8628 0.8440 -0.0815 -0.0372 -0.0601 55  ALA B O     
2453 C CB    . ALA B 55  ? 1.0451 1.0104 0.9729 -0.0813 -0.0494 -0.0282 55  ALA B CB    
2454 N N     . THR B 56  ? 0.9762 0.9338 0.8937 -0.0898 -0.0465 -0.0466 56  THR B N     
2455 C CA    . THR B 56  ? 0.9154 0.8608 0.8184 -0.0974 -0.0441 -0.0583 56  THR B CA    
2456 C C     . THR B 56  ? 0.9601 0.8931 0.8714 -0.0864 -0.0370 -0.0664 56  THR B C     
2457 O O     . THR B 56  ? 0.9157 0.8304 0.8156 -0.0878 -0.0320 -0.0772 56  THR B O     
2458 C CB    . THR B 56  ? 0.9259 0.8887 0.8275 -0.1090 -0.0504 -0.0532 56  THR B CB    
2459 O OG1   . THR B 56  ? 0.9400 0.9248 0.8641 -0.1019 -0.0537 -0.0404 56  THR B OG1   
2460 C CG2   . THR B 56  ? 1.0180 0.9869 0.9014 -0.1254 -0.0564 -0.0505 56  THR B CG2   
2461 N N     . ASP B 57  ? 0.9694 0.9128 0.9008 -0.0756 -0.0359 -0.0609 57  ASP B N     
2462 C CA    . ASP B 57  ? 0.9114 0.8444 0.8495 -0.0661 -0.0290 -0.0686 57  ASP B CA    
2463 C C     . ASP B 57  ? 0.8942 0.8076 0.8255 -0.0611 -0.0238 -0.0763 57  ASP B C     
2464 O O     . ASP B 57  ? 0.8909 0.7919 0.8183 -0.0590 -0.0189 -0.0849 57  ASP B O     
2465 C CB    . ASP B 57  ? 0.8928 0.8386 0.8527 -0.0554 -0.0271 -0.0621 57  ASP B CB    
2466 C CG    . ASP B 57  ? 0.9191 0.8815 0.8868 -0.0585 -0.0297 -0.0575 57  ASP B CG    
2467 O OD1   . ASP B 57  ? 0.9354 0.8948 0.8921 -0.0668 -0.0310 -0.0628 57  ASP B OD1   
2468 O OD2   . ASP B 57  ? 0.9448 0.9232 0.9308 -0.0525 -0.0299 -0.0480 57  ASP B OD2   
2469 N N     . ARG B 58  ? 0.8551 0.7671 0.7855 -0.0598 -0.0250 -0.0722 58  ARG B N     
2470 C CA    . ARG B 58  ? 0.8930 0.7872 0.8172 -0.0554 -0.0204 -0.0784 58  ARG B CA    
2471 C C     . ARG B 58  ? 0.9364 0.8157 0.8426 -0.0630 -0.0181 -0.0875 58  ARG B C     
2472 O O     . ARG B 58  ? 0.9139 0.7802 0.8190 -0.0585 -0.0127 -0.0942 58  ARG B O     
2473 C CB    . ARG B 58  ? 0.9452 0.8422 0.8704 -0.0546 -0.0229 -0.0712 58  ARG B CB    
2474 C CG    . ARG B 58  ? 0.9757 0.8554 0.8905 -0.0535 -0.0193 -0.0768 58  ARG B CG    
2475 C CD    . ARG B 58  ? 0.9717 0.8470 0.8997 -0.0424 -0.0156 -0.0754 58  ARG B CD    
2476 N NE    . ARG B 58  ? 1.0754 0.9365 0.9946 -0.0418 -0.0130 -0.0790 58  ARG B NE    
2477 C CZ    . ARG B 58  ? 1.0615 0.9236 0.9831 -0.0400 -0.0143 -0.0727 58  ARG B CZ    
2478 N NH1   . ARG B 58  ? 1.0398 0.9171 0.9722 -0.0392 -0.0184 -0.0615 58  ARG B NH1   
2479 N NH2   . ARG B 58  ? 1.0956 0.9447 1.0099 -0.0391 -0.0113 -0.0763 58  ARG B NH2   
2480 N N     . LEU B 59  ? 0.9244 0.8057 0.8174 -0.0745 -0.0215 -0.0872 59  LEU B N     
2481 C CA    . LEU B 59  ? 0.8705 0.7349 0.7477 -0.0810 -0.0170 -0.0963 59  LEU B CA    
2482 C C     . LEU B 59  ? 0.8830 0.7427 0.7644 -0.0788 -0.0131 -0.1016 59  LEU B C     
2483 O O     . LEU B 59  ? 0.8612 0.7059 0.7385 -0.0768 -0.0071 -0.1076 59  LEU B O     
2484 C CB    . LEU B 59  ? 0.9001 0.7658 0.7608 -0.0954 -0.0201 -0.0968 59  LEU B CB    
2485 C CG    . LEU B 59  ? 0.8772 0.7218 0.7217 -0.1016 -0.0129 -0.1070 59  LEU B CG    
2486 C CD1   . LEU B 59  ? 0.8889 0.7210 0.7264 -0.0988 -0.0087 -0.1092 59  LEU B CD1   
2487 C CD2   . LEU B 59  ? 0.8942 0.7377 0.7227 -0.1173 -0.0138 -0.1106 59  LEU B CD2   
2488 N N     . THR B 60  ? 0.8724 0.7459 0.7631 -0.0790 -0.0163 -0.0982 60  THR B N     
2489 C CA    . THR B 60  ? 0.8004 0.6717 0.6965 -0.0763 -0.0128 -0.1020 60  THR B CA    
2490 C C     . THR B 60  ? 0.8406 0.7034 0.7425 -0.0666 -0.0077 -0.1051 60  THR B C     
2491 O O     . THR B 60  ? 0.8188 0.6714 0.7182 -0.0662 -0.0029 -0.1096 60  THR B O     
2492 C CB    . THR B 60  ? 0.8296 0.7186 0.7387 -0.0741 -0.0161 -0.0970 60  THR B CB    
2493 O OG1   . THR B 60  ? 0.9083 0.8098 0.8147 -0.0833 -0.0221 -0.0919 60  THR B OG1   
2494 C CG2   . THR B 60  ? 0.8073 0.6936 0.7197 -0.0728 -0.0123 -0.1010 60  THR B CG2   
2495 N N     . ASP B 61  ? 0.8555 0.7229 0.7659 -0.0590 -0.0084 -0.1020 61  ASP B N     
2496 C CA    . ASP B 61  ? 0.8528 0.7152 0.7700 -0.0504 -0.0040 -0.1048 61  ASP B CA    
2497 C C     . ASP B 61  ? 0.8452 0.6918 0.7539 -0.0504 -0.0002 -0.1087 61  ASP B C     
2498 O O     . ASP B 61  ? 0.8685 0.7094 0.7779 -0.0486 0.0037  -0.1120 61  ASP B O     
2499 C CB    . ASP B 61  ? 0.8024 0.6725 0.7315 -0.0431 -0.0048 -0.1007 61  ASP B CB    
2500 C CG    . ASP B 61  ? 0.8474 0.7327 0.7891 -0.0405 -0.0056 -0.0974 61  ASP B CG    
2501 O OD1   . ASP B 61  ? 0.8456 0.7353 0.7871 -0.0433 -0.0053 -0.0993 61  ASP B OD1   
2502 O OD2   . ASP B 61  ? 0.8185 0.7116 0.7716 -0.0351 -0.0058 -0.0923 61  ASP B OD2   
2503 N N     . MET B 62  ? 0.8957 0.7363 0.7962 -0.0531 -0.0012 -0.1076 62  MET B N     
2504 C CA    . MET B 62  ? 0.8858 0.7117 0.7791 -0.0527 0.0033  -0.1110 62  MET B CA    
2505 C C     . MET B 62  ? 0.8806 0.6974 0.7667 -0.0579 0.0075  -0.1148 62  MET B C     
2506 O O     . MET B 62  ? 0.9062 0.7126 0.7912 -0.0558 0.0127  -0.1167 62  MET B O     
2507 C CB    . MET B 62  ? 0.8662 0.6876 0.7518 -0.0546 0.0022  -0.1092 62  MET B CB    
2508 C CG    . MET B 62  ? 0.9253 0.7537 0.8032 -0.0628 -0.0025 -0.1064 62  MET B CG    
2509 S SD    . MET B 62  ? 0.9734 0.7976 0.8424 -0.0647 -0.0034 -0.1036 62  MET B SD    
2510 C CE    . MET B 62  ? 0.8948 0.6984 0.7497 -0.0682 0.0049  -0.1113 62  MET B CE    
2511 N N     . MET B 63  ? 0.8401 0.6609 0.7228 -0.0647 0.0058  -0.1153 63  MET B N     
2512 C CA    . MET B 63  ? 0.8667 0.6777 0.7455 -0.0687 0.0111  -0.1186 63  MET B CA    
2513 C C     . MET B 63  ? 0.8289 0.6455 0.7190 -0.0639 0.0125  -0.1176 63  MET B C     
2514 O O     . MET B 63  ? 0.8146 0.6232 0.7066 -0.0625 0.0179  -0.1180 63  MET B O     
2515 C CB    . MET B 63  ? 0.8780 0.6890 0.7476 -0.0792 0.0096  -0.1202 63  MET B CB    
2516 C CG    . MET B 63  ? 0.8732 0.6797 0.7291 -0.0862 0.0083  -0.1214 63  MET B CG    
2517 S SD    . MET B 63  ? 0.9062 0.7111 0.7489 -0.1013 0.0077  -0.1249 63  MET B SD    
2518 C CE    . MET B 63  ? 0.8591 0.6443 0.7009 -0.1023 0.0187  -0.1307 63  MET B CE    
2519 N N     . ALA B 64  ? 0.8007 0.6319 0.6991 -0.0613 0.0080  -0.1154 64  ALA B N     
2520 C CA    . ALA B 64  ? 0.8654 0.7037 0.7735 -0.0573 0.0092  -0.1146 64  ALA B CA    
2521 C C     . ALA B 64  ? 0.8356 0.6691 0.7468 -0.0517 0.0127  -0.1150 64  ALA B C     
2522 O O     . ALA B 64  ? 0.7830 0.6161 0.6978 -0.0513 0.0160  -0.1140 64  ALA B O     
2523 C CB    . ALA B 64  ? 0.7300 0.5839 0.6460 -0.0547 0.0051  -0.1129 64  ALA B CB    
2524 N N     . GLU B 65  ? 0.8053 0.6362 0.7156 -0.0480 0.0119  -0.1154 65  GLU B N     
2525 C CA    . GLU B 65  ? 0.7592 0.5869 0.6725 -0.0436 0.0145  -0.1156 65  GLU B CA    
2526 C C     . GLU B 65  ? 0.7858 0.6034 0.6965 -0.0448 0.0192  -0.1145 65  GLU B C     
2527 O O     . GLU B 65  ? 0.8175 0.6375 0.7332 -0.0432 0.0214  -0.1126 65  GLU B O     
2528 C CB    . GLU B 65  ? 0.8314 0.6567 0.7441 -0.0402 0.0129  -0.1158 65  GLU B CB    
2529 C CG    . GLU B 65  ? 0.9539 0.7697 0.8644 -0.0380 0.0156  -0.1157 65  GLU B CG    
2530 C CD    . GLU B 65  ? 1.1913 1.0055 1.1025 -0.0347 0.0137  -0.1152 65  GLU B CD    
2531 O OE1   . GLU B 65  ? 1.2857 1.1073 1.2027 -0.0324 0.0115  -0.1151 65  GLU B OE1   
2532 O OE2   . GLU B 65  ? 1.2833 1.0888 1.1901 -0.0342 0.0151  -0.1144 65  GLU B OE2   
2533 N N     . ARG B 66  ? 0.8199 0.6269 0.7230 -0.0483 0.0214  -0.1151 66  ARG B N     
2534 C CA    . ARG B 66  ? 0.7749 0.5709 0.6771 -0.0487 0.0279  -0.1138 66  ARG B CA    
2535 C C     . ARG B 66  ? 0.8137 0.6120 0.7220 -0.0505 0.0310  -0.1114 66  ARG B C     
2536 O O     . ARG B 66  ? 0.8792 0.6712 0.7915 -0.0494 0.0369  -0.1080 66  ARG B O     
2537 C CB    . ARG B 66  ? 0.8355 0.6184 0.7268 -0.0526 0.0307  -0.1165 66  ARG B CB    
2538 C CG    . ARG B 66  ? 0.8375 0.6191 0.7240 -0.0506 0.0280  -0.1172 66  ARG B CG    
2539 C CD    . ARG B 66  ? 0.8513 0.6251 0.7250 -0.0566 0.0285  -0.1201 66  ARG B CD    
2540 N NE    . ARG B 66  ? 0.8120 0.5795 0.6807 -0.0547 0.0298  -0.1197 66  ARG B NE    
2541 C CZ    . ARG B 66  ? 0.8488 0.6226 0.7164 -0.0535 0.0243  -0.1181 66  ARG B CZ    
2542 N NH1   . ARG B 66  ? 0.8222 0.6085 0.6945 -0.0533 0.0176  -0.1165 66  ARG B NH1   
2543 N NH2   . ARG B 66  ? 0.9210 0.6887 0.7839 -0.0523 0.0259  -0.1174 66  ARG B NH2   
2544 N N     . LEU B 67  ? 0.7937 0.6016 0.7043 -0.0529 0.0275  -0.1118 67  LEU B N     
2545 C CA    . LEU B 67  ? 0.7775 0.5900 0.6956 -0.0542 0.0299  -0.1082 67  LEU B CA    
2546 C C     . LEU B 67  ? 0.7408 0.5633 0.6680 -0.0505 0.0301  -0.1034 67  LEU B C     
2547 O O     . LEU B 67  ? 0.7136 0.5382 0.6484 -0.0508 0.0338  -0.0978 67  LEU B O     
2548 C CB    . LEU B 67  ? 0.7352 0.5580 0.6541 -0.0576 0.0255  -0.1092 67  LEU B CB    
2549 C CG    . LEU B 67  ? 0.7810 0.5980 0.6912 -0.0635 0.0242  -0.1128 67  LEU B CG    
2550 C CD1   . LEU B 67  ? 0.7012 0.5322 0.6148 -0.0660 0.0190  -0.1122 67  LEU B CD1   
2551 C CD2   . LEU B 67  ? 0.7937 0.5955 0.7008 -0.0681 0.0312  -0.1134 67  LEU B CD2   
2552 N N     . ARG B 68  ? 0.7863 0.6159 0.7133 -0.0477 0.0263  -0.1052 68  ARG B N     
2553 C CA    . ARG B 68  ? 0.7060 0.5460 0.6391 -0.0461 0.0260  -0.1019 68  ARG B CA    
2554 C C     . ARG B 68  ? 0.6987 0.5529 0.6379 -0.0485 0.0250  -0.0988 68  ARG B C     
2555 O O     . ARG B 68  ? 0.7305 0.5894 0.6764 -0.0496 0.0275  -0.0920 68  ARG B O     
2556 C CB    . ARG B 68  ? 0.7542 0.5881 0.6905 -0.0448 0.0303  -0.0965 68  ARG B CB    
2557 C CG    . ARG B 68  ? 0.9134 0.7362 0.8441 -0.0423 0.0310  -0.0993 68  ARG B CG    
2558 C CD    . ARG B 68  ? 1.0554 0.8740 0.9911 -0.0407 0.0358  -0.0927 68  ARG B CD    
2559 N NE    . ARG B 68  ? 1.1654 0.9698 1.0950 -0.0388 0.0384  -0.0950 68  ARG B NE    
2560 C CZ    . ARG B 68  ? 1.2425 1.0458 1.1723 -0.0366 0.0384  -0.0935 68  ARG B CZ    
2561 N NH1   . ARG B 68  ? 1.2448 1.0598 1.1798 -0.0370 0.0357  -0.0903 68  ARG B NH1   
2562 N NH2   . ARG B 68  ? 1.2492 1.0398 1.1732 -0.0351 0.0411  -0.0954 68  ARG B NH2   
2563 N N     . ILE B 69  ? 0.7066 0.5688 0.6445 -0.0492 0.0216  -0.1029 69  ILE B N     
2564 C CA    . ILE B 69  ? 0.6870 0.5635 0.6299 -0.0517 0.0206  -0.1004 69  ILE B CA    
2565 C C     . ILE B 69  ? 0.7769 0.6655 0.7193 -0.0513 0.0186  -0.1045 69  ILE B C     
2566 O O     . ILE B 69  ? 0.7438 0.6279 0.6828 -0.0490 0.0183  -0.1092 69  ILE B O     
2567 C CB    . ILE B 69  ? 0.7697 0.6449 0.7122 -0.0537 0.0197  -0.1012 69  ILE B CB    
2568 C CG1   . ILE B 69  ? 0.7282 0.5999 0.6654 -0.0524 0.0168  -0.1068 69  ILE B CG1   
2569 C CG2   . ILE B 69  ? 0.6979 0.5597 0.6402 -0.0554 0.0234  -0.0982 69  ILE B CG2   
2570 C CD1   . ILE B 69  ? 0.7394 0.6169 0.6774 -0.0552 0.0144  -0.1070 69  ILE B CD1   
2571 N N     . GLY B 70  ? 0.7605 0.6637 0.7063 -0.0539 0.0181  -0.1029 70  GLY B N     
2572 C CA    . GLY B 70  ? 0.6849 0.5988 0.6293 -0.0544 0.0178  -0.1080 70  GLY B CA    
2573 C C     . GLY B 70  ? 0.7581 0.6847 0.7057 -0.0563 0.0173  -0.1073 70  GLY B C     
2574 O O     . GLY B 70  ? 0.7390 0.6644 0.6896 -0.0570 0.0165  -0.1034 70  GLY B O     
2575 N N     . ALA B 71  ? 0.7523 0.6909 0.6991 -0.0578 0.0185  -0.1113 71  ALA B N     
2576 C CA    . ALA B 71  ? 0.7434 0.6961 0.6937 -0.0602 0.0184  -0.1093 71  ALA B CA    
2577 C C     . ALA B 71  ? 0.7644 0.7249 0.7185 -0.0644 0.0174  -0.1000 71  ALA B C     
2578 O O     . ALA B 71  ? 0.7660 0.7273 0.7199 -0.0664 0.0176  -0.0958 71  ALA B O     
2579 C CB    . ALA B 71  ? 0.7300 0.6942 0.6777 -0.0618 0.0213  -0.1156 71  ALA B CB    
2580 N N     . GLY B 72  ? 0.8462 0.8125 0.8053 -0.0655 0.0166  -0.0957 72  GLY B N     
2581 C CA    . GLY B 72  ? 0.8571 0.8302 0.8224 -0.0690 0.0164  -0.0856 72  GLY B CA    
2582 C C     . GLY B 72  ? 0.8559 0.8144 0.8239 -0.0677 0.0174  -0.0803 72  GLY B C     
2583 O O     . GLY B 72  ? 0.8926 0.8565 0.8659 -0.0696 0.0184  -0.0718 72  GLY B O     
2584 N N     . SER B 73  ? 0.8086 0.7495 0.7733 -0.0646 0.0175  -0.0849 73  SER B N     
2585 C CA    . SER B 73  ? 0.7677 0.6927 0.7343 -0.0639 0.0199  -0.0812 73  SER B CA    
2586 C C     . SER B 73  ? 0.7520 0.6718 0.7202 -0.0660 0.0201  -0.0809 73  SER B C     
2587 O O     . SER B 73  ? 0.7371 0.6572 0.7011 -0.0662 0.0174  -0.0865 73  SER B O     
2588 C CB    . SER B 73  ? 0.7174 0.6259 0.6771 -0.0606 0.0204  -0.0871 73  SER B CB    
2589 O OG    . SER B 73  ? 0.7682 0.6782 0.7269 -0.0591 0.0209  -0.0867 73  SER B OG    
2590 N N     . ARG B 74  ? 0.7385 0.6532 0.7134 -0.0679 0.0235  -0.0739 74  ARG B N     
2591 C CA    . ARG B 74  ? 0.7282 0.6333 0.7031 -0.0711 0.0247  -0.0748 74  ARG B CA    
2592 C C     . ARG B 74  ? 0.7298 0.6137 0.6961 -0.0707 0.0267  -0.0811 74  ARG B C     
2593 O O     . ARG B 74  ? 0.7775 0.6500 0.7443 -0.0684 0.0310  -0.0796 74  ARG B O     
2594 C CB    . ARG B 74  ? 0.7713 0.6765 0.7574 -0.0733 0.0292  -0.0651 74  ARG B CB    
2595 C CG    . ARG B 74  ? 0.7420 0.6698 0.7380 -0.0742 0.0278  -0.0558 74  ARG B CG    
2596 C CD    . ARG B 74  ? 0.7271 0.6719 0.7216 -0.0766 0.0229  -0.0581 74  ARG B CD    
2597 N NE    . ARG B 74  ? 0.7135 0.6543 0.7103 -0.0804 0.0231  -0.0577 74  ARG B NE    
2598 C CZ    . ARG B 74  ? 0.7758 0.7310 0.7735 -0.0829 0.0196  -0.0580 74  ARG B CZ    
2599 N NH1   . ARG B 74  ? 0.9592 0.9332 0.9557 -0.0817 0.0167  -0.0589 74  ARG B NH1   
2600 N NH2   . ARG B 74  ? 0.7819 0.7322 0.7813 -0.0873 0.0196  -0.0576 74  ARG B NH2   
2601 N N     . VAL B 75  ? 0.7056 0.5856 0.6642 -0.0733 0.0235  -0.0875 75  VAL B N     
2602 C CA    . VAL B 75  ? 0.7308 0.5932 0.6795 -0.0747 0.0246  -0.0936 75  VAL B CA    
2603 C C     . VAL B 75  ? 0.7441 0.5986 0.6890 -0.0823 0.0252  -0.0956 75  VAL B C     
2604 O O     . VAL B 75  ? 0.7245 0.5908 0.6718 -0.0856 0.0213  -0.0945 75  VAL B O     
2605 C CB    . VAL B 75  ? 0.6749 0.5414 0.6167 -0.0718 0.0195  -0.0989 75  VAL B CB    
2606 C CG1   . VAL B 75  ? 0.7595 0.6139 0.6909 -0.0759 0.0185  -0.1039 75  VAL B CG1   
2607 C CG2   . VAL B 75  ? 0.7148 0.5797 0.6571 -0.0660 0.0210  -0.0987 75  VAL B CG2   
2608 N N     . LEU B 76  ? 0.7933 0.6276 0.7318 -0.0856 0.0308  -0.0989 76  LEU B N     
2609 C CA    . LEU B 76  ? 0.7739 0.5974 0.7060 -0.0948 0.0326  -0.1025 76  LEU B CA    
2610 C C     . LEU B 76  ? 0.7510 0.5689 0.6684 -0.0994 0.0289  -0.1096 76  LEU B C     
2611 O O     . LEU B 76  ? 0.7218 0.5285 0.6324 -0.0972 0.0317  -0.1130 76  LEU B O     
2612 C CB    . LEU B 76  ? 0.7820 0.5854 0.7168 -0.0971 0.0433  -0.1017 76  LEU B CB    
2613 C CG    . LEU B 76  ? 0.8073 0.5959 0.7332 -0.1082 0.0467  -0.1075 76  LEU B CG    
2614 C CD1   . LEU B 76  ? 0.7644 0.5683 0.6927 -0.1139 0.0398  -0.1056 76  LEU B CD1   
2615 C CD2   . LEU B 76  ? 0.8116 0.5795 0.7434 -0.1094 0.0594  -0.1062 76  LEU B CD2   
2616 N N     . ASP B 77  ? 0.7206 0.5477 0.6339 -0.1062 0.0227  -0.1108 77  ASP B N     
2617 C CA    . ASP B 77  ? 0.7777 0.6054 0.6786 -0.1118 0.0175  -0.1151 77  ASP B CA    
2618 C C     . ASP B 77  ? 0.8526 0.6656 0.7421 -0.1248 0.0209  -0.1202 77  ASP B C     
2619 O O     . ASP B 77  ? 0.8223 0.6429 0.7111 -0.1331 0.0170  -0.1194 77  ASP B O     
2620 C CB    . ASP B 77  ? 0.7971 0.6480 0.7030 -0.1105 0.0082  -0.1112 77  ASP B CB    
2621 C CG    . ASP B 77  ? 0.9086 0.7644 0.8046 -0.1162 0.0019  -0.1126 77  ASP B CG    
2622 O OD1   . ASP B 77  ? 0.9426 0.7841 0.8262 -0.1208 0.0044  -0.1174 77  ASP B OD1   
2623 O OD2   . ASP B 77  ? 0.9088 0.7839 0.8102 -0.1161 -0.0052 -0.1081 77  ASP B OD2   
2624 N N     . LEU B 78  ? 0.8264 0.6179 0.7065 -0.1273 0.0288  -0.1258 78  LEU B N     
2625 C CA    . LEU B 78  ? 0.8604 0.6359 0.7261 -0.1413 0.0331  -0.1328 78  LEU B CA    
2626 C C     . LEU B 78  ? 0.8785 0.6662 0.7317 -0.1506 0.0234  -0.1345 78  LEU B C     
2627 O O     . LEU B 78  ? 0.9696 0.7642 0.8186 -0.1467 0.0186  -0.1338 78  LEU B O     
2628 C CB    . LEU B 78  ? 0.8722 0.6226 0.7296 -0.1414 0.0444  -0.1391 78  LEU B CB    
2629 C CG    . LEU B 78  ? 0.8668 0.5948 0.7266 -0.1456 0.0575  -0.1420 78  LEU B CG    
2630 C CD1   . LEU B 78  ? 0.8904 0.6263 0.7714 -0.1365 0.0590  -0.1329 78  LEU B CD1   
2631 C CD2   . LEU B 78  ? 0.8315 0.5362 0.6850 -0.1438 0.0695  -0.1473 78  LEU B CD2   
2632 N N     . GLY B 79  ? 0.8030 0.5945 0.6513 -0.1632 0.0204  -0.1356 79  GLY B N     
2633 C CA    . GLY B 79  ? 0.8331 0.6360 0.6685 -0.1746 0.0117  -0.1364 79  GLY B CA    
2634 C C     . GLY B 79  ? 0.9461 0.7767 0.7925 -0.1666 0.0004  -0.1273 79  GLY B C     
2635 O O     . GLY B 79  ? 1.0160 0.8531 0.8603 -0.1614 -0.0034 -0.1255 79  GLY B O     
2636 N N     . CYS B 80  ? 0.8858 0.7324 0.7452 -0.1646 -0.0039 -0.1212 80  CYS B N     
2637 C CA    . CYS B 80  ? 0.8757 0.7444 0.7494 -0.1524 -0.0106 -0.1133 80  CYS B CA    
2638 C C     . CYS B 80  ? 0.9466 0.8350 0.8180 -0.1564 -0.0203 -0.1079 80  CYS B C     
2639 O O     . CYS B 80  ? 1.0430 0.9472 0.9263 -0.1454 -0.0242 -0.1017 80  CYS B O     
2640 C CB    . CYS B 80  ? 0.8981 0.7789 0.7867 -0.1486 -0.0114 -0.1081 80  CYS B CB    
2641 S SG    . CYS B 80  ? 0.9786 0.8708 0.8634 -0.1647 -0.0175 -0.1057 80  CYS B SG    
2642 N N     . GLY B 81  ? 0.9542 0.8427 0.8114 -0.1723 -0.0238 -0.1097 81  GLY B N     
2643 C CA    . GLY B 81  ? 0.9429 0.8548 0.8003 -0.1777 -0.0340 -0.1018 81  GLY B CA    
2644 C C     . GLY B 81  ? 0.9584 0.8942 0.8326 -0.1750 -0.0399 -0.0924 81  GLY B C     
2645 O O     . GLY B 81  ? 0.9225 0.8565 0.8021 -0.1763 -0.0374 -0.0933 81  GLY B O     
2646 N N     . VAL B 82  ? 1.0116 0.9705 0.8955 -0.1706 -0.0472 -0.0824 82  VAL B N     
2647 C CA    . VAL B 82  ? 0.9426 0.9269 0.8432 -0.1684 -0.0528 -0.0720 82  VAL B CA    
2648 C C     . VAL B 82  ? 0.9133 0.9006 0.8320 -0.1495 -0.0483 -0.0702 82  VAL B C     
2649 O O     . VAL B 82  ? 0.8985 0.9063 0.8337 -0.1431 -0.0508 -0.0616 82  VAL B O     
2650 C CB    . VAL B 82  ? 0.9214 0.9298 0.8236 -0.1752 -0.0624 -0.0609 82  VAL B CB    
2651 C CG1   . VAL B 82  ? 0.9928 0.9989 0.8937 -0.1676 -0.0623 -0.0595 82  VAL B CG1   
2652 C CG2   . VAL B 82  ? 0.9811 1.0183 0.9039 -0.1709 -0.0676 -0.0477 82  VAL B CG2   
2653 N N     . GLY B 83  ? 0.8880 0.8547 0.8031 -0.1411 -0.0409 -0.0784 83  GLY B N     
2654 C CA    . GLY B 83  ? 0.8783 0.8443 0.8063 -0.1263 -0.0356 -0.0791 83  GLY B CA    
2655 C C     . GLY B 83  ? 0.8499 0.8154 0.7837 -0.1133 -0.0336 -0.0786 83  GLY B C     
2656 O O     . GLY B 83  ? 0.8029 0.7619 0.7423 -0.1030 -0.0281 -0.0821 83  GLY B O     
2657 N N     . THR B 84  ? 0.9088 0.8813 0.8415 -0.1141 -0.0380 -0.0738 84  THR B N     
2658 C CA    . THR B 84  ? 0.8991 0.8747 0.8421 -0.1009 -0.0362 -0.0712 84  THR B CA    
2659 C C     . THR B 84  ? 0.8717 0.8262 0.8083 -0.0940 -0.0298 -0.0798 84  THR B C     
2660 O O     . THR B 84  ? 0.8524 0.8065 0.7986 -0.0828 -0.0254 -0.0811 84  THR B O     
2661 C CB    . THR B 84  ? 0.8205 0.8101 0.7658 -0.1036 -0.0424 -0.0620 84  THR B CB    
2662 O OG1   . THR B 84  ? 0.9525 0.9282 0.8812 -0.1103 -0.0432 -0.0664 84  THR B OG1   
2663 C CG2   . THR B 84  ? 0.8108 0.8204 0.7587 -0.1145 -0.0495 -0.0536 84  THR B CG2   
2664 N N     . PRO B 85  ? 0.8585 0.7954 0.7793 -0.1003 -0.0285 -0.0860 85  PRO B N     
2665 C CA    . PRO B 85  ? 0.8271 0.7465 0.7447 -0.0926 -0.0224 -0.0924 85  PRO B CA    
2666 C C     . PRO B 85  ? 0.8113 0.7252 0.7340 -0.0874 -0.0169 -0.0964 85  PRO B C     
2667 O O     . PRO B 85  ? 0.8056 0.7141 0.7324 -0.0784 -0.0129 -0.0988 85  PRO B O     
2668 C CB    . PRO B 85  ? 0.8513 0.7543 0.7515 -0.1019 -0.0214 -0.0975 85  PRO B CB    
2669 C CG    . PRO B 85  ? 0.8860 0.7915 0.7794 -0.1147 -0.0238 -0.0978 85  PRO B CG    
2670 C CD    . PRO B 85  ? 0.8500 0.7800 0.7551 -0.1150 -0.0307 -0.0888 85  PRO B CD    
2671 N N     . GLY B 86  ? 0.8429 0.7592 0.7656 -0.0937 -0.0169 -0.0965 86  GLY B N     
