data_8ZU5
# 
_entry.id   8ZU5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZU5         pdb_00008zu5 10.2210/pdb8zu5/pdb 
WWPDB D_1300048485 ?            ?                   
# 
_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       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        8ZU5 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-07 
_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                 3 
_pdbx_contact_author.email              feixu@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Fei 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1077-0431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, F.'  1 ? 
'Fan, S.' 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                     'Crystal Structure of Methyl parathion hydrolase mutant A66D/I143V/I145L/Q272D/S279A/' 
_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 'Xu, F.'  1 ? 
primary 'Fan, S.' 2 ? 
primary 'Li, Y.'  3 ? 
# 
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 'Methyl parathion hydrolase' 31219.289 2   ? 'A66D, I143V, I145L, Q272D, S279A' ? ? 
2 non-polymer syn 'ZINC ION'                   65.409    4   ? ?                                  ? ? 
3 water       nat water                        18.015    362 ? ?                                  ? ? 
# 
_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       
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVDLPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLAANLKAAGYQPEQVDEVYLTHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTDLDS
DSKAVAVERKKAFADAAKGGYLIAASHLSFPGIGHIRAEGKGYRFVPVNYSVVN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVDLPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLAANLKAAGYQPEQVDEVYLTHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTDLDS
DSKAVAVERKKAFADAAKGGYLIAASHLSFPGIGHIRAEGKGYRFVPVNYSVVN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ALA n 
1 3   PRO n 
1 4   GLN n 
1 5   VAL n 
1 6   ARG n 
1 7   THR n 
1 8   SER n 
1 9   ALA n 
1 10  PRO n 
1 11  GLY n 
1 12  TYR n 
1 13  TYR n 
1 14  ARG n 
1 15  MET n 
1 16  LEU n 
1 17  LEU n 
1 18  GLY n 
1 19  ASP n 
1 20  PHE n 
1 21  GLU n 
1 22  ILE n 
1 23  THR n 
1 24  ALA n 
1 25  LEU n 
1 26  SER n 
1 27  ASP n 
1 28  GLY n 
1 29  THR n 
1 30  VAL n 
1 31  ASP n 
1 32  LEU n 
1 33  PRO n 
1 34  VAL n 
1 35  ASP n 
1 36  LYS n 
1 37  ARG n 
1 38  LEU n 
1 39  ASN n 
1 40  GLN n 
1 41  PRO n 
1 42  ALA n 
1 43  PRO n 
1 44  LYS n 
1 45  THR n 
1 46  GLN n 
1 47  SER n 
1 48  ALA n 
1 49  LEU n 
1 50  ALA n 
1 51  LYS n 
1 52  SER n 
1 53  PHE n 
1 54  GLN n 
1 55  LYS n 
1 56  ALA n 
1 57  PRO n 
1 58  LEU n 
1 59  GLU n 
1 60  THR n 
1 61  SER n 
1 62  VAL n 
1 63  THR n 
1 64  GLY n 
1 65  TYR n 
1 66  LEU n 
1 67  VAL n 
1 68  ASN n 
1 69  THR n 
1 70  GLY n 
1 71  SER n 
1 72  LYS n 
1 73  LEU n 
1 74  VAL n 
1 75  LEU n 
1 76  VAL n 
1 77  ASP n 
1 78  THR n 
1 79  GLY n 
1 80  ALA n 
1 81  ALA n 
1 82  GLY n 
1 83  LEU n 
1 84  PHE n 
1 85  GLY n 
1 86  PRO n 
1 87  THR n 
1 88  LEU n 
1 89  GLY n 
1 90  ARG n 
1 91  LEU n 
1 92  ALA n 
1 93  ALA n 
1 94  ASN n 
1 95  LEU n 
1 96  LYS n 
1 97  ALA n 
1 98  ALA n 
1 99  GLY n 
1 100 TYR n 
1 101 GLN n 
1 102 PRO n 
1 103 GLU n 
1 104 GLN n 
1 105 VAL n 
1 106 ASP n 
1 107 GLU n 
1 108 VAL n 
1 109 TYR n 
1 110 LEU n 
1 111 THR n 
1 112 HIS n 
1 113 MET n 
1 114 HIS n 
1 115 PRO n 
1 116 ASP n 
1 117 HIS n 
1 118 VAL n 
1 119 GLY n 
1 120 GLY n 
1 121 LEU n 
1 122 MET n 
1 123 VAL n 
1 124 GLY n 
1 125 GLU n 
1 126 GLN n 
1 127 LEU n 
1 128 ALA n 
1 129 PHE n 
1 130 PRO n 
1 131 ASN n 
1 132 ALA n 
1 133 VAL n 
1 134 VAL n 
1 135 ARG n 
1 136 ALA n 
1 137 ASP n 
1 138 GLN n 
1 139 LYS n 
1 140 GLU n 
1 141 ALA n 
1 142 ASP n 
1 143 PHE n 
1 144 TRP n 
1 145 LEU n 
1 146 SER n 
1 147 GLN n 
1 148 THR n 
1 149 ASN n 
1 150 LEU n 
1 151 ASP n 
1 152 LYS n 
1 153 ALA n 
1 154 PRO n 
1 155 ASP n 
1 156 ASP n 
1 157 GLU n 
1 158 SER n 
1 159 LYS n 
1 160 GLY n 
1 161 PHE n 
1 162 PHE n 
1 163 LYS n 
1 164 GLY n 
1 165 ALA n 
1 166 MET n 
1 167 ALA n 
1 168 SER n 
1 169 LEU n 
1 170 ASN n 
1 171 PRO n 
1 172 TYR n 
1 173 VAL n 
1 174 LYS n 
1 175 ALA n 
1 176 GLY n 
1 177 LYS n 
1 178 PHE n 
1 179 LYS n 
1 180 PRO n 
1 181 PHE n 
1 182 SER n 
1 183 GLY n 
1 184 ASN n 
1 185 THR n 
1 186 ASP n 
1 187 LEU n 
1 188 VAL n 
1 189 PRO n 
1 190 GLY n 
1 191 ILE n 
1 192 LYS n 
1 193 ALA n 
1 194 LEU n 
1 195 ALA n 
1 196 SER n 
1 197 HIS n 
1 198 GLY n 
1 199 HIS n 
1 200 THR n 
1 201 PRO n 
1 202 GLY n 
1 203 HIS n 
1 204 THR n 
1 205 THR n 
1 206 TYR n 
1 207 VAL n 
1 208 VAL n 
1 209 GLU n 
1 210 SER n 
1 211 GLN n 
1 212 GLY n 
1 213 GLN n 
1 214 LYS n 
1 215 LEU n 
1 216 ALA n 
1 217 LEU n 
1 218 LEU n 
1 219 GLY n 
1 220 ASP n 
1 221 LEU n 
1 222 ILE n 
1 223 LEU n 
1 224 VAL n 
1 225 ALA n 
1 226 ALA n 
1 227 VAL n 
1 228 GLN n 
1 229 PHE n 
1 230 ASP n 
1 231 ASP n 
1 232 PRO n 
1 233 SER n 
1 234 VAL n 
1 235 THR n 
1 236 THR n 
1 237 ASP n 
1 238 LEU n 
1 239 ASP n 
1 240 SER n 
1 241 ASP n 
1 242 SER n 
1 243 LYS n 
1 244 ALA n 
1 245 VAL n 
1 246 ALA n 
1 247 VAL n 
1 248 GLU n 
1 249 ARG n 
1 250 LYS n 
1 251 LYS n 
1 252 ALA n 
1 253 PHE n 
1 254 ALA n 
1 255 ASP n 
1 256 ALA n 
1 257 ALA n 
1 258 LYS n 
1 259 GLY n 
1 260 GLY n 
1 261 TYR n 
1 262 LEU n 
1 263 ILE n 
1 264 ALA n 
1 265 ALA n 
1 266 SER n 
1 267 HIS n 
1 268 LEU n 
1 269 SER n 
1 270 PHE n 
1 271 PRO n 
1 272 GLY n 
1 273 ILE n 
1 274 GLY n 
1 275 HIS n 
1 276 ILE n 
1 277 ARG n 
1 278 ALA n 
1 279 GLU n 
1 280 GLY n 
1 281 LYS n 
1 282 GLY n 
1 283 TYR n 
1 284 ARG n 
1 285 PHE n 
1 286 VAL n 
1 287 PRO n 
1 288 VAL n 
1 289 ASN n 
1 290 TYR n 
1 291 SER n 
1 292 VAL n 
1 293 VAL n 
1 294 ASN 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                   294 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mpd 
_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      'Pseudomonas sp. WBC-3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     165468 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   36  36  ALA ALA A . n 
A 1 2   ALA 2   37  37  ALA ALA A . n 
A 1 3   PRO 3   38  38  PRO PRO A . n 
A 1 4   GLN 4   39  39  GLN GLN A . n 
A 1 5   VAL 5   40  40  VAL VAL A . n 
A 1 6   ARG 6   41  41  ARG ARG A . n 
A 1 7   THR 7   42  42  THR THR A . n 
A 1 8   SER 8   43  43  SER SER A . n 
A 1 9   ALA 9   44  44  ALA ALA A . n 
A 1 10  PRO 10  45  45  PRO PRO A . n 
A 1 11  GLY 11  46  46  GLY GLY A . n 
A 1 12  TYR 12  47  47  TYR TYR A . n 
A 1 13  TYR 13  48  48  TYR TYR A . n 
A 1 14  ARG 14  49  49  ARG ARG A . n 
A 1 15  MET 15  50  50  MET MET A . n 
A 1 16  LEU 16  51  51  LEU LEU A . n 
A 1 17  LEU 17  52  52  LEU LEU A . n 
A 1 18  GLY 18  53  53  GLY GLY A . n 
A 1 19  ASP 19  54  54  ASP ASP A . n 
A 1 20  PHE 20  55  55  PHE PHE A . n 
A 1 21  GLU 21  56  56  GLU GLU A . n 
A 1 22  ILE 22  57  57  ILE ILE A . n 
A 1 23  THR 23  58  58  THR THR A . n 
A 1 24  ALA 24  59  59  ALA ALA A . n 
A 1 25  LEU 25  60  60  LEU LEU A . n 
A 1 26  SER 26  61  61  SER SER A . n 
A 1 27  ASP 27  62  62  ASP ASP A . n 
A 1 28  GLY 28  63  63  GLY GLY A . n 
A 1 29  THR 29  64  64  THR THR A . n 
A 1 30  VAL 30  65  65  VAL VAL A . n 
A 1 31  ASP 31  66  66  ASP ASP A . n 
A 1 32  LEU 32  67  67  LEU LEU A . n 
A 1 33  PRO 33  68  68  PRO PRO A . n 
A 1 34  VAL 34  69  69  VAL VAL A . n 
A 1 35  ASP 35  70  70  ASP ASP A . n 
A 1 36  LYS 36  71  71  LYS LYS A . n 
A 1 37  ARG 37  72  72  ARG ARG A . n 
A 1 38  LEU 38  73  73  LEU LEU A . n 
A 1 39  ASN 39  74  74  ASN ASN A . n 
A 1 40  GLN 40  75  75  GLN GLN A . n 
A 1 41  PRO 41  76  76  PRO PRO A . n 
A 1 42  ALA 42  77  77  ALA ALA A . n 
A 1 43  PRO 43  78  78  PRO PRO A . n 
A 1 44  LYS 44  79  79  LYS LYS A . n 
A 1 45  THR 45  80  80  THR THR A . n 
A 1 46  GLN 46  81  81  GLN GLN A . n 
A 1 47  SER 47  82  82  SER SER A . n 
A 1 48  ALA 48  83  83  ALA ALA A . n 
A 1 49  LEU 49  84  84  LEU LEU A . n 
A 1 50  ALA 50  85  85  ALA ALA A . n 
A 1 51  LYS 51  86  86  LYS LYS A . n 
A 1 52  SER 52  87  87  SER SER A . n 
A 1 53  PHE 53  88  88  PHE PHE A . n 
A 1 54  GLN 54  89  89  GLN GLN A . n 
A 1 55  LYS 55  90  90  LYS LYS A . n 
A 1 56  ALA 56  91  91  ALA ALA A . n 
A 1 57  PRO 57  92  92  PRO PRO A . n 
A 1 58  LEU 58  93  93  LEU LEU A . n 
A 1 59  GLU 59  94  94  GLU GLU A . n 
A 1 60  THR 60  95  95  THR THR A . n 
A 1 61  SER 61  96  96  SER SER A . n 
A 1 62  VAL 62  97  97  VAL VAL A . n 
A 1 63  THR 63  98  98  THR THR A . n 
A 1 64  GLY 64  99  99  GLY GLY A . n 
A 1 65  TYR 65  100 100 TYR TYR A . n 
A 1 66  LEU 66  101 101 LEU LEU A . n 
A 1 67  VAL 67  102 102 VAL VAL A . n 
A 1 68  ASN 68  103 103 ASN ASN A . n 
A 1 69  THR 69  104 104 THR THR A . n 
A 1 70  GLY 70  105 105 GLY GLY A . n 
A 1 71  SER 71  106 106 SER SER A . n 
A 1 72  LYS 72  107 107 LYS LYS A . n 
A 1 73  LEU 73  108 108 LEU LEU A . n 
A 1 74  VAL 74  109 109 VAL VAL A . n 
A 1 75  LEU 75  110 110 LEU LEU A . n 
A 1 76  VAL 76  111 111 VAL VAL A . n 
A 1 77  ASP 77  112 112 ASP ASP A . n 
A 1 78  THR 78  113 113 THR THR A . n 
A 1 79  GLY 79  114 114 GLY GLY A . n 
A 1 80  ALA 80  115 115 ALA ALA A . n 
A 1 81  ALA 81  116 116 ALA ALA A . n 
A 1 82  GLY 82  117 117 GLY GLY A . n 
A 1 83  LEU 83  118 118 LEU LEU A . n 
A 1 84  PHE 84  119 119 PHE PHE A . n 
A 1 85  GLY 85  120 120 GLY GLY A . n 
A 1 86  PRO 86  121 121 PRO PRO A . n 
A 1 87  THR 87  122 122 THR THR A . n 
A 1 88  LEU 88  123 123 LEU LEU A . n 
A 1 89  GLY 89  124 124 GLY GLY A . n 
A 1 90  ARG 90  125 125 ARG ARG A . n 
A 1 91  LEU 91  126 126 LEU LEU A . n 
A 1 92  ALA 92  127 127 ALA ALA A . n 
A 1 93  ALA 93  128 128 ALA ALA A . n 
A 1 94  ASN 94  129 129 ASN ASN A . n 
A 1 95  LEU 95  130 130 LEU LEU A . n 
A 1 96  LYS 96  131 131 LYS LYS A . n 
A 1 97  ALA 97  132 132 ALA ALA A . n 
A 1 98  ALA 98  133 133 ALA ALA A . n 
A 1 99  GLY 99  134 134 GLY GLY A . n 
A 1 100 TYR 100 135 135 TYR TYR A . n 
A 1 101 GLN 101 136 136 GLN GLN A . n 
A 1 102 PRO 102 137 137 PRO PRO A . n 
A 1 103 GLU 103 138 138 GLU GLU A . n 
A 1 104 GLN 104 139 139 GLN GLN A . n 
A 1 105 VAL 105 140 140 VAL VAL A . n 
A 1 106 ASP 106 141 141 ASP ASP A . n 
A 1 107 GLU 107 142 142 GLU GLU A . n 
A 1 108 VAL 108 143 143 VAL VAL A . n 
A 1 109 TYR 109 144 144 TYR TYR A . n 
A 1 110 LEU 110 145 145 LEU LEU A . n 
A 1 111 THR 111 146 146 THR THR A . n 
A 1 112 HIS 112 147 147 HIS HIS A . n 
A 1 113 MET 113 148 148 MET MET A . n 
A 1 114 HIS 114 149 149 HIS HIS A . n 
A 1 115 PRO 115 150 150 PRO PRO A . n 
A 1 116 ASP 116 151 151 ASP ASP A . n 
A 1 117 HIS 117 152 152 HIS HIS A . n 
A 1 118 VAL 118 153 153 VAL VAL A . n 
A 1 119 GLY 119 154 154 GLY GLY A . n 
A 1 120 GLY 120 155 155 GLY GLY A . n 
A 1 121 LEU 121 156 156 LEU LEU A . n 
A 1 122 MET 122 157 157 MET MET A . n 
A 1 123 VAL 123 158 158 VAL VAL A . n 
A 1 124 GLY 124 159 159 GLY GLY A . n 
A 1 125 GLU 125 160 160 GLU GLU A . n 
A 1 126 GLN 126 161 161 GLN GLN A . n 
A 1 127 LEU 127 162 162 LEU LEU A . n 
A 1 128 ALA 128 163 163 ALA ALA A . n 
A 1 129 PHE 129 164 164 PHE PHE A . n 
A 1 130 PRO 130 165 165 PRO PRO A . n 
A 1 131 ASN 131 166 166 ASN ASN A . n 
A 1 132 ALA 132 167 167 ALA ALA A . n 
A 1 133 VAL 133 168 168 VAL VAL A . n 
A 1 134 VAL 134 169 169 VAL VAL A . n 
A 1 135 ARG 135 170 170 ARG ARG A . n 
A 1 136 ALA 136 171 171 ALA ALA A . n 
A 1 137 ASP 137 172 172 ASP ASP A . n 
A 1 138 GLN 138 173 173 GLN GLN A . n 
A 1 139 LYS 139 174 174 LYS LYS A . n 
A 1 140 GLU 140 175 175 GLU GLU A . n 
A 1 141 ALA 141 176 176 ALA ALA A . n 
A 1 142 ASP 142 177 177 ASP ASP A . n 
A 1 143 PHE 143 178 178 PHE PHE A . n 
A 1 144 TRP 144 179 179 TRP TRP A . n 
A 1 145 LEU 145 180 180 LEU LEU A . n 
A 1 146 SER 146 181 181 SER SER A . n 
A 1 147 GLN 147 182 182 GLN GLN A . n 
A 1 148 THR 148 183 183 THR THR A . n 
A 1 149 ASN 149 184 184 ASN ASN A . n 
A 1 150 LEU 150 185 185 LEU LEU A . n 
A 1 151 ASP 151 186 186 ASP ASP A . n 
A 1 152 LYS 152 187 187 LYS LYS A . n 
A 1 153 ALA 153 188 188 ALA ALA A . n 
A 1 154 PRO 154 189 189 PRO PRO A . n 
A 1 155 ASP 155 190 190 ASP ASP A . n 
A 1 156 ASP 156 191 191 ASP ASP A . n 
A 1 157 GLU 157 192 192 GLU GLU A . n 
A 1 158 SER 158 193 193 SER SER A . n 
A 1 159 LYS 159 194 194 LYS LYS A . n 
A 1 160 GLY 160 195 195 GLY GLY A . n 
A 1 161 PHE 161 196 196 PHE PHE A . n 
A 1 162 PHE 162 197 197 PHE PHE A . n 
A 1 163 LYS 163 198 198 LYS LYS A . n 
A 1 164 GLY 164 199 199 GLY GLY A . n 
A 1 165 ALA 165 200 200 ALA ALA A . n 
A 1 166 MET 166 201 201 MET MET A . n 
A 1 167 ALA 167 202 202 ALA ALA A . n 
A 1 168 SER 168 203 203 SER SER A . n 
A 1 169 LEU 169 204 204 LEU LEU A . n 
A 1 170 ASN 170 205 205 ASN ASN A . n 
A 1 171 PRO 171 206 206 PRO PRO A . n 
A 1 172 TYR 172 207 207 TYR TYR A . n 
A 1 173 VAL 173 208 208 VAL VAL A . n 
A 1 174 LYS 174 209 209 LYS LYS A . n 
A 1 175 ALA 175 210 210 ALA ALA A . n 
A 1 176 GLY 176 211 211 GLY GLY A . n 
A 1 177 LYS 177 212 212 LYS LYS A . n 
A 1 178 PHE 178 213 213 PHE PHE A . n 
A 1 179 LYS 179 214 214 LYS LYS A . n 
A 1 180 PRO 180 215 215 PRO PRO A . n 
A 1 181 PHE 181 216 216 PHE PHE A . n 
A 1 182 SER 182 217 217 SER SER A . n 
A 1 183 GLY 183 218 218 GLY GLY A . n 
A 1 184 ASN 184 219 219 ASN ASN A . n 
A 1 185 THR 185 220 220 THR THR A . n 
A 1 186 ASP 186 221 221 ASP ASP A . n 
A 1 187 LEU 187 222 222 LEU LEU A . n 
A 1 188 VAL 188 223 223 VAL VAL A . n 
A 1 189 PRO 189 224 224 PRO PRO A . n 
A 1 190 GLY 190 225 225 GLY GLY A . n 
A 1 191 ILE 191 226 226 ILE ILE A . n 
A 1 192 LYS 192 227 227 LYS LYS A . n 
A 1 193 ALA 193 228 228 ALA ALA A . n 
A 1 194 LEU 194 229 229 LEU LEU A . n 
A 1 195 ALA 195 230 230 ALA ALA A . n 
A 1 196 SER 196 231 231 SER SER A . n 
A 1 197 HIS 197 232 232 HIS HIS A . n 
A 1 198 GLY 198 233 233 GLY GLY A . n 
A 1 199 HIS 199 234 234 HIS HIS A . n 
A 1 200 THR 200 235 235 THR THR A . n 
A 1 201 PRO 201 236 236 PRO PRO A . n 
A 1 202 GLY 202 237 237 GLY GLY A . n 
A 1 203 HIS 203 238 238 HIS HIS A . n 
A 1 204 THR 204 239 239 THR THR A . n 
A 1 205 THR 205 240 240 THR THR A . n 
A 1 206 TYR 206 241 241 TYR TYR A . n 
A 1 207 VAL 207 242 242 VAL VAL A . n 
A 1 208 VAL 208 243 243 VAL VAL A . n 
A 1 209 GLU 209 244 244 GLU GLU A . n 
A 1 210 SER 210 245 245 SER SER A . n 
A 1 211 GLN 211 246 246 GLN GLN A . n 
A 1 212 GLY 212 247 247 GLY GLY A . n 
A 1 213 GLN 213 248 248 GLN GLN A . n 
A 1 214 LYS 214 249 249 LYS LYS A . n 
A 1 215 LEU 215 250 250 LEU LEU A . n 
A 1 216 ALA 216 251 251 ALA ALA A . n 
A 1 217 LEU 217 252 252 LEU LEU A . n 
A 1 218 LEU 218 253 253 LEU LEU A . n 
A 1 219 GLY 219 254 254 GLY GLY A . n 
A 1 220 ASP 220 255 255 ASP ASP A . n 
A 1 221 LEU 221 256 256 LEU LEU A . n 
A 1 222 ILE 222 257 257 ILE ILE A . n 
A 1 223 LEU 223 258 258 LEU LEU A . n 
A 1 224 VAL 224 259 259 VAL VAL A . n 
A 1 225 ALA 225 260 260 ALA ALA A . n 
A 1 226 ALA 226 261 261 ALA ALA A . n 
A 1 227 VAL 227 262 262 VAL VAL A . n 
A 1 228 GLN 228 263 263 GLN GLN A . n 
A 1 229 PHE 229 264 264 PHE PHE A . n 
A 1 230 ASP 230 265 265 ASP ASP A . n 
A 1 231 ASP 231 266 266 ASP ASP A . n 
A 1 232 PRO 232 267 267 PRO PRO A . n 
A 1 233 SER 233 268 268 SER SER A . n 
A 1 234 VAL 234 269 269 VAL VAL A . n 
A 1 235 THR 235 270 270 THR THR A . n 
A 1 236 THR 236 271 271 THR THR A . n 
A 1 237 ASP 237 272 272 ASP ASP A . n 
A 1 238 LEU 238 273 273 LEU LEU A . n 
A 1 239 ASP 239 274 274 ASP ASP A . n 
A 1 240 SER 240 275 275 SER SER A . n 
A 1 241 ASP 241 276 276 ASP ASP A . n 
A 1 242 SER 242 277 277 SER SER A . n 
A 1 243 LYS 243 278 278 LYS LYS A . n 
A 1 244 ALA 244 279 279 ALA ALA A . n 
A 1 245 VAL 245 280 280 VAL VAL A . n 
A 1 246 ALA 246 281 281 ALA ALA A . n 
A 1 247 VAL 247 282 282 VAL VAL A . n 
A 1 248 GLU 248 283 283 GLU GLU A . n 
A 1 249 ARG 249 284 284 ARG ARG A . n 
A 1 250 LYS 250 285 285 LYS LYS A . n 
A 1 251 LYS 251 286 286 LYS LYS A . n 
A 1 252 ALA 252 287 287 ALA ALA A . n 
A 1 253 PHE 253 288 288 PHE PHE A . n 
A 1 254 ALA 254 289 289 ALA ALA A . n 
A 1 255 ASP 255 290 290 ASP ASP A . n 
A 1 256 ALA 256 291 291 ALA ALA A . n 
A 1 257 ALA 257 292 292 ALA ALA A . n 
A 1 258 LYS 258 293 293 LYS LYS A . n 
A 1 259 GLY 259 294 294 GLY GLY A . n 
A 1 260 GLY 260 295 295 GLY GLY A . n 
A 1 261 TYR 261 296 296 TYR TYR A . n 
A 1 262 LEU 262 297 297 LEU LEU A . n 
A 1 263 ILE 263 298 298 ILE ILE A . n 
A 1 264 ALA 264 299 299 ALA ALA A . n 
A 1 265 ALA 265 300 300 ALA ALA A . n 
A 1 266 SER 266 301 301 SER SER A . n 
A 1 267 HIS 267 302 302 HIS HIS A . n 
A 1 268 LEU 268 303 303 LEU LEU A . n 
A 1 269 SER 269 304 304 SER SER A . n 
A 1 270 PHE 270 305 305 PHE PHE A . n 
A 1 271 PRO 271 306 306 PRO PRO A . n 
A 1 272 GLY 272 307 307 GLY GLY A . n 
A 1 273 ILE 273 308 308 ILE ILE A . n 
A 1 274 GLY 274 309 309 GLY GLY A . n 
A 1 275 HIS 275 310 310 HIS HIS A . n 
A 1 276 ILE 276 311 311 ILE ILE A . n 
A 1 277 ARG 277 312 312 ARG ARG A . n 
A 1 278 ALA 278 313 313 ALA ALA A . n 
A 1 279 GLU 279 314 314 GLU GLU A . n 
A 1 280 GLY 280 315 315 GLY GLY A . n 
A 1 281 LYS 281 316 316 LYS LYS A . n 
A 1 282 GLY 282 317 317 GLY GLY A . n 
A 1 283 TYR 283 318 318 TYR TYR A . n 
A 1 284 ARG 284 319 319 ARG ARG A . n 
A 1 285 PHE 285 320 320 PHE PHE A . n 
A 1 286 VAL 286 321 321 VAL VAL A . n 
A 1 287 PRO 287 322 322 PRO PRO A . n 
A 1 288 VAL 288 323 323 VAL VAL A . n 
A 1 289 ASN 289 324 324 ASN ASN A . n 
A 1 290 TYR 290 325 325 TYR TYR A . n 
A 1 291 SER 291 326 326 SER SER A . n 
A 1 292 VAL 292 327 327 VAL VAL A . n 
A 1 293 VAL 293 328 328 VAL VAL A . n 
A 1 294 ASN 294 329 329 ASN ASN A . n 
B 1 1   ALA 1   36  36  ALA ALA B . n 
B 1 2   ALA 2   37  37  ALA ALA B . n 
B 1 3   PRO 3   38  38  PRO PRO B . n 
B 1 4   GLN 4   39  39  GLN GLN B . n 
B 1 5   VAL 5   40  40  VAL VAL B . n 
B 1 6   ARG 6   41  41  ARG ARG B . n 
B 1 7   THR 7   42  42  THR THR B . n 
B 1 8   SER 8   43  43  SER SER B . n 
B 1 9   ALA 9   44  44  ALA ALA B . n 
B 1 10  PRO 10  45  45  PRO PRO B . n 
B 1 11  GLY 11  46  46  GLY GLY B . n 
B 1 12  TYR 12  47  47  TYR TYR B . n 
B 1 13  TYR 13  48  48  TYR TYR B . n 
B 1 14  ARG 14  49  49  ARG ARG B . n 
B 1 15  MET 15  50  50  MET MET B . n 
B 1 16  LEU 16  51  51  LEU LEU B . n 
B 1 17  LEU 17  52  52  LEU LEU B . n 
B 1 18  GLY 18  53  53  GLY GLY B . n 
B 1 19  ASP 19  54  54  ASP ASP B . n 
B 1 20  PHE 20  55  55  PHE PHE B . n 
B 1 21  GLU 21  56  56  GLU GLU B . n 
B 1 22  ILE 22  57  57  ILE ILE B . n 
B 1 23  THR 23  58  58  THR THR B . n 
B 1 24  ALA 24  59  59  ALA ALA B . n 
B 1 25  LEU 25  60  60  LEU LEU B . n 
B 1 26  SER 26  61  61  SER SER B . n 
B 1 27  ASP 27  62  62  ASP ASP B . n 
B 1 28  GLY 28  63  63  GLY GLY B . n 
B 1 29  THR 29  64  64  THR THR B . n 
B 1 30  VAL 30  65  65  VAL VAL B . n 
B 1 31  ASP 31  66  66  ASP ASP B . n 
B 1 32  LEU 32  67  67  LEU LEU B . n 
B 1 33  PRO 33  68  68  PRO PRO B . n 
B 1 34  VAL 34  69  69  VAL VAL B . n 
B 1 35  ASP 35  70  70  ASP ASP B . n 
B 1 36  LYS 36  71  71  LYS LYS B . n 
B 1 37  ARG 37  72  72  ARG ARG B . n 
B 1 38  LEU 38  73  73  LEU LEU B . n 
B 1 39  ASN 39  74  74  ASN ASN B . n 
B 1 40  GLN 40  75  75  GLN GLN B . n 
B 1 41  PRO 41  76  76  PRO PRO B . n 
B 1 42  ALA 42  77  77  ALA ALA B . n 
B 1 43  PRO 43  78  78  PRO PRO B . n 
B 1 44  LYS 44  79  79  LYS LYS B . n 
B 1 45  THR 45  80  80  THR THR B . n 
B 1 46  GLN 46  81  81  GLN GLN B . n 
B 1 47  SER 47  82  82  SER SER B . n 
B 1 48  ALA 48  83  83  ALA ALA B . n 
B 1 49  LEU 49  84  84  LEU LEU B . n 
B 1 50  ALA 50  85  85  ALA ALA B . n 
B 1 51  LYS 51  86  86  LYS LYS B . n 
B 1 52  SER 52  87  87  SER SER B . n 
B 1 53  PHE 53  88  88  PHE PHE B . n 
B 1 54  GLN 54  89  89  GLN GLN B . n 
B 1 55  LYS 55  90  90  LYS LYS B . n 
B 1 56  ALA 56  91  91  ALA ALA B . n 
B 1 57  PRO 57  92  92  PRO PRO B . n 
B 1 58  LEU 58  93  93  LEU LEU B . n 
B 1 59  GLU 59  94  94  GLU GLU B . n 
B 1 60  THR 60  95  95  THR THR B . n 
B 1 61  SER 61  96  96  SER SER B . n 
B 1 62  VAL 62  97  97  VAL VAL B . n 
B 1 63  THR 63  98  98  THR THR B . n 
B 1 64  GLY 64  99  99  GLY GLY B . n 
B 1 65  TYR 65  100 100 TYR TYR B . n 
B 1 66  LEU 66  101 101 LEU LEU B . n 
B 1 67  VAL 67  102 102 VAL VAL B . n 
B 1 68  ASN 68  103 103 ASN ASN B . n 
B 1 69  THR 69  104 104 THR THR B . n 
B 1 70  GLY 70  105 105 GLY GLY B . n 
B 1 71  SER 71  106 106 SER SER B . n 
B 1 72  LYS 72  107 107 LYS LYS B . n 
B 1 73  LEU 73  108 108 LEU LEU B . n 
B 1 74  VAL 74  109 109 VAL VAL B . n 
B 1 75  LEU 75  110 110 LEU LEU B . n 
B 1 76  VAL 76  111 111 VAL VAL B . n 
B 1 77  ASP 77  112 112 ASP ASP B . n 
B 1 78  THR 78  113 113 THR THR B . n 
B 1 79  GLY 79  114 114 GLY GLY B . n 
B 1 80  ALA 80  115 115 ALA ALA B . n 
B 1 81  ALA 81  116 116 ALA ALA B . n 
B 1 82  GLY 82  117 117 GLY GLY B . n 
B 1 83  LEU 83  118 118 LEU LEU B . n 
B 1 84  PHE 84  119 119 PHE PHE B . n 
B 1 85  GLY 85  120 120 GLY GLY B . n 
B 1 86  PRO 86  121 121 PRO PRO B . n 
B 1 87  THR 87  122 122 THR THR B . n 
B 1 88  LEU 88  123 123 LEU LEU B . n 
B 1 89  GLY 89  124 124 GLY GLY B . n 
B 1 90  ARG 90  125 125 ARG ARG B . n 
B 1 91  LEU 91  126 126 LEU LEU B . n 
B 1 92  ALA 92  127 127 ALA ALA B . n 
B 1 93  ALA 93  128 128 ALA ALA B . n 
B 1 94  ASN 94  129 129 ASN ASN B . n 
B 1 95  LEU 95  130 130 LEU LEU B . n 
B 1 96  LYS 96  131 131 LYS LYS B . n 
B 1 97  ALA 97  132 132 ALA ALA B . n 
B 1 98  ALA 98  133 133 ALA ALA B . n 
B 1 99  GLY 99  134 134 GLY GLY B . n 
B 1 100 TYR 100 135 135 TYR TYR B . n 
B 1 101 GLN 101 136 136 GLN GLN B . n 
B 1 102 PRO 102 137 137 PRO PRO B . n 
B 1 103 GLU 103 138 138 GLU GLU B . n 
B 1 104 GLN 104 139 139 GLN GLN B . n 
B 1 105 VAL 105 140 140 VAL VAL B . n 
B 1 106 ASP 106 141 141 ASP ASP B . n 
B 1 107 GLU 107 142 142 GLU GLU B . n 
B 1 108 VAL 108 143 143 VAL VAL B . n 
B 1 109 TYR 109 144 144 TYR TYR B . n 
B 1 110 LEU 110 145 145 LEU LEU B . n 
B 1 111 THR 111 146 146 THR THR B . n 
B 1 112 HIS 112 147 147 HIS HIS B . n 
B 1 113 MET 113 148 148 MET MET B . n 
B 1 114 HIS 114 149 149 HIS HIS B . n 
B 1 115 PRO 115 150 150 PRO PRO B . n 
B 1 116 ASP 116 151 151 ASP ASP B . n 
B 1 117 HIS 117 152 152 HIS HIS B . n 
B 1 118 VAL 118 153 153 VAL VAL B . n 
B 1 119 GLY 119 154 154 GLY GLY B . n 
B 1 120 GLY 120 155 155 GLY GLY B . n 
B 1 121 LEU 121 156 156 LEU LEU B . n 
B 1 122 MET 122 157 157 MET MET B . n 
B 1 123 VAL 123 158 158 VAL VAL B . n 
B 1 124 GLY 124 159 159 GLY GLY B . n 
B 1 125 GLU 125 160 160 GLU GLU B . n 
B 1 126 GLN 126 161 161 GLN GLN B . n 
B 1 127 LEU 127 162 162 LEU LEU B . n 
B 1 128 ALA 128 163 163 ALA ALA B . n 
B 1 129 PHE 129 164 164 PHE PHE B . n 
B 1 130 PRO 130 165 165 PRO PRO B . n 
B 1 131 ASN 131 166 166 ASN ASN B . n 
B 1 132 ALA 132 167 167 ALA ALA B . n 
B 1 133 VAL 133 168 168 VAL VAL B . n 
B 1 134 VAL 134 169 169 VAL VAL B . n 
B 1 135 ARG 135 170 170 ARG ARG B . n 
B 1 136 ALA 136 171 171 ALA ALA B . n 
B 1 137 ASP 137 172 172 ASP ASP B . n 
B 1 138 GLN 138 173 173 GLN GLN B . n 
B 1 139 LYS 139 174 174 LYS LYS B . n 
B 1 140 GLU 140 175 175 GLU GLU B . n 
B 1 141 ALA 141 176 176 ALA ALA B . n 
B 1 142 ASP 142 177 177 ASP ASP B . n 
B 1 143 PHE 143 178 178 PHE PHE B . n 
B 1 144 TRP 144 179 179 TRP TRP B . n 
B 1 145 LEU 145 180 180 LEU LEU B . n 
B 1 146 SER 146 181 181 SER SER B . n 
B 1 147 GLN 147 182 182 GLN GLN B . n 
B 1 148 THR 148 183 183 THR THR B . n 
B 1 149 ASN 149 184 184 ASN ASN B . n 
B 1 150 LEU 150 185 185 LEU LEU B . n 
B 1 151 ASP 151 186 186 ASP ASP B . n 
B 1 152 LYS 152 187 187 LYS LYS B . n 
B 1 153 ALA 153 188 188 ALA ALA B . n 
B 1 154 PRO 154 189 189 PRO PRO B . n 
B 1 155 ASP 155 190 190 ASP ASP B . n 
B 1 156 ASP 156 191 191 ASP ASP B . n 
B 1 157 GLU 157 192 192 GLU GLU B . n 
B 1 158 SER 158 193 193 SER SER B . n 
B 1 159 LYS 159 194 194 LYS LYS B . n 
B 1 160 GLY 160 195 195 GLY GLY B . n 
B 1 161 PHE 161 196 196 PHE PHE B . n 
B 1 162 PHE 162 197 197 PHE PHE B . n 
B 1 163 LYS 163 198 198 LYS LYS B . n 
B 1 164 GLY 164 199 199 GLY GLY B . n 
B 1 165 ALA 165 200 200 ALA ALA B . n 
B 1 166 MET 166 201 201 MET MET B . n 
B 1 167 ALA 167 202 202 ALA ALA B . n 
B 1 168 SER 168 203 203 SER SER B . n 
B 1 169 LEU 169 204 204 LEU LEU B . n 
B 1 170 ASN 170 205 205 ASN ASN B . n 
B 1 171 PRO 171 206 206 PRO PRO B . n 
B 1 172 TYR 172 207 207 TYR TYR B . n 
B 1 173 VAL 173 208 208 VAL VAL B . n 
B 1 174 LYS 174 209 209 LYS LYS B . n 
B 1 175 ALA 175 210 210 ALA ALA B . n 
B 1 176 GLY 176 211 211 GLY GLY B . n 
B 1 177 LYS 177 212 212 LYS LYS B . n 
B 1 178 PHE 178 213 213 PHE PHE B . n 
B 1 179 LYS 179 214 214 LYS LYS B . n 
B 1 180 PRO 180 215 215 PRO PRO B . n 
B 1 181 PHE 181 216 216 PHE PHE B . n 
B 1 182 SER 182 217 217 SER SER B . n 
B 1 183 GLY 183 218 218 GLY GLY B . n 
B 1 184 ASN 184 219 219 ASN ASN B . n 
B 1 185 THR 185 220 220 THR THR B . n 
B 1 186 ASP 186 221 221 ASP ASP B . n 
B 1 187 LEU 187 222 222 LEU LEU B . n 
B 1 188 VAL 188 223 223 VAL VAL B . n 
B 1 189 PRO 189 224 224 PRO PRO B . n 
B 1 190 GLY 190 225 225 GLY GLY B . n 
B 1 191 ILE 191 226 226 ILE ILE B . n 
B 1 192 LYS 192 227 227 LYS LYS B . n 
B 1 193 ALA 193 228 228 ALA ALA B . n 
B 1 194 LEU 194 229 229 LEU LEU B . n 
B 1 195 ALA 195 230 230 ALA ALA B . n 
B 1 196 SER 196 231 231 SER SER B . n 
B 1 197 HIS 197 232 232 HIS HIS B . n 
B 1 198 GLY 198 233 233 GLY GLY B . n 
B 1 199 HIS 199 234 234 HIS HIS B . n 
B 1 200 THR 200 235 235 THR THR B . n 
B 1 201 PRO 201 236 236 PRO PRO B . n 
B 1 202 GLY 202 237 237 GLY GLY B . n 
B 1 203 HIS 203 238 238 HIS HIS B . n 
B 1 204 THR 204 239 239 THR THR B . n 
B 1 205 THR 205 240 240 THR THR B . n 
B 1 206 TYR 206 241 241 TYR TYR B . n 
B 1 207 VAL 207 242 242 VAL VAL B . n 
B 1 208 VAL 208 243 243 VAL VAL B . n 
B 1 209 GLU 209 244 244 GLU GLU B . n 
B 1 210 SER 210 245 245 SER SER B . n 
B 1 211 GLN 211 246 246 GLN GLN B . n 
B 1 212 GLY 212 247 247 GLY GLY B . n 
B 1 213 GLN 213 248 248 GLN GLN B . n 
B 1 214 LYS 214 249 249 LYS LYS B . n 
B 1 215 LEU 215 250 250 LEU LEU B . n 
B 1 216 ALA 216 251 251 ALA ALA B . n 
B 1 217 LEU 217 252 252 LEU LEU B . n 
B 1 218 LEU 218 253 253 LEU LEU B . n 
B 1 219 GLY 219 254 254 GLY GLY B . n 
B 1 220 ASP 220 255 255 ASP ASP B . n 
B 1 221 LEU 221 256 256 LEU LEU B . n 
B 1 222 ILE 222 257 257 ILE ILE B . n 
B 1 223 LEU 223 258 258 LEU LEU B . n 
B 1 224 VAL 224 259 259 VAL VAL B . n 
B 1 225 ALA 225 260 260 ALA ALA B . n 
B 1 226 ALA 226 261 261 ALA ALA B . n 
B 1 227 VAL 227 262 262 VAL VAL B . n 
B 1 228 GLN 228 263 263 GLN GLN B . n 
B 1 229 PHE 229 264 264 PHE PHE B . n 
B 1 230 ASP 230 265 265 ASP ASP B . n 
B 1 231 ASP 231 266 266 ASP ASP B . n 
B 1 232 PRO 232 267 267 PRO PRO B . n 
B 1 233 SER 233 268 268 SER SER B . n 
B 1 234 VAL 234 269 269 VAL VAL B . n 
B 1 235 THR 235 270 270 THR THR B . n 
B 1 236 THR 236 271 271 THR THR B . n 
B 1 237 ASP 237 272 272 ASP ASP B . n 
B 1 238 LEU 238 273 273 LEU LEU B . n 
B 1 239 ASP 239 274 274 ASP ASP B . n 
B 1 240 SER 240 275 275 SER SER B . n 
B 1 241 ASP 241 276 276 ASP ASP B . n 
B 1 242 SER 242 277 277 SER SER B . n 
B 1 243 LYS 243 278 278 LYS LYS B . n 
B 1 244 ALA 244 279 279 ALA ALA B . n 
B 1 245 VAL 245 280 280 VAL VAL B . n 
B 1 246 ALA 246 281 281 ALA ALA B . n 
B 1 247 VAL 247 282 282 VAL VAL B . n 
B 1 248 GLU 248 283 283 GLU GLU B . n 
B 1 249 ARG 249 284 284 ARG ARG B . n 
B 1 250 LYS 250 285 285 LYS LYS B . n 
B 1 251 LYS 251 286 286 LYS LYS B . n 
B 1 252 ALA 252 287 287 ALA ALA B . n 
B 1 253 PHE 253 288 288 PHE PHE B . n 
B 1 254 ALA 254 289 289 ALA ALA B . n 
B 1 255 ASP 255 290 290 ASP ASP B . n 
B 1 256 ALA 256 291 291 ALA ALA B . n 
B 1 257 ALA 257 292 292 ALA ALA B . n 
B 1 258 LYS 258 293 293 LYS LYS B . n 
B 1 259 GLY 259 294 294 GLY GLY B . n 
B 1 260 GLY 260 295 295 GLY GLY B . n 
B 1 261 TYR 261 296 296 TYR TYR B . n 
B 1 262 LEU 262 297 297 LEU LEU B . n 
B 1 263 ILE 263 298 298 ILE ILE B . n 
B 1 264 ALA 264 299 299 ALA ALA B . n 
B 1 265 ALA 265 300 300 ALA ALA B . n 
B 1 266 SER 266 301 301 SER SER B . n 
B 1 267 HIS 267 302 302 HIS HIS B . n 
B 1 268 LEU 268 303 303 LEU LEU B . n 
B 1 269 SER 269 304 304 SER SER B . n 
B 1 270 PHE 270 305 305 PHE PHE B . n 
B 1 271 PRO 271 306 306 PRO PRO B . n 
B 1 272 GLY 272 307 307 GLY GLY B . n 
B 1 273 ILE 273 308 308 ILE ILE B . n 
B 1 274 GLY 274 309 309 GLY GLY B . n 
B 1 275 HIS 275 310 310 HIS HIS B . n 
B 1 276 ILE 276 311 311 ILE ILE B . n 
B 1 277 ARG 277 312 312 ARG ARG B . n 
B 1 278 ALA 278 313 313 ALA ALA B . n 
B 1 279 GLU 279 314 314 GLU GLU B . n 
B 1 280 GLY 280 315 315 GLY GLY B . n 
B 1 281 LYS 281 316 316 LYS LYS B . n 
B 1 282 GLY 282 317 317 GLY GLY B . n 
B 1 283 TYR 283 318 318 TYR TYR B . n 
B 1 284 ARG 284 319 319 ARG ARG B . n 
B 1 285 PHE 285 320 320 PHE PHE B . n 
B 1 286 VAL 286 321 321 VAL VAL B . n 
B 1 287 PRO 287 322 322 PRO PRO B . n 
B 1 288 VAL 288 323 323 VAL VAL B . n 
B 1 289 ASN 289 324 324 ASN ASN B . n 
B 1 290 TYR 290 325 325 TYR TYR B . n 
B 1 291 SER 291 326 326 SER SER B . n 
B 1 292 VAL 292 327 327 VAL VAL B . n 
B 1 293 VAL 293 328 328 VAL VAL B . n 
B 1 294 ASN 294 329 329 ASN ASN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   401 3   ZN  ZN  A . 
D 2 ZN  1   402 4   ZN  ZN  A . 
E 2 ZN  1   401 1   ZN  ZN  B . 
F 2 ZN  1   402 2   ZN  ZN  B . 
G 3 HOH 1   501 426 HOH HOH A . 
G 3 HOH 2   502 341 HOH HOH A . 
G 3 HOH 3   503 214 HOH HOH A . 
G 3 HOH 4   504 179 HOH HOH A . 
G 3 HOH 5   505 96  HOH HOH A . 
G 3 HOH 6   506 342 HOH HOH A . 
G 3 HOH 7   507 229 HOH HOH A . 
G 3 HOH 8   508 397 HOH HOH A . 
G 3 HOH 9   509 13  HOH HOH A . 
G 3 HOH 10  510 25  HOH HOH A . 
G 3 HOH 11  511 213 HOH HOH A . 
G 3 HOH 12  512 32  HOH HOH A . 
G 3 HOH 13  513 259 HOH HOH A . 
G 3 HOH 14  514 299 HOH HOH A . 
G 3 HOH 15  515 33  HOH HOH A . 
G 3 HOH 16  516 131 HOH HOH A . 
G 3 HOH 17  517 68  HOH HOH A . 
G 3 HOH 18  518 127 HOH HOH A . 
G 3 HOH 19  519 31  HOH HOH A . 
G 3 HOH 20  520 70  HOH HOH A . 
G 3 HOH 21  521 151 HOH HOH A . 
G 3 HOH 22  522 337 HOH HOH A . 
G 3 HOH 23  523 119 HOH HOH A . 
G 3 HOH 24  524 207 HOH HOH A . 
G 3 HOH 25  525 155 HOH HOH A . 
G 3 HOH 26  526 271 HOH HOH A . 
G 3 HOH 27  527 35  HOH HOH A . 
G 3 HOH 28  528 10  HOH HOH A . 
G 3 HOH 29  529 161 HOH HOH A . 
G 3 HOH 30  530 128 HOH HOH A . 
G 3 HOH 31  531 85  HOH HOH A . 
G 3 HOH 32  532 258 HOH HOH A . 
G 3 HOH 33  533 126 HOH HOH A . 
G 3 HOH 34  534 312 HOH HOH A . 
G 3 HOH 35  535 208 HOH HOH A . 
G 3 HOH 36  536 78  HOH HOH A . 
G 3 HOH 37  537 420 HOH HOH A . 
G 3 HOH 38  538 308 HOH HOH A . 
G 3 HOH 39  539 82  HOH HOH A . 
G 3 HOH 40  540 93  HOH HOH A . 
G 3 HOH 41  541 56  HOH HOH A . 
G 3 HOH 42  542 24  HOH HOH A . 
G 3 HOH 43  543 326 HOH HOH A . 
G 3 HOH 44  544 142 HOH HOH A . 
G 3 HOH 45  545 205 HOH HOH A . 
G 3 HOH 46  546 371 HOH HOH A . 
G 3 HOH 47  547 37  HOH HOH A . 
G 3 HOH 48  548 177 HOH HOH A . 
G 3 HOH 49  549 20  HOH HOH A . 
G 3 HOH 50  550 7   HOH HOH A . 
G 3 HOH 51  551 315 HOH HOH A . 
G 3 HOH 52  552 281 HOH HOH A . 
G 3 HOH 53  553 16  HOH HOH A . 
G 3 HOH 54  554 382 HOH HOH A . 
G 3 HOH 55  555 74  HOH HOH A . 
G 3 HOH 56  556 44  HOH HOH A . 
G 3 HOH 57  557 95  HOH HOH A . 
G 3 HOH 58  558 379 HOH HOH A . 
G 3 HOH 59  559 27  HOH HOH A . 
G 3 HOH 60  560 199 HOH HOH A . 
G 3 HOH 61  561 245 HOH HOH A . 
G 3 HOH 62  562 113 HOH HOH A . 
G 3 HOH 63  563 282 HOH HOH A . 
G 3 HOH 64  564 377 HOH HOH A . 
G 3 HOH 65  565 120 HOH HOH A . 
G 3 HOH 66  566 224 HOH HOH A . 
G 3 HOH 67  567 279 HOH HOH A . 
G 3 HOH 68  568 50  HOH HOH A . 
G 3 HOH 69  569 65  HOH HOH A . 
G 3 HOH 70  570 30  HOH HOH A . 
G 3 HOH 71  571 99  HOH HOH A . 
G 3 HOH 72  572 252 HOH HOH A . 
G 3 HOH 73  573 255 HOH HOH A . 
G 3 HOH 74  574 55  HOH HOH A . 
G 3 HOH 75  575 197 HOH HOH A . 
G 3 HOH 76  576 169 HOH HOH A . 
G 3 HOH 77  577 306 HOH HOH A . 
G 3 HOH 78  578 181 HOH HOH A . 
G 3 HOH 79  579 86  HOH HOH A . 
G 3 HOH 80  580 272 HOH HOH A . 
G 3 HOH 81  581 15  HOH HOH A . 
G 3 HOH 82  582 23  HOH HOH A . 
G 3 HOH 83  583 206 HOH HOH A . 
G 3 HOH 84  584 116 HOH HOH A . 
G 3 HOH 85  585 110 HOH HOH A . 
G 3 HOH 86  586 289 HOH HOH A . 
G 3 HOH 87  587 231 HOH HOH A . 
G 3 HOH 88  588 107 HOH HOH A . 
G 3 HOH 89  589 194 HOH HOH A . 
G 3 HOH 90  590 72  HOH HOH A . 
G 3 HOH 91  591 162 HOH HOH A . 
G 3 HOH 92  592 77  HOH HOH A . 
G 3 HOH 93  593 314 HOH HOH A . 
G 3 HOH 94  594 389 HOH HOH A . 
G 3 HOH 95  595 8   HOH HOH A . 
G 3 HOH 96  596 98  HOH HOH A . 
G 3 HOH 97  597 230 HOH HOH A . 
G 3 HOH 98  598 36  HOH HOH A . 
G 3 HOH 99  599 106 HOH HOH A . 
G 3 HOH 100 600 81  HOH HOH A . 
G 3 HOH 101 601 263 HOH HOH A . 
G 3 HOH 102 602 103 HOH HOH A . 
G 3 HOH 103 603 22  HOH HOH A . 
G 3 HOH 104 604 352 HOH HOH A . 
G 3 HOH 105 605 143 HOH HOH A . 
G 3 HOH 106 606 111 HOH HOH A . 
G 3 HOH 107 607 58  HOH HOH A . 
G 3 HOH 108 608 108 HOH HOH A . 
G 3 HOH 109 609 250 HOH HOH A . 
G 3 HOH 110 610 278 HOH HOH A . 
G 3 HOH 111 611 380 HOH HOH A . 
G 3 HOH 112 612 191 HOH HOH A . 
G 3 HOH 113 613 236 HOH HOH A . 
G 3 HOH 114 614 76  HOH HOH A . 
G 3 HOH 115 615 268 HOH HOH A . 
G 3 HOH 116 616 270 HOH HOH A . 
G 3 HOH 117 617 292 HOH HOH A . 
G 3 HOH 118 618 283 HOH HOH A . 
G 3 HOH 119 619 83  HOH HOH A . 
G 3 HOH 120 620 254 HOH HOH A . 
G 3 HOH 121 621 61  HOH HOH A . 
G 3 HOH 122 622 201 HOH HOH A . 
G 3 HOH 123 623 267 HOH HOH A . 
G 3 HOH 124 624 34  HOH HOH A . 
G 3 HOH 125 625 12  HOH HOH A . 
G 3 HOH 126 626 18  HOH HOH A . 
G 3 HOH 127 627 41  HOH HOH A . 
G 3 HOH 128 628 67  HOH HOH A . 
G 3 HOH 129 629 295 HOH HOH A . 
G 3 HOH 130 630 80  HOH HOH A . 
G 3 HOH 131 631 101 HOH HOH A . 
G 3 HOH 132 632 399 HOH HOH A . 
G 3 HOH 133 633 150 HOH HOH A . 
G 3 HOH 134 634 90  HOH HOH A . 
G 3 HOH 135 635 365 HOH HOH A . 
G 3 HOH 136 636 139 HOH HOH A . 
G 3 HOH 137 637 361 HOH HOH A . 
G 3 HOH 138 638 359 HOH HOH A . 
G 3 HOH 139 639 311 HOH HOH A . 
G 3 HOH 140 640 121 HOH HOH A . 
G 3 HOH 141 641 332 HOH HOH A . 
G 3 HOH 142 642 232 HOH HOH A . 
G 3 HOH 143 643 422 HOH HOH A . 
G 3 HOH 144 644 192 HOH HOH A . 
G 3 HOH 145 645 410 HOH HOH A . 
G 3 HOH 146 646 114 HOH HOH A . 
G 3 HOH 147 647 221 HOH HOH A . 
G 3 HOH 148 648 347 HOH HOH A . 
G 3 HOH 149 649 172 HOH HOH A . 
G 3 HOH 150 650 247 HOH HOH A . 
G 3 HOH 151 651 275 HOH HOH A . 
G 3 HOH 152 652 367 HOH HOH A . 
G 3 HOH 153 653 302 HOH HOH A . 
G 3 HOH 154 654 145 HOH HOH A . 
G 3 HOH 155 655 349 HOH HOH A . 
G 3 HOH 156 656 287 HOH HOH A . 
G 3 HOH 157 657 280 HOH HOH A . 
G 3 HOH 158 658 251 HOH HOH A . 
G 3 HOH 159 659 211 HOH HOH A . 
G 3 HOH 160 660 141 HOH HOH A . 
G 3 HOH 161 661 235 HOH HOH A . 
G 3 HOH 162 662 187 HOH HOH A . 
G 3 HOH 163 663 385 HOH HOH A . 
G 3 HOH 164 664 239 HOH HOH A . 
G 3 HOH 165 665 39  HOH HOH A . 
G 3 HOH 166 666 156 HOH HOH A . 
G 3 HOH 167 667 73  HOH HOH A . 
G 3 HOH 168 668 241 HOH HOH A . 
G 3 HOH 169 669 48  HOH HOH A . 
G 3 HOH 170 670 174 HOH HOH A . 
G 3 HOH 171 671 220 HOH HOH A . 
G 3 HOH 172 672 387 HOH HOH A . 
G 3 HOH 173 673 152 HOH HOH A . 
G 3 HOH 174 674 403 HOH HOH A . 
G 3 HOH 175 675 273 HOH HOH A . 
G 3 HOH 176 676 104 HOH HOH A . 
H 3 HOH 1   501 148 HOH HOH B . 
H 3 HOH 2   502 370 HOH HOH B . 
H 3 HOH 3   503 123 HOH HOH B . 
H 3 HOH 4   504 416 HOH HOH B . 
H 3 HOH 5   505 350 HOH HOH B . 
H 3 HOH 6   506 327 HOH HOH B . 
H 3 HOH 7   507 242 HOH HOH B . 
H 3 HOH 8   508 237 HOH HOH B . 
H 3 HOH 9   509 262 HOH HOH B . 
H 3 HOH 10  510 421 HOH HOH B . 
H 3 HOH 11  511 19  HOH HOH B . 
H 3 HOH 12  512 401 HOH HOH B . 
H 3 HOH 13  513 59  HOH HOH B . 
H 3 HOH 14  514 29  HOH HOH B . 
H 3 HOH 15  515 392 HOH HOH B . 
H 3 HOH 16  516 43  HOH HOH B . 
H 3 HOH 17  517 166 HOH HOH B . 
H 3 HOH 18  518 180 HOH HOH B . 
H 3 HOH 19  519 28  HOH HOH B . 
H 3 HOH 20  520 165 HOH HOH B . 
H 3 HOH 21  521 146 HOH HOH B . 
H 3 HOH 22  522 353 HOH HOH B . 
H 3 HOH 23  523 419 HOH HOH B . 
H 3 HOH 24  524 158 HOH HOH B . 
H 3 HOH 25  525 64  HOH HOH B . 
H 3 HOH 26  526 408 HOH HOH B . 
H 3 HOH 27  527 414 HOH HOH B . 
H 3 HOH 28  528 79  HOH HOH B . 
H 3 HOH 29  529 9   HOH HOH B . 
H 3 HOH 30  530 305 HOH HOH B . 
H 3 HOH 31  531 183 HOH HOH B . 
H 3 HOH 32  532 336 HOH HOH B . 
H 3 HOH 33  533 40  HOH HOH B . 
H 3 HOH 34  534 277 HOH HOH B . 
H 3 HOH 35  535 105 HOH HOH B . 
H 3 HOH 36  536 218 HOH HOH B . 
H 3 HOH 37  537 94  HOH HOH B . 
H 3 HOH 38  538 135 HOH HOH B . 
H 3 HOH 39  539 285 HOH HOH B . 
H 3 HOH 40  540 5   HOH HOH B . 
H 3 HOH 41  541 351 HOH HOH B . 
H 3 HOH 42  542 204 HOH HOH B . 
H 3 HOH 43  543 46  HOH HOH B . 
H 3 HOH 44  544 284 HOH HOH B . 
H 3 HOH 45  545 6   HOH HOH B . 
H 3 HOH 46  546 388 HOH HOH B . 
H 3 HOH 47  547 53  HOH HOH B . 
H 3 HOH 48  548 60  HOH HOH B . 
H 3 HOH 49  549 248 HOH HOH B . 
H 3 HOH 50  550 200 HOH HOH B . 
H 3 HOH 51  551 233 HOH HOH B . 
H 3 HOH 52  552 69  HOH HOH B . 
H 3 HOH 53  553 309 HOH HOH B . 
H 3 HOH 54  554 89  HOH HOH B . 
H 3 HOH 55  555 154 HOH HOH B . 
H 3 HOH 56  556 147 HOH HOH B . 
H 3 HOH 57  557 26  HOH HOH B . 
H 3 HOH 58  558 386 HOH HOH B . 