2672 C CA    . GLY B 86  ? 0.7699 0.6827 0.6976 -0.0901 -0.0121 -0.0986 86  GLY B CA    
2673 C C     . GLY B 86  ? 0.7744 0.7032 0.7157 -0.0819 -0.0121 -0.0954 86  GLY B C     
2674 O O     . GLY B 86  ? 0.7764 0.7026 0.7213 -0.0752 -0.0079 -0.0977 86  GLY B O     
2675 N N     . VAL B 87  ? 0.8068 0.7530 0.7555 -0.0828 -0.0163 -0.0899 87  VAL B N     
2676 C CA    . VAL B 87  ? 0.7544 0.7153 0.7164 -0.0746 -0.0146 -0.0873 87  VAL B CA    
2677 C C     . VAL B 87  ? 0.7551 0.7113 0.7198 -0.0650 -0.0113 -0.0898 87  VAL B C     
2678 O O     . VAL B 87  ? 0.8106 0.7690 0.7808 -0.0586 -0.0067 -0.0924 87  VAL B O     
2679 C CB    . VAL B 87  ? 0.6990 0.6798 0.6705 -0.0765 -0.0191 -0.0795 87  VAL B CB    
2680 C CG1   . VAL B 87  ? 0.7192 0.7130 0.7050 -0.0664 -0.0154 -0.0772 87  VAL B CG1   
2681 C CG2   . VAL B 87  ? 0.7128 0.7000 0.6837 -0.0853 -0.0215 -0.0773 87  VAL B CG2   
2682 N N     . ARG B 88  ? 0.7424 0.6914 0.7021 -0.0652 -0.0133 -0.0895 88  ARG B N     
2683 C CA    . ARG B 88  ? 0.8041 0.7471 0.7662 -0.0568 -0.0102 -0.0915 88  ARG B CA    
2684 C C     . ARG B 88  ? 0.7710 0.7011 0.7282 -0.0537 -0.0051 -0.0985 88  ARG B C     
2685 O O     . ARG B 88  ? 0.7771 0.7087 0.7400 -0.0472 -0.0008 -0.1010 88  ARG B O     
2686 C CB    . ARG B 88  ? 0.7396 0.6767 0.6953 -0.0593 -0.0137 -0.0894 88  ARG B CB    
2687 C CG    . ARG B 88  ? 0.7348 0.6660 0.6941 -0.0511 -0.0109 -0.0903 88  ARG B CG    
2688 C CD    . ARG B 88  ? 0.7724 0.7001 0.7253 -0.0546 -0.0149 -0.0869 88  ARG B CD    
2689 N NE    . ARG B 88  ? 0.8053 0.7284 0.7633 -0.0468 -0.0125 -0.0862 88  ARG B NE    
2690 C CZ    . ARG B 88  ? 0.7601 0.6929 0.7330 -0.0394 -0.0111 -0.0808 88  ARG B CZ    
2691 N NH1   . ARG B 88  ? 0.7397 0.6886 0.7246 -0.0381 -0.0117 -0.0752 88  ARG B NH1   
2692 N NH2   . ARG B 88  ? 0.6653 0.5913 0.6424 -0.0329 -0.0083 -0.0806 88  ARG B NH2   
2693 N N     . ILE B 89  ? 0.7380 0.6559 0.6851 -0.0591 -0.0049 -0.1012 89  ILE B N     
2694 C CA    . ILE B 89  ? 0.7268 0.6347 0.6708 -0.0569 -0.0005 -0.1054 89  ILE B CA    
2695 C C     . ILE B 89  ? 0.7466 0.6646 0.6972 -0.0551 0.0021  -0.1057 89  ILE B C     
2696 O O     . ILE B 89  ? 0.7014 0.6177 0.6527 -0.0516 0.0055  -0.1084 89  ILE B O     
2697 C CB    . ILE B 89  ? 0.7150 0.6091 0.6497 -0.0629 0.0003  -0.1066 89  ILE B CB    
2698 C CG1   . ILE B 89  ? 0.6677 0.5525 0.5944 -0.0648 -0.0015 -0.1073 89  ILE B CG1   
2699 C CG2   . ILE B 89  ? 0.6573 0.5443 0.5919 -0.0607 0.0049  -0.1083 89  ILE B CG2   
2700 C CD1   . ILE B 89  ? 0.6766 0.5470 0.5933 -0.0710 0.0006  -0.1095 89  ILE B CD1   
2701 N N     . ALA B 90  ? 0.7408 0.6701 0.6957 -0.0584 0.0004  -0.1026 90  ALA B N     
2702 C CA    . ALA B 90  ? 0.7368 0.6774 0.6977 -0.0571 0.0029  -0.1025 90  ALA B CA    
2703 C C     . ALA B 90  ? 0.7606 0.7100 0.7282 -0.0506 0.0058  -0.1044 90  ALA B C     
2704 O O     . ALA B 90  ? 0.7615 0.7132 0.7293 -0.0486 0.0097  -0.1078 90  ALA B O     
2705 C CB    . ALA B 90  ? 0.7479 0.6985 0.7122 -0.0626 0.0005  -0.0982 90  ALA B CB    
2706 N N     . ARG B 91  ? 0.7480 0.7027 0.7213 -0.0477 0.0043  -0.1020 91  ARG B N     
2707 C CA    . ARG B 91  ? 0.7324 0.6939 0.7143 -0.0408 0.0089  -0.1035 91  ARG B CA    
2708 C C     . ARG B 91  ? 0.7643 0.7140 0.7429 -0.0365 0.0128  -0.1092 91  ARG B C     
2709 O O     . ARG B 91  ? 0.8211 0.7728 0.8022 -0.0332 0.0187  -0.1140 91  ARG B O     
2710 C CB    . ARG B 91  ? 0.7691 0.7389 0.7604 -0.0382 0.0066  -0.0972 91  ARG B CB    
2711 C CG    . ARG B 91  ? 0.7406 0.7129 0.7424 -0.0297 0.0128  -0.0981 91  ARG B CG    
2712 C CD    . ARG B 91  ? 0.7557 0.7385 0.7695 -0.0271 0.0104  -0.0891 91  ARG B CD    
2713 N NE    . ARG B 91  ? 0.7130 0.6918 0.7207 -0.0319 0.0028  -0.0843 91  ARG B NE    
2714 C CZ    . ARG B 91  ? 0.7134 0.6822 0.7189 -0.0294 0.0024  -0.0842 91  ARG B CZ    
2715 N NH1   . ARG B 91  ? 0.7211 0.6809 0.7295 -0.0225 0.0088  -0.0892 91  ARG B NH1   
2716 N NH2   . ARG B 91  ? 0.8617 0.8300 0.8618 -0.0348 -0.0045 -0.0791 91  ARG B NH2   
2717 N N     . LEU B 92  ? 0.7225 0.6598 0.6950 -0.0371 0.0101  -0.1091 92  LEU B N     
2718 C CA    . LEU B 92  ? 0.7373 0.6638 0.7076 -0.0331 0.0135  -0.1136 92  LEU B CA    
2719 C C     . LEU B 92  ? 0.7745 0.6952 0.7370 -0.0359 0.0154  -0.1182 92  LEU B C     
2720 O O     . LEU B 92  ? 0.9427 0.8618 0.9051 -0.0340 0.0200  -0.1233 92  LEU B O     
2721 C CB    . LEU B 92  ? 0.6484 0.5656 0.6160 -0.0325 0.0100  -0.1109 92  LEU B CB    
2722 C CG    . LEU B 92  ? 0.7383 0.6632 0.7165 -0.0284 0.0092  -0.1053 92  LEU B CG    
2723 C CD1   . LEU B 92  ? 0.7221 0.6411 0.6964 -0.0299 0.0046  -0.1010 92  LEU B CD1   
2724 C CD2   . LEU B 92  ? 0.6914 0.6163 0.6791 -0.0211 0.0162  -0.1082 92  LEU B CD2   
2725 N N     . SER B 93  ? 0.7416 0.6596 0.6983 -0.0409 0.0125  -0.1161 93  SER B N     
2726 C CA    . SER B 93  ? 0.7059 0.6196 0.6574 -0.0432 0.0142  -0.1179 93  SER B CA    
2727 C C     . SER B 93  ? 0.7298 0.6558 0.6829 -0.0464 0.0157  -0.1174 93  SER B C     
2728 O O     . SER B 93  ? 0.7420 0.6685 0.6922 -0.0486 0.0171  -0.1178 93  SER B O     
2729 C CB    . SER B 93  ? 0.7317 0.6348 0.6779 -0.0462 0.0121  -0.1149 93  SER B CB    
2730 O OG    . SER B 93  ? 0.6983 0.6060 0.6454 -0.0506 0.0109  -0.1112 93  SER B OG    
2731 N N     . GLY B 94  ? 0.7207 0.6582 0.6788 -0.0471 0.0152  -0.1155 94  GLY B N     
2732 C CA    . GLY B 94  ? 0.7347 0.6848 0.6942 -0.0508 0.0162  -0.1139 94  GLY B CA    
2733 C C     . GLY B 94  ? 0.7271 0.6755 0.6852 -0.0553 0.0143  -0.1085 94  GLY B C     
2734 O O     . GLY B 94  ? 0.7994 0.7592 0.7598 -0.0586 0.0148  -0.1053 94  GLY B O     
2735 N N     . ALA B 95  ? 0.6732 0.6079 0.6284 -0.0555 0.0128  -0.1069 95  ALA B N     
2736 C CA    . ALA B 95  ? 0.6685 0.5996 0.6245 -0.0593 0.0125  -0.1016 95  ALA B CA    
2737 C C     . ALA B 95  ? 0.6831 0.6207 0.6427 -0.0625 0.0107  -0.0987 95  ALA B C     
2738 O O     . ALA B 95  ? 0.7658 0.7084 0.7266 -0.0616 0.0088  -0.1003 95  ALA B O     
2739 C CB    . ALA B 95  ? 0.7279 0.6411 0.6792 -0.0590 0.0128  -0.1019 95  ALA B CB    
2740 N N     . HIS B 96  ? 0.7075 0.6458 0.6703 -0.0663 0.0116  -0.0932 96  HIS B N     
2741 C CA    . HIS B 96  ? 0.6568 0.5983 0.6229 -0.0707 0.0103  -0.0899 96  HIS B CA    
2742 C C     . HIS B 96  ? 0.6836 0.6075 0.6451 -0.0738 0.0105  -0.0908 96  HIS B C     
2743 O O     . HIS B 96  ? 0.6534 0.5638 0.6130 -0.0736 0.0139  -0.0903 96  HIS B O     
2744 C CB    . HIS B 96  ? 0.6557 0.6067 0.6289 -0.0736 0.0120  -0.0829 96  HIS B CB    
2745 C CG    . HIS B 96  ? 0.7343 0.6873 0.7115 -0.0785 0.0110  -0.0793 96  HIS B CG    
2746 N ND1   . HIS B 96  ? 0.8101 0.7809 0.7927 -0.0802 0.0094  -0.0764 96  HIS B ND1   
2747 C CD2   . HIS B 96  ? 0.7249 0.6641 0.7011 -0.0829 0.0120  -0.0786 96  HIS B CD2   
2748 C CE1   . HIS B 96  ? 0.8370 0.8053 0.8223 -0.0854 0.0086  -0.0733 96  HIS B CE1   
2749 N NE2   . HIS B 96  ? 0.7408 0.6894 0.7218 -0.0875 0.0104  -0.0750 96  HIS B NE2   
2750 N N     . VAL B 97  ? 0.7584 0.6832 0.7181 -0.0775 0.0075  -0.0918 97  VAL B N     
2751 C CA    . VAL B 97  ? 0.7745 0.6840 0.7268 -0.0825 0.0072  -0.0942 97  VAL B CA    
2752 C C     . VAL B 97  ? 0.7574 0.6685 0.7120 -0.0901 0.0068  -0.0914 97  VAL B C     
2753 O O     . VAL B 97  ? 0.6856 0.6116 0.6441 -0.0921 0.0029  -0.0893 97  VAL B O     
2754 C CB    . VAL B 97  ? 0.7154 0.6260 0.6622 -0.0816 0.0030  -0.0976 97  VAL B CB    
2755 C CG1   . VAL B 97  ? 0.7561 0.6560 0.6942 -0.0897 0.0015  -0.0994 97  VAL B CG1   
2756 C CG2   . VAL B 97  ? 0.7470 0.6516 0.6911 -0.0749 0.0044  -0.1006 97  VAL B CG2   
2757 N N     . THR B 98  ? 0.7509 0.6468 0.7046 -0.0942 0.0118  -0.0908 98  THR B N     
2758 C CA    . THR B 98  ? 0.7708 0.6612 0.7240 -0.1032 0.0127  -0.0901 98  THR B CA    
2759 C C     . THR B 98  ? 0.8048 0.6777 0.7448 -0.1096 0.0133  -0.0966 98  THR B C     
2760 O O     . THR B 98  ? 0.7885 0.6446 0.7232 -0.1079 0.0183  -0.0999 98  THR B O     
2761 C CB    . THR B 98  ? 0.7703 0.6536 0.7321 -0.1040 0.0194  -0.0850 98  THR B CB    
2762 O OG1   . THR B 98  ? 0.8988 0.7622 0.8576 -0.1023 0.0262  -0.0871 98  THR B OG1   
2763 C CG2   . THR B 98  ? 0.8163 0.7171 0.7899 -0.0978 0.0192  -0.0778 98  THR B CG2   
2764 N N     . GLY B 99  ? 0.7987 0.6773 0.7332 -0.1174 0.0080  -0.0980 99  GLY B N     
2765 C CA    . GLY B 99  ? 0.8378 0.7039 0.7582 -0.1255 0.0072  -0.1039 99  GLY B CA    
2766 C C     . GLY B 99  ? 0.8704 0.7283 0.7855 -0.1388 0.0087  -0.1058 99  GLY B C     
2767 O O     . GLY B 99  ? 0.8826 0.7516 0.8056 -0.1420 0.0066  -0.1014 99  GLY B O     
2768 N N     . ILE B 100 ? 0.8702 0.7083 0.7712 -0.1474 0.0128  -0.1129 100 ILE B N     
2769 C CA    . ILE B 100 ? 0.9442 0.7693 0.8371 -0.1619 0.0162  -0.1171 100 ILE B CA    
2770 C C     . ILE B 100 ? 0.9394 0.7622 0.8140 -0.1742 0.0118  -0.1229 100 ILE B C     
2771 O O     . ILE B 100 ? 0.9031 0.7226 0.7692 -0.1714 0.0111  -0.1259 100 ILE B O     
2772 C CB    . ILE B 100 ? 0.9177 0.7161 0.8116 -0.1622 0.0294  -0.1207 100 ILE B CB    
2773 C CG1   . ILE B 100 ? 0.8840 0.6623 0.7654 -0.1617 0.0359  -0.1281 100 ILE B CG1   
2774 C CG2   . ILE B 100 ? 0.7754 0.5791 0.6882 -0.1496 0.0330  -0.1128 100 ILE B CG2   
2775 C CD1   . ILE B 100 ? 0.8709 0.6242 0.7567 -0.1594 0.0501  -0.1302 100 ILE B CD1   
2776 N N     . SER B 101 ? 0.8752 0.7019 0.7439 -0.1887 0.0083  -0.1237 101 SER B N     
2777 C CA    . SER B 101 ? 0.9176 0.7422 0.7673 -0.2045 0.0045  -0.1292 101 SER B CA    
2778 C C     . SER B 101 ? 0.9535 0.7665 0.7963 -0.2213 0.0083  -0.1338 101 SER B C     
2779 O O     . SER B 101 ? 1.0174 0.8325 0.8731 -0.2197 0.0102  -0.1297 101 SER B O     
2780 C CB    . SER B 101 ? 0.9511 0.8053 0.8023 -0.2054 -0.0090 -0.1218 101 SER B CB    
2781 O OG    . SER B 101 ? 1.0030 0.8578 0.8356 -0.2219 -0.0134 -0.1255 101 SER B OG    
2782 N N     . VAL B 102 ? 0.9696 0.7719 0.7915 -0.2385 0.0090  -0.1421 102 VAL B N     
2783 C CA    . VAL B 102 ? 1.0147 0.8029 0.8269 -0.2574 0.0136  -0.1485 102 VAL B CA    
2784 C C     . VAL B 102 ? 1.0401 0.8539 0.8471 -0.2721 0.0002  -0.1436 102 VAL B C     
2785 O O     . VAL B 102 ? 1.0905 0.8977 0.8908 -0.2887 0.0018  -0.1474 102 VAL B O     
2786 C CB    . VAL B 102 ? 1.0233 0.7794 0.8145 -0.2692 0.0258  -0.1627 102 VAL B CB    
2787 C CG1   . VAL B 102 ? 1.0735 0.8044 0.8731 -0.2548 0.0403  -0.1659 102 VAL B CG1   
2788 C CG2   . VAL B 102 ? 1.1062 0.8687 0.8773 -0.2775 0.0197  -0.1665 102 VAL B CG2   
2789 N N     . SER B 103 ? 0.9809 0.8230 0.7923 -0.2662 -0.0120 -0.1346 103 SER B N     
2790 C CA    . SER B 103 ? 1.0483 0.9187 0.8588 -0.2782 -0.0250 -0.1268 103 SER B CA    
2791 C C     . SER B 103 ? 1.0359 0.9306 0.8704 -0.2665 -0.0311 -0.1144 103 SER B C     
2792 O O     . SER B 103 ? 0.9663 0.8712 0.8162 -0.2472 -0.0321 -0.1082 103 SER B O     
2793 C CB    . SER B 103 ? 1.0223 0.9110 0.8246 -0.2800 -0.0344 -0.1226 103 SER B CB    
2794 O OG    . SER B 103 ? 1.0316 0.9549 0.8450 -0.2814 -0.0474 -0.1092 103 SER B OG    
2795 N N     . HIS B 104 ? 1.0974 1.0021 0.9341 -0.2793 -0.0352 -0.1111 104 HIS B N     
2796 C CA    . HIS B 104 ? 0.9840 0.9132 0.8427 -0.2699 -0.0408 -0.0992 104 HIS B CA    
2797 C C     . HIS B 104 ? 0.9484 0.9095 0.8174 -0.2608 -0.0515 -0.0874 104 HIS B C     
2798 O O     . HIS B 104 ? 0.9607 0.9349 0.8485 -0.2430 -0.0518 -0.0803 104 HIS B O     
2799 C CB    . HIS B 104 ? 1.0113 0.9455 0.8689 -0.2875 -0.0436 -0.0977 104 HIS B CB    
2800 C CG    . HIS B 104 ? 0.9306 0.8895 0.8104 -0.2792 -0.0485 -0.0855 104 HIS B CG    
2801 N ND1   . HIS B 104 ? 0.9483 0.9415 0.8376 -0.2794 -0.0601 -0.0731 104 HIS B ND1   
2802 C CD2   . HIS B 104 ? 0.9404 0.8957 0.8354 -0.2703 -0.0430 -0.0832 104 HIS B CD2   
2803 C CE1   . HIS B 104 ? 0.9887 0.9973 0.8973 -0.2710 -0.0609 -0.0647 104 HIS B CE1   
2804 N NE2   . HIS B 104 ? 0.9430 0.9295 0.8546 -0.2658 -0.0511 -0.0707 104 HIS B NE2   
2805 N N     . GLU B 105 ? 1.0342 1.0087 0.8918 -0.2731 -0.0598 -0.0848 105 GLU B N     
2806 C CA    . GLU B 105 ? 1.0251 1.0312 0.8958 -0.2642 -0.0694 -0.0714 105 GLU B CA    
2807 C C     . GLU B 105 ? 0.9922 0.9936 0.8713 -0.2426 -0.0652 -0.0716 105 GLU B C     
2808 O O     . GLU B 105 ? 0.9760 0.9989 0.8736 -0.2285 -0.0687 -0.0613 105 GLU B O     
2809 C CB    . GLU B 105 ? 1.0452 1.0677 0.9024 -0.2821 -0.0792 -0.0670 105 GLU B CB    
2810 C CG    . GLU B 105 ? 1.0634 1.1006 0.9162 -0.3034 -0.0862 -0.0628 105 GLU B CG    
2811 C CD    . GLU B 105 ? 1.1306 1.1963 1.0084 -0.2950 -0.0916 -0.0485 105 GLU B CD    
2812 O OE1   . GLU B 105 ? 1.2044 1.2895 1.1002 -0.2777 -0.0943 -0.0379 105 GLU B OE1   
2813 O OE2   . GLU B 105 ? 1.0615 1.1288 0.9411 -0.3052 -0.0921 -0.0481 105 GLU B OE2   
2814 N N     . GLN B 106 ? 0.9716 0.9448 0.8383 -0.2397 -0.0568 -0.0832 106 GLN B N     
2815 C CA    . GLN B 106 ? 0.9383 0.9058 0.8130 -0.2198 -0.0524 -0.0837 106 GLN B CA    
2816 C C     . GLN B 106 ? 0.9423 0.9097 0.8352 -0.2040 -0.0472 -0.0819 106 GLN B C     
2817 O O     . GLN B 106 ? 0.9396 0.9259 0.8489 -0.1905 -0.0499 -0.0738 106 GLN B O     
2818 C CB    . GLN B 106 ? 0.9686 0.9070 0.8257 -0.2216 -0.0446 -0.0957 106 GLN B CB    
2819 C CG    . GLN B 106 ? 0.9889 0.9331 0.8319 -0.2300 -0.0502 -0.0951 106 GLN B CG    
2820 C CD    . GLN B 106 ? 0.9498 0.8668 0.7763 -0.2302 -0.0421 -0.1064 106 GLN B CD    
2821 O OE1   . GLN B 106 ? 1.0126 0.9045 0.8367 -0.2267 -0.0317 -0.1154 106 GLN B OE1   
2822 N NE2   . GLN B 106 ? 0.8981 0.8214 0.7144 -0.2343 -0.0466 -0.1048 106 GLN B NE2   
2823 N N     . VAL B 107 ? 0.8809 0.8287 0.7720 -0.2061 -0.0395 -0.0885 107 VAL B N     
2824 C CA    . VAL B 107 ? 0.8408 0.7888 0.7478 -0.1926 -0.0345 -0.0863 107 VAL B CA    
2825 C C     . VAL B 107 ? 0.8830 0.8601 0.8074 -0.1874 -0.0407 -0.0755 107 VAL B C     
2826 O O     . VAL B 107 ? 0.8918 0.8753 0.8299 -0.1742 -0.0377 -0.0725 107 VAL B O     
2827 C CB    . VAL B 107 ? 0.8568 0.7834 0.7609 -0.1992 -0.0264 -0.0922 107 VAL B CB    
2828 C CG1   . VAL B 107 ? 0.9941 0.9274 0.8956 -0.2156 -0.0304 -0.0902 107 VAL B CG1   
2829 C CG2   . VAL B 107 ? 0.8335 0.7606 0.7538 -0.1851 -0.0210 -0.0890 107 VAL B CG2   
2830 N N     . VAL B 108 ? 0.8212 0.8176 0.7454 -0.1981 -0.0490 -0.0690 108 VAL B N     
2831 C CA    . VAL B 108 ? 0.8023 0.8276 0.7445 -0.1918 -0.0541 -0.0577 108 VAL B CA    
2832 C C     . VAL B 108 ? 0.8358 0.8756 0.7865 -0.1788 -0.0566 -0.0521 108 VAL B C     
2833 O O     . VAL B 108 ? 0.8111 0.8610 0.7768 -0.1642 -0.0539 -0.0483 108 VAL B O     
2834 C CB    . VAL B 108 ? 0.7816 0.8241 0.7232 -0.2084 -0.0619 -0.0510 108 VAL B CB    
2835 C CG1   . VAL B 108 ? 0.7374 0.8106 0.6995 -0.2009 -0.0663 -0.0383 108 VAL B CG1   
2836 C CG2   . VAL B 108 ? 0.7940 0.8196 0.7285 -0.2205 -0.0579 -0.0572 108 VAL B CG2   
2837 N N     . ARG B 109 ? 0.8267 0.8670 0.7680 -0.1839 -0.0609 -0.0517 109 ARG B N     
2838 C CA    . ARG B 109 ? 0.7737 0.8284 0.7257 -0.1714 -0.0628 -0.0448 109 ARG B CA    
2839 C C     . ARG B 109 ? 0.8477 0.8885 0.8045 -0.1541 -0.0547 -0.0508 109 ARG B C     
2840 O O     . ARG B 109 ? 0.8732 0.9267 0.8446 -0.1407 -0.0536 -0.0454 109 ARG B O     
2841 C CB    . ARG B 109 ? 0.8398 0.8963 0.7802 -0.1799 -0.0685 -0.0430 109 ARG B CB    
2842 C CG    . ARG B 109 ? 0.8478 0.9211 0.7824 -0.1989 -0.0775 -0.0361 109 ARG B CG    
2843 C CD    . ARG B 109 ? 1.0281 1.1267 0.9684 -0.2013 -0.0860 -0.0230 109 ARG B CD    
2844 N NE    . ARG B 109 ? 1.2381 1.3425 1.1614 -0.2244 -0.0937 -0.0219 109 ARG B NE    
2845 C CZ    . ARG B 109 ? 1.2700 1.4041 1.1983 -0.2351 -0.1039 -0.0076 109 ARG B CZ    
2846 N NH1   . ARG B 109 ? 1.2936 1.4559 1.2464 -0.2236 -0.1074 0.0085  109 ARG B NH1   
2847 N NH2   . ARG B 109 ? 1.2275 1.3635 1.1360 -0.2584 -0.1102 -0.0093 109 ARG B NH2   
2848 N N     . ALA B 110 ? 0.8126 0.8281 0.7584 -0.1543 -0.0484 -0.0615 110 ALA B N     
2849 C CA    . ALA B 110 ? 0.8025 0.8048 0.7507 -0.1399 -0.0414 -0.0670 110 ALA B CA    
2850 C C     . ALA B 110 ? 0.8225 0.8309 0.7840 -0.1300 -0.0369 -0.0659 110 ALA B C     
2851 O O     . ALA B 110 ? 0.8216 0.8334 0.7915 -0.1171 -0.0336 -0.0658 110 ALA B O     
2852 C CB    . ALA B 110 ? 0.8306 0.8051 0.7630 -0.1441 -0.0362 -0.0772 110 ALA B CB    
2853 N N     . ASN B 111 ? 0.8083 0.8182 0.7715 -0.1366 -0.0365 -0.0652 111 ASN B N     
2854 C CA    . ASN B 111 ? 0.7390 0.7606 0.7157 -0.1286 -0.0334 -0.0620 111 ASN B CA    
2855 C C     . ASN B 111 ? 0.7647 0.8104 0.7554 -0.1212 -0.0359 -0.0542 111 ASN B C     
2856 O O     . ASN B 111 ? 0.8203 0.8735 0.8209 -0.1104 -0.0315 -0.0537 111 ASN B O     
2857 C CB    . ASN B 111 ? 0.7725 0.7959 0.7503 -0.1384 -0.0339 -0.0600 111 ASN B CB    
2858 C CG    . ASN B 111 ? 0.7863 0.7864 0.7564 -0.1417 -0.0280 -0.0665 111 ASN B CG    
2859 O OD1   . ASN B 111 ? 0.7092 0.6949 0.6759 -0.1344 -0.0230 -0.0716 111 ASN B OD1   
2860 N ND2   . ASN B 111 ? 0.9007 0.8979 0.8700 -0.1526 -0.0282 -0.0655 111 ASN B ND2   
2861 N N     . ALA B 112 ? 0.7660 0.8244 0.7579 -0.1271 -0.0424 -0.0477 112 ALA B N     
2862 C CA    . ALA B 112 ? 0.7309 0.8131 0.7387 -0.1200 -0.0443 -0.0382 112 ALA B CA    
2863 C C     . ALA B 112 ? 0.8014 0.8796 0.8134 -0.1067 -0.0401 -0.0401 112 ALA B C     
2864 O O     . ALA B 112 ? 0.8030 0.8920 0.8289 -0.0953 -0.0354 -0.0374 112 ALA B O     
2865 C CB    . ALA B 112 ? 0.6801 0.7778 0.6882 -0.1312 -0.0530 -0.0291 112 ALA B CB    
2866 N N     . LEU B 113 ? 0.7259 0.7886 0.7260 -0.1084 -0.0412 -0.0447 113 LEU B N     
2867 C CA    . LEU B 113 ? 0.7786 0.8352 0.7820 -0.0963 -0.0369 -0.0471 113 LEU B CA    
2868 C C     . LEU B 113 ? 0.8399 0.8878 0.8457 -0.0864 -0.0287 -0.0545 113 LEU B C     
2869 O O     . LEU B 113 ? 0.8163 0.8715 0.8337 -0.0755 -0.0239 -0.0533 113 LEU B O     
2870 C CB    . LEU B 113 ? 0.7238 0.7632 0.7120 -0.1009 -0.0390 -0.0519 113 LEU B CB    
2871 C CG    . LEU B 113 ? 0.7507 0.7861 0.7438 -0.0893 -0.0356 -0.0523 113 LEU B CG    
2872 C CD1   . LEU B 113 ? 0.7903 0.8474 0.8032 -0.0813 -0.0355 -0.0418 113 LEU B CD1   
2873 C CD2   . LEU B 113 ? 0.7158 0.7408 0.6963 -0.0949 -0.0392 -0.0536 113 LEU B CD2   
2874 N N     . ALA B 114 ? 0.7833 0.8165 0.7788 -0.0906 -0.0267 -0.0616 114 ALA B N     
2875 C CA    . ALA B 114 ? 0.7066 0.7357 0.7043 -0.0836 -0.0201 -0.0667 114 ALA B CA    
2876 C C     . ALA B 114 ? 0.7812 0.8302 0.7929 -0.0788 -0.0176 -0.0620 114 ALA B C     
2877 O O     . ALA B 114 ? 0.8151 0.8665 0.8325 -0.0695 -0.0116 -0.0647 114 ALA B O     
2878 C CB    . ALA B 114 ? 0.6889 0.7049 0.6775 -0.0905 -0.0191 -0.0708 114 ALA B CB    
2879 N N     . GLU B 115 ? 0.8135 0.8769 0.8305 -0.0855 -0.0218 -0.0552 115 GLU B N     
2880 C CA    . GLU B 115 ? 0.7806 0.8639 0.8112 -0.0815 -0.0191 -0.0501 115 GLU B CA    
2881 C C     . GLU B 115 ? 0.8053 0.9005 0.8491 -0.0714 -0.0158 -0.0461 115 GLU B C     
2882 O O     . GLU B 115 ? 0.7798 0.8835 0.8326 -0.0636 -0.0089 -0.0469 115 GLU B O     
2883 C CB    . GLU B 115 ? 0.7590 0.8556 0.7930 -0.0916 -0.0249 -0.0426 115 GLU B CB    
2884 C CG    . GLU B 115 ? 0.8018 0.9097 0.8424 -0.0917 -0.0218 -0.0409 115 GLU B CG    
2885 C CD    . GLU B 115 ? 0.9175 1.0450 0.9734 -0.0823 -0.0169 -0.0365 115 GLU B CD    
2886 O OE1   . GLU B 115 ? 0.9461 1.0815 1.0103 -0.0777 -0.0175 -0.0315 115 GLU B OE1   
2887 O OE2   . GLU B 115 ? 0.9473 1.0824 1.0072 -0.0795 -0.0118 -0.0375 115 GLU B OE2   
2888 N N     . GLU B 116 ? 0.8644 0.9606 0.9098 -0.0717 -0.0200 -0.0414 116 GLU B N     
2889 C CA    . GLU B 116 ? 0.8862 0.9936 0.9471 -0.0615 -0.0161 -0.0357 116 GLU B CA    
2890 C C     . GLU B 116 ? 0.8839 0.9761 0.9428 -0.0514 -0.0085 -0.0443 116 GLU B C     
2891 O O     . GLU B 116 ? 0.9117 1.0102 0.9841 -0.0414 -0.0015 -0.0423 116 GLU B O     
2892 C CB    . GLU B 116 ? 0.8775 0.9953 0.9434 -0.0658 -0.0238 -0.0249 116 GLU B CB    
2893 C CG    . GLU B 116 ? 0.9560 1.0969 1.0446 -0.0584 -0.0213 -0.0127 116 GLU B CG    
2894 C CD    . GLU B 116 ? 1.0561 1.1926 1.1551 -0.0455 -0.0139 -0.0126 116 GLU B CD    
2895 O OE1   . GLU B 116 ? 1.0477 1.1698 1.1373 -0.0461 -0.0163 -0.0160 116 GLU B OE1   
2896 O OE2   . GLU B 116 ? 1.0617 1.2080 1.1780 -0.0351 -0.0051 -0.0095 116 GLU B OE2   
2897 N N     . ALA B 117 ? 0.8199 0.8921 0.8630 -0.0540 -0.0087 -0.0537 117 ALA B N     
2898 C CA    . ALA B 117 ? 0.7998 0.8582 0.8401 -0.0458 -0.0015 -0.0622 117 ALA B CA    
2899 C C     . ALA B 117 ? 0.7238 0.7820 0.7624 -0.0435 0.0054  -0.0693 117 ALA B C     
2900 O O     . ALA B 117 ? 0.6878 0.7352 0.7222 -0.0387 0.0114  -0.0774 117 ALA B O     
2901 C CB    . ALA B 117 ? 0.6960 0.7343 0.7211 -0.0494 -0.0049 -0.0679 117 ALA B CB    
2902 N N     . GLY B 118 ? 0.7614 0.8326 0.8032 -0.0476 0.0046  -0.0662 118 GLY B N     
2903 C CA    . GLY B 118 ? 0.7540 0.8273 0.7932 -0.0470 0.0104  -0.0719 118 GLY B CA    
2904 C C     . GLY B 118 ? 0.7547 0.8129 0.7796 -0.0514 0.0093  -0.0785 118 GLY B C     
2905 O O     . GLY B 118 ? 0.8270 0.8842 0.8479 -0.0501 0.0146  -0.0843 118 GLY B O     
2906 N N     . LEU B 119 ? 0.7019 0.7492 0.7190 -0.0573 0.0027  -0.0772 119 LEU B N     
2907 C CA    . LEU B 119 ? 0.7047 0.7364 0.7101 -0.0605 0.0024  -0.0822 119 LEU B CA    
2908 C C     . LEU B 119 ? 0.7429 0.7728 0.7445 -0.0694 -0.0021 -0.0786 119 LEU B C     
2909 O O     . LEU B 119 ? 0.7664 0.7809 0.7596 -0.0731 -0.0034 -0.0807 119 LEU B O     
2910 C CB    . LEU B 119 ? 0.6353 0.6506 0.6343 -0.0580 0.0017  -0.0859 119 LEU B CB    
2911 C CG    . LEU B 119 ? 0.6355 0.6497 0.6384 -0.0494 0.0071  -0.0899 119 LEU B CG    
2912 C CD1   . LEU B 119 ? 0.6932 0.6929 0.6909 -0.0479 0.0051  -0.0915 119 LEU B CD1   
2913 C CD2   . LEU B 119 ? 0.6746 0.6877 0.6740 -0.0476 0.0131  -0.0963 119 LEU B CD2   
2914 N N     . ALA B 120 ? 0.7055 0.7505 0.7141 -0.0730 -0.0036 -0.0730 120 ALA B N     
2915 C CA    . ALA B 120 ? 0.7028 0.7453 0.7089 -0.0821 -0.0073 -0.0695 120 ALA B CA    
2916 C C     . ALA B 120 ? 0.7991 0.8345 0.8014 -0.0838 -0.0043 -0.0710 120 ALA B C     
2917 O O     . ALA B 120 ? 0.7974 0.8238 0.7969 -0.0904 -0.0057 -0.0692 120 ALA B O     
2918 C CB    . ALA B 120 ? 0.6923 0.7539 0.7077 -0.0856 -0.0095 -0.0626 120 ALA B CB    
2919 N N     . ASP B 121 ? 0.8820 0.9209 0.8844 -0.0783 0.0002  -0.0740 121 ASP B N     
2920 C CA    . ASP B 121 ? 0.8806 0.9171 0.8812 -0.0804 0.0025  -0.0730 121 ASP B CA    
2921 C C     . ASP B 121 ? 0.8436 0.8614 0.8366 -0.0788 0.0035  -0.0772 121 ASP B C     
2922 O O     . ASP B 121 ? 0.8591 0.8706 0.8513 -0.0814 0.0047  -0.0746 121 ASP B O     
2923 C CB    . ASP B 121 ? 0.9236 0.9770 0.9273 -0.0779 0.0063  -0.0732 121 ASP B CB    
2924 C CG    . ASP B 121 ? 1.0000 1.0707 1.0110 -0.0765 0.0069  -0.0714 121 ASP B CG    
2925 O OD1   . ASP B 121 ? 1.0017 1.0728 1.0142 -0.0712 0.0083  -0.0750 121 ASP B OD1   
2926 O OD2   . ASP B 121 ? 0.9975 1.0814 1.0139 -0.0804 0.0062  -0.0656 121 ASP B OD2   
2927 N N     . ARG B 122 ? 0.8100 0.8200 0.7991 -0.0745 0.0033  -0.0822 122 ARG B N     
2928 C CA    . ARG B 122 ? 0.7895 0.7830 0.7716 -0.0723 0.0044  -0.0863 122 ARG B CA    
2929 C C     . ARG B 122 ? 0.7377 0.7150 0.7146 -0.0756 0.0019  -0.0867 122 ARG B C     
2930 O O     . ARG B 122 ? 0.6999 0.6623 0.6712 -0.0749 0.0034  -0.0891 122 ARG B O     
2931 C CB    . ARG B 122 ? 0.7159 0.7099 0.6967 -0.0657 0.0066  -0.0918 122 ARG B CB    
2932 C CG    . ARG B 122 ? 0.7026 0.6820 0.6768 -0.0634 0.0081  -0.0959 122 ARG B CG    
2933 C CD    . ARG B 122 ? 0.7018 0.6796 0.6756 -0.0575 0.0101  -0.1012 122 ARG B CD    
2934 N NE    . ARG B 122 ? 0.8024 0.7943 0.7806 -0.0551 0.0139  -0.1033 122 ARG B NE    
2935 C CZ    . ARG B 122 ? 0.8100 0.8009 0.7890 -0.0500 0.0181  -0.1087 122 ARG B CZ    
2936 N NH1   . ARG B 122 ? 0.7687 0.7464 0.7451 -0.0466 0.0180  -0.1115 122 ARG B NH1   
2937 N NH2   . ARG B 122 ? 0.7357 0.7385 0.7183 -0.0486 0.0232  -0.1114 122 ARG B NH2   
2938 N N     . ALA B 123 ? 0.7890 0.7696 0.7671 -0.0799 -0.0017 -0.0845 123 ALA B N     
2939 C CA    . ALA B 123 ? 0.7264 0.6932 0.6973 -0.0850 -0.0043 -0.0857 123 ALA B CA    
2940 C C     . ALA B 123 ? 0.7612 0.7327 0.7338 -0.0937 -0.0071 -0.0818 123 ALA B C     
2941 O O     . ALA B 123 ? 0.7680 0.7532 0.7447 -0.0954 -0.0110 -0.0787 123 ALA B O     
2942 C CB    . ALA B 123 ? 0.7061 0.6732 0.6748 -0.0819 -0.0070 -0.0874 123 ALA B CB    
2943 N N     . ARG B 124 ? 0.7879 0.7480 0.7583 -0.0993 -0.0047 -0.0814 124 ARG B N     
2944 C CA    . ARG B 124 ? 0.8204 0.7807 0.7915 -0.1089 -0.0062 -0.0786 124 ARG B CA    
2945 C C     . ARG B 124 ? 0.8154 0.7555 0.7752 -0.1171 -0.0057 -0.0831 124 ARG B C     
2946 O O     . ARG B 124 ? 0.8082 0.7302 0.7624 -0.1154 -0.0010 -0.0869 124 ARG B O     
2947 C CB    . ARG B 124 ? 0.7354 0.6980 0.7143 -0.1097 -0.0025 -0.0741 124 ARG B CB    
2948 C CG    . ARG B 124 ? 0.7929 0.7777 0.7813 -0.1043 -0.0033 -0.0698 124 ARG B CG    
2949 C CD    . ARG B 124 ? 0.7519 0.7391 0.7468 -0.1030 0.0009  -0.0653 124 ARG B CD    
2950 N NE    . ARG B 124 ? 0.7568 0.7666 0.7594 -0.1004 0.0002  -0.0611 124 ARG B NE    
2951 C CZ    . ARG B 124 ? 0.8380 0.8563 0.8470 -0.1001 0.0028  -0.0555 124 ARG B CZ    
2952 N NH1   . ARG B 124 ? 0.7288 0.7354 0.7395 -0.1012 0.0062  -0.0523 124 ARG B NH1   
2953 N NH2   . ARG B 124 ? 0.8680 0.9076 0.8824 -0.0988 0.0023  -0.0523 124 ARG B NH2   
2954 N N     . PHE B 125 ? 0.8410 0.7847 0.7970 -0.1267 -0.0101 -0.0825 125 PHE B N     
2955 C CA    . PHE B 125 ? 0.7770 0.7032 0.7198 -0.1371 -0.0099 -0.0876 125 PHE B CA    
2956 C C     . PHE B 125 ? 0.8027 0.7238 0.7448 -0.1492 -0.0087 -0.0870 125 PHE B C     
2957 O O     . PHE B 125 ? 0.8587 0.7969 0.8080 -0.1527 -0.0131 -0.0815 125 PHE B O     
2958 C CB    . PHE B 125 ? 0.7212 0.6567 0.6577 -0.1398 -0.0168 -0.0876 125 PHE B CB    
2959 C CG    . PHE B 125 ? 0.7990 0.7366 0.7366 -0.1285 -0.0169 -0.0884 125 PHE B CG    
2960 C CD1   . PHE B 125 ? 0.8305 0.7493 0.7583 -0.1269 -0.0132 -0.0942 125 PHE B CD1   
2961 C CD2   . PHE B 125 ? 0.8108 0.7679 0.7594 -0.1193 -0.0197 -0.0836 125 PHE B CD2   
2962 C CE1   . PHE B 125 ? 0.8386 0.7583 0.7674 -0.1169 -0.0132 -0.0949 125 PHE B CE1   
2963 C CE2   . PHE B 125 ? 0.8498 0.8067 0.7997 -0.1092 -0.0188 -0.0850 125 PHE B CE2   
2964 C CZ    . PHE B 125 ? 0.8771 0.8154 0.8170 -0.1082 -0.0160 -0.0904 125 PHE B CZ    
2965 N N     . GLN B 126 ? 0.8106 0.7074 0.7446 -0.1554 -0.0019 -0.0925 126 GLN B N     
2966 C CA    . GLN B 126 ? 0.8801 0.7670 0.8148 -0.1661 0.0020  -0.0927 126 GLN B CA    
2967 C C     . GLN B 126 ? 0.8990 0.7620 0.8171 -0.1787 0.0063  -0.1016 126 GLN B C     
2968 O O     . GLN B 126 ? 0.9327 0.7842 0.8403 -0.1770 0.0082  -0.1073 126 GLN B O     
2969 C CB    . GLN B 126 ? 0.8528 0.7324 0.7999 -0.1592 0.0100  -0.0888 126 GLN B CB    
2970 C CG    . GLN B 126 ? 0.7786 0.6305 0.7214 -0.1585 0.0205  -0.0939 126 GLN B CG    
2971 C CD    . GLN B 126 ? 0.8353 0.6838 0.7939 -0.1516 0.0280  -0.0870 126 GLN B CD    
2972 O OE1   . GLN B 126 ? 0.8450 0.7104 0.8141 -0.1415 0.0256  -0.0803 126 GLN B OE1   
2973 N NE2   . GLN B 126 ? 0.9304 0.7572 0.8908 -0.1577 0.0376  -0.0882 126 GLN B NE2   
2974 N N     . ARG B 127 ? 0.8853 0.7403 0.8005 -0.1922 0.0083  -0.1032 127 ARG B N     
2975 C CA    . ARG B 127 ? 0.8946 0.7260 0.7922 -0.2068 0.0134  -0.1131 127 ARG B CA    
2976 C C     . ARG B 127 ? 0.9068 0.7090 0.8068 -0.2041 0.0278  -0.1173 127 ARG B C     
2977 O O     . ARG B 127 ? 0.9359 0.7355 0.8503 -0.2013 0.0330  -0.1121 127 ARG B O     
2978 C CB    . ARG B 127 ? 0.8767 0.7129 0.7689 -0.2244 0.0091  -0.1135 127 ARG B CB    
2979 C CG    . ARG B 127 ? 0.9265 0.7487 0.7960 -0.2418 0.0094  -0.1236 127 ARG B CG    
2980 C CD    . ARG B 127 ? 1.0339 0.8612 0.8980 -0.2609 0.0052  -0.1239 127 ARG B CD    
2981 N NE    . ARG B 127 ? 1.0975 0.9216 0.9387 -0.2788 0.0013  -0.1315 127 ARG B NE    
2982 C CZ    . ARG B 127 ? 1.2318 1.0660 1.0643 -0.2980 -0.0055 -0.1314 127 ARG B CZ    
2983 N NH1   . ARG B 127 ? 1.1923 1.0379 1.0370 -0.3018 -0.0085 -0.1247 127 ARG B NH1   
2984 N NH2   . ARG B 127 ? 1.2560 1.0902 1.0666 -0.3144 -0.0098 -0.1375 127 ARG B NH2   
2985 N N     . ALA B 128 ? 0.8634 0.6451 0.7510 -0.2043 0.0344  -0.1256 128 ALA B N     
2986 C CA    . ALA B 128 ? 0.9317 0.6843 0.8217 -0.2017 0.0496  -0.1297 128 ALA B CA    
2987 C C     . ALA B 128 ? 1.0305 0.7614 0.9007 -0.2077 0.0557  -0.1411 128 ALA B C     
2988 O O     . ALA B 128 ? 1.0034 0.7448 0.8608 -0.2096 0.0473  -0.1439 128 ALA B O     
2989 C CB    . ALA B 128 ? 0.8891 0.6466 0.7981 -0.1834 0.0531  -0.1209 128 ALA B CB    
2990 N N     . ASP B 129 ? 1.0326 0.7331 0.9014 -0.2106 0.0712  -0.1473 129 ASP B N     
2991 C CA    . ASP B 129 ? 1.0690 0.7454 0.9179 -0.2184 0.0798  -0.1597 129 ASP B CA    
2992 C C     . ASP B 129 ? 1.1098 0.7762 0.9664 -0.2026 0.0881  -0.1578 129 ASP B C     
2993 O O     . ASP B 129 ? 1.1124 0.7681 0.9866 -0.1934 0.0986  -0.1522 129 ASP B O     
2994 C CB    . ASP B 129 ? 1.1724 0.8190 1.0125 -0.2342 0.0935  -0.1696 129 ASP B CB    
2995 C CG    . ASP B 129 ? 1.1270 0.7540 0.9394 -0.2491 0.0990  -0.1846 129 ASP B CG    
2996 O OD1   . ASP B 129 ? 1.1436 0.7657 0.9495 -0.2420 0.1016  -0.1875 129 ASP B OD1   
2997 O OD2   . ASP B 129 ? 1.2155 0.8328 1.0121 -0.2689 0.1005  -0.1935 129 ASP B OD2   
2998 N N     . ALA B 130 ? 1.1030 0.7732 0.9468 -0.2001 0.0837  -0.1615 130 ALA B N     
2999 C CA    . ALA B 130 ? 1.0361 0.6991 0.8872 -0.1854 0.0905  -0.1591 130 ALA B CA    
3000 C C     . ALA B 130 ? 1.0975 0.7277 0.9513 -0.1858 0.1103  -0.1641 130 ALA B C     
3001 O O     . ALA B 130 ? 1.1081 0.7328 0.9767 -0.1720 0.1181  -0.1579 130 ALA B O     
3002 C CB    . ALA B 130 ? 0.9826 0.6524 0.8176 -0.1853 0.0835  -0.1635 130 ALA B CB    
3003 N N     . MET B 131 ? 1.0523 0.6604 0.8927 -0.2019 0.1194  -0.1747 131 MET B N     
3004 C CA    . MET B 131 ? 1.1696 0.7440 1.0140 -0.2031 0.1405  -0.1798 131 MET B CA    
3005 C C     . MET B 131 ? 1.1203 0.6925 0.9914 -0.1956 0.1473  -0.1690 131 MET B C     
3006 O O     . MET B 131 ? 1.0991 0.6447 0.9797 -0.1938 0.1657  -0.1700 131 MET B O     
3007 C CB    . MET B 131 ? 1.1771 0.7284 0.9968 -0.2246 0.1482  -0.1960 131 MET B CB    
3008 C CG    . MET B 131 ? 1.1882 0.7460 0.9808 -0.2340 0.1397  -0.2052 131 MET B CG    
3009 S SD    . MET B 131 ? 1.2153 0.7357 0.9897 -0.2398 0.1608  -0.2204 131 MET B SD    
3010 C CE    . MET B 131 ? 1.2068 0.6980 0.9699 -0.2616 0.1749  -0.2334 131 MET B CE    
3011 N N     . ASP B 132 ? 1.1133 0.7130 0.9970 -0.1915 0.1334  -0.1582 132 ASP B N     
3012 C CA    . ASP B 132 ? 1.1006 0.7038 1.0105 -0.1841 0.1377  -0.1458 132 ASP B CA    
3013 C C     . ASP B 132 ? 1.0959 0.7362 1.0169 -0.1744 0.1199  -0.1336 132 ASP B C     
3014 O O     . ASP B 132 ? 1.0778 0.7358 0.9936 -0.1821 0.1077  -0.1335 132 ASP B O     
3015 C CB    . ASP B 132 ? 1.1523 0.7406 1.0603 -0.1990 0.1438  -0.1506 132 ASP B CB    
3016 C CG    . ASP B 132 ? 1.2101 0.7967 1.1463 -0.1918 0.1518  -0.1376 132 ASP B CG    
3017 O OD1   . ASP B 132 ? 1.1641 0.7631 1.1214 -0.1754 0.1520  -0.1239 132 ASP B OD1   
3018 O OD2   . ASP B 132 ? 1.1566 0.7299 1.0938 -0.2035 0.1578  -0.1406 132 ASP B OD2   
3019 N N     . LEU B 133 ? 1.0911 0.7428 1.0272 -0.1584 0.1193  -0.1234 133 LEU B N     
3020 C CA    . LEU B 133 ? 0.9295 0.6145 0.8738 -0.1490 0.1040  -0.1135 133 LEU B CA    
3021 C C     . LEU B 133 ? 0.9334 0.6317 0.9008 -0.1441 0.1040  -0.0999 133 LEU B C     
3022 O O     . LEU B 133 ? 0.9357 0.6271 0.9214 -0.1359 0.1143  -0.0907 133 LEU B O     
3023 C CB    . LEU B 133 ? 0.9304 0.6210 0.8770 -0.1362 0.1031  -0.1104 133 LEU B CB    
3024 C CG    . LEU B 133 ? 0.9087 0.5967 0.8350 -0.1375 0.0986  -0.1203 133 LEU B CG    
3025 C CD1   . LEU B 133 ? 0.8553 0.5593 0.7883 -0.1240 0.0931  -0.1136 133 LEU B CD1   
3026 C CD2   . LEU B 133 ? 0.9223 0.6228 0.8318 -0.1481 0.0859  -0.1271 133 LEU B CD2   
3027 N N     . PRO B 134 ? 0.8942 0.6135 0.8629 -0.1485 0.0928  -0.0967 134 PRO B N     
3028 C CA    . PRO B 134 ? 0.8749 0.6064 0.8649 -0.1456 0.0934  -0.0837 134 PRO B CA    
3029 C C     . PRO B 134 ? 0.8576 0.6168 0.8619 -0.1328 0.0861  -0.0711 134 PRO B C     
3030 O O     . PRO B 134 ? 0.8629 0.6472 0.8719 -0.1324 0.0760  -0.0653 134 PRO B O     
3031 C CB    . PRO B 134 ? 0.8243 0.5652 0.8065 -0.1576 0.0848  -0.0874 134 PRO B CB    
3032 C CG    . PRO B 134 ? 0.8307 0.5805 0.7926 -0.1612 0.0739  -0.0968 134 PRO B CG    
3033 C CD    . PRO B 134 ? 0.8607 0.5914 0.8117 -0.1582 0.0806  -0.1046 134 PRO B CD    
3034 N N     . PHE B 135 ? 0.8101 0.5650 0.8218 -0.1229 0.0921  -0.0665 135 PHE B N     
3035 C CA    . PHE B 135 ? 0.8476 0.6275 0.8684 -0.1124 0.0850  -0.0567 135 PHE B CA    
3036 C C     . PHE B 135 ? 0.8859 0.6606 0.9255 -0.1040 0.0955  -0.0448 135 PHE B C     
3037 O O     . PHE B 135 ? 0.9061 0.6564 0.9450 -0.1028 0.1069  -0.0484 135 PHE B O     
3038 C CB    . PHE B 135 ? 0.8395 0.6249 0.8441 -0.1093 0.0772  -0.0653 135 PHE B CB    
3039 C CG    . PHE B 135 ? 0.8186 0.6103 0.8059 -0.1167 0.0671  -0.0754 135 PHE B CG    
3040 C CD1   . PHE B 135 ? 0.8558 0.6680 0.8463 -0.1199 0.0586  -0.0720 135 PHE B CD1   
3041 C CD2   . PHE B 135 ? 0.8578 0.6372 0.8269 -0.1202 0.0660  -0.0871 135 PHE B CD2   
3042 C CE1   . PHE B 135 ? 0.8839 0.7040 0.8612 -0.1262 0.0495  -0.0793 135 PHE B CE1   
3043 C CE2   . PHE B 135 ? 0.8449 0.6330 0.8002 -0.1270 0.0563  -0.0940 135 PHE B CE2   
3044 C CZ    . PHE B 135 ? 0.8429 0.6514 0.8030 -0.1297 0.0482  -0.0898 135 PHE B CZ    
3045 N N     . GLU B 136 ? 0.8736 0.6726 0.9299 -0.0982 0.0916  -0.0302 136 GLU B N     
3046 C CA    . GLU B 136 ? 0.8488 0.6483 0.9252 -0.0904 0.1001  -0.0158 136 GLU B CA    
3047 C C     . GLU B 136 ? 0.8377 0.6245 0.9071 -0.0849 0.1043  -0.0209 136 GLU B C     
3048 O O     . GLU B 136 ? 0.8477 0.6351 0.8982 -0.0856 0.0970  -0.0328 136 GLU B O     
3049 C CB    . GLU B 136 ? 0.8904 0.7241 0.9797 -0.0862 0.0916  -0.0010 136 GLU B CB    
3050 C CG    . GLU B 136 ? 0.8472 0.6939 0.9532 -0.0893 0.0919  0.0114  136 GLU B CG    
3051 C CD    . GLU B 136 ? 0.8951 0.7210 1.0206 -0.0885 0.1071  0.0207  136 GLU B CD    
3052 O OE1   . GLU B 136 ? 1.0099 0.8227 1.1433 -0.0825 0.1165  0.0248  136 GLU B OE1   
3053 O OE2   . GLU B 136 ? 0.9026 0.7245 1.0363 -0.0937 0.1103  0.0241  136 GLU B OE2   
3054 N N     . ASP B 137 ? 0.8611 0.6360 0.9470 -0.0792 0.1168  -0.0113 137 ASP B N     
3055 C CA    . ASP B 137 ? 0.7900 0.5567 0.8716 -0.0732 0.1204  -0.0138 137 ASP B CA    
3056 C C     . ASP B 137 ? 0.8732 0.6691 0.9522 -0.0691 0.1072  -0.0093 137 ASP B C     
3057 O O     . ASP B 137 ? 0.9211 0.7432 1.0089 -0.0691 0.0995  0.0010  137 ASP B O     
3058 C CB    . ASP B 137 ? 0.7668 0.5201 0.8708 -0.0667 0.1363  -0.0010 137 ASP B CB    
3059 C CG    . ASP B 137 ? 0.9154 0.6338 1.0208 -0.0707 0.1527  -0.0079 137 ASP B CG    
3060 O OD1   . ASP B 137 ? 0.9208 0.6250 1.0070 -0.0797 0.1510  -0.0238 137 ASP B OD1   
3061 O OD2   . ASP B 137 ? 1.0661 0.7710 1.1924 -0.0653 0.1681  0.0030  137 ASP B OD2   
3062 N N     . GLU B 138 ? 0.8281 0.6193 0.8937 -0.0664 0.1049  -0.0177 138 GLU B N     
3063 C CA    . GLU B 138 ? 0.8130 0.6281 0.8762 -0.0626 0.0945  -0.0140 138 GLU B CA    
3064 C C     . GLU B 138 ? 0.8511 0.6906 0.9074 -0.0664 0.0811  -0.0159 138 GLU B C     
3065 O O     . GLU B 138 ? 1.0103 0.8749 1.0770 -0.0654 0.0760  -0.0043 138 GLU B O     
3066 C CB    . GLU B 138 ? 0.8112 0.6394 0.8963 -0.0564 0.0989  0.0048  138 GLU B CB    
3067 C CG    . GLU B 138 ? 0.8374 0.6474 0.9275 -0.0507 0.1097  0.0066  138 GLU B CG    
3068 C CD    . GLU B 138 ? 0.8567 0.6816 0.9714 -0.0448 0.1144  0.0278  138 GLU B CD    
3069 O OE1   . GLU B 138 ? 0.8592 0.7138 0.9815 -0.0456 0.1053  0.0394  138 GLU B OE1   
3070 O OE2   . GLU B 138 ? 0.9091 0.7164 1.0359 -0.0399 0.1277  0.0333  138 GLU B OE2   
3071 N N     . SER B 139 ? 0.8398 0.6728 0.8787 -0.0713 0.0759  -0.0303 139 SER B N     
3072 C CA    . SER B 139 ? 0.8232 0.6780 0.8558 -0.0743 0.0645  -0.0329 139 SER B CA    
3073 C C     . SER B 139 ? 0.7835 0.6390 0.7973 -0.0745 0.0566  -0.0462 139 SER B C     
3074 O O     . SER B 139 ? 0.7699 0.6392 0.7774 -0.0771 0.0486  -0.0505 139 SER B O     
3075 C CB    . SER B 139 ? 0.8525 0.7057 0.8876 -0.0803 0.0650  -0.0332 139 SER B CB    
3076 O OG    . SER B 139 ? 0.8347 0.6625 0.8595 -0.0850 0.0700  -0.0441 139 SER B OG    
3077 N N     . PHE B 140 ? 0.7371 0.5789 0.7433 -0.0715 0.0592  -0.0517 140 PHE B N     
3078 C CA    . PHE B 140 ? 0.7554 0.5971 0.7456 -0.0711 0.0525  -0.0628 140 PHE B CA    
3079 C C     . PHE B 140 ? 0.8070 0.6477 0.7960 -0.0657 0.0531  -0.0620 140 PHE B C     
3080 O O     . PHE B 140 ? 0.8398 0.6674 0.8343 -0.0630 0.0611  -0.0581 140 PHE B O     
3081 C CB    . PHE B 140 ? 0.8345 0.6565 0.8113 -0.0760 0.0542  -0.0739 140 PHE B CB    
3082 C CG    . PHE B 140 ? 0.7701 0.5950 0.7456 -0.0826 0.0516  -0.0759 140 PHE B CG    
3083 C CD1   . PHE B 140 ? 0.7437 0.5852 0.7138 -0.0841 0.0421  -0.0792 140 PHE B CD1   
3084 C CD2   . PHE B 140 ? 0.7487 0.5605 0.7300 -0.0870 0.0593  -0.0737 140 PHE B CD2   
3085 C CE1   . PHE B 140 ? 0.7752 0.6216 0.7454 -0.0902 0.0395  -0.0798 140 PHE B CE1   
3086 C CE2   . PHE B 140 ? 0.7554 0.5705 0.7359 -0.0939 0.0566  -0.0750 140 PHE B CE2   
3087 C CZ    . PHE B 140 ? 0.8089 0.6423 0.7838 -0.0956 0.0462  -0.0777 140 PHE B CZ    
3088 N N     . ASP B 141 ? 0.7576 0.6116 0.7400 -0.0641 0.0454  -0.0658 141 ASP B N     
3089 C CA    . ASP B 141 ? 0.7383 0.5906 0.7174 -0.0600 0.0451  -0.0668 141 ASP B CA    
3090 C C     . ASP B 141 ? 0.8096 0.6427 0.7761 -0.0597 0.0466  -0.0765 141 ASP B C     
3091 O O     . ASP B 141 ? 0.8043 0.6299 0.7698 -0.0564 0.0495  -0.0762 141 ASP B O     
3092 C CB    . ASP B 141 ? 0.7178 0.5895 0.6941 -0.0593 0.0374  -0.0682 141 ASP B CB    
3093 C CG    . ASP B 141 ? 0.7833 0.6764 0.7697 -0.0611 0.0355  -0.0591 141 ASP B CG    
3094 O OD1   . ASP B 141 ? 0.8048 0.7013 0.8031 -0.0606 0.0396  -0.0479 141 ASP B OD1   
3095 O OD2   . ASP B 141 ? 0.7584 0.6657 0.7414 -0.0631 0.0302  -0.0625 141 ASP B OD2   
3096 N N     . ALA B 142 ? 0.7274 0.5539 0.6845 -0.0637 0.0444  -0.0845 142 ALA B N     
3097 C CA    . ALA B 142 ? 0.7456 0.5571 0.6898 -0.0647 0.0449  -0.0928 142 ALA B CA    
3098 C C     . ALA B 142 ? 0.8157 0.6193 0.7519 -0.0717 0.0447  -0.0986 142 ALA B C     
3099 O O     . ALA B 142 ? 0.8018 0.6153 0.7415 -0.0749 0.0415  -0.0971 142 ALA B O     
3100 C CB    . ALA B 142 ? 0.6970 0.5174 0.6349 -0.0618 0.0376  -0.0969 142 ALA B CB    
3101 N N     . VAL B 143 ? 0.8291 0.6153 0.7541 -0.0751 0.0484  -0.1050 143 VAL B N     
3102 C CA    . VAL B 143 ? 0.7975 0.5769 0.7116 -0.0839 0.0474  -0.1114 143 VAL B CA    
3103 C C     . VAL B 143 ? 0.8037 0.5801 0.7036 -0.0860 0.0432  -0.1178 143 VAL B C     
3104 O O     . VAL B 143 ? 0.8530 0.6190 0.7484 -0.0832 0.0472  -0.1195 143 VAL B O     
3105 C CB    . VAL B 143 ? 0.7478 0.5069 0.6609 -0.0896 0.0581  -0.1133 143 VAL B CB    
3106 C CG1   . VAL B 143 ? 0.7993 0.5547 0.7008 -0.1007 0.0556  -0.1198 143 VAL B CG1   
3107 C CG2   . VAL B 143 ? 0.7380 0.4999 0.6680 -0.0862 0.0632  -0.1048 143 VAL B CG2   
3108 N N     . ILE B 144 ? 0.8552 0.6424 0.7493 -0.0909 0.0350  -0.1199 144 ILE B N     
3109 C CA    . ILE B 144 ? 0.8171 0.6046 0.6989 -0.0943 0.0302  -0.1239 144 ILE B CA    
3110 C C     . ILE B 144 ? 0.8178 0.5991 0.6880 -0.1068 0.0303  -0.1285 144 ILE B C     
3111 O O     . ILE B 144 ? 0.8163 0.6061 0.6899 -0.1115 0.0270  -0.1270 144 ILE B O     
3112 C CB    . ILE B 144 ? 0.7345 0.5422 0.6212 -0.0894 0.0206  -0.1207 144 ILE B CB    