H 3 HOH 59  559 225 HOH HOH B . 
H 3 HOH 60  560 182 HOH HOH B . 
H 3 HOH 61  561 3   HOH HOH B . 
H 3 HOH 62  562 296 HOH HOH B . 
H 3 HOH 63  563 167 HOH HOH B . 
H 3 HOH 64  564 223 HOH HOH B . 
H 3 HOH 65  565 2   HOH HOH B . 
H 3 HOH 66  566 238 HOH HOH B . 
H 3 HOH 67  567 178 HOH HOH B . 
H 3 HOH 68  568 84  HOH HOH B . 
H 3 HOH 69  569 391 HOH HOH B . 
H 3 HOH 70  570 133 HOH HOH B . 
H 3 HOH 71  571 369 HOH HOH B . 
H 3 HOH 72  572 216 HOH HOH B . 
H 3 HOH 73  573 42  HOH HOH B . 
H 3 HOH 74  574 261 HOH HOH B . 
H 3 HOH 75  575 157 HOH HOH B . 
H 3 HOH 76  576 4   HOH HOH B . 
H 3 HOH 77  577 265 HOH HOH B . 
H 3 HOH 78  578 175 HOH HOH B . 
H 3 HOH 79  579 227 HOH HOH B . 
H 3 HOH 80  580 170 HOH HOH B . 
H 3 HOH 81  581 102 HOH HOH B . 
H 3 HOH 82  582 92  HOH HOH B . 
H 3 HOH 83  583 63  HOH HOH B . 
H 3 HOH 84  584 71  HOH HOH B . 
H 3 HOH 85  585 188 HOH HOH B . 
H 3 HOH 86  586 185 HOH HOH B . 
H 3 HOH 87  587 17  HOH HOH B . 
H 3 HOH 88  588 115 HOH HOH B . 
H 3 HOH 89  589 38  HOH HOH B . 
H 3 HOH 90  590 112 HOH HOH B . 
H 3 HOH 91  591 124 HOH HOH B . 
H 3 HOH 92  592 176 HOH HOH B . 
H 3 HOH 93  593 310 HOH HOH B . 
H 3 HOH 94  594 91  HOH HOH B . 
H 3 HOH 95  595 171 HOH HOH B . 
H 3 HOH 96  596 138 HOH HOH B . 
H 3 HOH 97  597 355 HOH HOH B . 
H 3 HOH 98  598 240 HOH HOH B . 
H 3 HOH 99  599 260 HOH HOH B . 
H 3 HOH 100 600 212 HOH HOH B . 
H 3 HOH 101 601 196 HOH HOH B . 
H 3 HOH 102 602 117 HOH HOH B . 
H 3 HOH 103 603 343 HOH HOH B . 
H 3 HOH 104 604 132 HOH HOH B . 
H 3 HOH 105 605 49  HOH HOH B . 
H 3 HOH 106 606 228 HOH HOH B . 
H 3 HOH 107 607 62  HOH HOH B . 
H 3 HOH 108 608 209 HOH HOH B . 
H 3 HOH 109 609 109 HOH HOH B . 
H 3 HOH 110 610 198 HOH HOH B . 
H 3 HOH 111 611 288 HOH HOH B . 
H 3 HOH 112 612 11  HOH HOH B . 
H 3 HOH 113 613 297 HOH HOH B . 
H 3 HOH 114 614 97  HOH HOH B . 
H 3 HOH 115 615 164 HOH HOH B . 
H 3 HOH 116 616 219 HOH HOH B . 
H 3 HOH 117 617 184 HOH HOH B . 
H 3 HOH 118 618 163 HOH HOH B . 
H 3 HOH 119 619 75  HOH HOH B . 
H 3 HOH 120 620 193 HOH HOH B . 
H 3 HOH 121 621 293 HOH HOH B . 
H 3 HOH 122 622 45  HOH HOH B . 
H 3 HOH 123 623 202 HOH HOH B . 
H 3 HOH 124 624 47  HOH HOH B . 
H 3 HOH 125 625 290 HOH HOH B . 
H 3 HOH 126 626 303 HOH HOH B . 
H 3 HOH 127 627 274 HOH HOH B . 
H 3 HOH 128 628 14  HOH HOH B . 
H 3 HOH 129 629 203 HOH HOH B . 
H 3 HOH 130 630 173 HOH HOH B . 
H 3 HOH 131 631 189 HOH HOH B . 
H 3 HOH 132 632 51  HOH HOH B . 
H 3 HOH 133 633 307 HOH HOH B . 
H 3 HOH 134 634 256 HOH HOH B . 
H 3 HOH 135 635 122 HOH HOH B . 
H 3 HOH 136 636 234 HOH HOH B . 
H 3 HOH 137 637 300 HOH HOH B . 
H 3 HOH 138 638 1   HOH HOH B . 
H 3 HOH 139 639 57  HOH HOH B . 
H 3 HOH 140 640 210 HOH HOH B . 
H 3 HOH 141 641 190 HOH HOH B . 
H 3 HOH 142 642 321 HOH HOH B . 
H 3 HOH 143 643 118 HOH HOH B . 
H 3 HOH 144 644 264 HOH HOH B . 
H 3 HOH 145 645 407 HOH HOH B . 
H 3 HOH 146 646 244 HOH HOH B . 
H 3 HOH 147 647 253 HOH HOH B . 
H 3 HOH 148 648 324 HOH HOH B . 
H 3 HOH 149 649 291 HOH HOH B . 
H 3 HOH 150 650 301 HOH HOH B . 
H 3 HOH 151 651 269 HOH HOH B . 
H 3 HOH 152 652 226 HOH HOH B . 
H 3 HOH 153 653 276 HOH HOH B . 
H 3 HOH 154 654 398 HOH HOH B . 
H 3 HOH 155 655 140 HOH HOH B . 
H 3 HOH 156 656 396 HOH HOH B . 
H 3 HOH 157 657 137 HOH HOH B . 
H 3 HOH 158 658 266 HOH HOH B . 
H 3 HOH 159 659 257 HOH HOH B . 
H 3 HOH 160 660 390 HOH HOH B . 
H 3 HOH 161 661 316 HOH HOH B . 
H 3 HOH 162 662 195 HOH HOH B . 
H 3 HOH 163 663 136 HOH HOH B . 
H 3 HOH 164 664 54  HOH HOH B . 
H 3 HOH 165 665 286 HOH HOH B . 
H 3 HOH 166 666 21  HOH HOH B . 
H 3 HOH 167 667 243 HOH HOH B . 
H 3 HOH 168 668 217 HOH HOH B . 
H 3 HOH 169 669 134 HOH HOH B . 
H 3 HOH 170 670 186 HOH HOH B . 
H 3 HOH 171 671 125 HOH HOH B . 
H 3 HOH 172 672 375 HOH HOH B . 
H 3 HOH 173 673 412 HOH HOH B . 
H 3 HOH 174 674 129 HOH HOH B . 
H 3 HOH 175 675 144 HOH HOH B . 
H 3 HOH 176 676 88  HOH HOH B . 
H 3 HOH 177 677 149 HOH HOH B . 
H 3 HOH 178 678 294 HOH HOH B . 
H 3 HOH 179 679 383 HOH HOH B . 
H 3 HOH 180 680 160 HOH HOH B . 
H 3 HOH 181 681 100 HOH HOH B . 
H 3 HOH 182 682 215 HOH HOH B . 
H 3 HOH 183 683 130 HOH HOH B . 
H 3 HOH 184 684 381 HOH HOH B . 
H 3 HOH 185 685 400 HOH HOH B . 
H 3 HOH 186 686 66  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.33 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZU5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.801 
_cell.length_a_esd                 ? 
_cell.length_b                     83.719 
_cell.length_b_esd                 ? 
_cell.length_c                     115.492 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZU5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 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                   8ZU5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.81 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '25% PEG 3350,0.1 M Tris pH 8.6, 0.2 M NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-16 
_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   0.9781 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9781 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZU5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     48782 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.828 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.204 
_reflns.pdbx_Rpim_I_all                                0.086 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       269800 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.953 
_reflns.pdbx_CC_star                                   0.988 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.184 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.83 1.86  ? ? ? ? ? ? 2386 ? ? ? ? ? ? ? ? ? ? ? 5.1 0.734 ? ? 0.947 0.407 ? 1  1 0.782 0.937 ? 99.1 ? 0.851 ? ? ? ? ? ? ? ? ? 
1.86 1.90  ? ? ? ? ? ? 2482 ? ? ? ? ? ? ? ? ? ? ? 5.3 0.859 ? ? 0.805 0.337 ? 2  1 0.818 0.949 ? 99.8 ? 0.728 ? ? ? ? ? ? ? ? ? 
1.90 1.93  ? ? ? ? ? ? 2394 ? ? ? ? ? ? ? ? ? ? ? 5.5 0.975 ? ? 0.770 0.320 ? 3  1 0.838 0.955 ? 99.2 ? 0.698 ? ? ? ? ? ? ? ? ? 
1.93 1.97  ? ? ? ? ? ? 2489 ? ? ? ? ? ? ? ? ? ? ? 5.4 1.016 ? ? 0.665 0.277 ? 4  1 0.854 0.960 ? 99.1 ? 0.602 ? ? ? ? ? ? ? ? ? 
1.97 2.01  ? ? ? ? ? ? 2400 ? ? ? ? ? ? ? ? ? ? ? 5.5 1.066 ? ? 0.573 0.240 ? 5  1 0.898 0.973 ? 99.4 ? 0.519 ? ? ? ? ? ? ? ? ? 
2.01 2.06  ? ? ? ? ? ? 2473 ? ? ? ? ? ? ? ? ? ? ? 5.4 1.235 ? ? 0.531 0.223 ? 6  1 0.908 0.976 ? 99.2 ? 0.479 ? ? ? ? ? ? ? ? ? 
2.06 2.11  ? ? ? ? ? ? 2429 ? ? ? ? ? ? ? ? ? ? ? 5.4 1.372 ? ? 0.521 0.223 ? 7  1 0.994 0.998 ? 99.2 ? 0.467 ? ? ? ? ? ? ? ? ? 
2.11 2.17  ? ? ? ? ? ? 2422 ? ? ? ? ? ? ? ? ? ? ? 5.2 1.392 ? ? 0.454 0.196 ? 8  1 0.919 0.979 ? 99.3 ? 0.407 ? ? ? ? ? ? ? ? ? 
2.17 2.23  ? ? ? ? ? ? 2462 ? ? ? ? ? ? ? ? ? ? ? 5.4 1.500 ? ? 0.439 0.186 ? 9  1 0.928 0.981 ? 99.0 ? 0.396 ? ? ? ? ? ? ? ? ? 
2.23 2.31  ? ? ? ? ? ? 2424 ? ? ? ? ? ? ? ? ? ? ? 5.9 1.673 ? ? 0.439 0.177 ? 10 1 0.882 0.968 ? 99.2 ? 0.400 ? ? ? ? ? ? ? ? ? 
2.31 2.39  ? ? ? ? ? ? 2442 ? ? ? ? ? ? ? ? ? ? ? 5.9 1.647 ? ? 0.396 0.158 ? 11 1 0.952 0.988 ? 99.1 ? 0.361 ? ? ? ? ? ? ? ? ? 
2.39 2.48  ? ? ? ? ? ? 2425 ? ? ? ? ? ? ? ? ? ? ? 5.9 1.808 ? ? 0.344 0.139 ? 12 1 0.954 0.988 ? 98.5 ? 0.313 ? ? ? ? ? ? ? ? ? 
2.48 2.60  ? ? ? ? ? ? 2427 ? ? ? ? ? ? ? ? ? ? ? 5.8 1.909 ? ? 0.309 0.127 ? 13 1 0.953 0.988 ? 98.9 ? 0.280 ? ? ? ? ? ? ? ? ? 
2.60 2.73  ? ? ? ? ? ? 2436 ? ? ? ? ? ? ? ? ? ? ? 5.5 2.042 ? ? 0.268 0.112 ? 14 1 0.958 0.989 ? 98.2 ? 0.242 ? ? ? ? ? ? ? ? ? 
2.73 2.90  ? ? ? ? ? ? 2424 ? ? ? ? ? ? ? ? ? ? ? 5.3 2.249 ? ? 0.227 0.097 ? 15 1 0.965 0.991 ? 98.4 ? 0.204 ? ? ? ? ? ? ? ? ? 
2.90 3.13  ? ? ? ? ? ? 2432 ? ? ? ? ? ? ? ? ? ? ? 5.9 2.552 ? ? 0.188 0.077 ? 16 1 0.977 0.994 ? 97.8 ? 0.171 ? ? ? ? ? ? ? ? ? 
3.13 3.44  ? ? ? ? ? ? 2438 ? ? ? ? ? ? ? ? ? ? ? 5.7 2.838 ? ? 0.161 0.068 ? 17 1 0.975 0.994 ? 98.1 ? 0.146 ? ? ? ? ? ? ? ? ? 
3.44 3.94  ? ? ? ? ? ? 2441 ? ? ? ? ? ? ? ? ? ? ? 5.3 3.101 ? ? 0.142 0.062 ? 18 1 0.980 0.995 ? 98.2 ? 0.127 ? ? ? ? ? ? ? ? ? 
3.94 4.97  ? ? ? ? ? ? 2458 ? ? ? ? ? ? ? ? ? ? ? 5.5 3.221 ? ? 0.117 0.050 ? 19 1 0.988 0.997 ? 98.8 ? 0.105 ? ? ? ? ? ? ? ? ? 
4.97 50.00 ? ? ? ? ? ? 2498 ? ? ? ? ? ? ? ? ? ? ? 5.7 3.004 ? ? 0.120 0.050 ? 20 1 0.988 0.997 ? 98.5 ? 0.108 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8ZU5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.83 
_refine.ls_d_res_low                             29.32 
_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                     48578 
_refine.ls_number_reflns_R_free                  2369 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.36 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2096 
_refine.ls_R_factor_R_free                       0.2419 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2079 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.88 
_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                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.83 
_refine_hist.d_res_low                        29.32 
_refine_hist.number_atoms_solvent             362 
_refine_hist.number_atoms_total               4770 
_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        4404 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 6.469 ? 622 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.073 ? 690 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013 ? 804 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.83 1.87  . . 137 2610 96.00 . . . . 0.2901 . . . . . . . . . . . 0.3275 
'X-RAY DIFFRACTION' 1.87 1.91  . . 136 2752 99.00 . . . . 0.2493 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 1.91 1.95  . . 139 2694 98.00 . . . . 0.2266 . . . . . . . . . . . 0.2671 
'X-RAY DIFFRACTION' 1.95 2.00  . . 129 2706 99.00 . . . . 0.2190 . . . . . . . . . . . 0.2567 
'X-RAY DIFFRACTION' 2.00 2.05  . . 149 2696 99.00 . . . . 0.2140 . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 2.05 2.11  . . 148 2718 98.00 . . . . 0.2238 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.11 2.18  . . 139 2714 99.00 . . . . 0.2162 . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 2.18 2.26  . . 145 2726 99.00 . . . . 0.2127 . . . . . . . . . . . 0.2718 
'X-RAY DIFFRACTION' 2.26 2.35  . . 125 2749 99.00 . . . . 0.2153 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 2.35 2.46  . . 154 2706 99.00 . . . . 0.2223 . . . . . . . . . . . 0.2725 
'X-RAY DIFFRACTION' 2.46 2.59  . . 148 2698 99.00 . . . . 0.2104 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 2.59 2.75  . . 128 2717 98.00 . . . . 0.2154 . . . . . . . . . . . 0.2458 
'X-RAY DIFFRACTION' 2.75 2.96  . . 129 2752 98.00 . . . . 0.2184 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 2.96 3.26  . . 134 2704 98.00 . . . . 0.1986 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 3.26 3.73  . . 142 2716 98.00 . . . . 0.1960 . . . . . . . . . . . 0.2195 
'X-RAY DIFFRACTION' 3.73 4.69  . . 126 2766 99.00 . . . . 0.1835 . . . . . . . . . . . 0.1856 
'X-RAY DIFFRACTION' 4.69 29.32 . . 161 2785 99.00 . . . . 0.2011 . . . . . . . . . . . 0.2400 
# 
_struct.entry_id                     8ZU5 
_struct.title                        'Crystal Structure of Methyl parathion hydrolase mutant A66D/I143V/I145L/Q272D/S279A/' 
_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        8ZU5 
_struct_keywords.text            Hydrolase 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q841S6_PSEWB 
_struct_ref.pdbx_db_accession          Q841S6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AAPQVRTSAPGYYRMLLGDFEITALSDGTVALPVDKRLNQPAPKTQSALAKSFQKAPLETSVTGYLVNTGSKLVLVDTGA
AGLFGPTLGRLAANLKAAGYQPEQVDEIYITHMHPDHVGGLMVGEQLAFPNAVVRADQKEADFWLSQTNLDKAPDDESKG
FFKGAMASLNPYVKAGKFKPFSGNTDLVPGIKALASHGHTPGHTTYVVESQGQKLALLGDLILVAAVQFDDPSVTTQLDS
DSKSVAVERKKAFADAAKGGYLIAASHLSFPGIGHIRAEGKGYRFVPVNYSVVN
;
_struct_ref.pdbx_align_begin           36 
# 
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 8ZU5 A 1 ? 294 ? Q841S6 36 ? 329 ? 36 329 
2 1 8ZU5 B 1 ? 294 ? Q841S6 36 ? 329 ? 36 329 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZU5 ASP A 31  ? UNP Q841S6 ALA 66  'engineered mutation' 66  1  
1 8ZU5 VAL A 108 ? UNP Q841S6 ILE 143 'engineered mutation' 143 2  
1 8ZU5 LEU A 110 ? UNP Q841S6 ILE 145 'engineered mutation' 145 3  
1 8ZU5 ASP A 237 ? UNP Q841S6 GLN 272 'engineered mutation' 272 4  
1 8ZU5 ALA A 244 ? UNP Q841S6 SER 279 'engineered mutation' 279 5  
2 8ZU5 ASP B 31  ? UNP Q841S6 ALA 66  'engineered mutation' 66  6  
2 8ZU5 VAL B 108 ? UNP Q841S6 ILE 143 'engineered mutation' 143 7  
2 8ZU5 LEU B 110 ? UNP Q841S6 ILE 145 'engineered mutation' 145 8  
2 8ZU5 ASP B 237 ? UNP Q841S6 GLN 272 'engineered mutation' 272 9  
2 8ZU5 ALA B 244 ? UNP Q841S6 SER 279 'engineered mutation' 279 10 
# 
_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)' 4850  ? 
1 MORE         -165  ? 
1 'SSA (A^2)'  22600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 VAL A 34  ? LEU A 38  ? VAL A 69  LEU A 73  1 ? 5  
HELX_P HELX_P2  AA2 PRO A 41  ? SER A 52  ? PRO A 76  SER A 87  1 ? 12 
HELX_P HELX_P3  AA3 ARG A 90  ? ALA A 98  ? ARG A 125 ALA A 133 1 ? 9  
HELX_P HELX_P4  AA4 GLN A 101 ? VAL A 105 ? GLN A 136 VAL A 140 5 ? 5  
HELX_P HELX_P5  AA5 HIS A 114 ? GLY A 119 ? HIS A 149 GLY A 154 1 ? 6  
HELX_P HELX_P6  AA6 ASP A 137 ? LEU A 145 ? ASP A 172 LEU A 180 1 ? 9  
HELX_P HELX_P7  AA7 SER A 146 ? ALA A 153 ? SER A 181 ALA A 188 1 ? 8  
HELX_P HELX_P8  AA8 ASP A 155 ? ALA A 175 ? ASP A 190 ALA A 210 1 ? 21 
HELX_P HELX_P9  AA9 VAL A 224 ? PHE A 229 ? VAL A 259 PHE A 264 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 241 ? GLY A 260 ? ASP A 276 GLY A 295 1 ? 20 
HELX_P HELX_P11 AB2 PRO B 33  ? LEU B 38  ? PRO B 68  LEU B 73  1 ? 6  
HELX_P HELX_P12 AB3 PRO B 41  ? SER B 52  ? PRO B 76  SER B 87  1 ? 12 
HELX_P HELX_P13 AB4 ARG B 90  ? ALA B 98  ? ARG B 125 ALA B 133 1 ? 9  
HELX_P HELX_P14 AB5 GLN B 101 ? VAL B 105 ? GLN B 136 VAL B 140 5 ? 5  
HELX_P HELX_P15 AB6 HIS B 114 ? GLY B 119 ? HIS B 149 GLY B 154 1 ? 6  
HELX_P HELX_P16 AB7 ASP B 137 ? LEU B 145 ? ASP B 172 LEU B 180 1 ? 9  
HELX_P HELX_P17 AB8 SER B 146 ? ALA B 153 ? SER B 181 ALA B 188 1 ? 8  
HELX_P HELX_P18 AB9 ASP B 155 ? ALA B 175 ? ASP B 190 ALA B 210 1 ? 21 
HELX_P HELX_P19 AC1 VAL B 224 ? PHE B 229 ? VAL B 259 PHE B 264 1 ? 6  
HELX_P HELX_P20 AC2 ASP B 241 ? GLY B 260 ? ASP B 276 GLY B 295 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 112 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 147 A ZN 401 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc2  metalc ? ? A HIS 114 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 149 A ZN 401 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc3  metalc ? ? A ASP 116 OD2 ? ? ? 1_555 D ZN . ZN ? ? A ASP 151 A ZN 402 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc4  metalc ? ? A HIS 117 NE2 ? ? ? 1_555 D ZN . ZN ? ? A HIS 152 A ZN 402 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc5  metalc ? ? A HIS 199 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 234 A ZN 401 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc6  metalc ? ? A ASP 220 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 255 A ZN 401 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc7  metalc ? ? A ASP 220 OD2 ? ? ? 1_555 D ZN . ZN ? ? A ASP 255 A ZN 402 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc8  metalc ? ? A HIS 267 NE2 ? ? ? 1_555 D ZN . ZN ? ? A HIS 302 A ZN 402 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc9  metalc ? ? B HIS 112 NE2 ? ? ? 1_555 E ZN . ZN ? ? B HIS 147 B ZN 401 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc10 metalc ? ? B HIS 114 ND1 ? ? ? 1_555 E ZN . ZN ? ? B HIS 149 B ZN 401 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc11 metalc ? ? B ASP 116 OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 151 B ZN 402 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc12 metalc ? ? B HIS 117 NE2 ? ? ? 1_555 F ZN . ZN ? ? B HIS 152 B ZN 402 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc13 metalc ? ? B HIS 199 NE2 ? ? ? 1_555 E ZN . ZN ? ? B HIS 234 B ZN 401 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc14 metalc ? ? B ASP 220 OD2 ? ? ? 1_555 E ZN . ZN ? ? B ASP 255 B ZN 401 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc15 metalc ? ? B ASP 220 OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 255 B ZN 402 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc16 metalc ? ? B HIS 267 NE2 ? ? ? 1_555 F ZN . ZN ? ? B HIS 302 B ZN 402 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 ND1 ? A HIS 114 ? A HIS 149 ? 1_555 94.2  ? 
2  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS 199 ? A HIS 234 ? 1_555 90.2  ? 
3  ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 NE2 ? A HIS 199 ? A HIS 234 ? 1_555 92.1  ? 
4  NE2 ? A HIS 112 ? A HIS 147 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 82.4  ? 
5  ND1 ? A HIS 114 ? A HIS 149 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 169.4 ? 
6  NE2 ? A HIS 199 ? A HIS 234 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 98.0  ? 
7  OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 91.2  ? 
8  OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 171.3 ? 
9  NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 86.5  ? 
10 OD2 ? A ASP 116 ? A ASP 151 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 88.6  ? 
11 NE2 ? A HIS 117 ? A HIS 152 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 98.3  ? 
12 OD2 ? A ASP 220 ? A ASP 255 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 NE2 ? A HIS 267 ? A HIS 302 ? 1_555 100.0 ? 
13 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 91.6  ? 
14 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 89.7  ? 
15 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 90.1  ? 
16 NE2 ? B HIS 112 ? B HIS 147 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 85.2  ? 
17 ND1 ? B HIS 114 ? B HIS 149 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 172.3 ? 
18 NE2 ? B HIS 199 ? B HIS 234 ? 1_555 ZN ? E ZN . ? B ZN 401 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 96.9  ? 
19 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 89.4  ? 
20 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 169.9 ? 
21 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 88.8  ? 
22 OD2 ? B ASP 116 ? B ASP 151 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 82.9  ? 
23 NE2 ? B HIS 117 ? B HIS 152 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 101.4 ? 
24 OD2 ? B ASP 220 ? B ASP 255 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 NE2 ? B HIS 267 ? B HIS 302 ? 1_555 107.2 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 270 A . ? PHE 305 A PRO 271 A ? PRO 306 A 1 11.31 
2 PHE 270 B . ? PHE 305 B PRO 271 B ? PRO 306 B 1 6.52  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 12  ? LEU A 17  ? TYR A 47  LEU A 52  
AA1 2 PHE A 20  ? PRO A 33  ? PHE A 55  PRO A 68  
AA1 3 PRO A 57  ? ASN A 68  ? PRO A 92  ASN A 103 
AA1 4 LEU A 73  ? VAL A 76  ? LEU A 108 VAL A 111 
AA1 5 GLU A 107 ? TYR A 109 ? GLU A 142 TYR A 144 
AA1 6 VAL A 133 ? ARG A 135 ? VAL A 168 ARG A 170 
AA2 1 MET A 122 ? VAL A 123 ? MET A 157 VAL A 158 
AA2 2 GLN A 126 ? LEU A 127 ? GLN A 161 LEU A 162 
AA3 1 THR A 185 ? ASP A 186 ? THR A 220 ASP A 221 
AA3 2 ILE A 191 ? ALA A 195 ? ILE A 226 ALA A 230 
AA3 3 THR A 204 ? SER A 210 ? THR A 239 SER A 245 
AA3 4 GLN A 213 ? LEU A 217 ? GLN A 248 LEU A 252 
AA3 5 LEU A 262 ? ALA A 264 ? LEU A 297 ALA A 299 
AA3 6 ILE A 273 ? GLU A 279 ? ILE A 308 GLU A 314 
AA3 7 GLY A 282 ? PRO A 287 ? GLY A 317 PRO A 322 
AA4 1 TYR B 12  ? LEU B 17  ? TYR B 47  LEU B 52  
AA4 2 PHE B 20  ? LEU B 32  ? PHE B 55  LEU B 67  
AA4 3 LEU B 58  ? ASN B 68  ? LEU B 93  ASN B 103 
AA4 4 LEU B 73  ? VAL B 76  ? LEU B 108 VAL B 111 
AA4 5 GLU B 107 ? TYR B 109 ? GLU B 142 TYR B 144 
AA4 6 VAL B 133 ? ARG B 135 ? VAL B 168 ARG B 170 
AA5 1 MET B 122 ? VAL B 123 ? MET B 157 VAL B 158 
AA5 2 GLN B 126 ? LEU B 127 ? GLN B 161 LEU B 162 
AA6 1 THR B 185 ? ASP B 186 ? THR B 220 ASP B 221 
AA6 2 ILE B 191 ? ALA B 195 ? ILE B 226 ALA B 230 
AA6 3 THR B 204 ? SER B 210 ? THR B 239 SER B 245 
AA6 4 GLN B 213 ? LEU B 217 ? GLN B 248 LEU B 252 
AA6 5 LEU B 262 ? ALA B 264 ? LEU B 297 ALA B 299 
AA6 6 ILE B 273 ? GLU B 279 ? ILE B 308 GLU B 314 
AA6 7 GLY B 282 ? PRO B 287 ? GLY B 317 PRO B 322 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N MET A 15  ? N MET A 50  O ILE A 22  ? O ILE A 57  
AA1 2 3 N ASP A 27  ? N ASP A 62  O VAL A 62  ? O VAL A 97  
AA1 3 4 N VAL A 67  ? N VAL A 102 O VAL A 74  ? O VAL A 109 
AA1 4 5 N LEU A 75  ? N LEU A 110 O TYR A 109 ? O TYR A 144 
AA1 5 6 N VAL A 108 ? N VAL A 143 O ARG A 135 ? O ARG A 170 
AA2 1 2 N VAL A 123 ? N VAL A 158 O GLN A 126 ? O GLN A 161 
AA3 1 2 N THR A 185 ? N THR A 220 O ALA A 193 ? O ALA A 228 
AA3 2 3 N LEU A 194 ? N LEU A 229 O THR A 205 ? O THR A 240 
AA3 3 4 N TYR A 206 ? N TYR A 241 O LEU A 217 ? O LEU A 252 
AA3 4 5 N ALA A 216 ? N ALA A 251 O LEU A 262 ? O LEU A 297 
AA3 5 6 N ILE A 263 ? N ILE A 298 O GLY A 274 ? O GLY A 309 
AA3 6 7 N HIS A 275 ? N HIS A 310 O VAL A 286 ? O VAL A 321 
AA4 1 2 N MET B 15  ? N MET B 50  O ILE B 22  ? O ILE B 57  
AA4 2 3 N LEU B 25  ? N LEU B 60  O GLY B 64  ? O GLY B 99  
AA4 3 4 N VAL B 67  ? N VAL B 102 O VAL B 74  ? O VAL B 109 
AA4 4 5 N LEU B 75  ? N LEU B 110 O TYR B 109 ? O TYR B 144 
AA4 5 6 N VAL B 108 ? N VAL B 143 O ARG B 135 ? O ARG B 170 
AA5 1 2 N VAL B 123 ? N VAL B 158 O GLN B 126 ? O GLN B 161 
AA6 1 2 N THR B 185 ? N THR B 220 O ALA B 193 ? O ALA B 228 
AA6 2 3 N LEU B 194 ? N LEU B 229 O THR B 205 ? O THR B 240 
AA6 3 4 N TYR B 206 ? N TYR B 241 O LEU B 217 ? O LEU B 252 
AA6 4 5 N ALA B 216 ? N ALA B 251 O LEU B 262 ? O LEU B 297 
AA6 5 6 N ILE B 263 ? N ILE B 298 O GLY B 274 ? O GLY B 309 
AA6 6 7 N HIS B 275 ? N HIS B 310 O VAL B 286 ? O VAL B 321 
# 
_pdbx_entry_details.entry_id                   8ZU5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     82 
_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    OD1 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ASN 
_pdbx_validate_symm_contact.auth_seq_id_2     166 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_455 
_pdbx_validate_symm_contact.dist              1.92 
# 
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 ALA A 44  ? ? -49.43  156.63  
2  1 LYS A 90  ? ? -94.39  -98.21  
3  1 ALA A 91  ? ? -149.55 -57.17  
4  1 PRO A 92  ? ? -69.21  82.16   
5  1 ASP A 112 ? ? 65.64   153.65  
6  1 ALA A 116 ? ? 38.36   -121.62 
7  1 LEU A 222 ? ? -93.59  -151.18 
8  1 VAL A 223 ? ? -35.46  134.60  
9  1 ALA B 91  ? ? 58.79   -159.48 
10 1 ASP B 112 ? ? 64.29   155.76  
11 1 ALA B 116 ? ? 49.06   -125.36 
12 1 PRO B 189 ? ? -91.24  42.52   
13 1 ASP B 190 ? ? 175.67  159.98  
14 1 LEU B 222 ? ? -96.35  -152.57 
15 1 VAL B 223 ? ? -33.93  133.53  
# 
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 72  ? ? 0.229 'SIDE CHAIN' 
2 1 ARG A 319 ? ? 0.079 'SIDE CHAIN' 
3 1 ARG B 72  ? ? 0.294 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 1.8552   -8.7380  30.2564 0.2641 ? -0.0484 ? -0.0046 ? 0.2175 ? 0.0282  ? 0.2786 ? 0.9546 ? 
-0.3291 ? 1.5238  ? 2.0599 ? 0.3384  ? 2.7007 ? 0.0141  ? 0.1644  ? 0.0631  ? -0.0638 ? 0.0685  ? 0.4933  ? 0.7255  ? -0.5695 ? 
0.0048  ? 
2  'X-RAY DIFFRACTION' ? refined -5.8359  9.9879   44.5740 0.3272 ? 0.0947  ? 0.0069  ? 0.5324 ? -0.1175 ? 0.4079 ? 0.5058 ? 
-0.7437 ? 0.2845  ? 2.1456 ? -0.0220 ? 1.3275 ? -0.3039 ? -0.5204 ? 0.3614  ? 0.4349  ? 0.2684  ? 0.3611  ? -0.3840 ? -0.5573 ? 
0.1462  ? 
3  'X-RAY DIFFRACTION' ? refined 9.8160   -7.5845  39.9483 0.1795 ? -0.0060 ? -0.0154 ? 0.1286 ? 0.0069  ? 0.1374 ? 2.0673 ? 
0.0274  ? 0.7984  ? 2.7775 ? -0.3170 ? 3.8282 ? 0.1519  ? -0.1908 ? -0.2516 ? 0.1683  ? -0.1990 ? -0.0474 ? 0.1656  ? -0.1574 ? 
0.0195  ? 
4  'X-RAY DIFFRACTION' ? refined 15.0365  -8.5499  44.5669 0.1962 ? 0.0243  ? -0.0018 ? 0.2102 ? 0.0435  ? 0.1595 ? 2.8987 ? 
-0.3154 ? 1.0752  ? 1.8093 ? 0.4529  ? 3.6015 ? 0.1337  ? -0.2647 ? -0.2139 ? 0.0978  ? -0.0542 ? -0.0739 ? 0.4260  ? 0.1752  ? 
-0.0349 ? 
5  'X-RAY DIFFRACTION' ? refined 17.9841  -0.5961  51.4455 0.1630 ? 0.0055  ? -0.0270 ? 0.2923 ? -0.0281 ? 0.1667 ? 2.9454 ? 
-0.1724 ? 0.9515  ? 2.7842 ? -0.2673 ? 3.4656 ? -0.0462 ? -0.4834 ? 0.1596  ? 0.3742  ? -0.0015 ? -0.0211 ? 0.0923  ? -0.0277 ? 
0.0506  ? 
6  'X-RAY DIFFRACTION' ? refined 10.2222  9.7193   37.3671 0.1789 ? -0.0010 ? -0.0334 ? 0.1657 ? 0.0144  ? 0.2259 ? 2.3475 ? 
-0.8224 ? 0.6373  ? 2.0344 ? 0.6550  ? 2.8716 ? -0.1587 ? -0.1274 ? 0.4295  ? 0.0314  ? -0.0034 ? -0.1260 ? -0.4053 ? 0.1927  ? 
0.1905  ? 
7  'X-RAY DIFFRACTION' ? refined 4.2509   8.6986   26.3481 0.2480 ? 0.0118  ? -0.0575 ? 0.1803 ? 0.0182  ? 0.3694 ? 1.8185 ? 
1.3053  ? 0.7470  ? 6.8678 ? 2.5926  ? 4.2454 ? -0.1540 ? 0.2093  ? 0.6085  ? 0.0400  ? -0.2958 ? 0.8865  ? -0.5709 ? 0.0182  ? 
0.2732  ? 
8  'X-RAY DIFFRACTION' ? refined -4.1442  -8.2653  24.9773 0.2237 ? -0.0359 ? -0.0222 ? 0.1689 ? 0.0199  ? 0.1877 ? 1.9294 ? 
-0.7908 ? 0.8763  ? 1.0044 ? 0.2264  ? 1.2732 ? 0.0122  ? -0.3519 ? 0.0654  ? 0.1105  ? 0.1265  ? -0.0512 ? 0.4888  ? 0.0375  ? 
-0.0534 ? 
9  'X-RAY DIFFRACTION' ? refined 0.6587   13.3456  9.0877  0.2580 ? -0.0612 ? -0.0476 ? 0.2329 ? 0.0914  ? 0.4443 ? 1.8679 ? 
-0.5641 ? 0.4567  ? 2.2196 ? -0.7104 ? 1.7034 ? -0.1240 ? 0.3312  ? 0.5750  ? 0.1946  ? -0.3768 ? -0.5680 ? -0.0322 ? 0.4221  ? 
0.1984  ? 
10 'X-RAY DIFFRACTION' ? refined -3.8449  0.0431   17.8063 0.1571 ? -0.0135 ? -0.0076 ? 0.1261 ? 0.0171  ? 0.2480 ? 1.2790 ? 
-0.5552 ? 0.8258  ? 1.1178 ? 0.5358  ? 2.4368 ? -0.1331 ? 0.3526  ? 0.1041  ? 0.0282  ? 0.1377  ? -0.3151 ? 0.1026  ? -0.0003 ? 
0.0520  ? 
11 'X-RAY DIFFRACTION' ? refined -11.9297 -10.1225 15.4499 0.1800 ? -0.0712 ? -0.0451 ? 0.1331 ? 0.0003  ? 0.2252 ? 2.9276 ? 
-0.4510 ? -0.1986 ? 1.4433 ? 0.4474  ? 1.9178 ? 0.4441  ? -0.0854 ? -0.1763 ? -0.0837 ? -0.2911 ? -0.0035 ? 0.0825  ? -0.0902 ? 
-0.0469 ? 
12 'X-RAY DIFFRACTION' ? refined -17.7381 -11.3597 12.7556 0.1955 ? -0.0719 ? -0.0275 ? 0.1486 ? 0.0066  ? 0.2886 ? 1.7592 ? 
0.7694  ? 0.7025  ? 1.2393 ? -0.0173 ? 2.3278 ? 0.2555  ? -0.0521 ? -0.3036 ? 0.0865  ? -0.1568 ? 0.0709  ? 0.3791  ? -0.2044 ? 
-0.0144 ? 
13 'X-RAY DIFFRACTION' ? refined -17.0742 -6.7429  -2.7027 0.1353 ? -0.0374 ? -0.0201 ? 0.2408 ? 0.0040  ? 0.2352 ? 3.5297 ? 
-0.6008 ? 0.4901  ? 3.5859 ? -0.4019 ? 5.6280 ? -0.1842 ? 0.5647  ? 0.1934  ? -0.5144 ? 0.0935  ? -0.1433 ? 0.2471  ? 0.1200  ? 
0.0492  ? 
14 'X-RAY DIFFRACTION' ? refined -24.8568 -0.8368  17.9640 0.1198 ? -0.0574 ? 0.0274  ? 0.2357 ? -0.0303 ? 0.2728 ? 1.8161 ? 
0.3598  ? 0.5784  ? 1.6306 ? 0.2844  ? 1.7970 ? 0.0711  ? -0.2455 ? 0.1277  ? 0.1932  ? -0.1120 ? 0.2483  ? 0.1161  ? -0.4586 ? 
-0.0002 ? 
15 'X-RAY DIFFRACTION' ? refined -10.1765 10.6749  11.8338 0.1858 ? -0.0342 ? 0.0168  ? 0.1539 ? -0.0171 ? 0.3140 ? 2.3795 ? 
0.4836  ? 0.8037  ? 1.1153 ? -0.5593 ? 1.7581 ? -0.1264 ? 0.0130  ? 0.3730  ? -0.0605 ? 0.1580  ? -0.1113 ? -0.1927 ? -0.1406 ? 
0.1217  ? 
16 'X-RAY DIFFRACTION' ? refined -15.0149 8.9390   19.7688 0.1659 ? -0.0190 ? 0.0057  ? 0.1828 ? -0.0440 ? 0.3081 ? 2.1750 ? 
0.2072  ? 1.0393  ? 1.2754 ? -0.3489 ? 1.9633 ? -0.0087 ? -0.1630 ? 0.4098  ? 0.0770  ? -0.1047 ? 0.2351  ? -0.2300 ? -0.1790 ? 
0.1031  ? 
17 'X-RAY DIFFRACTION' ? refined -8.6821  8.2457   29.3950 0.1954 ? -0.0288 ? 0.0263  ? 0.2396 ? -0.0409 ? 0.2943 ? 2.6835 ? 
-0.9948 ? 1.4117  ? 4.1243 ? -1.8606 ? 3.7252 ? -0.1526 ? -0.4369 ? 0.5248  ? 0.1899  ? -0.0158 ? -0.2661 ? -0.3841 ? -0.3328 ? 
0.1020  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 36 through 63 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 64 through 97 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 98 through 125 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 126 through 179 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 180 through 238 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 239 through 308 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 309 through 329 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 36 through 67 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 68 through 87 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 88 through 103 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 104 through 125 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 126 through 179 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 180 through 209 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 210 through 252 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 253 through 276 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 277 through 308 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 309 through 329 )
;
# 
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  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
HIS N    N  N N 123 
HIS CA   C  N S 124 
HIS C    C  N N 125 
HIS O    O  N N 126 
HIS CB   C  N N 127 
HIS CG   C  Y N 128 
HIS ND1  N  Y N 129 
HIS CD2  C  Y N 130 
HIS CE1  C  Y N 131 
HIS NE2  N  Y N 132 
HIS OXT  O  N N 133 
HIS H    H  N N 134 
HIS H2   H  N N 135 
HIS HA   H  N N 136 
HIS HB2  H  N N 137 
HIS HB3  H  N N 138 
HIS HD1  H  N N 139 
HIS HD2  H  N N 140 
HIS HE1  H  N N 141 
HIS HE2  H  N N 142 
HIS HXT  H  N N 143 
HOH O    O  N N 144 
HOH H1   H  N N 145 
HOH H2   H  N N 146 
ILE N    N  N N 147 
ILE CA   C  N S 148 
ILE C    C  N N 149 
ILE O    O  N N 150 
ILE CB   C  N S 151 
ILE CG1  C  N N 152 
ILE CG2  C  N N 153 
ILE CD1  C  N N 154 
ILE OXT  O  N N 155 
ILE H    H  N N 156 
ILE H2   H  N N 157 
ILE HA   H  N N 158 
ILE HB   H  N N 159 
ILE HG12 H  N N 160 
ILE HG13 H  N N 161 
ILE HG21 H  N N 162 
ILE HG22 H  N N 163 
ILE HG23 H  N N 164 
ILE HD11 H  N N 165 
ILE HD12 H  N N 166 
ILE HD13 H  N N 167 
ILE HXT  H  N N 168 
LEU N    N  N N 169 
LEU CA   C  N S 170 
LEU C    C  N N 171 
LEU O    O  N N 172 
LEU CB   C  N N 173 
LEU CG   C  N N 174 
LEU CD1  C  N N 175 
LEU CD2  C  N N 176 
LEU OXT  O  N N 177 
LEU H    H  N N 178 
LEU H2   H  N N 179 
LEU HA   H  N N 180 
LEU HB2  H  N N 181 
LEU HB3  H  N N 182 
LEU HG   H  N N 183 
LEU HD11 H  N N 184 
LEU HD12 H  N N 185 
LEU HD13 H  N N 186 
LEU HD21 H  N N 187 
LEU HD22 H  N N 188 
LEU HD23 H  N N 189 
LEU HXT  H  N N 190 
LYS N    N  N N 191 
LYS CA   C  N S 192 
LYS C    C  N N 193 
LYS O    O  N N 194 
LYS CB   C  N N 195 
LYS CG   C  N N 196 
LYS CD   C  N N 197 
LYS CE   C  N N 198 
LYS NZ   N  N N 199 
LYS OXT  O  N N 200 
LYS H    H  N N 201 
LYS H2   H  N N 202 
LYS HA   H  N N 203 
LYS HB2  H  N N 204 
LYS HB3  H  N N 205 
LYS HG2  H  N N 206 
LYS HG3  H  N N 207 
LYS HD2  H  N N 208 
LYS HD3  H  N N 209 
LYS HE2  H  N N 210 
LYS HE3  H  N N 211 
LYS HZ1  H  N N 212 
LYS HZ2  H  N N 213 
LYS HZ3  H  N N 214 
LYS HXT  H  N N 215 
MET N    N  N N 216 
MET CA   C  N S 217 
MET C    C  N N 218 
MET O    O  N N 219 
MET CB   C  N N 220 
MET CG   C  N N 221 
MET SD   S  N N 222 
MET CE   C  N N 223 
MET OXT  O  N N 224 
MET H    H  N N 225 
MET H2   H  N N 226 
MET HA   H  N N 227 
MET HB2  H  N N 228 
MET HB3  H  N N 229 
MET HG2  H  N N 230 
MET HG3  H  N N 231 
MET HE1  H  N N 232 
MET HE2  H  N N 233 
MET HE3  H  N N 234 
MET HXT  H  N N 235 
PHE N    N  N N 236 
PHE CA   C  N S 237 
PHE C    C  N N 238 
PHE O    O  N N 239 
PHE CB   C  N N 240 
PHE CG   C  Y N 241 
PHE CD1  C  Y N 242 
PHE CD2  C  Y N 243 
PHE CE1  C  Y N 244 
PHE CE2  C  Y N 245 
PHE CZ   C  Y N 246 
PHE OXT  O  N N 247 
PHE H    H  N N 248 
PHE H2   H  N N 249 
PHE HA   H  N N 250 
PHE HB2  H  N N 251 
PHE HB3  H  N N 252 
PHE HD1  H  N N 253 
PHE HD2  H  N N 254 
PHE HE1  H  N N 255 
PHE HE2  H  N N 256 
PHE HZ   H  N N 257 
PHE HXT  H  N N 258 
PRO N    N  N N 259 
PRO CA   C  N S 260 
PRO C    C  N N 261 
PRO O    O  N N 262 
PRO CB   C  N N 263 
PRO CG   C  N N 264 
PRO CD   C  N N 265 
PRO OXT  O  N N 266 
PRO H    H  N N 267 
PRO HA   H  N N 268 
PRO HB2  H  N N 269 
PRO HB3  H  N N 270 
PRO HG2  H  N N 271 
PRO HG3  H  N N 272 
PRO HD2  H  N N 273 
PRO HD3  H  N N 274 
PRO HXT  H  N N 275 
SER N    N  N N 276 
SER CA   C  N S 277 
SER C    C  N N 278 
SER O    O  N N 279 
SER CB   C  N N 280 
SER OG   O  N N 281 
SER OXT  O  N N 282 
SER H    H  N N 283 
SER H2   H  N N 284 
SER HA   H  N N 285 
SER HB2  H  N N 286 
SER HB3  H  N N 287 
SER HG   H  N N 288 
SER HXT  H  N N 289 
THR N    N  N N 290 
THR CA   C  N S 291 
THR C    C  N N 292 
THR O    O  N N 293 
THR CB   C  N R 294 
THR OG1  O  N N 295 
THR CG2  C  N N 296 
THR OXT  O  N N 297 
THR H    H  N N 298 
THR H2   H  N N 299 
THR HA   H  N N 300 
THR HB   H  N N 301 
THR HG1  H  N N 302 
THR HG21 H  N N 303 
THR HG22 H  N N 304 
THR HG23 H  N N 305 
THR HXT  H  N N 306 
TRP N    N  N N 307 
TRP CA   C  N S 308 
TRP C    C  N N 309 
TRP O    O  N N 310 
TRP CB   C  N N 311 
TRP CG   C  Y N 312 
TRP CD1  C  Y N 313 
TRP CD2  C  Y N 314 
TRP NE1  N  Y N 315 
TRP CE2  C  Y N 316 
TRP CE3  C  Y N 317 
TRP CZ2  C  Y N 318 
TRP CZ3  C  Y N 319 
TRP CH2  C  Y N 320 
TRP OXT  O  N N 321 
TRP H    H  N N 322 
TRP H2   H  N N 323 
TRP HA   H  N N 324 
TRP HB2  H  N N 325 
TRP HB3  H  N N 326 
TRP HD1  H  N N 327 
TRP HE1  H  N N 328 
TRP HE3  H  N N 329 
TRP HZ2  H  N N 330 
TRP HZ3  H  N N 331 
TRP HH2  H  N N 332 
TRP HXT  H  N N 333 
TYR N    N  N N 334 
TYR CA   C  N S 335 
TYR C    C  N N 336 
TYR O    O  N N 337 
TYR CB   C  N N 338 
TYR CG   C  Y N 339 
TYR CD1  C  Y N 340 
TYR CD2  C  Y N 341 
TYR CE1  C  Y N 342 
TYR CE2  C  Y N 343 
TYR CZ   C  Y N 344 
TYR OH   O  N N 345 
TYR OXT  O  N N 346 
TYR H    H  N N 347 
TYR H2   H  N N 348 
TYR HA   H  N N 349 
TYR HB2  H  N N 350 
TYR HB3  H  N N 351 
TYR HD1  H  N N 352 
TYR HD2  H  N N 353 
TYR HE1  H  N N 354 
TYR HE2  H  N N 355 
TYR HH   H  N N 356 
TYR HXT  H  N N 357 
VAL N    N  N N 358 
VAL CA   C  N S 359 
VAL C    C  N N 360 
VAL O    O  N N 361 
VAL CB   C  N N 362 
VAL CG1  C  N N 363 
VAL CG2  C  N N 364 
VAL OXT  O  N N 365 
VAL H    H  N N 366 
VAL H2   H  N N 367 
VAL HA   H  N N 368 
VAL HB   H  N N 369 
VAL HG11 H  N N 370 
VAL HG12 H  N N 371 
VAL HG13 H  N N 372 
VAL HG21 H  N N 373 
VAL HG22 H  N N 374 
VAL HG23 H  N N 375 
VAL HXT  H  N N 376 
ZN  ZN   ZN N N 377 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22078129 
_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   1P9E 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZU5 
_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]   0.017007 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001288 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011945 
_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]   0.008683 
_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  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -24.244 -18.055 25.183  1.00 79.18 ? 36  ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -23.769 -17.309 26.344  1.00 77.17 ? 36  ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -22.451 -17.866 26.825  1.00 74.25 ? 36  ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -21.853 -18.722 26.169  1.00 73.53 ? 36  ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -24.780 -17.357 27.456  1.00 80.55 ? 36  ALA A CB  1 
ATOM   6    N  N   . ALA A 1 2   ? -21.994 -17.350 27.968  1.00 72.67 ? 37  ALA A N   1 
ATOM   7    C  CA  . ALA A 1 2   ? -20.875 -17.904 28.719  1.00 70.51 ? 37  ALA A CA  1 
ATOM   8    C  C   . ALA A 1 2   ? -20.862 -17.287 30.112  1.00 70.20 ? 37  ALA A C   1 
ATOM   9    O  O   . ALA A 1 2   ? -21.182 -16.100 30.263  1.00 71.76 ? 37  ALA A O   1 
ATOM   10   C  CB  . ALA A 1 2   ? -19.535 -17.652 28.017  1.00 66.43 ? 37  ALA A CB  1 
ATOM   11   N  N   . PRO A 1 3   ? -20.551 -18.060 31.155  1.00 71.51 ? 38  PRO A N   1 
ATOM   12   C  CA  . PRO A 1 3   ? -20.211 -17.442 32.442  1.00 69.61 ? 38  PRO A CA  1 
ATOM   13   C  C   . PRO A 1 3   ? -18.987 -16.552 32.316  1.00 65.15 ? 38  PRO A C   1 
ATOM   14   O  O   . PRO A 1 3   ? -18.026 -16.864 31.607  1.00 62.72 ? 38  PRO A O   1 
ATOM   15   C  CB  . PRO A 1 3   ? -19.960 -18.641 33.362  1.00 70.92 ? 38  PRO A CB  1 
ATOM   16   C  CG  . PRO A 1 3   ? -20.800 -19.747 32.746  1.00 74.44 ? 38  PRO A CG  1 
ATOM   17   C  CD  . PRO A 1 3   ? -20.688 -19.522 31.266  1.00 73.10 ? 38  PRO A CD  1 
ATOM   18   N  N   . GLN A 1 4   ? -19.035 -15.426 33.015  1.00 64.29 ? 39  GLN A N   1 
ATOM   19   C  CA  . GLN A 1 4   ? -18.005 -14.420 32.848  1.00 60.41 ? 39  GLN A CA  1 
ATOM   20   C  C   . GLN A 1 4   ? -16.711 -14.941 33.444  1.00 57.93 ? 39  GLN A C   1 
ATOM   21   O  O   . GLN A 1 4   ? -16.703 -15.474 34.559  1.00 61.66 ? 39  GLN A O   1 
ATOM   22   C  CB  . GLN A 1 4   ? -18.433 -13.127 33.526  1.00 60.50 ? 39  GLN A CB  1 
ATOM   23   C  CG  . GLN A 1 4   ? -19.790 -12.660 33.037  1.00 63.44 ? 39  GLN A CG  1 
ATOM   24   C  CD  . GLN A 1 4   ? -20.165 -11.332 33.615  1.00 63.51 ? 39  GLN A CD  1 
ATOM   25   O  OE1 . GLN A 1 4   ? -19.524 -10.860 34.550  1.00 61.83 ? 39  GLN A OE1 1 
ATOM   26   N  NE2 . GLN A 1 4   ? -21.234 -10.736 33.103  1.00 65.71 ? 39  GLN A NE2 1 
ATOM   27   N  N   . VAL A 1 5   ? -15.624 -14.836 32.680  1.00 54.85 ? 40  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? -14.342 -15.311 33.176  1.00 52.52 ? 40  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? -13.846 -14.409 34.300  1.00 56.81 ? 40  VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? -13.397 -14.887 35.353  1.00 50.75 ? 40  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? -13.335 -15.394 32.014  1.00 49.95 ? 40  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? -12.015 -15.990 32.484  1.00 47.87 ? 40  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? -13.923 -16.207 30.885  1.00 51.86 ? 40  VAL A CG2 1 
ATOM   34   N  N   . ARG A 1 6   ? -13.960 -13.094 34.102  1.00 52.01 ? 41  ARG A N   1 
ATOM   35   C  CA  . ARG A 1 6   ? -13.483 -12.078 35.036  1.00 49.55 ? 41  ARG A CA  1 
ATOM   36   C  C   . ARG A 1 6   ? -12.115 -12.440 35.613  1.00 47.96 ? 41  ARG A C   1 
ATOM   37   O  O   . ARG A 1 6   ? -11.900 -12.454 36.829  1.00 49.39 ? 41  ARG A O   1 