3113 C CG1   . ILE B 144 ? 0.8354 0.6464 0.7116 -0.0941 0.0150  -0.1225 144 ILE B CG1   
3114 C CG2   . ILE B 144 ? 0.7599 0.5828 0.6554 -0.0903 0.0165  -0.1173 144 ILE B CG2   
3115 C CD1   . ILE B 144 ? 0.8172 0.6456 0.7006 -0.0877 0.0076  -0.1184 144 ILE B CD1   
3116 N N     . ALA B 145 ? 0.8679 0.6347 0.7237 -0.1130 0.0342  -0.1343 145 ALA B N     
3117 C CA    . ALA B 145 ? 0.8766 0.6374 0.7179 -0.1273 0.0343  -0.1398 145 ALA B CA    
3118 C C     . ALA B 145 ? 0.9277 0.6970 0.7565 -0.1324 0.0267  -0.1408 145 ALA B C     
3119 O O     . ALA B 145 ? 0.9840 0.7411 0.7992 -0.1369 0.0308  -0.1458 145 ALA B O     
3120 C CB    . ALA B 145 ? 0.9157 0.6515 0.7500 -0.1324 0.0471  -0.1462 145 ALA B CB    
3121 N N     . LEU B 146 ? 0.8946 0.6858 0.7286 -0.1322 0.0159  -0.1352 146 LEU B N     
3122 C CA    . LEU B 146 ? 0.9281 0.7328 0.7572 -0.1332 0.0076  -0.1319 146 LEU B CA    
3123 C C     . LEU B 146 ? 0.9317 0.7389 0.7442 -0.1501 0.0039  -0.1345 146 LEU B C     
3124 O O     . LEU B 146 ? 0.9497 0.7729 0.7647 -0.1565 -0.0034 -0.1305 146 LEU B O     
3125 C CB    . LEU B 146 ? 0.8803 0.7071 0.7259 -0.1237 -0.0004 -0.1237 146 LEU B CB    
3126 C CG    . LEU B 146 ? 0.8595 0.7047 0.7084 -0.1213 -0.0091 -0.1169 146 LEU B CG    
3127 C CD1   . LEU B 146 ? 0.8935 0.7315 0.7316 -0.1225 -0.0083 -0.1184 146 LEU B CD1   
3128 C CD2   . LEU B 146 ? 0.8886 0.7434 0.7554 -0.1071 -0.0101 -0.1123 146 LEU B CD2   
3129 N N     . GLU B 147 ? 0.9079 0.7002 0.7030 -0.1580 0.0090  -0.1411 147 GLU B N     
3130 C CA    . GLU B 147 ? 0.9858 0.7777 0.7608 -0.1766 0.0070  -0.1455 147 GLU B CA    
3131 C C     . GLU B 147 ? 0.9852 0.7679 0.7552 -0.1883 0.0112  -0.1512 147 GLU B C     
3132 O O     . GLU B 147 ? 0.9572 0.7514 0.7196 -0.2021 0.0045  -0.1504 147 GLU B O     
3133 C CB    . GLU B 147 ? 1.0261 0.8447 0.8011 -0.1812 -0.0062 -0.1365 147 GLU B CB    
3134 C CG    . GLU B 147 ? 1.0441 0.8635 0.8070 -0.1843 -0.0076 -0.1362 147 GLU B CG    
3135 C CD    . GLU B 147 ? 1.1220 0.9677 0.8826 -0.1929 -0.0199 -0.1269 147 GLU B CD    
3136 O OE1   . GLU B 147 ? 1.2640 1.1178 1.0157 -0.2085 -0.0243 -0.1272 147 GLU B OE1   
3137 O OE2   . GLU B 147 ? 1.1687 1.0277 0.9378 -0.1843 -0.0253 -0.1183 147 GLU B OE2   
3138 N N     . SER B 148 ? 1.0099 0.7723 0.7849 -0.1831 0.0223  -0.1563 148 SER B N     
3139 C CA    . SER B 148 ? 1.0282 0.7812 0.8026 -0.1919 0.0272  -0.1605 148 SER B CA    
3140 C C     . SER B 148 ? 1.0250 0.7475 0.7861 -0.1998 0.0422  -0.1720 148 SER B C     
3141 O O     . SER B 148 ? 0.9853 0.6982 0.7343 -0.2155 0.0457  -0.1789 148 SER B O     
3142 C CB    . SER B 148 ? 0.9175 0.6756 0.7148 -0.1782 0.0277  -0.1541 148 SER B CB    
3143 O OG    . SER B 148 ? 0.9320 0.6776 0.7384 -0.1642 0.0360  -0.1539 148 SER B OG    
3144 N N     . ILE B 149 ? 1.0565 0.7630 0.8204 -0.1892 0.0519  -0.1740 149 ILE B N     
3145 C CA    . ILE B 149 ? 0.9859 0.6621 0.7408 -0.1946 0.0685  -0.1841 149 ILE B CA    
3146 C C     . ILE B 149 ? 1.0972 0.7639 0.8246 -0.2148 0.0710  -0.1949 149 ILE B C     
3147 O O     . ILE B 149 ? 1.1357 0.7777 0.8527 -0.2252 0.0843  -0.2052 149 ILE B O     
3148 C CB    . ILE B 149 ? 1.0409 0.7053 0.8048 -0.1793 0.0776  -0.1826 149 ILE B CB    
3149 C CG1   . ILE B 149 ? 1.0151 0.6519 0.7850 -0.1773 0.0956  -0.1871 149 ILE B CG1   
3150 C CG2   . ILE B 149 ? 1.1240 0.7849 0.8704 -0.1832 0.0783  -0.1872 149 ILE B CG2   
3151 C CD1   . ILE B 149 ? 1.0707 0.6953 0.8491 -0.1637 0.1060  -0.1851 149 ILE B CD1   
3152 N N     . ILE B 150 ? 1.1059 0.7930 0.8218 -0.2216 0.0582  -0.1922 150 ILE B N     
3153 C CA    . ILE B 150 ? 1.1285 0.8109 0.8165 -0.2415 0.0590  -0.2012 150 ILE B CA    
3154 C C     . ILE B 150 ? 1.1654 0.8408 0.8399 -0.2619 0.0610  -0.2090 150 ILE B C     
3155 O O     . ILE B 150 ? 1.2862 0.9425 0.9373 -0.2790 0.0706  -0.2217 150 ILE B O     
3156 C CB    . ILE B 150 ? 1.1154 0.8265 0.7983 -0.2435 0.0431  -0.1928 150 ILE B CB    
3157 C CG1   . ILE B 150 ? 1.1393 0.8801 0.8394 -0.2390 0.0275  -0.1802 150 ILE B CG1   
3158 C CG2   . ILE B 150 ? 1.0907 0.8010 0.7787 -0.2287 0.0448  -0.1893 150 ILE B CG2   
3159 C CD1   . ILE B 150 ? 1.1617 0.9313 0.8600 -0.2410 0.0128  -0.1702 150 ILE B CD1   
3160 N N     . HIS B 151 ? 1.0608 0.7516 0.7487 -0.2616 0.0524  -0.2022 151 HIS B N     
3161 C CA    . HIS B 151 ? 1.1066 0.7927 0.7840 -0.2808 0.0532  -0.2083 151 HIS B CA    
3162 C C     . HIS B 151 ? 1.1538 0.8086 0.8362 -0.2803 0.0705  -0.2167 151 HIS B C     
3163 O O     . HIS B 151 ? 1.2047 0.8583 0.8883 -0.2905 0.0702  -0.2182 151 HIS B O     
3164 C CB    . HIS B 151 ? 1.1238 0.8399 0.8156 -0.2800 0.0374  -0.1963 151 HIS B CB    
3165 C CG    . HIS B 151 ? 1.1130 0.8616 0.8035 -0.2809 0.0207  -0.1860 151 HIS B CG    
3166 N ND1   . HIS B 151 ? 1.2758 1.0347 0.9434 -0.3011 0.0142  -0.1884 151 HIS B ND1   
3167 C CD2   . HIS B 151 ? 1.1558 0.9300 0.8662 -0.2647 0.0095  -0.1723 151 HIS B CD2   
3168 C CE1   . HIS B 151 ? 1.3375 1.1278 1.0129 -0.2964 -0.0006 -0.1751 151 HIS B CE1   
3169 N NE2   . HIS B 151 ? 1.2113 1.0101 0.9128 -0.2741 -0.0031 -0.1658 151 HIS B NE2   
3170 N N     . MET B 152 ? 1.2023 0.8332 0.8906 -0.2683 0.0855  -0.2207 152 MET B N     
3171 C CA    . MET B 152 ? 1.2119 0.8228 0.9152 -0.2640 0.0979  -0.2222 152 MET B CA    
3172 C C     . MET B 152 ? 1.2592 0.8321 0.9488 -0.2736 0.1194  -0.2370 152 MET B C     
3173 O O     . MET B 152 ? 1.2431 0.8030 0.9170 -0.2761 0.1272  -0.2447 152 MET B O     
3174 C CB    . MET B 152 ? 1.1156 0.7323 0.8481 -0.2392 0.0984  -0.2103 152 MET B CB    
3175 C CG    . MET B 152 ? 1.1836 0.8350 0.9303 -0.2300 0.0796  -0.1971 152 MET B CG    
3176 S SD    . MET B 152 ? 1.1160 0.7741 0.8955 -0.2081 0.0805  -0.1847 152 MET B SD    
3177 C CE    . MET B 152 ? 1.1433 0.7878 0.9260 -0.1935 0.0903  -0.1849 152 MET B CE    
3178 N N     . PRO B 153 ? 1.2646 0.8187 0.9599 -0.2793 0.1300  -0.2412 153 PRO B N     
3179 C CA    . PRO B 153 ? 1.2806 0.7969 0.9602 -0.2923 0.1514  -0.2571 153 PRO B CA    
3180 C C     . PRO B 153 ? 1.2880 0.7796 0.9764 -0.2774 0.1701  -0.2590 153 PRO B C     
3181 O O     . PRO B 153 ? 1.3675 0.8418 1.0348 -0.2856 0.1803  -0.2707 153 PRO B O     
3182 C CB    . PRO B 153 ? 1.2911 0.7965 0.9808 -0.2991 0.1569  -0.2578 153 PRO B CB    
3183 C CG    . PRO B 153 ? 1.3220 0.8643 1.0189 -0.3001 0.1340  -0.2462 153 PRO B CG    
3184 C CD    . PRO B 153 ? 1.2611 0.8302 0.9716 -0.2801 0.1210  -0.2332 153 PRO B CD    
3185 N N     . ASP B 154 ? 1.2766 0.7678 0.9952 -0.2562 0.1746  -0.2473 154 ASP B N     
3186 C CA    . ASP B 154 ? 1.2407 0.7097 0.9695 -0.2426 0.1928  -0.2476 154 ASP B CA    
3187 C C     . ASP B 154 ? 1.2172 0.7087 0.9683 -0.2196 0.1834  -0.2317 154 ASP B C     
3188 O O     . ASP B 154 ? 1.2111 0.7106 0.9894 -0.2053 0.1823  -0.2190 154 ASP B O     
3189 C CB    . ASP B 154 ? 1.2021 0.6410 0.9467 -0.2408 0.2140  -0.2494 154 ASP B CB    
3190 C CG    . ASP B 154 ? 1.2784 0.6927 1.0324 -0.2286 0.2349  -0.2502 154 ASP B CG    
3191 O OD1   . ASP B 154 ? 1.3877 0.7930 1.1211 -0.2335 0.2401  -0.2600 154 ASP B OD1   
3192 O OD2   . ASP B 154 ? 1.3210 0.7266 1.1035 -0.2140 0.2460  -0.2400 154 ASP B OD2   
3193 N N     . ARG B 155 ? 1.2270 0.7273 0.9660 -0.2168 0.1778  -0.2328 155 ARG B N     
3194 C CA    . ARG B 155 ? 1.1908 0.7116 0.9479 -0.1968 0.1688  -0.2193 155 ARG B CA    
3195 C C     . ARG B 155 ? 1.1992 0.7078 0.9839 -0.1797 0.1828  -0.2104 155 ARG B C     
3196 O O     . ARG B 155 ? 1.2024 0.7303 1.0101 -0.1659 0.1742  -0.1965 155 ARG B O     
3197 C CB    . ARG B 155 ? 1.1261 0.6509 0.8655 -0.1975 0.1657  -0.2234 155 ARG B CB    
3198 C CG    . ARG B 155 ? 1.1223 0.6720 0.8428 -0.2087 0.1460  -0.2246 155 ARG B CG    
3199 C CD    . ARG B 155 ? 1.1711 0.7249 0.8764 -0.2085 0.1436  -0.2269 155 ARG B CD    
3200 N NE    . ARG B 155 ? 1.1795 0.7611 0.8727 -0.2160 0.1239  -0.2239 155 ARG B NE    
3201 C CZ    . ARG B 155 ? 1.2399 0.8234 0.9069 -0.2361 0.1202  -0.2325 155 ARG B CZ    
3202 N NH1   . ARG B 155 ? 1.2378 0.7955 0.8845 -0.2524 0.1350  -0.2470 155 ARG B NH1   
3203 N NH2   . ARG B 155 ? 1.2311 0.8434 0.8921 -0.2404 0.1017  -0.2261 155 ARG B NH2   
3204 N N     . ALA B 156 ? 1.2225 0.6995 1.0060 -0.1812 0.2050  -0.2178 156 ALA B N     
3205 C CA    . ALA B 156 ? 1.2262 0.6932 1.0382 -0.1642 0.2190  -0.2071 156 ALA B CA    
3206 C C     . ALA B 156 ? 1.2136 0.6897 1.0509 -0.1582 0.2160  -0.1952 156 ALA B C     
3207 O O     . ALA B 156 ? 1.1844 0.6691 1.0488 -0.1420 0.2176  -0.1802 156 ALA B O     
3208 C CB    . ALA B 156 ? 1.1871 0.6164 0.9950 -0.1678 0.2457  -0.2173 156 ALA B CB    
3209 N N     . GLN B 157 ? 1.2058 0.6837 1.0346 -0.1715 0.2098  -0.2005 157 GLN B N     
3210 C CA    . GLN B 157 ? 1.2085 0.6941 1.0609 -0.1670 0.2079  -0.1894 157 GLN B CA    
3211 C C     . GLN B 157 ? 1.2116 0.7352 1.0714 -0.1604 0.1843  -0.1780 157 GLN B C     
3212 O O     . GLN B 157 ? 1.1672 0.7051 1.0523 -0.1473 0.1815  -0.1632 157 GLN B O     
3213 C CB    . GLN B 157 ? 1.1904 0.6595 1.0313 -0.1849 0.2131  -0.2001 157 GLN B CB    
3214 C CG    . GLN B 157 ? 1.2362 0.7067 1.1028 -0.1806 0.2161  -0.1891 157 GLN B CG    
3215 C CD    . GLN B 157 ? 1.3058 0.7781 1.1597 -0.1980 0.2088  -0.1962 157 GLN B CD    
3216 O OE1   . GLN B 157 ? 1.4086 0.8767 1.2786 -0.1990 0.2133  -0.1908 157 GLN B OE1   
3217 N NE2   . GLN B 157 ? 1.2774 0.7573 1.1029 -0.2122 0.1974  -0.2075 157 GLN B NE2   
3218 N N     . VAL B 158 ? 1.2026 0.7419 1.0411 -0.1697 0.1686  -0.1844 158 VAL B N     
3219 C CA    . VAL B 158 ? 1.1284 0.7022 0.9732 -0.1632 0.1477  -0.1746 158 VAL B CA    
3220 C C     . VAL B 158 ? 1.0939 0.6808 0.9565 -0.1448 0.1454  -0.1628 158 VAL B C     
3221 O O     . VAL B 158 ? 1.0367 0.6423 0.9193 -0.1351 0.1386  -0.1504 158 VAL B O     
3222 C CB    . VAL B 158 ? 1.1202 0.7075 0.9404 -0.1744 0.1334  -0.1824 158 VAL B CB    
3223 C CG1   . VAL B 158 ? 0.9814 0.6008 0.8115 -0.1643 0.1156  -0.1717 158 VAL B CG1   
3224 C CG2   . VAL B 158 ? 1.0790 0.6617 0.8842 -0.1933 0.1315  -0.1909 158 VAL B CG2   
3225 N N     . LEU B 159 ? 1.1423 0.7192 0.9977 -0.1407 0.1518  -0.1664 159 LEU B N     
3226 C CA    . LEU B 159 ? 1.1082 0.6947 0.9805 -0.1243 0.1517  -0.1553 159 LEU B CA    
3227 C C     . LEU B 159 ? 1.0667 0.6486 0.9666 -0.1143 0.1625  -0.1433 159 LEU B C     
3228 O O     . LEU B 159 ? 1.0456 0.6477 0.9638 -0.1028 0.1556  -0.1301 159 LEU B O     
3229 C CB    . LEU B 159 ? 1.0542 0.6265 0.9146 -0.1228 0.1599  -0.1615 159 LEU B CB    
3230 C CG    . LEU B 159 ? 1.1017 0.6777 0.9353 -0.1322 0.1512  -0.1721 159 LEU B CG    
3231 C CD1   . LEU B 159 ? 1.0521 0.6119 0.8774 -0.1295 0.1626  -0.1767 159 LEU B CD1   
3232 C CD2   . LEU B 159 ? 1.0161 0.6227 0.8498 -0.1283 0.1304  -0.1660 159 LEU B CD2   
3233 N N     . ALA B 160 ? 1.1075 0.6633 1.0112 -0.1188 0.1801  -0.1471 160 ALA B N     
3234 C CA    . ALA B 160 ? 1.0648 0.6178 0.9974 -0.1095 0.1904  -0.1335 160 ALA B CA    
3235 C C     . ALA B 160 ? 1.0173 0.5933 0.9627 -0.1091 0.1778  -0.1239 160 ALA B C     
3236 O O     . ALA B 160 ? 0.9481 0.5366 0.9184 -0.0987 0.1784  -0.1083 160 ALA B O     
3237 C CB    . ALA B 160 ? 1.1244 0.6425 1.0590 -0.1150 0.2132  -0.1401 160 ALA B CB    
3238 N N     . GLN B 161 ? 1.0455 0.6285 0.9745 -0.1207 0.1665  -0.1323 161 GLN B N     
3239 C CA    . GLN B 161 ? 1.0234 0.6308 0.9633 -0.1201 0.1534  -0.1234 161 GLN B CA    
3240 C C     . GLN B 161 ? 0.9762 0.6144 0.9230 -0.1095 0.1381  -0.1136 161 GLN B C     
3241 O O     . GLN B 161 ? 0.9622 0.6178 0.9293 -0.1017 0.1349  -0.1001 161 GLN B O     
3242 C CB    . GLN B 161 ? 1.0393 0.6482 0.9601 -0.1353 0.1449  -0.1342 161 GLN B CB    
3243 C CG    . GLN B 161 ? 1.0523 0.6415 0.9767 -0.1451 0.1561  -0.1373 161 GLN B CG    
3244 C CD    . GLN B 161 ? 1.0394 0.6397 0.9918 -0.1374 0.1573  -0.1216 161 GLN B CD    
3245 O OE1   . GLN B 161 ? 1.0938 0.7170 1.0498 -0.1389 0.1440  -0.1163 161 GLN B OE1   
3246 N NE2   . GLN B 161 ? 1.0239 0.6093 0.9971 -0.1290 0.1733  -0.1131 161 GLN B NE2   
3247 N N     . VAL B 162 ? 0.9599 0.6046 0.8900 -0.1096 0.1295  -0.1203 162 VAL B N     
3248 C CA    . VAL B 162 ? 0.8812 0.5520 0.8158 -0.1005 0.1162  -0.1132 162 VAL B CA    
3249 C C     . VAL B 162 ? 0.8920 0.5660 0.8465 -0.0881 0.1225  -0.1009 162 VAL B C     
3250 O O     . VAL B 162 ? 0.9276 0.6245 0.8950 -0.0814 0.1143  -0.0903 162 VAL B O     
3251 C CB    . VAL B 162 ? 0.8956 0.5682 0.8091 -0.1034 0.1084  -0.1228 162 VAL B CB    
3252 C CG1   . VAL B 162 ? 0.8009 0.4948 0.7199 -0.0934 0.0982  -0.1161 162 VAL B CG1   
3253 C CG2   . VAL B 162 ? 0.8659 0.5445 0.7631 -0.1150 0.0987  -0.1310 162 VAL B CG2   
3254 N N     . GLY B 163 ? 0.8432 0.4953 0.8007 -0.0855 0.1375  -0.1016 163 GLY B N     
3255 C CA    . GLY B 163 ? 0.8817 0.5385 0.8599 -0.0740 0.1437  -0.0881 163 GLY B CA    
3256 C C     . GLY B 163 ? 0.9263 0.5949 0.9289 -0.0700 0.1454  -0.0731 163 GLY B C     
3257 O O     . GLY B 163 ? 0.9526 0.6360 0.9732 -0.0612 0.1450  -0.0589 163 GLY B O     
3258 N N     . ARG B 164 ? 0.8855 0.5496 0.8887 -0.0771 0.1465  -0.0753 164 ARG B N     
3259 C CA    . ARG B 164 ? 0.8338 0.5085 0.8599 -0.0745 0.1484  -0.0610 164 ARG B CA    
3260 C C     . ARG B 164 ? 0.9105 0.6182 0.9391 -0.0737 0.1310  -0.0544 164 ARG B C     
3261 O O     . ARG B 164 ? 0.8312 0.5582 0.8795 -0.0677 0.1292  -0.0387 164 ARG B O     
3262 C CB    . ARG B 164 ? 0.8505 0.5043 0.8751 -0.0836 0.1577  -0.0674 164 ARG B CB    
3263 C CG    . ARG B 164 ? 0.8547 0.5156 0.9038 -0.0815 0.1618  -0.0526 164 ARG B CG    
3264 C CD    . ARG B 164 ? 0.9367 0.5733 0.9822 -0.0915 0.1719  -0.0609 164 ARG B CD    
3265 N NE    . ARG B 164 ? 0.8900 0.5309 0.9119 -0.1027 0.1595  -0.0748 164 ARG B NE    
3266 C CZ    . ARG B 164 ? 0.9365 0.6010 0.9604 -0.1055 0.1461  -0.0704 164 ARG B CZ    
3267 N NH1   . ARG B 164 ? 0.8310 0.5171 0.8769 -0.0986 0.1428  -0.0536 164 ARG B NH1   
3268 N NH2   . ARG B 164 ? 0.9196 0.5872 0.9231 -0.1158 0.1361  -0.0824 164 ARG B NH2   
3269 N N     . VAL B 165 ? 0.9057 0.6205 0.9148 -0.0802 0.1189  -0.0658 165 VAL B N     
3270 C CA    . VAL B 165 ? 0.8457 0.5898 0.8551 -0.0798 0.1037  -0.0617 165 VAL B CA    
3271 C C     . VAL B 165 ? 0.8608 0.6220 0.8687 -0.0728 0.0957  -0.0588 165 VAL B C     
3272 O O     . VAL B 165 ? 0.9231 0.7092 0.9376 -0.0704 0.0867  -0.0514 165 VAL B O     
3273 C CB    . VAL B 165 ? 0.8274 0.5736 0.8190 -0.0888 0.0945  -0.0736 165 VAL B CB    
3274 C CG1   . VAL B 165 ? 0.8380 0.5756 0.8342 -0.0962 0.0995  -0.0734 165 VAL B CG1   
3275 C CG2   . VAL B 165 ? 0.8514 0.5816 0.8220 -0.0930 0.0948  -0.0875 165 VAL B CG2   
3276 N N     . LEU B 166 ? 0.8764 0.6250 0.8748 -0.0704 0.0989  -0.0651 166 LEU B N     
3277 C CA    . LEU B 166 ? 0.8261 0.5892 0.8232 -0.0644 0.0919  -0.0626 166 LEU B CA    
3278 C C     . LEU B 166 ? 0.8372 0.6144 0.8553 -0.0578 0.0946  -0.0462 166 LEU B C     
3279 O O     . LEU B 166 ? 0.8737 0.6391 0.9057 -0.0544 0.1066  -0.0382 166 LEU B O     
3280 C CB    . LEU B 166 ? 0.8230 0.5683 0.8074 -0.0634 0.0963  -0.0713 166 LEU B CB    
3281 C CG    . LEU B 166 ? 0.7852 0.5363 0.7506 -0.0663 0.0851  -0.0823 166 LEU B CG    
3282 C CD1   . LEU B 166 ? 0.8055 0.5412 0.7588 -0.0656 0.0889  -0.0896 166 LEU B CD1   
3283 C CD2   . LEU B 166 ? 0.8841 0.6601 0.8541 -0.0621 0.0744  -0.0768 166 LEU B CD2   
3284 N N     . ARG B 167 ? 0.7974 0.6005 0.8183 -0.0565 0.0839  -0.0407 167 ARG B N     
3285 C CA    . ARG B 167 ? 0.8158 0.6359 0.8541 -0.0519 0.0847  -0.0250 167 ARG B CA    
3286 C C     . ARG B 167 ? 0.7883 0.5994 0.8268 -0.0468 0.0896  -0.0240 167 ARG B C     
3287 O O     . ARG B 167 ? 0.7419 0.5385 0.7645 -0.0471 0.0894  -0.0364 167 ARG B O     
3288 C CB    . ARG B 167 ? 0.7830 0.6323 0.8200 -0.0535 0.0722  -0.0219 167 ARG B CB    
3289 C CG    . ARG B 167 ? 0.7649 0.6267 0.8029 -0.0583 0.0671  -0.0215 167 ARG B CG    
3290 C CD    . ARG B 167 ? 0.7745 0.6648 0.8097 -0.0604 0.0562  -0.0198 167 ARG B CD    
3291 N NE    . ARG B 167 ? 0.8717 0.7749 0.9117 -0.0644 0.0535  -0.0161 167 ARG B NE    
3292 C CZ    . ARG B 167 ? 0.8043 0.7202 0.8349 -0.0676 0.0457  -0.0232 167 ARG B CZ    
3293 N NH1   . ARG B 167 ? 0.7681 0.6877 0.7851 -0.0672 0.0398  -0.0333 167 ARG B NH1   
3294 N NH2   . ARG B 167 ? 0.8077 0.7324 0.8436 -0.0710 0.0447  -0.0195 167 ARG B NH2   
3295 N N     . PRO B 168 ? 0.7744 0.5938 0.8315 -0.0423 0.0947  -0.0084 168 PRO B N     
3296 C CA    . PRO B 168 ? 0.8286 0.6434 0.8865 -0.0376 0.0981  -0.0062 168 PRO B CA    
3297 C C     . PRO B 168 ? 0.8306 0.6564 0.8722 -0.0390 0.0862  -0.0149 168 PRO B C     
3298 O O     . PRO B 168 ? 0.9220 0.7688 0.9607 -0.0421 0.0759  -0.0143 168 PRO B O     
3299 C CB    . PRO B 168 ? 0.8561 0.6880 0.9389 -0.0339 0.1020  0.0152  168 PRO B CB    
3300 C CG    . PRO B 168 ? 0.7823 0.6131 0.8789 -0.0351 0.1077  0.0227  168 PRO B CG    
3301 C CD    . PRO B 168 ? 0.8144 0.6461 0.8944 -0.0413 0.0991  0.0093  168 PRO B CD    
3302 N N     . GLY B 169 ? 0.8483 0.6592 0.8793 -0.0370 0.0885  -0.0233 169 GLY B N     
3303 C CA    . GLY B 169 ? 0.8761 0.6935 0.8921 -0.0380 0.0788  -0.0321 169 GLY B CA    
3304 C C     . GLY B 169 ? 0.7720 0.5816 0.7690 -0.0417 0.0729  -0.0480 169 GLY B C     
3305 O O     . GLY B 169 ? 0.8055 0.6142 0.7902 -0.0417 0.0674  -0.0562 169 GLY B O     
3306 N N     . GLY B 170 ? 0.7659 0.5704 0.7615 -0.0451 0.0741  -0.0516 170 GLY B N     
3307 C CA    . GLY B 170 ? 0.7924 0.5919 0.7716 -0.0492 0.0683  -0.0648 170 GLY B CA    
3308 C C     . GLY B 170 ? 0.8207 0.5992 0.7868 -0.0497 0.0726  -0.0745 170 GLY B C     
3309 O O     . GLY B 170 ? 0.9149 0.6783 0.8846 -0.0475 0.0826  -0.0723 170 GLY B O     
3310 N N     . ARG B 171 ? 0.7836 0.5624 0.7352 -0.0528 0.0654  -0.0845 171 ARG B N     
3311 C CA    . ARG B 171 ? 0.7438 0.5062 0.6813 -0.0543 0.0677  -0.0933 171 ARG B CA    
3312 C C     . ARG B 171 ? 0.8024 0.5581 0.7276 -0.0616 0.0657  -0.1021 171 ARG B C     
3313 O O     . ARG B 171 ? 0.8326 0.6013 0.7581 -0.0640 0.0583  -0.1025 171 ARG B O     
3314 C CB    . ARG B 171 ? 0.8000 0.5705 0.7312 -0.0515 0.0600  -0.0959 171 ARG B CB    
3315 C CG    . ARG B 171 ? 0.8590 0.6260 0.7946 -0.0463 0.0642  -0.0913 171 ARG B CG    
3316 C CD    . ARG B 171 ? 0.9015 0.6776 0.8321 -0.0442 0.0561  -0.0936 171 ARG B CD    
3317 N NE    . ARG B 171 ? 0.9757 0.7541 0.9134 -0.0398 0.0584  -0.0872 171 ARG B NE    
3318 C CZ    . ARG B 171 ? 1.0056 0.7989 0.9544 -0.0382 0.0563  -0.0791 171 ARG B CZ    
3319 N NH1   . ARG B 171 ? 1.0069 0.8130 0.9612 -0.0403 0.0529  -0.0764 171 ARG B NH1   
3320 N NH2   . ARG B 171 ? 1.0924 0.8888 1.0464 -0.0354 0.0574  -0.0733 171 ARG B NH2   
3321 N N     . LEU B 172 ? 0.8624 0.5992 0.7770 -0.0657 0.0725  -0.1085 172 LEU B N     
3322 C CA    . LEU B 172 ? 0.8239 0.5539 0.7240 -0.0747 0.0708  -0.1173 172 LEU B CA    
3323 C C     . LEU B 172 ? 0.8721 0.6028 0.7578 -0.0764 0.0649  -0.1231 172 LEU B C     
3324 O O     . LEU B 172 ? 0.8722 0.5934 0.7538 -0.0737 0.0697  -0.1241 172 LEU B O     
3325 C CB    . LEU B 172 ? 0.8453 0.5527 0.7422 -0.0801 0.0838  -0.1211 172 LEU B CB    
3326 C CG    . LEU B 172 ? 0.8181 0.5121 0.6954 -0.0913 0.0855  -0.1320 172 LEU B CG    
3327 C CD1   . LEU B 172 ? 0.7879 0.4939 0.6605 -0.0989 0.0759  -0.1341 172 LEU B CD1   
3328 C CD2   . LEU B 172 ? 0.8121 0.4815 0.6887 -0.0950 0.1014  -0.1356 172 LEU B CD2   
3329 N N     . VAL B 173 ? 0.8215 0.5646 0.7008 -0.0805 0.0548  -0.1255 173 VAL B N     
3330 C CA    . VAL B 173 ? 0.8530 0.5988 0.7200 -0.0828 0.0487  -0.1293 173 VAL B CA    
3331 C C     . VAL B 173 ? 0.9175 0.6610 0.7711 -0.0946 0.0464  -0.1348 173 VAL B C     
3332 O O     . VAL B 173 ? 0.8467 0.6010 0.7034 -0.0982 0.0410  -0.1336 173 VAL B O     
3333 C CB    . VAL B 173 ? 0.8781 0.6429 0.7517 -0.0766 0.0386  -0.1253 173 VAL B CB    
3334 C CG1   . VAL B 173 ? 0.8476 0.6147 0.7110 -0.0781 0.0334  -0.1272 173 VAL B CG1   
3335 C CG2   . VAL B 173 ? 0.9449 0.7134 0.8310 -0.0672 0.0404  -0.1202 173 VAL B CG2   
3336 N N     . LEU B 174 ? 0.9162 0.6472 0.7544 -0.1012 0.0504  -0.1405 174 LEU B N     
3337 C CA    . LEU B 174 ? 0.9390 0.6673 0.7614 -0.1148 0.0488  -0.1464 174 LEU B CA    
3338 C C     . LEU B 174 ? 0.9777 0.7091 0.7859 -0.1193 0.0443  -0.1483 174 LEU B C     
3339 O O     . LEU B 174 ? 0.9946 0.7225 0.8026 -0.1129 0.0463  -0.1472 174 LEU B O     
3340 C CB    . LEU B 174 ? 0.8921 0.5977 0.7065 -0.1230 0.0615  -0.1535 174 LEU B CB    
3341 C CG    . LEU B 174 ? 0.9436 0.6293 0.7540 -0.1199 0.0739  -0.1569 174 LEU B CG    
3342 C CD1   . LEU B 174 ? 1.0018 0.6786 0.7898 -0.1316 0.0760  -0.1651 174 LEU B CD1   
3343 C CD2   . LEU B 174 ? 0.9256 0.5931 0.7449 -0.1185 0.0877  -0.1578 174 LEU B CD2   
3344 N N     . THR B 175 ? 0.9834 0.7232 0.7802 -0.1310 0.0376  -0.1500 175 THR B N     
3345 C CA    . THR B 175 ? 0.9803 0.7191 0.7588 -0.1406 0.0360  -0.1533 175 THR B CA    
3346 C C     . THR B 175 ? 1.0720 0.7919 0.8324 -0.1554 0.0453  -0.1635 175 THR B C     
3347 O O     . THR B 175 ? 1.0801 0.7908 0.8445 -0.1581 0.0510  -0.1665 175 THR B O     
3348 C CB    . THR B 175 ? 0.9803 0.7437 0.7584 -0.1447 0.0220  -0.1468 175 THR B CB    
3349 O OG1   . THR B 175 ? 0.9566 0.7303 0.7395 -0.1500 0.0170  -0.1451 175 THR B OG1   
3350 C CG2   . THR B 175 ? 0.9366 0.7137 0.7302 -0.1304 0.0158  -0.1383 175 THR B CG2   
3351 N N     . ASP B 176 ? 1.0977 0.8108 0.8384 -0.1651 0.0480  -0.1689 176 ASP B N     
3352 C CA    . ASP B 176 ? 1.0753 0.7707 0.7933 -0.1823 0.0571  -0.1803 176 ASP B CA    
3353 C C     . ASP B 176 ? 1.0815 0.7831 0.7789 -0.1931 0.0531  -0.1821 176 ASP B C     
3354 O O     . ASP B 176 ? 1.0855 0.7984 0.7877 -0.1845 0.0474  -0.1751 176 ASP B O     
3355 C CB    . ASP B 176 ? 1.0712 0.7372 0.7897 -0.1784 0.0754  -0.1880 176 ASP B CB    
3356 C CG    . ASP B 176 ? 1.1304 0.7768 0.8373 -0.1927 0.0859  -0.1987 176 ASP B CG    
3357 O OD1   . ASP B 176 ? 1.1671 0.8202 0.8578 -0.2097 0.0799  -0.2028 176 ASP B OD1   
3358 O OD2   . ASP B 176 ? 1.1092 0.7335 0.8241 -0.1871 0.1007  -0.2022 176 ASP B OD2   
3359 N N     . PHE B 177 ? 1.1575 0.8518 0.8314 -0.2130 0.0564  -0.1913 177 PHE B N     
3360 C CA    . PHE B 177 ? 1.1143 0.8116 0.7644 -0.2267 0.0552  -0.1950 177 PHE B CA    
3361 C C     . PHE B 177 ? 1.2118 0.8798 0.8483 -0.2285 0.0733  -0.2068 177 PHE B C     
3362 O O     . PHE B 177 ? 1.2559 0.8996 0.8951 -0.2271 0.0875  -0.2148 177 PHE B O     
3363 C CB    . PHE B 177 ? 1.1134 0.8201 0.7428 -0.2500 0.0490  -0.1990 177 PHE B CB    
3364 C CG    . PHE B 177 ? 1.1319 0.8721 0.7703 -0.2514 0.0302  -0.1857 177 PHE B CG    
3365 C CD1   . PHE B 177 ? 1.1507 0.9138 0.7955 -0.2447 0.0191  -0.1737 177 PHE B CD1   
3366 C CD2   . PHE B 177 ? 1.1225 0.8716 0.7637 -0.2601 0.0243  -0.1847 177 PHE B CD2   
3367 C CE1   . PHE B 177 ? 1.1276 0.9219 0.7830 -0.2457 0.0029  -0.1602 177 PHE B CE1   
3368 C CE2   . PHE B 177 ? 1.1819 0.9632 0.8326 -0.2616 0.0076  -0.1714 177 PHE B CE2   
3369 C CZ    . PHE B 177 ? 1.1302 0.9340 0.7887 -0.2540 -0.0027 -0.1589 177 PHE B CZ    
3370 N N     . PHE B 178 ? 1.2808 0.9521 0.9042 -0.2313 0.0731  -0.2067 178 PHE B N     
3371 C CA    . PHE B 178 ? 1.2128 0.8569 0.8234 -0.2325 0.0913  -0.2176 178 PHE B CA    
3372 C C     . PHE B 178 ? 1.2858 0.9357 0.8725 -0.2445 0.0901  -0.2200 178 PHE B C     
3373 O O     . PHE B 178 ? 1.2698 0.9471 0.8547 -0.2481 0.0741  -0.2102 178 PHE B O     
3374 C CB    . PHE B 178 ? 1.2084 0.8422 0.8425 -0.2097 0.0989  -0.2125 178 PHE B CB    
3375 C CG    . PHE B 178 ? 1.2563 0.9057 0.8996 -0.1971 0.0909  -0.2020 178 PHE B CG    
3376 C CD1   . PHE B 178 ? 1.2077 0.8848 0.8636 -0.1912 0.0731  -0.1894 178 PHE B CD1   
3377 C CD2   . PHE B 178 ? 1.1971 0.8325 0.8383 -0.1904 0.1023  -0.2042 178 PHE B CD2   
3378 C CE1   . PHE B 178 ? 1.2115 0.9008 0.8767 -0.1798 0.0669  -0.1800 178 PHE B CE1   
3379 C CE2   . PHE B 178 ? 1.2863 0.9355 0.9364 -0.1793 0.0951  -0.1943 178 PHE B CE2   
3380 C CZ    . PHE B 178 ? 1.2696 0.9451 0.9316 -0.1742 0.0775  -0.1825 178 PHE B CZ    
3381 N N     . GLU B 179 ? 1.4230 1.0475 0.9917 -0.2515 0.1077  -0.2329 179 GLU B N     
3382 C CA    . GLU B 179 ? 1.3579 0.9845 0.9031 -0.2622 0.1099  -0.2365 179 GLU B CA    
3383 C C     . GLU B 179 ? 1.3439 0.9708 0.9052 -0.2422 0.1121  -0.2283 179 GLU B C     
3384 O O     . GLU B 179 ? 1.2637 0.8675 0.8346 -0.2306 0.1279  -0.2326 179 GLU B O     
3385 C CB    . GLU B 179 ? 1.4064 1.0043 0.9236 -0.2803 0.1293  -0.2555 179 GLU B CB    
3386 C CG    . GLU B 179 ? 1.4173 1.0106 0.9180 -0.3015 0.1293  -0.2655 179 GLU B CG    
3387 C CD    . GLU B 179 ? 1.6025 1.1729 1.0671 -0.3260 0.1456  -0.2851 179 GLU B CD    
3388 O OE1   . GLU B 179 ? 1.6618 1.1984 1.1241 -0.3231 0.1682  -0.2975 179 GLU B OE1   
3389 O OE2   . GLU B 179 ? 1.6470 1.2341 1.0856 -0.3488 0.1361  -0.2876 179 GLU B OE2   
3390 N N     . ARG B 180 ? 1.3748 1.0286 0.9410 -0.2381 0.0963  -0.2153 180 ARG B N     
3391 C CA    . ARG B 180 ? 1.3845 1.0401 0.9643 -0.2212 0.0973  -0.2073 180 ARG B CA    
3392 C C     . ARG B 180 ? 1.4588 1.0947 1.0189 -0.2271 0.1140  -0.2175 180 ARG B C     
3393 O O     . ARG B 180 ? 1.4739 1.0969 1.0462 -0.2123 0.1242  -0.2163 180 ARG B O     
3394 C CB    . ARG B 180 ? 1.3668 1.0543 0.9531 -0.2188 0.0781  -0.1922 180 ARG B CB    
3395 C CG    . ARG B 180 ? 1.2908 0.9983 0.8945 -0.2151 0.0627  -0.1828 180 ARG B CG    
3396 C CD    . ARG B 180 ? 1.2649 1.0039 0.8731 -0.2161 0.0451  -0.1681 180 ARG B CD    
3397 N NE    . ARG B 180 ? 1.1640 0.9099 0.7946 -0.1967 0.0411  -0.1569 180 ARG B NE    
3398 C CZ    . ARG B 180 ? 1.1766 0.9474 0.8216 -0.1910 0.0268  -0.1423 180 ARG B CZ    
3399 N NH1   . ARG B 180 ? 1.1921 0.9858 0.8335 -0.2021 0.0145  -0.1353 180 ARG B NH1   
3400 N NH2   . ARG B 180 ? 1.2165 0.9894 0.8809 -0.1740 0.0253  -0.1341 180 ARG B NH2   
3401 N N     . ALA B 181 ? 1.4279 1.0622 0.9576 -0.2491 0.1170  -0.2273 181 ALA B N     
3402 C CA    . ALA B 181 ? 1.4879 1.0989 0.9939 -0.2592 0.1361  -0.2413 181 ALA B CA    
3403 C C     . ALA B 181 ? 1.6232 1.2357 1.0966 -0.2872 0.1356  -0.2527 181 ALA B C     
3404 O O     . ALA B 181 ? 1.5369 1.1696 1.0111 -0.2951 0.1197  -0.2472 181 ALA B O     
3405 C CB    . ALA B 181 ? 1.5216 1.1407 1.0253 -0.2533 0.1359  -0.2348 181 ALA B CB    
3406 N N     . PRO B 182 ? 1.7223 1.3142 1.1659 -0.3035 0.1529  -0.2688 182 PRO B N     
3407 C CA    . PRO B 182 ? 1.6463 1.2414 1.0547 -0.3333 0.1519  -0.2801 182 PRO B CA    
3408 C C     . PRO B 182 ? 1.6127 1.2475 1.0155 -0.3452 0.1268  -0.2670 182 PRO B C     
3409 O O     . PRO B 182 ? 1.6242 1.2842 1.0311 -0.3406 0.1142  -0.2530 182 PRO B O     
3410 C CB    . PRO B 182 ? 1.6260 1.2055 1.0071 -0.3438 0.1689  -0.2921 182 PRO B CB    
3411 C CG    . PRO B 182 ? 1.6625 1.2152 1.0657 -0.3199 0.1874  -0.2935 182 PRO B CG    
3412 C CD    . PRO B 182 ? 1.7215 1.2808 1.1641 -0.2958 0.1775  -0.2796 182 PRO B CD    
3413 N N     . LEU B 183 ? 1.6597 1.2923 1.0474 -0.3658 0.1249  -0.2763 183 LEU B N     
3414 C CA    . LEU B 183 ? 1.6308 1.3006 1.0140 -0.3798 0.1017  -0.2643 183 LEU B CA    
3415 C C     . LEU B 183 ? 1.6486 1.3403 1.0030 -0.4003 0.0949  -0.2620 183 LEU B C     
3416 O O     . LEU B 183 ? 1.6955 1.3682 1.0189 -0.4173 0.1105  -0.2786 183 LEU B O     
3417 C CB    . LEU B 183 ? 1.6831 1.3444 1.0547 -0.3977 0.1031  -0.2752 183 LEU B CB    
3418 C CG    . LEU B 183 ? 1.6303 1.2757 1.0311 -0.3795 0.1067  -0.2749 183 LEU B CG    
3419 C CD1   . LEU B 183 ? 1.6611 1.2950 1.0464 -0.4001 0.1106  -0.2876 183 LEU B CD1   
3420 C CD2   . LEU B 183 ? 1.4761 1.1509 0.9109 -0.3593 0.0866  -0.2532 183 LEU B CD2   
3421 N N     . ALA B 184 ? 1.6504 1.3853 1.0215 -0.3942 0.0705  -0.2376 184 ALA B N     
3422 C CA    . ALA B 184 ? 1.6858 1.4443 1.0267 -0.4191 0.0631  -0.2353 184 ALA B CA    
3423 C C     . ALA B 184 ? 1.6718 1.4324 0.9838 -0.4497 0.0619  -0.2466 184 ALA B C     
3424 O O     . ALA B 184 ? 1.6558 1.4274 0.9812 -0.4504 0.0511  -0.2410 184 ALA B O     
3425 C CB    . ALA B 184 ? 1.6427 1.4444 1.0021 -0.4124 0.0402  -0.2092 184 ALA B CB    
3426 N N     . PRO B 185 ? 1.7739 1.5234 1.0458 -0.4760 0.0734  -0.2633 185 PRO B N     
3427 C CA    . PRO B 185 ? 1.7521 1.5039 0.9938 -0.5081 0.0720  -0.2749 185 PRO B CA    
3428 C C     . PRO B 185 ? 1.7995 1.5996 1.0437 -0.5218 0.0455  -0.2545 185 PRO B C     
3429 O O     . PRO B 185 ? 1.7632 1.5680 1.0015 -0.5374 0.0399  -0.2578 185 PRO B O     
3430 C CB    . PRO B 185 ? 1.5367 1.2720 0.7368 -0.5317 0.0889  -0.2937 185 PRO B CB    
3431 C CG    . PRO B 185 ? 1.4653 1.1923 0.6720 -0.5130 0.0973  -0.2912 185 PRO B CG    
3432 C CD    . PRO B 185 ? 1.6861 1.4136 0.9389 -0.4767 0.0917  -0.2755 185 PRO B CD    
3433 N N     . GLU B 186 ? 1.7328 1.5688 0.9900 -0.5141 0.0292  -0.2319 186 GLU B N     
3434 C CA    . GLU B 186 ? 1.7543 1.6383 1.0177 -0.5256 0.0045  -0.2095 186 GLU B CA    
3435 C C     . GLU B 186 ? 1.8043 1.6952 1.0969 -0.5146 -0.0056 -0.2011 186 GLU B C     
3436 O O     . GLU B 186 ? 1.7961 1.7194 1.0863 -0.5317 -0.0221 -0.1895 186 GLU B O     
3437 C CB    . GLU B 186 ? 1.7245 1.6405 1.0075 -0.5110 -0.0088 -0.1851 186 GLU B CB    
3438 N N     . GLY B 187 ? 1.7724 1.6349 1.0928 -0.4868 0.0039  -0.2060 187 GLY B N     
3439 C CA    . GLY B 187 ? 1.7558 1.6247 1.1056 -0.4740 -0.0050 -0.1975 187 GLY B CA    
3440 C C     . GLY B 187 ? 1.7937 1.6266 1.1423 -0.4736 0.0092  -0.2169 187 GLY B C     
3441 O O     . GLY B 187 ? 1.7572 1.5970 1.1308 -0.4628 0.0015  -0.2091 187 GLY B O     
3442 N N     . ARG B 188 ? 1.8388 1.6341 1.1602 -0.4850 0.0301  -0.2413 188 ARG B N     
3443 C CA    . ARG B 188 ? 1.7739 1.5346 1.0953 -0.4855 0.0444  -0.2589 188 ARG B CA    
3444 C C     . ARG B 188 ? 1.7661 1.5446 1.0841 -0.5040 0.0321  -0.2561 188 ARG B C     
3445 O O     . ARG B 188 ? 1.6959 1.4529 1.0228 -0.5006 0.0394  -0.2649 188 ARG B O     
3446 C CB    . ARG B 188 ? 1.7757 1.4975 1.0629 -0.5024 0.0682  -0.2853 188 ARG B CB    
3447 C CG    . ARG B 188 ? 1.7271 1.4408 1.0039 -0.4970 0.0779  -0.2883 188 ARG B CG    
3448 C CD    . ARG B 188 ? 1.6763 1.3579 0.9234 -0.5139 0.1014  -0.3106 188 ARG B CD    
3449 N NE    . ARG B 188 ? 1.6488 1.2874 0.9118 -0.4945 0.1242  -0.3234 188 ARG B NE    
3450 C CZ    . ARG B 188 ? 1.6308 1.2461 0.8978 -0.4977 0.1377  -0.3335 188 ARG B CZ    
3451 N NH1   . ARG B 188 ? 1.6073 1.2362 0.8626 -0.5195 0.1309  -0.3338 188 ARG B NH1   
3452 N NH2   . ARG B 188 ? 1.6773 1.2556 0.9606 -0.4789 0.1587  -0.3426 188 ARG B NH2   
3453 N N     . ALA B 189 ? 1.7717 1.5896 1.0765 -0.5245 0.0141  -0.2434 189 ALA B N     
3454 C CA    . ALA B 189 ? 1.7742 1.6172 1.0774 -0.5428 -0.0008 -0.2363 189 ALA B CA    
3455 C C     . ALA B 189 ? 1.6943 1.5501 1.0400 -0.5173 -0.0116 -0.2197 189 ALA B C     
3456 O O     . ALA B 189 ? 1.6966 1.5339 1.0503 -0.5152 -0.0061 -0.2279 189 ALA B O     
3457 C CB    . ALA B 189 ? 1.7857 1.6747 1.0726 -0.5655 -0.0197 -0.2203 189 ALA B CB    
3458 N N     . ALA B 190 ? 1.6984 1.5842 1.0715 -0.4976 -0.0257 -0.1967 190 ALA B N     
3459 C CA    . ALA B 190 ? 1.6488 1.5531 1.0610 -0.4760 -0.0377 -0.1788 190 ALA B CA    
3460 C C     . ALA B 190 ? 1.6266 1.4952 1.0600 -0.4519 -0.0240 -0.1893 190 ALA B C     
3461 O O     . ALA B 190 ? 1.5191 1.3931 0.9745 -0.4432 -0.0293 -0.1834 190 ALA B O     
3462 C CB    . ALA B 190 ? 1.6322 1.5687 1.0697 -0.4576 -0.0513 -0.1545 190 ALA B CB    
3463 N N     . VAL B 191 ? 1.6540 1.4877 1.0819 -0.4409 -0.0062 -0.2038 191 VAL B N     
3464 C CA    . VAL B 191 ? 1.5588 1.3588 1.0052 -0.4204 0.0078  -0.2137 191 VAL B CA    
3465 C C     . VAL B 191 ? 1.5623 1.3373 0.9912 -0.4387 0.0187  -0.2319 191 VAL B C     
3466 O O     . VAL B 191 ? 1.5987 1.3637 1.0475 -0.4277 0.0208  -0.2323 191 VAL B O     
3467 C CB    . VAL B 191 ? 1.5535 1.3266 1.0027 -0.4022 0.0231  -0.2209 191 VAL B CB    
3468 C CG1   . VAL B 191 ? 1.4751 1.2734 0.9423 -0.3851 0.0118  -0.2024 191 VAL B CG1   
3469 C CG2   . VAL B 191 ? 1.7163 1.4670 1.1297 -0.4220 0.0380  -0.2393 191 VAL B CG2   
3470 N N     . GLN B 192 ? 1.6643 1.4289 1.0555 -0.4675 0.0261  -0.2473 192 GLN B N     
3471 C CA    . GLN B 192 ? 1.6356 1.3775 1.0089 -0.4879 0.0358  -0.2646 192 GLN B CA    
3472 C C     . GLN B 192 ? 1.5803 1.3491 0.9662 -0.4947 0.0191  -0.2528 192 GLN B C     
3473 O O     . GLN B 192 ? 1.5471 1.2965 0.9343 -0.4998 0.0263  -0.2626 192 GLN B O     
3474 C CB    . GLN B 192 ? 1.6948 1.4273 1.0230 -0.5215 0.0440  -0.2818 192 GLN B CB    
3475 N N     . ARG B 193 ? 1.5912 1.4047 0.9879 -0.4948 -0.0026 -0.2310 193 ARG B N     
3476 C CA    . ARG B 193 ? 1.5219 1.3677 0.9315 -0.5021 -0.0202 -0.2164 193 ARG B CA    
3477 C C     . ARG B 193 ? 1.5152 1.3644 0.9663 -0.4718 -0.0242 -0.2041 193 ARG B C     
3478 O O     . ARG B 193 ? 1.4500 1.3003 0.9109 -0.4745 -0.0269 -0.2036 193 ARG B O     
3479 C CB    . ARG B 193 ? 1.3476 1.2413 0.7530 -0.5148 -0.0407 -0.1965 193 ARG B CB    
3480 N N     . TYR B 194 ? 1.5293 1.3827 1.0044 -0.4441 -0.0254 -0.1935 194 TYR B N     
3481 C CA    . TYR B 194 ? 1.4458 1.2976 0.9579 -0.4147 -0.0263 -0.1846 194 TYR B CA    
3482 C C     . TYR B 194 ? 1.4780 1.2902 0.9928 -0.4078 -0.0090 -0.2013 194 TYR B C     
3483 O O     . TYR B 194 ? 1.4109 1.2235 0.9423 -0.4030 -0.0109 -0.1989 194 TYR B O     
3484 C CB    . TYR B 194 ? 1.3848 1.2411 0.9155 -0.3897 -0.0271 -0.1746 194 TYR B CB    
3485 C CG    . TYR B 194 ? 1.3891 1.2594 0.9580 -0.3622 -0.0342 -0.1591 194 TYR B CG    
3486 C CD1   . TYR B 194 ? 1.4372 1.3407 1.0235 -0.3627 -0.0496 -0.1425 194 TYR B CD1   
3487 C CD2   . TYR B 194 ? 1.3451 1.1969 0.9326 -0.3362 -0.0255 -0.1604 194 TYR B CD2   
3488 C CE1   . TYR B 194 ? 1.3629 1.2786 0.9832 -0.3380 -0.0548 -0.1291 194 TYR B CE1   
3489 C CE2   . TYR B 194 ? 1.2891 1.1536 0.9091 -0.3128 -0.0316 -0.1473 194 TYR B CE2   
3490 C CZ    . TYR B 194 ? 1.3484 1.2438 0.9838 -0.3140 -0.0456 -0.1324 194 TYR B CZ    
3491 O OH    . TYR B 194 ? 1.4023 1.3093 1.0687 -0.2917 -0.0502 -0.1205 194 TYR B OH    
3492 N N     . LEU B 195 ? 1.4817 1.2602 0.9809 -0.4074 0.0085  -0.2175 195 LEU B N     
3493 C CA    . LEU B 195 ? 1.4656 1.2050 0.9696 -0.3990 0.0270  -0.2322 195 LEU B CA    
3494 C C     . LEU B 195 ? 1.4944 1.2242 0.9881 -0.4185 0.0299  -0.2416 195 LEU B C     
3495 O O     . LEU B 195 ? 1.5175 1.2342 1.0305 -0.4073 0.0350  -0.2424 195 LEU B O     
3496 C CB    . LEU B 195 ? 1.4724 1.1791 0.9570 -0.4006 0.0459  -0.2482 195 LEU B CB    
3497 C CG    . LEU B 195 ? 1.4449 1.1375 0.9464 -0.3741 0.0548  -0.2461 195 LEU B CG    
3498 C CD1   . LEU B 195 ? 1.3813 1.0364 0.8617 -0.3804 0.0771  -0.2650 195 LEU B CD1   
3499 C CD2   . LEU B 195 ? 1.4250 1.1120 0.9610 -0.3488 0.0562  -0.2391 195 LEU B CD2   
3500 N N     . HIS B 196 ? 1.5560 1.2930 1.0190 -0.4488 0.0265  -0.2484 196 HIS B N     
3501 C CA    . HIS B 196 ? 1.5789 1.3083 1.0305 -0.4702 0.0282  -0.2572 196 HIS B CA    
3502 C C     . HIS B 196 ? 1.5321 1.2957 1.0066 -0.4665 0.0095  -0.2392 196 HIS B C     
3503 O O     . HIS B 196 ? 1.5280 1.2814 1.0195 -0.4593 0.0128  -0.2399 196 HIS B O     
3504 C CB    . HIS B 196 ? 1.6480 1.3763 1.0579 -0.5061 0.0299  -0.2702 196 HIS B CB    
3505 C CG    . HIS B 196 ? 1.7227 1.4448 1.1184 -0.5312 0.0307  -0.2794 196 HIS B CG    
3506 N ND1   . HIS B 196 ? 1.7002 1.4594 1.0920 -0.5501 0.0113  -0.2677 196 HIS B ND1   
3507 C CD2   . HIS B 196 ? 1.7538 1.4392 1.1428 -0.5379 0.0495  -0.2962 196 HIS B CD2   
3508 C CE1   . HIS B 196 ? 1.7373 1.4828 1.1197 -0.5673 0.0177  -0.2773 196 HIS B CE1   
3509 N NE2   . HIS B 196 ? 1.8238 1.5257 1.2070 -0.5579 0.0413  -0.2930 196 HIS B NE2   
3510 N N     . ASP B 197 ? 1.5566 1.3614 1.0343 -0.4695 -0.0097 -0.2217 197 ASP B N     
3511 C CA    . ASP B 197 ? 1.5442 1.3829 1.0398 -0.4713 -0.0269 -0.2052 197 ASP B CA    
3512 C C     . ASP B 197 ? 1.4671 1.3064 1.0005 -0.4415 -0.0277 -0.1952 197 ASP B C     
3513 O O     . ASP B 197 ? 1.4632 1.3244 1.0124 -0.4421 -0.0385 -0.1841 197 ASP B O     
3514 C CB    . ASP B 197 ? 1.5695 1.4539 1.0660 -0.4776 -0.0466 -0.1855 197 ASP B CB    
3515 C CG    . ASP B 197 ? 1.5778 1.4719 1.0379 -0.5120 -0.0503 -0.1916 197 ASP B CG    
3516 O OD1   . ASP B 197 ? 1.5847 1.4450 1.0161 -0.5271 -0.0347 -0.2134 197 ASP B OD1   
3517 O OD2   . ASP B 197 ? 1.6531 1.5886 1.1138 -0.5241 -0.0683 -0.1743 197 ASP B OD2   
3518 N N     . PHE B 198 ? 1.4446 1.2625 0.9928 -0.4162 -0.0170 -0.1982 198 PHE B N     
3519 C CA    . PHE B 198 ? 1.4241 1.2411 1.0054 -0.3909 -0.0167 -0.1904 198 PHE B CA    
3520 C C     . PHE B 198 ? 1.4083 1.1845 0.9931 -0.3801 0.0025  -0.2048 198 PHE B C     
3521 O O     . PHE B 198 ? 1.3233 1.0957 0.9342 -0.3559 0.0050  -0.1991 198 PHE B O     
3522 C CB    . PHE B 198 ? 1.3699 1.2095 0.9756 -0.3667 -0.0259 -0.1738 198 PHE B CB    
3523 C CG    . PHE B 198 ? 1.4386 1.3201 1.0477 -0.3740 -0.0443 -0.1564 198 PHE B CG    
3524 C CD1   . PHE B 198 ? 1.4238 1.3314 1.0506 -0.3741 -0.0558 -0.1435 198 PHE B CD1   
3525 C CD2   . PHE B 198 ? 1.4969 1.3929 1.0926 -0.3808 -0.0498 -0.1516 198 PHE B CD2   
3526 C CE1   . PHE B 198 ? 1.5574 1.5048 1.1907 -0.3799 -0.0721 -0.1255 198 PHE B CE1   
3527 C CE2   . PHE B 198 ? 1.5594 1.4962 1.1614 -0.3870 -0.0668 -0.1329 198 PHE B CE2   
3528 C CZ    . PHE B 198 ? 1.6111 1.5736 1.2327 -0.3862 -0.0778 -0.1196 198 PHE B CZ    
3529 N N     . MET B 199 ? 1.4117 1.1581 0.9712 -0.3983 0.0165  -0.2230 199 MET B N     
3530 C CA    . MET B 199 ? 1.4165 1.1241 0.9803 -0.3913 0.0357  -0.2359 199 MET B CA    
3531 C C     . MET B 199 ? 1.3980 1.0922 0.9807 -0.3635 0.0443  -0.2335 199 MET B C     
3532 O O     . MET B 199 ? 1.2767 0.9677 0.8857 -0.3436 0.0464  -0.2274 199 MET B O     
3533 C CB    . MET B 199 ? 1.3126 1.0222 0.8944 -0.3899 0.0335  -0.2320 199 MET B CB    
3534 C CG    . MET B 199 ? 1.2438 0.9795 0.8164 -0.4127 0.0190  -0.2272 199 MET B CG    
3535 S SD    . MET B 199 ? 1.2544 0.9734 0.8366 -0.4190 0.0258  -0.2323 199 MET B SD    
3536 C CE    . MET B 199 ? 1.2918 1.0498 0.8668 -0.4429 0.0053  -0.2222 199 MET B CE    
3537 N N     . MET B 200 ? 1.4202 1.1082 0.9889 -0.3629 0.0489  -0.2378 200 MET B N     
3538 C CA    . MET B 200 ? 1.3343 1.0131 0.9199 -0.3377 0.0555  -0.2342 200 MET B CA    
3539 C C     . MET B 200 ? 1.3996 1.0447 0.9671 -0.3414 0.0749  -0.2495 200 MET B C     
3540 O O     . MET B 200 ? 1.5250 1.1522 1.0657 -0.3635 0.0843  -0.2641 200 MET B O     
3541 C CB    . MET B 200 ? 1.2958 1.0065 0.8902 -0.3269 0.0396  -0.2192 200 MET B CB    
3542 C CG    . MET B 200 ? 1.2779 1.0235 0.8892 -0.3240 0.0211  -0.2035 200 MET B CG    
3543 S SD    . MET B 200 ? 1.3700 1.1443 0.9913 -0.3101 0.0081  -0.1881 200 MET B SD    
3544 C CE    . MET B 200 ? 1.3953 1.2112 1.0145 -0.3255 -0.0124 -0.1741 200 MET B CE    
3545 N N     . THR B 201 ? 1.3992 1.0362 0.9811 -0.3199 0.0813  -0.2461 201 THR B N     
3546 C CA    . THR B 201 ? 1.4118 1.0167 0.9823 -0.3190 0.1012  -0.2587 201 THR B CA    
3547 C C     . THR B 201 ? 1.3868 0.9980 0.9714 -0.2973 0.0999  -0.2498 201 THR B C     
3548 O O     . THR B 201 ? 1.3743 0.9964 0.9865 -0.2765 0.0939  -0.2378 201 THR B O     
3549 C CB    . THR B 201 ? 1.4175 0.9886 0.9975 -0.3154 0.1204  -0.2676 201 THR B CB    
3550 O OG1   . THR B 201 ? 1.4337 0.9759 1.0125 -0.3071 0.1402  -0.2755 201 THR B OG1   
3551 C CG2   . THR B 201 ? 1.4032 0.9840 1.0166 -0.2962 0.1146  -0.2549 201 THR B CG2   
3552 N N     . MET B 202 ? 1.3982 1.0036 0.9631 -0.3032 0.1052  -0.2557 202 MET B N     