ATOM   38   C  CB  . ARG A 1 6   ? -14.511 -11.799 36.146  1.00 53.24 ? 41  ARG A CB  1 
ATOM   39   C  CG  . ARG A 1 6   ? -15.725 -11.003 35.659  1.00 54.93 ? 41  ARG A CG  1 
ATOM   40   C  CD  . ARG A 1 6   ? -16.700 -10.629 36.771  1.00 58.62 ? 41  ARG A CD  1 
ATOM   41   N  NE  . ARG A 1 6   ? -17.806 -9.832  36.242  1.00 68.61 ? 41  ARG A NE  1 
ATOM   42   C  CZ  . ARG A 1 6   ? -18.832 -9.378  36.954  1.00 64.29 ? 41  ARG A CZ  1 
ATOM   43   N  NH1 . ARG A 1 6   ? -18.962 -9.660  38.239  1.00 74.56 ? 41  ARG A NH1 1 
ATOM   44   N  NH2 . ARG A 1 6   ? -19.755 -8.628  36.357  1.00 61.69 ? 41  ARG A NH2 1 
ATOM   45   N  N   . THR A 1 7   ? -11.176 -12.730 34.711  1.00 43.44 ? 42  THR A N   1 
ATOM   46   C  CA  . THR A 1 7   ? -9.768  -12.913 35.059  1.00 45.84 ? 42  THR A CA  1 
ATOM   47   C  C   . THR A 1 7   ? -8.928  -12.083 34.103  1.00 43.28 ? 42  THR A C   1 
ATOM   48   O  O   . THR A 1 7   ? -9.050  -12.230 32.882  1.00 45.56 ? 42  THR A O   1 
ATOM   49   C  CB  . THR A 1 7   ? -9.342  -14.396 35.000  1.00 56.16 ? 42  THR A CB  1 
ATOM   50   O  OG1 . THR A 1 7   ? -9.311  -14.846 33.638  1.00 55.43 ? 42  THR A OG1 1 
ATOM   51   C  CG2 . THR A 1 7   ? -10.288 -15.278 35.798  1.00 46.58 ? 42  THR A CG2 1 
ATOM   52   N  N   . SER A 1 8   ? -8.093  -11.207 34.660  1.00 37.92 ? 43  SER A N   1 
ATOM   53   C  CA  . SER A 1 8   ? -7.219  -10.374 33.851  1.00 41.86 ? 43  SER A CA  1 
ATOM   54   C  C   . SER A 1 8   ? -6.147  -11.211 33.158  1.00 41.26 ? 43  SER A C   1 
ATOM   55   O  O   . SER A 1 8   ? -5.715  -12.255 33.654  1.00 32.70 ? 43  SER A O   1 
ATOM   56   C  CB  . SER A 1 8   ? -6.541  -9.306  34.719  1.00 39.04 ? 43  SER A CB  1 
ATOM   57   O  OG  . SER A 1 8   ? -7.460  -8.312  35.124  1.00 39.07 ? 43  SER A OG  1 
ATOM   58   N  N   . ALA A 1 9   ? -5.705  -10.723 32.006  1.00 36.55 ? 44  ALA A N   1 
ATOM   59   C  CA  . ALA A 1 9   ? -4.559  -11.237 31.270  1.00 43.51 ? 44  ALA A CA  1 
ATOM   60   C  C   . ALA A 1 9   ? -3.363  -11.384 32.207  1.00 38.86 ? 44  ALA A C   1 
ATOM   61   O  O   . ALA A 1 9   ? -3.302  -10.681 33.226  1.00 32.47 ? 44  ALA A O   1 
ATOM   62   C  CB  . ALA A 1 9   ? -4.225  -10.277 30.123  1.00 34.98 ? 44  ALA A CB  1 
ATOM   63   N  N   . PRO A 1 10  ? -2.386  -12.241 31.901  1.00 38.10 ? 45  PRO A N   1 
ATOM   64   C  CA  . PRO A 1 10  ? -1.186  -12.272 32.746  1.00 36.65 ? 45  PRO A CA  1 
ATOM   65   C  C   . PRO A 1 10  ? -0.539  -10.902 32.776  1.00 29.65 ? 45  PRO A C   1 
ATOM   66   O  O   . PRO A 1 10  ? -0.464  -10.208 31.766  1.00 33.53 ? 45  PRO A O   1 
ATOM   67   C  CB  . PRO A 1 10  ? -0.279  -13.312 32.075  1.00 40.74 ? 45  PRO A CB  1 
ATOM   68   C  CG  . PRO A 1 10  ? -0.862  -13.577 30.718  1.00 46.76 ? 45  PRO A CG  1 
ATOM   69   C  CD  . PRO A 1 10  ? -2.143  -12.818 30.565  1.00 44.52 ? 45  PRO A CD  1 
ATOM   70   N  N   . GLY A 1 11  ? -0.090  -10.514 33.957  1.00 30.95 ? 46  GLY A N   1 
ATOM   71   C  CA  . GLY A 1 11  ? 0.579   -9.253  34.102  1.00 27.24 ? 46  GLY A CA  1 
ATOM   72   C  C   . GLY A 1 11  ? 2.022   -9.295  33.654  1.00 28.12 ? 46  GLY A C   1 
ATOM   73   O  O   . GLY A 1 11  ? 2.930   -9.219  34.486  1.00 22.47 ? 46  GLY A O   1 
ATOM   74   N  N   . TYR A 1 12  ? 2.259   -9.413  32.348  1.00 20.03 ? 47  TYR A N   1 
ATOM   75   C  CA  . TYR A 1 12  ? 3.572   -9.076  31.822  1.00 18.69 ? 47  TYR A CA  1 
ATOM   76   C  C   . TYR A 1 12  ? 3.368   -8.360  30.496  1.00 28.84 ? 47  TYR A C   1 
ATOM   77   O  O   . TYR A 1 12  ? 2.326   -8.505  29.845  1.00 22.24 ? 47  TYR A O   1 
ATOM   78   C  CB  . TYR A 1 12  ? 4.509   -10.311 31.724  1.00 22.31 ? 47  TYR A CB  1 
ATOM   79   C  CG  . TYR A 1 12  ? 4.146   -11.367 30.695  1.00 19.64 ? 47  TYR A CG  1 
ATOM   80   C  CD1 . TYR A 1 12  ? 3.230   -12.366 30.996  1.00 21.15 ? 47  TYR A CD1 1 
ATOM   81   C  CD2 . TYR A 1 12  ? 4.714   -11.346 29.424  1.00 20.64 ? 47  TYR A CD2 1 
ATOM   82   C  CE1 . TYR A 1 12  ? 2.911   -13.341 30.066  1.00 27.47 ? 47  TYR A CE1 1 
ATOM   83   C  CE2 . TYR A 1 12  ? 4.409   -12.315 28.485  1.00 22.32 ? 47  TYR A CE2 1 
ATOM   84   C  CZ  . TYR A 1 12  ? 3.503   -13.307 28.811  1.00 23.06 ? 47  TYR A CZ  1 
ATOM   85   O  OH  . TYR A 1 12  ? 3.169   -14.242 27.864  1.00 23.64 ? 47  TYR A OH  1 
ATOM   86   N  N   . TYR A 1 13  ? 4.331   -7.500  30.169  1.00 22.26 ? 48  TYR A N   1 
ATOM   87   C  CA  . TYR A 1 13  ? 4.275   -6.649  28.981  1.00 23.49 ? 48  TYR A CA  1 
ATOM   88   C  C   . TYR A 1 13  ? 5.661   -6.603  28.358  1.00 16.41 ? 48  TYR A C   1 
ATOM   89   O  O   . TYR A 1 13  ? 6.624   -6.210  29.021  1.00 17.64 ? 48  TYR A O   1 
ATOM   90   C  CB  . TYR A 1 13  ? 3.815   -5.232  29.321  1.00 19.82 ? 48  TYR A CB  1 
ATOM   91   C  CG  . TYR A 1 13  ? 3.586   -4.357  28.125  1.00 17.71 ? 48  TYR A CG  1 
ATOM   92   C  CD1 . TYR A 1 13  ? 4.621   -3.602  27.592  1.00 16.31 ? 48  TYR A CD1 1 
ATOM   93   C  CD2 . TYR A 1 13  ? 2.316   -4.275  27.522  1.00 20.80 ? 48  TYR A CD2 1 
ATOM   94   C  CE1 . TYR A 1 13  ? 4.411   -2.779  26.487  1.00 19.11 ? 48  TYR A CE1 1 
ATOM   95   C  CE2 . TYR A 1 13  ? 2.099   -3.468  26.425  1.00 18.68 ? 48  TYR A CE2 1 
ATOM   96   C  CZ  . TYR A 1 13  ? 3.150   -2.703  25.928  1.00 24.44 ? 48  TYR A CZ  1 
ATOM   97   O  OH  . TYR A 1 13  ? 2.956   -1.892  24.833  1.00 21.04 ? 48  TYR A OH  1 
ATOM   98   N  N   . ARG A 1 14  ? 5.757   -7.004  27.090  1.00 17.09 ? 49  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 14  ? 7.044   -7.168  26.441  1.00 17.24 ? 49  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 14  ? 7.333   -5.973  25.538  1.00 17.57 ? 49  ARG A C   1 
ATOM   101  O  O   . ARG A 1 14  ? 6.469   -5.513  24.783  1.00 17.32 ? 49  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 14  ? 7.099   -8.445  25.622  1.00 17.86 ? 49  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 14  ? 8.540   -8.884  25.413  1.00 18.45 ? 49  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 14  ? 9.019   -9.748  26.585  1.00 17.35 ? 49  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 14  ? 8.367   -11.058 26.503  1.00 18.44 ? 49  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 14  ? 8.459   -12.013 27.415  1.00 18.62 ? 49  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 14  ? 9.163   -11.848 28.519  1.00 21.96 ? 49  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 14  ? 7.859   -13.192 27.192  1.00 20.20 ? 49  ARG A NH2 1 
ATOM   109  N  N   . MET A 1 15  ? 8.573   -5.505  25.595  1.00 15.97 ? 50  MET A N   1 
ATOM   110  C  CA  . MET A 1 15  ? 8.999   -4.351  24.808  1.00 16.06 ? 50  MET A CA  1 
ATOM   111  C  C   . MET A 1 15  ? 10.469  -4.487  24.456  1.00 19.56 ? 50  MET A C   1 
ATOM   112  O  O   . MET A 1 15  ? 11.288  -4.769  25.328  1.00 21.22 ? 50  MET A O   1 
ATOM   113  C  CB  . MET A 1 15  ? 8.783   -3.044  25.570  1.00 17.05 ? 50  MET A CB  1 
ATOM   114  C  CG  . MET A 1 15  ? 9.035   -1.816  24.726  1.00 20.96 ? 50  MET A CG  1 
ATOM   115  S  SD  . MET A 1 15  ? 8.949   -0.295  25.720  1.00 20.22 ? 50  MET A SD  1 
ATOM   116  C  CE  . MET A 1 15  ? 10.514  -0.405  26.596  1.00 18.15 ? 50  MET A CE  1 
ATOM   117  N  N   . LEU A 1 16  ? 10.795  -4.280  23.186  1.00 21.23 ? 51  LEU A N   1 
ATOM   118  C  CA  . LEU A 1 16  ? 12.176  -4.277  22.745  1.00 23.56 ? 51  LEU A CA  1 
ATOM   119  C  C   . LEU A 1 16  ? 12.791  -2.909  23.034  1.00 22.20 ? 51  LEU A C   1 
ATOM   120  O  O   . LEU A 1 16  ? 12.109  -1.889  23.007  1.00 21.12 ? 51  LEU A O   1 
ATOM   121  C  CB  . LEU A 1 16  ? 12.232  -4.602  21.250  1.00 21.50 ? 51  LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 16  ? 11.751  -6.019  20.877  1.00 20.39 ? 51  LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 16  ? 11.950  -6.324  19.385  1.00 21.43 ? 51  LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 16  ? 12.484  -7.067  21.744  1.00 23.60 ? 51  LEU A CD2 1 
ATOM   125  N  N   . LEU A 1 17  ? 14.079  -2.896  23.359  1.00 17.06 ? 52  LEU A N   1 
ATOM   126  C  CA  . LEU A 1 17  ? 14.810  -1.642  23.521  1.00 16.59 ? 52  LEU A CA  1 
ATOM   127  C  C   . LEU A 1 17  ? 16.170  -1.876  22.889  1.00 24.50 ? 52  LEU A C   1 
ATOM   128  O  O   . LEU A 1 17  ? 17.038  -2.466  23.532  1.00 21.67 ? 52  LEU A O   1 
ATOM   129  C  CB  . LEU A 1 17  ? 14.967  -1.263  24.989  1.00 26.93 ? 52  LEU A CB  1 
ATOM   130  C  CG  . LEU A 1 17  ? 15.688  0.070   25.279  1.00 19.19 ? 52  LEU A CG  1 
ATOM   131  C  CD1 . LEU A 1 17  ? 14.667  1.184   25.179  1.00 20.58 ? 52  LEU A CD1 1 
ATOM   132  C  CD2 . LEU A 1 17  ? 16.408  0.006   26.669  1.00 15.29 ? 52  LEU A CD2 1 
ATOM   133  N  N   . GLY A 1 18  ? 16.354  -1.431  21.655  1.00 22.51 ? 53  GLY A N   1 
ATOM   134  C  CA  . GLY A 1 18  ? 17.568  -1.827  20.949  1.00 19.82 ? 53  GLY A CA  1 
ATOM   135  C  C   . GLY A 1 18  ? 17.652  -3.338  20.864  1.00 26.30 ? 53  GLY A C   1 
ATOM   136  O  O   . GLY A 1 18  ? 16.731  -4.016  20.390  1.00 21.82 ? 53  GLY A O   1 
ATOM   137  N  N   . ASP A 1 19  ? 18.769  -3.888  21.344  1.00 21.01 ? 54  ASP A N   1 
ATOM   138  C  CA  . ASP A 1 19  ? 18.995  -5.321  21.367  1.00 20.72 ? 54  ASP A CA  1 
ATOM   139  C  C   . ASP A 1 19  ? 18.518  -5.962  22.662  1.00 19.62 ? 54  ASP A C   1 
ATOM   140  O  O   . ASP A 1 19  ? 18.559  -7.194  22.775  1.00 28.00 ? 54  ASP A O   1 
ATOM   141  C  CB  . ASP A 1 19  ? 20.502  -5.568  21.166  1.00 25.47 ? 54  ASP A CB  1 
ATOM   142  C  CG  . ASP A 1 19  ? 20.893  -5.619  19.697  1.00 29.82 ? 54  ASP A CG  1 
ATOM   143  O  OD1 . ASP A 1 19  ? 20.025  -5.329  18.838  1.00 30.61 ? 54  ASP A OD1 1 
ATOM   144  O  OD2 . ASP A 1 19  ? 22.098  -5.804  19.412  1.00 31.00 ? 54  ASP A OD2 1 
ATOM   145  N  N   . PHE A 1 20  ? 18.095  -5.163  23.646  1.00 17.92 ? 55  PHE A N   1 
ATOM   146  C  CA  . PHE A 1 20  ? 17.629  -5.706  24.913  1.00 16.74 ? 55  PHE A CA  1 
ATOM   147  C  C   . PHE A 1 20  ? 16.143  -6.042  24.857  1.00 25.93 ? 55  PHE A C   1 
ATOM   148  O  O   . PHE A 1 20  ? 15.358  -5.432  24.122  1.00 21.06 ? 55  PHE A O   1 
ATOM   149  C  CB  . PHE A 1 20  ? 17.829  -4.742  26.086  1.00 15.54 ? 55  PHE A CB  1 
ATOM   150  C  CG  . PHE A 1 20  ? 19.261  -4.379  26.382  1.00 19.55 ? 55  PHE A CG  1 
ATOM   151  C  CD1 . PHE A 1 20  ? 20.305  -5.020  25.765  1.00 20.64 ? 55  PHE A CD1 1 
ATOM   152  C  CD2 . PHE A 1 20  ? 19.544  -3.412  27.345  1.00 19.36 ? 55  PHE A CD2 1 
ATOM   153  C  CE1 . PHE A 1 20  ? 21.605  -4.666  26.064  1.00 26.29 ? 55  PHE A CE1 1 
ATOM   154  C  CE2 . PHE A 1 20  ? 20.835  -3.075  27.656  1.00 25.20 ? 55  PHE A CE2 1 
ATOM   155  C  CZ  . PHE A 1 20  ? 21.861  -3.699  27.022  1.00 19.80 ? 55  PHE A CZ  1 
ATOM   156  N  N   . GLU A 1 21  ? 15.750  -6.980  25.703  1.00 24.40 ? 56  GLU A N   1 
ATOM   157  C  CA  . GLU A 1 21  ? 14.345  -7.284  25.905  1.00 20.44 ? 56  GLU A CA  1 
ATOM   158  C  C   . GLU A 1 21  ? 13.933  -6.798  27.287  1.00 18.50 ? 56  GLU A C   1 
ATOM   159  O  O   . GLU A 1 21  ? 14.561  -7.153  28.287  1.00 17.60 ? 56  GLU A O   1 
ATOM   160  C  CB  . GLU A 1 21  ? 14.099  -8.783  25.752  1.00 20.57 ? 56  GLU A CB  1 
ATOM   161  C  CG  . GLU A 1 21  ? 12.717  -9.225  26.143  1.00 20.25 ? 56  GLU A CG  1 
ATOM   162  C  CD  . GLU A 1 21  ? 12.699  -10.658 26.670  1.00 20.10 ? 56  GLU A CD  1 
ATOM   163  O  OE1 . GLU A 1 21  ? 13.030  -10.877 27.859  1.00 16.63 ? 56  GLU A OE1 1 
ATOM   164  O  OE2 . GLU A 1 21  ? 12.314  -11.554 25.886  1.00 22.47 ? 56  GLU A OE2 1 
ATOM   165  N  N   . ILE A 1 22  ? 12.882  -5.999  27.340  1.00 16.40 ? 57  ILE A N   1 
ATOM   166  C  CA  . ILE A 1 22  ? 12.316  -5.489  28.578  1.00 19.52 ? 57  ILE A CA  1 
ATOM   167  C  C   . ILE A 1 22  ? 10.994  -6.198  28.787  1.00 19.58 ? 57  ILE A C   1 
ATOM   168  O  O   . ILE A 1 22  ? 10.204  -6.358  27.842  1.00 15.83 ? 57  ILE A O   1 
ATOM   169  C  CB  . ILE A 1 22  ? 12.090  -3.963  28.540  1.00 19.21 ? 57  ILE A CB  1 
ATOM   170  C  CG1 . ILE A 1 22  ? 13.311  -3.234  27.971  1.00 19.61 ? 57  ILE A CG1 1 
ATOM   171  C  CG2 . ILE A 1 22  ? 11.721  -3.430  29.926  1.00 20.06 ? 57  ILE A CG2 1 
ATOM   172  C  CD1 . ILE A 1 22  ? 14.607  -3.441  28.828  1.00 14.94 ? 57  ILE A CD1 1 
ATOM   173  N  N   . THR A 1 23  ? 10.749  -6.624  30.020  1.00 16.86 ? 58  THR A N   1 
ATOM   174  C  CA  . THR A 1 23  ? 9.449   -7.177  30.393  1.00 18.43 ? 58  THR A CA  1 
ATOM   175  C  C   . THR A 1 23  ? 8.973   -6.453  31.642  1.00 18.39 ? 58  THR A C   1 
ATOM   176  O  O   . THR A 1 23  ? 9.546   -6.639  32.721  1.00 18.87 ? 58  THR A O   1 
ATOM   177  C  CB  . THR A 1 23  ? 9.522   -8.688  30.653  1.00 17.19 ? 58  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 23  ? 10.134  -9.366  29.543  1.00 16.91 ? 58  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 23  ? 8.111   -9.242  30.815  1.00 20.11 ? 58  THR A CG2 1 
ATOM   180  N  N   . ALA A 1 24  ? 7.918   -5.655  31.517  1.00 15.11 ? 59  ALA A N   1 
ATOM   181  C  CA  . ALA A 1 24  ? 7.260   -5.151  32.714  1.00 16.62 ? 59  ALA A CA  1 
ATOM   182  C  C   . ALA A 1 24  ? 6.523   -6.330  33.368  1.00 22.17 ? 59  ALA A C   1 
ATOM   183  O  O   . ALA A 1 24  ? 5.833   -7.095  32.687  1.00 17.45 ? 59  ALA A O   1 
ATOM   184  C  CB  . ALA A 1 24  ? 6.304   -3.994  32.358  1.00 13.69 ? 59  ALA A CB  1 
ATOM   185  N  N   . LEU A 1 25  ? 6.736   -6.520  34.673  1.00 18.01 ? 60  LEU A N   1 
ATOM   186  C  CA  . LEU A 1 25  ? 6.110   -7.582  35.450  1.00 16.36 ? 60  LEU A CA  1 
ATOM   187  C  C   . LEU A 1 25  ? 5.182   -6.986  36.503  1.00 19.40 ? 60  LEU A C   1 
ATOM   188  O  O   . LEU A 1 25  ? 5.636   -6.288  37.422  1.00 17.20 ? 60  LEU A O   1 
ATOM   189  C  CB  . LEU A 1 25  ? 7.177   -8.446  36.112  1.00 18.24 ? 60  LEU A CB  1 
ATOM   190  C  CG  . LEU A 1 25  ? 8.134   -9.156  35.166  1.00 20.13 ? 60  LEU A CG  1 
ATOM   191  C  CD1 . LEU A 1 25  ? 9.237   -9.887  35.979  1.00 15.12 ? 60  LEU A CD1 1 
ATOM   192  C  CD2 . LEU A 1 25  ? 7.314   -10.126 34.274  1.00 18.59 ? 60  LEU A CD2 1 
ATOM   193  N  N   . SER A 1 26  ? 3.883   -7.274  36.383  1.00 20.01 ? 61  SER A N   1 
ATOM   194  C  CA  . SER A 1 26  ? 2.921   -6.745  37.337  1.00 17.39 ? 61  SER A CA  1 
ATOM   195  C  C   . SER A 1 26  ? 3.004   -7.510  38.654  1.00 17.89 ? 61  SER A C   1 
ATOM   196  O  O   . SER A 1 26  ? 3.096   -8.737  38.664  1.00 18.55 ? 61  SER A O   1 
ATOM   197  C  CB  . SER A 1 26  ? 1.505   -6.834  36.772  1.00 18.95 ? 61  SER A CB  1 
ATOM   198  O  OG  . SER A 1 26  ? 0.599   -6.418  37.757  1.00 19.95 ? 61  SER A OG  1 
ATOM   199  N  N   . ASP A 1 27  ? 3.010   -6.782  39.767  1.00 18.66 ? 62  ASP A N   1 
ATOM   200  C  CA  . ASP A 1 27  ? 2.866   -7.417  41.067  1.00 25.31 ? 62  ASP A CA  1 
ATOM   201  C  C   . ASP A 1 27  ? 1.432   -7.423  41.561  1.00 24.75 ? 62  ASP A C   1 
ATOM   202  O  O   . ASP A 1 27  ? 1.148   -8.040  42.604  1.00 25.45 ? 62  ASP A O   1 
ATOM   203  C  CB  . ASP A 1 27  ? 3.750   -6.728  42.089  1.00 18.34 ? 62  ASP A CB  1 
ATOM   204  C  CG  . ASP A 1 27  ? 3.958   -7.560  43.316  1.00 18.09 ? 62  ASP A CG  1 
ATOM   205  O  OD1 . ASP A 1 27  ? 4.352   -8.737  43.216  1.00 22.17 ? 62  ASP A OD1 1 
ATOM   206  O  OD2 . ASP A 1 27  ? 3.665   -7.029  44.404  1.00 23.19 ? 62  ASP A OD2 1 
ATOM   207  N  N   . GLY A 1 28  ? 0.528   -6.812  40.806  1.00 21.00 ? 63  GLY A N   1 
ATOM   208  C  CA  . GLY A 1 28  ? -0.841  -6.607  41.206  1.00 22.92 ? 63  GLY A CA  1 
ATOM   209  C  C   . GLY A 1 28  ? -1.133  -5.128  41.284  1.00 22.61 ? 63  GLY A C   1 
ATOM   210  O  O   . GLY A 1 28  ? -0.370  -4.294  40.784  1.00 20.98 ? 63  GLY A O   1 
ATOM   211  N  N   . THR A 1 29  ? -2.282  -4.799  41.884  1.00 22.84 ? 64  THR A N   1 
ATOM   212  C  CA  . THR A 1 29  ? -2.612  -3.417  42.219  1.00 21.97 ? 64  THR A CA  1 
ATOM   213  C  C   . THR A 1 29  ? -3.071  -3.350  43.673  1.00 23.84 ? 64  THR A C   1 
ATOM   214  O  O   . THR A 1 29  ? -3.442  -4.366  44.276  1.00 29.53 ? 64  THR A O   1 
ATOM   215  C  CB  . THR A 1 29  ? -3.697  -2.871  41.309  1.00 22.39 ? 64  THR A CB  1 
ATOM   216  O  OG1 . THR A 1 29  ? -4.930  -3.567  41.567  1.00 23.70 ? 64  THR A OG1 1 
ATOM   217  C  CG2 . THR A 1 29  ? -3.295  -3.085  39.859  1.00 28.36 ? 64  THR A CG2 1 
ATOM   218  N  N   . VAL A 1 30  ? -3.047  -2.149  44.251  1.00 26.29 ? 65  VAL A N   1 
ATOM   219  C  CA  . VAL A 1 30  ? -3.574  -1.963  45.610  1.00 27.24 ? 65  VAL A CA  1 
ATOM   220  C  C   . VAL A 1 30  ? -4.249  -0.591  45.703  1.00 27.30 ? 65  VAL A C   1 
ATOM   221  O  O   . VAL A 1 30  ? -3.773  0.375   45.118  1.00 26.75 ? 65  VAL A O   1 
ATOM   222  C  CB  . VAL A 1 30  ? -2.454  -2.110  46.662  1.00 26.09 ? 65  VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 30  ? -1.327  -1.158  46.353  1.00 26.67 ? 65  VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 30  ? -2.986  -1.887  48.070  1.00 35.45 ? 65  VAL A CG2 1 
ATOM   225  N  N   . ASP A 1 31  ? -5.357  -0.489  46.438  1.00 29.04 ? 66  ASP A N   1 
ATOM   226  C  CA  . ASP A 1 31  ? -6.031  0.809   46.550  1.00 30.31 ? 66  ASP A CA  1 
ATOM   227  C  C   . ASP A 1 31  ? -5.337  1.669   47.600  1.00 35.78 ? 66  ASP A C   1 
ATOM   228  O  O   . ASP A 1 31  ? -5.147  1.230   48.735  1.00 34.99 ? 66  ASP A O   1 
ATOM   229  C  CB  . ASP A 1 31  ? -7.503  0.651   46.920  1.00 33.68 ? 66  ASP A CB  1 
ATOM   230  C  CG  . ASP A 1 31  ? -8.268  -0.169  45.917  1.00 41.72 ? 66  ASP A CG  1 
ATOM   231  O  OD1 . ASP A 1 31  ? -8.172  0.109   44.704  1.00 42.36 ? 66  ASP A OD1 1 
ATOM   232  O  OD2 . ASP A 1 31  ? -8.990  -1.080  46.352  1.00 51.14 ? 66  ASP A OD2 1 
ATOM   233  N  N   . LEU A 1 32  ? -4.968  2.899   47.223  1.00 36.81 ? 67  LEU A N   1 
ATOM   234  C  CA  . LEU A 1 32  ? -4.222  3.795   48.102  1.00 32.42 ? 67  LEU A CA  1 
ATOM   235  C  C   . LEU A 1 32  ? -4.993  5.088   48.355  1.00 36.98 ? 67  LEU A C   1 
ATOM   236  O  O   . LEU A 1 32  ? -5.556  5.673   47.416  1.00 38.02 ? 67  LEU A O   1 
ATOM   237  C  CB  . LEU A 1 32  ? -2.828  4.143   47.527  1.00 30.10 ? 67  LEU A CB  1 
ATOM   238  C  CG  . LEU A 1 32  ? -1.871  2.969   47.282  1.00 33.08 ? 67  LEU A CG  1 
ATOM   239  C  CD1 . LEU A 1 32  ? -0.522  3.399   46.689  1.00 34.72 ? 67  LEU A CD1 1 
ATOM   240  C  CD2 . LEU A 1 32  ? -1.673  2.188   48.577  1.00 32.53 ? 67  LEU A CD2 1 
ATOM   241  N  N   . PRO A 1 33  ? -5.058  5.549   49.626  1.00 34.88 ? 68  PRO A N   1 
ATOM   242  C  CA  . PRO A 1 33  ? -5.702  6.841   49.950  1.00 38.47 ? 68  PRO A CA  1 
ATOM   243  C  C   . PRO A 1 33  ? -4.777  8.006   49.626  1.00 44.91 ? 68  PRO A C   1 
ATOM   244  O  O   . PRO A 1 33  ? -4.224  8.688   50.502  1.00 40.10 ? 68  PRO A O   1 
ATOM   245  C  CB  . PRO A 1 33  ? -5.981  6.703   51.449  1.00 42.06 ? 68  PRO A CB  1 
ATOM   246  C  CG  . PRO A 1 33  ? -4.920  5.799   51.947  1.00 39.61 ? 68  PRO A CG  1 
ATOM   247  C  CD  . PRO A 1 33  ? -4.687  4.801   50.841  1.00 39.87 ? 68  PRO A CD  1 
ATOM   248  N  N   . VAL A 1 34  ? -4.584  8.230   48.323  1.00 36.60 ? 69  VAL A N   1 
ATOM   249  C  CA  . VAL A 1 34  ? -3.649  9.249   47.855  1.00 36.45 ? 69  VAL A CA  1 
ATOM   250  C  C   . VAL A 1 34  ? -4.018  10.629  48.399  1.00 42.77 ? 69  VAL A C   1 
ATOM   251  O  O   . VAL A 1 34  ? -3.149  11.485  48.602  1.00 42.09 ? 69  VAL A O   1 
ATOM   252  C  CB  . VAL A 1 34  ? -3.598  9.248   46.319  1.00 42.99 ? 69  VAL A CB  1 
ATOM   253  C  CG1 . VAL A 1 34  ? -3.263  7.861   45.809  1.00 50.12 ? 69  VAL A CG1 1 
ATOM   254  C  CG2 . VAL A 1 34  ? -4.919  9.745   45.757  1.00 44.69 ? 69  VAL A CG2 1 
ATOM   255  N  N   . ASP A 1 35  ? -5.310  10.865  48.651  1.00 40.98 ? 70  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 35  ? -5.739  12.164  49.159  1.00 43.29 ? 70  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 35  ? -5.217  12.411  50.564  1.00 47.51 ? 70  ASP A C   1 
ATOM   258  O  O   . ASP A 1 35  ? -4.978  13.564  50.949  1.00 51.54 ? 70  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 35  ? -7.264  12.257  49.126  1.00 43.92 ? 70  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 35  ? -7.928  11.163  49.920  1.00 44.42 ? 70  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 35  ? -7.394  10.031  49.936  1.00 50.75 ? 70  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 35  ? -8.984  11.435  50.528  1.00 57.24 ? 70  ASP A OD2 1 
ATOM   263  N  N   . LYS A 1 36  ? -5.003  11.353  51.321  1.00 43.29 ? 71  LYS A N   1 
ATOM   264  C  CA  . LYS A 1 36  ? -4.439  11.536  52.677  1.00 51.20 ? 71  LYS A CA  1 
ATOM   265  C  C   . LYS A 1 36  ? -2.907  11.584  52.648  1.00 46.89 ? 71  LYS A C   1 
ATOM   266  O  O   . LYS A 1 36  ? -2.324  12.156  53.579  1.00 55.35 ? 71  LYS A O   1 
ATOM   267  C  CB  . LYS A 1 36  ? -4.919  10.363  53.534  1.00 51.20 ? 71  LYS A CB  1 
ATOM   268  C  CG  . LYS A 1 36  ? -6.421  10.299  53.732  1.00 48.99 ? 71  LYS A CG  1 
ATOM   269  C  CD  . LYS A 1 36  ? -6.872  8.946   54.264  1.00 56.76 ? 71  LYS A CD  1 
ATOM   270  C  CE  . LYS A 1 36  ? -5.792  8.266   55.044  1.00 61.34 ? 71  LYS A CE  1 
ATOM   271  N  NZ  . LYS A 1 36  ? -6.086  6.848   55.261  1.00 63.25 ? 71  LYS A NZ  1 
ATOM   272  N  N   . ARG A 1 37  ? -2.279  11.020  51.621  1.00 46.43 ? 72  ARG A N   1 
ATOM   273  C  CA  . ARG A 1 37  ? -0.796  10.915  51.656  1.00 46.15 ? 72  ARG A CA  1 
ATOM   274  C  C   . ARG A 1 37  ? -0.111  12.107  50.964  1.00 42.89 ? 72  ARG A C   1 
ATOM   275  O  O   . ARG A 1 37  ? 0.987   12.478  51.403  1.00 40.12 ? 72  ARG A O   1 
ATOM   276  C  CB  . ARG A 1 37  ? -0.405  9.532   51.118  1.00 50.55 ? 72  ARG A CB  1 
ATOM   277  C  CG  . ARG A 1 37  ? -0.855  8.412   52.045  1.00 50.97 ? 72  ARG A CG  1 
ATOM   278  C  CD  . ARG A 1 37  ? -0.437  7.033   51.559  1.00 53.79 ? 72  ARG A CD  1 
ATOM   279  N  NE  . ARG A 1 37  ? -0.941  5.962   52.428  1.00 63.16 ? 72  ARG A NE  1 
ATOM   280  C  CZ  . ARG A 1 37  ? -0.829  4.660   52.190  1.00 58.71 ? 72  ARG A CZ  1 
ATOM   281  N  NH1 . ARG A 1 37  ? -1.246  4.156   51.044  1.00 64.82 ? 72  ARG A NH1 1 
ATOM   282  N  NH2 . ARG A 1 37  ? -0.308  3.862   53.105  1.00 57.50 ? 72  ARG A NH2 1 
ATOM   283  N  N   . LEU A 1 38  ? -0.716  12.664  49.924  1.00 37.70 ? 73  LEU A N   1 
ATOM   284  C  CA  . LEU A 1 38  ? -0.099  13.804  49.199  1.00 36.92 ? 73  LEU A CA  1 
ATOM   285  C  C   . LEU A 1 38  ? -0.054  15.060  50.089  1.00 41.88 ? 73  LEU A C   1 
ATOM   286  O  O   . LEU A 1 38  ? -1.052  15.348  50.771  1.00 43.73 ? 73  LEU A O   1 
ATOM   287  C  CB  . LEU A 1 38  ? -0.795  14.105  47.876  1.00 36.20 ? 73  LEU A CB  1 
ATOM   288  C  CG  . LEU A 1 38  ? -0.511  13.144  46.720  1.00 35.66 ? 73  LEU A CG  1 
ATOM   289  C  CD1 . LEU A 1 38  ? -1.653  13.233  45.736  1.00 33.83 ? 73  LEU A CD1 1 
ATOM   290  C  CD2 . LEU A 1 38  ? 0.793   13.492  46.039  1.00 35.02 ? 73  LEU A CD2 1 
ATOM   291  N  N   . ASN A 1 39  ? 1.039   15.813  50.009  1.00 41.88 ? 74  ASN A N   1 
ATOM   292  C  CA  . ASN A 1 39  ? 1.219   17.010  50.834  1.00 41.06 ? 74  ASN A CA  1 
ATOM   293  C  C   . ASN A 1 39  ? 0.587   18.222  50.149  1.00 41.76 ? 74  ASN A C   1 
ATOM   294  O  O   . ASN A 1 39  ? 1.259   19.143  49.680  1.00 44.16 ? 74  ASN A O   1 
ATOM   295  C  CB  . ASN A 1 39  ? 2.697   17.237  51.121  1.00 41.08 ? 74  ASN A CB  1 
ATOM   296  C  CG  . ASN A 1 39  ? 3.281   16.181  52.042  1.00 44.18 ? 74  ASN A CG  1 
ATOM   297  O  OD1 . ASN A 1 39  ? 2.609   15.718  52.966  1.00 47.68 ? 74  ASN A OD1 1 
ATOM   298  N  ND2 . ASN A 1 39  ? 4.552   15.823  51.822  1.00 42.41 ? 74  ASN A ND2 1 
ATOM   299  N  N   . GLN A 1 40  ? -0.738  18.225  50.128  1.00 42.34 ? 75  GLN A N   1 
ATOM   300  C  CA  . GLN A 1 40  ? -1.502  19.294  49.500  1.00 43.11 ? 75  GLN A CA  1 
ATOM   301  C  C   . GLN A 1 40  ? -2.942  19.194  49.984  1.00 44.34 ? 75  GLN A C   1 
ATOM   302  O  O   . GLN A 1 40  ? -3.352  18.149  50.487  1.00 44.13 ? 75  GLN A O   1 
ATOM   303  C  CB  . GLN A 1 40  ? -1.436  19.193  47.969  1.00 44.32 ? 75  GLN A CB  1 
ATOM   304  C  CG  . GLN A 1 40  ? -2.356  18.151  47.388  1.00 40.27 ? 75  GLN A CG  1 
ATOM   305  C  CD  . GLN A 1 40  ? -2.423  18.249  45.886  1.00 43.51 ? 75  GLN A CD  1 
ATOM   306  O  OE1 . GLN A 1 40  ? -1.869  19.180  45.292  1.00 41.11 ? 75  GLN A OE1 1 
ATOM   307  N  NE2 . GLN A 1 40  ? -3.094  17.288  45.257  1.00 37.88 ? 75  GLN A NE2 1 
ATOM   308  N  N   . PRO A 1 41  ? -3.719  20.269  49.865  1.00 45.76 ? 76  PRO A N   1 
ATOM   309  C  CA  . PRO A 1 41  ? -5.115  20.198  50.311  1.00 47.11 ? 76  PRO A CA  1 
ATOM   310  C  C   . PRO A 1 41  ? -5.886  19.126  49.547  1.00 46.84 ? 76  PRO A C   1 
ATOM   311  O  O   . PRO A 1 41  ? -5.706  18.938  48.341  1.00 45.49 ? 76  PRO A O   1 
ATOM   312  C  CB  . PRO A 1 41  ? -5.661  21.603  50.026  1.00 48.61 ? 76  PRO A CB  1 
ATOM   313  C  CG  . PRO A 1 41  ? -4.472  22.482  49.931  1.00 48.62 ? 76  PRO A CG  1 
ATOM   314  C  CD  . PRO A 1 41  ? -3.318  21.632  49.487  1.00 48.71 ? 76  PRO A CD  1 
ATOM   315  N  N   . ALA A 1 42  ? -6.738  18.406  50.273  1.00 46.59 ? 77  ALA A N   1 
ATOM   316  C  CA  . ALA A 1 42  ? -7.602  17.415  49.640  1.00 49.79 ? 77  ALA A CA  1 
ATOM   317  C  C   . ALA A 1 42  ? -8.425  17.974  48.484  1.00 47.91 ? 77  ALA A C   1 
ATOM   318  O  O   . ALA A 1 42  ? -8.597  17.244  47.494  1.00 46.52 ? 77  ALA A O   1 
ATOM   319  C  CB  . ALA A 1 42  ? -8.518  16.774  50.692  1.00 56.49 ? 77  ALA A CB  1 
ATOM   320  N  N   . PRO A 1 43  ? -8.983  19.201  48.545  1.00 47.46 ? 78  PRO A N   1 
ATOM   321  C  CA  . PRO A 1 43  ? -9.691  19.745  47.370  1.00 49.91 ? 78  PRO A CA  1 
ATOM   322  C  C   . PRO A 1 43  ? -8.881  19.672  46.093  1.00 45.25 ? 78  PRO A C   1 
ATOM   323  O  O   . PRO A 1 43  ? -9.402  19.309  45.025  1.00 44.40 ? 78  PRO A O   1 
ATOM   324  C  CB  . PRO A 1 43  ? -9.926  21.201  47.772  1.00 49.35 ? 78  PRO A CB  1 
ATOM   325  C  CG  . PRO A 1 43  ? -10.127 21.139  49.226  1.00 51.04 ? 78  PRO A CG  1 
ATOM   326  C  CD  . PRO A 1 43  ? -9.198  20.054  49.729  1.00 51.16 ? 78  PRO A CD  1 
ATOM   327  N  N   . LYS A 1 44  ? -7.594  20.014  46.188  1.00 44.55 ? 79  LYS A N   1 
ATOM   328  C  CA  . LYS A 1 44  ? -6.722  19.939  45.029  1.00 42.70 ? 79  LYS A CA  1 
ATOM   329  C  C   . LYS A 1 44  ? -6.645  18.509  44.509  1.00 40.99 ? 79  LYS A C   1 
ATOM   330  O  O   . LYS A 1 44  ? -6.796  18.268  43.305  1.00 39.69 ? 79  LYS A O   1 
ATOM   331  C  CB  . LYS A 1 44  ? -5.339  20.470  45.404  1.00 42.67 ? 79  LYS A CB  1 
ATOM   332  C  CG  . LYS A 1 44  ? -5.062  21.909  44.986  1.00 47.48 ? 79  LYS A CG  1 
ATOM   333  C  CD  . LYS A 1 44  ? -3.568  22.198  45.006  1.00 49.24 ? 79  LYS A CD  1 
ATOM   334  C  CE  . LYS A 1 44  ? -3.211  23.312  44.048  1.00 51.10 ? 79  LYS A CE  1 
ATOM   335  N  NZ  . LYS A 1 44  ? -3.438  22.848  42.652  1.00 45.61 ? 79  LYS A NZ  1 
ATOM   336  N  N   . THR A 1 45  ? -6.434  17.544  45.411  1.00 40.59 ? 80  THR A N   1 
ATOM   337  C  CA  . THR A 1 45  ? -6.244  16.156  44.988  1.00 38.83 ? 80  THR A CA  1 
ATOM   338  C  C   . THR A 1 45  ? -7.517  15.572  44.379  1.00 38.85 ? 80  THR A C   1 
ATOM   339  O  O   . THR A 1 45  ? -7.453  14.915  43.331  1.00 38.66 ? 80  THR A O   1 
ATOM   340  C  CB  . THR A 1 45  ? -5.749  15.299  46.166  1.00 38.80 ? 80  THR A CB  1 
ATOM   341  O  OG1 . THR A 1 45  ? -4.477  15.782  46.626  1.00 38.70 ? 80  THR A OG1 1 
ATOM   342  C  CG2 . THR A 1 45  ? -5.571  13.840  45.750  1.00 37.07 ? 80  THR A CG2 1 
ATOM   343  N  N   . GLN A 1 46  ? -8.679  15.796  45.011  1.00 41.25 ? 81  GLN A N   1 
ATOM   344  C  CA  . GLN A 1 46  ? -9.941  15.354  44.411  1.00 43.98 ? 81  GLN A CA  1 
ATOM   345  C  C   . GLN A 1 46  ? -10.122 15.963  43.033  1.00 41.47 ? 81  GLN A C   1 
ATOM   346  O  O   . GLN A 1 46  ? -10.538 15.274  42.094  1.00 45.36 ? 81  GLN A O   1 
ATOM   347  C  CB  . GLN A 1 46  ? -11.167 15.736  45.252  1.00 43.33 ? 81  GLN A CB  1 
ATOM   348  C  CG  . GLN A 1 46  ? -11.207 17.195  45.638  1.00 50.03 ? 81  GLN A CG  1 
ATOM   349  C  CD  . GLN A 1 46  ? -12.607 17.764  45.915  1.00 66.38 ? 81  GLN A CD  1 
ATOM   350  O  OE1 . GLN A 1 46  ? -13.314 17.342  46.832  1.00 69.21 ? 81  GLN A OE1 1 
ATOM   351  N  NE2 . GLN A 1 46  ? -12.990 18.765  45.116  1.00 55.05 ? 81  GLN A NE2 1 
ATOM   352  N  N   . SER A 1 47  ? -9.835  17.262  42.901  1.00 47.06 ? 82  SER A N   1 
ATOM   353  C  CA  . SER A 1 47  ? -9.912  17.914  41.602  1.00 47.50 ? 82  SER A CA  1 
ATOM   354  C  C   . SER A 1 47  ? -9.070  17.175  40.569  1.00 38.54 ? 82  SER A C   1 
ATOM   355  O  O   . SER A 1 47  ? -9.576  16.774  39.517  1.00 37.93 ? 82  SER A O   1 
ATOM   356  C  CB  . SER A 1 47  ? -9.450  19.365  41.742  1.00 41.71 ? 82  SER A CB  1 
ATOM   357  O  OG  . SER A 1 47  ? -9.532  20.032  40.501  1.00 50.08 ? 82  SER A OG  1 
ATOM   358  N  N   . ALA A 1 48  ? -7.789  16.954  40.878  1.00 37.44 ? 83  ALA A N   1 
ATOM   359  C  CA  . ALA A 1 48  ? -6.870  16.346  39.915  1.00 36.75 ? 83  ALA A CA  1 
ATOM   360  C  C   . ALA A 1 48  ? -7.322  14.938  39.533  1.00 39.52 ? 83  ALA A C   1 
ATOM   361  O  O   . ALA A 1 48  ? -7.318  14.553  38.346  1.00 33.33 ? 83  ALA A O   1 
ATOM   362  C  CB  . ALA A 1 48  ? -5.454  16.322  40.501  1.00 36.15 ? 83  ALA A CB  1 
ATOM   363  N  N   . LEU A 1 49  ? -7.728  14.156  40.534  1.00 34.83 ? 84  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 49  ? -8.166  12.791  40.272  1.00 39.30 ? 84  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 49  ? -9.408  12.787  39.388  1.00 39.77 ? 84  LEU A C   1 
ATOM   366  O  O   . LEU A 1 49  ? -9.494  12.021  38.421  1.00 38.52 ? 84  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 49  ? -8.427  12.063  41.593  1.00 39.80 ? 84  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 49  ? -7.227  11.504  42.381  1.00 44.88 ? 84  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 49  ? -7.703  10.504  43.421  1.00 48.04 ? 84  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 49  ? -6.151  10.861  41.494  1.00 46.16 ? 84  LEU A CD2 1 
ATOM   371  N  N   . ALA A 1 50  ? -10.376 13.660  39.687  1.00 36.39 ? 85  ALA A N   1 
ATOM   372  C  CA  . ALA A 1 50  ? -11.572 13.727  38.853  1.00 37.14 ? 85  ALA A CA  1 
ATOM   373  C  C   . ALA A 1 50  ? -11.245 14.213  37.447  1.00 36.26 ? 85  ALA A C   1 
ATOM   374  O  O   . ALA A 1 50  ? -11.893 13.803  36.479  1.00 36.10 ? 85  ALA A O   1 
ATOM   375  C  CB  . ALA A 1 50  ? -12.617 14.624  39.509  1.00 39.41 ? 85  ALA A CB  1 
ATOM   376  N  N   . LYS A 1 51  ? -10.249 15.088  37.317  1.00 41.57 ? 86  LYS A N   1 
ATOM   377  C  CA  . LYS A 1 51  ? -9.810  15.525  35.999  1.00 37.44 ? 86  LYS A CA  1 
ATOM   378  C  C   . LYS A 1 51  ? -9.363  14.337  35.175  1.00 33.22 ? 86  LYS A C   1 
ATOM   379  O  O   . LYS A 1 51  ? -9.658  14.251  33.978  1.00 36.35 ? 86  LYS A O   1 
ATOM   380  C  CB  . LYS A 1 51  ? -8.670  16.530  36.132  1.00 38.06 ? 86  LYS A CB  1 
ATOM   381  C  CG  . LYS A 1 51  ? -8.289  17.229  34.843  1.00 49.29 ? 86  LYS A CG  1 
ATOM   382  C  CD  . LYS A 1 51  ? -7.124  18.184  35.069  1.00 52.04 ? 86  LYS A CD  1 
ATOM   383  C  CE  . LYS A 1 51  ? -6.462  18.572  33.758  1.00 57.20 ? 86  LYS A CE  1 
ATOM   384  N  NZ  . LYS A 1 51  ? -5.006  18.806  33.942  1.00 55.37 ? 86  LYS A NZ  1 
ATOM   385  N  N   . SER A 1 52  ? -8.654  13.408  35.807  1.00 32.88 ? 87  SER A N   1 
ATOM   386  C  CA  . SER A 1 52  ? -8.245  12.178  35.149  1.00 35.33 ? 87  SER A CA  1 
ATOM   387  C  C   . SER A 1 52  ? -9.274  11.054  35.283  1.00 35.18 ? 87  SER A C   1 
ATOM   388  O  O   . SER A 1 52  ? -8.949  9.896   35.006  1.00 29.83 ? 87  SER A O   1 
ATOM   389  C  CB  . SER A 1 52  ? -6.892  11.741  35.691  1.00 34.07 ? 87  SER A CB  1 
ATOM   390  O  OG  . SER A 1 52  ? -5.881  12.511  35.093  1.00 44.00 ? 87  SER A OG  1 
ATOM   391  N  N   . PHE A 1 53  ? -10.505 11.384  35.680  1.00 32.50 ? 88  PHE A N   1 
ATOM   392  C  CA  . PHE A 1 53  ? -11.614 10.437  35.793  1.00 34.29 ? 88  PHE A CA  1 
ATOM   393  C  C   . PHE A 1 53  ? -11.358 9.386   36.869  1.00 38.44 ? 88  PHE A C   1 
ATOM   394  O  O   . PHE A 1 53  ? -11.821 8.248   36.765  1.00 40.33 ? 88  PHE A O   1 
ATOM   395  C  CB  . PHE A 1 53  ? -11.917 9.774   34.443  1.00 35.99 ? 88  PHE A CB  1 
ATOM   396  C  CG  . PHE A 1 53  ? -12.210 10.762  33.361  1.00 32.85 ? 88  PHE A CG  1 
ATOM   397  C  CD1 . PHE A 1 53  ? -13.503 11.197  33.148  1.00 34.55 ? 88  PHE A CD1 1 
ATOM   398  C  CD2 . PHE A 1 53  ? -11.183 11.302  32.592  1.00 34.51 ? 88  PHE A CD2 1 
ATOM   399  C  CE1 . PHE A 1 53  ? -13.792 12.117  32.171  1.00 35.39 ? 88  PHE A CE1 1 
ATOM   400  C  CE2 . PHE A 1 53  ? -11.474 12.237  31.603  1.00 35.46 ? 88  PHE A CE2 1 
ATOM   401  C  CZ  . PHE A 1 53  ? -12.787 12.638  31.400  1.00 33.97 ? 88  PHE A CZ  1 
ATOM   402  N  N   . GLN A 1 54  ? -10.647 9.766   37.922  1.00 33.89 ? 89  GLN A N   1 
ATOM   403  C  CA  . GLN A 1 54  ? -10.317 8.852   39.002  1.00 41.72 ? 89  GLN A CA  1 
ATOM   404  C  C   . GLN A 1 54  ? -10.992 9.313   40.288  1.00 43.66 ? 89  GLN A C   1 
ATOM   405  O  O   . GLN A 1 54  ? -11.408 10.472  40.420  1.00 42.35 ? 89  GLN A O   1 
ATOM   406  C  CB  . GLN A 1 54  ? -8.798  8.752   39.213  1.00 41.38 ? 89  GLN A CB  1 
ATOM   407  C  CG  . GLN A 1 54  ? -8.012  7.996   38.133  1.00 41.35 ? 89  GLN A CG  1 
ATOM   408  C  CD  . GLN A 1 54  ? -6.490  8.134   38.304  1.00 50.46 ? 89  GLN A CD  1 
ATOM   409  O  OE1 . GLN A 1 54  ? -5.984  9.191   38.708  1.00 47.25 ? 89  GLN A OE1 1 
ATOM   410  N  NE2 . GLN A 1 54  ? -5.753  7.058   37.996  1.00 48.14 ? 89  GLN A NE2 1 
ATOM   411  N  N   . LYS A 1 55  ? -11.168 8.396   41.247  1.00 45.73 ? 90  LYS A N   1 
ATOM   412  C  CA  . LYS A 1 55  ? -11.955 8.744   42.466  1.00 52.97 ? 90  LYS A CA  1 
ATOM   413  C  C   . LYS A 1 55  ? -11.058 9.221   43.620  1.00 51.72 ? 90  LYS A C   1 
ATOM   414  O  O   . LYS A 1 55  ? -10.749 10.429  43.650  1.00 53.88 ? 90  LYS A O   1 
ATOM   415  C  CB  . LYS A 1 55  ? -12.796 7.541   42.910  1.00 58.73 ? 90  LYS A CB  1 
ATOM   416  C  CG  . LYS A 1 55  ? -12.392 6.210   42.298  1.00 63.36 ? 90  LYS A CG  1 
ATOM   417  C  CD  . LYS A 1 55  ? -11.613 5.342   43.278  1.00 61.85 ? 90  LYS A CD  1 
ATOM   418  C  CE  . LYS A 1 55  ? -12.399 4.171   43.771  1.00 62.00 ? 90  LYS A CE  1 
ATOM   419  N  NZ  . LYS A 1 55  ? -11.525 3.166   44.381  1.00 53.13 ? 90  LYS A NZ  1 
ATOM   420  N  N   . ALA A 1 56  ? -10.732 8.329   44.565  1.00 57.26 ? 91  ALA A N   1 
ATOM   421  C  CA  . ALA A 1 56  ? -9.878  8.688   45.728  1.00 53.96 ? 91  ALA A CA  1 
ATOM   422  C  C   . ALA A 1 56  ? -9.070  7.468   46.186  1.00 52.32 ? 91  ALA A C   1 
ATOM   423  O  O   . ALA A 1 56  ? -7.827  7.597   46.222  1.00 51.32 ? 91  ALA A O   1 
ATOM   424  C  CB  . ALA A 1 56  ? -10.704 9.305   46.844  1.00 64.07 ? 91  ALA A CB  1 
ATOM   425  N  N   . PRO A 1 57  ? -9.665  6.303   46.552  1.00 55.96 ? 92  PRO A N   1 
ATOM   426  C  CA  . PRO A 1 57  ? -8.881  5.114   46.864  1.00 51.13 ? 92  PRO A CA  1 
ATOM   427  C  C   . PRO A 1 57  ? -8.309  4.704   45.527  1.00 40.98 ? 92  PRO A C   1 
ATOM   428  O  O   . PRO A 1 57  ? -8.868  3.799   44.875  1.00 46.06 ? 92  PRO A O   1 
ATOM   429  C  CB  . PRO A 1 57  ? -9.874  4.094   47.422  1.00 52.41 ? 92  PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 57  ? -11.109 4.910   47.725  1.00 53.97 ? 92  PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 57  ? -11.090 6.056   46.728  1.00 55.38 ? 92  PRO A CD  1 
ATOM   432  N  N   . LEU A 1 58  ? -7.211  5.339   45.118  1.00 38.42 ? 93  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 58  ? -6.662  5.095   43.762  1.00 31.18 ? 93  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 58  ? -6.150  3.661   43.607  1.00 31.21 ? 93  LEU A C   1 
ATOM   435  O  O   . LEU A 1 58  ? -5.180  3.302   44.310  1.00 28.75 ? 93  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 58  ? -5.536  6.098   43.532  1.00 43.02 ? 93  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 58  ? -5.181  6.363   42.068  1.00 38.29 ? 93  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 58  ? -6.439  6.243   41.230  1.00 45.79 ? 93  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 58  ? -4.591  7.751   41.954  1.00 40.55 ? 93  LEU A CD2 1 
ATOM   440  N  N   . GLU A 1 59  ? -6.771  2.879   42.719  1.00 29.11 ? 94  GLU A N   1 
ATOM   441  C  CA  . GLU A 1 59  ? -6.204  1.557   42.447  1.00 27.22 ? 94  GLU A CA  1 
ATOM   442  C  C   . GLU A 1 59  ? -4.840  1.737   41.793  1.00 25.54 ? 94  GLU A C   1 
ATOM   443  O  O   . GLU A 1 59  ? -4.756  2.162   40.637  1.00 25.07 ? 94  GLU A O   1 
ATOM   444  C  CB  . GLU A 1 59  ? -7.123  0.740   41.545  1.00 29.59 ? 94  GLU A CB  1 
ATOM   445  C  CG  . GLU A 1 59  ? -6.476  -0.533  41.018  1.00 25.57 ? 94  GLU A CG  1 
ATOM   446  C  CD  . GLU A 1 59  ? -7.485  -1.494  40.429  1.00 32.16 ? 94  GLU A CD  1 
ATOM   447  O  OE1 . GLU A 1 59  ? -8.567  -1.017  40.001  1.00 31.68 ? 94  GLU A OE1 1 
ATOM   448  O  OE2 . GLU A 1 59  ? -7.194  -2.718  40.378  1.00 27.98 ? 94  GLU A OE2 1 
ATOM   449  N  N   . THR A 1 60  ? -3.769  1.425   42.509  1.00 25.04 ? 95  THR A N   1 
ATOM   450  C  CA  . THR A 1 60  ? -2.414  1.795   42.096  1.00 23.84 ? 95  THR A CA  1 
ATOM   451  C  C   . THR A 1 60  ? -1.644  0.541   41.703  1.00 22.40 ? 95  THR A C   1 
ATOM   452  O  O   . THR A 1 60  ? -1.528  -0.395  42.504  1.00 22.51 ? 95  THR A O   1 
ATOM   453  C  CB  . THR A 1 60  ? -1.686  2.540   43.219  1.00 24.56 ? 95  THR A CB  1 
ATOM   454  O  OG1 . THR A 1 60  ? -2.470  3.659   43.666  1.00 26.07 ? 95  THR A OG1 1 
ATOM   455  C  CG2 . THR A 1 60  ? -0.291  3.000   42.758  1.00 23.53 ? 95  THR A CG2 1 
ATOM   456  N  N   . SER A 1 61  ? -1.123  0.505   40.472  1.00 21.16 ? 96  SER A N   1 
ATOM   457  C  CA  . SER A 1 61  ? -0.374  -0.722  40.199  1.00 19.93 ? 96  SER A CA  1 
ATOM   458  C  C   . SER A 1 61  ? 1.037   -0.680  40.808  1.00 19.50 ? 96  SER A C   1 