3553 C CA    . MET B 202 ? 1.3420 0.9491 0.9177 -0.2846 0.1068  -0.2492 202 MET B CA    
3554 C C     . MET B 202 ? 1.3480 0.9224 0.9336 -0.2720 0.1282  -0.2559 202 MET B C     
3555 O O     . MET B 202 ? 1.4241 0.9719 1.0037 -0.2800 0.1438  -0.2675 202 MET B O     
3556 C CB    . MET B 202 ? 1.3885 1.0039 0.9394 -0.2966 0.1040  -0.2519 202 MET B CB    
3557 C CG    . MET B 202 ? 1.3887 1.0380 0.9297 -0.3104 0.0835  -0.2436 202 MET B CG    
3558 S SD    . MET B 202 ? 1.5773 1.2367 1.0909 -0.3233 0.0813  -0.2451 202 MET B SD    
3559 C CE    . MET B 202 ? 1.4879 1.1828 0.9840 -0.3484 0.0609  -0.2385 202 MET B CE    
3560 N N     . VAL B 203 ? 1.2434 0.8187 0.8436 -0.2535 0.1301  -0.2489 203 VAL B N     
3561 C CA    . VAL B 203 ? 1.3182 0.8656 0.9319 -0.2397 0.1499  -0.2522 203 VAL B CA    
3562 C C     . VAL B 203 ? 1.3393 0.8851 0.9508 -0.2307 0.1546  -0.2503 203 VAL B C     
3563 O O     . VAL B 203 ? 1.3574 0.9259 0.9619 -0.2322 0.1403  -0.2442 203 VAL B O     
3564 C CB    . VAL B 203 ? 1.2456 0.7985 0.8922 -0.2209 0.1465  -0.2407 203 VAL B CB    
3565 C CG1   . VAL B 203 ? 1.2243 0.8012 0.8904 -0.2024 0.1328  -0.2259 203 VAL B CG1   
3566 C CG2   . VAL B 203 ? 1.2554 0.7789 0.9157 -0.2126 0.1676  -0.2446 203 VAL B CG2   
3567 N N     . SER B 204 ? 1.3365 0.8574 0.9544 -0.2220 0.1738  -0.2544 204 SER B N     
3568 C CA    . SER B 204 ? 1.3558 0.8727 0.9738 -0.2126 0.1806  -0.2525 204 SER B CA    
3569 C C     . SER B 204 ? 1.2977 0.8269 0.9477 -0.1888 0.1746  -0.2369 204 SER B C     
3570 O O     . SER B 204 ? 1.2554 0.7798 0.9279 -0.1783 0.1781  -0.2317 204 SER B O     
3571 C CB    . SER B 204 ? 1.4100 0.8921 1.0185 -0.2163 0.2070  -0.2654 204 SER B CB    
3572 O OG    . SER B 204 ? 1.4163 0.8835 1.0533 -0.1988 0.2199  -0.2596 204 SER B OG    
3573 N N     . ALA B 205 ? 1.2924 0.8385 0.9444 -0.1810 0.1651  -0.2288 205 ALA B N     
3574 C CA    . ALA B 205 ? 1.1792 0.7384 0.8598 -0.1602 0.1583  -0.2144 205 ALA B CA    
3575 C C     . ALA B 205 ? 1.2059 0.7435 0.9042 -0.1481 0.1771  -0.2134 205 ALA B C     
3576 O O     . ALA B 205 ? 1.2793 0.8249 1.0034 -0.1335 0.1735  -0.2024 205 ALA B O     
3577 C CB    . ALA B 205 ? 0.9908 0.5658 0.6679 -0.1558 0.1491  -0.2081 205 ALA B CB    
3578 N N     . GLU B 206 ? 1.1912 0.7031 0.8762 -0.1548 0.1970  -0.2243 206 GLU B N     
3579 C CA    . GLU B 206 ? 1.1922 0.6831 0.8959 -0.1426 0.2172  -0.2221 206 GLU B CA    
3580 C C     . GLU B 206 ? 1.2219 0.6975 0.9367 -0.1439 0.2267  -0.2247 206 GLU B C     
3581 O O     . GLU B 206 ? 1.2420 0.6988 0.9735 -0.1350 0.2450  -0.2226 206 GLU B O     
3582 C CB    . GLU B 206 ? 1.2544 0.7236 0.9402 -0.1483 0.2361  -0.2326 206 GLU B CB    
3583 C CG    . GLU B 206 ? 1.3427 0.7970 0.9956 -0.1706 0.2428  -0.2504 206 GLU B CG    
3584 C CD    . GLU B 206 ? 1.3822 0.8551 1.0083 -0.1840 0.2276  -0.2539 206 GLU B CD    
3585 O OE1   . GLU B 206 ? 1.3080 0.8077 0.9428 -0.1763 0.2083  -0.2419 206 GLU B OE1   
3586 O OE2   . GLU B 206 ? 1.5040 0.9645 1.1006 -0.2028 0.2355  -0.2684 206 GLU B OE2   
3587 N N     . ALA B 207 ? 1.1855 0.6699 0.8926 -0.1545 0.2148  -0.2280 207 ALA B N     
3588 C CA    . ALA B 207 ? 1.1625 0.6339 0.8807 -0.1562 0.2226  -0.2297 207 ALA B CA    
3589 C C     . ALA B 207 ? 1.2072 0.6968 0.9567 -0.1400 0.2124  -0.2133 207 ALA B C     
3590 O O     . ALA B 207 ? 1.1887 0.6654 0.9591 -0.1317 0.2254  -0.2085 207 ALA B O     
3591 C CB    . ALA B 207 ? 1.1104 0.5845 0.8069 -0.1754 0.2141  -0.2397 207 ALA B CB    
3592 N N     . TYR B 208 ? 1.1324 0.6508 0.8851 -0.1359 0.1909  -0.2050 208 TYR B N     
3593 C CA    . TYR B 208 ? 1.0888 0.6263 0.8679 -0.1230 0.1799  -0.1909 208 TYR B CA    
3594 C C     . TYR B 208 ? 1.0920 0.6240 0.8975 -0.1068 0.1913  -0.1800 208 TYR B C     
3595 O O     . TYR B 208 ? 1.0658 0.5994 0.8914 -0.1011 0.1931  -0.1725 208 TYR B O     
3596 C CB    . TYR B 208 ? 1.0941 0.6608 0.8712 -0.1210 0.1576  -0.1848 208 TYR B CB    
3597 C CG    . TYR B 208 ? 1.1605 0.7405 0.9310 -0.1306 0.1441  -0.1869 208 TYR B CG    
3598 C CD1   . TYR B 208 ? 1.1167 0.6991 0.9026 -0.1285 0.1433  -0.1827 208 TYR B CD1   
3599 C CD2   . TYR B 208 ? 1.1284 0.7199 0.8783 -0.1422 0.1324  -0.1919 208 TYR B CD2   
3600 C CE1   . TYR B 208 ? 1.1160 0.7112 0.8968 -0.1372 0.1313  -0.1839 208 TYR B CE1   
3601 C CE2   . TYR B 208 ? 1.1478 0.7531 0.8933 -0.1510 0.1202  -0.1923 208 TYR B CE2   
3602 C CZ    . TYR B 208 ? 1.1870 0.7938 0.9478 -0.1484 0.1199  -0.1887 208 TYR B CZ    
3603 O OH    . TYR B 208 ? 1.2257 0.8468 0.9832 -0.1568 0.1081  -0.1885 208 TYR B OH    
3604 N N     . PRO B 209 ? 1.1030 0.6314 0.9114 -0.0989 0.1981  -0.1768 209 PRO B N     
3605 C CA    . PRO B 209 ? 1.0883 0.6155 0.9243 -0.0838 0.2075  -0.1639 209 PRO B CA    
3606 C C     . PRO B 209 ? 1.0923 0.5986 0.9426 -0.0830 0.2260  -0.1635 209 PRO B C     
3607 O O     . PRO B 209 ? 1.1068 0.6238 0.9800 -0.0753 0.2227  -0.1516 209 PRO B O     
3608 C CB    . PRO B 209 ? 1.1200 0.6425 0.9510 -0.0793 0.2143  -0.1639 209 PRO B CB    
3609 C CG    . PRO B 209 ? 1.1354 0.6694 0.9414 -0.0884 0.1994  -0.1715 209 PRO B CG    
3610 C CD    . PRO B 209 ? 1.1430 0.6721 0.9310 -0.1034 0.1958  -0.1829 209 PRO B CD    
3611 N N     . PRO B 210 ? 1.1419 0.6188 0.9803 -0.0908 0.2459  -0.1756 210 PRO B N     
3612 C CA    . PRO B 210 ? 1.0911 0.5469 0.9445 -0.0902 0.2640  -0.1751 210 PRO B CA    
3613 C C     . PRO B 210 ? 1.1162 0.5800 0.9699 -0.0974 0.2530  -0.1760 210 PRO B C     
3614 O O     . PRO B 210 ? 1.0840 0.5457 0.9605 -0.0916 0.2588  -0.1670 210 PRO B O     
3615 C CB    . PRO B 210 ? 1.0511 0.4748 0.8818 -0.1020 0.2841  -0.1929 210 PRO B CB    
3616 C CG    . PRO B 210 ? 1.1277 0.5559 0.9414 -0.1022 0.2812  -0.1969 210 PRO B CG    
3617 C CD    . PRO B 210 ? 1.1834 0.6451 0.9940 -0.1009 0.2535  -0.1902 210 PRO B CD    
3618 N N     . LEU B 211 ? 1.0914 0.5655 0.9207 -0.1098 0.2372  -0.1856 211 LEU B N     
3619 C CA    . LEU B 211 ? 1.0609 0.5449 0.8888 -0.1175 0.2254  -0.1866 211 LEU B CA    
3620 C C     . LEU B 211 ? 1.0877 0.5962 0.9423 -0.1050 0.2131  -0.1697 211 LEU B C     
3621 O O     . LEU B 211 ? 1.1245 0.6321 0.9930 -0.1051 0.2150  -0.1653 211 LEU B O     
3622 C CB    . LEU B 211 ? 1.0975 0.5951 0.8981 -0.1304 0.2083  -0.1959 211 LEU B CB    
3623 C CG    . LEU B 211 ? 1.0773 0.5539 0.8552 -0.1490 0.2169  -0.2119 211 LEU B CG    
3624 C CD1   . LEU B 211 ? 1.0773 0.5695 0.8285 -0.1629 0.2002  -0.2195 211 LEU B CD1   
3625 C CD2   . LEU B 211 ? 1.1201 0.5939 0.9136 -0.1497 0.2188  -0.2082 211 LEU B CD2   
3626 N N     . LEU B 212 ? 1.0535 0.5848 0.9144 -0.0954 0.1999  -0.1605 212 LEU B N     
3627 C CA    . LEU B 212 ? 1.0235 0.5786 0.9078 -0.0850 0.1886  -0.1452 212 LEU B CA    
3628 C C     . LEU B 212 ? 1.0536 0.6021 0.9659 -0.0735 0.2031  -0.1323 212 LEU B C     
3629 O O     . LEU B 212 ? 1.0840 0.6422 1.0157 -0.0696 0.2009  -0.1220 212 LEU B O     
3630 C CB    . LEU B 212 ? 1.0258 0.6056 0.9078 -0.0794 0.1713  -0.1402 212 LEU B CB    
3631 C CG    . LEU B 212 ? 1.0329 0.6224 0.8913 -0.0900 0.1564  -0.1501 212 LEU B CG    
3632 C CD1   . LEU B 212 ? 1.0084 0.6103 0.8585 -0.0866 0.1467  -0.1494 212 LEU B CD1   
3633 C CD2   . LEU B 212 ? 0.9742 0.5829 0.8384 -0.0917 0.1423  -0.1461 212 LEU B CD2   
3634 N N     . ARG B 213 ? 1.0412 0.5766 0.9594 -0.0675 0.2171  -0.1302 213 ARG B N     
3635 C CA    . ARG B 213 ? 1.0376 0.5687 0.9860 -0.0559 0.2313  -0.1152 213 ARG B CA    
3636 C C     . ARG B 213 ? 1.0819 0.5961 1.0394 -0.0602 0.2435  -0.1163 213 ARG B C     
3637 O O     . ARG B 213 ? 1.1289 0.6517 1.1139 -0.0522 0.2463  -0.1006 213 ARG B O     
3638 C CB    . ARG B 213 ? 1.0277 0.5420 0.9780 -0.0502 0.2482  -0.1154 213 ARG B CB    
3639 C CG    . ARG B 213 ? 1.0934 0.6268 1.0423 -0.0436 0.2371  -0.1096 213 ARG B CG    
3640 C CD    . ARG B 213 ? 1.0951 0.6131 1.0495 -0.0370 0.2548  -0.1076 213 ARG B CD    
3641 N NE    . ARG B 213 ? 1.0486 0.5339 0.9866 -0.0450 0.2741  -0.1234 213 ARG B NE    
3642 C CZ    . ARG B 213 ? 1.0782 0.5517 0.9911 -0.0515 0.2776  -0.1370 213 ARG B CZ    
3643 N NH1   . ARG B 213 ? 1.1769 0.6690 1.0742 -0.0535 0.2596  -0.1393 213 ARG B NH1   
3644 N NH2   . ARG B 213 ? 1.1830 0.6261 1.0867 -0.0563 0.2998  -0.1484 213 ARG B NH2   
3645 N N     . GLY B 214 ? 1.0622 0.5517 0.9956 -0.0740 0.2516  -0.1352 214 GLY B N     
3646 C CA    . GLY B 214 ? 1.0277 0.5015 0.9692 -0.0792 0.2620  -0.1367 214 GLY B CA    
3647 C C     . GLY B 214 ? 1.1369 0.6354 1.0903 -0.0786 0.2453  -0.1268 214 GLY B C     
3648 O O     . GLY B 214 ? 1.1866 0.6850 1.1651 -0.0732 0.2523  -0.1147 214 GLY B O     
3649 N N     . ALA B 215 ? 1.1515 0.6724 1.0887 -0.0837 0.2236  -0.1307 215 ALA B N     
3650 C CA    . ALA B 215 ? 1.0816 0.6279 1.0280 -0.0832 0.2070  -0.1223 215 ALA B CA    
3651 C C     . ALA B 215 ? 1.0291 0.5997 1.0027 -0.0694 0.2012  -0.1023 215 ALA B C     
3652 O O     . ALA B 215 ? 1.0169 0.6091 0.9997 -0.0686 0.1889  -0.0943 215 ALA B O     
3653 C CB    . ALA B 215 ? 1.0830 0.6465 1.0059 -0.0909 0.1870  -0.1312 215 ALA B CB    
3654 N N     . GLY B 216 ? 1.0239 0.5930 1.0098 -0.0593 0.2093  -0.0940 216 GLY B N     
3655 C CA    . GLY B 216 ? 1.0654 0.6602 1.0749 -0.0481 0.2024  -0.0750 216 GLY B CA    
3656 C C     . GLY B 216 ? 1.0482 0.6688 1.0482 -0.0463 0.1829  -0.0742 216 GLY B C     
3657 O O     . GLY B 216 ? 1.0181 0.6641 1.0331 -0.0409 0.1728  -0.0608 216 GLY B O     
3658 N N     . LEU B 217 ? 0.9969 0.6116 0.9722 -0.0511 0.1779  -0.0882 217 LEU B N     
3659 C CA    . LEU B 217 ? 0.9516 0.5868 0.9165 -0.0499 0.1611  -0.0892 217 LEU B CA    
3660 C C     . LEU B 217 ? 1.0045 0.6302 0.9606 -0.0470 0.1664  -0.0932 217 LEU B C     
3661 O O     . LEU B 217 ? 1.0632 0.6650 1.0082 -0.0510 0.1794  -0.1028 217 LEU B O     
3662 C CB    . LEU B 217 ? 0.9694 0.6103 0.9127 -0.0592 0.1475  -0.1015 217 LEU B CB    
3663 C CG    . LEU B 217 ? 1.0240 0.6666 0.9693 -0.0655 0.1451  -0.1026 217 LEU B CG    
3664 C CD1   . LEU B 217 ? 1.0404 0.6851 0.9624 -0.0754 0.1343  -0.1155 217 LEU B CD1   
3665 C CD2   . LEU B 217 ? 0.9726 0.6399 0.9372 -0.0598 0.1363  -0.0889 217 LEU B CD2   
3666 N N     . TRP B 218 ? 1.0256 0.6700 0.9850 -0.0412 0.1562  -0.0866 218 TRP B N     
3667 C CA    . TRP B 218 ? 1.0063 0.6456 0.9573 -0.0385 0.1585  -0.0894 218 TRP B CA    
3668 C C     . TRP B 218 ? 0.9796 0.6246 0.9073 -0.0446 0.1449  -0.1008 218 TRP B C     
3669 O O     . TRP B 218 ? 0.9634 0.6276 0.8901 -0.0454 0.1299  -0.0996 218 TRP B O     
3670 C CB    . TRP B 218 ? 0.9842 0.6408 0.9541 -0.0291 0.1560  -0.0742 218 TRP B CB    
3671 C CG    . TRP B 218 ? 1.0949 0.7467 1.0896 -0.0223 0.1707  -0.0605 218 TRP B CG    
3672 C CD1   . TRP B 218 ? 1.1138 0.7451 1.1153 -0.0230 0.1869  -0.0615 218 TRP B CD1   
3673 C CD2   . TRP B 218 ? 1.0613 0.7294 1.0787 -0.0139 0.1713  -0.0428 218 TRP B CD2   
3674 N NE1   . TRP B 218 ? 1.0992 0.7330 1.1280 -0.0145 0.1980  -0.0446 218 TRP B NE1   
3675 C CE2   . TRP B 218 ? 1.0575 0.7152 1.0965 -0.0091 0.1881  -0.0323 218 TRP B CE2   
3676 C CE3   . TRP B 218 ? 0.9952 0.6859 1.0171 -0.0108 0.1595  -0.0344 218 TRP B CE3   
3677 C CZ2   . TRP B 218 ? 1.0609 0.7326 1.1269 -0.0009 0.1928  -0.0121 218 TRP B CZ2   
3678 C CZ3   . TRP B 218 ? 1.0241 0.7284 1.0706 -0.0040 0.1637  -0.0156 218 TRP B CZ3   
3679 C CH2   . TRP B 218 ? 1.0593 0.7553 1.1282 0.0010  0.1798  -0.0038 218 TRP B CH2   
3680 N N     . LEU B 219 ? 0.9753 0.6044 0.8851 -0.0490 0.1506  -0.1113 219 LEU B N     
3681 C CA    . LEU B 219 ? 0.9909 0.6280 0.8816 -0.0537 0.1377  -0.1189 219 LEU B CA    
3682 C C     . LEU B 219 ? 0.9749 0.6320 0.8746 -0.0461 0.1268  -0.1101 219 LEU B C     
3683 O O     . LEU B 219 ? 0.9610 0.6204 0.8755 -0.0384 0.1321  -0.1005 219 LEU B O     
3684 C CB    . LEU B 219 ? 0.9405 0.5600 0.8118 -0.0592 0.1459  -0.1292 219 LEU B CB    
3685 C CG    . LEU B 219 ? 0.9183 0.5487 0.7724 -0.0633 0.1323  -0.1343 219 LEU B CG    
3686 C CD1   . LEU B 219 ? 0.9966 0.6375 0.8426 -0.0708 0.1199  -0.1387 219 LEU B CD1   
3687 C CD2   . LEU B 219 ? 0.9333 0.5488 0.7682 -0.0692 0.1401  -0.1431 219 LEU B CD2   
3688 N N     . GLU B 220 ? 0.9431 0.6149 0.8349 -0.0485 0.1120  -0.1128 220 GLU B N     
3689 C CA    . GLU B 220 ? 1.0073 0.6958 0.9050 -0.0429 0.1020  -0.1067 220 GLU B CA    
3690 C C     . GLU B 220 ? 0.9509 0.6407 0.8330 -0.0456 0.0949  -0.1128 220 GLU B C     
3691 O O     . GLU B 220 ? 0.8988 0.5937 0.7839 -0.0409 0.0925  -0.1088 220 GLU B O     
3692 C CB    . GLU B 220 ? 0.9575 0.6648 0.8641 -0.0420 0.0910  -0.1025 220 GLU B CB    
3693 C CG    . GLU B 220 ? 0.9308 0.6541 0.8462 -0.0367 0.0834  -0.0956 220 GLU B CG    
3694 C CD    . GLU B 220 ? 1.0872 0.8281 1.0072 -0.0375 0.0728  -0.0943 220 GLU B CD    
3695 O OE1   . GLU B 220 ? 1.1777 0.9228 1.0881 -0.0407 0.0649  -0.1008 220 GLU B OE1   
3696 O OE2   . GLU B 220 ? 1.0392 0.7906 0.9729 -0.0351 0.0730  -0.0860 220 GLU B OE2   
3697 N N     . GLU B 221 ? 0.9745 0.6608 0.8410 -0.0534 0.0916  -0.1214 221 GLU B N     
3698 C CA    . GLU B 221 ? 0.9863 0.6785 0.8402 -0.0562 0.0828  -0.1249 221 GLU B CA    
3699 C C     . GLU B 221 ? 0.9844 0.6684 0.8201 -0.0669 0.0840  -0.1337 221 GLU B C     
3700 O O     . GLU B 221 ? 0.9841 0.6712 0.8182 -0.0721 0.0806  -0.1363 221 GLU B O     
3701 C CB    . GLU B 221 ? 0.9920 0.7033 0.8527 -0.0534 0.0693  -0.1214 221 GLU B CB    
3702 C CG    . GLU B 221 ? 1.0047 0.7235 0.8575 -0.0541 0.0606  -0.1222 221 GLU B CG    
3703 C CD    . GLU B 221 ? 0.9867 0.7211 0.8420 -0.0547 0.0489  -0.1216 221 GLU B CD    
3704 O OE1   . GLU B 221 ? 0.9658 0.7066 0.8284 -0.0545 0.0468  -0.1210 221 GLU B OE1   
3705 O OE2   . GLU B 221 ? 1.0619 0.8027 0.9130 -0.0551 0.0425  -0.1211 221 GLU B OE2   
3706 N N     . PHE B 222 ? 0.9967 0.6708 0.8183 -0.0711 0.0891  -0.1382 222 PHE B N     
3707 C CA    . PHE B 222 ? 0.9893 0.6609 0.7911 -0.0829 0.0870  -0.1459 222 PHE B CA    
3708 C C     . PHE B 222 ? 1.0579 0.7434 0.8539 -0.0832 0.0757  -0.1431 222 PHE B C     
3709 O O     . PHE B 222 ? 0.9890 0.6754 0.7885 -0.0770 0.0762  -0.1392 222 PHE B O     
3710 C CB    . PHE B 222 ? 1.0192 0.6697 0.8065 -0.0897 0.1015  -0.1537 222 PHE B CB    
3711 C CG    . PHE B 222 ? 1.0379 0.6869 0.8020 -0.1042 0.0993  -0.1620 222 PHE B CG    
3712 C CD1   . PHE B 222 ? 1.0212 0.6775 0.7727 -0.1080 0.0937  -0.1617 222 PHE B CD1   
3713 C CD2   . PHE B 222 ? 1.0882 0.7294 0.8430 -0.1150 0.1027  -0.1693 222 PHE B CD2   
3714 C CE1   . PHE B 222 ? 1.0981 0.7561 0.8279 -0.1227 0.0908  -0.1679 222 PHE B CE1   
3715 C CE2   . PHE B 222 ? 1.0838 0.7254 0.8161 -0.1303 0.1001  -0.1766 222 PHE B CE2   
3716 C CZ    . PHE B 222 ? 1.0973 0.7482 0.8168 -0.1345 0.0939  -0.1756 222 PHE B CZ    
3717 N N     . LEU B 223 ? 1.0382 0.7352 0.8265 -0.0907 0.0658  -0.1443 223 LEU B N     
3718 C CA    . LEU B 223 ? 1.0453 0.7577 0.8315 -0.0906 0.0548  -0.1395 223 LEU B CA    
3719 C C     . LEU B 223 ? 1.1018 0.8196 0.8701 -0.1044 0.0501  -0.1429 223 LEU B C     
3720 O O     . LEU B 223 ? 1.1175 0.8416 0.8847 -0.1105 0.0455  -0.1441 223 LEU B O     
3721 C CB    . LEU B 223 ? 0.9847 0.7131 0.7884 -0.0822 0.0448  -0.1327 223 LEU B CB    
3722 C CG    . LEU B 223 ? 1.0013 0.7413 0.8122 -0.0756 0.0373  -0.1260 223 LEU B CG    
3723 C CD1   . LEU B 223 ? 1.0057 0.7360 0.8156 -0.0710 0.0439  -0.1252 223 LEU B CD1   
3724 C CD2   . LEU B 223 ? 1.0296 0.7800 0.8583 -0.0669 0.0317  -0.1217 223 LEU B CD2   
3725 N N     . ASP B 224 ? 1.1007 0.8175 0.8548 -0.1099 0.0509  -0.1436 224 ASP B N     
3726 C CA    . ASP B 224 ? 1.0037 0.7301 0.7404 -0.1240 0.0447  -0.1446 224 ASP B CA    
3727 C C     . ASP B 224 ? 1.0109 0.7611 0.7586 -0.1207 0.0302  -0.1342 224 ASP B C     
3728 O O     . ASP B 224 ? 1.0725 0.8308 0.8270 -0.1141 0.0260  -0.1270 224 ASP B O     
3729 C CB    . ASP B 224 ? 1.0748 0.7936 0.7935 -0.1308 0.0509  -0.1480 224 ASP B CB    
3730 C CG    . ASP B 224 ? 1.1159 0.8450 0.8132 -0.1482 0.0453  -0.1495 224 ASP B CG    
3731 O OD1   . ASP B 224 ? 1.0550 0.8042 0.7560 -0.1520 0.0329  -0.1428 224 ASP B OD1   
3732 O OD2   . ASP B 224 ? 1.1690 0.8868 0.8456 -0.1587 0.0538  -0.1571 224 ASP B OD2   
3733 N N     . ILE B 225 ? 0.9969 0.7584 0.7480 -0.1250 0.0233  -0.1327 225 ILE B N     
3734 C CA    . ILE B 225 ? 1.0642 0.8481 0.8277 -0.1216 0.0110  -0.1221 225 ILE B CA    
3735 C C     . ILE B 225 ? 1.0861 0.8857 0.8357 -0.1364 0.0033  -0.1187 225 ILE B C     
3736 O O     . ILE B 225 ? 1.0974 0.9168 0.8567 -0.1367 -0.0065 -0.1100 225 ILE B O     
3737 C CB    . ILE B 225 ? 0.9903 0.7799 0.7717 -0.1138 0.0078  -0.1201 225 ILE B CB    
3738 C CG1   . ILE B 225 ? 1.0093 0.7973 0.7827 -0.1244 0.0085  -0.1258 225 ILE B CG1   
3739 C CG2   . ILE B 225 ? 0.9630 0.7393 0.7564 -0.1013 0.0150  -0.1229 225 ILE B CG2   
3740 C CD1   . ILE B 225 ? 0.9741 0.7716 0.7644 -0.1181 0.0041  -0.1224 225 ILE B CD1   
3741 N N     . SER B 226 ? 1.1101 0.9017 0.8373 -0.1492 0.0081  -0.1250 226 SER B N     
3742 C CA    . SER B 226 ? 1.1131 0.9209 0.8241 -0.1665 0.0006  -0.1222 226 SER B CA    
3743 C C     . SER B 226 ? 1.1430 0.9749 0.8628 -0.1640 -0.0105 -0.1073 226 SER B C     
3744 O O     . SER B 226 ? 1.1353 0.9893 0.8578 -0.1711 -0.0207 -0.0985 226 SER B O     
3745 C CB    . SER B 226 ? 1.1065 0.8992 0.7900 -0.1816 0.0095  -0.1335 226 SER B CB    
3746 O OG    . SER B 226 ? 1.1026 0.8688 0.7835 -0.1786 0.0229  -0.1459 226 SER B OG    
3747 N N     . ASP B 227 ? 1.1250 0.9536 0.8507 -0.1541 -0.0083 -0.1034 227 ASP B N     
3748 C CA    . ASP B 227 ? 1.1355 0.9858 0.8700 -0.1519 -0.0177 -0.0886 227 ASP B CA    
3749 C C     . ASP B 227 ? 1.1204 0.9870 0.8818 -0.1403 -0.0257 -0.0771 227 ASP B C     
3750 O O     . ASP B 227 ? 1.1006 0.9876 0.8727 -0.1388 -0.0338 -0.0629 227 ASP B O     
3751 C CB    . ASP B 227 ? 1.2299 1.0709 0.9657 -0.1435 -0.0126 -0.0875 227 ASP B CB    
3752 C CG    . ASP B 227 ? 1.2725 1.0965 0.9829 -0.1538 -0.0029 -0.0989 227 ASP B CG    
3753 O OD1   . ASP B 227 ? 1.1854 1.0155 0.8741 -0.1714 -0.0044 -0.1018 227 ASP B OD1   
3754 O OD2   . ASP B 227 ? 1.3044 1.1094 1.0166 -0.1447 0.0066  -0.1049 227 ASP B OD2   
3755 N N     . GLN B 228 ? 1.1046 0.9626 0.8777 -0.1319 -0.0229 -0.0824 228 GLN B N     
3756 C CA    . GLN B 228 ? 1.0660 0.9373 0.8636 -0.1211 -0.0284 -0.0734 228 GLN B CA    
3757 C C     . GLN B 228 ? 1.0437 0.9267 0.8421 -0.1285 -0.0333 -0.0727 228 GLN B C     
3758 O O     . GLN B 228 ? 1.0832 0.9792 0.9017 -0.1205 -0.0378 -0.0647 228 GLN B O     
3759 C CB    . GLN B 228 ? 1.0337 0.8890 0.8461 -0.1052 -0.0218 -0.0789 228 GLN B CB    
3760 C CG    . GLN B 228 ? 1.0058 0.8513 0.8216 -0.0964 -0.0177 -0.0781 228 GLN B CG    
3761 C CD    . GLN B 228 ? 1.1144 0.9428 0.9100 -0.1027 -0.0102 -0.0872 228 GLN B CD    
3762 O OE1   . GLN B 228 ? 1.2647 1.0938 1.0540 -0.1043 -0.0100 -0.0836 228 GLN B OE1   
3763 N NE2   . GLN B 228 ? 1.0654 0.8784 0.8516 -0.1061 -0.0032 -0.0985 228 GLN B NE2   
3764 N N     . THR B 229 ? 1.0326 0.9103 0.8100 -0.1436 -0.0317 -0.0813 229 THR B N     
3765 C CA    . THR B 229 ? 1.0712 0.9558 0.8486 -0.1508 -0.0349 -0.0829 229 THR B CA    
3766 C C     . THR B 229 ? 1.1185 1.0201 0.8794 -0.1706 -0.0421 -0.0791 229 THR B C     
3767 O O     . THR B 229 ? 1.0959 1.0196 0.8670 -0.1737 -0.0507 -0.0690 229 THR B O     
3768 C CB    . THR B 229 ? 1.0540 0.9141 0.8232 -0.1512 -0.0251 -0.0981 229 THR B CB    
3769 O OG1   . THR B 229 ? 1.0962 0.9365 0.8474 -0.1553 -0.0164 -0.1075 229 THR B OG1   
3770 C CG2   . THR B 229 ? 1.0147 0.8673 0.8046 -0.1340 -0.0214 -0.0990 229 THR B CG2   
3771 N N     . LEU B 230 ? 1.1524 1.0447 0.8877 -0.1847 -0.0384 -0.0870 230 LEU B N     
3772 C CA    . LEU B 230 ? 1.1305 1.0334 0.8448 -0.2069 -0.0430 -0.0884 230 LEU B CA    
3773 C C     . LEU B 230 ? 1.1649 1.1020 0.8843 -0.2142 -0.0563 -0.0703 230 LEU B C     
3774 O O     . LEU B 230 ? 1.1329 1.0902 0.8597 -0.2201 -0.0645 -0.0622 230 LEU B O     
3775 C CB    . LEU B 230 ? 1.0705 0.9524 0.7548 -0.2207 -0.0336 -0.1031 230 LEU B CB    
3776 C CG    . LEU B 230 ? 1.0726 0.9209 0.7496 -0.2174 -0.0191 -0.1208 230 LEU B CG    
3777 C CD1   . LEU B 230 ? 1.1484 0.9774 0.7978 -0.2299 -0.0088 -0.1336 230 LEU B CD1   
3778 C CD2   . LEU B 230 ? 1.0468 0.8912 0.7242 -0.2235 -0.0185 -0.1267 230 LEU B CD2   
3779 N N     . GLU B 231 ? 1.2398 1.1852 0.9579 -0.2131 -0.0586 -0.0621 231 GLU B N     
3780 C CA    . GLU B 231 ? 1.2461 1.2252 0.9661 -0.2232 -0.0709 -0.0441 231 GLU B CA    
3781 C C     . GLU B 231 ? 1.2040 1.2071 0.9545 -0.2128 -0.0795 -0.0271 231 GLU B C     
3782 O O     . GLU B 231 ? 1.2213 1.2466 0.9717 -0.2249 -0.0879 -0.0192 231 GLU B O     
3783 C CB    . GLU B 231 ? 1.2547 1.2385 0.9728 -0.2205 -0.0714 -0.0363 231 GLU B CB    
3784 C CG    . GLU B 231 ? 1.3136 1.3361 1.0405 -0.2282 -0.0848 -0.0133 231 GLU B CG    
3785 C CD    . GLU B 231 ? 1.4762 1.5079 1.1950 -0.2323 -0.0867 -0.0049 231 GLU B CD    
3786 O OE1   . GLU B 231 ? 1.5491 1.5572 1.2503 -0.2323 -0.0774 -0.0185 231 GLU B OE1   
3787 O OE2   . GLU B 231 ? 1.4961 1.5604 1.2276 -0.2354 -0.0974 0.0167  231 GLU B OE2   
3788 N N     . LYS B 232 ? 1.1848 1.1833 0.9619 -0.1906 -0.0768 -0.0219 232 LYS B N     
3789 C CA    . LYS B 232 ? 1.1420 1.1657 0.9493 -0.1805 -0.0842 -0.0029 232 LYS B CA    
3790 C C     . LYS B 232 ? 1.1888 1.2217 1.0031 -0.1838 -0.0874 -0.0026 232 LYS B C     
3791 O O     . LYS B 232 ? 1.1944 1.2560 1.0262 -0.1848 -0.0959 0.0148  232 LYS B O     
3792 C CB    . LYS B 232 ? 1.1000 1.1119 0.9323 -0.1569 -0.0783 -0.0009 232 LYS B CB    
3793 C CG    . LYS B 232 ? 1.1040 1.1403 0.9689 -0.1454 -0.0837 0.0195  232 LYS B CG    
3794 C CD    . LYS B 232 ? 1.0860 1.1108 0.9720 -0.1252 -0.0775 0.0221  232 LYS B CD    
3795 C CE    . LYS B 232 ? 1.1756 1.2270 1.0898 -0.1182 -0.0830 0.0454  232 LYS B CE    
3796 N NZ    . LYS B 232 ? 1.0906 1.1648 1.0205 -0.1199 -0.0883 0.0562  232 LYS B NZ    
3797 N N     . THR B 233 ? 1.1970 1.2066 0.9995 -0.1853 -0.0805 -0.0206 233 THR B N     
3798 C CA    . THR B 233 ? 1.1835 1.2009 0.9871 -0.1926 -0.0837 -0.0218 233 THR B CA    
3799 C C     . THR B 233 ? 1.2208 1.2602 1.0062 -0.2167 -0.0928 -0.0159 233 THR B C     
3800 O O     . THR B 233 ? 1.2560 1.3230 1.0537 -0.2217 -0.1017 -0.0018 233 THR B O     
3801 C CB    . THR B 233 ? 1.2037 1.1907 0.9949 -0.1921 -0.0739 -0.0424 233 THR B CB    
3802 O OG1   . THR B 233 ? 1.1225 1.0861 0.9209 -0.1747 -0.0647 -0.0502 233 THR B OG1   
3803 C CG2   . THR B 233 ? 1.1609 1.1543 0.9640 -0.1910 -0.0757 -0.0419 233 THR B CG2   
3804 N N     . PHE B 234 ? 1.2628 1.2905 1.0182 -0.2324 -0.0902 -0.0267 234 PHE B N     
3805 C CA    . PHE B 234 ? 1.2435 1.2881 0.9754 -0.2587 -0.0974 -0.0250 234 PHE B CA    
3806 C C     . PHE B 234 ? 1.2959 1.3814 1.0416 -0.2635 -0.1108 0.0000  234 PHE B C     
3807 O O     . PHE B 234 ? 1.3703 1.4813 1.1183 -0.2762 -0.1200 0.0102  234 PHE B O     
3808 C CB    . PHE B 234 ? 1.2432 1.2666 0.9416 -0.2725 -0.0903 -0.0408 234 PHE B CB    
3809 C CG    . PHE B 234 ? 1.2099 1.1959 0.8913 -0.2741 -0.0772 -0.0648 234 PHE B CG    
3810 C CD1   . PHE B 234 ? 1.2239 1.2042 0.9079 -0.2770 -0.0760 -0.0713 234 PHE B CD1   
3811 C CD2   . PHE B 234 ? 1.2573 1.2149 0.9212 -0.2732 -0.0656 -0.0797 234 PHE B CD2   
3812 C CE1   . PHE B 234 ? 1.1817 1.1283 0.8521 -0.2786 -0.0635 -0.0917 234 PHE B CE1   
3813 C CE2   . PHE B 234 ? 1.2119 1.1358 0.8627 -0.2743 -0.0526 -0.1000 234 PHE B CE2   
3814 C CZ    . PHE B 234 ? 1.1100 1.0286 0.7645 -0.2770 -0.0516 -0.1056 234 PHE B CZ    
3815 N N     . ARG B 235 ? 1.2745 1.3674 1.0326 -0.2523 -0.1118 0.0116  235 ARG B N     
3816 C CA    . ARG B 235 ? 1.2697 1.4017 1.0459 -0.2541 -0.1236 0.0380  235 ARG B CA    
3817 C C     . ARG B 235 ? 1.3407 1.4946 1.1477 -0.2452 -0.1291 0.0531  235 ARG B C     
3818 O O     . ARG B 235 ? 1.3867 1.5763 1.2010 -0.2565 -0.1403 0.0723  235 ARG B O     
3819 C CB    . ARG B 235 ? 1.1601 1.2916 0.9514 -0.2382 -0.1214 0.0477  235 ARG B CB    
3820 N N     . LEU B 236 ? 1.3540 1.4881 1.1787 -0.2259 -0.1213 0.0447  236 LEU B N     
3821 C CA    . LEU B 236 ? 1.3206 1.4747 1.1762 -0.2154 -0.1250 0.0592  236 LEU B CA    
3822 C C     . LEU B 236 ? 1.3304 1.4923 1.1769 -0.2303 -0.1292 0.0550  236 LEU B C     
3823 O O     . LEU B 236 ? 1.3275 1.5204 1.1927 -0.2327 -0.1373 0.0732  236 LEU B O     
3824 C CB    . LEU B 236 ? 1.2936 1.4257 1.1725 -0.1893 -0.1148 0.0530  236 LEU B CB    
3825 C CG    . LEU B 236 ? 1.3192 1.4702 1.2348 -0.1710 -0.1158 0.0741  236 LEU B CG    
3826 C CD1   . LEU B 236 ? 1.2970 1.4250 1.2322 -0.1480 -0.1049 0.0650  236 LEU B CD1   
3827 C CD2   . LEU B 236 ? 1.2598 1.4507 1.1955 -0.1769 -0.1258 0.0976  236 LEU B CD2   
3828 N N     . LEU B 237 ? 1.3456 1.4803 1.1653 -0.2400 -0.1233 0.0323  237 LEU B N     
3829 C CA    . LEU B 237 ? 1.4420 1.5822 1.2541 -0.2538 -0.1265 0.0280  237 LEU B CA    
3830 C C     . LEU B 237 ? 1.4771 1.6470 1.2723 -0.2808 -0.1384 0.0384  237 LEU B C     
3831 O O     . LEU B 237 ? 1.4616 1.6584 1.2672 -0.2888 -0.1468 0.0510  237 LEU B O     
3832 C CB    . LEU B 237 ? 1.4522 1.5548 1.2422 -0.2570 -0.1161 0.0018  237 LEU B CB    
3833 C CG    . LEU B 237 ? 1.5118 1.6234 1.2960 -0.2723 -0.1205 -0.0001 237 LEU B CG    
3834 C CD1   . LEU B 237 ? 1.4667 1.5912 1.2835 -0.2558 -0.1217 0.0104  237 LEU B CD1   
3835 C CD2   . LEU B 237 ? 1.5323 1.6115 1.2882 -0.2845 -0.1119 -0.0241 237 LEU B CD2   
3836 N N     . SER B 238 ? 1.4734 1.6400 1.2416 -0.2961 -0.1391 0.0334  238 SER B N     
3837 C CA    . SER B 238 ? 1.4982 1.6973 1.2509 -0.3223 -0.1513 0.0458  238 SER B CA    
3838 C C     . SER B 238 ? 1.4928 1.7353 1.2773 -0.3161 -0.1628 0.0771  238 SER B C     
3839 O O     . SER B 238 ? 1.5259 1.8024 1.3112 -0.3334 -0.1742 0.0923  238 SER B O     
3840 C CB    . SER B 238 ? 1.5166 1.7051 1.2361 -0.3381 -0.1492 0.0359  238 SER B CB    
3841 O OG    . SER B 238 ? 1.4477 1.6536 1.1811 -0.3289 -0.1530 0.0531  238 SER B OG    
3842 N N     . GLU B 239 ? 1.4737 1.7158 1.2865 -0.2914 -0.1593 0.0877  239 GLU B N     
3843 C CA    . GLU B 239 ? 1.4334 1.7149 1.2808 -0.2831 -0.1681 0.1183  239 GLU B CA    
3844 C C     . GLU B 239 ? 1.4007 1.6957 1.2765 -0.2734 -0.1694 0.1275  239 GLU B C     
3845 O O     . GLU B 239 ? 1.3805 1.7150 1.2750 -0.2794 -0.1798 0.1518  239 GLU B O     
3846 C CB    . GLU B 239 ? 1.3309 1.6052 1.2003 -0.2598 -0.1624 0.1259  239 GLU B CB    
3847 N N     . ARG B 240 ? 1.4374 1.7014 1.3179 -0.2580 -0.1590 0.1096  240 ARG B N     
3848 C CA    . ARG B 240 ? 1.4155 1.6911 1.3178 -0.2519 -0.1599 0.1156  240 ARG B CA    
3849 C C     . ARG B 240 ? 1.4626 1.7606 1.3476 -0.2789 -0.1703 0.1189  240 ARG B C     
3850 O O     . ARG B 240 ? 1.4631 1.7971 1.3695 -0.2820 -0.1790 0.1408  240 ARG B O     
3851 C CB    . ARG B 240 ? 1.3037 1.5414 1.2067 -0.2357 -0.1474 0.0932  240 ARG B CB    
3852 N N     . ILE B 241 ? 1.4814 1.7593 1.3277 -0.2995 -0.1694 0.0982  241 ILE B N     
3853 C CA    . ILE B 241 ? 1.5162 1.8103 1.3425 -0.3270 -0.1778 0.0975  241 ILE B CA    
3854 C C     . ILE B 241 ? 1.5678 1.9090 1.3963 -0.3455 -0.1928 0.1235  241 ILE B C     
3855 O O     . ILE B 241 ? 1.5150 1.8900 1.3586 -0.3536 -0.2024 0.1415  241 ILE B O     
3856 C CB    . ILE B 241 ? 1.4756 1.7344 1.2596 -0.3447 -0.1712 0.0685  241 ILE B CB    
3857 N N     . ASN B 242 ? 1.5826 1.9288 1.3984 -0.3517 -0.1952 0.1277  242 ASN B N     
3858 C CA    . ASN B 242 ? 1.5775 1.9687 1.3897 -0.3734 -0.2098 0.1513  242 ASN B CA    
3859 C C     . ASN B 242 ? 1.5626 1.9949 1.4195 -0.3585 -0.2173 0.1855  242 ASN B C     
3860 O O     . ASN B 242 ? 1.5839 2.0591 1.4441 -0.3750 -0.2303 0.2098  242 ASN B O     
3861 C CB    . ASN B 242 ? 1.5608 1.9459 1.3465 -0.3840 -0.2096 0.1463  242 ASN B CB    
3862 C CG    . ASN B 242 ? 1.6170 1.9733 1.3547 -0.4082 -0.2049 0.1174  242 ASN B CG    
3863 O OD1   . ASN B 242 ? 1.6092 1.9214 1.3311 -0.3989 -0.1915 0.0919  242 ASN B OD1   
3864 N ND2   . ASN B 242 ? 1.6250 2.0060 1.3396 -0.4399 -0.2153 0.1210  242 ASN B ND2   
3865 N N     . SER B 243 ? 1.5535 1.9742 1.4450 -0.3284 -0.2088 0.1884  243 SER B N     
3866 C CA    . SER B 243 ? 1.4728 1.9307 1.4088 -0.3140 -0.2139 0.2200  243 SER B CA    
3867 C C     . SER B 243 ? 1.4849 1.9690 1.4338 -0.3224 -0.2207 0.2310  243 SER B C     
3868 O O     . SER B 243 ? 1.4697 1.9918 1.4547 -0.3150 -0.2266 0.2606  243 SER B O     
3869 C CB    . SER B 243 ? 1.3928 1.8277 1.3606 -0.2793 -0.2008 0.2184  243 SER B CB    
3870 O OG    . SER B 243 ? 1.2716 1.7402 1.2838 -0.2648 -0.2035 0.2479  243 SER B OG    
3871 N N     . SER B 244 ? 1.5254 1.9900 1.4484 -0.3362 -0.2194 0.2089  244 SER B N     
3872 C CA    . SER B 244 ? 1.6097 2.0996 1.5423 -0.3469 -0.2266 0.2188  244 SER B CA    
3873 C C     . SER B 244 ? 1.6739 2.1576 1.5638 -0.3798 -0.2321 0.2009  244 SER B C     
3874 O O     . SER B 244 ? 1.6961 2.1741 1.5833 -0.3852 -0.2315 0.1922  244 SER B O     
3875 C CB    . SER B 244 ? 1.5705 2.0421 1.5295 -0.3218 -0.2161 0.2124  244 SER B CB    
3876 O OG    . SER B 244 ? 1.5141 2.0015 1.5172 -0.2950 -0.2124 0.2341  244 SER B OG    
3877 N N     . LYS B 245 ? 1.6816 2.1670 1.5377 -0.4031 -0.2374 0.1957  245 LYS B N     
3878 C CA    . LYS B 245 ? 1.6833 2.1587 1.4961 -0.4354 -0.2406 0.1761  245 LYS B CA    
3879 C C     . LYS B 245 ? 1.8260 2.3429 1.6423 -0.4585 -0.2544 0.1938  245 LYS B C     
3880 O O     . LYS B 245 ? 1.8873 2.3940 1.6717 -0.4840 -0.2560 0.1768  245 LYS B O     
3881 C CB    . LYS B 245 ? 1.6071 2.0776 1.3832 -0.4558 -0.2424 0.1677  245 LYS B CB    
3882 N N     . GLN B 246 ? 1.7763 2.3388 1.6316 -0.4499 -0.2637 0.2276  246 GLN B N     
3883 C CA    . GLN B 246 ? 1.7726 2.3740 1.6408 -0.4650 -0.2752 0.2463  246 GLN B CA    
3884 C C     . GLN B 246 ? 1.8552 2.4377 1.7420 -0.4480 -0.2671 0.2368  246 GLN B C     
3885 O O     . GLN B 246 ? 1.8635 2.4753 1.7614 -0.4594 -0.2755 0.2506  246 GLN B O     
3886 C CB    . GLN B 246 ? 1.7048 2.3634 1.6114 -0.4606 -0.2871 0.2882  246 GLN B CB    
3887 N N     . ARG B 247 ? 1.8237 2.3609 1.7157 -0.4210 -0.2513 0.2155  247 ARG B N     
3888 C CA    . ARG B 247 ? 1.8547 2.3677 1.7556 -0.4082 -0.2426 0.2009  247 ARG B CA    
3889 C C     . ARG B 247 ? 1.9951 2.4723 1.8549 -0.4286 -0.2382 0.1695  247 ARG B C     
3890 O O     . ARG B 247 ? 2.0179 2.4796 1.8825 -0.4236 -0.2330 0.1589  247 ARG B O     
3891 C CB    . ARG B 247 ? 1.6844 2.1667 1.6096 -0.3712 -0.2277 0.1929  247 ARG B CB    
3892 N N     . LEU B 248 ? 1.9506 2.4146 1.7712 -0.4514 -0.2395 0.1548  248 LEU B N     
3893 C CA    . LEU B 248 ? 2.0354 2.4734 1.8169 -0.4771 -0.2370 0.1291  248 LEU B CA    
3894 C C     . LEU B 248 ? 2.0662 2.5382 1.8467 -0.5023 -0.2495 0.1416  248 LEU B C     
3895 O O     . LEU B 248 ? 2.0867 2.5375 1.8434 -0.5198 -0.2465 0.1220  248 LEU B O     
3896 C CB    . LEU B 248 ? 2.0664 2.4888 1.8067 -0.4983 -0.2361 0.1138  248 LEU B CB    
3897 N N     . GLU B 249 ? 2.0587 2.5830 1.8660 -0.5043 -0.2630 0.1746  249 GLU B N     
3898 C CA    . GLU B 249 ? 2.0709 2.6332 1.8827 -0.5266 -0.2758 0.1907  249 GLU B CA    
3899 C C     . GLU B 249 ? 2.0918 2.6395 1.9205 -0.5144 -0.2695 0.1834  249 GLU B C     
3900 O O     . GLU B 249 ? 2.1376 2.7122 1.9681 -0.5336 -0.2790 0.1936  249 GLU B O     
3901 C CB    . GLU B 249 ? 2.0126 2.6355 1.8570 -0.5257 -0.2902 0.2311  249 GLU B CB    
3902 N N     . THR B 250 ? 2.0763 2.5868 1.9201 -0.4827 -0.2546 0.1690  250 THR B N     
3903 C CA    . THR B 250 ? 2.0403 2.5265 1.8922 -0.4717 -0.2459 0.1552  250 THR B CA    
3904 C C     . THR B 250 ? 2.0445 2.4719 1.8730 -0.4629 -0.2300 0.1211  250 THR B C     
3905 O O     . THR B 250 ? 2.0435 2.4471 1.8727 -0.4579 -0.2224 0.1068  250 THR B O     
3906 C CB    . THR B 250 ? 1.9954 2.5001 1.8946 -0.4408 -0.2435 0.1750  250 THR B CB    
3907 N N     . GLN B 251 ? 2.0692 2.4717 1.8784 -0.4596 -0.2238 0.1079  251 GLN B N     
3908 C CA    . GLN B 251 ? 2.0281 2.3777 1.8255 -0.4444 -0.2075 0.0797  251 GLN B CA    
3909 C C     . GLN B 251 ? 2.0641 2.3793 1.8178 -0.4696 -0.2020 0.0524  251 GLN B C     
3910 O O     . GLN B 251 ? 2.0841 2.3556 1.8282 -0.4586 -0.1880 0.0295  251 GLN B O     
3911 C CB    . GLN B 251 ? 2.0366 2.3704 1.8441 -0.4184 -0.1997 0.0784  251 GLN B CB    
3912 C CG    . GLN B 251 ? 2.0218 2.3784 1.8696 -0.3899 -0.2007 0.1007  251 GLN B CG    
3913 C CD    . GLN B 251 ? 2.0187 2.3966 1.9015 -0.3756 -0.2022 0.1161  251 GLN B CD    
3914 O OE1   . GLN B 251 ? 2.0347 2.4005 1.9175 -0.3765 -0.1985 0.1065  251 GLN B OE1   
3915 N NE2   . GLN B 251 ? 1.9416 2.3506 1.8565 -0.3604 -0.2063 0.1407  251 GLN B NE2   
3916 N N     . PHE B 252 ? 2.0957 2.4294 1.8235 -0.5034 -0.2118 0.0542  252 PHE B N     
3917 C CA    . PHE B 252 ? 2.0829 2.3853 1.7667 -0.5289 -0.2058 0.0288  252 PHE B CA    
3918 C C     . PHE B 252 ? 2.0943 2.3776 1.7641 -0.5211 -0.1991 0.0201  252 PHE B C     
3919 O O     . PHE B 252 ? 2.0470 2.2917 1.6852 -0.5313 -0.1880 -0.0052 252 PHE B O     
3920 C CB    . PHE B 252 ? 2.0152 2.2730 1.6873 -0.5289 -0.1922 0.0030  252 PHE B CB    
3921 N N     . GLY B 253 ? 2.0816 2.3896 1.7767 -0.5013 -0.2043 0.0407  253 GLY B N     
3922 C CA    . GLY B 253 ? 2.0591 2.3538 1.7432 -0.4941 -0.1995 0.0357  253 GLY B CA    
3923 C C     . GLY B 253 ? 2.0492 2.3535 1.6963 -0.5263 -0.2054 0.0322  253 GLY B C     
3924 O O     . GLY B 253 ? 2.0336 2.3116 1.6587 -0.5267 -0.1969 0.0167  253 GLY B O     
3925 N N     . GLU B 254 ? 2.0936 2.4357 1.7325 -0.5546 -0.2196 0.0461  254 GLU B N     
3926 C CA    . GLU B 254 ? 2.1020 2.4512 1.7004 -0.5896 -0.2245 0.0395  254 GLU B CA    
3927 C C     . GLU B 254 ? 2.1373 2.4344 1.6963 -0.6041 -0.2091 0.0036  254 GLU B C     
3928 O O     . GLU B 254 ? 2.1632 2.4531 1.6860 -0.6276 -0.2075 -0.0081 254 GLU B O     
3929 C CB    . GLU B 254 ? 2.0942 2.4922 1.6888 -0.6204 -0.2424 0.0592  254 GLU B CB    
3930 N N     . GLU B 255 ? 2.1476 2.4079 1.7138 -0.5900 -0.1967 -0.0135 255 GLU B N     
3931 C CA    . GLU B 255 ? 2.1213 2.3289 1.6572 -0.5986 -0.1796 -0.0465 255 GLU B CA    
3932 C C     . GLU B 255 ? 2.0395 2.2038 1.5876 -0.5659 -0.1626 -0.0613 255 GLU B C     
3933 O O     . GLU B 255 ? 2.0534 2.1750 1.5756 -0.5718 -0.1474 -0.0868 255 GLU B O     
3934 C CB    . GLU B 255 ? 2.1278 2.3278 1.6586 -0.6152 -0.1790 -0.0550 255 GLU B CB    
3935 N N     . MET B 256 ? 2.0769 2.2507 1.6628 -0.5334 -0.1641 -0.0463 256 MET B N     
3936 C CA    . MET B 256 ? 1.9436 2.0781 1.5427 -0.5035 -0.1486 -0.0598 256 MET B CA    
3937 C C     . MET B 256 ? 1.8658 2.0064 1.4862 -0.4758 -0.1485 -0.0483 256 MET B C     
3938 O O     . MET B 256 ? 1.8468 1.9525 1.4652 -0.4587 -0.1351 -0.0630 256 MET B O     
3939 C CB    . MET B 256 ? 1.8383 1.9666 1.4636 -0.4875 -0.1459 -0.0586 256 MET B CB    
3940 N N     . VAL B 257 ? 1.8897 2.0732 1.5313 -0.4707 -0.1622 -0.0223 257 VAL B N     
3941 C CA    . VAL B 257 ? 1.8441 2.0302 1.5049 -0.4453 -0.1607 -0.0127 257 VAL B CA    
3942 C C     . VAL B 257 ? 1.8185 1.9979 1.4507 -0.4581 -0.1589 -0.0196 257 VAL B C     
3943 O O     . VAL B 257 ? 1.8380 2.0034 1.4768 -0.4386 -0.1525 -0.0211 257 VAL B O     
3944 C CB    . VAL B 257 ? 1.7580 1.9888 1.4558 -0.4317 -0.1735 0.0180  257 VAL B CB    
3945 C CG1   . VAL B 257 ? 1.7392 1.9767 1.4634 -0.4207 -0.1744 0.0238  257 VAL B CG1   
3946 C CG2   . VAL B 257 ? 1.6847 1.9598 1.3749 -0.4554 -0.1891 0.0381  257 VAL B CG2   
3947 N N     . ASN B 258 ? 1.8203 2.0101 1.4200 -0.4914 -0.1644 -0.0237 258 ASN B N     
3948 C CA    . ASN B 258 ? 1.8405 2.0191 1.4085 -0.5055 -0.1603 -0.0342 258 ASN B CA    
3949 C C     . ASN B 258 ? 1.8705 1.9952 1.4220 -0.4962 -0.1407 -0.0627 258 ASN B C     
3950 O O     . ASN B 258 ? 1.8378 1.9478 1.3798 -0.4893 -0.1339 -0.0686 258 ASN B O     
3951 C CB    . ASN B 258 ? 1.8653 2.0644 1.3990 -0.5457 -0.1691 -0.0352 258 ASN B CB    
3952 C CG    . ASN B 258 ? 1.9717 2.1607 1.4939 -0.5642 -0.1677 -0.0473 258 ASN B CG    
3953 O OD1   . ASN B 258 ? 2.0035 2.1888 1.5520 -0.5475 -0.1667 -0.0441 258 ASN B OD1   
3954 N ND2   . ASN B 258 ? 1.9869 2.1717 1.4695 -0.5994 -0.1674 -0.0611 258 ASN B ND2   
3955 N N     . GLN B 259 ? 1.8578 1.9531 1.4064 -0.4962 -0.1310 -0.0796 259 GLN B N     
3956 C CA    . GLN B 259 ? 1.8324 1.8782 1.3739 -0.4825 -0.1120 -0.1030 259 GLN B CA    
3957 C C     . GLN B 259 ? 1.8037 1.8427 1.3778 -0.4458 -0.1080 -0.0956 259 GLN B C     
3958 O O     . GLN B 259 ? 1.8123 1.8220 1.3804 -0.4337 -0.0958 -0.1079 259 GLN B O     
3959 C CB    . GLN B 259 ? 1.7954 1.8146 1.3310 -0.4899 -0.1032 -0.1194 259 GLN B CB    
3960 N N     . PHE B 260 ? 1.7615 1.8277 1.3700 -0.4284 -0.1179 -0.0755 260 PHE B N     
3961 C CA    . PHE B 260 ? 1.7389 1.8000 1.3784 -0.3950 -0.1143 -0.0684 260 PHE B CA    
3962 C C     . PHE B 260 ? 1.7465 1.8250 1.3918 -0.3867 -0.1193 -0.0550 260 PHE B C     
3963 O O     . PHE B 260 ? 1.7209 1.7836 1.3809 -0.3627 -0.1122 -0.0565 260 PHE B O     
3964 C CB    . PHE B 260 ? 1.6935 1.7755 1.3669 -0.3800 -0.1211 -0.0531 260 PHE B CB    
3965 N N     . ASP B 261 ? 1.7181 1.8309 1.3534 -0.4063 -0.1318 -0.0407 261 ASP B N     
3966 C CA    . ASP B 261 ? 1.6446 1.7776 1.2869 -0.3996 -0.1375 -0.0253 261 ASP B CA    
3967 C C     . ASP B 261 ? 1.6989 1.8000 1.3228 -0.3946 -0.1255 -0.0415 261 ASP B C     
3968 O O     . ASP B 261 ? 1.7400 1.8268 1.3290 -0.4162 -0.1206 -0.0567 261 ASP B O     
3969 C CB    . ASP B 261 ? 1.6257 1.7990 1.2548 -0.4256 -0.1520 -0.0090 261 ASP B CB    
3970 C CG    . ASP B 261 ? 1.6578 1.8438 1.2860 -0.4219 -0.1548 0.0019  261 ASP B CG    
3971 O OD1   . ASP B 261 ? 1.5971 1.8026 1.2583 -0.4006 -0.1597 0.0220  261 ASP B OD1   
3972 O OD2   . ASP B 261 ? 1.7002 1.8747 1.2956 -0.4393 -0.1509 -0.0104 261 ASP B OD2   
3973 N N     . PRO B 262 ? 1.6335 1.7243 1.2801 -0.3669 -0.1203 -0.0379 262 PRO B N     
3974 C CA    . PRO B 262 ? 1.6123 1.6698 1.2453 -0.3587 -0.1075 -0.0539 262 PRO B CA    
3975 C C     . PRO B 262 ? 1.5823 1.6545 1.2054 -0.3640 -0.1115 -0.0450 262 PRO B C     
3976 O O     . PRO B 262 ? 1.5897 1.6361 1.2000 -0.3589 -0.1011 -0.0577 262 PRO B O     
3977 C CB    . PRO B 262 ? 1.5641 1.6073 1.2290 -0.3267 -0.1015 -0.0523 262 PRO B CB    
3978 C CG    . PRO B 262 ? 1.5564 1.6368 1.2528 -0.3174 -0.1140 -0.0276 262 PRO B CG    
3979 C CD    . PRO B 262 ? 1.6025 1.7090 1.2892 -0.3414 -0.1246 -0.0207 262 PRO B CD    
3980 N N     . GLY B 263 ? 1.5741 1.6879 1.2037 -0.3743 -0.1263 -0.0229 263 GLY B N     
3981 C CA    . GLY B 263 ? 1.5445 1.6760 1.1703 -0.3767 -0.1310 -0.0107 263 GLY B CA    
3982 C C     . GLY B 263 ? 1.5683 1.6793 1.1545 -0.3953 -0.1230 -0.0290 263 GLY B C     
3983 O O     . GLY B 263 ? 1.5069 1.6135 1.0903 -0.3885 -0.1197 -0.0276 263 GLY B O     
3984 N N     . ASP B 264 ? 1.6196 1.7160 1.1750 -0.4186 -0.1185 -0.0474 264 ASP B N     
3985 C CA    . ASP B 264 ? 1.6435 1.7158 1.1596 -0.4369 -0.1080 -0.0680 264 ASP B CA    
3986 C C     . ASP B 264 ? 1.6309 1.6602 1.1476 -0.4162 -0.0905 -0.0857 264 ASP B C     
3987 O O     . ASP B 264 ? 1.6124 1.6200 1.0996 -0.4279 -0.0797 -0.1023 264 ASP B O     
3988 C CB    . ASP B 264 ? 1.6607 1.7234 1.1448 -0.4665 -0.1052 -0.0852 264 ASP B CB    
3989 C CG    . ASP B 264 ? 1.7432 1.7829 1.2403 -0.4572 -0.0988 -0.0962 264 ASP B CG    
3990 O OD1   . ASP B 264 ? 1.7143 1.7741 1.2433 -0.4429 -0.1080 -0.0800 264 ASP B OD1   
3991 O OD2   . ASP B 264 ? 1.7649 1.7672 1.2403 -0.4651 -0.0841 -0.1206 264 ASP B OD2   
3992 N N     . LEU B 265 ? 1.6470 1.6645 1.1965 -0.3865 -0.0870 -0.0824 265 LEU B N     