ATOM   459  O  O   . SER A 1 61  ? 1.532   0.360   41.241  1.00 20.01 ? 96  SER A O   1 
ATOM   460  C  CB  . SER A 1 61  ? -0.398  -1.086  38.700  1.00 30.06 ? 96  SER A CB  1 
ATOM   461  O  OG  . SER A 1 61  ? -0.463  -0.030  37.776  1.00 29.05 ? 96  SER A OG  1 
ATOM   462  N  N   . VAL A 1 62  ? 1.634   -1.874  40.931  1.00 18.72 ? 97  VAL A N   1 
ATOM   463  C  CA  . VAL A 1 62  ? 2.961   -2.089  41.521  1.00 18.35 ? 97  VAL A CA  1 
ATOM   464  C  C   . VAL A 1 62  ? 3.704   -2.949  40.525  1.00 21.21 ? 97  VAL A C   1 
ATOM   465  O  O   . VAL A 1 62  ? 3.272   -4.081  40.256  1.00 17.81 ? 97  VAL A O   1 
ATOM   466  C  CB  . VAL A 1 62  ? 2.875   -2.816  42.878  1.00 19.08 ? 97  VAL A CB  1 
ATOM   467  C  CG1 . VAL A 1 62  ? 4.318   -3.148  43.437  1.00 18.70 ? 97  VAL A CG1 1 
ATOM   468  C  CG2 . VAL A 1 62  ? 1.984   -2.027  43.886  1.00 22.42 ? 97  VAL A CG2 1 
ATOM   469  N  N   . THR A 1 63  ? 4.794   -2.423  39.952  1.00 20.69 ? 98  THR A N   1 
ATOM   470  C  CA  . THR A 1 63  ? 5.437   -3.058  38.802  1.00 14.83 ? 98  THR A CA  1 
ATOM   471  C  C   . THR A 1 63  ? 6.938   -3.224  39.038  1.00 16.51 ? 98  THR A C   1 
ATOM   472  O  O   . THR A 1 63  ? 7.573   -2.360  39.653  1.00 16.04 ? 98  THR A O   1 
ATOM   473  C  CB  . THR A 1 63  ? 5.185   -2.215  37.538  1.00 18.23 ? 98  THR A CB  1 
ATOM   474  O  OG1 . THR A 1 63  ? 3.780   -1.938  37.386  1.00 13.98 ? 98  THR A OG1 1 
ATOM   475  C  CG2 . THR A 1 63  ? 5.679   -2.899  36.286  1.00 16.36 ? 98  THR A CG2 1 
ATOM   476  N  N   . GLY A 1 64  ? 7.496   -4.347  38.569  1.00 17.07 ? 99  GLY A N   1 
ATOM   477  C  CA  . GLY A 1 64  ? 8.943   -4.519  38.480  1.00 18.32 ? 99  GLY A CA  1 
ATOM   478  C  C   . GLY A 1 64  ? 9.354   -4.633  37.020  1.00 17.85 ? 99  GLY A C   1 
ATOM   479  O  O   . GLY A 1 64  ? 8.493   -4.863  36.183  1.00 13.13 ? 99  GLY A O   1 
ATOM   480  N  N   . TYR A 1 65  ? 10.631  -4.469  36.675  1.00 16.97 ? 100 TYR A N   1 
ATOM   481  C  CA  . TYR A 1 65  ? 11.017  -4.474  35.259  1.00 16.01 ? 100 TYR A CA  1 
ATOM   482  C  C   . TYR A 1 65  ? 12.169  -5.424  35.030  1.00 18.03 ? 100 TYR A C   1 
ATOM   483  O  O   . TYR A 1 65  ? 13.216  -5.274  35.648  1.00 17.37 ? 100 TYR A O   1 
ATOM   484  C  CB  . TYR A 1 65  ? 11.388  -3.061  34.781  1.00 13.30 ? 100 TYR A CB  1 
ATOM   485  C  CG  . TYR A 1 65  ? 10.170  -2.156  34.865  1.00 17.10 ? 100 TYR A CG  1 
ATOM   486  C  CD1 . TYR A 1 65  ? 9.290   -2.049  33.787  1.00 17.10 ? 100 TYR A CD1 1 
ATOM   487  C  CD2 . TYR A 1 65  ? 9.907   -1.436  36.008  1.00 15.94 ? 100 TYR A CD2 1 
ATOM   488  C  CE1 . TYR A 1 65  ? 8.172   -1.250  33.845  1.00 15.50 ? 100 TYR A CE1 1 
ATOM   489  C  CE2 . TYR A 1 65  ? 8.752   -0.616  36.099  1.00 16.99 ? 100 TYR A CE2 1 
ATOM   490  C  CZ  . TYR A 1 65  ? 7.919   -0.534  35.010  1.00 17.34 ? 100 TYR A CZ  1 
ATOM   491  O  OH  . TYR A 1 65  ? 6.804   0.247   35.075  1.00 12.77 ? 100 TYR A OH  1 
ATOM   492  N  N   . LEU A 1 66  ? 11.988  -6.360  34.104  1.00 14.96 ? 101 LEU A N   1 
ATOM   493  C  CA  . LEU A 1 66  ? 12.988  -7.353  33.736  1.00 19.65 ? 101 LEU A CA  1 
ATOM   494  C  C   . LEU A 1 66  ? 13.758  -6.873  32.507  1.00 21.70 ? 101 LEU A C   1 
ATOM   495  O  O   . LEU A 1 66  ? 13.164  -6.365  31.545  1.00 18.06 ? 101 LEU A O   1 
ATOM   496  C  CB  . LEU A 1 66  ? 12.303  -8.693  33.478  1.00 16.87 ? 101 LEU A CB  1 
ATOM   497  C  CG  . LEU A 1 66  ? 13.144  -9.993  33.411  1.00 21.74 ? 101 LEU A CG  1 
ATOM   498  C  CD1 . LEU A 1 66  ? 13.759  -10.408 34.771  1.00 25.71 ? 101 LEU A CD1 1 
ATOM   499  C  CD2 . LEU A 1 66  ? 12.243  -11.093 32.957  1.00 14.32 ? 101 LEU A CD2 1 
ATOM   500  N  N   . VAL A 1 67  ? 15.078  -7.019  32.545  1.00 17.32 ? 102 VAL A N   1 
ATOM   501  C  CA  . VAL A 1 67  ? 15.946  -6.610  31.455  1.00 17.45 ? 102 VAL A CA  1 
ATOM   502  C  C   . VAL A 1 67  ? 16.771  -7.827  31.091  1.00 17.98 ? 102 VAL A C   1 
ATOM   503  O  O   . VAL A 1 67  ? 17.570  -8.308  31.906  1.00 19.76 ? 102 VAL A O   1 
ATOM   504  C  CB  . VAL A 1 67  ? 16.859  -5.426  31.831  1.00 14.67 ? 102 VAL A CB  1 
ATOM   505  C  CG1 . VAL A 1 67  ? 17.713  -5.014  30.639  1.00 18.30 ? 102 VAL A CG1 1 
ATOM   506  C  CG2 . VAL A 1 67  ? 16.050  -4.213  32.383  1.00 18.94 ? 102 VAL A CG2 1 
ATOM   507  N  N   . ASN A 1 68  ? 16.580  -8.329  29.882  1.00 16.82 ? 103 ASN A N   1 
ATOM   508  C  CA  . ASN A 1 68  ? 17.415  -9.402  29.356  1.00 20.54 ? 103 ASN A CA  1 
ATOM   509  C  C   . ASN A 1 68  ? 18.314  -8.734  28.328  1.00 23.29 ? 103 ASN A C   1 
ATOM   510  O  O   . ASN A 1 68  ? 17.869  -8.395  27.224  1.00 23.73 ? 103 ASN A O   1 
ATOM   511  C  CB  . ASN A 1 68  ? 16.571  -10.533 28.757  1.00 26.30 ? 103 ASN A CB  1 
ATOM   512  C  CG  . ASN A 1 68  ? 17.406  -11.746 28.400  1.00 24.61 ? 103 ASN A CG  1 
ATOM   513  O  OD1 . ASN A 1 68  ? 18.572  -11.612 28.094  1.00 23.61 ? 103 ASN A OD1 1 
ATOM   514  N  ND2 . ASN A 1 68  ? 16.797  -12.926 28.404  1.00 23.72 ? 103 ASN A ND2 1 
ATOM   515  N  N   . THR A 1 69  ? 19.578  -8.512  28.703  1.00 24.12 ? 104 THR A N   1 
ATOM   516  C  CA  . THR A 1 69  ? 20.517  -7.861  27.797  1.00 26.14 ? 104 THR A CA  1 
ATOM   517  C  C   . THR A 1 69  ? 21.030  -8.802  26.720  1.00 25.78 ? 104 THR A C   1 
ATOM   518  O  O   . THR A 1 69  ? 21.758  -8.355  25.835  1.00 27.14 ? 104 THR A O   1 
ATOM   519  C  CB  . THR A 1 69  ? 21.716  -7.281  28.566  1.00 28.74 ? 104 THR A CB  1 
ATOM   520  O  OG1 . THR A 1 69  ? 22.546  -8.361  29.019  1.00 26.65 ? 104 THR A OG1 1 
ATOM   521  C  CG2 . THR A 1 69  ? 21.243  -6.454  29.768  1.00 23.03 ? 104 THR A CG2 1 
ATOM   522  N  N   . GLY A 1 70  ? 20.628  -10.078 26.761  1.00 27.50 ? 105 GLY A N   1 
ATOM   523  C  CA  . GLY A 1 70  ? 21.151  -11.106 25.902  1.00 26.86 ? 105 GLY A CA  1 
ATOM   524  C  C   . GLY A 1 70  ? 22.274  -11.888 26.531  1.00 30.07 ? 105 GLY A C   1 
ATOM   525  O  O   . GLY A 1 70  ? 22.524  -13.023 26.129  1.00 32.20 ? 105 GLY A O   1 
ATOM   526  N  N   . SER A 1 71  ? 22.890  -11.320 27.562  1.00 26.94 ? 106 SER A N   1 
ATOM   527  C  CA  . SER A 1 71  ? 24.011  -11.895 28.285  1.00 34.48 ? 106 SER A CA  1 
ATOM   528  C  C   . SER A 1 71  ? 23.740  -11.988 29.773  1.00 29.50 ? 106 SER A C   1 
ATOM   529  O  O   . SER A 1 71  ? 24.372  -12.808 30.449  1.00 27.89 ? 106 SER A O   1 
ATOM   530  C  CB  . SER A 1 71  ? 25.267  -11.034 28.079  1.00 35.00 ? 106 SER A CB  1 
ATOM   531  O  OG  . SER A 1 71  ? 25.882  -11.306 26.838  1.00 39.53 ? 106 SER A OG  1 
ATOM   532  N  N   . LYS A 1 72  ? 22.846  -11.161 30.306  1.00 23.98 ? 107 LYS A N   1 
ATOM   533  C  CA  . LYS A 1 72  ? 22.473  -11.161 31.710  1.00 26.01 ? 107 LYS A CA  1 
ATOM   534  C  C   . LYS A 1 72  ? 20.972  -10.964 31.814  1.00 26.20 ? 107 LYS A C   1 
ATOM   535  O  O   . LYS A 1 72  ? 20.354  -10.336 30.953  1.00 23.89 ? 107 LYS A O   1 
ATOM   536  C  CB  . LYS A 1 72  ? 23.183  -10.059 32.517  1.00 24.12 ? 107 LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 72  ? 24.691  -10.242 32.637  1.00 31.29 ? 107 LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 72  ? 25.015  -11.444 33.574  1.00 34.81 ? 107 LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 72  ? 26.522  -11.710 33.738  1.00 39.96 ? 107 LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 72  ? 27.203  -10.648 34.522  1.00 44.60 ? 107 LYS A NZ  1 
ATOM   541  N  N   . LEU A 1 73  ? 20.402  -11.514 32.877  1.00 23.03 ? 108 LEU A N   1 
ATOM   542  C  CA  . LEU A 1 73  ? 18.996  -11.357 33.212  1.00 17.86 ? 108 LEU A CA  1 
ATOM   543  C  C   . LEU A 1 73  ? 18.937  -10.582 34.524  1.00 22.02 ? 108 LEU A C   1 
ATOM   544  O  O   . LEU A 1 73  ? 19.371  -11.089 35.565  1.00 22.49 ? 108 LEU A O   1 
ATOM   545  C  CB  . LEU A 1 73  ? 18.309  -12.727 33.303  1.00 22.03 ? 108 LEU A CB  1 
ATOM   546  C  CG  . LEU A 1 73  ? 16.788  -12.581 33.379  1.00 20.25 ? 108 LEU A CG  1 
ATOM   547  C  CD1 . LEU A 1 73  ? 16.208  -11.971 32.090  1.00 24.63 ? 108 LEU A CD1 1 
ATOM   548  C  CD2 . LEU A 1 73  ? 16.128  -13.935 33.695  1.00 21.04 ? 108 LEU A CD2 1 
ATOM   549  N  N   . VAL A 1 74  ? 18.441  -9.344  34.456  1.00 21.86 ? 109 VAL A N   1 
ATOM   550  C  CA  . VAL A 1 74  ? 18.412  -8.384  35.565  1.00 21.31 ? 109 VAL A CA  1 
ATOM   551  C  C   . VAL A 1 74  ? 16.976  -7.989  35.864  1.00 21.91 ? 109 VAL A C   1 
ATOM   552  O  O   . VAL A 1 74  ? 16.220  -7.659  34.952  1.00 16.67 ? 109 VAL A O   1 
ATOM   553  C  CB  . VAL A 1 74  ? 19.242  -7.113  35.269  1.00 20.19 ? 109 VAL A CB  1 
ATOM   554  C  CG1 . VAL A 1 74  ? 19.158  -6.155  36.463  1.00 18.03 ? 109 VAL A CG1 1 
ATOM   555  C  CG2 . VAL A 1 74  ? 20.707  -7.441  35.033  1.00 19.53 ? 109 VAL A CG2 1 
ATOM   556  N  N   . LEU A 1 75  ? 16.614  -7.975  37.144  1.00 21.88 ? 110 LEU A N   1 
ATOM   557  C  CA  . LEU A 1 75  ? 15.283  -7.595  37.572  1.00 16.18 ? 110 LEU A CA  1 
ATOM   558  C  C   . LEU A 1 75  ? 15.415  -6.329  38.414  1.00 19.30 ? 110 LEU A C   1 
ATOM   559  O  O   . LEU A 1 75  ? 16.261  -6.249  39.309  1.00 17.33 ? 110 LEU A O   1 
ATOM   560  C  CB  . LEU A 1 75  ? 14.607  -8.711  38.375  1.00 19.14 ? 110 LEU A CB  1 
ATOM   561  C  CG  . LEU A 1 75  ? 13.235  -8.342  38.964  1.00 19.17 ? 110 LEU A CG  1 
ATOM   562  C  CD1 . LEU A 1 75  ? 12.258  -8.043  37.828  1.00 21.91 ? 110 LEU A CD1 1 
ATOM   563  C  CD2 . LEU A 1 75  ? 12.682  -9.379  39.898  1.00 20.02 ? 110 LEU A CD2 1 
ATOM   564  N  N   . VAL A 1 76  ? 14.602  -5.332  38.117  1.00 19.60 ? 111 VAL A N   1 
ATOM   565  C  CA  . VAL A 1 76  ? 14.639  -4.070  38.850  1.00 14.01 ? 111 VAL A CA  1 
ATOM   566  C  C   . VAL A 1 76  ? 13.354  -4.000  39.661  1.00 19.41 ? 111 VAL A C   1 
ATOM   567  O  O   . VAL A 1 76  ? 12.269  -3.828  39.089  1.00 19.27 ? 111 VAL A O   1 
ATOM   568  C  CB  . VAL A 1 76  ? 14.775  -2.878  37.898  1.00 19.15 ? 111 VAL A CB  1 
ATOM   569  C  CG1 . VAL A 1 76  ? 14.838  -1.571  38.664  1.00 13.55 ? 111 VAL A CG1 1 
ATOM   570  C  CG2 . VAL A 1 76  ? 16.000  -3.073  37.003  1.00 12.34 ? 111 VAL A CG2 1 
ATOM   571  N  N   . ASP A 1 77  ? 13.498  -4.098  40.993  1.00 17.13 ? 112 ASP A N   1 
ATOM   572  C  CA  . ASP A 1 77  ? 12.419  -4.160  41.972  1.00 17.70 ? 112 ASP A CA  1 
ATOM   573  C  C   . ASP A 1 77  ? 11.598  -5.435  41.827  1.00 17.11 ? 112 ASP A C   1 
ATOM   574  O  O   . ASP A 1 77  ? 11.561  -6.042  40.754  1.00 20.32 ? 112 ASP A O   1 
ATOM   575  C  CB  . ASP A 1 77  ? 11.535  -2.929  41.869  1.00 19.17 ? 112 ASP A CB  1 
ATOM   576  C  CG  . ASP A 1 77  ? 12.263  -1.660  42.276  1.00 22.63 ? 112 ASP A CG  1 
ATOM   577  O  OD1 . ASP A 1 77  ? 13.413  -1.718  42.807  1.00 19.52 ? 112 ASP A OD1 1 
ATOM   578  O  OD2 . ASP A 1 77  ? 11.674  -0.592  42.022  1.00 15.80 ? 112 ASP A OD2 1 
ATOM   579  N  N   . THR A 1 78  ? 10.977  -5.873  42.924  1.00 17.57 ? 113 THR A N   1 
ATOM   580  C  CA  . THR A 1 78  ? 10.473  -7.242  43.039  1.00 16.53 ? 113 THR A CA  1 
ATOM   581  C  C   . THR A 1 78  ? 9.040   -7.334  43.551  1.00 21.36 ? 113 THR A C   1 
ATOM   582  O  O   . THR A 1 78  ? 8.571   -8.453  43.842  1.00 17.20 ? 113 THR A O   1 
ATOM   583  C  CB  . THR A 1 78  ? 11.382  -8.074  43.962  1.00 21.95 ? 113 THR A CB  1 
ATOM   584  O  OG1 . THR A 1 78  ? 11.270  -7.603  45.314  1.00 21.07 ? 113 THR A OG1 1 
ATOM   585  C  CG2 . THR A 1 78  ? 12.833  -7.970  43.515  1.00 25.45 ? 113 THR A CG2 1 
ATOM   586  N  N   . GLY A 1 79  ? 8.320   -6.210  43.643  1.00 16.14 ? 114 GLY A N   1 
ATOM   587  C  CA  . GLY A 1 79  ? 6.997   -6.254  44.223  1.00 21.09 ? 114 GLY A CA  1 
ATOM   588  C  C   . GLY A 1 79  ? 7.081   -6.490  45.730  1.00 23.52 ? 114 GLY A C   1 
ATOM   589  O  O   . GLY A 1 79  ? 8.147   -6.447  46.347  1.00 22.33 ? 114 GLY A O   1 
ATOM   590  N  N   . ALA A 1 80  ? 5.916   -6.770  46.309  1.00 18.20 ? 115 ALA A N   1 
ATOM   591  C  CA  . ALA A 1 80  ? 5.715   -6.786  47.758  1.00 24.64 ? 115 ALA A CA  1 
ATOM   592  C  C   . ALA A 1 80  ? 5.634   -8.180  48.363  1.00 26.18 ? 115 ALA A C   1 
ATOM   593  O  O   . ALA A 1 80  ? 5.537   -8.296  49.593  1.00 21.50 ? 115 ALA A O   1 
ATOM   594  C  CB  . ALA A 1 80  ? 4.433   -6.016  48.110  1.00 24.61 ? 115 ALA A CB  1 
ATOM   595  N  N   . ALA A 1 81  ? 5.682   -9.236  47.541  1.00 26.07 ? 116 ALA A N   1 
ATOM   596  C  CA  . ALA A 1 81  ? 5.282   -10.582 47.963  1.00 22.88 ? 116 ALA A CA  1 
ATOM   597  C  C   . ALA A 1 81  ? 4.066   -10.500 48.873  1.00 31.34 ? 116 ALA A C   1 
ATOM   598  O  O   . ALA A 1 81  ? 3.032   -9.954  48.479  1.00 32.35 ? 116 ALA A O   1 
ATOM   599  C  CB  . ALA A 1 81  ? 6.424   -11.325 48.649  1.00 27.30 ? 116 ALA A CB  1 
ATOM   600  N  N   . GLY A 1 82  ? 4.181   -11.013 50.097  1.00 31.05 ? 117 GLY A N   1 
ATOM   601  C  CA  . GLY A 1 82  ? 3.087   -10.937 51.045  1.00 34.13 ? 117 GLY A CA  1 
ATOM   602  C  C   . GLY A 1 82  ? 3.186   -9.809  52.059  1.00 33.22 ? 117 GLY A C   1 
ATOM   603  O  O   . GLY A 1 82  ? 2.468   -9.832  53.055  1.00 45.25 ? 117 GLY A O   1 
ATOM   604  N  N   . LEU A 1 83  ? 4.043   -8.809  51.835  1.00 34.74 ? 118 LEU A N   1 
ATOM   605  C  CA  . LEU A 1 83  ? 4.219   -7.759  52.843  1.00 34.02 ? 118 LEU A CA  1 
ATOM   606  C  C   . LEU A 1 83  ? 3.137   -6.687  52.827  1.00 35.96 ? 118 LEU A C   1 
ATOM   607  O  O   . LEU A 1 83  ? 2.996   -5.969  53.823  1.00 33.35 ? 118 LEU A O   1 
ATOM   608  C  CB  . LEU A 1 83  ? 5.564   -7.064  52.681  1.00 24.15 ? 118 LEU A CB  1 
ATOM   609  C  CG  . LEU A 1 83  ? 6.770   -8.006  52.671  1.00 36.44 ? 118 LEU A CG  1 
ATOM   610  C  CD1 . LEU A 1 83  ? 8.076   -7.217  52.679  1.00 29.54 ? 118 LEU A CD1 1 
ATOM   611  C  CD2 . LEU A 1 83  ? 6.709   -8.918  53.857  1.00 35.80 ? 118 LEU A CD2 1 
ATOM   612  N  N   . PHE A 1 84  ? 2.359   -6.570  51.756  1.00 35.43 ? 119 PHE A N   1 
ATOM   613  C  CA  . PHE A 1 84  ? 1.483   -5.414  51.619  1.00 42.88 ? 119 PHE A CA  1 
ATOM   614  C  C   . PHE A 1 84  ? 0.095   -5.846  51.170  1.00 39.23 ? 119 PHE A C   1 
ATOM   615  O  O   . PHE A 1 84  ? -0.525  -5.213  50.306  1.00 39.90 ? 119 PHE A O   1 
ATOM   616  C  CB  . PHE A 1 84  ? 2.090   -4.387  50.655  1.00 42.39 ? 119 PHE A CB  1 
ATOM   617  C  CG  . PHE A 1 84  ? 1.671   -2.980  50.934  1.00 48.39 ? 119 PHE A CG  1 
ATOM   618  C  CD1 . PHE A 1 84  ? 0.476   -2.478  50.433  1.00 51.34 ? 119 PHE A CD1 1 
ATOM   619  C  CD2 . PHE A 1 84  ? 2.479   -2.148  51.697  1.00 54.31 ? 119 PHE A CD2 1 
ATOM   620  C  CE1 . PHE A 1 84  ? 0.080   -1.172  50.701  1.00 59.79 ? 119 PHE A CE1 1 
ATOM   621  C  CE2 . PHE A 1 84  ? 2.091   -0.842  51.974  1.00 58.48 ? 119 PHE A CE2 1 
ATOM   622  C  CZ  . PHE A 1 84  ? 0.887   -0.351  51.470  1.00 60.33 ? 119 PHE A CZ  1 
ATOM   623  N  N   . GLY A 1 85  ? -0.403  -6.946  51.742  1.00 35.51 ? 120 GLY A N   1 
ATOM   624  C  CA  . GLY A 1 85  ? -1.785  -7.331  51.575  1.00 33.82 ? 120 GLY A CA  1 
ATOM   625  C  C   . GLY A 1 85  ? -1.998  -8.396  50.521  1.00 45.16 ? 120 GLY A C   1 
ATOM   626  O  O   . GLY A 1 85  ? -1.087  -8.738  49.762  1.00 42.40 ? 120 GLY A O   1 
ATOM   627  N  N   . PRO A 1 86  ? -3.227  -8.922  50.429  1.00 39.30 ? 121 PRO A N   1 
ATOM   628  C  CA  . PRO A 1 86  ? -3.474  -10.053 49.525  1.00 38.48 ? 121 PRO A CA  1 
ATOM   629  C  C   . PRO A 1 86  ? -3.613  -9.702  48.046  1.00 38.26 ? 121 PRO A C   1 
ATOM   630  O  O   . PRO A 1 86  ? -3.659  -10.635 47.228  1.00 42.13 ? 121 PRO A O   1 
ATOM   631  C  CB  . PRO A 1 86  ? -4.776  -10.662 50.080  1.00 43.54 ? 121 PRO A CB  1 
ATOM   632  C  CG  . PRO A 1 86  ? -5.439  -9.558  50.900  1.00 42.96 ? 121 PRO A CG  1 
ATOM   633  C  CD  . PRO A 1 86  ? -4.486  -8.367  50.954  1.00 43.89 ? 121 PRO A CD  1 
ATOM   634  N  N   . THR A 1 87  ? -3.659  -8.424  47.655  1.00 35.47 ? 122 THR A N   1 
ATOM   635  C  CA  . THR A 1 87  ? -3.761  -8.105  46.232  1.00 33.12 ? 122 THR A CA  1 
ATOM   636  C  C   . THR A 1 87  ? -2.403  -7.981  45.552  1.00 32.81 ? 122 THR A C   1 
ATOM   637  O  O   . THR A 1 87  ? -2.362  -7.789  44.335  1.00 28.94 ? 122 THR A O   1 
ATOM   638  C  CB  . THR A 1 87  ? -4.487  -6.780  45.977  1.00 35.87 ? 122 THR A CB  1 
ATOM   639  O  OG1 . THR A 1 87  ? -3.827  -5.713  46.682  1.00 29.44 ? 122 THR A OG1 1 
ATOM   640  C  CG2 . THR A 1 87  ? -5.921  -6.876  46.446  1.00 40.00 ? 122 THR A CG2 1 
ATOM   641  N  N   . LEU A 1 88  ? -1.297  -8.045  46.293  1.00 32.05 ? 123 LEU A N   1 
ATOM   642  C  CA  . LEU A 1 88  ? 0.018   -7.904  45.685  1.00 25.87 ? 123 LEU A CA  1 
ATOM   643  C  C   . LEU A 1 88  ? 0.746   -9.242  45.762  1.00 28.42 ? 123 LEU A C   1 
ATOM   644  O  O   . LEU A 1 88  ? 0.200   -10.248 46.213  1.00 34.22 ? 123 LEU A O   1 
ATOM   645  C  CB  . LEU A 1 88  ? 0.810   -6.790  46.374  1.00 25.76 ? 123 LEU A CB  1 
ATOM   646  C  CG  . LEU A 1 88  ? 0.170   -5.408  46.208  1.00 27.42 ? 123 LEU A CG  1 
ATOM   647  C  CD1 . LEU A 1 88  ? 1.045   -4.288  46.833  1.00 33.76 ? 123 LEU A CD1 1 
ATOM   648  C  CD2 . LEU A 1 88  ? -0.203  -5.111  44.737  1.00 25.72 ? 123 LEU A CD2 1 
ATOM   649  N  N   . GLY A 1 89  ? 1.996   -9.260  45.322  1.00 23.64 ? 124 GLY A N   1 
ATOM   650  C  CA  . GLY A 1 89  ? 2.742   -10.505 45.298  1.00 26.36 ? 124 GLY A CA  1 
ATOM   651  C  C   . GLY A 1 89  ? 2.600   -11.311 44.028  1.00 30.97 ? 124 GLY A C   1 
ATOM   652  O  O   . GLY A 1 89  ? 2.990   -12.488 44.011  1.00 26.16 ? 124 GLY A O   1 
ATOM   653  N  N   . ARG A 1 90  ? 2.088   -10.711 42.952  1.00 25.82 ? 125 ARG A N   1 
ATOM   654  C  CA  . ARG A 1 90  ? 1.888   -11.452 41.709  1.00 27.97 ? 125 ARG A CA  1 
ATOM   655  C  C   . ARG A 1 90  ? 3.169   -11.582 40.890  1.00 23.35 ? 125 ARG A C   1 
ATOM   656  O  O   . ARG A 1 90  ? 3.182   -12.322 39.899  1.00 23.54 ? 125 ARG A O   1 
ATOM   657  C  CB  . ARG A 1 90  ? 0.823   -10.762 40.856  1.00 22.14 ? 125 ARG A CB  1 
ATOM   658  C  CG  . ARG A 1 90  ? -0.615  -11.188 41.101  1.00 30.72 ? 125 ARG A CG  1 
ATOM   659  C  CD  . ARG A 1 90  ? -0.853  -11.546 42.541  1.00 32.64 ? 125 ARG A CD  1 
ATOM   660  N  NE  . ARG A 1 90  ? -2.250  -11.369 42.918  1.00 41.32 ? 125 ARG A NE  1 
ATOM   661  C  CZ  . ARG A 1 90  ? -2.669  -11.223 44.168  1.00 36.77 ? 125 ARG A CZ  1 
ATOM   662  N  NH1 . ARG A 1 90  ? -1.825  -11.229 45.185  1.00 37.16 ? 125 ARG A NH1 1 
ATOM   663  N  NH2 . ARG A 1 90  ? -3.967  -11.053 44.400  1.00 42.22 ? 125 ARG A NH2 1 
ATOM   664  N  N   . LEU A 1 91  ? 4.247   -10.898 41.280  1.00 20.62 ? 126 LEU A N   1 
ATOM   665  C  CA  . LEU A 1 91  ? 5.408   -10.778 40.391  1.00 21.39 ? 126 LEU A CA  1 
ATOM   666  C  C   . LEU A 1 91  ? 6.051   -12.128 40.095  1.00 24.08 ? 126 LEU A C   1 
ATOM   667  O  O   . LEU A 1 91  ? 6.436   -12.389 38.954  1.00 23.70 ? 126 LEU A O   1 
ATOM   668  C  CB  . LEU A 1 91  ? 6.433   -9.781  40.973  1.00 19.85 ? 126 LEU A CB  1 
ATOM   669  C  CG  . LEU A 1 91  ? 7.614   -9.486  40.062  1.00 17.61 ? 126 LEU A CG  1 
ATOM   670  C  CD1 . LEU A 1 91  ? 8.073   -8.010  40.012  1.00 16.37 ? 126 LEU A CD1 1 
ATOM   671  C  CD2 . LEU A 1 91  ? 8.768   -10.367 40.476  1.00 20.72 ? 126 LEU A CD2 1 
ATOM   672  N  N   . ALA A 1 92  ? 6.178   -12.999 41.102  1.00 23.67 ? 127 ALA A N   1 
ATOM   673  C  CA  . ALA A 1 92  ? 6.793   -14.313 40.892  1.00 25.48 ? 127 ALA A CA  1 
ATOM   674  C  C   . ALA A 1 92  ? 6.101   -15.081 39.771  1.00 25.89 ? 127 ALA A C   1 
ATOM   675  O  O   . ALA A 1 92  ? 6.740   -15.551 38.806  1.00 25.32 ? 127 ALA A O   1 
ATOM   676  C  CB  . ALA A 1 92  ? 6.731   -15.115 42.196  1.00 22.87 ? 127 ALA A CB  1 
ATOM   677  N  N   . ALA A 1 93  ? 4.777   -15.204 39.873  1.00 28.57 ? 128 ALA A N   1 
ATOM   678  C  CA  . ALA A 1 93  ? 4.045   -15.987 38.890  1.00 28.38 ? 128 ALA A CA  1 
ATOM   679  C  C   . ALA A 1 93  ? 4.114   -15.328 37.525  1.00 28.65 ? 128 ALA A C   1 
ATOM   680  O  O   . ALA A 1 93  ? 4.162   -16.024 36.502  1.00 23.07 ? 128 ALA A O   1 
ATOM   681  C  CB  . ALA A 1 93  ? 2.599   -16.175 39.334  1.00 30.61 ? 128 ALA A CB  1 
ATOM   682  N  N   . ASN A 1 94  ? 4.115   -13.979 37.485  1.00 20.71 ? 129 ASN A N   1 
ATOM   683  C  CA  . ASN A 1 94  ? 4.161   -13.282 36.201  1.00 23.46 ? 129 ASN A CA  1 
ATOM   684  C  C   . ASN A 1 94  ? 5.547   -13.317 35.559  1.00 20.39 ? 129 ASN A C   1 
ATOM   685  O  O   . ASN A 1 94  ? 5.652   -13.293 34.332  1.00 22.63 ? 129 ASN A O   1 
ATOM   686  C  CB  . ASN A 1 94  ? 3.659   -11.834 36.349  1.00 19.95 ? 129 ASN A CB  1 
ATOM   687  C  CG  . ASN A 1 94  ? 2.152   -11.783 36.536  1.00 22.43 ? 129 ASN A CG  1 
ATOM   688  O  OD1 . ASN A 1 94  ? 1.430   -12.639 35.976  1.00 24.92 ? 129 ASN A OD1 1 
ATOM   689  N  ND2 . ASN A 1 94  ? 1.654   -10.785 37.278  1.00 19.10 ? 129 ASN A ND2 1 
ATOM   690  N  N   . LEU A 1 95  ? 6.614   -13.355 36.352  1.00 22.30 ? 130 LEU A N   1 
ATOM   691  C  CA  . LEU A 1 95  ? 7.920   -13.699 35.798  1.00 21.32 ? 130 LEU A CA  1 
ATOM   692  C  C   . LEU A 1 95  ? 7.852   -15.067 35.128  1.00 26.18 ? 130 LEU A C   1 
ATOM   693  O  O   . LEU A 1 95  ? 8.388   -15.281 34.032  1.00 23.13 ? 130 LEU A O   1 
ATOM   694  C  CB  . LEU A 1 95  ? 8.961   -13.723 36.920  1.00 21.13 ? 130 LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 95  ? 10.400  -14.149 36.642  1.00 25.56 ? 130 LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 95  ? 11.015  -13.307 35.534  1.00 28.15 ? 130 LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 95  ? 11.235  -14.072 37.911  1.00 30.29 ? 130 LEU A CD2 1 
ATOM   698  N  N   . LYS A 1 96  ? 7.170   -16.003 35.760  1.00 22.27 ? 131 LYS A N   1 
ATOM   699  C  CA  . LYS A 1 96  ? 7.080   -17.321 35.110  1.00 23.66 ? 131 LYS A CA  1 
ATOM   700  C  C   . LYS A 1 96  ? 6.232   -17.268 33.833  1.00 29.18 ? 131 LYS A C   1 
ATOM   701  O  O   . LYS A 1 96  ? 6.611   -17.852 32.805  1.00 26.41 ? 131 LYS A O   1 
ATOM   702  C  CB  . LYS A 1 96  ? 6.542   -18.357 36.080  1.00 29.68 ? 131 LYS A CB  1 
ATOM   703  C  CG  . LYS A 1 96  ? 7.517   -18.675 37.189  1.00 31.20 ? 131 LYS A CG  1 
ATOM   704  C  CD  . LYS A 1 96  ? 6.869   -19.653 38.172  1.00 31.26 ? 131 LYS A CD  1 
ATOM   705  C  CE  . LYS A 1 96  ? 7.860   -20.101 39.231  1.00 35.49 ? 131 LYS A CE  1 
ATOM   706  N  NZ  . LYS A 1 96  ? 7.871   -19.081 40.315  1.00 41.68 ? 131 LYS A NZ  1 
ATOM   707  N  N   . ALA A 1 97  ? 5.089   -16.563 33.873  1.00 24.73 ? 132 ALA A N   1 
ATOM   708  C  CA  . ALA A 1 97  ? 4.277   -16.384 32.675  1.00 24.18 ? 132 ALA A CA  1 
ATOM   709  C  C   . ALA A 1 97  ? 5.081   -15.746 31.548  1.00 23.35 ? 132 ALA A C   1 
ATOM   710  O  O   . ALA A 1 97  ? 4.857   -16.048 30.371  1.00 24.39 ? 132 ALA A O   1 
ATOM   711  C  CB  . ALA A 1 97  ? 3.044   -15.532 32.999  1.00 28.62 ? 132 ALA A CB  1 
ATOM   712  N  N   . ALA A 1 98  ? 6.041   -14.888 31.894  1.00 21.74 ? 133 ALA A N   1 
ATOM   713  C  CA  . ALA A 1 98  ? 6.885   -14.196 30.930  1.00 23.14 ? 133 ALA A CA  1 
ATOM   714  C  C   . ALA A 1 98  ? 7.946   -15.080 30.312  1.00 28.58 ? 133 ALA A C   1 
ATOM   715  O  O   . ALA A 1 98  ? 8.761   -14.576 29.530  1.00 24.98 ? 133 ALA A O   1 
ATOM   716  C  CB  . ALA A 1 98  ? 7.565   -13.000 31.596  1.00 19.36 ? 133 ALA A CB  1 
ATOM   717  N  N   . GLY A 1 99  ? 7.977   -16.360 30.648  1.00 24.77 ? 134 GLY A N   1 
ATOM   718  C  CA  . GLY A 1 99  ? 8.912   -17.287 30.035  1.00 25.20 ? 134 GLY A CA  1 
ATOM   719  C  C   . GLY A 1 99  ? 10.203  -17.512 30.788  1.00 25.82 ? 134 GLY A C   1 
ATOM   720  O  O   . GLY A 1 99  ? 11.060  -18.264 30.291  1.00 33.23 ? 134 GLY A O   1 
ATOM   721  N  N   . TYR A 1 100 ? 10.349  -16.960 31.994  1.00 24.77 ? 135 TYR A N   1 
ATOM   722  C  CA  . TYR A 1 100 ? 11.587  -17.093 32.748  1.00 33.58 ? 135 TYR A CA  1 
ATOM   723  C  C   . TYR A 1 100 ? 11.345  -17.797 34.075  1.00 35.04 ? 135 TYR A C   1 
ATOM   724  O  O   . TYR A 1 100 ? 10.238  -17.769 34.621  1.00 32.12 ? 135 TYR A O   1 
ATOM   725  C  CB  . TYR A 1 100 ? 12.208  -15.733 33.049  1.00 21.62 ? 135 TYR A CB  1 
ATOM   726  C  CG  . TYR A 1 100 ? 12.693  -15.026 31.825  1.00 27.53 ? 135 TYR A CG  1 
ATOM   727  C  CD1 . TYR A 1 100 ? 13.884  -15.398 31.201  1.00 28.44 ? 135 TYR A CD1 1 
ATOM   728  C  CD2 . TYR A 1 100 ? 11.946  -13.986 31.271  1.00 21.61 ? 135 TYR A CD2 1 
ATOM   729  C  CE1 . TYR A 1 100 ? 14.310  -14.750 30.058  1.00 26.54 ? 135 TYR A CE1 1 
ATOM   730  C  CE2 . TYR A 1 100 ? 12.364  -13.337 30.147  1.00 20.54 ? 135 TYR A CE2 1 
ATOM   731  C  CZ  . TYR A 1 100 ? 13.548  -13.700 29.555  1.00 22.05 ? 135 TYR A CZ  1 
ATOM   732  O  OH  . TYR A 1 100 ? 13.956  -13.051 28.424  1.00 24.64 ? 135 TYR A OH  1 
ATOM   733  N  N   . GLN A 1 101 ? 12.437  -18.382 34.626  1.00 30.12 ? 136 GLN A N   1 
ATOM   734  C  CA  . GLN A 1 101 ? 12.407  -18.871 35.988  1.00 31.29 ? 136 GLN A CA  1 
ATOM   735  C  C   . GLN A 1 101 ? 13.189  -17.941 36.927  1.00 34.02 ? 136 GLN A C   1 
ATOM   736  O  O   . GLN A 1 101 ? 14.147  -17.283 36.506  1.00 27.46 ? 136 GLN A O   1 
ATOM   737  C  CB  . GLN A 1 101 ? 13.014  -20.273 36.068  1.00 33.42 ? 136 GLN A CB  1 
ATOM   738  C  CG  . GLN A 1 101 ? 12.196  -21.342 35.361  1.00 36.79 ? 136 GLN A CG  1 
ATOM   739  C  CD  . GLN A 1 101 ? 10.801  -21.448 35.922  1.00 42.12 ? 136 GLN A CD  1 
ATOM   740  O  OE1 . GLN A 1 101 ? 10.607  -21.748 37.099  1.00 47.70 ? 136 GLN A OE1 1 
ATOM   741  N  NE2 . GLN A 1 101 ? 9.811   -21.242 35.062  1.00 44.64 ? 136 GLN A NE2 1 
ATOM   742  N  N   . PRO A 1 102 ? 12.829  -17.897 38.217  1.00 30.77 ? 137 PRO A N   1 
ATOM   743  C  CA  . PRO A 1 102 ? 13.615  -17.099 39.175  1.00 22.96 ? 137 PRO A CA  1 
ATOM   744  C  C   . PRO A 1 102 ? 15.080  -17.503 39.239  1.00 32.37 ? 137 PRO A C   1 
ATOM   745  O  O   . PRO A 1 102 ? 15.943  -16.649 39.487  1.00 29.80 ? 137 PRO A O   1 
ATOM   746  C  CB  . PRO A 1 102 ? 12.936  -17.398 40.517  1.00 29.66 ? 137 PRO A CB  1 
ATOM   747  C  CG  . PRO A 1 102 ? 11.621  -17.897 40.192  1.00 38.72 ? 137 PRO A CG  1 
ATOM   748  C  CD  . PRO A 1 102 ? 11.763  -18.649 38.898  1.00 31.99 ? 137 PRO A CD  1 
ATOM   749  N  N   . GLU A 1 103 ? 15.382  -18.797 39.054  1.00 28.54 ? 138 GLU A N   1 
ATOM   750  C  CA  . GLU A 1 103 ? 16.775  -19.229 39.072  1.00 34.86 ? 138 GLU A CA  1 
ATOM   751  C  C   . GLU A 1 103 ? 17.579  -18.582 37.957  1.00 31.84 ? 138 GLU A C   1 
ATOM   752  O  O   . GLU A 1 103 ? 18.813  -18.549 38.037  1.00 29.30 ? 138 GLU A O   1 
ATOM   753  C  CB  . GLU A 1 103 ? 16.870  -20.756 38.987  1.00 33.84 ? 138 GLU A CB  1 
ATOM   754  C  CG  . GLU A 1 103 ? 16.351  -21.431 40.218  1.00 37.25 ? 138 GLU A CG  1 
ATOM   755  C  CD  . GLU A 1 103 ? 14.853  -21.583 40.189  1.00 47.02 ? 138 GLU A CD  1 
ATOM   756  O  OE1 . GLU A 1 103 ? 14.254  -21.312 39.126  1.00 37.90 ? 138 GLU A OE1 1 
ATOM   757  O  OE2 . GLU A 1 103 ? 14.273  -21.968 41.226  1.00 58.56 ? 138 GLU A OE2 1 
ATOM   758  N  N   . GLN A 1 104 ? 16.912  -18.036 36.934  1.00 29.48 ? 139 GLN A N   1 
ATOM   759  C  CA  . GLN A 1 104 ? 17.658  -17.471 35.822  1.00 30.90 ? 139 GLN A CA  1 
ATOM   760  C  C   . GLN A 1 104 ? 18.131  -16.055 36.088  1.00 24.81 ? 139 GLN A C   1 
ATOM   761  O  O   . GLN A 1 104 ? 19.030  -15.583 35.385  1.00 25.39 ? 139 GLN A O   1 
ATOM   762  C  CB  . GLN A 1 104 ? 16.821  -17.511 34.543  1.00 24.92 ? 139 GLN A CB  1 
ATOM   763  C  CG  . GLN A 1 104 ? 16.568  -18.923 33.984  1.00 28.93 ? 139 GLN A CG  1 
ATOM   764  C  CD  . GLN A 1 104 ? 15.711  -18.887 32.716  1.00 36.95 ? 139 GLN A CD  1 
ATOM   765  O  OE1 . GLN A 1 104 ? 14.510  -18.604 32.770  1.00 27.24 ? 139 GLN A OE1 1 
ATOM   766  N  NE2 . GLN A 1 104 ? 16.333  -19.162 31.566  1.00 39.30 ? 139 GLN A NE2 1 
ATOM   767  N  N   . VAL A 1 105 ? 17.552  -15.377 37.080  1.00 25.72 ? 140 VAL A N   1 
ATOM   768  C  CA  . VAL A 1 105 ? 17.880  -13.977 37.348  1.00 22.91 ? 140 VAL A CA  1 
ATOM   769  C  C   . VAL A 1 105 ? 19.303  -13.884 37.894  1.00 22.95 ? 140 VAL A C   1 
ATOM   770  O  O   . VAL A 1 105 ? 19.632  -14.494 38.918  1.00 30.74 ? 140 VAL A O   1 
ATOM   771  C  CB  . VAL A 1 105 ? 16.864  -13.373 38.325  1.00 19.20 ? 140 VAL A CB  1 
ATOM   772  C  CG1 . VAL A 1 105 ? 17.288  -11.945 38.785  1.00 17.60 ? 140 VAL A CG1 1 
ATOM   773  C  CG2 . VAL A 1 105 ? 15.459  -13.405 37.725  1.00 24.83 ? 140 VAL A CG2 1 
ATOM   774  N  N   . ASP A 1 106 ? 20.159  -13.123 37.206  1.00 20.86 ? 141 ASP A N   1 
ATOM   775  C  CA  . ASP A 1 106 ? 21.568  -12.963 37.586  1.00 24.31 ? 141 ASP A CA  1 
ATOM   776  C  C   . ASP A 1 106 ? 21.773  -11.877 38.645  1.00 27.70 ? 141 ASP A C   1 
ATOM   777  O  O   . ASP A 1 106 ? 22.630  -12.020 39.531  1.00 21.48 ? 141 ASP A O   1 
ATOM   778  C  CB  . ASP A 1 106 ? 22.389  -12.601 36.345  1.00 29.41 ? 141 ASP A CB  1 
ATOM   779  C  CG  . ASP A 1 106 ? 22.417  -13.706 35.312  1.00 30.68 ? 141 ASP A CG  1 
ATOM   780  O  OD1 . ASP A 1 106 ? 22.757  -14.845 35.679  1.00 25.56 ? 141 ASP A OD1 1 
ATOM   781  O  OD2 . ASP A 1 106 ? 22.035  -13.451 34.137  1.00 28.37 ? 141 ASP A OD2 1 
ATOM   782  N  N   . GLU A 1 107 ? 21.050  -10.757 38.524  1.00 21.54 ? 142 GLU A N   1 
ATOM   783  C  CA  . GLU A 1 107 ? 21.192  -9.607  39.412  1.00 18.39 ? 142 GLU A CA  1 
ATOM   784  C  C   . GLU A 1 107 ? 19.825  -8.982  39.650  1.00 25.51 ? 142 GLU A C   1 
ATOM   785  O  O   . GLU A 1 107 ? 18.975  -8.948  38.752  1.00 22.90 ? 142 GLU A O   1 
ATOM   786  C  CB  . GLU A 1 107 ? 22.161  -8.543  38.834  1.00 25.18 ? 142 GLU A CB  1 
ATOM   787  C  CG  . GLU A 1 107 ? 23.435  -9.128  38.232  1.00 25.10 ? 142 GLU A CG  1 
ATOM   788  C  CD  . GLU A 1 107 ? 24.632  -8.202  38.276  1.00 30.64 ? 142 GLU A CD  1 
ATOM   789  O  OE1 . GLU A 1 107 ? 24.507  -6.987  38.538  1.00 21.78 ? 142 GLU A OE1 1 
ATOM   790  O  OE2 . GLU A 1 107 ? 25.735  -8.707  38.015  1.00 31.99 ? 142 GLU A OE2 1 
ATOM   791  N  N   . VAL A 1 108 ? 19.633  -8.472  40.869  1.00 18.88 ? 143 VAL A N   1 
ATOM   792  C  CA  . VAL A 1 108 ? 18.422  -7.762  41.252  1.00 16.56 ? 143 VAL A CA  1 
ATOM   793  C  C   . VAL A 1 108 ? 18.817  -6.354  41.673  1.00 23.82 ? 143 VAL A C   1 
ATOM   794  O  O   . VAL A 1 108 ? 19.626  -6.190  42.595  1.00 20.81 ? 143 VAL A O   1 
ATOM   795  C  CB  . VAL A 1 108 ? 17.672  -8.457  42.391  1.00 19.99 ? 143 VAL A CB  1 
ATOM   796  C  CG1 . VAL A 1 108 ? 16.485  -7.546  42.830  1.00 18.38 ? 143 VAL A CG1 1 
ATOM   797  C  CG2 . VAL A 1 108 ? 17.157  -9.787  41.944  1.00 16.84 ? 143 VAL A CG2 1 
ATOM   798  N  N   . TYR A 1 109 ? 18.231  -5.338  41.028  1.00 16.80 ? 144 TYR A N   1 
ATOM   799  C  CA  . TYR A 1 109 ? 18.530  -3.941  41.350  1.00 19.80 ? 144 TYR A CA  1 
ATOM   800  C  C   . TYR A 1 109 ? 17.318  -3.356  42.065  1.00 18.09 ? 144 TYR A C   1 
ATOM   801  O  O   . TYR A 1 109 ? 16.186  -3.520  41.599  1.00 16.29 ? 144 TYR A O   1 
ATOM   802  C  CB  . TYR A 1 109 ? 18.875  -3.123  40.089  1.00 19.86 ? 144 TYR A CB  1 
ATOM   803  C  CG  . TYR A 1 109 ? 20.112  -3.578  39.336  1.00 22.75 ? 144 TYR A CG  1 
ATOM   804  C  CD1 . TYR A 1 109 ? 21.006  -4.463  39.912  1.00 18.79 ? 144 TYR A CD1 1 
ATOM   805  C  CD2 . TYR A 1 109 ? 20.329  -3.209  38.014  1.00 20.66 ? 144 TYR A CD2 1 
ATOM   806  C  CE1 . TYR A 1 109 ? 22.120  -4.928  39.223  1.00 25.65 ? 144 TYR A CE1 1 
ATOM   807  C  CE2 . TYR A 1 109 ? 21.432  -3.691  37.308  1.00 18.62 ? 144 TYR A CE2 1 
ATOM   808  C  CZ  . TYR A 1 109 ? 22.322  -4.547  37.927  1.00 20.96 ? 144 TYR A CZ  1 
ATOM   809  O  OH  . TYR A 1 109 ? 23.423  -5.030  37.266  1.00 25.02 ? 144 TYR A OH  1 
ATOM   810  N  N   . LEU A 1 110 ? 17.549  -2.686  43.191  1.00 14.82 ? 145 LEU A N   1 
ATOM   811  C  CA  . LEU A 1 110 ? 16.460  -2.077  43.972  1.00 17.56 ? 145 LEU A CA  1 
ATOM   812  C  C   . LEU A 1 110 ? 16.483  -0.562  43.800  1.00 16.47 ? 145 LEU A C   1 
ATOM   813  O  O   . LEU A 1 110 ? 17.489  0.080   44.132  1.00 18.51 ? 145 LEU A O   1 
ATOM   814  C  CB  . LEU A 1 110 ? 16.618  -2.427  45.449  1.00 17.02 ? 145 LEU A CB  1 
ATOM   815  C  CG  . LEU A 1 110 ? 16.587  -3.938  45.711  1.00 15.79 ? 145 LEU A CG  1 
ATOM   816  C  CD1 . LEU A 1 110 ? 16.899  -4.223  47.183  1.00 14.91 ? 145 LEU A CD1 1 
ATOM   817  C  CD2 . LEU A 1 110 ? 15.228  -4.535  45.371  1.00 17.54 ? 145 LEU A CD2 1 
ATOM   818  N  N   . THR A 1 111 ? 15.375  0.017   43.298  1.00 14.98 ? 146 THR A N   1 
ATOM   819  C  CA  . THR A 1 111 ? 15.284  1.470   43.309  1.00 14.04 ? 146 THR A CA  1 
ATOM   820  C  C   . THR A 1 111 ? 15.309  1.980   44.743  1.00 14.61 ? 146 THR A C   1 
ATOM   821  O  O   . THR A 1 111 ? 15.977  2.982   45.036  1.00 18.67 ? 146 THR A O   1 
ATOM   822  C  CB  . THR A 1 111 ? 14.042  1.974   42.558  1.00 15.18 ? 146 THR A CB  1 
ATOM   823  O  OG1 . THR A 1 111 ? 12.871  1.475   43.180  1.00 15.12 ? 146 THR A OG1 1 
ATOM   824  C  CG2 . THR A 1 111 ? 14.114  1.511   41.057  1.00 13.53 ? 146 THR A CG2 1 
ATOM   825  N  N   . HIS A 1 112 ? 14.675  1.257   45.655  1.00 14.38 ? 147 HIS A N   1 
ATOM   826  C  CA  . HIS A 1 112 ? 14.664  1.587   47.076  1.00 15.41 ? 147 HIS A CA  1 
ATOM   827  C  C   . HIS A 1 112 ? 14.048  0.416   47.817  1.00 17.06 ? 147 HIS A C   1 
ATOM   828  O  O   . HIS A 1 112 ? 13.601  -0.554  47.198  1.00 18.42 ? 147 HIS A O   1 
ATOM   829  C  CB  . HIS A 1 112 ? 13.895  2.878   47.350  1.00 15.75 ? 147 HIS A CB  1 
ATOM   830  C  CG  . HIS A 1 112 ? 12.422  2.808   47.065  1.00 15.46 ? 147 HIS A CG  1 
ATOM   831  N  ND1 . HIS A 1 112 ? 11.916  2.519   45.817  1.00 14.75 ? 147 HIS A ND1 1 
ATOM   832  C  CD2 . HIS A 1 112 ? 11.352  3.145   47.834  1.00 19.79 ? 147 HIS A CD2 1 
ATOM   833  C  CE1 . HIS A 1 112 ? 10.598  2.637   45.842  1.00 15.45 ? 147 HIS A CE1 1 
ATOM   834  N  NE2 . HIS A 1 112 ? 10.232  3.011   47.056  1.00 18.07 ? 147 HIS A NE2 1 
ATOM   835  N  N   . MET A 1 113 ? 13.956  0.542   49.149  1.00 19.66 ? 148 MET A N   1 
ATOM   836  C  CA  . MET A 1 113 ? 13.702  -0.629  49.978  1.00 18.37 ? 148 MET A CA  1 
ATOM   837  C  C   . MET A 1 113 ? 12.313  -0.640  50.624  1.00 19.13 ? 148 MET A C   1 
ATOM   838  O  O   . MET A 1 113 ? 12.104  -1.355  51.614  1.00 17.46 ? 148 MET A O   1 
ATOM   839  C  CB  . MET A 1 113 ? 14.786  -0.697  51.034  1.00 19.90 ? 148 MET A CB  1 
ATOM   840  C  CG  . MET A 1 113 ? 16.038  -1.211  50.380  1.00 26.14 ? 148 MET A CG  1 
ATOM   841  S  SD  . MET A 1 113 ? 17.393  -1.568  51.459  1.00 24.03 ? 148 MET A SD  1 
ATOM   842  C  CE  . MET A 1 113 ? 18.675  -1.888  50.253  1.00 25.17 ? 148 MET A CE  1 
ATOM   843  N  N   . HIS A 1 114 ? 11.367  0.169   50.120  1.00 17.09 ? 149 HIS A N   1 
ATOM   844  C  CA  . HIS A 1 114 ? 9.992   0.083   50.619  1.00 20.06 ? 149 HIS A CA  1 
ATOM   845  C  C   . HIS A 1 114 ? 9.433   -1.319  50.336  1.00 19.96 ? 149 HIS A C   1 
ATOM   846  O  O   . HIS A 1 114 ? 9.928   -2.021  49.446  1.00 18.94 ? 149 HIS A O   1 
ATOM   847  C  CB  . HIS A 1 114 ? 9.116   1.141   49.950  1.00 21.88 ? 149 HIS A CB  1 
ATOM   848  C  CG  . HIS A 1 114 ? 9.165   2.496   50.602  1.00 25.82 ? 149 HIS A CG  1 
ATOM   849  N  ND1 . HIS A 1 114 ? 8.641   3.619   49.999  1.00 18.88 ? 149 HIS A ND1 1 
ATOM   850  C  CD2 . HIS A 1 114 ? 9.694   2.914   51.779  1.00 33.39 ? 149 HIS A CD2 1 
ATOM   851  C  CE1 . HIS A 1 114 ? 8.847   4.670   50.774  1.00 24.44 ? 149 HIS A CE1 1 
ATOM   852  N  NE2 . HIS A 1 114 ? 9.464   4.269   51.870  1.00 22.71 ? 149 HIS A NE2 1 
ATOM   853  N  N   . PRO A 1 115 ? 8.411   -1.757  51.091  1.00 23.69 ? 150 PRO A N   1 
ATOM   854  C  CA  . PRO A 1 115 ? 8.016   -3.180  51.053  1.00 20.83 ? 150 PRO A CA  1 
ATOM   855  C  C   . PRO A 1 115 ? 7.526   -3.675  49.707  1.00 23.48 ? 150 PRO A C   1 
ATOM   856  O  O   . PRO A 1 115 ? 7.715   -4.863  49.393  1.00 19.21 ? 150 PRO A O   1 
ATOM   857  C  CB  . PRO A 1 115 ? 6.897   -3.274  52.100  1.00 25.61 ? 150 PRO A CB  1 
ATOM   858  C  CG  . PRO A 1 115 ? 7.054   -2.113  52.959  1.00 35.11 ? 150 PRO A CG  1 
ATOM   859  C  CD  . PRO A 1 115 ? 7.613   -1.015  52.079  1.00 37.11 ? 150 PRO A CD  1 
ATOM   860  N  N   . ASP A 1 116 ? 6.877   -2.818  48.926  1.00 17.82 ? 151 ASP A N   1 
ATOM   861  C  CA  . ASP A 1 116 ? 6.316   -3.129  47.617  1.00 16.24 ? 151 ASP A CA  1 
ATOM   862  C  C   . ASP A 1 116 ? 7.358   -3.172  46.512  1.00 20.15 ? 151 ASP A C   1 
ATOM   863  O  O   . ASP A 1 116 ? 7.011   -3.300  45.323  1.00 16.12 ? 151 ASP A O   1 
ATOM   864  C  CB  . ASP A 1 116 ? 5.198   -2.118  47.289  1.00 23.00 ? 151 ASP A CB  1 
ATOM   865  C  CG  . ASP A 1 116 ? 5.618   -0.674  47.505  1.00 18.80 ? 151 ASP A CG  1 
ATOM   866  O  OD1 . ASP A 1 116 ? 6.031   -0.333  48.644  1.00 23.05 ? 151 ASP A OD1 1 
ATOM   867  O  OD2 . ASP A 1 116 ? 5.548   0.138   46.532  1.00 18.89 ? 151 ASP A OD2 1 
ATOM   868  N  N   . HIS A 1 117 ? 8.626   -3.070  46.888  1.00 14.73 ? 152 HIS A N   1 
ATOM   869  C  CA  . HIS A 1 117 ? 9.770   -3.194  46.000  1.00 20.20 ? 152 HIS A CA  1 
ATOM   870  C  C   . HIS A 1 117 ? 10.759  -4.257  46.447  1.00 20.31 ? 152 HIS A C   1 
ATOM   871  O  O   . HIS A 1 117 ? 11.448  -4.840  45.600  1.00 19.94 ? 152 HIS A O   1 
ATOM   872  C  CB  . HIS A 1 117 ? 10.503  -1.844  45.915  1.00 20.62 ? 152 HIS A CB  1 
ATOM   873  C  CG  . HIS A 1 117 ? 9.654   -0.751  45.353  1.00 16.07 ? 152 HIS A CG  1 
ATOM   874  N  ND1 . HIS A 1 117 ? 9.786   -0.308  44.053  1.00 17.86 ? 152 HIS A ND1 1 
ATOM   875  C  CD2 . HIS A 1 117 ? 8.642   -0.022  45.904  1.00 16.07 ? 152 HIS A CD2 1 
ATOM   876  C  CE1 . HIS A 1 117 ? 8.917   0.665   43.834  1.00 18.97 ? 152 HIS A CE1 1 
ATOM   877  N  NE2 . HIS A 1 117 ? 8.190   0.834   44.928  1.00 15.74 ? 152 HIS A NE2 1 
ATOM   878  N  N   . VAL A 1 118 ? 10.822  -4.555  47.745  1.00 17.81 ? 153 VAL A N   1 
ATOM   879  C  CA  . VAL A 1 118 ? 11.763  -5.546  48.256  1.00 21.11 ? 153 VAL A CA  1 
ATOM   880  C  C   . VAL A 1 118 ? 11.086  -6.823  48.704  1.00 21.49 ? 153 VAL A C   1 
ATOM   881  O  O   . VAL A 1 118 ? 11.791  -7.820  48.919  1.00 22.95 ? 153 VAL A O   1 
ATOM   882  C  CB  . VAL A 1 118 ? 12.612  -4.987  49.420  1.00 21.34 ? 153 VAL A CB  1 
ATOM   883  C  CG1 . VAL A 1 118 ? 13.250  -3.753  48.985  1.00 29.95 ? 153 VAL A CG1 1 
ATOM   884  C  CG2 . VAL A 1 118 ? 11.764  -4.757  50.695  1.00 20.70 ? 153 VAL A CG2 1 
ATOM   885  N  N   . GLY A 1 119 ? 9.758   -6.834  48.865  1.00 20.49 ? 154 GLY A N   1 
ATOM   886  C  CA  . GLY A 1 119 ? 9.104   -8.015  49.404  1.00 20.99 ? 154 GLY A CA  1 
ATOM   887  C  C   . GLY A 1 119 ? 9.421   -9.270  48.607  1.00 22.24 ? 154 GLY A C   1 
ATOM   888  O  O   . GLY A 1 119 ? 9.707   -10.324 49.178  1.00 21.45 ? 154 GLY A O   1 
ATOM   889  N  N   . GLY A 1 120 ? 9.408   -9.162  47.274  1.00 22.89 ? 155 GLY A N   1 
ATOM   890  C  CA  . GLY A 1 120 ? 9.563   -10.308 46.393  1.00 22.06 ? 155 GLY A CA  1 
ATOM   891  C  C   . GLY A 1 120 ? 10.936  -10.930 46.394  1.00 28.20 ? 155 GLY A C   1 
ATOM   892  O  O   . GLY A 1 120 ? 11.145  -11.956 45.729  1.00 23.43 ? 155 GLY A O   1 
ATOM   893  N  N   . LEU A 1 121 ? 11.879  -10.361 47.141  1.00 21.28 ? 156 LEU A N   1 
ATOM   894  C  CA  . LEU A 1 121 ? 13.179  -11.018 47.272  1.00 26.13 ? 156 LEU A CA  1 
ATOM   895  C  C   . LEU A 1 121 ? 13.089  -12.353 48.018  1.00 26.75 ? 156 LEU A C   1 
ATOM   896  O  O   . LEU A 1 121 ? 14.030  -13.160 47.947  1.00 23.13 ? 156 LEU A O   1 
ATOM   897  C  CB  . LEU A 1 121 ? 14.162  -10.083 47.983  1.00 26.26 ? 156 LEU A CB  1 
ATOM   898  C  CG  . LEU A 1 121 ? 14.796  -9.031  47.058  1.00 20.86 ? 156 LEU A CG  1 
ATOM   899  C  CD1 . LEU A 1 121 ? 15.593  -7.984  47.868  1.00 24.05 ? 156 LEU A CD1 1 
ATOM   900  C  CD2 . LEU A 1 121 ? 15.675  -9.679  45.992  1.00 21.74 ? 156 LEU A CD2 1 
ATOM   901  N  N   . MET A 1 122 ? 11.982  -12.606 48.714  1.00 26.90 ? 157 MET A N   1 
ATOM   902  C  CA  . MET A 1 122 ? 11.835  -13.762 49.598  1.00 28.58 ? 157 MET A CA  1 
ATOM   903  C  C   . MET A 1 122 ? 10.495  -14.431 49.328  1.00 34.79 ? 157 MET A C   1 
ATOM   904  O  O   . MET A 1 122 ? 9.454   -13.767 49.310  1.00 40.60 ? 157 MET A O   1 
ATOM   905  C  CB  . MET A 1 122 ? 11.951  -13.306 51.070  1.00 28.90 ? 157 MET A CB  1 
ATOM   906  C  CG  . MET A 1 122 ? 13.331  -12.810 51.455  1.00 27.13 ? 157 MET A CG  1 
ATOM   907  S  SD  . MET A 1 122 ? 14.676  -14.045 51.404  1.00 36.12 ? 157 MET A SD  1 
ATOM   908  C  CE  . MET A 1 122 ? 13.900  -15.339 52.342  1.00 40.03 ? 157 MET A CE  1 
ATOM   909  N  N   . VAL A 1 123 ? 10.526  -15.737 49.094  1.00 37.87 ? 158 VAL A N   1 
ATOM   910  C  CA  . VAL A 1 123 ? 9.323   -16.546 48.954  1.00 40.17 ? 158 VAL A CA  1 
ATOM   911  C  C   . VAL A 1 123 ? 9.312   -17.560 50.087  1.00 51.88 ? 158 VAL A C   1 
ATOM   912  O  O   . VAL A 1 123 ? 10.291  -18.291 50.286  1.00 53.82 ? 158 VAL A O   1 
ATOM   913  C  CB  . VAL A 1 123 ? 9.248   -17.238 47.581  1.00 47.25 ? 158 VAL A CB  1 
ATOM   914  C  CG1 . VAL A 1 123 ? 10.582  -17.892 47.236  1.00 48.02 ? 158 VAL A CG1 1 
ATOM   915  C  CG2 . VAL A 1 123 ? 8.125   -18.275 47.590  1.00 37.06 ? 158 VAL A CG2 1 
ATOM   916  N  N   . GLY A 1 124 ? 8.205   -17.607 50.822  1.00 62.09 ? 159 GLY A N   1 
ATOM   917  C  CA  . GLY A 1 124 ? 8.263   -18.254 52.119  1.00 55.45 ? 159 GLY A CA  1 
ATOM   918  C  C   . GLY A 1 124 ? 9.255   -17.482 52.958  1.00 53.90 ? 159 GLY A C   1 
ATOM   919  O  O   . GLY A 1 124 ? 9.270   -16.246 52.960  1.00 53.80 ? 159 GLY A O   1 
ATOM   920  N  N   . GLU A 1 125 ? 10.119  -18.194 53.663  1.00 53.87 ? 160 GLU A N   1 
ATOM   921  C  CA  . GLU A 1 125 ? 11.253  -17.536 54.286  1.00 57.57 ? 160 GLU A CA  1 
ATOM   922  C  C   . GLU A 1 125 ? 12.513  -18.024 53.575  1.00 57.00 ? 160 GLU A C   1 
ATOM   923  O  O   . GLU A 1 125 ? 13.508  -18.388 54.199  1.00 58.92 ? 160 GLU A O   1 
ATOM   924  C  CB  . GLU A 1 125 ? 11.281  -17.786 55.795  1.00 60.00 ? 160 GLU A CB  1 
ATOM   925  C  CG  . GLU A 1 125 ? 11.899  -16.608 56.595  1.00 72.13 ? 160 GLU A CG  1 
ATOM   926  C  CD  . GLU A 1 125 ? 13.411  -16.503 56.624  1.00 83.57 ? 160 GLU A CD  1 
ATOM   927  O  OE1 . GLU A 1 125 ? 14.125  -17.524 56.509  1.00 87.72 ? 160 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A 1 125 ? 13.885  -15.347 56.731  1.00 72.71 ? 160 GLU A OE2 1 
ATOM   929  N  N   . GLN A 1 126 ? 12.452  -18.087 52.242  1.00 55.46 ? 161 GLN A N   1 
ATOM   930  C  CA  . GLN A 1 126 ? 13.534  -18.660 51.459  1.00 46.35 ? 161 GLN A CA  1 
ATOM   931  C  C   . GLN A 1 126 ? 13.775  -17.815 50.205  1.00 43.00 ? 161 GLN A C   1 
ATOM   932  O  O   . GLN A 1 126 ? 12.846  -17.207 49.674  1.00 35.06 ? 161 GLN A O   1 
ATOM   933  C  CB  . GLN A 1 126 ? 13.177  -20.099 51.146  1.00 63.53 ? 161 GLN A CB  1 
ATOM   934  C  CG  . GLN A 1 126 ? 14.183  -20.875 50.393  1.00 66.03 ? 161 GLN A CG  1 
ATOM   935  C  CD  . GLN A 1 126 ? 14.079  -22.315 50.812  1.00 63.36 ? 161 GLN A CD  1 
ATOM   936  O  OE1 . GLN A 1 126 ? 13.368  -22.626 51.772  1.00 73.02 ? 161 GLN A OE1 1 
ATOM   937  N  NE2 . GLN A 1 126 ? 14.810  -23.197 50.145  1.00 85.08 ? 161 GLN A NE2 1 
ATOM   938  N  N   . LEU A 1 127 ? 15.034  -17.779 49.747  1.00 35.29 ? 162 LEU A N   1 
ATOM   939  C  CA  . LEU A 1 127 ? 15.462  -16.851 48.692  1.00 34.38 ? 162 LEU A CA  1 
ATOM   940  C  C   . LEU A 1 127 ? 14.724  -17.065 47.379  1.00 32.93 ? 162 LEU A C   1 
ATOM   941  O  O   . LEU A 1 127 ? 14.754  -18.157 46.805  1.00 29.61 ? 162 LEU A O   1 
ATOM   942  C  CB  . LEU A 1 127 ? 16.960  -16.999 48.427  1.00 36.30 ? 162 LEU A CB  1 
ATOM   943  C  CG  . LEU A 1 127 ? 17.963  -16.933 49.579  1.00 51.48 ? 162 LEU A CG  1 
ATOM   944  C  CD1 . LEU A 1 127 ? 19.387  -16.958 49.042  1.00 44.28 ? 162 LEU A CD1 1 
ATOM   945  C  CD2 . LEU A 1 127 ? 17.721  -15.663 50.367  1.00 38.30 ? 162 LEU A CD2 1 
ATOM   946  N  N   . ALA A 1 128 ? 14.136  -15.985 46.854  1.00 29.52 ? 163 ALA A N   1 
ATOM   947  C  CA  . ALA A 1 128 ? 13.385  -16.088 45.607  1.00 32.36 ? 163 ALA A CA  1 
ATOM   948  C  C   . ALA A 1 128 ? 14.290  -16.151 44.379  1.00 27.99 ? 163 ALA A C   1 
ATOM   949  O  O   . ALA A 1 128 ? 13.895  -16.725 43.363  1.00 32.74 ? 163 ALA A O   1 
ATOM   950  C  CB  . ALA A 1 128 ? 12.410  -14.909 45.476  1.00 25.99 ? 163 ALA A CB  1 
ATOM   951  N  N   . PHE A 1 129 ? 15.486  -15.569 44.437  1.00 25.42 ? 164 PHE A N   1 
ATOM   952  C  CA  . PHE A 1 129 ? 16.379  -15.471 43.286  1.00 24.75 ? 164 PHE A CA  1 
ATOM   953  C  C   . PHE A 1 129 ? 17.698  -16.079 43.727  1.00 27.02 ? 164 PHE A C   1 
ATOM   954  O  O   . PHE A 1 129 ? 18.680  -15.373 43.973  1.00 28.71 ? 164 PHE A O   1 
ATOM   955  C  CB  . PHE A 1 129 ? 16.529  -14.032 42.788  1.00 20.32 ? 164 PHE A CB  1 
ATOM   956  C  CG  . PHE A 1 129 ? 15.211  -13.363 42.501  1.00 19.89 ? 164 PHE A CG  1 
ATOM   957  C  CD1 . PHE A 1 129 ? 14.579  -13.561 41.291  1.00 18.33 ? 164 PHE A CD1 1 
ATOM   958  C  CD2 . PHE A 1 129 ? 14.624  -12.522 43.435  1.00 26.02 ? 164 PHE A CD2 1 
ATOM   959  C  CE1 . PHE A 1 129 ? 13.365  -12.951 41.026  1.00 24.82 ? 164 PHE A CE1 1 
ATOM   960  C  CE2 . PHE A 1 129 ? 13.437  -11.900 43.177  1.00 25.35 ? 164 PHE A CE2 1 
ATOM   961  C  CZ  . PHE A 1 129 ? 12.796  -12.120 41.967  1.00 27.07 ? 164 PHE A CZ  1 
ATOM   962  N  N   . PRO A 1 130 ? 17.751  -17.405 43.826  1.00 32.58 ? 165 PRO A N   1 
ATOM   963  C  CA  . PRO A 1 130 ? 18.892  -18.064 44.470  1.00 32.10 ? 165 PRO A CA  1 
ATOM   964  C  C   . PRO A 1 130 ? 20.216  -17.855 43.760  1.00 30.14 ? 165 PRO A C   1 
ATOM   965  O  O   . PRO A 1 130 ? 21.264  -18.093 44.374  1.00 40.56 ? 165 PRO A O   1 
ATOM   966  C  CB  . PRO A 1 130 ? 18.480  -19.540 44.441  1.00 30.67 ? 165 PRO A CB  1 
ATOM   967  C  CG  . PRO A 1 130 ? 17.650  -19.630 43.221  1.00 28.13 ? 165 PRO A CG  1 
ATOM   968  C  CD  . PRO A 1 130 ? 16.840  -18.378 43.208  1.00 31.96 ? 165 PRO A CD  1 
ATOM   969  N  N   . ASN A 1 131 ? 20.208  -17.389 42.527  1.00 30.13 ? 166 ASN A N   1 
ATOM   970  C  CA  . ASN A 1 131 ? 21.479  -17.246 41.783  1.00 31.46 ? 166 ASN A CA  1 
ATOM   971  C  C   . ASN A 1 131 ? 21.829  -15.775 41.587  1.00 33.51 ? 166 ASN A C   1 
ATOM   972  O  O   . ASN A 1 131 ? 22.799  -15.504 40.873  1.00 32.51 ? 166 ASN A O   1 
ATOM   973  C  CB  . ASN A 1 131 ? 21.351  -17.926 40.437  1.00 31.05 ? 166 ASN A CB  1 
ATOM   974  C  CG  . ASN A 1 131 ? 21.268  -19.422 40.592  1.00 40.26 ? 166 ASN A CG  1 
ATOM   975  O  OD1 . ASN A 1 131 ? 20.441  -20.076 39.951  1.00 44.85 ? 166 ASN A OD1 1 
ATOM   976  N  ND2 . ASN A 1 131 ? 22.107  -19.974 41.453  1.00 41.20 ? 166 ASN A ND2 1 
ATOM   977  N  N   . ALA A 1 132 ? 21.151  -14.871 42.291  1.00 26.20 ? 167 ALA A N   1 
ATOM   978  C  CA  . ALA A 1 132 ? 21.270  -13.461 41.977  1.00 22.27 ? 167 ALA A CA  1 
ATOM   979  C  C   . ALA A 1 132 ? 22.142  -12.747 42.992  1.00 29.45 ? 167 ALA A C   1 
ATOM   980  O  O   . ALA A 1 132 ? 22.162  -13.090 44.175  1.00 33.35 ? 167 ALA A O   1 
ATOM   981  C  CB  . ALA A 1 132 ? 19.879  -12.806 41.940  1.00 23.54 ? 167 ALA A CB  1 
ATOM   982  N  N   . VAL A 1 133 ? 22.859  -11.763 42.524  1.00 25.12 ? 168 VAL A N   1 
ATOM   983  C  CA  . VAL A 1 133 ? 23.424  -10.751 43.410  1.00 25.18 ? 168 VAL A CA  1 
ATOM   984  C  C   . VAL A 1 133 ? 22.412  -9.623  43.492  1.00 23.54 ? 168 VAL A C   1 
ATOM   985  O  O   . VAL A 1 133 ? 21.740  -9.303  42.501  1.00 26.20 ? 168 VAL A O   1 
ATOM   986  C  CB  . VAL A 1 133 ? 24.787  -10.251 42.904  1.00 22.40 ? 168 VAL A CB  1 
ATOM   987  C  CG1 . VAL A 1 133 ? 25.180  -8.993  43.619  1.00 26.58 ? 168 VAL A CG1 1 
ATOM   988  C  CG2 . VAL A 1 133 ? 25.875  -11.320 43.107  1.00 33.84 ? 168 VAL A CG2 1 
ATOM   989  N  N   . VAL A 1 134 ? 22.248  -9.053  44.681  1.00 23.88 ? 169 VAL A N   1 
ATOM   990  C  CA  . VAL A 1 134 ? 21.335  -7.934  44.896  1.00 22.04 ? 169 VAL A CA  1 
ATOM   991  C  C   . VAL A 1 134 ? 22.162  -6.659  45.047  1.00 25.89 ? 169 VAL A C   1 
ATOM   992  O  O   . VAL A 1 134 ? 23.147  -6.647  45.785  1.00 22.66 ? 169 VAL A O   1 
ATOM   993  C  CB  . VAL A 1 134 ? 20.454  -8.162  46.136  1.00 25.03 ? 169 VAL A CB  1 
ATOM   994  C  CG1 . VAL A 1 134 ? 19.581  -6.935  46.393  1.00 24.29 ? 169 VAL A CG1 1 
ATOM   995  C  CG2 . VAL A 1 134 ? 19.586  -9.411  45.975  1.00 21.81 ? 169 VAL A CG2 1 
ATOM   996  N  N   . ARG A 1 135 ? 21.759  -5.582  44.357  1.00 21.58 ? 170 ARG A N   1 
ATOM   997  C  CA  . ARG A 1 135 ? 22.469  -4.306  44.382  1.00 22.65 ? 170 ARG A CA  1 
ATOM   998  C  C   . ARG A 1 135 ? 21.488  -3.210  44.806  1.00 23.51 ? 170 ARG A C   1 
ATOM   999  O  O   . ARG A 1 135 ? 20.345  -3.191  44.334  1.00 17.44 ? 170 ARG A O   1 
ATOM   1000 C  CB  . ARG A 1 135 ? 23.014  -3.908  42.976  1.00 21.77 ? 170 ARG A CB  1 
ATOM   1001 C  CG  . ARG A 1 135 ? 23.935  -4.865  42.149  1.00 24.86 ? 170 ARG A CG  1 
ATOM   1002 C  CD  . ARG A 1 135 ? 25.259  -5.175  42.736  1.00 31.31 ? 170 ARG A CD  1 
ATOM   1003 N  NE  . ARG A 1 135 ? 26.137  -4.046  43.047  1.00 23.23 ? 170 ARG A NE  1 
ATOM   1004 C  CZ  . ARG A 1 135 ? 27.052  -3.485  42.266  1.00 31.04 ? 170 ARG A CZ  1 
ATOM   1005 N  NH1 . ARG A 1 135 ? 27.226  -3.856  41.001  1.00 29.81 ? 170 ARG A NH1 1 
ATOM   1006 N  NH2 . ARG A 1 135 ? 27.865  -2.568  42.792  1.00 23.70 ? 170 ARG A NH2 1 
ATOM   1007 N  N   . ALA A 1 136 ? 21.946  -2.278  45.651  1.00 25.35 ? 171 ALA A N   1 
ATOM   1008 C  CA  . ALA A 1 136 ? 21.221  -1.045  45.971  1.00 20.57 ? 171 ALA A CA  1 
ATOM   1009 C  C   . ALA A 1 136 ? 22.226  -0.001  46.437  1.00 19.18 ? 171 ALA A C   1 
ATOM   1010 O  O   . ALA A 1 136 ? 23.407  -0.292  46.640  1.00 19.33 ? 171 ALA A O   1 
ATOM   1011 C  CB  . ALA A 1 136 ? 20.156  -1.241  47.059  1.00 19.06 ? 171 ALA A CB  1 
ATOM   1012 N  N   . ASP A 1 137 ? 21.761  1.235   46.610  1.00 21.72 ? 172 ASP A N   1 
ATOM   1013 C  CA  . ASP A 1 137 ? 22.725  2.241   47.043  1.00 19.90 ? 172 ASP A CA  1 
ATOM   1014 C  C   . ASP A 1 137 ? 23.071  2.006   48.504  1.00 20.61 ? 172 ASP A C   1 
ATOM   1015 O  O   . ASP A 1 137 ? 22.240  1.559   49.301  1.00 20.03 ? 172 ASP A O   1 
ATOM   1016 C  CB  . ASP A 1 137 ? 22.201  3.684   46.858  1.00 20.29 ? 172 ASP A CB  1 
ATOM   1017 C  CG  . ASP A 1 137 ? 23.325  4.740   46.991  1.00 27.85 ? 172 ASP A CG  1 
ATOM   1018 O  OD1 . ASP A 1 137 ? 23.680  5.142   48.117  1.00 29.18 ? 172 ASP A OD1 1 
ATOM   1019 O  OD2 . ASP A 1 137 ? 23.891  5.151   45.956  1.00 24.80 ? 172 ASP A OD2 1 
ATOM   1020 N  N   . GLN A 1 138 ? 24.295  2.347   48.888  1.00 22.14 ? 173 GLN A N   1 
ATOM   1021 C  CA  . GLN A 1 138 ? 24.741  2.109   50.283  1.00 24.02 ? 173 GLN A CA  1 
ATOM   1022 C  C   . GLN A 1 138 ? 23.872  2.901   51.259  1.00 23.32 ? 173 GLN A C   1 
ATOM   1023 O  O   . GLN A 1 138 ? 23.577  2.403   52.345  1.00 23.49 ? 173 GLN A O   1 
ATOM   1024 C  CB  . GLN A 1 138 ? 26.199  2.538   50.435  1.00 25.03 ? 173 GLN A CB  1 
ATOM   1025 C  CG  . GLN A 1 138 ? 26.835  2.107   51.749  1.00 28.97 ? 173 GLN A CG  1 
ATOM   1026 C  CD  . GLN A 1 138 ? 27.380  0.700   51.703  1.00 35.48 ? 173 GLN A CD  1 
ATOM   1027 O  OE1 . GLN A 1 138 ? 28.252  0.376   50.892  1.00 33.81 ? 173 GLN A OE1 1 
ATOM   1028 N  NE2 . GLN A 1 138 ? 26.866  -0.151  52.578  1.00 34.65 ? 173 GLN A NE2 1 
ATOM   1029 N  N   . LYS A 1 139 ? 23.477  4.093   50.846  1.00 25.01 ? 174 LYS A N   1 
ATOM   1030 C  CA  . LYS A 1 139 ? 22.660  4.952   51.734  1.00 28.81 ? 174 LYS A CA  1 
ATOM   1031 C  C   . LYS A 1 139 ? 21.306  4.268   51.972  1.00 24.00 ? 174 LYS A C   1 
ATOM   1032 O  O   . LYS A 1 139 ? 20.770  4.376   53.072  1.00 23.90 ? 174 LYS A O   1 
ATOM   1033 C  CB  . LYS A 1 139 ? 22.569  6.338   51.106  1.00 30.39 ? 174 LYS A CB  1 
ATOM   1034 C  CG  . LYS A 1 139 ? 23.905  7.010   50.867  1.00 39.11 ? 174 LYS A CG  1 
ATOM   1035 C  CD  . LYS A 1 139 ? 23.709  8.355   50.185  1.00 40.25 ? 174 LYS A CD  1 
ATOM   1036 C  CE  . LYS A 1 139 ? 24.654  9.400   50.671  1.00 37.57 ? 174 LYS A CE  1 
ATOM   1037 N  NZ  . LYS A 1 139 ? 25.165  10.185  49.546  1.00 42.39 ? 174 LYS A NZ  1 
ATOM   1038 N  N   . GLU A 1 140 ? 20.804  3.576   50.958  1.00 22.02 ? 175 GLU A N   1 
ATOM   1039 C  CA  . GLU A 1 140 ? 19.540  2.855   51.118  1.00 23.10 ? 175 GLU A CA  1 
ATOM   1040 C  C   . GLU A 1 140 ? 19.660  1.737   52.151  1.00 25.62 ? 175 GLU A C   1 
ATOM   1041 O  O   . GLU A 1 140 ? 18.876  1.672   53.109  1.00 25.20 ? 175 GLU A O   1 
ATOM   1042 C  CB  . GLU A 1 140 ? 19.106  2.295   49.765  1.00 21.08 ? 175 GLU A CB  1 
ATOM   1043 C  CG  . GLU A 1 140 ? 17.648  1.842   49.725  1.00 18.18 ? 175 GLU A CG  1 
ATOM   1044 C  CD  . GLU A 1 140 ? 16.636  2.985   49.863  1.00 20.66 ? 175 GLU A CD  1 
ATOM   1045 O  OE1 . GLU A 1 140 ? 17.014  4.183   49.802  1.00 20.05 ? 175 GLU A OE1 1 
ATOM   1046 O  OE2 . GLU A 1 140 ? 15.441  2.670   50.055  1.00 19.93 ? 175 GLU A OE2 1 
ATOM   1047 N  N   . ALA A 1 141 ? 20.663  0.863   51.986  1.00 22.60 ? 176 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 141 ? 20.865  -0.242  52.921  1.00 24.28 ? 176 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 141 ? 21.227  0.264   54.313  1.00 22.28 ? 176 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 141 ? 20.731  -0.247  55.324  1.00 26.21 ? 176 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 141 ? 21.965  -1.173  52.404  1.00 23.17 ? 176 ALA A CB  1 
ATOM   1052 N  N   . ASP A 1 142 ? 22.107  1.256   54.392  1.00 24.93 ? 177 ASP A N   1 
ATOM   1053 C  CA  . ASP A 1 142 ? 22.517  1.731   55.701  1.00 25.01 ? 177 ASP A CA  1 
ATOM   1054 C  C   . ASP A 1 142 ? 21.325  2.247   56.494  1.00 29.88 ? 177 ASP A C   1 
ATOM   1055 O  O   . ASP A 1 142 ? 21.255  2.035   57.714  1.00 26.43 ? 177 ASP A O   1 
ATOM   1056 C  CB  . ASP A 1 142 ? 23.580  2.814   55.565  1.00 30.67 ? 177 ASP A CB  1 
ATOM   1057 C  CG  . ASP A 1 142 ? 24.917  2.257   55.139  1.00 29.94 ? 177 ASP A CG  1 
ATOM   1058 O  OD1 . ASP A 1 142 ? 25.013  1.019   54.918  1.00 28.16 ? 177 ASP A OD1 1 
ATOM   1059 O  OD2 . ASP A 1 142 ? 25.869  3.053   55.063  1.00 31.06 ? 177 ASP A OD2 1 
ATOM   1060 N  N   . PHE A 1 143 ? 20.379  2.929   55.816  1.00 24.33 ? 178 PHE A N   1 
ATOM   1061 C  CA  . PHE A 1 143 ? 19.220  3.493   56.507  1.00 28.91 ? 178 PHE A CA  1 
ATOM   1062 C  C   . PHE A 1 143 ? 18.190  2.419   56.871  1.00 25.26 ? 178 PHE A C   1 
ATOM   1063 O  O   . PHE A 1 143 ? 17.761  2.329   58.027  1.00 27.98 ? 178 PHE A O   1 
ATOM   1064 C  CB  . PHE A 1 143 ? 18.571  4.584   55.649  1.00 25.16 ? 178 PHE A CB  1 
ATOM   1065 C  CG  . PHE A 1 143 ? 17.321  5.196   56.274  1.00 27.24 ? 178 PHE A CG  1 
ATOM   1066 C  CD1 . PHE A 1 143 ? 17.429  6.144   57.285  1.00 26.94 ? 178 PHE A CD1 1 
ATOM   1067 C  CD2 . PHE A 1 143 ? 16.054  4.781   55.883  1.00 27.76 ? 178 PHE A CD2 1 
ATOM   1068 C  CE1 . PHE A 1 143 ? 16.294  6.698   57.876  1.00 33.22 ? 178 PHE A CE1 1 
ATOM   1069 C  CE2 . PHE A 1 143 ? 14.916  5.339   56.459  1.00 28.46 ? 178 PHE A CE2 1 
ATOM   1070 C  CZ  . PHE A 1 143 ? 15.040  6.296   57.464  1.00 27.18 ? 178 PHE A CZ  1 
ATOM   1071 N  N   . TRP A 1 144 ? 17.802  1.570   55.917  1.00 23.75 ? 179 TRP A N   1 
ATOM   1072 C  CA  . TRP A 1 144 ? 16.698  0.650   56.202  1.00 26.20 ? 179 TRP A CA  1 
ATOM   1073 C  C   . TRP A 1 144 ? 17.129  -0.581  56.993  1.00 23.07 ? 179 TRP A C   1 
ATOM   1074 O  O   . TRP A 1 144 ? 16.280  -1.190  57.654  1.00 23.63 ? 179 TRP A O   1 
ATOM   1075 C  CB  . TRP A 1 144 ? 16.007  0.218   54.897  1.00 24.36 ? 179 TRP A CB  1 
ATOM   1076 C  CG  . TRP A 1 144 ? 15.276  1.355   54.227  1.00 22.37 ? 179 TRP A CG  1 
ATOM   1077 C  CD1 . TRP A 1 144 ? 15.626  1.973   53.061  1.00 22.43 ? 179 TRP A CD1 1 
ATOM   1078 C  CD2 . TRP A 1 144 ? 14.067  2.009   54.680  1.00 25.35 ? 179 TRP A CD2 1 
ATOM   1079 N  NE1 . TRP A 1 144 ? 14.725  2.988   52.770  1.00 19.59 ? 179 TRP A NE1 1 
ATOM   1080 C  CE2 . TRP A 1 144 ? 13.760  3.018   53.741  1.00 25.94 ? 179 TRP A CE2 1 
ATOM   1081 C  CE3 . TRP A 1 144 ? 13.226  1.835   55.780  1.00 29.43 ? 179 TRP A CE3 1 
ATOM   1082 C  CZ2 . TRP A 1 144 ? 12.638  3.850   53.868  1.00 26.67 ? 179 TRP A CZ2 1 
ATOM   1083 C  CZ3 . TRP A 1 144 ? 12.106  2.665   55.909  1.00 34.10 ? 179 TRP A CZ3 1 
ATOM   1084 C  CH2 . TRP A 1 144 ? 11.830  3.657   54.960  1.00 30.95 ? 179 TRP A CH2 1 
ATOM   1085 N  N   . LEU A 1 145 ? 18.411  -0.965  56.951  1.00 22.04 ? 180 LEU A N   1 
ATOM   1086 C  CA  . LEU A 1 145 ? 18.893  -2.147  57.672  1.00 25.92 ? 180 LEU A CA  1 
ATOM   1087 C  C   . LEU A 1 145 ? 19.410  -1.815  59.062  1.00 26.38 ? 180 LEU A C   1 
ATOM   1088 O  O   . LEU A 1 145 ? 19.960  -2.690  59.737  1.00 26.25 ? 180 LEU A O   1 
ATOM   1089 C  CB  . LEU A 1 145 ? 19.982  -2.873  56.862  1.00 25.46 ? 180 LEU A CB  1 
ATOM   1090 C  CG  . LEU A 1 145 ? 19.448  -3.249  55.471  1.00 23.11 ? 180 LEU A CG  1 
ATOM   1091 C  CD1 . LEU A 1 145 ? 20.468  -3.969  54.568  1.00 24.30 ? 180 LEU A CD1 1 
ATOM   1092 C  CD2 . LEU A 1 145 ? 18.165  -4.069  55.617  1.00 27.98 ? 180 LEU A CD2 1 
ATOM   1093 N  N   . SER A 1 146 ? 19.235  -0.574  59.502  1.00 30.21 ? 181 SER A N   1 
ATOM   1094 C  CA  . SER A 1 146 ? 19.722  -0.118  60.800  1.00 29.15 ? 181 SER A CA  1 
ATOM   1095 C  C   . SER A 1 146 ? 18.761  -0.575  61.894  1.00 37.70 ? 181 SER A C   1 
ATOM   1096 O  O   . SER A 1 146 ? 17.641  -0.062  61.995  1.00 34.92 ? 181 SER A O   1 
ATOM   1097 C  CB  . SER A 1 146 ? 19.855  1.401   60.785  1.00 32.57 ? 181 SER A CB  1 
ATOM   1098 O  OG  . SER A 1 146 ? 20.050  1.919   62.093  1.00 33.25 ? 181 SER A OG  1 
ATOM   1099 N  N   . GLN A 1 147 ? 19.204  -1.528  62.724  1.00 35.77 ? 182 GLN A N   1 
ATOM   1100 C  CA  . GLN A 1 147 ? 18.412  -1.955  63.878  1.00 38.88 ? 182 GLN A CA  1 
ATOM   1101 C  C   . GLN A 1 147 ? 17.996  -0.755  64.712  1.00 41.80 ? 182 GLN A C   1 
ATOM   1102 O  O   . GLN A 1 147 ? 16.904  -0.724  65.298  1.00 43.68 ? 182 GLN A O   1 
ATOM   1103 C  CB  . GLN A 1 147 ? 19.230  -2.900  64.755  1.00 44.38 ? 182 GLN A CB  1 
ATOM   1104 C  CG  . GLN A 1 147 ? 19.603  -4.239  64.154  1.00 43.43 ? 182 GLN A CG  1 
ATOM   1105 C  CD  . GLN A 1 147 ? 20.998  -4.216  63.535  1.00 55.68 ? 182 GLN A CD  1 
ATOM   1106 O  OE1 . GLN A 1 147 ? 21.361  -3.278  62.801  1.00 47.64 ? 182 GLN A OE1 1 
ATOM   1107 N  NE2 . GLN A 1 147 ? 21.818  -5.204  63.900  1.00 34.51 ? 182 GLN A NE2 1 
ATOM   1108 N  N   . THR A 1 148 ? 18.856  0.244   64.807  1.00 36.10 ? 183 THR A N   1 
ATOM   1109 C  CA  . THR A 1 148 ? 18.502  1.364   65.695  1.00 38.91 ? 183 THR A CA  1 
ATOM   1110 C  C   . THR A 1 148 ? 17.428  2.219   65.051  1.00 42.27 ? 183 THR A C   1 
ATOM   1111 O  O   . THR A 1 148 ? 16.535  2.637   65.793  1.00 39.86 ? 183 THR A O   1 
ATOM   1112 C  CB  . THR A 1 148 ? 19.729  2.160   66.133  1.00 37.39 ? 183 THR A CB  1 
ATOM   1113 O  OG1 . THR A 1 148 ? 20.493  2.514   64.987  1.00 56.89 ? 183 THR A OG1 1 
ATOM   1114 C  CG2 . THR A 1 148 ? 20.593  1.350   67.083  1.00 40.33 ? 183 THR A CG2 1 
ATOM   1115 N  N   . ASN A 1 149 ? 17.481  2.475   63.738  1.00 35.45 ? 184 ASN A N   1 
ATOM   1116 C  CA  . ASN A 1 149 ? 16.391  3.211   63.109  1.00 43.05 ? 184 ASN A CA  1 
ATOM   1117 C  C   . ASN A 1 149 ? 15.064  2.487   63.308  1.00 40.64 ? 184 ASN A C   1 
ATOM   1118 O  O   . ASN A 1 149 ? 14.038  3.123   63.578  1.00 46.93 ? 184 ASN A O   1 
ATOM   1119 C  CB  . ASN A 1 149 ? 16.694  3.424   61.618  1.00 35.42 ? 184 ASN A CB  1 
ATOM   1120 C  CG  . ASN A 1 149 ? 17.831  4.423   61.380  1.00 35.70 ? 184 ASN A CG  1 
ATOM   1121 O  OD1 . ASN A 1 149 ? 18.285  5.086   62.309  1.00 38.47 ? 184 ASN A OD1 1 
ATOM   1122 N  ND2 . ASN A 1 149 ? 18.307  4.513   60.137  1.00 34.02 ? 184 ASN A ND2 1 
ATOM   1123 N  N   . LEU A 1 150 ? 15.070  1.156   63.196  1.00 40.16 ? 185 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 150 ? 13.898  0.363   63.550  1.00 39.94 ? 185 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 150 ? 13.423  0.682   64.959  1.00 46.51 ? 185 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 150 ? 12.289  1.131   65.160  1.00 48.60 ? 185 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 150 ? 14.205  -1.128  63.433  1.00 40.00 ? 185 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 150 ? 13.093  -2.055  63.944  1.00 40.49 ? 185 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 150 ? 11.721  -1.710  63.366  1.00 42.96 ? 185 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 150 ? 13.446  -3.516  63.707  1.00 41.06 ? 185 LEU A CD2 1 
ATOM   1131 N  N   . ASP A 1 151 ? 14.285  0.459   65.955  1.00 39.18 ? 186 ASP A N   1 
ATOM   1132 C  CA  . ASP A 1 151 ? 13.845  0.683   67.330  1.00 46.34 ? 186 ASP A CA  1 
ATOM   1133 C  C   . ASP A 1 151 ? 13.522  2.145   67.603  1.00 43.93 ? 186 ASP A C   1 
ATOM   1134 O  O   . ASP A 1 151 ? 12.790  2.436   68.548  1.00 55.26 ? 186 ASP A O   1 
ATOM   1135 C  CB  . ASP A 1 151 ? 14.890  0.149   68.314  1.00 48.85 ? 186 ASP A CB  1 
ATOM   1136 C  CG  . ASP A 1 151 ? 15.128  -1.330  68.132  1.00 62.09 ? 186 ASP A CG  1 
ATOM   1137 O  OD1 . ASP A 1 151 ? 14.124  -2.067  67.962  1.00 64.38 ? 186 ASP A OD1 1 
ATOM   1138 O  OD2 . ASP A 1 151 ? 16.302  -1.757  68.152  1.00 64.94 ? 186 ASP A OD2 1 
ATOM   1139 N  N   . LYS A 1 152 ? 13.999  3.057   66.770  1.00 42.09 ? 187 LYS A N   1 
ATOM   1140 C  CA  . LYS A 1 152 ? 13.798  4.486   66.919  1.00 45.01 ? 187 LYS A CA  1 
ATOM   1141 C  C   . LYS A 1 152 ? 12.619  5.000   66.090  1.00 55.50 ? 187 LYS A C   1 
ATOM   1142 O  O   . LYS A 1 152 ? 12.236  6.155   66.250  1.00 62.81 ? 187 LYS A O   1 
ATOM   1143 C  CB  . LYS A 1 152 ? 15.107  5.198   66.520  1.00 52.94 ? 187 LYS A CB  1 
ATOM   1144 C  CG  . LYS A 1 152 ? 15.235  6.679   66.784  1.00 65.53 ? 187 LYS A CG  1 
ATOM   1145 C  CD  . LYS A 1 152 ? 16.474  7.178   66.028  1.00 67.46 ? 187 LYS A CD  1 
ATOM   1146 C  CE  . LYS A 1 152 ? 16.525  8.695   65.927  1.00 74.71 ? 187 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A 1 152 ? 17.795  9.144   65.287  1.00 56.95 ? 187 LYS A NZ  1 
ATOM   1148 N  N   . ALA A 1 153 ? 12.004  4.161   65.253  1.00 50.96 ? 188 ALA A N   1 
ATOM   1149 C  CA  . ALA A 1 153 ? 10.984  4.615   64.311  1.00 48.17 ? 188 ALA A CA  1 
ATOM   1150 C  C   . ALA A 1 153 ? 9.766   5.129   65.082  1.00 56.81 ? 188 ALA A C   1 
ATOM   1151 O  O   . ALA A 1 153 ? 9.409   4.562   66.134  1.00 59.52 ? 188 ALA A O   1 
ATOM   1152 C  CB  . ALA A 1 153 ? 10.573  3.476   63.374  1.00 47.03 ? 188 ALA A CB  1 
ATOM   1153 N  N   . PRO A 1 154 ? 9.111   6.215   64.598  1.00 58.64 ? 189 PRO A N   1 
ATOM   1154 C  CA  . PRO A 1 154 ? 8.026   6.810   65.371  1.00 61.53 ? 189 PRO A CA  1 
ATOM   1155 C  C   . PRO A 1 154 ? 6.761   5.979   65.453  1.00 57.15 ? 189 PRO A C   1 
ATOM   1156 O  O   . PRO A 1 154 ? 6.252   5.710   66.555  1.00 59.56 ? 189 PRO A O   1 
ATOM   1157 C  CB  . PRO A 1 154 ? 7.773   8.147   64.666  1.00 62.47 ? 189 PRO A CB  1 
ATOM   1158 C  CG  . PRO A 1 154 ? 8.697   8.146   63.439  1.00 63.66 ? 189 PRO A CG  1 
ATOM   1159 C  CD  . PRO A 1 154 ? 9.078   6.707   63.251  1.00 59.36 ? 189 PRO A CD  1 
ATOM   1160 N  N   . ASP A 1 155 ? 6.266   5.551   64.299  1.00 60.85 ? 190 ASP A N   1 
ATOM   1161 C  CA  . ASP A 1 155 ? 5.038   4.770   64.188  1.00 62.24 ? 190 ASP A CA  1 
ATOM   1162 C  C   . ASP A 1 155 ? 5.325   3.348   63.725  1.00 58.60 ? 190 ASP A C   1 
ATOM   1163 O  O   . ASP A 1 155 ? 6.423   3.026   63.270  1.00 52.82 ? 190 ASP A O   1 
ATOM   1164 C  CB  . ASP A 1 155 ? 4.042   5.457   63.236  1.00 60.68 ? 190 ASP A CB  1 
ATOM   1165 C  CG  . ASP A 1 155 ? 4.616   5.695   61.840  1.00 67.90 ? 190 ASP A CG  1 
ATOM   1166 O  OD1 . ASP A 1 155 ? 5.471   4.912   61.366  1.00 61.62 ? 190 ASP A OD1 1 
ATOM   1167 O  OD2 . ASP A 1 155 ? 4.176   6.670   61.192  1.00 68.57 ? 190 ASP A OD2 1 
ATOM   1168 N  N   . ASP A 1 156 ? 4.296   2.504   63.810  1.00 57.66 ? 191 ASP A N   1 
ATOM   1169 C  CA  . ASP A 1 156 ? 4.479   1.107   63.442  1.00 58.14 ? 191 ASP A CA  1 
ATOM   1170 C  C   . ASP A 1 156 ? 4.400   0.906   61.923  1.00 57.74 ? 191 ASP A C   1 
ATOM   1171 O  O   . ASP A 1 156 ? 4.820   -0.139  61.412  1.00 54.75 ? 191 ASP A O   1 
ATOM   1172 C  CB  . ASP A 1 156 ? 3.440   0.243   64.187  1.00 56.12 ? 191 ASP A CB  1 
ATOM   1173 C  CG  . ASP A 1 156 ? 3.659   -1.266  64.013  1.00 68.67 ? 191 ASP A CG  1 
ATOM   1174 O  OD1 . ASP A 1 156 ? 4.626   -1.691  63.348  1.00 66.44 ? 191 ASP A OD1 1 
ATOM   1175 O  OD2 . ASP A 1 156 ? 2.858   -2.037  64.582  1.00 68.22 ? 191 ASP A OD2 1 
ATOM   1176 N  N   . GLU A 1 157 ? 3.910   1.897   61.177  1.00 56.05 ? 192 GLU A N   1 
ATOM   1177 C  CA  . GLU A 1 157 ? 4.015   1.835   59.723  1.00 58.29 ? 192 GLU A CA  1 
ATOM   1178 C  C   . GLU A 1 157 ? 5.481   1.862   59.293  1.00 46.34 ? 192 GLU A C   1 
ATOM   1179 O  O   . GLU A 1 157 ? 5.947   0.996   58.537  1.00 45.00 ? 192 GLU A O   1 
ATOM   1180 C  CB  . GLU A 1 157 ? 3.226   2.995   59.116  1.00 59.18 ? 192 GLU A CB  1 
ATOM   1181 C  CG  . GLU A 1 157 ? 1.719   2.877   59.363  1.00 77.77 ? 192 GLU A CG  1 
ATOM   1182 C  CD  . GLU A 1 157 ? 0.917   4.059   58.836  1.00 92.26 ? 192 GLU A CD  1 
ATOM   1183 O  OE1 . GLU A 1 157 ? 1.533   5.070   58.432  1.00 90.40 ? 192 GLU A OE1 1 
ATOM   1184 O  OE2 . GLU A 1 157 ? -0.335  3.982   58.853  1.00 87.24 ? 192 GLU A OE2 1 
ATOM   1185 N  N   . SER A 1 158 ? 6.239   2.826   59.818  1.00 49.96 ? 193 SER A N   1 
ATOM   1186 C  CA  . SER A 1 158 ? 7.673   2.868   59.556  1.00 48.82 ? 193 SER A CA  1 
ATOM   1187 C  C   . SER A 1 158 ? 8.384   1.640   60.124  1.00 34.93 ? 193 SER A C   1 
ATOM   1188 O  O   . SER A 1 158 ? 9.282   1.085   59.476  1.00 34.74 ? 193 SER A O   1 
ATOM   1189 C  CB  . SER A 1 158 ? 8.268   4.154   60.125  1.00 52.54 ? 193 SER A CB  1 
ATOM   1190 O  OG  . SER A 1 158 ? 7.767   4.398   61.425  1.00 57.40 ? 193 SER A OG  1 
ATOM   1191 N  N   . LYS A 1 159 ? 8.010   1.205   61.333  1.00 41.60 ? 194 LYS A N   1 
ATOM   1192 C  CA  . LYS A 1 159 ? 8.618   -0.005  61.884  1.00 43.53 ? 194 LYS A CA  1 
ATOM   1193 C  C   . LYS A 1 159 ? 8.443   -1.174  60.927  1.00 39.12 ? 194 LYS A C   1 
ATOM   1194 O  O   . LYS A 1 159 ? 9.393   -1.915  60.656  1.00 34.49 ? 194 LYS A O   1 
ATOM   1195 C  CB  . LYS A 1 159 ? 8.025   -0.340  63.256  1.00 46.76 ? 194 LYS A CB  1 
ATOM   1196 C  CG  . LYS A 1 159 ? 8.232   0.723   64.330  1.00 54.29 ? 194 LYS A CG  1 
ATOM   1197 C  CD  . LYS A 1 159 ? 8.123   0.121   65.731  1.00 52.10 ? 194 LYS A CD  1 
ATOM   1198 C  CE  . LYS A 1 159 ? 8.272   1.183   66.830  1.00 57.53 ? 194 LYS A CE  1 
ATOM   1199 N  NZ  . LYS A 1 159 ? 9.361   2.152   66.526  1.00 57.00 ? 194 LYS A NZ  1 
ATOM   1200 N  N   . GLY A 1 160 ? 7.235   -1.332  60.383  1.00 44.22 ? 195 GLY A N   1 
ATOM   1201 C  CA  . GLY A 1 160 ? 7.004   -2.354  59.381  1.00 34.88 ? 195 GLY A CA  1 
ATOM   1202 C  C   . GLY A 1 160 ? 7.868   -2.181  58.147  1.00 34.04 ? 195 GLY A C   1 
ATOM   1203 O  O   . GLY A 1 160 ? 8.301   -3.161  57.545  1.00 36.37 ? 195 GLY A O   1 
ATOM   1204 N  N   . PHE A 1 161 ? 8.126   -0.938  57.742  1.00 38.03 ? 196 PHE A N   1 
ATOM   1205 C  CA  . PHE A 1 161 ? 9.044   -0.740  56.620  1.00 28.69 ? 196 PHE A CA  1 
ATOM   1206 C  C   . PHE A 1 161 ? 10.425  -1.304  56.940  1.00 33.12 ? 196 PHE A C   1 
ATOM   1207 O  O   . PHE A 1 161 ? 11.043  -2.007  56.114  1.00 27.66 ? 196 PHE A O   1 
ATOM   1208 C  CB  . PHE A 1 161 ? 9.164   0.738   56.266  1.00 33.37 ? 196 PHE A CB  1 
ATOM   1209 C  CG  . PHE A 1 161 ? 7.918   1.322   55.660  1.00 36.67 ? 196 PHE A CG  1 
ATOM   1210 C  CD1 . PHE A 1 161 ? 7.022   0.523   54.996  1.00 36.17 ? 196 PHE A CD1 1 
ATOM   1211 C  CD2 . PHE A 1 161 ? 7.659   2.683   55.748  1.00 45.17 ? 196 PHE A CD2 1 
ATOM   1212 C  CE1 . PHE A 1 161 ? 5.872   1.055   54.432  1.00 38.82 ? 196 PHE A CE1 1 
ATOM   1213 C  CE2 . PHE A 1 161 ? 6.516   3.225   55.186  1.00 43.37 ? 196 PHE A CE2 1 
ATOM   1214 C  CZ  . PHE A 1 161 ? 5.625   2.406   54.526  1.00 38.02 ? 196 PHE A CZ  1 
ATOM   1215 N  N   . PHE A 1 162 ? 10.937  -0.995  58.137  1.00 30.02 ? 197 PHE A N   1 
ATOM   1216 C  CA  . PHE A 1 162 ? 12.284  -1.470  58.449  1.00 27.28 ? 197 PHE A CA  1 
ATOM   1217 C  C   . PHE A 1 162 ? 12.302  -2.981  58.546  1.00 27.07 ? 197 PHE A C   1 
ATOM   1218 O  O   . PHE A 1 162 ? 13.221  -3.629  58.036  1.00 31.39 ? 197 PHE A O   1 
ATOM   1219 C  CB  . PHE A 1 162 ? 12.846  -0.905  59.759  1.00 30.91 ? 197 PHE A CB  1 
ATOM   1220 C  CG  . PHE A 1 162 ? 13.084  0.560   59.738  1.00 29.32 ? 197 PHE A CG  1 
ATOM   1221 C  CD1 . PHE A 1 162 ? 12.052  1.446   60.002  1.00 36.69 ? 197 PHE A CD1 1 
ATOM   1222 C  CD2 . PHE A 1 162 ? 14.292  1.062   59.279  1.00 28.24 ? 197 PHE A CD2 1 
ATOM   1223 C  CE1 . PHE A 1 162 ? 12.254  2.803   59.969  1.00 33.63 ? 197 PHE A CE1 1 
ATOM   1224 C  CE2 . PHE A 1 162 ? 14.505  2.421   59.209  1.00 32.26 ? 197 PHE A CE2 1 
ATOM   1225 C  CZ  . PHE A 1 162 ? 13.483  3.300   59.556  1.00 35.65 ? 197 PHE A CZ  1 
ATOM   1226 N  N   . LYS A 1 163 ? 11.303  -3.553  59.222  1.00 32.41 ? 198 LYS A N   1 
ATOM   1227 C  CA  . LYS A 1 163 ? 11.256  -4.997  59.375  1.00 29.28 ? 198 LYS A CA  1 
ATOM   1228 C  C   . LYS A 1 163 ? 11.119  -5.682  58.026  1.00 31.91 ? 198 LYS A C   1 
ATOM   1229 O  O   . LYS A 1 163 ? 11.716  -6.741  57.803  1.00 27.35 ? 198 LYS A O   1 
ATOM   1230 C  CB  . LYS A 1 163 ? 10.113  -5.411  60.304  1.00 31.98 ? 198 LYS A CB  1 
ATOM   1231 C  CG  . LYS A 1 163 ? 10.108  -4.720  61.654  1.00 34.11 ? 198 LYS A CG  1 
ATOM   1232 C  CD  . LYS A 1 163 ? 9.448   -5.593  62.733  1.00 37.14 ? 198 LYS A CD  1 
ATOM   1233 C  CE  . LYS A 1 163 ? 7.923   -5.556  62.675  1.00 38.72 ? 198 LYS A CE  1 
ATOM   1234 N  NZ  . LYS A 1 163 ? 7.300   -6.351  63.792  1.00 46.75 ? 198 LYS A NZ  1 
ATOM   1235 N  N   . GLY A 1 164 ? 10.323  -5.110  57.121  1.00 30.86 ? 199 GLY A N   1 
ATOM   1236 C  CA  . GLY A 1 164 ? 10.168  -5.719  55.811  1.00 29.53 ? 199 GLY A CA  1 
ATOM   1237 C  C   . GLY A 1 164 ? 11.470  -5.725  55.043  1.00 30.68 ? 199 GLY A C   1 
ATOM   1238 O  O   . GLY A 1 164 ? 11.852  -6.739  54.450  1.00 31.69 ? 199 GLY A O   1 
ATOM   1239 N  N   . ALA A 1 165 ? 12.200  -4.610  55.098  1.00 29.58 ? 200 ALA A N   1 
ATOM   1240 C  CA  . ALA A 1 165 ? 13.486  -4.516  54.410  1.00 27.11 ? 200 ALA A CA  1 
ATOM   1241 C  C   . ALA A 1 165 ? 14.515  -5.475  55.005  1.00 28.08 ? 200 ALA A C   1 
ATOM   1242 O  O   . ALA A 1 165 ? 15.294  -6.115  54.287  1.00 26.95 ? 200 ALA A O   1 
ATOM   1243 C  CB  . ALA A 1 165 ? 13.987  -3.072  54.489  1.00 25.97 ? 200 ALA A CB  1 
ATOM   1244 N  N   . MET A 1 166 ? 14.543  -5.573  56.326  1.00 31.55 ? 201 MET A N   1 
ATOM   1245 C  CA  . MET A 1 166 ? 15.440  -6.506  56.994  1.00 30.53 ? 201 MET A CA  1 
ATOM   1246 C  C   . MET A 1 166 ? 15.120  -7.943  56.611  1.00 32.65 ? 201 MET A C   1 
ATOM   1247 O  O   . MET A 1 166 ? 16.006  -8.712  56.209  1.00 30.34 ? 201 MET A O   1 
ATOM   1248 C  CB  . MET A 1 166 ? 15.293  -6.272  58.490  1.00 30.97 ? 201 MET A CB  1 
ATOM   1249 C  CG  . MET A 1 166 ? 15.975  -5.005  58.906  1.00 26.60 ? 201 MET A CG  1 
ATOM   1250 S  SD  . MET A 1 166 ? 15.757  -4.676  60.658  1.00 33.06 ? 201 MET A SD  1 
ATOM   1251 C  CE  . MET A 1 166 ? 15.802  -2.896  60.613  1.00 38.38 ? 201 MET A CE  1 
ATOM   1252 N  N   . ALA A 1 167 ? 13.837  -8.304  56.681  1.00 28.41 ? 202 ALA A N   1 
ATOM   1253 C  CA  . ALA A 1 167 ? 13.424  -9.654  56.357  1.00 29.88 ? 202 ALA A CA  1 
ATOM   1254 C  C   . ALA A 1 167 ? 13.706  -9.980  54.906  1.00 28.34 ? 202 ALA A C   1 
ATOM   1255 O  O   . ALA A 1 167 ? 14.006  -11.134 54.589  1.00 28.24 ? 202 ALA A O   1 
ATOM   1256 C  CB  . ALA A 1 167 ? 11.941  -9.838  56.679  1.00 28.20 ? 202 ALA A CB  1 
ATOM   1257 N  N   . SER A 1 168 ? 13.657  -8.981  54.017  1.00 25.31 ? 203 SER A N   1 
ATOM   1258 C  CA  . SER A 1 168 ? 13.831  -9.249  52.591  1.00 33.24 ? 203 SER A CA  1 
ATOM   1259 C  C   . SER A 1 168 ? 15.287  -9.272  52.130  1.00 31.49 ? 203 SER A C   1 
ATOM   1260 O  O   . SER A 1 168 ? 15.640  -10.109 51.279  1.00 25.13 ? 203 SER A O   1 
ATOM   1261 C  CB  . SER A 1 168 ? 13.026  -8.239  51.769  1.00 22.27 ? 203 SER A CB  1 
ATOM   1262 O  OG  . SER A 1 168 ? 11.655  -8.248  52.178  1.00 26.66 ? 203 SER A OG  1 
ATOM   1263 N  N   . LEU A 1 169 ? 16.144  -8.386  52.665  1.00 30.71 ? 204 LEU A N   1 
ATOM   1264 C  CA  . LEU A 1 169 ? 17.558  -8.336  52.274  1.00 25.34 ? 204 LEU A CA  1 
ATOM   1265 C  C   . LEU A 1 169 ? 18.519  -9.095  53.156  1.00 29.16 ? 204 LEU A C   1 
ATOM   1266 O  O   . LEU A 1 169 ? 19.514  -9.594  52.631  1.00 27.27 ? 204 LEU A O   1 
ATOM   1267 C  CB  . LEU A 1 169 ? 18.125  -6.922  52.187  1.00 27.74 ? 204 LEU A CB  1 
ATOM   1268 C  CG  . LEU A 1 169 ? 17.978  -6.173  50.890  1.00 35.75 ? 204 LEU A CG  1 
ATOM   1269 C  CD1 . LEU A 1 169 ? 18.514  -4.876  51.205  1.00 36.16 ? 204 LEU A CD1 1 
ATOM   1270 C  CD2 . LEU A 1 169 ? 18.908  -6.860  49.922  1.00 34.55 ? 204 LEU A CD2 1 
ATOM   1271 N  N   . ASN A 1 170 ? 18.343  -9.106  54.479  1.00 31.43 ? 205 ASN A N   1 
ATOM   1272 C  CA  . ASN A 1 170 ? 19.344  -9.754  55.317  1.00 24.86 ? 205 ASN A CA  1 
ATOM   1273 C  C   . ASN A 1 170 ? 19.654  -11.190 54.903  1.00 30.56 ? 205 ASN A C   1 
ATOM   1274 O  O   . ASN A 1 170 ? 20.832  -11.576 54.995  1.00 31.54 ? 205 ASN A O   1 
ATOM   1275 C  CB  . ASN A 1 170 ? 18.922  -9.651  56.790  1.00 28.79 ? 205 ASN A CB  1 
ATOM   1276 C  CG  . ASN A 1 170 ? 19.149  -8.260  57.342  1.00 35.47 ? 205 ASN A CG  1 
ATOM   1277 O  OD1 . ASN A 1 170 ? 19.900  -7.487  56.752  1.00 37.43 ? 205 ASN A OD1 1 
ATOM   1278 N  ND2 . ASN A 1 170 ? 18.495  -7.924  58.450  1.00 32.01 ? 205 ASN A ND2 1 
ATOM   1279 N  N   . PRO A 1 171 ? 18.699  -12.010 54.436  1.00 29.69 ? 206 PRO A N   1 
ATOM   1280 C  CA  . PRO A 1 171 ? 19.084  -13.341 53.926  1.00 34.21 ? 206 PRO A CA  1 
ATOM   1281 C  C   . PRO A 1 171 ? 20.121  -13.299 52.808  1.00 32.28 ? 206 PRO A C   1 
ATOM   1282 O  O   . PRO A 1 171 ? 20.978  -14.200 52.730  1.00 32.88 ? 206 PRO A O   1 
ATOM   1283 C  CB  . PRO A 1 171 ? 17.748  -13.916 53.436  1.00 31.49 ? 206 PRO A CB  1 
ATOM   1284 C  CG  . PRO A 1 171 ? 16.742  -13.274 54.304  1.00 30.38 ? 206 PRO A CG  1 
ATOM   1285 C  CD  . PRO A 1 171 ? 17.227  -11.859 54.451  1.00 30.50 ? 206 PRO A CD  1 
ATOM   1286 N  N   . TYR A 1 172 ? 20.044  -12.302 51.913  1.00 31.25 ? 207 TYR A N   1 
ATOM   1287 C  CA  . TYR A 1 172 ? 21.056  -12.176 50.869  1.00 25.41 ? 207 TYR A CA  1 
ATOM   1288 C  C   . TYR A 1 172 ? 22.353  -11.612 51.434  1.00 30.06 ? 207 TYR A C   1 
ATOM   1289 O  O   . TYR A 1 172 ? 23.442  -12.045 51.041  1.00 29.97 ? 207 TYR A O   1 
ATOM   1290 C  CB  . TYR A 1 172 ? 20.561  -11.293 49.729  1.00 22.72 ? 207 TYR A CB  1 
ATOM   1291 C  CG  . TYR A 1 172 ? 19.421  -11.890 48.922  1.00 25.79 ? 207 TYR A CG  1 
ATOM   1292 C  CD1 . TYR A 1 172 ? 18.121  -11.864 49.411  1.00 29.42 ? 207 TYR A CD1 1 
ATOM   1293 C  CD2 . TYR A 1 172 ? 19.634  -12.472 47.674  1.00 29.80 ? 207 TYR A CD2 1 
ATOM   1294 C  CE1 . TYR A 1 172 ? 17.053  -12.400 48.683  1.00 28.92 ? 207 TYR A CE1 1 
ATOM   1295 C  CE2 . TYR A 1 172 ? 18.570  -13.009 46.931  1.00 26.95 ? 207 TYR A CE2 1 
ATOM   1296 C  CZ  . TYR A 1 172 ? 17.281  -12.967 47.448  1.00 26.88 ? 207 TYR A CZ  1 
ATOM   1297 O  OH  . TYR A 1 172 ? 16.213  -13.481 46.741  1.00 30.24 ? 207 TYR A OH  1 
ATOM   1298 N  N   . VAL A 1 173 ? 22.263  -10.656 52.365  1.00 26.47 ? 208 VAL A N   1 
ATOM   1299 C  CA  . VAL A 1 173 ? 23.474  -10.160 53.024  1.00 29.63 ? 208 VAL A CA  1 
ATOM   1300 C  C   . VAL A 1 173 ? 24.250  -11.312 53.646  1.00 28.73 ? 208 VAL A C   1 
ATOM   1301 O  O   . VAL A 1 173 ? 25.462  -11.438 53.448  1.00 33.57 ? 208 VAL A O   1 
ATOM   1302 C  CB  . VAL A 1 173 ? 23.135  -9.098  54.084  1.00 32.26 ? 208 VAL A CB  1 
ATOM   1303 C  CG1 . VAL A 1 173 ? 24.403  -8.656  54.793  1.00 28.28 ? 208 VAL A CG1 1 
ATOM   1304 C  CG2 . VAL A 1 173 ? 22.428  -7.909  53.452  1.00 27.61 ? 208 VAL A CG2 1 