3993 C CA    . LEU B 265 ? 1.5380 1.5159 1.0894 -0.3678 -0.0709 -0.0986 265 LEU B CA    
3994 C C     . LEU B 265 ? 1.4149 1.3964 0.9873 -0.3449 -0.0712 -0.0871 265 LEU B C     
3995 O O     . LEU B 265 ? 1.4137 1.3661 0.9824 -0.3335 -0.0585 -0.0993 265 LEU B O     
3996 C CB    . LEU B 265 ? 1.4294 1.3850 0.9972 -0.3539 -0.0640 -0.1078 265 LEU B CB    
3997 C CG    . LEU B 265 ? 1.4831 1.4169 1.0250 -0.3743 -0.0556 -0.1276 265 LEU B CG    
3998 C CD1   . LEU B 265 ? 1.4153 1.3448 0.9764 -0.3662 -0.0561 -0.1282 265 LEU B CD1   
3999 C CD2   . LEU B 265 ? 1.4038 1.2972 0.9246 -0.3750 -0.0367 -0.1496 265 LEU B CD2   
4000 N N     . VAL B 266 ? 1.4085 1.4248 1.0026 -0.3387 -0.0849 -0.0635 266 VAL B N     
4001 C CA    . VAL B 266 ? 1.3750 1.3954 0.9837 -0.3220 -0.0850 -0.0529 266 VAL B CA    
4002 C C     . VAL B 266 ? 1.4204 1.4273 0.9979 -0.3349 -0.0773 -0.0642 266 VAL B C     
4003 O O     . VAL B 266 ? 1.4790 1.4902 1.0249 -0.3611 -0.0778 -0.0716 266 VAL B O     
4004 C CB    . VAL B 266 ? 1.2929 1.3558 0.9251 -0.3194 -0.1007 -0.0248 266 VAL B CB    
4005 C CG1   . VAL B 266 ? 1.2264 1.3042 0.8843 -0.3120 -0.1076 -0.0149 266 VAL B CG1   
4006 C CG2   . VAL B 266 ? 1.3832 1.4751 0.9917 -0.3465 -0.1103 -0.0159 266 VAL B CG2   
4007 N N     . GLY B 267 ? 1.3769 1.3651 0.9618 -0.3172 -0.0689 -0.0675 267 GLY B N     
4008 C CA    . GLY B 267 ? 1.4183 1.3956 0.9773 -0.3269 -0.0615 -0.0759 267 GLY B CA    
4009 C C     . GLY B 267 ? 1.4437 1.3818 0.9778 -0.3327 -0.0442 -0.1021 267 GLY B C     
4010 O O     . GLY B 267 ? 1.4859 1.4076 1.0060 -0.3320 -0.0343 -0.1102 267 GLY B O     
4011 N N     . VAL B 268 ? 1.3603 1.2822 0.8894 -0.3379 -0.0392 -0.1152 268 VAL B N     
4012 C CA    . VAL B 268 ? 1.4549 1.3389 0.9602 -0.3444 -0.0212 -0.1394 268 VAL B CA    
4013 C C     . VAL B 268 ? 1.4337 1.2916 0.9581 -0.3179 -0.0096 -0.1437 268 VAL B C     
4014 O O     . VAL B 268 ? 1.3856 1.2322 0.9336 -0.3000 -0.0074 -0.1441 268 VAL B O     
4015 C CB    . VAL B 268 ? 1.4444 1.3151 0.9409 -0.3562 -0.0172 -0.1524 268 VAL B CB    
4016 C CG1   . VAL B 268 ? 1.4287 1.2649 0.8926 -0.3717 0.0012  -0.1768 268 VAL B CG1   
4017 C CG2   . VAL B 268 ? 1.4466 1.3516 0.9369 -0.3765 -0.0334 -0.1411 268 VAL B CG2   
4018 N N     . LYS B 269 ? 1.4836 1.3331 0.9975 -0.3162 -0.0025 -0.1463 269 LYS B N     
4019 C CA    . LYS B 269 ? 1.4285 1.2659 0.9656 -0.2906 0.0027  -0.1425 269 LYS B CA    
4020 C C     . LYS B 269 ? 1.3915 1.1907 0.9286 -0.2804 0.0211  -0.1597 269 LYS B C     
4021 O O     . LYS B 269 ? 1.3660 1.1562 0.9274 -0.2581 0.0239  -0.1560 269 LYS B O     
4022 C CB    . LYS B 269 ? 1.4461 1.2948 0.9763 -0.2912 0.0011  -0.1345 269 LYS B CB    
4023 N N     . GLU B 270 ? 1.4079 1.1846 0.9195 -0.2961 0.0340  -0.1778 270 GLU B N     
4024 C CA    . GLU B 270 ? 1.4082 1.1498 0.9249 -0.2851 0.0516  -0.1918 270 GLU B CA    
4025 C C     . GLU B 270 ? 1.3695 1.1048 0.8994 -0.2821 0.0507  -0.1948 270 GLU B C     
4026 O O     . GLU B 270 ? 1.2968 1.0046 0.8332 -0.2735 0.0648  -0.2050 270 GLU B O     
4027 C CB    . GLU B 270 ? 1.3937 1.1093 0.8791 -0.3007 0.0699  -0.2104 270 GLU B CB    
4028 N N     . PHE B 271 ? 1.3219 1.0835 0.8572 -0.2890 0.0347  -0.1850 271 PHE B N     
4029 C CA    . PHE B 271 ? 1.3141 1.0749 0.8662 -0.2838 0.0314  -0.1845 271 PHE B CA    
4030 C C     . PHE B 271 ? 1.3108 1.0734 0.8971 -0.2567 0.0284  -0.1742 271 PHE B C     
4031 O O     . PHE B 271 ? 1.3157 1.0998 0.9173 -0.2465 0.0174  -0.1597 271 PHE B O     
4032 C CB    . PHE B 271 ? 1.2714 1.0624 0.8199 -0.2990 0.0150  -0.1753 271 PHE B CB    
4033 C CG    . PHE B 271 ? 1.2830 1.0729 0.8446 -0.2975 0.0124  -0.1762 271 PHE B CG    
4034 C CD1   . PHE B 271 ? 1.2937 1.0533 0.8498 -0.2996 0.0268  -0.1919 271 PHE B CD1   
4035 C CD2   . PHE B 271 ? 1.2549 1.0744 0.8349 -0.2944 -0.0037 -0.1608 271 PHE B CD2   
4036 C CE1   . PHE B 271 ? 1.2406 1.0004 0.8091 -0.2985 0.0242  -0.1918 271 PHE B CE1   
4037 C CE2   . PHE B 271 ? 1.1339 0.9533 0.7255 -0.2934 -0.0058 -0.1614 271 PHE B CE2   
4038 C CZ    . PHE B 271 ? 1.1281 0.9179 0.7134 -0.2957 0.0077  -0.1769 271 PHE B CZ    
4039 N N     . GLY B 272 ? 1.2452 0.9865 0.8440 -0.2461 0.0380  -0.1812 272 GLY B N     
4040 C CA    . GLY B 272 ? 1.2827 1.0203 0.9096 -0.2218 0.0390  -0.1745 272 GLY B CA    
4041 C C     . GLY B 272 ? 1.2056 0.9444 0.8533 -0.2126 0.0360  -0.1720 272 GLY B C     
4042 O O     . GLY B 272 ? 1.1657 0.8920 0.8072 -0.2211 0.0419  -0.1808 272 GLY B O     
4043 N N     . TYR B 273 ? 1.1393 0.8931 0.8116 -0.1957 0.0273  -0.1600 273 TYR B N     
4044 C CA    . TYR B 273 ? 1.1123 0.8689 0.8067 -0.1842 0.0246  -0.1564 273 TYR B CA    
4045 C C     . TYR B 273 ? 1.0419 0.7871 0.7544 -0.1648 0.0311  -0.1549 273 TYR B C     
4046 O O     . TYR B 273 ? 1.1060 0.8558 0.8232 -0.1565 0.0291  -0.1493 273 TYR B O     
4047 C CB    . TYR B 273 ? 1.0863 0.8720 0.7943 -0.1818 0.0090  -0.1434 273 TYR B CB    
4048 C CG    . TYR B 273 ? 1.0802 0.8715 0.8067 -0.1746 0.0057  -0.1404 273 TYR B CG    
4049 C CD1   . TYR B 273 ? 1.0395 0.8152 0.7633 -0.1788 0.0132  -0.1492 273 TYR B CD1   
4050 C CD2   . TYR B 273 ? 1.0919 0.9044 0.8393 -0.1637 -0.0044 -0.1285 273 TYR B CD2   
4051 C CE1   . TYR B 273 ? 1.0634 0.8462 0.8042 -0.1727 0.0096  -0.1457 273 TYR B CE1   
4052 C CE2   . TYR B 273 ? 1.1030 0.9216 0.8668 -0.1574 -0.0070 -0.1260 273 TYR B CE2   
4053 C CZ    . TYR B 273 ? 1.0709 0.8754 0.8309 -0.1621 -0.0005 -0.1344 273 TYR B CZ    
4054 O OH    . TYR B 273 ? 0.9282 0.7400 0.7040 -0.1563 -0.0032 -0.1313 273 TYR B OH    
4055 N N     . LEU B 274 ? 0.9984 0.7300 0.7214 -0.1581 0.0384  -0.1589 274 LEU B N     
4056 C CA    . LEU B 274 ? 1.0324 0.7531 0.7710 -0.1419 0.0456  -0.1575 274 LEU B CA    
4057 C C     . LEU B 274 ? 0.9823 0.7091 0.7423 -0.1311 0.0424  -0.1527 274 LEU B C     
4058 O O     . LEU B 274 ? 0.9858 0.7132 0.7469 -0.1364 0.0418  -0.1548 274 LEU B O     
4059 C CB    . LEU B 274 ? 1.0383 0.7322 0.7682 -0.1438 0.0622  -0.1669 274 LEU B CB    
4060 C CG    . LEU B 274 ? 1.0749 0.7529 0.8046 -0.1488 0.0716  -0.1741 274 LEU B CG    
4061 C CD1   . LEU B 274 ? 0.9740 0.6419 0.7242 -0.1345 0.0798  -0.1712 274 LEU B CD1   
4062 C CD2   . LEU B 274 ? 1.1003 0.7581 0.8069 -0.1634 0.0838  -0.1860 274 LEU B CD2   
4063 N N     . LEU B 275 ? 0.9811 0.7123 0.7575 -0.1167 0.0408  -0.1465 275 LEU B N     
4064 C CA    . LEU B 275 ? 0.9362 0.6707 0.7318 -0.1061 0.0403  -0.1428 275 LEU B CA    
4065 C C     . LEU B 275 ? 0.8976 0.6143 0.6987 -0.0998 0.0526  -0.1450 275 LEU B C     
4066 O O     . LEU B 275 ? 0.9713 0.6783 0.7684 -0.0971 0.0588  -0.1459 275 LEU B O     
4067 C CB    . LEU B 275 ? 0.9107 0.6616 0.7204 -0.0956 0.0313  -0.1348 275 LEU B CB    
4068 C CG    . LEU B 275 ? 0.8828 0.6409 0.7112 -0.0852 0.0293  -0.1307 275 LEU B CG    
4069 C CD1   . LEU B 275 ? 0.8806 0.6508 0.7131 -0.0889 0.0232  -0.1296 275 LEU B CD1   
4070 C CD2   . LEU B 275 ? 0.8501 0.6175 0.6876 -0.0762 0.0242  -0.1253 275 LEU B CD2   
4071 N N     . LEU B 276 ? 0.8798 0.5929 0.6909 -0.0975 0.0564  -0.1449 276 LEU B N     
4072 C CA    . LEU B 276 ? 0.9430 0.6408 0.7620 -0.0917 0.0685  -0.1449 276 LEU B CA    
4073 C C     . LEU B 276 ? 0.9363 0.6432 0.7747 -0.0833 0.0664  -0.1384 276 LEU B C     
4074 O O     . LEU B 276 ? 0.9094 0.6276 0.7518 -0.0855 0.0595  -0.1373 276 LEU B O     
4075 C CB    . LEU B 276 ? 0.8938 0.5711 0.7018 -0.1010 0.0809  -0.1528 276 LEU B CB    
4076 C CG    . LEU B 276 ? 0.9133 0.5738 0.7324 -0.0950 0.0954  -0.1516 276 LEU B CG    
4077 C CD1   . LEU B 276 ? 0.9913 0.6285 0.7959 -0.1028 0.1097  -0.1605 276 LEU B CD1   
4078 C CD2   . LEU B 276 ? 0.9282 0.5905 0.7610 -0.0938 0.0965  -0.1484 276 LEU B CD2   
4079 N N     . VAL B 277 ? 0.8841 0.5873 0.7346 -0.0743 0.0723  -0.1335 277 VAL B N     
4080 C CA    . VAL B 277 ? 0.9008 0.6130 0.7693 -0.0673 0.0714  -0.1263 277 VAL B CA    
4081 C C     . VAL B 277 ? 0.9341 0.6329 0.8118 -0.0634 0.0844  -0.1228 277 VAL B C     
4082 O O     . VAL B 277 ? 0.9803 0.6695 0.8556 -0.0607 0.0911  -0.1229 277 VAL B O     
4083 C CB    . VAL B 277 ? 0.8697 0.5984 0.7463 -0.0600 0.0623  -0.1209 277 VAL B CB    
4084 C CG1   . VAL B 277 ? 0.8614 0.5992 0.7544 -0.0543 0.0625  -0.1137 277 VAL B CG1   
4085 C CG2   . VAL B 277 ? 0.8538 0.5959 0.7253 -0.0626 0.0509  -0.1230 277 VAL B CG2   
4086 N N     . ALA B 278 ? 0.9364 0.6350 0.8258 -0.0629 0.0886  -0.1189 278 ALA B N     
4087 C CA    . ALA B 278 ? 0.8972 0.5857 0.8005 -0.0581 0.1013  -0.1125 278 ALA B CA    
4088 C C     . ALA B 278 ? 0.9169 0.6219 0.8390 -0.0532 0.0975  -0.1020 278 ALA B C     
4089 O O     . ALA B 278 ? 0.9163 0.6356 0.8383 -0.0553 0.0875  -0.1023 278 ALA B O     
4090 C CB    . ALA B 278 ? 0.9403 0.6073 0.8391 -0.0643 0.1142  -0.1183 278 ALA B CB    
4091 N N     . GLN B 279 ? 0.9089 0.6129 0.8477 -0.0469 0.1057  -0.0919 279 GLN B N     
4092 C CA    . GLN B 279 ? 0.8622 0.5854 0.8190 -0.0426 0.1014  -0.0799 279 GLN B CA    
4093 C C     . GLN B 279 ? 0.9727 0.6894 0.9481 -0.0397 0.1139  -0.0698 279 GLN B C     
4094 O O     . GLN B 279 ? 1.0398 0.7431 1.0214 -0.0359 0.1259  -0.0663 279 GLN B O     
4095 C CB    . GLN B 279 ? 0.9218 0.6599 0.8831 -0.0375 0.0950  -0.0737 279 GLN B CB    
4096 C CG    . GLN B 279 ? 0.9656 0.7255 0.9445 -0.0346 0.0907  -0.0605 279 GLN B CG    
4097 C CD    . GLN B 279 ? 0.9851 0.7597 0.9664 -0.0316 0.0841  -0.0554 279 GLN B CD    
4098 O OE1   . GLN B 279 ? 1.0268 0.7934 1.0047 -0.0291 0.0872  -0.0565 279 GLN B OE1   
4099 N NE2   . GLN B 279 ? 0.9034 0.6997 0.8903 -0.0329 0.0753  -0.0500 279 GLN B NE2   
4100 N N     . ARG B 280 ? 0.9514 0.6781 0.9372 -0.0411 0.1118  -0.0639 280 ARG B N     
4101 C CA    . ARG B 280 ? 0.9923 0.7165 0.9997 -0.0375 0.1230  -0.0510 280 ARG B CA    
4102 C C     . ARG B 280 ? 0.9870 0.7325 1.0124 -0.0313 0.1201  -0.0349 280 ARG B C     
4103 O O     . ARG B 280 ? 0.9527 0.7210 0.9782 -0.0325 0.1076  -0.0316 280 ARG B O     
4104 C CB    . ARG B 280 ? 0.9266 0.6541 0.9390 -0.0419 0.1219  -0.0498 280 ARG B CB    
4105 C CG    . ARG B 280 ? 0.9009 0.6365 0.9400 -0.0375 0.1291  -0.0320 280 ARG B CG    
4106 C CD    . ARG B 280 ? 0.8251 0.5570 0.8710 -0.0416 0.1326  -0.0306 280 ARG B CD    
4107 N NE    . ARG B 280 ? 0.8451 0.5848 0.9186 -0.0365 0.1405  -0.0115 280 ARG B NE    
4108 C CZ    . ARG B 280 ? 0.8556 0.5975 0.9426 -0.0383 0.1439  -0.0041 280 ARG B CZ    
4109 N NH1   . ARG B 280 ? 0.8510 0.5871 0.9261 -0.0455 0.1402  -0.0147 280 ARG B NH1   
4110 N NH2   . ARG B 280 ? 1.0059 0.7572 1.1200 -0.0329 0.1510  0.0157  280 ARG B NH2   
4111 N N     . PRO B 281 ? 0.9893 0.7286 1.0303 -0.0254 0.1317  -0.0242 281 PRO B N     
4112 C CA    . PRO B 281 ? 0.9940 0.7551 1.0499 -0.0207 0.1278  -0.0089 281 PRO B CA    
4113 C C     . PRO B 281 ? 1.0094 0.7969 1.0808 -0.0217 0.1206  0.0051  281 PRO B C     
4114 O O     . PRO B 281 ? 1.0185 0.8049 1.0985 -0.0231 0.1242  0.0088  281 PRO B O     
4115 C CB    . PRO B 281 ? 1.0476 0.7947 1.1200 -0.0140 0.1443  0.0007  281 PRO B CB    
4116 C CG    . PRO B 281 ? 1.0639 0.7796 1.1200 -0.0160 0.1547  -0.0159 281 PRO B CG    
4117 C CD    . PRO B 281 ? 1.0113 0.7228 1.0542 -0.0233 0.1490  -0.0274 281 PRO B CD    
4118 N N     . GLY B 282 ? 0.9392 0.7510 1.0134 -0.0219 0.1104  0.0129  282 GLY B N     
4119 C CA    . GLY B 282 ? 0.9909 0.8312 1.0755 -0.0250 0.1017  0.0248  282 GLY B CA    
4120 C C     . GLY B 282 ? 1.0957 0.9527 1.1630 -0.0307 0.0864  0.0155  282 GLY B C     
4121 O O     . GLY B 282 ? 1.0778 0.9269 1.1285 -0.0311 0.0823  0.0029  282 GLY B O     
4122 N N     . LYS B 283 ? 1.1115 0.9925 1.1844 -0.0350 0.0790  0.0231  283 LYS B N     
4123 C CA    . LYS B 283 ? 1.1537 1.0526 1.2120 -0.0410 0.0660  0.0153  283 LYS B CA    
4124 C C     . LYS B 283 ? 1.3089 1.2134 1.3612 -0.0413 0.0616  0.0143  283 LYS B C     
4125 O O     . LYS B 283 ? 1.3525 1.2587 1.4174 -0.0381 0.0666  0.0262  283 LYS B O     
4126 C CB    . LYS B 283 ? 1.1018 0.9887 1.1413 -0.0432 0.0619  -0.0033 283 LYS B CB    
4127 C CG    . LYS B 283 ? 1.1323 1.0365 1.1594 -0.0485 0.0508  -0.0108 283 LYS B CG    
4128 C CD    . LYS B 283 ? 1.1579 1.0485 1.1670 -0.0490 0.0474  -0.0288 283 LYS B CD    
4129 C CE    . LYS B 283 ? 1.0141 0.8913 1.0227 -0.0488 0.0513  -0.0332 283 LYS B CE    
4130 N NZ    . LYS B 283 ? 0.9111 0.7807 0.9037 -0.0503 0.0466  -0.0484 283 LYS B NZ    
4131 O OXT   . LYS B 283 ? 1.3828 1.2904 1.4187 -0.0449 0.0535  0.0019  283 LYS B OXT   
4132 N N     . SAH C .   ? 0.9027 0.6205 0.8369 0.0047  0.1211  -0.0208 301 SAH A N     
4133 C CA    . SAH C .   ? 0.9471 0.6744 0.8955 0.0073  0.1221  -0.0080 301 SAH A CA    
4134 C CB    . SAH C .   ? 0.8989 0.6242 0.8600 0.0130  0.1377  0.0010  301 SAH A CB    
4135 C CG    . SAH C .   ? 0.9000 0.6173 0.8632 0.0151  0.1471  -0.0024 301 SAH A CG    
4136 S SD    . SAH C .   ? 0.8813 0.5986 0.8663 0.0231  0.1659  0.0120  301 SAH A SD    
4137 C C     . SAH C .   ? 0.8965 0.6387 0.8575 0.0050  0.1101  -0.0020 301 SAH A C     
4138 O O     . SAH C .   ? 1.0184 0.7702 0.9883 0.0044  0.1062  0.0069  301 SAH A O     
4139 O OXT   . SAH C .   ? 0.8168 0.5606 0.7775 0.0033  0.1056  -0.0065 301 SAH A OXT   
4140 C "C5'" . SAH C .   ? 0.9830 0.6764 0.9505 0.0243  0.1847  0.0004  301 SAH A "C5'" 
4141 C "C4'" . SAH C .   ? 1.0217 0.7119 0.9732 0.0215  0.1830  -0.0042 301 SAH A "C4'" 
4142 O "O4'" . SAH C .   ? 1.0097 0.6811 0.9432 0.0199  0.1971  -0.0158 301 SAH A "O4'" 
4143 C "C3'" . SAH C .   ? 1.0059 0.7057 0.9714 0.0258  0.1867  0.0097  301 SAH A "C3'" 
4144 O "O3'" . SAH C .   ? 1.0014 0.7080 0.9575 0.0216  0.1739  0.0087  301 SAH A "O3'" 
4145 C "C2'" . SAH C .   ? 0.9595 0.6438 0.9201 0.0292  0.2078  0.0072  301 SAH A "C2'" 
4146 O "O2'" . SAH C .   ? 1.0544 0.7431 1.0169 0.0310  0.2115  0.0144  301 SAH A "O2'" 
4147 C "C1'" . SAH C .   ? 0.9992 0.6687 0.9321 0.0222  0.2069  -0.0113 301 SAH A "C1'" 
4148 N N9    . SAH C .   ? 1.0429 0.6930 0.9653 0.0225  0.2273  -0.0199 301 SAH A N9    
4149 C C8    . SAH C .   ? 1.0942 0.7336 1.0289 0.0277  0.2447  -0.0180 301 SAH A C8    
4150 N N7    . SAH C .   ? 1.1536 0.7734 1.0730 0.0257  0.2624  -0.0290 301 SAH A N7    
4151 C C5    . SAH C .   ? 1.1036 0.7234 0.9984 0.0181  0.2552  -0.0379 301 SAH A C5    
4152 C C6    . SAH C .   ? 1.1212 0.7265 0.9899 0.0111  0.2658  -0.0513 301 SAH A C6    
4153 N N6    . SAH C .   ? 1.1878 0.7725 1.0495 0.0106  0.2880  -0.0600 301 SAH A N6    
4154 N N1    . SAH C .   ? 1.1311 0.7441 0.9809 0.0040  0.2532  -0.0551 301 SAH A N1    
4155 C C2    . SAH C .   ? 1.0616 0.6930 0.9194 0.0048  0.2325  -0.0467 301 SAH A C2    
4156 N N3    . SAH C .   ? 1.0413 0.6854 0.9218 0.0105  0.2218  -0.0357 301 SAH A N3    
4157 C C4    . SAH C .   ? 1.0472 0.6856 0.9449 0.0167  0.2335  -0.0317 301 SAH A C4    
4158 N N     . SAH D .   ? 0.9359 0.7884 0.7758 -0.1503 -0.0126 -0.1196 301 SAH B N     
4159 C CA    . SAH D .   ? 0.9660 0.8413 0.8116 -0.1563 -0.0215 -0.1124 301 SAH B CA    
4160 C CB    . SAH D .   ? 0.9658 0.8391 0.7946 -0.1761 -0.0235 -0.1160 301 SAH B CB    
4161 C CG    . SAH D .   ? 1.1210 0.9764 0.9282 -0.1865 -0.0190 -0.1244 301 SAH B CG    
4162 S SD    . SAH D .   ? 1.0404 0.9008 0.8267 -0.2127 -0.0240 -0.1272 301 SAH B SD    
4163 C C     . SAH D .   ? 0.9915 0.8868 0.8444 -0.1505 -0.0293 -0.1035 301 SAH B C     
4164 O O     . SAH D .   ? 0.9983 0.9159 0.8617 -0.1510 -0.0364 -0.0948 301 SAH B O     
4165 O OXT   . SAH D .   ? 0.9352 0.8216 0.7838 -0.1452 -0.0267 -0.1055 301 SAH B OXT   
4166 C "C5'" . SAH D .   ? 1.0502 0.8755 0.8236 -0.2210 -0.0094 -0.1421 301 SAH B "C5'" 
4167 C "C4'" . SAH D .   ? 0.9803 0.8038 0.7701 -0.2143 -0.0064 -0.1404 301 SAH B "C4'" 
4168 O "O4'" . SAH D .   ? 0.9988 0.7925 0.7827 -0.2159 0.0072  -0.1506 301 SAH B "O4'" 
4169 C "C3'" . SAH D .   ? 1.0045 0.8427 0.7953 -0.2270 -0.0131 -0.1369 301 SAH B "C3'" 
4170 O "O3'" . SAH D .   ? 1.0609 0.9179 0.8741 -0.2135 -0.0182 -0.1271 301 SAH B "O3'" 
4171 C "C2'" . SAH D .   ? 0.9917 0.8036 0.7745 -0.2369 -0.0019 -0.1473 301 SAH B "C2'" 
4172 O "O2'" . SAH D .   ? 0.9701 0.7880 0.7650 -0.2379 -0.0030 -0.1436 301 SAH B "O2'" 
4173 C "C1'" . SAH D .   ? 0.9979 0.7880 0.7874 -0.2215 0.0098  -0.1513 301 SAH B "C1'" 
4174 N N9    . SAH D .   ? 1.0065 0.7663 0.7856 -0.2299 0.0234  -0.1622 301 SAH B N9    
4175 C C8    . SAH D .   ? 1.0977 0.8387 0.8535 -0.2451 0.0300  -0.1734 301 SAH B C8    
4176 N N7    . SAH D .   ? 1.1853 0.8975 0.9371 -0.2498 0.0446  -0.1826 301 SAH B N7    
4177 C C5    . SAH D .   ? 1.0923 0.8055 0.8670 -0.2366 0.0471  -0.1757 301 SAH B C5    
4178 C C6    . SAH D .   ? 1.0920 0.7832 0.8772 -0.2335 0.0605  -0.1780 301 SAH B C6    
4179 N N6    . SAH D .   ? 1.1303 0.7907 0.9038 -0.2432 0.0757  -0.1893 301 SAH B N6    
4180 N N1    . SAH D .   ? 1.1117 0.8133 0.9201 -0.2202 0.0589  -0.1681 301 SAH B N1    
4181 C C2    . SAH D .   ? 1.0413 0.7723 0.8602 -0.2111 0.0451  -0.1582 301 SAH B C2    
4182 N N3    . SAH D .   ? 0.9964 0.7486 0.8084 -0.2121 0.0327  -0.1555 301 SAH B N3    
4183 C C4    . SAH D .   ? 1.0158 0.7589 0.8064 -0.2248 0.0338  -0.1637 301 SAH B C4    
4184 C C1    . MQA E .   ? 1.4390 1.3036 1.1665 -0.2572 -0.0313 -0.1346 302 MQA B C1    
4185 C C2    . MQA E .   ? 1.4008 1.2386 1.1140 -0.2554 -0.0199 -0.1458 302 MQA B C2    
4186 C C3    . MQA E .   ? 1.4255 1.2735 1.1155 -0.2739 -0.0255 -0.1458 302 MQA B C3    
4187 C C5    . MQA E .   ? 1.4435 1.3411 1.1619 -0.2495 -0.0450 -0.1155 302 MQA B C5    
4188 C C6    . MQA E .   ? 1.3764 1.3017 1.1174 -0.2355 -0.0550 -0.0977 302 MQA B C6    
4189 C C7    . MQA E .   ? 1.4250 1.3800 1.1888 -0.2315 -0.0654 -0.0826 302 MQA B C7    
4190 C C8    . MQA E .   ? 1.4780 1.4361 1.2411 -0.2420 -0.0671 -0.0852 302 MQA B C8    
4191 C C9    . MQA E .   ? 1.4573 1.3807 1.1896 -0.2716 -0.0561 -0.1106 302 MQA B C9    
4192 C C10   . MQA E .   ? 1.4063 1.3397 1.1628 -0.2598 -0.0584 -0.1039 302 MQA B C10   
4193 C C11   . MQA E .   ? 1.5250 1.4997 1.2668 -0.2960 -0.0766 -0.0918 302 MQA B C11   
4194 O O5    . MQA E .   ? 1.4432 1.3178 1.1453 -0.2524 -0.0356 -0.1269 302 MQA B O5    
4195 C CM6   . MQA E .   ? 1.3142 1.2376 1.0567 -0.2252 -0.0537 -0.0943 302 MQA B CM6   
4196 O O7    . MQA E .   ? 1.4290 1.4082 1.2152 -0.2186 -0.0727 -0.0659 302 MQA B O7    
4197 C C24   . MQA E .   ? 1.4241 1.4273 1.2045 -0.2300 -0.0821 -0.0538 302 MQA B C24   
4198 O O8    . MQA E .   ? 1.4902 1.4718 1.2716 -0.2383 -0.0745 -0.0729 302 MQA B O8    
4199 C C4A   . MQA E .   ? 1.4481 1.3482 1.1659 -0.2603 -0.0466 -0.1179 302 MQA B C4A   
4200 C C8A   . MQA E .   ? 1.4582 1.3898 1.1992 -0.2564 -0.0584 -0.1023 302 MQA B C8A   
4201 N N4    . MQA E .   ? 1.4630 1.3444 1.1688 -0.2711 -0.0395 -0.1298 302 MQA B N4    
4202 C C9A   . MQA E .   ? 1.4801 1.3667 1.1935 -0.2761 -0.0419 -0.1289 302 MQA B C9A   
4203 O O24   . MQA E .   ? 1.4370 1.3137 1.1259 -0.3008 -0.0393 -0.1394 302 MQA B O24   
4204 C C25   . MQA E .   ? 1.3852 1.2711 1.0772 -0.3115 -0.0437 -0.1376 302 MQA B C25   
4205 N N2    . MQA E .   ? 1.3277 1.1785 1.0691 -0.2350 -0.0240 -0.1355 302 MQA B N2    
4206 O O10   . MQA E .   ? 1.4217 1.3752 1.1785 -0.2747 -0.0667 -0.0978 302 MQA B O10   
4207 O O11   . MQA E .   ? 1.5374 1.5301 1.2802 -0.2952 -0.0832 -0.0819 302 MQA B O11   
4208 N N12   . MQA E .   ? 1.5571 1.5325 1.2822 -0.3202 -0.0788 -0.0970 302 MQA B N12   
4209 O O     . HOH F .   ? 0.8516 0.6391 0.8192 -0.0382 0.0360  -0.0203 401 HOH A O     
4210 O O     . HOH F .   ? 0.8362 0.6444 0.6765 -0.0443 0.0404  0.0487  402 HOH A O     
4211 O O     . HOH G .   ? 1.6020 1.1277 1.0245 -0.3757 0.1671  -0.3213 401 HOH B O     
4212 O O     . HOH G .   ? 1.2151 1.0165 0.6721 -0.3336 0.0313  -0.1775 402 HOH B O     
# 