ATOM   1305 N  N   . LYS A 1 174 ? 23.565  -12.177 54.404  1.00 34.98 ? 209 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 174 ? 24.255  -13.286 55.068  1.00 31.64 ? 209 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 174 ? 24.786  -14.321 54.084  1.00 35.09 ? 209 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 174 ? 25.750  -15.025 54.408  1.00 42.75 ? 209 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 174 ? 23.355  -13.981 56.100  1.00 33.65 ? 209 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 174 ? 22.426  -13.085 56.919  1.00 39.89 ? 209 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 174 ? 23.065  -12.587 58.217  1.00 45.32 ? 209 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 174 ? 22.464  -11.250 58.687  1.00 46.99 ? 209 LYS A CE  1 
ATOM   1313 N  NZ  . LYS A 1 174 ? 23.144  -10.058 58.083  1.00 42.14 ? 209 LYS A NZ  1 
ATOM   1314 N  N   . ALA A 1 175 ? 24.194  -14.428 52.899  1.00 36.15 ? 210 ALA A N   1 
ATOM   1315 C  CA  . ALA A 1 175 ? 24.694  -15.332 51.874  1.00 36.80 ? 210 ALA A CA  1 
ATOM   1316 C  C   . ALA A 1 175 ? 25.830  -14.725 51.059  1.00 36.41 ? 210 ALA A C   1 
ATOM   1317 O  O   . ALA A 1 175 ? 26.342  -15.391 50.150  1.00 36.01 ? 210 ALA A O   1 
ATOM   1318 C  CB  . ALA A 1 175 ? 23.552  -15.757 50.947  1.00 32.67 ? 210 ALA A CB  1 
ATOM   1319 N  N   . GLY A 1 176 ? 26.251  -13.498 51.379  1.00 29.41 ? 211 GLY A N   1 
ATOM   1320 C  CA  . GLY A 1 176 ? 27.273  -12.820 50.611  1.00 32.68 ? 211 GLY A CA  1 
ATOM   1321 C  C   . GLY A 1 176 ? 26.802  -12.255 49.290  1.00 34.05 ? 211 GLY A C   1 
ATOM   1322 O  O   . GLY A 1 176 ? 27.621  -12.032 48.393  1.00 33.68 ? 211 GLY A O   1 
ATOM   1323 N  N   . LYS A 1 177 ? 25.500  -12.010 49.141  1.00 30.16 ? 212 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 177 ? 24.918  -11.674 47.843  1.00 29.06 ? 212 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 177 ? 24.447  -10.230 47.719  1.00 27.59 ? 212 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 177 ? 23.898  -9.863  46.669  1.00 30.31 ? 212 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 177 ? 23.736  -12.603 47.553  1.00 28.55 ? 212 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 177 ? 24.141  -14.035 47.347  1.00 37.69 ? 212 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 177 ? 22.952  -14.932 47.087  1.00 40.90 ? 212 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 177 ? 23.441  -16.358 46.864  1.00 44.86 ? 212 LYS A CE  1 
ATOM   1331 N  NZ  . LYS A 1 177 ? 22.335  -17.288 46.629  1.00 45.12 ? 212 LYS A NZ  1 
ATOM   1332 N  N   . PHE A 1 178 ? 24.606  -9.399  48.745  1.00 26.15 ? 213 PHE A N   1 
ATOM   1333 C  CA  . PHE A 1 178 ? 24.258  -7.988  48.623  1.00 28.03 ? 213 PHE A CA  1 
ATOM   1334 C  C   . PHE A 1 178 ? 25.510  -7.185  48.279  1.00 33.69 ? 213 PHE A C   1 
ATOM   1335 O  O   . PHE A 1 178 ? 26.460  -7.120  49.076  1.00 30.37 ? 213 PHE A O   1 
ATOM   1336 C  CB  . PHE A 1 178 ? 23.630  -7.440  49.900  1.00 25.76 ? 213 PHE A CB  1 
ATOM   1337 C  CG  . PHE A 1 178 ? 23.246  -6.017  49.777  1.00 28.21 ? 213 PHE A CG  1 
ATOM   1338 C  CD1 . PHE A 1 178 ? 22.259  -5.638  48.873  1.00 27.07 ? 213 PHE A CD1 1 
ATOM   1339 C  CD2 . PHE A 1 178 ? 23.946  -5.036  50.473  1.00 30.89 ? 213 PHE A CD2 1 
ATOM   1340 C  CE1 . PHE A 1 178 ? 21.909  -4.317  48.722  1.00 23.57 ? 213 PHE A CE1 1 
ATOM   1341 C  CE2 . PHE A 1 178 ? 23.603  -3.697  50.324  1.00 29.62 ? 213 PHE A CE2 1 
ATOM   1342 C  CZ  . PHE A 1 178 ? 22.584  -3.341  49.437  1.00 25.64 ? 213 PHE A CZ  1 
ATOM   1343 N  N   . LYS A 1 179 ? 25.517  -6.566  47.100  1.00 23.67 ? 214 LYS A N   1 
ATOM   1344 C  CA  . LYS A 1 179 ? 26.672  -5.778  46.678  1.00 32.13 ? 214 LYS A CA  1 
ATOM   1345 C  C   . LYS A 1 179 ? 26.202  -4.343  46.478  1.00 23.66 ? 214 LYS A C   1 
ATOM   1346 O  O   . LYS A 1 179 ? 25.711  -3.982  45.397  1.00 22.38 ? 214 LYS A O   1 
ATOM   1347 C  CB  . LYS A 1 179 ? 27.292  -6.344  45.406  1.00 29.56 ? 214 LYS A CB  1 
ATOM   1348 C  CG  . LYS A 1 179 ? 27.710  -7.792  45.537  1.00 38.99 ? 214 LYS A CG  1 
ATOM   1349 C  CD  . LYS A 1 179 ? 28.826  -8.035  46.520  1.00 42.52 ? 214 LYS A CD  1 
ATOM   1350 C  CE  . LYS A 1 179 ? 29.171  -9.515  46.544  1.00 40.73 ? 214 LYS A CE  1 
ATOM   1351 N  NZ  . LYS A 1 179 ? 30.231  -9.814  47.543  1.00 51.20 ? 214 LYS A NZ  1 
ATOM   1352 N  N   . PRO A 1 180 ? 26.343  -3.484  47.479  1.00 23.72 ? 215 PRO A N   1 
ATOM   1353 C  CA  . PRO A 1 180 ? 25.897  -2.098  47.315  1.00 21.03 ? 215 PRO A CA  1 
ATOM   1354 C  C   . PRO A 1 180 ? 26.793  -1.333  46.350  1.00 24.41 ? 215 PRO A C   1 
ATOM   1355 O  O   . PRO A 1 180 ? 27.934  -1.722  46.061  1.00 27.06 ? 215 PRO A O   1 
ATOM   1356 C  CB  . PRO A 1 180 ? 25.989  -1.531  48.736  1.00 20.77 ? 215 PRO A CB  1 
ATOM   1357 C  CG  . PRO A 1 180 ? 27.090  -2.316  49.350  1.00 36.57 ? 215 PRO A CG  1 
ATOM   1358 C  CD  . PRO A 1 180 ? 26.913  -3.716  48.818  1.00 25.33 ? 215 PRO A CD  1 
ATOM   1359 N  N   . PHE A 1 181 ? 26.251  -0.224  45.855  1.00 25.65 ? 216 PHE A N   1 
ATOM   1360 C  CA  . PHE A 1 181 ? 26.989  0.798   45.119  1.00 28.27 ? 216 PHE A CA  1 
ATOM   1361 C  C   . PHE A 1 181 ? 26.785  2.145   45.796  1.00 25.46 ? 216 PHE A C   1 
ATOM   1362 O  O   . PHE A 1 181 ? 25.992  2.273   46.731  1.00 27.36 ? 216 PHE A O   1 
ATOM   1363 C  CB  . PHE A 1 181 ? 26.562  0.845   43.647  1.00 18.33 ? 216 PHE A CB  1 
ATOM   1364 C  CG  . PHE A 1 181 ? 25.092  0.995   43.455  1.00 21.01 ? 216 PHE A CG  1 
ATOM   1365 C  CD1 . PHE A 1 181 ? 24.467  2.224   43.615  1.00 19.90 ? 216 PHE A CD1 1 
ATOM   1366 C  CD2 . PHE A 1 181 ? 24.330  -0.102  43.146  1.00 19.43 ? 216 PHE A CD2 1 
ATOM   1367 C  CE1 . PHE A 1 181 ? 23.081  2.350   43.450  1.00 23.11 ? 216 PHE A CE1 1 
ATOM   1368 C  CE2 . PHE A 1 181 ? 22.953  0.010   42.972  1.00 18.13 ? 216 PHE A CE2 1 
ATOM   1369 C  CZ  . PHE A 1 181 ? 22.331  1.248   43.128  1.00 24.49 ? 216 PHE A CZ  1 
ATOM   1370 N  N   . SER A 1 182 ? 27.512  3.163   45.325  1.00 22.37 ? 217 SER A N   1 
ATOM   1371 C  CA  . SER A 1 182 ? 27.384  4.518   45.867  1.00 28.89 ? 217 SER A CA  1 
ATOM   1372 C  C   . SER A 1 182 ? 27.181  5.513   44.739  1.00 34.97 ? 217 SER A C   1 
ATOM   1373 O  O   . SER A 1 182 ? 28.101  5.745   43.948  1.00 34.60 ? 217 SER A O   1 
ATOM   1374 C  CB  . SER A 1 182 ? 28.612  4.913   46.665  1.00 34.20 ? 217 SER A CB  1 
ATOM   1375 O  OG  . SER A 1 182 ? 28.523  6.200   47.234  1.00 33.50 ? 217 SER A OG  1 
ATOM   1376 N  N   . GLY A 1 183 ? 26.007  6.138   44.706  1.00 31.57 ? 218 GLY A N   1 
ATOM   1377 C  CA  . GLY A 1 183 ? 25.711  7.142   43.709  1.00 29.76 ? 218 GLY A CA  1 
ATOM   1378 C  C   . GLY A 1 183 ? 25.765  6.557   42.309  1.00 24.93 ? 218 GLY A C   1 
ATOM   1379 O  O   . GLY A 1 183 ? 25.538  5.352   42.085  1.00 29.60 ? 218 GLY A O   1 
ATOM   1380 N  N   . ASN A 1 184 ? 26.078  7.426   41.355  1.00 21.21 ? 219 ASN A N   1 
ATOM   1381 C  CA  . ASN A 1 184 ? 26.149  7.058   39.946  1.00 21.39 ? 219 ASN A CA  1 
ATOM   1382 C  C   . ASN A 1 184 ? 27.198  5.980   39.738  1.00 27.83 ? 219 ASN A C   1 
ATOM   1383 O  O   . ASN A 1 184 ? 28.380  6.193   40.042  1.00 29.79 ? 219 ASN A O   1 
ATOM   1384 C  CB  . ASN A 1 184 ? 26.500  8.279   39.100  1.00 26.29 ? 219 ASN A CB  1 
ATOM   1385 C  CG  . ASN A 1 184 ? 25.457  9.382   39.180  1.00 31.66 ? 219 ASN A CG  1 
ATOM   1386 O  OD1 . ASN A 1 184 ? 24.372  9.221   39.742  1.00 28.41 ? 219 ASN A OD1 1 
ATOM   1387 N  ND2 . ASN A 1 184 ? 25.788  10.508  38.602  1.00 31.16 ? 219 ASN A ND2 1 
ATOM   1388 N  N   . THR A 1 185 ? 26.767  4.842   39.192  1.00 23.04 ? 220 THR A N   1 
ATOM   1389 C  CA  . THR A 1 185 ? 27.576  3.633   39.098  1.00 30.85 ? 220 THR A CA  1 
ATOM   1390 C  C   . THR A 1 185 ? 27.243  2.857   37.834  1.00 24.67 ? 220 THR A C   1 
ATOM   1391 O  O   . THR A 1 185 ? 26.075  2.547   37.568  1.00 25.12 ? 220 THR A O   1 
ATOM   1392 C  CB  . THR A 1 185 ? 27.369  2.721   40.318  1.00 24.91 ? 220 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 185 ? 27.655  3.450   41.515  1.00 31.36 ? 220 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 185 ? 28.285  1.506   40.237  1.00 26.13 ? 220 THR A CG2 1 
ATOM   1395 N  N   . ASP A 1 186 ? 28.273  2.548   37.058  1.00 25.46 ? 221 ASP A N   1 
ATOM   1396 C  CA  . ASP A 1 186 ? 28.106  1.630   35.945  1.00 29.17 ? 221 ASP A CA  1 
ATOM   1397 C  C   . ASP A 1 186 ? 27.977  0.212   36.490  1.00 31.51 ? 221 ASP A C   1 
ATOM   1398 O  O   . ASP A 1 186 ? 28.895  -0.306  37.137  1.00 29.85 ? 221 ASP A O   1 
ATOM   1399 C  CB  . ASP A 1 186 ? 29.285  1.739   34.977  1.00 26.13 ? 221 ASP A CB  1 
ATOM   1400 C  CG  . ASP A 1 186 ? 29.217  2.988   34.096  1.00 35.93 ? 221 ASP A CG  1 
ATOM   1401 O  OD1 . ASP A 1 186 ? 28.271  3.796   34.250  1.00 35.78 ? 221 ASP A OD1 1 
ATOM   1402 O  OD2 . ASP A 1 186 ? 30.132  3.163   33.252  1.00 36.52 ? 221 ASP A OD2 1 
ATOM   1403 N  N   . LEU A 1 187 ? 26.815  -0.390  36.270  1.00 27.71 ? 222 LEU A N   1 
ATOM   1404 C  CA  . LEU A 1 187 ? 26.519  -1.764  36.642  1.00 29.58 ? 222 LEU A CA  1 
ATOM   1405 C  C   . LEU A 1 187 ? 26.820  -2.642  35.436  1.00 36.08 ? 222 LEU A C   1 
ATOM   1406 O  O   . LEU A 1 187 ? 27.774  -2.373  34.696  1.00 45.20 ? 222 LEU A O   1 
ATOM   1407 C  CB  . LEU A 1 187 ? 25.073  -1.897  37.134  1.00 26.90 ? 222 LEU A CB  1 
ATOM   1408 C  CG  . LEU A 1 187 ? 24.721  -0.883  38.231  1.00 22.14 ? 222 LEU A CG  1 
ATOM   1409 C  CD1 . LEU A 1 187 ? 23.246  -1.021  38.657  1.00 23.39 ? 222 LEU A CD1 1 
ATOM   1410 C  CD2 . LEU A 1 187 ? 25.676  -1.004  39.429  1.00 29.25 ? 222 LEU A CD2 1 
ATOM   1411 N  N   . VAL A 1 188 ? 26.119  -3.759  35.314  1.00 33.23 ? 223 VAL A N   1 
ATOM   1412 C  CA  . VAL A 1 188 ? 26.097  -4.562  34.092  1.00 26.88 ? 223 VAL A CA  1 
ATOM   1413 C  C   . VAL A 1 188 ? 26.166  -3.660  32.859  1.00 31.54 ? 223 VAL A C   1 
ATOM   1414 O  O   . VAL A 1 188 ? 25.492  -2.617  32.828  1.00 29.39 ? 223 VAL A O   1 
ATOM   1415 C  CB  . VAL A 1 188 ? 24.828  -5.434  34.087  1.00 29.89 ? 223 VAL A CB  1 
ATOM   1416 C  CG1 . VAL A 1 188 ? 24.357  -5.745  32.685  1.00 36.71 ? 223 VAL A CG1 1 
ATOM   1417 C  CG2 . VAL A 1 188 ? 25.075  -6.725  34.878  1.00 35.83 ? 223 VAL A CG2 1 
ATOM   1418 N  N   . PRO A 1 189 ? 27.019  -3.987  31.837  1.00 30.62 ? 224 PRO A N   1 
ATOM   1419 C  CA  . PRO A 1 189 ? 26.988  -3.243  30.568  1.00 31.81 ? 224 PRO A CA  1 
ATOM   1420 C  C   . PRO A 1 189 ? 25.575  -3.004  30.073  1.00 26.15 ? 224 PRO A C   1 
ATOM   1421 O  O   . PRO A 1 189 ? 24.818  -3.952  29.882  1.00 26.32 ? 224 PRO A O   1 
ATOM   1422 C  CB  . PRO A 1 189 ? 27.756  -4.162  29.609  1.00 32.24 ? 224 PRO A CB  1 
ATOM   1423 C  CG  . PRO A 1 189 ? 28.762  -4.821  30.494  1.00 34.91 ? 224 PRO A CG  1 
ATOM   1424 C  CD  . PRO A 1 189 ? 28.013  -5.078  31.798  1.00 27.73 ? 224 PRO A CD  1 
ATOM   1425 N  N   . GLY A 1 190 ? 25.213  -1.747  29.860  1.00 32.59 ? 225 GLY A N   1 
ATOM   1426 C  CA  . GLY A 1 190 ? 23.878  -1.388  29.439  1.00 25.00 ? 225 GLY A CA  1 
ATOM   1427 C  C   . GLY A 1 190 ? 23.001  -0.859  30.545  1.00 23.60 ? 225 GLY A C   1 
ATOM   1428 O  O   . GLY A 1 190 ? 21.939  -0.306  30.254  1.00 23.77 ? 225 GLY A O   1 
ATOM   1429 N  N   . ILE A 1 191 ? 23.385  -1.032  31.802  1.00 21.68 ? 226 ILE A N   1 
ATOM   1430 C  CA  . ILE A 1 191 ? 22.564  -0.552  32.903  1.00 22.56 ? 226 ILE A CA  1 
ATOM   1431 C  C   . ILE A 1 191 ? 23.445  0.276   33.830  1.00 25.38 ? 226 ILE A C   1 
ATOM   1432 O  O   . ILE A 1 191 ? 24.534  -0.167  34.222  1.00 23.90 ? 226 ILE A O   1 
ATOM   1433 C  CB  . ILE A 1 191 ? 21.898  -1.707  33.666  1.00 21.33 ? 226 ILE A CB  1 
ATOM   1434 C  CG1 . ILE A 1 191 ? 21.034  -2.552  32.722  1.00 24.40 ? 226 ILE A CG1 1 
ATOM   1435 C  CG2 . ILE A 1 191 ? 20.937  -1.127  34.710  1.00 23.73 ? 226 ILE A CG2 1 
ATOM   1436 C  CD1 . ILE A 1 191 ? 20.560  -3.833  33.345  1.00 18.75 ? 226 ILE A CD1 1 
ATOM   1437 N  N   . LYS A 1 192 ? 22.979  1.477   34.164  1.00 21.65 ? 227 LYS A N   1 
ATOM   1438 C  CA  . LYS A 1 192 ? 23.675  2.409   35.041  1.00 22.13 ? 227 LYS A CA  1 
ATOM   1439 C  C   . LYS A 1 192 ? 22.779  2.767   36.215  1.00 29.48 ? 227 LYS A C   1 
ATOM   1440 O  O   . LYS A 1 192 ? 21.566  2.953   36.052  1.00 22.47 ? 227 LYS A O   1 
ATOM   1441 C  CB  . LYS A 1 192 ? 24.017  3.702   34.301  1.00 24.64 ? 227 LYS A CB  1 
ATOM   1442 C  CG  . LYS A 1 192 ? 24.981  3.582   33.155  1.00 32.42 ? 227 LYS A CG  1 
ATOM   1443 C  CD  . LYS A 1 192 ? 25.073  4.951   32.449  1.00 35.47 ? 227 LYS A CD  1 
ATOM   1444 C  CE  . LYS A 1 192 ? 26.441  5.292   31.892  1.00 44.05 ? 227 LYS A CE  1 
ATOM   1445 N  NZ  . LYS A 1 192 ? 26.294  6.401   30.896  1.00 43.91 ? 227 LYS A NZ  1 
ATOM   1446 N  N   . ALA A 1 193 ? 23.372  2.890   37.392  1.00 22.65 ? 228 ALA A N   1 
ATOM   1447 C  CA  . ALA A 1 193 ? 22.669  3.466   38.525  1.00 19.84 ? 228 ALA A CA  1 
ATOM   1448 C  C   . ALA A 1 193 ? 22.849  4.980   38.500  1.00 22.83 ? 228 ALA A C   1 
ATOM   1449 O  O   . ALA A 1 193 ? 23.974  5.483   38.355  1.00 23.24 ? 228 ALA A O   1 
ATOM   1450 C  CB  . ALA A 1 193 ? 23.169  2.866   39.849  1.00 20.99 ? 228 ALA A CB  1 
ATOM   1451 N  N   . LEU A 1 194 ? 21.732  5.703   38.610  1.00 19.26 ? 229 LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 194 ? 21.721  7.155   38.702  1.00 25.12 ? 229 LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 194 ? 21.059  7.574   40.014  1.00 21.47 ? 229 LEU A C   1 
ATOM   1454 O  O   . LEU A 1 194 ? 19.893  7.253   40.249  1.00 19.34 ? 229 LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 194 ? 20.967  7.741   37.512  1.00 23.48 ? 229 LEU A CB  1 
ATOM   1456 C  CG  . LEU A 1 194 ? 20.827  9.247   37.582  1.00 32.39 ? 229 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A 1 194 ? 22.148  9.873   37.085  1.00 29.67 ? 229 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A 1 194 ? 19.635  9.677   36.749  1.00 27.37 ? 229 LEU A CD2 1 
ATOM   1459 N  N   . ALA A 1 195 ? 21.775  8.339   40.829  1.00 20.78 ? 230 ALA A N   1 
ATOM   1460 C  CA  . ALA A 1 195 ? 21.275  8.720   42.149  1.00 20.90 ? 230 ALA A CA  1 
ATOM   1461 C  C   . ALA A 1 195 ? 20.109  9.689   42.009  1.00 20.48 ? 230 ALA A C   1 
ATOM   1462 O  O   . ALA A 1 195 ? 20.237  10.732  41.370  1.00 24.57 ? 230 ALA A O   1 
ATOM   1463 C  CB  . ALA A 1 195 ? 22.391  9.354   42.963  1.00 26.70 ? 230 ALA A CB  1 
ATOM   1464 N  N   . SER A 1 196 ? 18.970  9.338   42.594  1.00 19.91 ? 231 SER A N   1 
ATOM   1465 C  CA  . SER A 1 196 ? 17.769  10.165  42.604  1.00 24.79 ? 231 SER A CA  1 
ATOM   1466 C  C   . SER A 1 196 ? 17.224  10.223  44.017  1.00 24.54 ? 231 SER A C   1 
ATOM   1467 O  O   . SER A 1 196 ? 16.058  9.925   44.290  1.00 22.18 ? 231 SER A O   1 
ATOM   1468 C  CB  . SER A 1 196 ? 16.731  9.668   41.602  1.00 24.21 ? 231 SER A CB  1 
ATOM   1469 O  OG  . SER A 1 196 ? 16.317  8.340   41.887  1.00 22.45 ? 231 SER A OG  1 
ATOM   1470 N  N   . HIS A 1 197 ? 18.121  10.557  44.941  1.00 27.04 ? 232 HIS A N   1 
ATOM   1471 C  CA  . HIS A 1 197 ? 17.808  10.463  46.357  1.00 27.00 ? 232 HIS A CA  1 
ATOM   1472 C  C   . HIS A 1 197 ? 16.704  11.425  46.760  1.00 29.43 ? 232 HIS A C   1 
ATOM   1473 O  O   . HIS A 1 197 ? 16.680  12.594  46.341  1.00 22.96 ? 232 HIS A O   1 
ATOM   1474 C  CB  . HIS A 1 197 ? 19.043  10.738  47.225  1.00 24.16 ? 232 HIS A CB  1 
ATOM   1475 C  CG  . HIS A 1 197 ? 20.239  9.891   46.889  1.00 25.73 ? 232 HIS A CG  1 
ATOM   1476 N  ND1 . HIS A 1 197 ? 20.134  8.644   46.301  1.00 21.86 ? 232 HIS A ND1 1 
ATOM   1477 C  CD2 . HIS A 1 197 ? 21.553  10.062  47.168  1.00 21.09 ? 232 HIS A CD2 1 
ATOM   1478 C  CE1 . HIS A 1 197 ? 21.342  8.112   46.180  1.00 22.09 ? 232 HIS A CE1 1 
ATOM   1479 N  NE2 . HIS A 1 197 ? 22.217  8.952   46.698  1.00 27.43 ? 232 HIS A NE2 1 
ATOM   1480 N  N   . GLY A 1 198 ? 15.853  10.945  47.668  1.00 21.47 ? 233 GLY A N   1 
ATOM   1481 C  CA  . GLY A 1 198 ? 14.953  11.829  48.387  1.00 29.78 ? 233 GLY A CA  1 
ATOM   1482 C  C   . GLY A 1 198 ? 13.591  11.241  48.699  1.00 25.58 ? 233 GLY A C   1 
ATOM   1483 O  O   . GLY A 1 198 ? 13.045  11.501  49.771  1.00 26.73 ? 233 GLY A O   1 
ATOM   1484 N  N   . HIS A 1 199 ? 13.071  10.366  47.852  1.00 21.67 ? 234 HIS A N   1 
ATOM   1485 C  CA  . HIS A 1 199 ? 11.884  9.571   48.257  1.00 26.43 ? 234 HIS A CA  1 
ATOM   1486 C  C   . HIS A 1 199 ? 12.388  8.708   49.412  1.00 22.16 ? 234 HIS A C   1 
ATOM   1487 O  O   . HIS A 1 199 ? 11.665  8.535   50.404  1.00 24.08 ? 234 HIS A O   1 
ATOM   1488 C  CB  . HIS A 1 199 ? 11.415  8.689   47.103  1.00 22.84 ? 234 HIS A CB  1 
ATOM   1489 C  CG  . HIS A 1 199 ? 10.358  7.705   47.452  1.00 23.81 ? 234 HIS A CG  1 
ATOM   1490 N  ND1 . HIS A 1 199 ? 9.122   8.067   47.940  1.00 26.64 ? 234 HIS A ND1 1 
ATOM   1491 C  CD2 . HIS A 1 199 ? 10.348  6.374   47.363  1.00 19.01 ? 234 HIS A CD2 1 
ATOM   1492 C  CE1 . HIS A 1 199 ? 8.400   6.978   48.141  1.00 24.71 ? 234 HIS A CE1 1 
ATOM   1493 N  NE2 . HIS A 1 199 ? 9.125   5.941   47.795  1.00 23.08 ? 234 HIS A NE2 1 
ATOM   1494 N  N   . THR A 1 200 ? 13.586  8.133   49.246  1.00 20.48 ? 235 THR A N   1 
ATOM   1495 C  CA  . THR A 1 200 ? 14.275  7.416   50.327  1.00 20.21 ? 235 THR A CA  1 
ATOM   1496 C  C   . THR A 1 200 ? 15.704  7.941   50.310  1.00 21.91 ? 235 THR A C   1 
ATOM   1497 O  O   . THR A 1 200 ? 16.124  8.491   49.294  1.00 23.40 ? 235 THR A O   1 
ATOM   1498 C  CB  . THR A 1 200 ? 14.238  5.904   50.125  1.00 20.71 ? 235 THR A CB  1 
ATOM   1499 O  OG1 . THR A 1 200 ? 14.858  5.640   48.871  1.00 22.23 ? 235 THR A OG1 1 
ATOM   1500 C  CG2 . THR A 1 200 ? 12.824  5.353   50.163  1.00 18.82 ? 235 THR A CG2 1 
ATOM   1501 N  N   . PRO A 1 201 ? 16.466  7.836   51.409  1.00 23.03 ? 236 PRO A N   1 
ATOM   1502 C  CA  . PRO A 1 201 ? 17.826  8.355   51.420  1.00 29.08 ? 236 PRO A CA  1 
ATOM   1503 C  C   . PRO A 1 201 ? 18.740  7.837   50.295  1.00 24.25 ? 236 PRO A C   1 
ATOM   1504 O  O   . PRO A 1 201 ? 19.703  8.521   49.933  1.00 23.48 ? 236 PRO A O   1 
ATOM   1505 C  CB  . PRO A 1 201 ? 18.310  7.913   52.804  1.00 27.53 ? 236 PRO A CB  1 
ATOM   1506 C  CG  . PRO A 1 201 ? 17.054  7.905   53.638  1.00 22.86 ? 236 PRO A CG  1 
ATOM   1507 C  CD  . PRO A 1 201 ? 16.041  7.297   52.690  1.00 23.11 ? 236 PRO A CD  1 
ATOM   1508 N  N   . GLY A 1 202 ? 18.438  6.660   49.748  1.00 23.47 ? 237 GLY A N   1 
ATOM   1509 C  CA  . GLY A 1 202 ? 19.244  6.140   48.656  1.00 22.83 ? 237 GLY A CA  1 
ATOM   1510 C  C   . GLY A 1 202 ? 18.489  5.736   47.401  1.00 22.75 ? 237 GLY A C   1 
ATOM   1511 O  O   . GLY A 1 202 ? 18.969  4.905   46.615  1.00 18.51 ? 237 GLY A O   1 
ATOM   1512 N  N   . HIS A 1 203 ? 17.314  6.323   47.187  1.00 20.61 ? 238 HIS A N   1 
ATOM   1513 C  CA  . HIS A 1 203 ? 16.514  5.977   46.018  1.00 20.40 ? 238 HIS A CA  1 
ATOM   1514 C  C   . HIS A 1 203 ? 17.329  6.172   44.749  1.00 20.73 ? 238 HIS A C   1 
ATOM   1515 O  O   . HIS A 1 203 ? 17.956  7.221   44.547  1.00 21.42 ? 238 HIS A O   1 
ATOM   1516 C  CB  . HIS A 1 203 ? 15.263  6.850   45.926  1.00 17.11 ? 238 HIS A CB  1 
ATOM   1517 C  CG  . HIS A 1 203 ? 14.369  6.483   44.783  1.00 21.57 ? 238 HIS A CG  1 
ATOM   1518 N  ND1 . HIS A 1 203 ? 14.609  6.902   43.492  1.00 23.32 ? 238 HIS A ND1 1 
ATOM   1519 C  CD2 . HIS A 1 203 ? 13.170  5.851   44.755  1.00 18.22 ? 238 HIS A CD2 1 
ATOM   1520 C  CE1 . HIS A 1 203 ? 13.650  6.448   42.698  1.00 19.61 ? 238 HIS A CE1 1 
ATOM   1521 N  NE2 . HIS A 1 203 ? 12.758  5.823   43.443  1.00 16.93 ? 238 HIS A NE2 1 
ATOM   1522 N  N   . THR A 1 204 ? 17.271  5.189   43.868  1.00 20.97 ? 239 THR A N   1 
ATOM   1523 C  CA  . THR A 1 204 ? 18.112  5.170   42.690  1.00 18.27 ? 239 THR A CA  1 
ATOM   1524 C  C   . THR A 1 204 ? 17.269  4.878   41.465  1.00 17.32 ? 239 THR A C   1 
ATOM   1525 O  O   . THR A 1 204 ? 16.336  4.062   41.513  1.00 17.65 ? 239 THR A O   1 
ATOM   1526 C  CB  . THR A 1 204 ? 19.244  4.128   42.864  1.00 24.04 ? 239 THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 204 ? 20.026  4.462   44.025  1.00 20.49 ? 239 THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 204 ? 20.199  4.107   41.646  1.00 19.21 ? 239 THR A CG2 1 
ATOM   1529 N  N   . THR A 1 205 ? 17.602  5.566   40.378  1.00 18.19 ? 240 THR A N   1 
ATOM   1530 C  CA  . THR A 1 205 ? 17.032  5.374   39.058  1.00 16.20 ? 240 THR A CA  1 
ATOM   1531 C  C   . THR A 1 205 ? 17.979  4.468   38.297  1.00 20.61 ? 240 THR A C   1 
ATOM   1532 O  O   . THR A 1 205 ? 19.194  4.607   38.427  1.00 20.69 ? 240 THR A O   1 
ATOM   1533 C  CB  . THR A 1 205 ? 16.915  6.737   38.345  1.00 18.72 ? 240 THR A CB  1 
ATOM   1534 O  OG1 . THR A 1 205 ? 15.981  7.582   39.037  1.00 20.91 ? 240 THR A OG1 1 
ATOM   1535 C  CG2 . THR A 1 205 ? 16.487  6.591   36.881  1.00 19.90 ? 240 THR A CG2 1 
ATOM   1536 N  N   . TYR A 1 206 ? 17.444  3.538   37.512  1.00 16.88 ? 241 TYR A N   1 
ATOM   1537 C  CA  . TYR A 1 206 ? 18.290  2.662   36.698  1.00 15.78 ? 241 TYR A CA  1 
ATOM   1538 C  C   . TYR A 1 206 ? 18.089  3.008   35.229  1.00 15.66 ? 241 TYR A C   1 
ATOM   1539 O  O   . TYR A 1 206 ? 16.961  3.012   34.728  1.00 17.68 ? 241 TYR A O   1 
ATOM   1540 C  CB  . TYR A 1 206 ? 17.997  1.182   37.001  1.00 16.72 ? 241 TYR A CB  1 
ATOM   1541 C  CG  . TYR A 1 206 ? 18.380  0.861   38.421  1.00 15.76 ? 241 TYR A CG  1 
ATOM   1542 C  CD1 . TYR A 1 206 ? 19.731  0.682   38.788  1.00 16.98 ? 241 TYR A CD1 1 
ATOM   1543 C  CD2 . TYR A 1 206 ? 17.423  0.825   39.430  1.00 17.25 ? 241 TYR A CD2 1 
ATOM   1544 C  CE1 . TYR A 1 206 ? 20.072  0.415   40.100  1.00 20.31 ? 241 TYR A CE1 1 
ATOM   1545 C  CE2 . TYR A 1 206 ? 17.782  0.560   40.766  1.00 16.48 ? 241 TYR A CE2 1 
ATOM   1546 C  CZ  . TYR A 1 206 ? 19.101  0.358   41.085  1.00 17.16 ? 241 TYR A CZ  1 
ATOM   1547 O  OH  . TYR A 1 206 ? 19.443  0.113   42.400  1.00 18.52 ? 241 TYR A OH  1 
ATOM   1548 N  N   . VAL A 1 207 ? 19.174  3.372   34.554  1.00 18.24 ? 242 VAL A N   1 
ATOM   1549 C  CA  . VAL A 1 207 ? 19.115  3.834   33.177  1.00 19.68 ? 242 VAL A CA  1 
ATOM   1550 C  C   . VAL A 1 207 ? 19.628  2.717   32.286  1.00 19.59 ? 242 VAL A C   1 
ATOM   1551 O  O   . VAL A 1 207 ? 20.797  2.312   32.390  1.00 23.61 ? 242 VAL A O   1 
ATOM   1552 C  CB  . VAL A 1 207 ? 19.937  5.112   32.978  1.00 25.85 ? 242 VAL A CB  1 
ATOM   1553 C  CG1 . VAL A 1 207 ? 19.944  5.506   31.488  1.00 25.12 ? 242 VAL A CG1 1 
ATOM   1554 C  CG2 . VAL A 1 207 ? 19.410  6.216   33.881  1.00 29.00 ? 242 VAL A CG2 1 
ATOM   1555 N  N   . VAL A 1 208 ? 18.751  2.221   31.424  1.00 20.10 ? 243 VAL A N   1 
ATOM   1556 C  CA  . VAL A 1 208 ? 19.010  1.081   30.551  1.00 21.59 ? 243 VAL A CA  1 
ATOM   1557 C  C   . VAL A 1 208 ? 19.244  1.620   29.156  1.00 20.19 ? 243 VAL A C   1 
ATOM   1558 O  O   . VAL A 1 208 ? 18.478  2.462   28.679  1.00 17.49 ? 243 VAL A O   1 
ATOM   1559 C  CB  . VAL A 1 208 ? 17.812  0.114   30.549  1.00 15.51 ? 243 VAL A CB  1 
ATOM   1560 C  CG1 . VAL A 1 208 ? 18.130  -1.092  29.695  1.00 16.22 ? 243 VAL A CG1 1 
ATOM   1561 C  CG2 . VAL A 1 208 ? 17.500  -0.312  31.973  1.00 15.18 ? 243 VAL A CG2 1 
ATOM   1562 N  N   . GLU A 1 209 ? 20.264  1.125   28.475  1.00 18.87 ? 244 GLU A N   1 
ATOM   1563 C  CA  . GLU A 1 209 ? 20.505  1.702   27.158  1.00 20.02 ? 244 GLU A CA  1 
ATOM   1564 C  C   . GLU A 1 209 ? 21.106  0.651   26.255  1.00 20.94 ? 244 GLU A C   1 
ATOM   1565 O  O   . GLU A 1 209 ? 22.143  0.073   26.605  1.00 21.79 ? 244 GLU A O   1 
ATOM   1566 C  CB  . GLU A 1 209 ? 21.443  2.923   27.241  1.00 23.19 ? 244 GLU A CB  1 
ATOM   1567 C  CG  . GLU A 1 209 ? 21.730  3.564   25.864  1.00 30.39 ? 244 GLU A CG  1 
ATOM   1568 C  CD  . GLU A 1 209 ? 22.345  4.961   25.950  1.00 47.33 ? 244 GLU A CD  1 
ATOM   1569 O  OE1 . GLU A 1 209 ? 22.763  5.385   27.056  1.00 43.94 ? 244 GLU A OE1 1 
ATOM   1570 O  OE2 . GLU A 1 209 ? 22.396  5.639   24.901  1.00 55.15 ? 244 GLU A OE2 1 
ATOM   1571 N  N   . SER A 1 210 ? 20.516  0.486   25.065  1.00 21.05 ? 245 SER A N   1 
ATOM   1572 C  CA  . SER A 1 210 ? 21.054  -0.440  24.070  1.00 22.20 ? 245 SER A CA  1 
ATOM   1573 C  C   . SER A 1 210 ? 20.923  0.140   22.672  1.00 23.36 ? 245 SER A C   1 
ATOM   1574 O  O   . SER A 1 210 ? 19.837  0.579   22.272  1.00 22.63 ? 245 SER A O   1 
ATOM   1575 C  CB  . SER A 1 210 ? 20.346  -1.800  24.110  1.00 22.69 ? 245 SER A CB  1 
ATOM   1576 O  OG  . SER A 1 210 ? 20.802  -2.607  23.022  1.00 23.18 ? 245 SER A OG  1 
ATOM   1577 N  N   . GLN A 1 211 ? 22.032  0.115   21.935  1.00 25.38 ? 246 GLN A N   1 
ATOM   1578 C  CA  . GLN A 1 211 ? 22.100  0.631   20.568  1.00 27.00 ? 246 GLN A CA  1 
ATOM   1579 C  C   . GLN A 1 211 ? 21.496  2.038   20.480  1.00 29.09 ? 246 GLN A C   1 
ATOM   1580 O  O   . GLN A 1 211 ? 20.832  2.391   19.502  1.00 32.09 ? 246 GLN A O   1 
ATOM   1581 C  CB  . GLN A 1 211 ? 21.402  -0.323  19.588  1.00 26.91 ? 246 GLN A CB  1 
ATOM   1582 C  CG  . GLN A 1 211 ? 21.892  -1.781  19.587  1.00 27.22 ? 246 GLN A CG  1 
ATOM   1583 C  CD  . GLN A 1 211 ? 23.329  -1.948  19.166  1.00 29.53 ? 246 GLN A CD  1 
ATOM   1584 O  OE1 . GLN A 1 211 ? 24.001  -0.988  18.786  1.00 31.10 ? 246 GLN A OE1 1 
ATOM   1585 N  NE2 . GLN A 1 211 ? 23.802  -3.189  19.184  1.00 30.02 ? 246 GLN A NE2 1 
ATOM   1586 N  N   . GLY A 1 212 ? 21.699  2.841   21.528  1.00 30.22 ? 247 GLY A N   1 
ATOM   1587 C  CA  . GLY A 1 212 ? 21.247  4.221   21.520  1.00 28.03 ? 247 GLY A CA  1 
ATOM   1588 C  C   . GLY A 1 212 ? 19.812  4.445   21.960  1.00 34.86 ? 247 GLY A C   1 
ATOM   1589 O  O   . GLY A 1 212 ? 19.381  5.602   22.034  1.00 30.69 ? 247 GLY A O   1 
ATOM   1590 N  N   . GLN A 1 213 ? 19.065  3.390   22.274  1.00 24.20 ? 248 GLN A N   1 
ATOM   1591 C  CA  . GLN A 1 213 ? 17.713  3.517   22.803  1.00 23.77 ? 248 GLN A CA  1 
ATOM   1592 C  C   . GLN A 1 213 ? 17.779  3.445   24.324  1.00 23.06 ? 248 GLN A C   1 
ATOM   1593 O  O   . GLN A 1 213 ? 18.320  2.485   24.877  1.00 23.49 ? 248 GLN A O   1 
ATOM   1594 C  CB  . GLN A 1 213 ? 16.811  2.405   22.259  1.00 22.59 ? 248 GLN A CB  1 
ATOM   1595 C  CG  . GLN A 1 213 ? 17.086  2.048   20.799  1.00 32.15 ? 248 GLN A CG  1 
ATOM   1596 C  CD  . GLN A 1 213 ? 16.752  3.176   19.859  1.00 35.27 ? 248 GLN A CD  1 
ATOM   1597 O  OE1 . GLN A 1 213 ? 15.961  4.053   20.196  1.00 40.85 ? 248 GLN A OE1 1 
ATOM   1598 N  NE2 . GLN A 1 213 ? 17.397  3.199   18.695  1.00 44.48 ? 248 GLN A NE2 1 
ATOM   1599 N  N   . LYS A 1 214 ? 17.227  4.454   24.992  1.00 21.53 ? 249 LYS A N   1 
ATOM   1600 C  CA  . LYS A 1 214 ? 17.332  4.603   26.432  1.00 20.66 ? 249 LYS A CA  1 
ATOM   1601 C  C   . LYS A 1 214 ? 15.961  4.426   27.097  1.00 26.45 ? 249 LYS A C   1 
ATOM   1602 O  O   . LYS A 1 214 ? 14.910  4.755   26.526  1.00 23.93 ? 249 LYS A O   1 
ATOM   1603 C  CB  . LYS A 1 214 ? 17.937  5.975   26.777  1.00 26.41 ? 249 LYS A CB  1 
ATOM   1604 C  CG  . LYS A 1 214 ? 18.274  6.192   28.255  1.00 30.05 ? 249 LYS A CG  1 
ATOM   1605 C  CD  . LYS A 1 214 ? 18.769  7.619   28.510  1.00 35.34 ? 249 LYS A CD  1 
ATOM   1606 C  CE  . LYS A 1 214 ? 20.156  7.854   27.974  1.00 43.27 ? 249 LYS A CE  1 
ATOM   1607 N  NZ  . LYS A 1 214 ? 20.642  9.214   28.363  1.00 43.34 ? 249 LYS A NZ  1 
ATOM   1608 N  N   . LEU A 1 215 ? 15.988  3.875   28.306  1.00 19.31 ? 250 LEU A N   1 
ATOM   1609 C  CA  . LEU A 1 215 ? 14.817  3.704   29.161  1.00 17.23 ? 250 LEU A CA  1 
ATOM   1610 C  C   . LEU A 1 215 ? 15.250  4.010   30.585  1.00 15.99 ? 250 LEU A C   1 
ATOM   1611 O  O   . LEU A 1 215 ? 16.170  3.358   31.088  1.00 17.95 ? 250 LEU A O   1 
ATOM   1612 C  CB  . LEU A 1 215 ? 14.287  2.258   29.091  1.00 14.23 ? 250 LEU A CB  1 
ATOM   1613 C  CG  . LEU A 1 215 ? 13.293  1.828   30.160  1.00 13.79 ? 250 LEU A CG  1 
ATOM   1614 C  CD1 . LEU A 1 215 ? 11.958  2.652   30.044  1.00 18.16 ? 250 LEU A CD1 1 
ATOM   1615 C  CD2 . LEU A 1 215 ? 13.055  0.306   30.109  1.00 16.44 ? 250 LEU A CD2 1 
ATOM   1616 N  N   . ALA A 1 216 ? 14.622  4.997   31.233  1.00 15.37 ? 251 ALA A N   1 
ATOM   1617 C  CA  . ALA A 1 216 ? 14.956  5.352   32.615  1.00 17.86 ? 251 ALA A CA  1 
ATOM   1618 C  C   . ALA A 1 216 ? 13.890  4.802   33.561  1.00 15.89 ? 251 ALA A C   1 
ATOM   1619 O  O   . ALA A 1 216 ? 12.742  5.252   33.541  1.00 20.94 ? 251 ALA A O   1 
ATOM   1620 C  CB  . ALA A 1 216 ? 15.105  6.865   32.774  1.00 19.07 ? 251 ALA A CB  1 
ATOM   1621 N  N   . LEU A 1 217 ? 14.286  3.839   34.390  1.00 16.18 ? 252 LEU A N   1 
ATOM   1622 C  CA  . LEU A 1 217 ? 13.456  3.204   35.405  1.00 15.12 ? 252 LEU A CA  1 
ATOM   1623 C  C   . LEU A 1 217 ? 13.525  4.089   36.634  1.00 19.83 ? 252 LEU A C   1 
ATOM   1624 O  O   . LEU A 1 217 ? 14.488  4.025   37.408  1.00 19.33 ? 252 LEU A O   1 
ATOM   1625 C  CB  . LEU A 1 217 ? 13.966  1.796   35.710  1.00 14.48 ? 252 LEU A CB  1 
ATOM   1626 C  CG  . LEU A 1 217 ? 14.076  0.823   34.517  1.00 17.26 ? 252 LEU A CG  1 
ATOM   1627 C  CD1 . LEU A 1 217 ? 14.713  -0.493  34.956  1.00 16.11 ? 252 LEU A CD1 1 
ATOM   1628 C  CD2 . LEU A 1 217 ? 12.698  0.553   33.943  1.00 22.07 ? 252 LEU A CD2 1 
ATOM   1629 N  N   . LEU A 1 218 ? 12.506  4.942   36.778  1.00 19.12 ? 253 LEU A N   1 
ATOM   1630 C  CA  . LEU A 1 218 ? 12.375  5.975   37.796  1.00 13.51 ? 253 LEU A CA  1 
ATOM   1631 C  C   . LEU A 1 218 ? 11.973  5.485   39.177  1.00 19.79 ? 253 LEU A C   1 
ATOM   1632 O  O   . LEU A 1 218 ? 11.972  6.296   40.110  1.00 16.65 ? 253 LEU A O   1 
ATOM   1633 C  CB  . LEU A 1 218 ? 11.373  7.019   37.276  1.00 21.11 ? 253 LEU A CB  1 
ATOM   1634 C  CG  . LEU A 1 218 ? 11.997  8.168   36.485  1.00 27.09 ? 253 LEU A CG  1 
ATOM   1635 C  CD1 . LEU A 1 218 ? 12.730  7.825   35.237  1.00 29.05 ? 253 LEU A CD1 1 
ATOM   1636 C  CD2 . LEU A 1 218 ? 10.825  9.027   36.048  1.00 18.29 ? 253 LEU A CD2 1 
ATOM   1637 N  N   . GLY A 1 219 ? 11.653  4.205   39.357  1.00 17.86 ? 254 GLY A N   1 
ATOM   1638 C  CA  . GLY A 1 219 ? 11.258  3.783   40.689  1.00 16.10 ? 254 GLY A CA  1 
ATOM   1639 C  C   . GLY A 1 219 ? 10.035  4.567   41.151  1.00 19.28 ? 254 GLY A C   1 
ATOM   1640 O  O   . GLY A 1 219 ? 8.997   4.590   40.470  1.00 18.97 ? 254 GLY A O   1 
ATOM   1641 N  N   . ASP A 1 220 ? 10.162  5.220   42.311  1.00 18.60 ? 255 ASP A N   1 
ATOM   1642 C  CA  . ASP A 1 220 ? 9.081   5.986   42.919  1.00 22.03 ? 255 ASP A CA  1 
ATOM   1643 C  C   . ASP A 1 220 ? 9.322   7.493   42.845  1.00 27.88 ? 255 ASP A C   1 
ATOM   1644 O  O   . ASP A 1 220 ? 8.977   8.237   43.775  1.00 20.84 ? 255 ASP A O   1 
ATOM   1645 C  CB  . ASP A 1 220 ? 8.888   5.540   44.369  1.00 17.97 ? 255 ASP A CB  1 
ATOM   1646 C  CG  . ASP A 1 220 ? 8.100   4.263   44.465  1.00 15.15 ? 255 ASP A CG  1 
ATOM   1647 O  OD1 . ASP A 1 220 ? 7.880   3.652   43.408  1.00 18.30 ? 255 ASP A OD1 1 
ATOM   1648 O  OD2 . ASP A 1 220 ? 7.735   3.851   45.580  1.00 18.17 ? 255 ASP A OD2 1 
ATOM   1649 N  N   . LEU A 1 221 ? 9.960   7.963   41.769  1.00 26.24 ? 256 LEU A N   1 
ATOM   1650 C  CA  . LEU A 1 221 ? 10.068  9.406   41.610  1.00 26.53 ? 256 LEU A CA  1 
ATOM   1651 C  C   . LEU A 1 221 ? 8.732   10.051  41.320  1.00 29.16 ? 256 LEU A C   1 
ATOM   1652 O  O   . LEU A 1 221 ? 8.621   11.269  41.444  1.00 37.98 ? 256 LEU A O   1 
ATOM   1653 C  CB  . LEU A 1 221 ? 11.043  9.797   40.508  1.00 24.59 ? 256 LEU A CB  1 
ATOM   1654 C  CG  . LEU A 1 221 ? 12.528  9.741   40.823  1.00 29.62 ? 256 LEU A CG  1 
ATOM   1655 C  CD1 . LEU A 1 221 ? 13.323  10.169  39.590  1.00 19.25 ? 256 LEU A CD1 1 
ATOM   1656 C  CD2 . LEU A 1 221 ? 12.736  10.711  41.966  1.00 28.28 ? 256 LEU A CD2 1 
ATOM   1657 N  N   . ILE A 1 222 ? 7.742   9.272   40.903  1.00 30.06 ? 257 ILE A N   1 
ATOM   1658 C  CA  . ILE A 1 222 ? 6.362   9.719   40.798  1.00 26.80 ? 257 ILE A CA  1 
ATOM   1659 C  C   . ILE A 1 222 ? 5.459   8.640   41.376  1.00 24.29 ? 257 ILE A C   1 
ATOM   1660 O  O   . ILE A 1 222 ? 5.672   7.445   41.155  1.00 32.40 ? 257 ILE A O   1 
ATOM   1661 C  CB  . ILE A 1 222 ? 5.965   10.051  39.351  1.00 32.01 ? 257 ILE A CB  1 
ATOM   1662 C  CG1 . ILE A 1 222 ? 4.564   10.658  39.342  1.00 23.10 ? 257 ILE A CG1 1 
ATOM   1663 C  CG2 . ILE A 1 222 ? 6.028   8.823   38.474  1.00 24.42 ? 257 ILE A CG2 1 
ATOM   1664 C  CD1 . ILE A 1 222 ? 4.194   11.303  38.037  1.00 32.17 ? 257 ILE A CD1 1 
ATOM   1665 N  N   . LEU A 1 223 ? 4.479   9.064   42.163  1.00 27.31 ? 258 LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 223 ? 3.579   8.154   42.846  1.00 27.01 ? 258 LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 223 ? 2.134   8.279   42.387  1.00 32.07 ? 258 LEU A C   1 
ATOM   1668 O  O   . LEU A 1 223 ? 1.424   7.272   42.346  1.00 25.17 ? 258 LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 223 ? 3.668   8.398   44.360  1.00 27.87 ? 258 LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 223 ? 5.075   8.131   44.945  1.00 33.62 ? 258 LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 223 ? 5.232   8.683   46.375  1.00 33.68 ? 258 LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 223 ? 5.462   6.617   44.880  1.00 22.38 ? 258 LEU A CD2 1 
ATOM   1673 N  N   . VAL A 1 224 ? 1.682   9.485   42.033  1.00 25.69 ? 259 VAL A N   1 
ATOM   1674 C  CA  . VAL A 1 224 ? 0.303   9.725   41.619  1.00 22.09 ? 259 VAL A CA  1 
ATOM   1675 C  C   . VAL A 1 224 ? 0.347   10.498  40.309  1.00 26.93 ? 259 VAL A C   1 
ATOM   1676 O  O   . VAL A 1 224 ? 0.460   11.727  40.317  1.00 25.68 ? 259 VAL A O   1 
ATOM   1677 C  CB  . VAL A 1 224 ? -0.479  10.502  42.678  1.00 23.52 ? 259 VAL A CB  1 
ATOM   1678 C  CG1 . VAL A 1 224 ? -1.957  10.555  42.300  1.00 27.78 ? 259 VAL A CG1 1 
ATOM   1679 C  CG2 . VAL A 1 224 ? -0.280  9.874   44.046  1.00 26.92 ? 259 VAL A CG2 1 
ATOM   1680 N  N   . ALA A 1 225 ? 0.223   9.789   39.179  1.00 24.22 ? 260 ALA A N   1 
ATOM   1681 C  CA  . ALA A 1 225 ? 0.294   10.445  37.870  1.00 26.46 ? 260 ALA A CA  1 
ATOM   1682 C  C   . ALA A 1 225 ? -0.730  11.575  37.706  1.00 29.60 ? 260 ALA A C   1 
ATOM   1683 O  O   . ALA A 1 225 ? -0.420  12.617  37.114  1.00 26.98 ? 260 ALA A O   1 
ATOM   1684 C  CB  . ALA A 1 225 ? 0.113   9.408   36.766  1.00 23.64 ? 260 ALA A CB  1 
ATOM   1685 N  N   . ALA A 1 226 ? -1.953  11.397  38.208  1.00 26.62 ? 261 ALA A N   1 
ATOM   1686 C  CA  . ALA A 1 226 ? -2.992  12.411  37.999  1.00 28.07 ? 261 ALA A CA  1 
ATOM   1687 C  C   . ALA A 1 226 ? -2.658  13.744  38.660  1.00 30.01 ? 261 ALA A C   1 
ATOM   1688 O  O   . ALA A 1 226 ? -3.290  14.755  38.331  1.00 34.23 ? 261 ALA A O   1 
ATOM   1689 C  CB  . ALA A 1 226 ? -4.340  11.912  38.520  1.00 23.87 ? 261 ALA A CB  1 
ATOM   1690 N  N   . VAL A 1 227 ? -1.694  13.762  39.583  1.00 25.66 ? 262 VAL A N   1 
ATOM   1691 C  CA  . VAL A 1 227 ? -1.290  14.960  40.316  1.00 26.44 ? 262 VAL A CA  1 
ATOM   1692 C  C   . VAL A 1 227 ? 0.079   15.460  39.868  1.00 25.99 ? 262 VAL A C   1 
ATOM   1693 O  O   . VAL A 1 227 ? 0.250   16.632  39.524  1.00 26.54 ? 262 VAL A O   1 
ATOM   1694 C  CB  . VAL A 1 227 ? -1.295  14.695  41.841  1.00 30.89 ? 262 VAL A CB  1 
ATOM   1695 C  CG1 . VAL A 1 227 ? -0.880  15.946  42.601  1.00 34.51 ? 262 VAL A CG1 1 
ATOM   1696 C  CG2 . VAL A 1 227 ? -2.678  14.242  42.307  1.00 33.80 ? 262 VAL A CG2 1 
ATOM   1697 N  N   . GLN A 1 228 ? 1.070   14.576  39.880  1.00 24.58 ? 263 GLN A N   1 
ATOM   1698 C  CA  . GLN A 1 228 ? 2.473   14.929  39.886  1.00 30.99 ? 263 GLN A CA  1 
ATOM   1699 C  C   . GLN A 1 228 ? 3.082   15.061  38.496  1.00 29.88 ? 263 GLN A C   1 
ATOM   1700 O  O   . GLN A 1 228 ? 4.257   15.418  38.386  1.00 29.91 ? 263 GLN A O   1 
ATOM   1701 C  CB  . GLN A 1 228 ? 3.225   13.874  40.700  1.00 23.98 ? 263 GLN A CB  1 
ATOM   1702 C  CG  . GLN A 1 228 ? 3.357   14.205  42.176  1.00 28.06 ? 263 GLN A CG  1 
ATOM   1703 C  CD  . GLN A 1 228 ? 3.505   12.954  43.031  1.00 30.37 ? 263 GLN A CD  1 
ATOM   1704 O  OE1 . GLN A 1 228 ? 3.340   11.843  42.540  1.00 29.15 ? 263 GLN A OE1 1 
ATOM   1705 N  NE2 . GLN A 1 228 ? 3.870   13.127  44.293  1.00 27.24 ? 263 GLN A NE2 1 
ATOM   1706 N  N   . PHE A 1 229 ? 2.346   14.747  37.438  1.00 22.54 ? 264 PHE A N   1 
ATOM   1707 C  CA  . PHE A 1 229 ? 2.820   15.144  36.122  1.00 25.55 ? 264 PHE A CA  1 
ATOM   1708 C  C   . PHE A 1 229 ? 2.480   16.609  35.864  1.00 30.08 ? 264 PHE A C   1 
ATOM   1709 O  O   . PHE A 1 229 ? 3.329   17.360  35.374  1.00 31.38 ? 264 PHE A O   1 
ATOM   1710 C  CB  . PHE A 1 229 ? 2.217   14.253  35.028  1.00 28.46 ? 264 PHE A CB  1 
ATOM   1711 C  CG  . PHE A 1 229 ? 2.887   12.890  34.879  1.00 25.42 ? 264 PHE A CG  1 
ATOM   1712 C  CD1 . PHE A 1 229 ? 4.261   12.771  34.652  1.00 28.33 ? 264 PHE A CD1 1 
ATOM   1713 C  CD2 . PHE A 1 229 ? 2.131   11.735  34.947  1.00 25.29 ? 264 PHE A CD2 1 
ATOM   1714 C  CE1 . PHE A 1 229 ? 4.867   11.519  34.502  1.00 26.91 ? 264 PHE A CE1 1 
ATOM   1715 C  CE2 . PHE A 1 229 ? 2.730   10.480  34.792  1.00 28.58 ? 264 PHE A CE2 1 
ATOM   1716 C  CZ  . PHE A 1 229 ? 4.099   10.378  34.575  1.00 23.96 ? 264 PHE A CZ  1 
ATOM   1717 N  N   . ASP A 1 230 ? 1.245   17.036  36.194  1.00 29.13 ? 265 ASP A N   1 
ATOM   1718 C  CA  . ASP A 1 230 ? 0.882   18.446  36.041  1.00 36.86 ? 265 ASP A CA  1 
ATOM   1719 C  C   . ASP A 1 230 ? 1.574   19.335  37.067  1.00 34.60 ? 265 ASP A C   1 
ATOM   1720 O  O   . ASP A 1 230 ? 1.784   20.533  36.809  1.00 32.41 ? 265 ASP A O   1 
ATOM   1721 C  CB  . ASP A 1 230 ? -0.627  18.654  36.161  1.00 35.94 ? 265 ASP A CB  1 
ATOM   1722 C  CG  . ASP A 1 230 ? -1.396  18.072  34.996  1.00 47.60 ? 265 ASP A CG  1 
ATOM   1723 O  OD1 . ASP A 1 230 ? -1.032  18.354  33.835  1.00 48.44 ? 265 ASP A OD1 1 
ATOM   1724 O  OD2 . ASP A 1 230 ? -2.418  17.403  35.245  1.00 55.37 ? 265 ASP A OD2 1 
ATOM   1725 N  N   . ASP A 1 231 ? 1.870   18.807  38.254  1.00 28.89 ? 266 ASP A N   1 
ATOM   1726 C  CA  . ASP A 1 231 ? 2.535   19.579  39.305  1.00 34.02 ? 266 ASP A CA  1 
ATOM   1727 C  C   . ASP A 1 231 ? 3.601   18.738  39.971  1.00 28.58 ? 266 ASP A C   1 
ATOM   1728 O  O   . ASP A 1 231 ? 3.393   18.194  41.062  1.00 36.38 ? 266 ASP A O   1 
ATOM   1729 C  CB  . ASP A 1 231 ? 1.529   20.123  40.325  1.00 34.37 ? 266 ASP A CB  1 
ATOM   1730 C  CG  . ASP A 1 231 ? 2.126   21.236  41.201  1.00 38.97 ? 266 ASP A CG  1 
ATOM   1731 O  OD1 . ASP A 1 231 ? 3.370   21.417  41.195  1.00 36.77 ? 266 ASP A OD1 1 
ATOM   1732 O  OD2 . ASP A 1 231 ? 1.354   21.948  41.879  1.00 36.72 ? 266 ASP A OD2 1 
ATOM   1733 N  N   . PRO A 1 232 ? 4.778   18.620  39.344  1.00 30.33 ? 267 PRO A N   1 
ATOM   1734 C  CA  . PRO A 1 232 ? 5.870   17.826  39.938  1.00 29.76 ? 267 PRO A CA  1 
ATOM   1735 C  C   . PRO A 1 232 ? 6.299   18.282  41.319  1.00 33.19 ? 267 PRO A C   1 
ATOM   1736 O  O   . PRO A 1 232 ? 7.044   17.547  41.983  1.00 30.00 ? 267 PRO A O   1 
ATOM   1737 C  CB  . PRO A 1 232 ? 7.019   18.000  38.932  1.00 34.34 ? 267 PRO A CB  1 
ATOM   1738 C  CG  . PRO A 1 232 ? 6.325   18.306  37.631  1.00 33.71 ? 267 PRO A CG  1 
ATOM   1739 C  CD  . PRO A 1 232 ? 5.139   19.142  38.013  1.00 31.58 ? 267 PRO A CD  1 
ATOM   1740 N  N   . SER A 1 233 ? 5.895   19.463  41.771  1.00 34.57 ? 268 SER A N   1 
ATOM   1741 C  CA  . SER A 1 233 ? 6.355   19.897  43.082  1.00 32.64 ? 268 SER A CA  1 
ATOM   1742 C  C   . SER A 1 233 ? 5.558   19.290  44.227  1.00 34.62 ? 268 SER A C   1 
ATOM   1743 O  O   . SER A 1 233 ? 5.985   19.422  45.373  1.00 36.43 ? 268 SER A O   1 
ATOM   1744 C  CB  . SER A 1 233 ? 6.313   21.422  43.200  1.00 33.05 ? 268 SER A CB  1 
ATOM   1745 O  OG  . SER A 1 233 ? 4.985   21.892  43.147  1.00 45.70 ? 268 SER A OG  1 
ATOM   1746 N  N   . VAL A 1 234 ? 4.426   18.625  43.970  1.00 35.27 ? 269 VAL A N   1 
ATOM   1747 C  CA  . VAL A 1 234 ? 3.638   18.059  45.065  1.00 33.85 ? 269 VAL A CA  1 
ATOM   1748 C  C   . VAL A 1 234 ? 4.330   16.805  45.579  1.00 33.62 ? 269 VAL A C   1 
ATOM   1749 O  O   . VAL A 1 234 ? 4.697   15.919  44.797  1.00 28.17 ? 269 VAL A O   1 
ATOM   1750 C  CB  . VAL A 1 234 ? 2.200   17.748  44.618  1.00 40.42 ? 269 VAL A CB  1 
ATOM   1751 C  CG1 . VAL A 1 234 ? 1.427   17.097  45.766  1.00 33.87 ? 269 VAL A CG1 1 
ATOM   1752 C  CG2 . VAL A 1 234 ? 1.497   19.021  44.131  1.00 31.64 ? 269 VAL A CG2 1 
ATOM   1753 N  N   . THR A 1 235 ? 4.500   16.711  46.892  1.00 30.99 ? 270 THR A N   1 
ATOM   1754 C  CA  . THR A 1 235 ? 5.146   15.521  47.462  1.00 30.47 ? 270 THR A CA  1 
ATOM   1755 C  C   . THR A 1 235 ? 4.188   14.773  48.378  1.00 29.41 ? 270 THR A C   1 
ATOM   1756 O  O   . THR A 1 235 ? 3.026   15.135  48.531  1.00 37.90 ? 270 THR A O   1 
ATOM   1757 C  CB  . THR A 1 235 ? 6.433   15.894  48.201  1.00 30.40 ? 270 THR A CB  1 
ATOM   1758 O  OG1 . THR A 1 235 ? 6.113   16.620  49.396  1.00 31.88 ? 270 THR A OG1 1 
ATOM   1759 C  CG2 . THR A 1 235 ? 7.338   16.727  47.308  1.00 34.59 ? 270 THR A CG2 1 
ATOM   1760 N  N   . THR A 1 236 ? 4.684   13.696  48.980  1.00 33.44 ? 271 THR A N   1 
ATOM   1761 C  CA  . THR A 1 236 ? 3.878   12.885  49.876  1.00 30.25 ? 271 THR A CA  1 
ATOM   1762 C  C   . THR A 1 236 ? 4.570   12.773  51.226  1.00 33.57 ? 271 THR A C   1 
ATOM   1763 O  O   . THR A 1 236 ? 5.765   13.046  51.367  1.00 33.31 ? 271 THR A O   1 
ATOM   1764 C  CB  . THR A 1 236 ? 3.622   11.485  49.296  1.00 32.63 ? 271 THR A CB  1 
ATOM   1765 O  OG1 . THR A 1 236 ? 4.795   10.683  49.465  1.00 38.27 ? 271 THR A OG1 1 
ATOM   1766 C  CG2 . THR A 1 236 ? 3.315   11.577  47.822  1.00 32.39 ? 271 THR A CG2 1 
ATOM   1767 N  N   . ASP A 1 237 ? 3.783   12.393  52.233  1.00 34.43 ? 272 ASP A N   1 
ATOM   1768 C  CA  . ASP A 1 237 ? 4.327   12.099  53.552  1.00 32.32 ? 272 ASP A CA  1 
ATOM   1769 C  C   . ASP A 1 237 ? 5.260   10.890  53.527  1.00 37.14 ? 272 ASP A C   1 
ATOM   1770 O  O   . ASP A 1 237 ? 5.994   10.669  54.494  1.00 41.68 ? 272 ASP A O   1 
ATOM   1771 C  CB  . ASP A 1 237 ? 3.183   11.829  54.516  1.00 40.75 ? 272 ASP A CB  1 
ATOM   1772 C  CG  . ASP A 1 237 ? 2.621   10.443  54.335  1.00 47.75 ? 272 ASP A CG  1 
ATOM   1773 O  OD1 . ASP A 1 237 ? 3.147   9.491   54.961  1.00 60.22 ? 272 ASP A OD1 1 
ATOM   1774 O  OD2 . ASP A 1 237 ? 1.667   10.300  53.549  1.00 53.57 ? 272 ASP A OD2 1 
ATOM   1775 N  N   . LEU A 1 238 ? 5.222   10.088  52.464  1.00 32.76 ? 273 LEU A N   1 
ATOM   1776 C  CA  . LEU A 1 238 ? 6.131   8.953   52.323  1.00 33.55 ? 273 LEU A CA  1 
ATOM   1777 C  C   . LEU A 1 238 ? 7.514   9.347   51.844  1.00 38.93 ? 273 LEU A C   1 
ATOM   1778 O  O   . LEU A 1 238 ? 8.416   8.494   51.863  1.00 38.87 ? 273 LEU A O   1 
ATOM   1779 C  CB  . LEU A 1 238 ? 5.600   7.940   51.325  1.00 37.13 ? 273 LEU A CB  1 
ATOM   1780 C  CG  . LEU A 1 238 ? 4.264   7.249   51.484  1.00 45.58 ? 273 LEU A CG  1 
ATOM   1781 C  CD1 . LEU A 1 238 ? 4.049   6.469   50.170  1.00 29.35 ? 273 LEU A CD1 1 
ATOM   1782 C  CD2 . LEU A 1 238 ? 4.283   6.365   52.723  1.00 45.64 ? 273 LEU A CD2 1 
ATOM   1783 N  N   . ASP A 1 239 ? 7.697   10.585  51.374  1.00 25.29 ? 274 ASP A N   1 
ATOM   1784 C  CA  . ASP A 1 239 ? 8.997   10.995  50.867  1.00 34.76 ? 274 ASP A CA  1 
ATOM   1785 C  C   . ASP A 1 239 ? 9.897   11.423  52.020  1.00 34.19 ? 274 ASP A C   1 
ATOM   1786 O  O   . ASP A 1 239 ? 9.513   12.259  52.841  1.00 33.64 ? 274 ASP A O   1 
ATOM   1787 C  CB  . ASP A 1 239 ? 8.858   12.121  49.844  1.00 28.14 ? 274 ASP A CB  1 
ATOM   1788 C  CG  . ASP A 1 239 ? 8.060   11.711  48.636  1.00 36.50 ? 274 ASP A CG  1 
ATOM   1789 O  OD1 . ASP A 1 239 ? 8.519   10.786  47.928  1.00 32.66 ? 274 ASP A OD1 1 
ATOM   1790 O  OD2 . ASP A 1 239 ? 7.004   12.340  48.366  1.00 35.32 ? 274 ASP A OD2 1 
ATOM   1791 N  N   . SER A 1 240 ? 11.094  10.826  52.088  1.00 31.88 ? 275 SER A N   1 
ATOM   1792 C  CA  . SER A 1 240 ? 12.034  11.150  53.160  1.00 27.81 ? 275 SER A CA  1 
ATOM   1793 C  C   . SER A 1 240 ? 12.441  12.615  53.124  1.00 41.97 ? 275 SER A C   1 
ATOM   1794 O  O   . SER A 1 240 ? 12.590  13.251  54.177  1.00 39.98 ? 275 SER A O   1 
ATOM   1795 C  CB  . SER A 1 240 ? 13.276  10.258  53.065  1.00 28.14 ? 275 SER A CB  1 
ATOM   1796 O  OG  . SER A 1 240 ? 12.919  8.891   53.216  1.00 39.97 ? 275 SER A OG  1 
ATOM   1797 N  N   . ASP A 1 241 ? 12.653  13.161  51.926  1.00 36.78 ? 276 ASP A N   1 
ATOM   1798 C  CA  . ASP A 1 241 ? 13.121  14.540  51.744  1.00 41.11 ? 276 ASP A CA  1 
ATOM   1799 C  C   . ASP A 1 241 ? 12.293  15.173  50.629  1.00 37.64 ? 276 ASP A C   1 
ATOM   1800 O  O   . ASP A 1 241 ? 12.545  14.915  49.447  1.00 30.82 ? 276 ASP A O   1 
ATOM   1801 C  CB  . ASP A 1 241 ? 14.626  14.570  51.440  1.00 39.53 ? 276 ASP A CB  1 
ATOM   1802 C  CG  . ASP A 1 241 ? 15.198  15.978  51.395  1.00 43.10 ? 276 ASP A CG  1 
ATOM   1803 O  OD1 . ASP A 1 241 ? 14.417  16.941  51.321  1.00 39.52 ? 276 ASP A OD1 1 
ATOM   1804 O  OD2 . ASP A 1 241 ? 16.439  16.133  51.428  1.00 44.70 ? 276 ASP A OD2 1 
ATOM   1805 N  N   . SER A 1 242 ? 11.314  16.006  51.016  1.00 32.12 ? 277 SER A N   1 
ATOM   1806 C  CA  . SER A 1 242 ? 10.370  16.572  50.047  1.00 39.61 ? 277 SER A CA  1 
ATOM   1807 C  C   . SER A 1 242 ? 11.061  17.482  49.035  1.00 41.74 ? 277 SER A C   1 
ATOM   1808 O  O   . SER A 1 242 ? 10.769  17.430  47.833  1.00 42.17 ? 277 SER A O   1 
ATOM   1809 C  CB  . SER A 1 242 ? 9.266   17.345  50.768  1.00 39.33 ? 277 SER A CB  1 
ATOM   1810 O  OG  . SER A 1 242 ? 8.250   16.476  51.220  1.00 47.77 ? 277 SER A OG  1 
ATOM   1811 N  N   . LYS A 1 243 ? 11.961  18.340  49.505  1.00 37.58 ? 278 LYS A N   1 
ATOM   1812 C  CA  . LYS A 1 243 ? 12.680  19.227  48.595  1.00 42.39 ? 278 LYS A CA  1 
ATOM   1813 C  C   . LYS A 1 243 ? 13.519  18.430  47.605  1.00 39.92 ? 278 LYS A C   1 
ATOM   1814 O  O   . LYS A 1 243 ? 13.542  18.739  46.400  1.00 36.38 ? 278 LYS A O   1 
ATOM   1815 C  CB  . LYS A 1 243 ? 13.560  20.186  49.392  1.00 37.49 ? 278 LYS A CB  1 
ATOM   1816 C  CG  . LYS A 1 243 ? 12.799  21.173  50.270  1.00 52.00 ? 278 LYS A CG  1 
ATOM   1817 C  CD  . LYS A 1 243 ? 12.466  20.613  51.648  1.00 54.58 ? 278 LYS A CD  1 
ATOM   1818 C  CE  . LYS A 1 243 ? 11.501  21.534  52.395  1.00 60.97 ? 278 LYS A CE  1 
ATOM   1819 N  NZ  . LYS A 1 243 ? 11.015  20.930  53.672  1.00 53.48 ? 278 LYS A NZ  1 
ATOM   1820 N  N   . ALA A 1 244 ? 14.213  17.397  48.102  1.00 34.98 ? 279 ALA A N   1 
ATOM   1821 C  CA  . ALA A 1 244 ? 15.031  16.554  47.239  1.00 35.68 ? 279 ALA A CA  1 
ATOM   1822 C  C   . ALA A 1 244 ? 14.174  15.831  46.213  1.00 33.37 ? 279 ALA A C   1 
ATOM   1823 O  O   . ALA A 1 244 ? 14.535  15.751  45.033  1.00 31.31 ? 279 ALA A O   1 
ATOM   1824 C  CB  . ALA A 1 244 ? 15.822  15.550  48.079  1.00 37.28 ? 279 ALA A CB  1 
ATOM   1825 N  N   . VAL A 1 245 ? 13.039  15.276  46.641  1.00 25.63 ? 280 VAL A N   1 
ATOM   1826 C  CA  . VAL A 1 245 ? 12.260  14.502  45.676  1.00 28.98 ? 280 VAL A CA  1 
ATOM   1827 C  C   . VAL A 1 245 ? 11.683  15.437  44.619  1.00 37.50 ? 280 VAL A C   1 
ATOM   1828 O  O   . VAL A 1 245 ? 11.659  15.099  43.433  1.00 32.87 ? 280 VAL A O   1 
ATOM   1829 C  CB  . VAL A 1 245 ? 11.160  13.655  46.352  1.00 28.10 ? 280 VAL A CB  1 
ATOM   1830 C  CG1 . VAL A 1 245 ? 10.348  14.455  47.321  1.00 37.82 ? 280 VAL A CG1 1 
ATOM   1831 C  CG2 . VAL A 1 245 ? 10.237  13.040  45.315  1.00 38.04 ? 280 VAL A CG2 1 
ATOM   1832 N  N   . ALA A 1 246 ? 11.257  16.645  45.022  1.00 29.57 ? 281 ALA A N   1 
ATOM   1833 C  CA  . ALA A 1 246 ? 10.791  17.622  44.038  1.00 35.99 ? 281 ALA A CA  1 
ATOM   1834 C  C   . ALA A 1 246 ? 11.867  17.910  42.999  1.00 36.29 ? 281 ALA A C   1 
ATOM   1835 O  O   . ALA A 1 246 ? 11.620  17.819  41.786  1.00 31.58 ? 281 ALA A O   1 
ATOM   1836 C  CB  . ALA A 1 246 ? 10.367  18.918  44.733  1.00 32.90 ? 281 ALA A CB  1 
ATOM   1837 N  N   . VAL A 1 247 ? 13.077  18.243  43.462  1.00 33.93 ? 282 VAL A N   1 
ATOM   1838 C  CA  . VAL A 1 247 ? 14.176  18.547  42.547  1.00 32.21 ? 282 VAL A CA  1 
ATOM   1839 C  C   . VAL A 1 247 ? 14.476  17.366  41.631  1.00 35.90 ? 282 VAL A C   1 
ATOM   1840 O  O   . VAL A 1 247 ? 14.667  17.535  40.420  1.00 34.85 ? 282 VAL A O   1 
ATOM   1841 C  CB  . VAL A 1 247 ? 15.423  18.958  43.339  1.00 33.51 ? 282 VAL A CB  1 
ATOM   1842 C  CG1 . VAL A 1 247 ? 16.633  18.992  42.417  1.00 33.50 ? 282 VAL A CG1 1 
ATOM   1843 C  CG2 . VAL A 1 247 ? 15.210  20.329  43.986  1.00 40.75 ? 282 VAL A CG2 1 
ATOM   1844 N  N   . GLU A 1 248 ? 14.541  16.157  42.186  1.00 29.60 ? 283 GLU A N   1 
ATOM   1845 C  CA  . GLU A 1 248 ? 14.969  15.022  41.376  1.00 27.42 ? 283 GLU A CA  1 
ATOM   1846 C  C   . GLU A 1 248 ? 13.895  14.632  40.367  1.00 31.05 ? 283 GLU A C   1 
ATOM   1847 O  O   . GLU A 1 248 ? 14.205  14.279  39.220  1.00 23.68 ? 283 GLU A O   1 
ATOM   1848 C  CB  . GLU A 1 248 ? 15.337  13.841  42.272  1.00 27.80 ? 283 GLU A CB  1 
ATOM   1849 C  CG  . GLU A 1 248 ? 16.697  13.964  42.959  1.00 33.40 ? 283 GLU A CG  1 
ATOM   1850 C  CD  . GLU A 1 248 ? 17.862  14.114  41.974  1.00 35.64 ? 283 GLU A CD  1 
ATOM   1851 O  OE1 . GLU A 1 248 ? 18.841  14.782  42.329  1.00 39.36 ? 283 GLU A OE1 1 
ATOM   1852 O  OE2 . GLU A 1 248 ? 17.809  13.556  40.853  1.00 39.46 ? 283 GLU A OE2 1 
ATOM   1853 N  N   . ARG A 1 249 ? 12.628  14.693  40.769  1.00 30.84 ? 284 ARG A N   1 
ATOM   1854 C  CA  . ARG A 1 249 ? 11.558  14.405  39.827  1.00 30.06 ? 284 ARG A CA  1 
ATOM   1855 C  C   . ARG A 1 249 ? 11.587  15.405  38.687  1.00 29.21 ? 284 ARG A C   1 
ATOM   1856 O  O   . ARG A 1 249 ? 11.507  15.020  37.514  1.00 25.97 ? 284 ARG A O   1 
ATOM   1857 C  CB  . ARG A 1 249 ? 10.204  14.438  40.528  1.00 28.68 ? 284 ARG A CB  1 
ATOM   1858 C  CG  . ARG A 1 249 ? 9.014   14.323  39.567  1.00 26.97 ? 284 ARG A CG  1 
ATOM   1859 C  CD  . ARG A 1 249 ? 7.713   14.307  40.330  1.00 30.35 ? 284 ARG A CD  1 
ATOM   1860 N  NE  . ARG A 1 249 ? 7.832   13.478  41.520  1.00 34.46 ? 284 ARG A NE  1 
ATOM   1861 C  CZ  . ARG A 1 249 ? 7.233   13.729  42.673  1.00 35.02 ? 284 ARG A CZ  1 
ATOM   1862 N  NH1 . ARG A 1 249 ? 6.490   14.812  42.847  1.00 37.72 ? 284 ARG A NH1 1 
ATOM   1863 N  NH2 . ARG A 1 249 ? 7.409   12.891  43.686  1.00 31.64 ? 284 ARG A NH2 1 
ATOM   1864 N  N   . LYS A 1 250 ? 11.698  16.706  39.016  1.00 29.66 ? 285 LYS A N   1 
ATOM   1865 C  CA  . LYS A 1 250 ? 11.723  17.721  37.968  1.00 29.49 ? 285 LYS A CA  1 
ATOM   1866 C  C   . LYS A 1 250 ? 12.923  17.516  37.053  1.00 32.37 ? 285 LYS A C   1 
ATOM   1867 O  O   . LYS A 1 250 ? 12.815  17.672  35.835  1.00 30.72 ? 285 LYS A O   1 
ATOM   1868 C  CB  . LYS A 1 250 ? 11.728  19.112  38.589  1.00 36.00 ? 285 LYS A CB  1 
ATOM   1869 C  CG  . LYS A 1 250 ? 10.441  19.479  39.331  1.00 35.66 ? 285 LYS A CG  1 
ATOM   1870 C  CD  . LYS A 1 250 ? 10.638  20.766  40.137  1.00 43.64 ? 285 LYS A CD  1 
ATOM   1871 C  CE  . LYS A 1 250 ? 9.460   21.078  41.040  1.00 44.91 ? 285 LYS A CE  1 
ATOM   1872 N  NZ  . LYS A 1 250 ? 9.516   22.493  41.493  1.00 42.78 ? 285 LYS A NZ  1 
ATOM   1873 N  N   . LYS A 1 251 ? 14.060  17.093  37.617  1.00 29.45 ? 286 LYS A N   1 
ATOM   1874 C  CA  . LYS A 1 251 ? 15.247  16.819  36.810  1.00 25.50 ? 286 LYS A CA  1 
ATOM   1875 C  C   . LYS A 1 251 ? 15.020  15.644  35.856  1.00 26.43 ? 286 LYS A C   1 
ATOM   1876 O  O   . LYS A 1 251 ? 15.359  15.719  34.670  1.00 28.75 ? 286 LYS A O   1 
ATOM   1877 C  CB  . LYS A 1 251 ? 16.418  16.542  37.749  1.00 28.76 ? 286 LYS A CB  1 
ATOM   1878 C  CG  . LYS A 1 251 ? 17.668  17.361  37.527  1.00 44.11 ? 286 LYS A CG  1 
ATOM   1879 C  CD  . LYS A 1 251 ? 18.856  16.689  38.221  1.00 46.75 ? 286 LYS A CD  1 
ATOM   1880 C  CE  . LYS A 1 251 ? 19.107  17.329  39.582  1.00 39.26 ? 286 LYS A CE  1 
ATOM   1881 N  NZ  . LYS A 1 251 ? 19.951  16.497  40.495  1.00 46.06 ? 286 LYS A NZ  1 
ATOM   1882 N  N   . ALA A 1 252 ? 14.429  14.553  36.355  1.00 27.32 ? 287 ALA A N   1 
ATOM   1883 C  CA  . ALA A 1 252 ? 14.137  13.400  35.502  1.00 23.54 ? 287 ALA A CA  1 
ATOM   1884 C  C   . ALA A 1 252 ? 13.154  13.768  34.398  1.00 28.83 ? 287 ALA A C   1 
ATOM   1885 O  O   . ALA A 1 252 ? 13.301  13.350  33.238  1.00 23.52 ? 287 ALA A O   1 
ATOM   1886 C  CB  . ALA A 1 252 ? 13.579  12.259  36.355  1.00 22.59 ? 287 ALA A CB  1 
ATOM   1887 N  N   . PHE A 1 253 ? 12.134  14.545  34.744  1.00 24.66 ? 288 PHE A N   1 
ATOM   1888 C  CA  . PHE A 1 253 ? 11.119  14.881  33.761  1.00 24.36 ? 288 PHE A CA  1 
ATOM   1889 C  C   . PHE A 1 253 ? 11.714  15.789  32.693  1.00 31.03 ? 288 PHE A C   1 
ATOM   1890 O  O   . PHE A 1 253 ? 11.540  15.548  31.489  1.00 29.30 ? 288 PHE A O   1 
ATOM   1891 C  CB  . PHE A 1 253 ? 9.919   15.535  34.448  1.00 26.84 ? 288 PHE A CB  1 
ATOM   1892 C  CG  . PHE A 1 253 ? 9.075   14.582  35.264  1.00 25.16 ? 288 PHE A CG  1 
ATOM   1893 C  CD1 . PHE A 1 253 ? 9.385   13.226  35.341  1.00 25.28 ? 288 PHE A CD1 1 
ATOM   1894 C  CD2 . PHE A 1 253 ? 7.941   15.030  35.927  1.00 27.74 ? 288 PHE A CD2 1 
ATOM   1895 C  CE1 . PHE A 1 253 ? 8.600   12.368  36.077  1.00 23.38 ? 288 PHE A CE1 1 
ATOM   1896 C  CE2 . PHE A 1 253 ? 7.137   14.139  36.659  1.00 24.76 ? 288 PHE A CE2 1 
ATOM   1897 C  CZ  . PHE A 1 253 ? 7.470   12.828  36.728  1.00 25.02 ? 288 PHE A CZ  1 
ATOM   1898 N  N   . ALA A 1 254 ? 12.464  16.815  33.118  1.00 31.31 ? 289 ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 254 ? 13.096  17.703  32.151  1.00 31.06 ? 289 ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 254 ? 14.042  16.924  31.247  1.00 29.48 ? 289 ALA A C   1 
ATOM   1901 O  O   . ALA A 1 254 ? 14.053  17.132  30.031  1.00 29.60 ? 289 ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 254 ? 13.821  18.844  32.866  1.00 31.52 ? 289 ALA A CB  1 
ATOM   1903 N  N   . ASP A 1 255 ? 14.796  15.975  31.807  1.00 32.51 ? 290 ASP A N   1 
ATOM   1904 C  CA  . ASP A 1 255 ? 15.772  15.252  30.998  1.00 31.74 ? 290 ASP A CA  1 
ATOM   1905 C  C   . ASP A 1 255 ? 15.100  14.308  30.007  1.00 30.62 ? 290 ASP A C   1 
ATOM   1906 O  O   . ASP A 1 255 ? 15.537  14.199  28.852  1.00 26.52 ? 290 ASP A O   1 
ATOM   1907 C  CB  . ASP A 1 255 ? 16.731  14.475  31.897  1.00 26.42 ? 290 ASP A CB  1 
ATOM   1908 C  CG  . ASP A 1 255 ? 17.995  14.045  31.159  1.00 32.40 ? 290 ASP A CG  1 
ATOM   1909 O  OD1 . ASP A 1 255 ? 18.817  14.921  30.829  1.00 30.64 ? 290 ASP A OD1 1 
ATOM   1910 O  OD2 . ASP A 1 255 ? 18.165  12.848  30.880  1.00 30.07 ? 290 ASP A OD2 1 
ATOM   1911 N  N   . ALA A 1 256 ? 14.042  13.604  30.429  1.00 26.49 ? 291 ALA A N   1 
ATOM   1912 C  CA  . ALA A 1 256 ? 13.385  12.710  29.488  1.00 22.67 ? 291 ALA A CA  1 
ATOM   1913 C  C   . ALA A 1 256 ? 12.624  13.490  28.417  1.00 28.62 ? 291 ALA A C   1 
ATOM   1914 O  O   . ALA A 1 256 ? 12.564  13.050  27.261  1.00 27.20 ? 291 ALA A O   1 
ATOM   1915 C  CB  . ALA A 1 256 ? 12.463  11.749  30.234  1.00 25.28 ? 291 ALA A CB  1 
ATOM   1916 N  N   . ALA A 1 257 ? 12.069  14.660  28.763  1.00 23.80 ? 292 ALA A N   1 
ATOM   1917 C  CA  . ALA A 1 257 ? 11.403  15.465  27.749  1.00 25.09 ? 292 ALA A CA  1 
ATOM   1918 C  C   . ALA A 1 257 ? 12.404  16.074  26.775  1.00 33.58 ? 292 ALA A C   1 
ATOM   1919 O  O   . ALA A 1 257 ? 12.106  16.218  25.583  1.00 32.54 ? 292 ALA A O   1 
ATOM   1920 C  CB  . ALA A 1 257 ? 10.561  16.551  28.402  1.00 31.18 ? 292 ALA A CB  1 
ATOM   1921 N  N   . LYS A 1 258 ? 13.585  16.467  27.264  1.00 27.15 ? 293 LYS A N   1 
ATOM   1922 C  CA  . LYS A 1 258 ? 14.633  16.934  26.363  1.00 33.77 ? 293 LYS A CA  1 
ATOM   1923 C  C   . LYS A 1 258 ? 15.110  15.820  25.441  1.00 34.37 ? 293 LYS A C   1 
ATOM   1924 O  O   . LYS A 1 258 ? 15.266  16.026  24.230  1.00 32.71 ? 293 LYS A O   1 
ATOM   1925 C  CB  . LYS A 1 258 ? 15.816  17.473  27.165  1.00 37.85 ? 293 LYS A CB  1 
ATOM   1926 C  CG  . LYS A 1 258 ? 15.521  18.727  27.964  1.00 54.52 ? 293 LYS A CG  1 
ATOM   1927 C  CD  . LYS A 1 258 ? 16.728  19.185  28.779  1.00 42.19 ? 293 LYS A CD  1 
ATOM   1928 C  CE  . LYS A 1 258 ? 16.363  20.431  29.568  1.00 57.45 ? 293 LYS A CE  1 
ATOM   1929 N  NZ  . LYS A 1 258 ? 17.453  20.973  30.436  1.00 57.12 ? 293 LYS A NZ  1 
ATOM   1930 N  N   . GLY A 1 259 ? 15.362  14.633  26.003  1.00 29.58 ? 294 GLY A N   1 
ATOM   1931 C  CA  . GLY A 1 259 ? 15.978  13.546  25.270  1.00 26.41 ? 294 GLY A CA  1 
ATOM   1932 C  C   . GLY A 1 259 ? 14.983  12.735  24.467  1.00 31.83 ? 294 GLY A C   1 
ATOM   1933 O  O   . GLY A 1 259 ? 15.358  12.045  23.513  1.00 30.76 ? 294 GLY A O   1 
ATOM   1934 N  N   . GLY A 1 260 ? 13.709  12.815  24.841  1.00 25.64 ? 295 GLY A N   1 
ATOM   1935 C  CA  . GLY A 1 260 ? 12.693  12.047  24.147  1.00 28.62 ? 295 GLY A CA  1 
ATOM   1936 C  C   . GLY A 1 260 ? 12.888  10.559  24.246  1.00 26.35 ? 295 GLY A C   1 
ATOM   1937 O  O   . GLY A 1 260 ? 12.597  9.836   23.287  1.00 29.22 ? 295 GLY A O   1 
ATOM   1938 N  N   . TYR A 1 261 ? 13.380  10.077  25.384  1.00 25.32 ? 296 TYR A N   1 
ATOM   1939 C  CA  . TYR A 1 261 ? 13.523  8.647   25.625  1.00 23.10 ? 296 TYR A CA  1 
ATOM   1940 C  C   . TYR A 1 261 ? 12.444  8.174   26.601  1.00 23.82 ? 296 TYR A C   1 
ATOM   1941 O  O   . TYR A 1 261 ? 11.715  8.972   27.207  1.00 17.19 ? 296 TYR A O   1 
ATOM   1942 C  CB  . TYR A 1 261 ? 14.967  8.333   26.100  1.00 20.19 ? 296 TYR A CB  1 
ATOM   1943 C  CG  . TYR A 1 261 ? 15.402  9.067   27.358  1.00 19.58 ? 296 TYR A CG  1 
ATOM   1944 C  CD1 . TYR A 1 261 ? 14.959  8.638   28.615  1.00 18.37 ? 296 TYR A CD1 1 
ATOM   1945 C  CD2 . TYR A 1 261 ? 16.245  10.193  27.301  1.00 27.64 ? 296 TYR A CD2 1 
ATOM   1946 C  CE1 . TYR A 1 261 ? 15.316  9.299   29.760  1.00 18.47 ? 296 TYR A CE1 1 
ATOM   1947 C  CE2 . TYR A 1 261 ? 16.626  10.857  28.475  1.00 25.17 ? 296 TYR A CE2 1 
ATOM   1948 C  CZ  . TYR A 1 261 ? 16.148  10.383  29.701  1.00 26.86 ? 296 TYR A CZ  1 
ATOM   1949 O  OH  . TYR A 1 261 ? 16.467  10.985  30.897  1.00 25.80 ? 296 TYR A OH  1 
ATOM   1950 N  N   . LEU A 1 262 ? 12.307  6.848   26.712  1.00 20.59 ? 297 LEU A N   1 
ATOM   1951 C  CA  . LEU A 1 262 ? 11.248  6.270   27.525  1.00 17.85 ? 297 LEU A CA  1 
ATOM   1952 C  C   . LEU A 1 262 ? 11.618  6.289   28.996  1.00 18.70 ? 297 LEU A C   1 
ATOM   1953 O  O   . LEU A 1 262 ? 12.785  6.168   29.363  1.00 19.18 ? 297 LEU A O   1 
ATOM   1954 C  CB  . LEU A 1 262 ? 10.966  4.828   27.104  1.00 21.84 ? 297 LEU A CB  1 
ATOM   1955 C  CG  . LEU A 1 262 ? 10.264  4.574   25.771  1.00 23.68 ? 297 LEU A CG  1 
ATOM   1956 C  CD1 . LEU A 1 262 ? 10.299  3.091   25.436  1.00 22.55 ? 297 LEU A CD1 1 
ATOM   1957 C  CD2 . LEU A 1 262 ? 8.835   4.998   25.878  1.00 17.41 ? 297 LEU A CD2 1 
ATOM   1958 N  N   . ILE A 1 263 ? 10.599  6.429   29.841  1.00 14.76 ? 298 ILE A N   1 
ATOM   1959 C  CA  . ILE A 1 263 ? 10.710  6.281   31.283  1.00 16.37 ? 298 ILE A CA  1 
ATOM   1960 C  C   . ILE A 1 263 ? 9.753   5.168   31.676  1.00 15.57 ? 298 ILE A C   1 
ATOM   1961 O  O   . ILE A 1 263 ? 8.822   4.829   30.941  1.00 15.63 ? 298 ILE A O   1 
ATOM   1962 C  CB  . ILE A 1 263 ? 10.369  7.584   32.048  1.00 18.55 ? 298 ILE A CB  1 
ATOM   1963 C  CG1 . ILE A 1 263 ? 8.871   7.872   31.918  1.00 24.06 ? 298 ILE A CG1 1 
ATOM   1964 C  CG2 . ILE A 1 263 ? 11.181  8.751   31.522  1.00 17.03 ? 298 ILE A CG2 1 
ATOM   1965 C  CD1 . ILE A 1 263 ? 8.342   8.978   32.764  1.00 26.13 ? 298 ILE A CD1 1 
ATOM   1966 N  N   . ALA A 1 264 ? 9.966   4.620   32.861  1.00 14.08 ? 299 ALA A N   1 
ATOM   1967 C  CA  . ALA A 1 264 ? 8.975   3.736   33.466  1.00 17.90 ? 299 ALA A CA  1 
ATOM   1968 C  C   . ALA A 1 264 ? 8.978   4.001   34.961  1.00 20.30 ? 299 ALA A C   1 
ATOM   1969 O  O   . ALA A 1 264 ? 9.993   4.398   35.530  1.00 21.45 ? 299 ALA A O   1 
ATOM   1970 C  CB  . ALA A 1 264 ? 9.263   2.257   33.202  1.00 14.85 ? 299 ALA A CB  1 
ATOM   1971 N  N   . ALA A 1 265 ? 7.836   3.817   35.592  1.00 15.00 ? 300 ALA A N   1 
ATOM   1972 C  CA  . ALA A 1 265 ? 7.802   4.014   37.029  1.00 19.89 ? 300 ALA A CA  1 
ATOM   1973 C  C   . ALA A 1 265 ? 6.903   2.967   37.652  1.00 14.01 ? 300 ALA A C   1 
ATOM   1974 O  O   . ALA A 1 265 ? 5.887   2.586   37.068  1.00 17.12 ? 300 ALA A O   1 
ATOM   1975 C  CB  . ALA A 1 265 ? 7.300   5.407   37.403  1.00 23.12 ? 300 ALA A CB  1 
ATOM   1976 N  N   . SER A 1 266 ? 7.244   2.598   38.893  1.00 15.98 ? 301 SER A N   1 
ATOM   1977 C  CA  . SER A 1 266 ? 6.635   1.449   39.571  1.00 13.43 ? 301 SER A CA  1 
ATOM   1978 C  C   . SER A 1 266 ? 5.128   1.574   39.695  1.00 19.24 ? 301 SER A C   1 
ATOM   1979 O  O   . SER A 1 266 ? 4.404   0.566   39.633  1.00 15.98 ? 301 SER A O   1 
ATOM   1980 C  CB  . SER A 1 266 ? 7.239   1.304   40.970  1.00 20.34 ? 301 SER A CB  1 
ATOM   1981 O  OG  . SER A 1 266 ? 8.671   1.348   40.961  1.00 26.98 ? 301 SER A OG  1 
ATOM   1982 N  N   . HIS A 1 267 ? 4.638   2.786   39.941  1.00 13.80 ? 302 HIS A N   1 
ATOM   1983 C  CA  . HIS A 1 267 ? 3.221   2.997   40.214  1.00 17.07 ? 302 HIS A CA  1 
ATOM   1984 C  C   . HIS A 1 267 ? 2.494   3.798   39.147  1.00 17.34 ? 302 HIS A C   1 
ATOM   1985 O  O   . HIS A 1 267 ? 1.344   4.212   39.388  1.00 18.69 ? 302 HIS A O   1 
ATOM   1986 C  CB  . HIS A 1 267 ? 3.064   3.653   41.586  1.00 17.70 ? 302 HIS A CB  1 
ATOM   1987 C  CG  . HIS A 1 267 ? 3.761   2.882   42.652  1.00 22.35 ? 302 HIS A CG  1 
ATOM   1988 N  ND1 . HIS A 1 267 ? 3.453   1.564   42.929  1.00 20.20 ? 302 HIS A ND1 1 
ATOM   1989 C  CD2 . HIS A 1 267 ? 4.805   3.200   43.449  1.00 22.25 ? 302 HIS A CD2 1 
ATOM   1990 C  CE1 . HIS A 1 267 ? 4.243   1.121   43.890  1.00 17.46 ? 302 HIS A CE1 1 
ATOM   1991 N  NE2 . HIS A 1 267 ? 5.085   2.090   44.205  1.00 17.49 ? 302 HIS A NE2 1 
ATOM   1992 N  N   . LEU A 1 268 ? 3.086   3.986   37.963  1.00 14.47 ? 303 LEU A N   1 
ATOM   1993 C  CA  . LEU A 1 268 ? 2.243   4.391   36.854  1.00 14.97 ? 303 LEU A CA  1 
ATOM   1994 C  C   . LEU A 1 268 ? 1.380   3.201   36.409  1.00 14.22 ? 303 LEU A C   1 
ATOM   1995 O  O   . LEU A 1 268 ? 1.716   2.027   36.645  1.00 18.86 ? 303 LEU A O   1 
ATOM   1996 C  CB  . LEU A 1 268 ? 3.084   4.932   35.691  1.00 17.27 ? 303 LEU A CB  1 
ATOM   1997 C  CG  . LEU A 1 268 ? 3.965   6.178   35.905  1.00 19.35 ? 303 LEU A CG  1 
ATOM   1998 C  CD1 . LEU A 1 268 ? 4.743   6.464   34.648  1.00 18.22 ? 303 LEU A CD1 1 
ATOM   1999 C  CD2 . LEU A 1 268 ? 3.046   7.357   36.201  1.00 15.98 ? 303 LEU A CD2 1 
ATOM   2000 N  N   . SER A 1 269 ? 0.236   3.500   35.805  1.00 13.70 ? 304 SER A N   1 
ATOM   2001 C  CA  . SER A 1 269 ? -0.679  2.448   35.379  1.00 15.63 ? 304 SER A CA  1 
ATOM   2002 C  C   . SER A 1 269 ? 0.034   1.379   34.539  1.00 18.00 ? 304 SER A C   1 
ATOM   2003 O  O   . SER A 1 269 ? 0.602   1.697   33.494  1.00 17.52 ? 304 SER A O   1 
ATOM   2004 C  CB  . SER A 1 269 ? -1.816  3.084   34.585  1.00 22.49 ? 304 SER A CB  1 
ATOM   2005 O  OG  . SER A 1 269 ? -2.785  2.120   34.220  1.00 19.27 ? 304 SER A OG  1 
ATOM   2006 N  N   . PHE A 1 270 ? -0.057  0.108   34.964  1.00 14.20 ? 305 PHE A N   1 
ATOM   2007 C  CA  . PHE A 1 270 ? 0.725   -0.961  34.347  1.00 15.54 ? 305 PHE A CA  1 
ATOM   2008 C  C   . PHE A 1 270 ? 0.500   -0.957  32.832  1.00 16.43 ? 305 PHE A C   1 
ATOM   2009 O  O   . PHE A 1 270 ? -0.656  -0.864  32.389  1.00 15.49 ? 305 PHE A O   1 
ATOM   2010 C  CB  . PHE A 1 270 ? 0.305   -2.322  34.928  1.00 19.75 ? 305 PHE A CB  1 
ATOM   2011 C  CG  . PHE A 1 270 ? 1.045   -3.465  34.334  1.00 14.71 ? 305 PHE A CG  1 
ATOM   2012 C  CD1 . PHE A 1 270 ? 2.316   -3.732  34.766  1.00 16.76 ? 305 PHE A CD1 1 
ATOM   2013 C  CD2 . PHE A 1 270 ? 0.482   -4.269  33.361  1.00 14.18 ? 305 PHE A CD2 1 
ATOM   2014 C  CE1 . PHE A 1 270 ? 3.067   -4.787  34.208  1.00 20.58 ? 305 PHE A CE1 1 
ATOM   2015 C  CE2 . PHE A 1 270 ? 1.211   -5.339  32.800  1.00 21.34 ? 305 PHE A CE2 1 
ATOM   2016 C  CZ  . PHE A 1 270 ? 2.492   -5.599  33.224  1.00 21.35 ? 305 PHE A CZ  1 
ATOM   2017 N  N   . PRO A 1 271 ? 1.560   -1.070  32.012  1.00 14.57 ? 306 PRO A N   1 
ATOM   2018 C  CA  . PRO A 1 271 ? 2.947   -1.433  32.384  1.00 13.33 ? 306 PRO A CA  1 
ATOM   2019 C  C   . PRO A 1 271 ? 3.777   -0.275  32.887  1.00 17.84 ? 306 PRO A C   1 
ATOM   2020 O  O   . PRO A 1 271 ? 4.909   -0.480  33.297  1.00 15.76 ? 306 PRO A O   1 
ATOM   2021 C  CB  . PRO A 1 271 ? 3.534   -1.956  31.066  1.00 17.78 ? 306 PRO A CB  1 
ATOM   2022 C  CG  . PRO A 1 271 ? 2.804   -1.096  30.012  1.00 16.88 ? 306 PRO A CG  1 
ATOM   2023 C  CD  . PRO A 1 271 ? 1.383   -1.010  30.540  1.00 12.59 ? 306 PRO A CD  1 
ATOM   2024 N  N   . GLY A 1 272 ? 3.252   0.945   32.831  1.00 18.99 ? 307 GLY A N   1 
ATOM   2025 C  CA  . GLY A 1 272 ? 3.954   2.092   33.368  1.00 19.93 ? 307 GLY A CA  1 
ATOM   2026 C  C   . GLY A 1 272 ? 5.106   2.642   32.550  1.00 18.55 ? 307 GLY A C   1 
ATOM   2027 O  O   . GLY A 1 272 ? 5.984   3.278   33.112  1.00 11.87 ? 307 GLY A O   1 
ATOM   2028 N  N   . ILE A 1 273 ? 5.094   2.476   31.239  1.00 20.53 ? 308 ILE A N   1 
ATOM   2029 C  CA  . ILE A 1 273 ? 6.206   2.834   30.360  1.00 14.54 ? 308 ILE A CA  1 
ATOM   2030 C  C   . ILE A 1 273 ? 5.716   3.865   29.368  1.00 16.25 ? 308 ILE A C   1 
ATOM   2031 O  O   . ILE A 1 273 ? 4.639   3.709   28.787  1.00 17.27 ? 308 ILE A O   1 
ATOM   2032 C  CB  . ILE A 1 273 ? 6.752   1.603   29.591  1.00 13.15 ? 308 ILE A CB  1 
ATOM   2033 C  CG1 . ILE A 1 273 ? 7.166   0.455   30.482  1.00 15.89 ? 308 ILE A CG1 1 
ATOM   2034 C  CG2 . ILE A 1 273 ? 7.818   2.021   28.539  1.00 19.54 ? 308 ILE A CG2 1 
ATOM   2035 C  CD1 . ILE A 1 273 ? 7.431   -0.806  29.629  1.00 12.36 ? 308 ILE A CD1 1 
ATOM   2036 N  N   . GLY A 1 274 ? 6.493   4.920   29.155  1.00 16.91 ? 309 GLY A N   1 
ATOM   2037 C  CA  . GLY A 1 274 ? 6.062   5.859   28.135  1.00 17.38 ? 309 GLY A CA  1 
ATOM   2038 C  C   . GLY A 1 274 ? 7.026   7.021   28.040  1.00 17.88 ? 309 GLY A C   1 
ATOM   2039 O  O   . GLY A 1 274 ? 8.061   7.059   28.707  1.00 17.81 ? 309 GLY A O   1 
ATOM   2040 N  N   . HIS A 1 275 ? 6.685   7.962   27.175  1.00 19.59 ? 310 HIS A N   1 
ATOM   2041 C  CA  . HIS A 1 275 ? 7.484   9.167   26.996  1.00 19.73 ? 310 HIS A CA  1 
ATOM   2042 C  C   . HIS A 1 275 ? 6.905   10.315  27.822  1.00 25.55 ? 310 HIS A C   1 
ATOM   2043 O  O   . HIS A 1 275 ? 5.805   10.244  28.365  1.00 26.28 ? 310 HIS A O   1 
ATOM   2044 C  CB  . HIS A 1 275 ? 7.540   9.596   25.519  1.00 20.53 ? 310 HIS A CB  1 
ATOM   2045 C  CG  . HIS A 1 275 ? 8.243   8.632   24.625  1.00 25.22 ? 310 HIS A CG  1 
ATOM   2046 N  ND1 . HIS A 1 275 ? 7.581   7.617   23.966  1.00 23.99 ? 310 HIS A ND1 1 
ATOM   2047 C  CD2 . HIS A 1 275 ? 9.552   8.499   24.309  1.00 26.89 ? 310 HIS A CD2 1 
ATOM   2048 C  CE1 . HIS A 1 275 ? 8.453   6.913   23.265  1.00 32.46 ? 310 HIS A CE1 1 
ATOM   2049 N  NE2 . HIS A 1 275 ? 9.659   7.409   23.477  1.00 29.49 ? 310 HIS A NE2 1 
ATOM   2050 N  N   . ILE A 1 276 ? 7.633   11.419  27.856  1.00 22.92 ? 311 ILE A N   1 
ATOM   2051 C  CA  . ILE A 1 276 ? 7.232   12.570  28.649  1.00 24.34 ? 311 ILE A CA  1 
ATOM   2052 C  C   . ILE A 1 276 ? 7.524   13.808  27.829  1.00 32.25 ? 311 ILE A C   1 
ATOM   2053 O  O   . ILE A 1 276 ? 8.583   13.898  27.202  1.00 30.18 ? 311 ILE A O   1 
ATOM   2054 C  CB  . ILE A 1 276 ? 7.972   12.613  30.005  1.00 27.85 ? 311 ILE A CB  1 
ATOM   2055 C  CG1 . ILE A 1 276 ? 7.474   13.758  30.888  1.00 33.39 ? 311 ILE A CG1 1 
ATOM   2056 C  CG2 . ILE A 1 276 ? 9.420   12.785  29.819  1.00 29.08 ? 311 ILE A CG2 1 
ATOM   2057 C  CD1 . ILE A 1 276 ? 6.042   13.681  31.136  1.00 36.69 ? 311 ILE A CD1 1 
ATOM   2058 N  N   . ARG A 1 277 ? 6.583   14.749  27.799  1.00 27.18 ? 312 ARG A N   1 
ATOM   2059 C  CA  . ARG A 1 277 ? 6.867   16.045  27.202  1.00 37.17 ? 312 ARG A CA  1 
ATOM   2060 C  C   . ARG A 1 277 ? 6.397   17.156  28.113  1.00 31.23 ? 312 ARG A C   1 
ATOM   2061 O  O   . ARG A 1 277 ? 5.456   17.007  28.898  1.00 31.45 ? 312 ARG A O   1 
ATOM   2062 C  CB  . ARG A 1 277 ? 6.251   16.238  25.803  1.00 34.64 ? 312 ARG A CB  1 
ATOM   2063 C  CG  . ARG A 1 277 ? 4.806   15.905  25.688  1.00 37.82 ? 312 ARG A CG  1 
ATOM   2064 C  CD  . ARG A 1 277 ? 4.314   16.200  24.286  1.00 36.58 ? 312 ARG A CD  1 
ATOM   2065 N  NE  . ARG A 1 277 ? 2.957   16.720  24.279  1.00 43.15 ? 312 ARG A NE  1 
ATOM   2066 C  CZ  . ARG A 1 277 ? 1.894   15.971  24.017  1.00 48.38 ? 312 ARG A CZ  1 
ATOM   2067 N  NH1 . ARG A 1 277 ? 2.011   14.674  23.758  1.00 44.41 ? 312 ARG A NH1 1 
ATOM   2068 N  NH2 . ARG A 1 277 ? 0.687   16.535  24.009  1.00 62.85 ? 312 ARG A NH2 1 
ATOM   2069 N  N   . ALA A 1 278 ? 7.113   18.257  28.009  1.00 32.88 ? 313 ALA A N   1 
ATOM   2070 C  CA  . ALA A 1 278 ? 6.742   19.471  28.707  1.00 38.25 ? 313 ALA A CA  1 
ATOM   2071 C  C   . ALA A 1 278 ? 5.367   19.936  28.256  1.00 38.41 ? 313 ALA A C   1 
ATOM   2072 O  O   . ALA A 1 278 ? 5.047   19.931  27.062  1.00 45.96 ? 313 ALA A O   1 
ATOM   2073 C  CB  . ALA A 1 278 ? 7.784   20.548  28.439  1.00 44.45 ? 313 ALA A CB  1 
ATOM   2074 N  N   . GLU A 1 279 ? 4.546   20.336  29.221  1.00 38.83 ? 314 GLU A N   1 
ATOM   2075 C  CA  . GLU A 1 279 ? 3.244   20.918  28.920  1.00 41.43 ? 314 GLU A CA  1 
ATOM   2076 C  C   . GLU A 1 279 ? 2.933   21.917  30.026  1.00 48.88 ? 314 GLU A C   1 
ATOM   2077 O  O   . GLU A 1 279 ? 2.812   21.526  31.191  1.00 42.99 ? 314 GLU A O   1 
ATOM   2078 C  CB  . GLU A 1 279 ? 2.192   19.820  28.827  1.00 40.55 ? 314 GLU A CB  1 
ATOM   2079 C  CG  . GLU A 1 279 ? 0.934   20.233  28.146  1.00 56.03 ? 314 GLU A CG  1 
ATOM   2080 C  CD  . GLU A 1 279 ? 1.046   19.934  26.669  1.00 60.85 ? 314 GLU A CD  1 
ATOM   2081 O  OE1 . GLU A 1 279 ? 0.283   19.084  26.173  1.00 51.14 ? 314 GLU A OE1 1 
ATOM   2082 O  OE2 . GLU A 1 279 ? 1.899   20.567  26.002  1.00 60.05 ? 314 GLU A OE2 1 
ATOM   2083 N  N   . GLY A 1 280 ? 2.853   23.205  29.681  1.00 46.96 ? 315 GLY A N   1 
ATOM   2084 C  CA  . GLY A 1 280 ? 2.551   24.194  30.698  1.00 49.55 ? 315 GLY A CA  1 
ATOM   2085 C  C   . GLY A 1 280 ? 3.590   24.210  31.799  1.00 48.03 ? 315 GLY A C   1 
ATOM   2086 O  O   . GLY A 1 280 ? 4.788   24.008  31.564  1.00 46.58 ? 315 GLY A O   1 
ATOM   2087 N  N   . LYS A 1 281 ? 3.117   24.461  33.028  1.00 49.33 ? 316 LYS A N   1 
ATOM   2088 C  CA  . LYS A 1 281 ? 3.946   24.371  34.229  1.00 48.26 ? 316 LYS A CA  1 
ATOM   2089 C  C   . LYS A 1 281 ? 4.474   22.970  34.489  1.00 46.88 ? 316 LYS A C   1 
ATOM   2090 O  O   . LYS A 1 281 ? 5.365   22.802  35.334  1.00 43.89 ? 316 LYS A O   1 
ATOM   2091 C  CB  . LYS A 1 281 ? 3.164   24.817  35.468  1.00 50.81 ? 316 LYS A CB  1 
ATOM   2092 C  CG  . LYS A 1 281 ? 2.550   26.218  35.454  1.00 57.36 ? 316 LYS A CG  1 
ATOM   2093 C  CD  . LYS A 1 281 ? 3.571   27.259  35.045  1.00 55.98 ? 316 LYS A CD  1 
ATOM   2094 C  CE  . LYS A 1 281 ? 3.430   28.483  35.950  1.00 67.66 ? 316 LYS A CE  1 
ATOM   2095 N  NZ  . LYS A 1 281 ? 4.274   29.645  35.559  1.00 61.44 ? 316 LYS A NZ  1 
ATOM   2096 N  N   . GLY A 1 282 ? 3.923   21.953  33.834  1.00 43.41 ? 317 GLY A N   1 
ATOM   2097 C  CA  . GLY A 1 282 ? 4.367   20.607  34.115  1.00 43.38 ? 317 GLY A CA  1 
ATOM   2098 C  C   . GLY A 1 282 ? 4.633   19.769  32.882  1.00 38.76 ? 317 GLY A C   1 
ATOM   2099 O  O   . GLY A 1 282 ? 5.291   20.220  31.943  1.00 37.51 ? 317 GLY A O   1 
ATOM   2100 N  N   . TYR A 1 283 ? 4.071   18.562  32.860  1.00 35.88 ? 318 TYR A N   1 
ATOM   2101 C  CA  . TYR A 1 283 ? 4.395   17.544  31.874  1.00 33.47 ? 318 TYR A CA  1 
ATOM   2102 C  C   . TYR A 1 283 ? 3.160   16.705  31.586  1.00 36.73 ? 318 TYR A C   1 
ATOM   2103 O  O   . TYR A 1 283 ? 2.282   16.549  32.447  1.00 37.66 ? 318 TYR A O   1 
ATOM   2104 C  CB  . TYR A 1 283 ? 5.523   16.652  32.387  1.00 31.12 ? 318 TYR A CB  1 
ATOM   2105 C  CG  . TYR A 1 283 ? 6.832   17.371  32.597  1.00 39.41 ? 318 TYR A CG  1 
ATOM   2106 C  CD1 . TYR A 1 283 ? 7.758   17.470  31.570  1.00 38.15 ? 318 TYR A CD1 1 
ATOM   2107 C  CD2 . TYR A 1 283 ? 7.125   17.986  33.812  1.00 32.72 ? 318 TYR A CD2 1 
ATOM   2108 C  CE1 . TYR A 1 283 ? 8.946   18.141  31.746  1.00 34.72 ? 318 TYR A CE1 1 
ATOM   2109 C  CE2 . TYR A 1 283 ? 8.318   18.677  33.999  1.00 38.01 ? 318 TYR A CE2 1 
ATOM   2110 C  CZ  . TYR A 1 283 ? 9.222   18.735  32.959  1.00 35.48 ? 318 TYR A CZ  1 
ATOM   2111 O  OH  . TYR A 1 283 ? 10.408  19.393  33.116  1.00 41.66 ? 318 TYR A OH  1 
ATOM   2112 N  N   . ARG A 1 284 ? 3.192   16.055  30.412  1.00 35.96 ? 319 ARG A N   1 
ATOM   2113 C  CA  . ARG A 1 284 ? 2.105   15.127  30.004  1.00 35.37 ? 319 ARG A CA  1 
ATOM   2114 C  C   . ARG A 1 284 ? 2.745   13.778  29.620  1.00 34.05 ? 319 ARG A C   1 
ATOM   2115 O  O   . ARG A 1 284 ? 3.599   13.773  28.703  1.00 27.45 ? 319 ARG A O   1 
ATOM   2116 C  CB  . ARG A 1 284 ? 1.312   15.742  28.845  1.00 40.70 ? 319 ARG A CB  1 
ATOM   2117 C  CG  . ARG A 1 284 ? 0.668   14.748  27.888  1.00 60.22 ? 319 ARG A CG  1 
ATOM   2118 C  CD  . ARG A 1 284 ? -0.618  15.292  27.291  1.00 62.76 ? 319 ARG A CD  1 
ATOM   2119 N  NE  . ARG A 1 284 ? -1.650  15.485  28.315  1.00 73.91 ? 319 ARG A NE  1 
ATOM   2120 C  CZ  . ARG A 1 284 ? -2.380  16.584  28.451  1.00 74.85 ? 319 ARG A CZ  1 
ATOM   2121 N  NH1 . ARG A 1 284 ? -2.005  17.703  27.857  1.00 91.43 ? 319 ARG A NH1 1 
ATOM   2122 N  NH2 . ARG A 1 284 ? -3.483  16.560  29.177  1.00 60.07 ? 319 ARG A NH2 1 
ATOM   2123 N  N   . PHE A 1 285 ? 2.380   12.690  30.306  1.00 29.99 ? 320 PHE A N   1 
ATOM   2124 C  CA  . PHE A 1 285 ? 2.919   11.329  30.046  1.00 25.42 ? 320 PHE A CA  1 
ATOM   2125 C  C   . PHE A 1 285 ? 2.255   10.761  28.812  1.00 25.76 ? 320 PHE A C   1 
ATOM   2126 O  O   . PHE A 1 285 ? 1.031   10.838  28.697  1.00 29.08 ? 320 PHE A O   1 
ATOM   2127 C  CB  . PHE A 1 285 ? 2.578   10.429  31.226  1.00 28.24 ? 320 PHE A CB  1 
ATOM   2128 C  CG  . PHE A 1 285 ? 3.124   9.014   31.164  1.00 29.24 ? 320 PHE A CG  1 
ATOM   2129 C  CD1 . PHE A 1 285 ? 4.490   8.784   31.075  1.00 25.93 ? 320 PHE A CD1 1 
ATOM   2130 C  CD2 . PHE A 1 285 ? 2.269   7.922   31.216  1.00 23.39 ? 320 PHE A CD2 1 
ATOM   2131 C  CE1 . PHE A 1 285 ? 4.982   7.493   31.033  1.00 20.63 ? 320 PHE A CE1 1 
ATOM   2132 C  CE2 . PHE A 1 285 ? 2.769   6.634   31.170  1.00 25.91 ? 320 PHE A CE2 1 
ATOM   2133 C  CZ  . PHE A 1 285 ? 4.120   6.425   31.081  1.00 24.03 ? 320 PHE A CZ  1 
ATOM   2134 N  N   . VAL A 1 286 ? 3.050   10.187  27.919  1.00 23.69 ? 321 VAL A N   1 
ATOM   2135 C  CA  . VAL A 1 286 ? 2.513   9.565   26.721  1.00 23.60 ? 321 VAL A CA  1 
ATOM   2136 C  C   . VAL A 1 286 ? 2.831   8.075   26.787  1.00 21.60 ? 321 VAL A C   1 
ATOM   2137 O  O   . VAL A 1 286 ? 3.977   7.669   26.532  1.00 20.13 ? 321 VAL A O   1 
ATOM   2138 C  CB  . VAL A 1 286 ? 3.069   10.221  25.449  1.00 24.10 ? 321 VAL A CB  1 
ATOM   2139 C  CG1 . VAL A 1 286 ? 2.432   9.598   24.215  1.00 24.47 ? 321 VAL A CG1 1 
ATOM   2140 C  CG2 . VAL A 1 286 ? 2.771   11.764  25.463  1.00 26.53 ? 321 VAL A CG2 1 
ATOM   2141 N  N   . PRO A 1 287 ? 1.854   7.241   27.142  1.00 21.86 ? 322 PRO A N   1 
ATOM   2142 C  CA  . PRO A 1 287 ? 2.104   5.795   27.240  1.00 20.59 ? 322 PRO A CA  1 
ATOM   2143 C  C   . PRO A 1 287 ? 2.646   5.245   25.931  1.00 19.24 ? 322 PRO A C   1 
ATOM   2144 O  O   . PRO A 1 287 ? 2.245   5.666   24.845  1.00 20.15 ? 322 PRO A O   1 
ATOM   2145 C  CB  . PRO A 1 287 ? 0.722   5.214   27.565  1.00 21.62 ? 322 PRO A CB  1 
ATOM   2146 C  CG  . PRO A 1 287 ? -0.036  6.387   28.196  1.00 23.82 ? 322 PRO A CG  1 
ATOM   2147 C  CD  . PRO A 1 287 ? 0.485   7.631   27.548  1.00 24.10 ? 322 PRO A CD  1 
ATOM   2148 N  N   . VAL A 1 288 ? 3.596   4.320   26.049  1.00 17.68 ? 323 VAL A N   1 
ATOM   2149 C  CA  . VAL A 1 288 ? 4.237   3.776   24.867  1.00 18.62 ? 323 VAL A CA  1 
ATOM   2150 C  C   . VAL A 1 288 ? 3.189   3.152   23.942  1.00 20.29 ? 323 VAL A C   1 
ATOM   2151 O  O   . VAL A 1 288 ? 2.217   2.520   24.388  1.00 17.91 ? 323 VAL A O   1 
ATOM   2152 C  CB  . VAL A 1 288 ? 5.324   2.765   25.281  1.00 15.65 ? 323 VAL A CB  1 
ATOM   2153 C  CG1 . VAL A 1 288 ? 4.735   1.635   26.134  1.00 17.86 ? 323 VAL A CG1 1 
ATOM   2154 C  CG2 . VAL A 1 288 ? 6.035   2.216   24.043  1.00 21.53 ? 323 VAL A CG2 1 
ATOM   2155 N  N   . ASN A 1 289 ? 3.356   3.393   22.646  1.00 20.16 ? 324 ASN A N   1 
ATOM   2156 C  CA  . ASN A 1 289 ? 2.502   2.792   21.631  1.00 18.77 ? 324 ASN A CA  1 
ATOM   2157 C  C   . ASN A 1 289 ? 2.602   1.270   21.721  1.00 18.28 ? 324 ASN A C   1 
ATOM   2158 O  O   . ASN A 1 289 ? 3.709   0.722   21.785  1.00 16.43 ? 324 ASN A O   1 
ATOM   2159 C  CB  . ASN A 1 289 ? 2.968   3.281   20.257  1.00 19.64 ? 324 ASN A CB  1 
ATOM   2160 C  CG  . ASN A 1 289 ? 2.062   2.847   19.132  1.00 24.19 ? 324 ASN A CG  1 
ATOM   2161 O  OD1 . ASN A 1 289 ? 0.841   3.005   19.212  1.00 28.32 ? 324 ASN A OD1 1 
ATOM   2162 N  ND2 . ASN A 1 289 ? 2.649   2.351   18.044  1.00 22.46 ? 324 ASN A ND2 1 
ATOM   2163 N  N   . TYR A 1 290 ? 1.447   0.585   21.721  1.00 18.36 ? 325 TYR A N   1 
ATOM   2164 C  CA  . TYR A 1 290 ? 1.449   -0.879  21.770  1.00 17.65 ? 325 TYR A CA  1 
ATOM   2165 C  C   . TYR A 1 290 ? 2.164   -1.424  20.541  1.00 17.28 ? 325 TYR A C   1 
ATOM   2166 O  O   . TYR A 1 290 ? 1.942   -0.955  19.420  1.00 18.37 ? 325 TYR A O   1 
ATOM   2167 C  CB  . TYR A 1 290 ? 0.015   -1.449  21.854  1.00 19.07 ? 325 TYR A CB  1 
ATOM   2168 C  CG  . TYR A 1 290 ? -0.008  -2.978  21.839  1.00 18.64 ? 325 TYR A CG  1 
ATOM   2169 C  CD1 . TYR A 1 290 ? 0.338   -3.713  22.972  1.00 18.88 ? 325 TYR A CD1 1 
ATOM   2170 C  CD2 . TYR A 1 290 ? -0.397  -3.693  20.680  1.00 20.49 ? 325 TYR A CD2 1 
ATOM   2171 C  CE1 . TYR A 1 290 ? 0.328   -5.143  22.955  1.00 22.14 ? 325 TYR A CE1 1 
ATOM   2172 C  CE2 . TYR A 1 290 ? -0.423  -5.124  20.659  1.00 19.18 ? 325 TYR A CE2 1 
ATOM   2173 C  CZ  . TYR A 1 290 ? -0.056  -5.828  21.796  1.00 23.03 ? 325 TYR A CZ  1 
ATOM   2174 O  OH  . TYR A 1 290 ? -0.061  -7.216  21.768  1.00 21.40 ? 325 TYR A OH  1 
ATOM   2175 N  N   . SER A 1 291 ? 3.060   -2.387  20.764  1.00 16.27 ? 326 SER A N   1 
ATOM   2176 C  CA  . SER A 1 291 ? 3.842   -2.959  19.686  1.00 19.49 ? 326 SER A CA  1 
ATOM   2177 C  C   . SER A 1 291 ? 3.955   -4.463  19.910  1.00 24.26 ? 326 SER A C   1 
ATOM   2178 O  O   . SER A 1 291 ? 4.003   -4.932  21.050  1.00 24.37 ? 326 SER A O   1 
ATOM   2179 C  CB  . SER A 1 291 ? 5.218   -2.259  19.599  1.00 17.91 ? 326 SER A CB  1 
ATOM   2180 O  OG  . SER A 1 291 ? 5.928   -2.671  18.446  1.00 26.60 ? 326 SER A OG  1 
ATOM   2181 N  N   . VAL A 1 292 ? 3.927   -5.226  18.827  1.00 20.91 ? 327 VAL A N   1 
ATOM   2182 C  CA  . VAL A 1 292 ? 3.949   -6.677  18.930  1.00 22.19 ? 327 VAL A CA  1 
ATOM   2183 C  C   . VAL A 1 292 ? 5.414   -7.102  18.887  1.00 26.53 ? 327 VAL A C   1 
ATOM   2184 O  O   . VAL A 1 292 ? 6.191   -6.581  18.079  1.00 26.08 ? 327 VAL A O   1 
ATOM   2185 C  CB  . VAL A 1 292 ? 3.128   -7.308  17.791  1.00 25.53 ? 327 VAL A CB  1 
ATOM   2186 C  CG1 . VAL A 1 292 ? 3.436   -8.799  17.632  1.00 24.65 ? 327 VAL A CG1 1 
ATOM   2187 C  CG2 . VAL A 1 292 ? 1.625   -7.022  17.981  1.00 19.87 ? 327 VAL A CG2 1 
ATOM   2188 N  N   . VAL A 1 293 ? 5.822   -7.984  19.792  1.00 22.96 ? 328 VAL A N   1 
ATOM   2189 C  CA  . VAL A 1 293 ? 7.200   -8.488  19.816  1.00 26.34 ? 328 VAL A CA  1 
ATOM   2190 C  C   . VAL A 1 293 ? 7.174   -9.940  19.352  1.00 29.74 ? 328 VAL A C   1 
ATOM   2191 O  O   . VAL A 1 293 ? 6.426   -10.759 19.902  1.00 28.97 ? 328 VAL A O   1 
ATOM   2192 C  CB  . VAL A 1 293 ? 7.850   -8.374  21.212  1.00 22.78 ? 328 VAL A CB  1 
ATOM   2193 C  CG1 . VAL A 1 293 ? 9.271   -8.968  21.187  1.00 24.57 ? 328 VAL A CG1 1 
ATOM   2194 C  CG2 . VAL A 1 293 ? 7.910   -6.912  21.687  1.00 17.73 ? 328 VAL A CG2 1 
ATOM   2195 N  N   . ASN A 1 294 ? 7.978   -10.253 18.341  1.00 29.79 ? 329 ASN A N   1 
ATOM   2196 C  CA  . ASN A 1 294 ? 8.107   -11.624 17.825  1.00 35.75 ? 329 ASN A CA  1 
ATOM   2197 C  C   . ASN A 1 294 ? 9.520   -12.148 18.063  1.00 31.80 ? 329 ASN A C   1 
ATOM   2198 O  O   . ASN A 1 294 ? 10.486  -11.407 17.894  1.00 33.23 ? 329 ASN A O   1 
ATOM   2199 C  CB  . ASN A 1 294 ? 7.800   -11.679 16.330  1.00 35.82 ? 329 ASN A CB  1 
ATOM   2200 C  CG  . ASN A 1 294 ? 6.357   -11.347 16.017  1.00 37.88 ? 329 ASN A CG  1 
ATOM   2201 O  OD1 . ASN A 1 294 ? 5.436   -11.875 16.637  1.00 35.98 ? 329 ASN A OD1 1 
ATOM   2202 N  ND2 . ASN A 1 294 ? 6.157   -10.431 15.082  1.00 33.03 ? 329 ASN A ND2 1 
ATOM   2203 N  N   . ALA B 1 1   ? 22.986  -15.690 29.429  1.00 42.62 ? 36  ALA B N   1 
ATOM   2204 C  CA  . ALA B 1 1   ? 22.830  -17.014 28.855  1.00 33.79 ? 36  ALA B CA  1 
ATOM   2205 C  C   . ALA B 1 1   ? 21.368  -17.452 28.906  1.00 35.03 ? 36  ALA B C   1 
ATOM   2206 O  O   . ALA B 1 1   ? 20.981  -18.366 28.181  1.00 42.55 ? 36  ALA B O   1 
ATOM   2207 C  CB  . ALA B 1 1   ? 23.752  -18.054 29.571  1.00 35.37 ? 36  ALA B CB  1 
ATOM   2208 N  N   . ALA B 1 2   ? 20.551  -16.803 29.740  1.00 34.10 ? 37  ALA B N   1 
ATOM   2209 C  CA  . ALA B 1 2   ? 19.106  -17.002 29.639  1.00 30.94 ? 37  ALA B CA  1 
ATOM   2210 C  C   . ALA B 1 2   ? 18.639  -16.497 28.281  1.00 29.87 ? 37  ALA B C   1 
ATOM   2211 O  O   . ALA B 1 2   ? 18.886  -15.332 27.945  1.00 31.94 ? 37  ALA B O   1 
ATOM   2212 C  CB  . ALA B 1 2   ? 18.365  -16.265 30.753  1.00 37.09 ? 37  ALA B CB  1 
ATOM   2213 N  N   . PRO B 1 3   ? 17.969  -17.324 27.481  1.00 29.61 ? 38  PRO B N   1 
ATOM   2214 C  CA  . PRO B 1 3   ? 17.483  -16.856 26.181  1.00 31.46 ? 38  PRO B CA  1 
ATOM   2215 C  C   . PRO B 1 3   ? 16.443  -15.746 26.322  1.00 27.35 ? 38  PRO B C   1 
ATOM   2216 O  O   . PRO B 1 3   ? 15.659  -15.703 27.273  1.00 27.97 ? 38  PRO B O   1 
ATOM   2217 C  CB  . PRO B 1 3   ? 16.873  -18.120 25.562  1.00 40.19 ? 38  PRO B CB  1 
ATOM   2218 C  CG  . PRO B 1 3   ? 16.468  -18.949 26.754  1.00 44.65 ? 38  PRO B CG  1 
ATOM   2219 C  CD  . PRO B 1 3   ? 17.556  -18.711 27.762  1.00 33.27 ? 38  PRO B CD  1 
ATOM   2220 N  N   . GLN B 1 4   ? 16.449  -14.831 25.360  1.00 26.71 ? 39  GLN B N   1 
ATOM   2221 C  CA  . GLN B 1 4   ? 15.321  -13.918 25.235  1.00 25.45 ? 39  GLN B CA  1 
ATOM   2222 C  C   . GLN B 1 4   ? 14.106  -14.681 24.717  1.00 26.39 ? 39  GLN B C   1 
ATOM   2223 O  O   . GLN B 1 4   ? 14.228  -15.571 23.874  1.00 33.16 ? 39  GLN B O   1 
ATOM   2224 C  CB  . GLN B 1 4   ? 15.666  -12.753 24.301  1.00 26.11 ? 39  GLN B CB  1 
ATOM   2225 C  CG  . GLN B 1 4   ? 16.797  -11.869 24.822  1.00 27.18 ? 39  GLN B CG  1 
ATOM   2226 C  CD  . GLN B 1 4   ? 17.092  -10.660 23.945  1.00 32.93 ? 39  GLN B CD  1 
ATOM   2227 O  OE1 . GLN B 1 4   ? 16.726  -10.627 22.766  1.00 40.75 ? 39  GLN B OE1 1 
ATOM   2228 N  NE2 . GLN B 1 4   ? 17.714  -9.637  24.533  1.00 27.70 ? 39  GLN B NE2 1 
ATOM   2229 N  N   . VAL B 1 5   ? 12.931  -14.360 25.260  1.00 24.05 ? 40  VAL B N   1 
ATOM   2230 C  CA  . VAL B 1 5   ? 11.699  -15.040 24.873  1.00 26.26 ? 40  VAL B CA  1 
ATOM   2231 C  C   . VAL B 1 5   ? 11.098  -14.387 23.644  1.00 29.59 ? 40  VAL B C   1 
ATOM   2232 O  O   . VAL B 1 5   ? 10.726  -15.073 22.680  1.00 22.65 ? 40  VAL B O   1 
ATOM   2233 C  CB  . VAL B 1 5   ? 10.712  -15.043 26.054  1.00 24.11 ? 40  VAL B CB  1 
ATOM   2234 C  CG1 . VAL B 1 5   ? 9.445   -15.796 25.690  1.00 32.09 ? 40  VAL B CG1 1 
ATOM   2235 C  CG2 . VAL B 1 5   ? 11.379  -15.657 27.273  1.00 28.56 ? 40  VAL B CG2 1 
ATOM   2236 N  N   . ARG B 1 6   ? 11.008  -13.044 23.673  1.00 24.84 ? 41  ARG B N   1 
ATOM   2237 C  CA  . ARG B 1 6   ? 10.582  -12.224 22.538  1.00 28.28 ? 41  ARG B CA  1 
ATOM   2238 C  C   . ARG B 1 6   ? 9.221   -12.621 21.980  1.00 24.85 ? 41  ARG B C   1 
ATOM   2239 O  O   . ARG B 1 6   ? 9.016   -12.654 20.774  1.00 24.74 ? 41  ARG B O   1 
ATOM   2240 C  CB  . ARG B 1 6   ? 11.617  -12.221 21.419  1.00 29.14 ? 41  ARG B CB  1 
ATOM   2241 C  CG  . ARG B 1 6   ? 12.793  -11.316 21.707  1.00 33.60 ? 41  ARG B CG  1 
ATOM   2242 C  CD  . ARG B 1 6   ? 13.552  -11.056 20.445  1.00 33.08 ? 41  ARG B CD  1 
ATOM   2243 N  NE  . ARG B 1 6   ? 14.794  -10.346 20.705  1.00 39.66 ? 41  ARG B NE  1 
ATOM   2244 C  CZ  . ARG B 1 6   ? 15.250  -9.354  19.954  1.00 40.49 ? 41  ARG B CZ  1 
ATOM   2245 N  NH1 . ARG B 1 6   ? 14.569  -8.922  18.899  1.00 31.92 ? 41  ARG B NH1 1 
ATOM   2246 N  NH2 . ARG B 1 6   ? 16.424  -8.792  20.261  1.00 34.73 ? 41  ARG B NH2 1 
ATOM   2247 N  N   . THR B 1 7   ? 8.265   -12.885 22.856  1.00 21.68 ? 42  THR B N   1 
ATOM   2248 C  CA  . THR B 1 7   ? 6.863   -13.001 22.459  1.00 26.23 ? 42  THR B CA  1 
ATOM   2249 C  C   . THR B 1 7   ? 6.018   -12.044 23.296  1.00 23.91 ? 42  THR B C   1 
ATOM   2250 O  O   . THR B 1 7   ? 6.187   -11.945 24.519  1.00 27.36 ? 42  THR B O   1 
ATOM   2251 C  CB  . THR B 1 7   ? 6.377   -14.451 22.601  1.00 26.59 ? 42  THR B CB  1 
ATOM   2252 O  OG1 . THR B 1 7   ? 6.386   -14.821 23.988  1.00 34.60 ? 42  THR B OG1 1 
ATOM   2253 C  CG2 . THR B 1 7   ? 7.284   -15.379 21.827  1.00 27.78 ? 42  THR B CG2 1 
ATOM   2254 N  N   . SER B 1 8   ? 5.135   -11.308 22.643  1.00 25.38 ? 43  SER B N   1 
ATOM   2255 C  CA  . SER B 1 8   ? 4.244   -10.459 23.405  1.00 24.74 ? 43  SER B CA  1 
ATOM   2256 C  C   . SER B 1 8   ? 3.319   -11.321 24.255  1.00 24.14 ? 43  SER B C   1 
ATOM   2257 O  O   . SER B 1 8   ? 3.077   -12.485 23.950  1.00 23.13 ? 43  SER B O   1 
ATOM   2258 C  CB  . SER B 1 8   ? 3.459   -9.530  22.467  1.00 22.01 ? 43  SER B CB  1 
ATOM   2259 O  OG  . SER B 1 8   ? 4.333   -8.522  21.939  1.00 23.21 ? 43  SER B OG  1 
ATOM   2260 N  N   . ALA B 1 9   ? 2.826   -10.753 25.358  1.00 24.90 ? 44  ALA B N   1 
ATOM   2261 C  CA  . ALA B 1 9   ? 1.833   -11.463 26.155  1.00 22.87 ? 44  ALA B CA  1 
ATOM   2262 C  C   . ALA B 1 9   ? 0.592   -11.671 25.288  1.00 23.12 ? 44  ALA B C   1 
ATOM   2263 O  O   . ALA B 1 9   ? 0.411   -10.976 24.290  1.00 20.31 ? 44  ALA B O   1 
ATOM   2264 C  CB  . ALA B 1 9   ? 1.478   -10.668 27.419  1.00 23.87 ? 44  ALA B CB  1 
ATOM   2265 N  N   . PRO B 1 10  ? -0.257  -12.644 25.611  1.00 25.87 ? 45  PRO B N   1 
ATOM   2266 C  CA  . PRO B 1 10  ? -1.483  -12.808 24.820  1.00 22.38 ? 45  PRO B CA  1 
ATOM   2267 C  C   . PRO B 1 10  ? -2.241  -11.486 24.774  1.00 20.71 ? 45  PRO B C   1 
ATOM   2268 O  O   . PRO B 1 10  ? -2.302  -10.740 25.761  1.00 21.13 ? 45  PRO B O   1 
ATOM   2269 C  CB  . PRO B 1 10  ? -2.254  -13.904 25.569  1.00 23.72 ? 45  PRO B CB  1 
ATOM   2270 C  CG  . PRO B 1 10  ? -1.198  -14.636 26.353  1.00 32.83 ? 45  PRO B CG  1 
ATOM   2271 C  CD  . PRO B 1 10  ? -0.168  -13.606 26.720  1.00 26.19 ? 45  PRO B CD  1 
ATOM   2272 N  N   . GLY B 1 11  ? -2.726  -11.149 23.579  1.00 19.30 ? 46  GLY B N   1 
ATOM   2273 C  CA  . GLY B 1 11  ? -3.355  -9.870  23.348  1.00 24.18 ? 46  GLY B CA  1 
ATOM   2274 C  C   . GLY B 1 11  ? -4.827  -9.867  23.696  1.00 20.91 ? 46  GLY B C   1 
ATOM   2275 O  O   . GLY B 1 11  ? -5.679  -9.844  22.804  1.00 21.01 ? 46  GLY B O   1 
ATOM   2276 N  N   . TYR B 1 12  ? -5.134  -9.918  24.991  1.00 21.18 ? 47  TYR B N   1 
ATOM   2277 C  CA  . TYR B 1 12  ? -6.478  -9.649  25.466  1.00 23.79 ? 47  TYR B CA  1 
ATOM   2278 C  C   . TYR B 1 12  ? -6.394  -8.829  26.742  1.00 24.31 ? 47  TYR B C   1 
ATOM   2279 O  O   . TYR B 1 12  ? -5.451  -8.968  27.525  1.00 25.25 ? 47  TYR B O   1 
ATOM   2280 C  CB  . TYR B 1 12  ? -7.276  -10.949 25.682  1.00 21.26 ? 47  TYR B CB  1 
ATOM   2281 C  CG  . TYR B 1 12  ? -6.798  -11.852 26.805  1.00 28.44 ? 47  TYR B CG  1 
ATOM   2282 C  CD1 . TYR B 1 12  ? -5.803  -12.823 26.596  1.00 24.66 ? 47  TYR B CD1 1 
ATOM   2283 C  CD2 . TYR B 1 12  ? -7.346  -11.738 28.075  1.00 26.95 ? 47  TYR B CD2 1 
ATOM   2284 C  CE1 . TYR B 1 12  ? -5.380  -13.652 27.627  1.00 23.58 ? 47  TYR B CE1 1 
ATOM   2285 C  CE2 . TYR B 1 12  ? -6.934  -12.559 29.107  1.00 27.05 ? 47  TYR B CE2 1 
ATOM   2286 C  CZ  . TYR B 1 12  ? -5.950  -13.507 28.886  1.00 30.85 ? 47  TYR B CZ  1 
ATOM   2287 O  OH  . TYR B 1 12  ? -5.572  -14.297 29.948  1.00 32.94 ? 47  TYR B OH  1 
ATOM   2288 N  N   . TYR B 1 13  ? -7.400  -7.984  26.951  1.00 19.21 ? 48  TYR B N   1 
ATOM   2289 C  CA  . TYR B 1 13  ? -7.440  -7.073  28.097  1.00 19.89 ? 48  TYR B CA  1 
ATOM   2290 C  C   . TYR B 1 13  ? -8.844  -7.027  28.680  1.00 20.39 ? 48  TYR B C   1 
ATOM   2291 O  O   . TYR B 1 13  ? -9.778  -6.661  27.972  1.00 20.55 ? 48  TYR B O   1 
ATOM   2292 C  CB  . TYR B 1 13  ? -7.017  -5.675  27.670  1.00 19.68 ? 48  TYR B CB  1 
ATOM   2293 C  CG  . TYR B 1 13  ? -6.880  -4.703  28.789  1.00 21.02 ? 48  TYR B CG  1 
ATOM   2294 C  CD1 . TYR B 1 13  ? -8.008  -4.042  29.303  1.00 19.65 ? 48  TYR B CD1 1 
ATOM   2295 C  CD2 . TYR B 1 13  ? -5.610  -4.348  29.272  1.00 24.59 ? 48  TYR B CD2 1 
ATOM   2296 C  CE1 . TYR B 1 13  ? -7.882  -3.129  30.328  1.00 23.76 ? 48  TYR B CE1 1 
ATOM   2297 C  CE2 . TYR B 1 13  ? -5.472  -3.408  30.280  1.00 25.38 ? 48  TYR B CE2 1 
ATOM   2298 C  CZ  . TYR B 1 13  ? -6.594  -2.805  30.797  1.00 27.87 ? 48  TYR B CZ  1 
ATOM   2299 O  OH  . TYR B 1 13  ? -6.429  -1.871  31.798  1.00 28.24 ? 48  TYR B OH  1 
ATOM   2300 N  N   . ARG B 1 14  ? -8.976  -7.348  29.974  1.00 21.84 ? 49  ARG B N   1 
ATOM   2301 C  CA  . ARG B 1 14  ? -10.256 -7.580  30.643  1.00 23.14 ? 49  ARG B CA  1 
ATOM   2302 C  C   . ARG B 1 14  ? -10.663 -6.360  31.453  1.00 27.90 ? 49  ARG B C   1 
ATOM   2303 O  O   . ARG B 1 14  ? -9.828  -5.769  32.148  1.00 23.42 ? 49  ARG B O   1 
ATOM   2304 C  CB  . ARG B 1 14  ? -10.163 -8.777  31.596  1.00 27.61 ? 49  ARG B CB  1 
ATOM   2305 C  CG  . ARG B 1 14  ? -11.481 -9.416  31.978  1.00 33.94 ? 49  ARG B CG  1 
ATOM   2306 C  CD  . ARG B 1 14  ? -11.838 -10.495 31.013  1.00 33.33 ? 49  ARG B CD  1 
ATOM   2307 N  NE  . ARG B 1 14  ? -10.949 -11.636 31.172  1.00 39.93 ? 49  ARG B NE  1 
ATOM   2308 C  CZ  . ARG B 1 14  ? -10.915 -12.677 30.352  1.00 39.41 ? 49  ARG B CZ  1 
ATOM   2309 N  NH1 . ARG B 1 14  ? -11.741 -12.770 29.316  1.00 32.36 ? 49  ARG B NH1 1 
ATOM   2310 N  NH2 . ARG B 1 14  ? -10.016 -13.634 30.562  1.00 38.07 ? 49  ARG B NH2 1 
ATOM   2311 N  N   . MET B 1 15  ? -11.952 -6.010  31.392  1.00 24.73 ? 50  MET B N   1 
ATOM   2312 C  CA  . MET B 1 15  ? -12.446 -4.832  32.090  1.00 27.74 ? 50  MET B CA  1 
ATOM   2313 C  C   . MET B 1 15  ? -13.892 -5.038  32.482  1.00 28.58 ? 50  MET B C   1 
ATOM   2314 O  O   . MET B 1 15  ? -14.705 -5.479  31.670  1.00 29.49 ? 50  MET B O   1 
ATOM   2315 C  CB  . MET B 1 15  ? -12.264 -3.573  31.225  1.00 31.05 ? 50  MET B CB  1 
ATOM   2316 C  CG  . MET B 1 15  ? -12.429 -2.236  31.955  1.00 25.70 ? 50  MET B CG  1 
ATOM   2317 S  SD  . MET B 1 15  ? -12.722 -0.869  30.790  1.00 23.45 ? 50  MET B SD  1 
ATOM   2318 C  CE  . MET B 1 15  ? -14.346 -1.249  30.029  1.00 19.51 ? 50  MET B CE  1 
ATOM   2319 N  N   . LEU B 1 16  ? -14.208 -4.764  33.738  1.00 24.94 ? 51  LEU B N   1 
ATOM   2320 C  CA  . LEU B 1 16  ? -15.600 -4.836  34.141  1.00 32.15 ? 51  LEU B CA  1 
ATOM   2321 C  C   . LEU B 1 16  ? -16.302 -3.554  33.710  1.00 33.19 ? 51  LEU B C   1 
ATOM   2322 O  O   . LEU B 1 16  ? -15.702 -2.478  33.678  1.00 31.87 ? 51  LEU B O   1 
ATOM   2323 C  CB  . LEU B 1 16  ? -15.721 -5.047  35.649  1.00 27.31 ? 51  LEU B CB  1 
ATOM   2324 C  CG  . LEU B 1 16  ? -15.030 -6.286  36.204  1.00 39.76 ? 51  LEU B CG  1 
ATOM   2325 C  CD1 . LEU B 1 16  ? -15.504 -6.526  37.630  1.00 41.23 ? 51  LEU B CD1 1 
ATOM   2326 C  CD2 . LEU B 1 16  ? -15.313 -7.496  35.326  1.00 45.83 ? 51  LEU B CD2 1 
ATOM   2327 N  N   . LEU B 1 17  ? -17.560 -3.681  33.314  1.00 27.71 ? 52  LEU B N   1 
ATOM   2328 C  CA  . LEU B 1 17  ? -18.419 -2.542  33.020  1.00 30.10 ? 52  LEU B CA  1 
ATOM   2329 C  C   . LEU B 1 17  ? -19.740 -2.856  33.711  1.00 33.76 ? 52  LEU B C   1 
ATOM   2330 O  O   . LEU B 1 17  ? -20.585 -3.552  33.153  1.00 31.96 ? 52  LEU B O   1 
ATOM   2331 C  CB  . LEU B 1 17  ? -18.585 -2.335  31.523  1.00 30.22 ? 52  LEU B CB  1 
ATOM   2332 C  CG  . LEU B 1 17  ? -19.376 -1.091  31.106  1.00 31.34 ? 52  LEU B CG  1 
ATOM   2333 C  CD1 . LEU B 1 17  ? -18.493 0.167   31.135  1.00 30.26 ? 52  LEU B CD1 1 
ATOM   2334 C  CD2 . LEU B 1 17  ? -19.950 -1.298  29.722  1.00 23.43 ? 52  LEU B CD2 1 
ATOM   2335 N  N   . GLY B 1 18  ? -19.903 -2.371  34.932  1.00 36.83 ? 53  GLY B N   1 
ATOM   2336 C  CA  . GLY B 1 18  ? -21.092 -2.735  35.684  1.00 26.76 ? 53  GLY B CA  1 
ATOM   2337 C  C   . GLY B 1 18  ? -21.114 -4.236  35.888  1.00 35.94 ? 53  GLY B C   1 
ATOM   2338 O  O   . GLY B 1 18  ? -20.153 -4.825  36.394  1.00 35.20 ? 53  GLY B O   1 
ATOM   2339 N  N   . ASP B 1 19  ? -22.211 -4.881  35.484  1.00 31.08 ? 54  ASP B N   1 
ATOM   2340 C  CA  . ASP B 1 19  ? -22.290 -6.333  35.577  1.00 35.12 ? 54  ASP B CA  1 
ATOM   2341 C  C   . ASP B 1 19  ? -21.817 -7.045  34.314  1.00 37.53 ? 54  ASP B C   1 
ATOM   2342 O  O   . ASP B 1 19  ? -21.850 -8.279  34.274  1.00 39.17 ? 54  ASP B O   1 
ATOM   2343 C  CB  . ASP B 1 19  ? -23.719 -6.769  35.923  1.00 34.22 ? 54  ASP B CB  1 
ATOM   2344 C  CG  . ASP B 1 19  ? -24.127 -6.363  37.335  1.00 48.62 ? 54  ASP B CG  1 
ATOM   2345 O  OD1 . ASP B 1 19  ? -23.232 -6.305  38.210  1.00 47.35 ? 54  ASP B OD1 1 
ATOM   2346 O  OD2 . ASP B 1 19  ? -25.332 -6.113  37.570  1.00 45.16 ? 54  ASP B OD2 1 
ATOM   2347 N  N   . PHE B 1 20  ? -21.380 -6.316  33.291  1.00 27.61 ? 55  PHE B N   1 
ATOM   2348 C  CA  . PHE B 1 20  ? -20.843 -6.945  32.087  1.00 30.73 ? 55  PHE B CA  1 
ATOM   2349 C  C   . PHE B 1 20  ? -19.327 -7.096  32.196  1.00 33.33 ? 55  PHE B C   1 
ATOM   2350 O  O   . PHE B 1 20  ? -18.656 -6.339  32.902  1.00 29.75 ? 55  PHE B O   1 
ATOM   2351 C  CB  . PHE B 1 20  ? -21.163 -6.134  30.828  1.00 28.20 ? 55  PHE B CB  1 
ATOM   2352 C  CG  . PHE B 1 20  ? -22.626 -5.946  30.559  1.00 31.02 ? 55  PHE B CG  1 
ATOM   2353 C  CD1 . PHE B 1 20  ? -23.586 -6.690  31.239  1.00 29.36 ? 55  PHE B CD1 1 
ATOM   2354 C  CD2 . PHE B 1 20  ? -23.044 -5.037  29.594  1.00 22.13 ? 55  PHE B CD2 1 
ATOM   2355 C  CE1 . PHE B 1 20  ? -24.936 -6.504  30.983  1.00 31.76 ? 55  PHE B CE1 1 
ATOM   2356 C  CE2 . PHE B 1 20  ? -24.405 -4.852  29.325  1.00 24.71 ? 55  PHE B CE2 1 
ATOM   2357 C  CZ  . PHE B 1 20  ? -25.350 -5.595  30.021  1.00 24.38 ? 55  PHE B CZ  1 
ATOM   2358 N  N   . GLU B 1 21  ? -18.789 -8.067  31.453  1.00 24.21 ? 56  GLU B N   1 
ATOM   2359 C  CA  . GLU B 1 21  ? -17.347 -8.230  31.279  1.00 26.65 ? 56  GLU B CA  1 
ATOM   2360 C  C   . GLU B 1 21  ? -16.934 -7.890  29.846  1.00 28.74 ? 56  GLU B C   1 
ATOM   2361 O  O   . GLU B 1 21  ? -17.482 -8.428  28.889  1.00 28.43 ? 56  GLU B O   1 
ATOM   2362 C  CB  . GLU B 1 21  ? -16.934 -9.661  31.631  1.00 32.27 ? 56  GLU B CB  1 
ATOM   2363 C  CG  . GLU B 1 21  ? -15.511 -10.022 31.318  1.00 32.77 ? 56  GLU B CG  1 
ATOM   2364 C  CD  . GLU B 1 21  ? -15.353 -11.519 31.049  1.00 44.61 ? 56  GLU B CD  1 
ATOM   2365 O  OE1 . GLU B 1 21  ? -15.672 -11.980 29.927  1.00 35.51 ? 56  GLU B OE1 1 
ATOM   2366 O  OE2 . GLU B 1 21  ? -14.934 -12.237 31.984  1.00 45.99 ? 56  GLU B OE2 1 
ATOM   2367 N  N   . ILE B 1 22  ? -15.959 -7.006  29.699  1.00 26.99 ? 57  ILE B N   1 
ATOM   2368 C  CA  . ILE B 1 22  ? -15.443 -6.583  28.407  1.00 24.96 ? 57  ILE B CA  1 
ATOM   2369 C  C   . ILE B 1 22  ? -14.067 -7.195  28.250  1.00 23.92 ? 57  ILE B C   1 
ATOM   2370 O  O   . ILE B 1 22  ? -13.310 -7.282  29.218  1.00 28.34 ? 57  ILE B O   1 
ATOM   2371 C  CB  . ILE B 1 22  ? -15.371 -5.050  28.305  1.00 23.82 ? 57  ILE B CB  1 
ATOM   2372 C  CG1 . ILE B 1 22  ? -16.624 -4.425  28.900  1.00 20.07 ? 57  ILE B CG1 1 
ATOM   2373 C  CG2 . ILE B 1 22  ? -15.098 -4.606  26.869  1.00 24.02 ? 57  ILE B CG2 1 
ATOM   2374 C  CD1 . ILE B 1 22  ? -17.928 -4.793  28.161  1.00 21.29 ? 57  ILE B CD1 1 
ATOM   2375 N  N   . THR B 1 23  ? -13.766 -7.667  27.047  1.00 19.89 ? 58  THR B N   1 
ATOM   2376 C  CA  . THR B 1 23  ? -12.443 -8.166  26.712  1.00 21.01 ? 58  THR B CA  1 
ATOM   2377 C  C   . THR B 1 23  ? -12.052 -7.538  25.384  1.00 23.51 ? 58  THR B C   1 
ATOM   2378 O  O   . THR B 1 23  ? -12.586 -7.920  24.341  1.00 21.22 ? 58  THR B O   1 
ATOM   2379 C  CB  . THR B 1 23  ? -12.389 -9.697  26.621  1.00 20.43 ? 58  THR B CB  1 
ATOM   2380 O  OG1 . THR B 1 23  ? -12.968 -10.280 27.800  1.00 20.92 ? 58  THR B OG1 1 
ATOM   2381 C  CG2 . THR B 1 23  ? -10.917 -10.119 26.539  1.00 24.51 ? 58  THR B CG2 1 
ATOM   2382 N  N   . ALA B 1 24  ? -11.146 -6.564  25.422  1.00 20.62 ? 59  ALA B N   1 
ATOM   2383 C  CA  . ALA B 1 24  ? -10.511 -6.109  24.196  1.00 14.22 ? 59  ALA B CA  1 
ATOM   2384 C  C   . ALA B 1 24  ? -9.664  -7.263  23.654  1.00 20.25 ? 59  ALA B C   1 
ATOM   2385 O  O   . ALA B 1 24  ? -8.878  -7.854  24.400  1.00 15.91 ? 59  ALA B O   1 
ATOM   2386 C  CB  . ALA B 1 24  ? -9.631  -4.881  24.481  1.00 13.88 ? 59  ALA B CB  1 
ATOM   2387 N  N   . LEU B 1 25  ? -9.806  -7.571  22.363  1.00 18.97 ? 60  LEU B N   1 
ATOM   2388 C  CA  . LEU B 1 25  ? -9.092  -8.672  21.718  1.00 22.41 ? 60  LEU B CA  1 
ATOM   2389 C  C   . LEU B 1 25  ? -8.215  -8.114  20.606  1.00 17.56 ? 60  LEU B C   1 
ATOM   2390 O  O   . LEU B 1 25  ? -8.724  -7.542  19.634  1.00 14.76 ? 60  LEU B O   1 
ATOM   2391 C  CB  . LEU B 1 25  ? -10.054 -9.730  21.153  1.00 18.34 ? 60  LEU B CB  1 
ATOM   2392 C  CG  . LEU B 1 25  ? -10.973 -10.478 22.119  1.00 18.00 ? 60  LEU B CG  1 
ATOM   2393 C  CD1 . LEU B 1 25  ? -12.016 -11.316 21.371  1.00 21.43 ? 60  LEU B CD1 1 
ATOM   2394 C  CD2 . LEU B 1 25  ? -10.174 -11.412 23.042  1.00 23.51 ? 60  LEU B CD2 1 
ATOM   2395 N  N   . SER B 1 26  ? -6.905  -8.298  20.736  1.00 14.97 ? 61  SER B N   1 
ATOM   2396 C  CA  . SER B 1 26  ? -5.990  -7.757  19.740  1.00 13.28 ? 61  SER B CA  1 
ATOM   2397 C  C   . SER B 1 26  ? -5.900  -8.667  18.530  1.00 15.54 ? 61  SER B C   1 
ATOM   2398 O  O   . SER B 1 26  ? -5.719  -9.887  18.668  1.00 17.89 ? 61  SER B O   1 
ATOM   2399 C  CB  . SER B 1 26  ? -4.596  -7.561  20.324  1.00 18.32 ? 61  SER B CB  1 
ATOM   2400 O  OG  . SER B 1 26  ? -3.734  -7.092  19.299  1.00 16.60 ? 61  SER B OG  1 
ATOM   2401 N  N   . ASP B 1 27  ? -6.011  -8.084  17.341  1.00 14.99 ? 62  ASP B N   1 
ATOM   2402 C  CA  . ASP B 1 27  ? -5.748  -8.794  16.092  1.00 17.84 ? 62  ASP B CA  1 
ATOM   2403 C  C   . ASP B 1 27  ? -4.296  -8.676  15.663  1.00 18.27 ? 62  ASP B C   1 
ATOM   2404 O  O   . ASP B 1 27  ? -3.908  -9.270  14.643  1.00 19.71 ? 62  ASP B O   1 
ATOM   2405 C  CB  . ASP B 1 27  ? -6.662  -8.264  14.971  1.00 14.11 ? 62  ASP B CB  1 
ATOM   2406 C  CG  . ASP B 1 27  ? -6.750  -9.218  13.783  1.00 16.37 ? 62  ASP B CG  1 
ATOM   2407 O  OD1 . ASP B 1 27  ? -7.056  -10.405 13.991  1.00 21.34 ? 62  ASP B OD1 1 
ATOM   2408 O  OD2 . ASP B 1 27  ? -6.510  -8.770  12.635  1.00 16.69 ? 62  ASP B OD2 1 
ATOM   2409 N  N   . GLY B 1 28  ? -3.499  -7.940  16.423  1.00 13.39 ? 63  GLY B N   1 
ATOM   2410 C  CA  . GLY B 1 28  ? -2.143  -7.632  16.071  1.00 17.46 ? 63  GLY B CA  1 
ATOM   2411 C  C   . GLY B 1 28  ? -2.010  -6.164  15.733  1.00 17.66 ? 63  GLY B C   1 
ATOM   2412 O  O   . GLY B 1 28  ? -2.865  -5.341  16.050  1.00 17.06 ? 63  GLY B O   1 
ATOM   2413 N  N   . THR B 1 29  ? -0.918  -5.833  15.074  1.00 16.34 ? 64  THR B N   1 
ATOM   2414 C  CA  . THR B 1 29  ? -0.735  -4.476  14.607  1.00 15.63 ? 64  THR B CA  1 
ATOM   2415 C  C   . THR B 1 29  ? -0.289  -4.518  13.159  1.00 18.54 ? 64  THR B C   1 
ATOM   2416 O  O   . THR B 1 29  ? 0.159   -5.554  12.663  1.00 22.21 ? 64  THR B O   1 
ATOM   2417 C  CB  . THR B 1 29  ? 0.296   -3.692  15.433  1.00 21.64 ? 64  THR B CB  1 
ATOM   2418 O  OG1 . THR B 1 29  ? 1.587   -4.251  15.190  1.00 20.51 ? 64  THR B OG1 1 
ATOM   2419 C  CG2 . THR B 1 29  ? -0.016  -3.742  16.930  1.00 21.22 ? 64  THR B CG2 1 
ATOM   2420 N  N   . VAL B 1 30  ? -0.389  -3.372  12.486  1.00 16.91 ? 65  VAL B N   1 
ATOM   2421 C  CA  . VAL B 1 30  ? 0.075   -3.249  11.097  1.00 18.40 ? 65  VAL B CA  1 
ATOM   2422 C  C   . VAL B 1 30  ? 0.606   -1.827  10.876  1.00 16.94 ? 65  VAL B C   1 
ATOM   2423 O  O   . VAL B 1 30  ? 0.064   -0.867  11.427  1.00 14.71 ? 65  VAL B O   1 
ATOM   2424 C  CB  . VAL B 1 30  ? -1.066  -3.625  10.117  1.00 23.54 ? 65  VAL B CB  1 
ATOM   2425 C  CG1 . VAL B 1 30  ? -2.256  -2.709  10.297  1.00 19.32 ? 65  VAL B CG1 1 
ATOM   2426 C  CG2 . VAL B 1 30  ? -0.599  -3.562  8.697   1.00 25.27 ? 65  VAL B CG2 1 
ATOM   2427 N  N   . ASP B 1 31  ? 1.688   -1.684  10.093  1.00 15.87 ? 66  ASP B N   1 
ATOM   2428 C  CA  . ASP B 1 31  ? 2.272   -0.344  9.861   1.00 17.73 ? 66  ASP B CA  1 
ATOM   2429 C  C   . ASP B 1 31  ? 1.530   0.393   8.751   1.00 25.23 ? 66  ASP B C   1 
ATOM   2430 O  O   . ASP B 1 31  ? 1.463   -0.101  7.621   1.00 27.51 ? 66  ASP B O   1 
ATOM   2431 C  CB  . ASP B 1 31  ? 3.759   -0.423  9.478   1.00 19.90 ? 66  ASP B CB  1 
ATOM   2432 C  CG  . ASP B 1 31  ? 4.658   -0.788  10.637  1.00 22.87 ? 66  ASP B CG  1 
ATOM   2433 O  OD1 . ASP B 1 31  ? 4.227   -0.729  11.805  1.00 25.93 ? 66  ASP B OD1 1 
ATOM   2434 O  OD2 . ASP B 1 31  ? 5.818   -1.173  10.375  1.00 33.79 ? 66  ASP B OD2 1 
ATOM   2435 N  N   . LEU B 1 32  ? 1.003   1.595   9.049   1.00 18.24 ? 67  LEU B N   1 
ATOM   2436 C  CA  . LEU B 1 32  ? 0.153   2.317   8.090   1.00 19.25 ? 67  LEU B CA  1 
ATOM   2437 C  C   . LEU B 1 32  ? 0.782   3.642   7.694   1.00 21.78 ? 67  LEU B C   1 
ATOM   2438 O  O   . LEU B 1 32  ? 1.255   4.373   8.568   1.00 23.09 ? 67  LEU B O   1 
ATOM   2439 C  CB  . LEU B 1 32  ? -1.253  2.593   8.654   1.00 16.67 ? 67  LEU B CB  1 
ATOM   2440 C  CG  . LEU B 1 32  ? -2.049  1.328   9.051   1.00 21.46 ? 67  LEU B CG  1 
ATOM   2441 C  CD1 . LEU B 1 32  ? -3.392  1.725   9.618   1.00 22.91 ? 67  LEU B CD1 1 
ATOM   2442 C  CD2 . LEU B 1 32  ? -2.229  0.367   7.890   1.00 26.17 ? 67  LEU B CD2 1 
ATOM   2443 N  N   . PRO B 1 33  ? 0.792   3.996   6.391   1.00 22.88 ? 68  PRO B N   1 
ATOM   2444 C  CA  . PRO B 1 33  ? 1.304   5.305   5.936   1.00 23.56 ? 68  PRO B CA  1 
ATOM   2445 C  C   . PRO B 1 33  ? 0.255   6.390   6.178   1.00 24.25 ? 68  PRO B C   1 
ATOM   2446 O  O   . PRO B 1 33  ? -0.419  6.898   5.282   1.00 22.53 ? 68  PRO B O   1 
ATOM   2447 C  CB  . PRO B 1 33  ? 1.580   5.047   4.449   1.00 28.33 ? 68  PRO B CB  1 
ATOM   2448 C  CG  . PRO B 1 33  ? 0.518   4.046   4.061   1.00 23.77 ? 68  PRO B CG  1 
ATOM   2449 C  CD  . PRO B 1 33  ? 0.374   3.138   5.267   1.00 23.07 ? 68  PRO B CD  1 
ATOM   2450 N  N   . VAL B 1 34  ? 0.090   6.723   7.457   1.00 22.11 ? 69  VAL B N   1 
ATOM   2451 C  CA  . VAL B 1 34  ? -0.989  7.591   7.907   1.00 21.28 ? 69  VAL B CA  1 
ATOM   2452 C  C   . VAL B 1 34  ? -0.843  8.999   7.335   1.00 22.75 ? 69  VAL B C   1 
ATOM   2453 O  O   . VAL B 1 34  ? -1.837  9.678   7.052   1.00 21.40 ? 69  VAL B O   1 
ATOM   2454 C  CB  . VAL B 1 34  ? -1.002  7.570   9.443   1.00 25.06 ? 69  VAL B CB  1 
ATOM   2455 C  CG1 . VAL B 1 34  ? -1.657  8.786   9.976   1.00 35.28 ? 69  VAL B CG1 1 
ATOM   2456 C  CG2 . VAL B 1 34  ? -1.717  6.262   9.922   1.00 21.94 ? 69  VAL B CG2 1 
ATOM   2457 N  N   . ASP B 1 35  ? 0.389   9.420   7.099   1.00 23.09 ? 70  ASP B N   1 
ATOM   2458 C  CA  . ASP B 1 35  ? 0.653   10.756  6.500   1.00 25.14 ? 70  ASP B CA  1 
ATOM   2459 C  C   . ASP B 1 35  ? 0.080   10.847  5.083   1.00 30.21 ? 70  ASP B C   1 
ATOM   2460 O  O   . ASP B 1 35  ? -0.348  11.940  4.691   1.00 29.75 ? 70  ASP B O   1 
ATOM   2461 C  CB  . ASP B 1 35  ? 2.148   11.034  6.513   1.00 25.48 ? 70  ASP B CB  1 
ATOM   2462 C  CG  . ASP B 1 35  ? 3.033   9.969   5.887   1.00 31.41 ? 70  ASP B CG  1 
ATOM   2463 O  OD1 . ASP B 1 35  ? 2.584   8.810   5.789   1.00 26.87 ? 70  ASP B OD1 1 
ATOM   2464 O  OD2 . ASP B 1 35  ? 4.170   10.312  5.515   1.00 36.46 ? 70  ASP B OD2 1 
ATOM   2465 N  N   . LYS B 1 36  ? 0.083   9.741   4.341   1.00 24.38 ? 71  LYS B N   1 
ATOM   2466 C  CA  . LYS B 1 36  ? -0.487  9.736   2.969   1.00 27.92 ? 71  LYS B CA  1 
ATOM   2467 C  C   . LYS B 1 36  ? -2.018  9.625   3.001   1.00 29.53 ? 71  LYS B C   1 
ATOM   2468 O  O   . LYS B 1 36  ? -2.639  9.971   2.005   1.00 31.32 ? 71  LYS B O   1 
ATOM   2469 C  CB  . LYS B 1 36  ? 0.035   8.535   2.186   1.00 30.57 ? 71  LYS B CB  1 
ATOM   2470 C  CG  . LYS B 1 36  ? 1.547   8.484   2.031   1.00 35.69 ? 71  LYS B CG  1 
ATOM   2471 C  CD  . LYS B 1 36  ? 2.113   9.812   1.550   1.00 39.08 ? 71  LYS B CD  1 
ATOM   2472 C  CE  . LYS B 1 36  ? 3.588   9.765   1.319   1.00 45.57 ? 71  LYS B CE  1 
ATOM   2473 N  NZ  . LYS B 1 36  ? 4.020   10.822  0.401   1.00 40.01 ? 71  LYS B NZ  1 
ATOM   2474 N  N   . ARG B 1 37  ? -2.572  9.102   4.098   1.00 25.18 ? 72  ARG B N   1 
ATOM   2475 C  CA  . ARG B 1 37  ? -4.039  8.884   4.177   1.00 26.02 ? 72  ARG B CA  1 
ATOM   2476 C  C   . ARG B 1 37  ? -4.732  10.166  4.648   1.00 22.80 ? 72  ARG B C   1 
ATOM   2477 O  O   . ARG B 1 37  ? -5.761  10.535  4.041   1.00 23.19 ? 72  ARG B O   1 
ATOM   2478 C  CB  . ARG B 1 37  ? -4.363  7.751   5.155   1.00 32.37 ? 72  ARG B CB  1 
ATOM   2479 C  CG  . ARG B 1 37  ? -3.652  6.441   4.851   1.00 45.36 ? 72  ARG B CG  1 
ATOM   2480 C  CD  . ARG B 1 37  ? -4.645  5.325   4.577   1.00 47.41 ? 72  ARG B CD  1 
ATOM   2481 N  NE  . ARG B 1 37  ? -5.423  5.566   3.357   1.00 58.63 ? 72  ARG B NE  1 
ATOM   2482 C  CZ  . ARG B 1 37  ? -5.057  5.171   2.145   1.00 62.70 ? 72  ARG B CZ  1 
ATOM   2483 N  NH1 . ARG B 1 37  ? -4.270  5.938   1.412   1.00 52.65 ? 72  ARG B NH1 1 
ATOM   2484 N  NH2 . ARG B 1 37  ? -5.484  4.015   1.670   1.00 61.87 ? 72  ARG B NH2 1 
ATOM   2485 N  N   . LEU B 1 38  ? -4.187  10.822  5.676   1.00 23.53 ? 73  LEU B N   1 
ATOM   2486 C  CA  . LEU B 1 38  ? -4.860  11.991  6.222   1.00 20.47 ? 73  LEU B CA  1 
ATOM   2487 C  C   . LEU B 1 38  ? -4.976  13.087  5.175   1.00 21.20 ? 73  LEU B C   1 
ATOM   2488 O  O   . LEU B 1 38  ? -4.081  13.272  4.346   1.00 25.50 ? 73  LEU B O   1 
ATOM   2489 C  CB  . LEU B 1 38  ? -4.121  12.511  7.451   1.00 20.82 ? 73  LEU B CB  1 
ATOM   2490 C  CG  . LEU B 1 38  ? -4.323  11.518  8.613   1.00 24.56 ? 73  LEU B CG  1 
ATOM   2491 C  CD1 . LEU B 1 38  ? -3.301  11.744  9.689   1.00 23.04 ? 73  LEU B CD1 1 
ATOM   2492 C  CD2 . LEU B 1 38  ? -5.755  11.576  9.164   1.00 29.31 ? 73  LEU B CD2 1 
ATOM   2493 N  N   . ASN B 1 39  ? -6.078  13.837  5.235   1.00 21.01 ? 74  ASN B N   1 
ATOM   2494 C  CA  . ASN B 1 39  ? -6.352  14.920  4.282   1.00 21.66 ? 74  ASN B CA  1 
ATOM   2495 C  C   . ASN B 1 39  ? -5.768  16.237  4.813   1.00 24.75 ? 74  ASN B C   1 
ATOM   2496 O  O   . ASN B 1 39  ? -6.474  17.207  5.090   1.00 25.22 ? 74  ASN B O   1 
ATOM   2497 C  CB  . ASN B 1 39  ? -7.861  15.038  4.039   1.00 21.10 ? 74  ASN B CB  1 
ATOM   2498 C  CG  . ASN B 1 39  ? -8.420  13.908  3.123   1.00 33.59 ? 74  ASN B CG  1 
ATOM   2499 O  OD1 . ASN B 1 39  ? -7.679  13.256  2.369   1.00 28.60 ? 74  ASN B OD1 1 
ATOM   2500 N  ND2 . ASN B 1 39  ? -9.729  13.652  3.236   1.00 30.27 ? 74  ASN B ND2 1 
ATOM   2501 N  N   . GLN B 1 40  ? -4.447  16.251  4.986   1.00 23.29 ? 75  GLN B N   1 
ATOM   2502 C  CA  . GLN B 1 40  ? -3.698  17.446  5.370   1.00 25.44 ? 75  GLN B CA  1 
ATOM   2503 C  C   . GLN B 1 40  ? -2.255  17.227  4.951   1.00 25.53 ? 75  GLN B C   1 
ATOM   2504 O  O   . GLN B 1 40  ? -1.888  16.107  4.603   1.00 25.19 ? 75  GLN B O   1 
ATOM   2505 C  CB  . GLN B 1 40  ? -3.821  17.714  6.885   1.00 24.23 ? 75  GLN B CB  1 
ATOM   2506 C  CG  . GLN B 1 40  ? -2.892  16.855  7.727   1.00 24.12 ? 75  GLN B CG  1 
ATOM   2507 C  CD  . GLN B 1 40  ? -2.990  17.151  9.213   1.00 24.12 ? 75  GLN B CD  1 
ATOM   2508 O  OE1 . GLN B 1 40  ? -3.651  18.112  9.640   1.00 24.39 ? 75  GLN B OE1 1 
ATOM   2509 N  NE2 . GLN B 1 40  ? -2.411  16.266  10.015  1.00 23.87 ? 75  GLN B NE2 1 
ATOM   2510 N  N   . PRO B 1 41  ? -1.432  18.277  4.902   1.00 27.00 ? 76  PRO B N   1 
ATOM   2511 C  CA  . PRO B 1 41  ? -0.060  18.102  4.405   1.00 28.27 ? 76  PRO B CA  1 
ATOM   2512 C  C   . PRO B 1 41  ? 0.694   17.049  5.199   1.00 27.92 ? 76  PRO B C   1 
ATOM   2513 O  O   . PRO B 1 41  ? 0.612   16.991  6.427   1.00 27.44 ? 76  PRO B O   1 
ATOM   2514 C  CB  . PRO B 1 41  ? 0.568   19.497  4.585   1.00 29.95 ? 76  PRO B CB  1 
ATOM   2515 C  CG  . PRO B 1 41  ? -0.601  20.422  4.521   1.00 29.66 ? 76  PRO B CG  1 
ATOM   2516 C  CD  . PRO B 1 41  ? -1.713  19.690  5.219   1.00 27.82 ? 76  PRO B CD  1 
ATOM   2517 N  N   . ALA B 1 42  ? 1.450   16.223  4.485   1.00 28.36 ? 77  ALA B N   1 
ATOM   2518 C  CA  . ALA B 1 42  ? 2.210   15.179  5.168   1.00 28.20 ? 77  ALA B CA  1 
ATOM   2519 C  C   . ALA B 1 42  ? 3.133   15.725  6.254   1.00 29.19 ? 77  ALA B C   1 
ATOM   2520 O  O   . ALA B 1 42  ? 3.271   15.049  7.287   1.00 28.61 ? 77  ALA B O   1 
ATOM   2521 C  CB  . ALA B 1 42  ? 2.990   14.347  4.147   1.00 31.20 ? 77  ALA B CB  1 
ATOM   2522 N  N   . PRO B 1 43  ? 3.815   16.875  6.094   1.00 33.35 ? 78  PRO B N   1 
ATOM   2523 C  CA  . PRO B 1 43  ? 4.632   17.397  7.214   1.00 32.92 ? 78  PRO B CA  1 
ATOM   2524 C  C   . PRO B 1 43  ? 3.834   17.773  8.448   1.00 32.33 ? 78  PRO B C   1 
ATOM   2525 O  O   . PRO B 1 43  ? 4.355   17.702  9.574   1.00 31.48 ? 78  PRO B O   1 
ATOM   2526 C  CB  . PRO B 1 43  ? 5.311   18.632  6.609   1.00 33.94 ? 78  PRO B CB  1 
ATOM   2527 C  CG  . PRO B 1 43  ? 5.334   18.378  5.163   1.00 34.20 ? 78  PRO B CG  1 
ATOM   2528 C  CD  . PRO B 1 43  ? 4.047   17.669  4.867   1.00 35.06 ? 78  PRO B CD  1 
ATOM   2529 N  N   . LYS B 1 44  ? 2.571   18.165  8.275   1.00 29.99 ? 79  LYS B N   1 
ATOM   2530 C  CA  . LYS B 1 44  ? 1.736   18.471  9.428   1.00 30.55 ? 79  LYS B CA  1 
ATOM   2531 C  C   . LYS B 1 44  ? 1.420   17.199  10.211  1.00 27.87 ? 79  LYS B C   1 
ATOM   2532 O  O   . LYS B 1 44  ? 1.553   17.144  11.446  1.00 27.99 ? 79  LYS B O   1 
ATOM   2533 C  CB  . LYS B 1 44  ? 0.463   19.180  8.952   1.00 28.66 ? 79  LYS B CB  1 
ATOM   2534 C  CG  . LYS B 1 44  ? -0.151  20.032  10.012  1.00 35.90 ? 79  LYS B CG  1 
ATOM   2535 C  CD  . LYS B 1 44  ? -1.306  20.855  9.483   1.00 35.94 ? 79  LYS B CD  1 
ATOM   2536 C  CE  . LYS B 1 44  ? -1.850  21.712  10.597  1.00 37.93 ? 79  LYS B CE  1 
ATOM   2537 N  NZ  . LYS B 1 44  ? -2.481  22.967  10.091  1.00 47.85 ? 79  LYS B NZ  1 
ATOM   2538 N  N   . THR B 1 45  ? 1.039   16.151  9.499   1.00 26.73 ? 80  THR B N   1 
ATOM   2539 C  CA  . THR B 1 45  ? 0.850   14.863  10.154  1.00 25.62 ? 80  THR B CA  1 
ATOM   2540 C  C   . THR B 1 45  ? 2.151   14.382  10.785  1.00 26.55 ? 80  THR B C   1 
ATOM   2541 O  O   . THR B 1 45  ? 2.173   13.889  11.924  1.00 26.27 ? 80  THR B O   1 
ATOM   2542 C  CB  . THR B 1 45  ? 0.343   13.858  9.128   1.00 24.61 ? 80  THR B CB  1 
ATOM   2543 O  OG1 . THR B 1 45  ? -0.961  14.236  8.669   1.00 23.78 ? 80  THR B OG1 1 
ATOM   2544 C  CG2 . THR B 1 45  ? 0.292   12.412  9.751   1.00 23.72 ? 80  THR B CG2 1 
ATOM   2545 N  N   . GLN B 1 46  ? 3.246   14.513  10.046  1.00 27.80 ? 81  GLN B N   1 
ATOM   2546 C  CA  . GLN B 1 46  ? 4.568   14.125  10.528  1.00 32.55 ? 81  GLN B CA  1 
ATOM   2547 C  C   . GLN B 1 46  ? 4.839   14.737  11.898  1.00 31.32 ? 81  GLN B C   1 
ATOM   2548 O  O   . GLN B 1 46  ? 5.243   14.041  12.849  1.00 31.49 ? 81  GLN B O   1 
ATOM   2549 C  CB  . GLN B 1 46  ? 5.588   14.610  9.493   1.00 40.52 ? 81  GLN B CB  1 
ATOM   2550 C  CG  . GLN B 1 46  ? 7.048   14.724  9.890   1.00 50.72 ? 81  GLN B CG  1 
ATOM   2551 C  CD  . GLN B 1 46  ? 7.931   15.027  8.677   1.00 61.07 ? 81  GLN B CD  1 
ATOM   2552 O  OE1 . GLN B 1 46  ? 9.144   15.208  8.805   1.00 61.41 ? 81  GLN B OE1 1 
ATOM   2553 N  NE2 . GLN B 1 46  ? 7.300   15.167  7.505   1.00 57.52 ? 81  GLN B NE2 1 
ATOM   2554 N  N   . SER B 1 47  ? 4.604   16.054  12.009  1.00 36.19 ? 82  SER B N   1 
ATOM   2555 C  CA  . SER B 1 47  ? 4.853   16.772  13.255  1.00 34.69 ? 82  SER B CA  1 
ATOM   2556 C  C   . SER B 1 47  ? 3.928   16.314  14.384  1.00 34.78 ? 82  SER B C   1 
ATOM   2557 O  O   . SER B 1 47  ? 4.379   16.150  15.523  1.00 33.37 ? 82  SER B O   1 
ATOM   2558 C  CB  . SER B 1 47  ? 4.739   18.286  13.009  1.00 33.36 ? 82  SER B CB  1 
ATOM   2559 O  OG  . SER B 1 47  ? 3.394   18.760  12.960  1.00 32.62 ? 82  SER B OG  1 
ATOM   2560 N  N   . ALA B 1 48  ? 2.630   16.133  14.109  1.00 35.13 ? 83  ALA B N   1 
ATOM   2561 C  CA  . ALA B 1 48  ? 1.733   15.652  15.169  1.00 30.60 ? 83  ALA B CA  1 
ATOM   2562 C  C   . ALA B 1 48  ? 2.164   14.272  15.686  1.00 27.91 ? 83  ALA B C   1 
ATOM   2563 O  O   . ALA B 1 48  ? 2.241   14.029  16.909  1.00 28.34 ? 83  ALA B O   1 
ATOM   2564 C  CB  . ALA B 1 48  ? 0.296   15.617  14.652  1.00 30.04 ? 83  ALA B CB  1 
ATOM   2565 N  N   . LEU B 1 49  ? 2.503   13.375  14.764  1.00 26.68 ? 84  LEU B N   1 
ATOM   2566 C  CA  . LEU B 1 49  ? 3.049   12.079  15.160  1.00 28.98 ? 84  LEU B CA  1 
ATOM   2567 C  C   . LEU B 1 49  ? 4.270   12.267  16.054  1.00 28.30 ? 84  LEU B C   1 
ATOM   2568 O  O   . LEU B 1 49  ? 4.378   11.654  17.120  1.00 30.01 ? 84  LEU B O   1 
ATOM   2569 C  CB  . LEU B 1 49  ? 3.420   11.281  13.912  1.00 28.84 ? 84  LEU B CB  1 
ATOM   2570 C  CG  . LEU B 1 49  ? 2.297   10.680  13.068  1.00 29.49 ? 84  LEU B CG  1 
ATOM   2571 C  CD1 . LEU B 1 49  ? 2.828   9.576   12.165  1.00 32.35 ? 84  LEU B CD1 1 
ATOM   2572 C  CD2 . LEU B 1 49  ? 1.178   10.172  13.957  1.00 32.45 ? 84  LEU B CD2 1 
ATOM   2573 N  N   . ALA B 1 50  ? 5.187   13.130  15.647  1.00 31.13 ? 85  ALA B N   1 
ATOM   2574 C  CA  . ALA B 1 50  ? 6.453   13.282  16.406  1.00 34.94 ? 85  ALA B CA  1 
ATOM   2575 C  C   . ALA B 1 50  ? 6.189   13.881  17.783  1.00 36.75 ? 85  ALA B C   1 
ATOM   2576 O  O   . ALA B 1 50  ? 6.936   13.571  18.715  1.00 37.28 ? 85  ALA B O   1 
ATOM   2577 C  CB  . ALA B 1 50  ? 7.440   14.095  15.601  1.00 35.28 ? 85  ALA B CB  1 
ATOM   2578 N  N   . LYS B 1 51  ? 5.133   14.671  17.919  1.00 35.25 ? 86  LYS B N   1 
ATOM   2579 C  CA  . LYS B 1 51  ? 4.771   15.236  19.243  1.00 43.73 ? 86  LYS B CA  1 
ATOM   2580 C  C   . LYS B 1 51  ? 4.357   14.095  20.184  1.00 33.93 ? 86  LYS B C   1 
ATOM   2581 O  O   . LYS B 1 51  ? 4.483   14.269  21.399  1.00 40.75 ? 86  LYS B O   1 
ATOM   2582 C  CB  . LYS B 1 51  ? 3.659   16.277  19.100  1.00 39.80 ? 86  LYS B CB  1 
ATOM   2583 C  CG  . LYS B 1 51  ? 3.929   17.630  19.725  1.00 46.54 ? 86  LYS B CG  1 
ATOM   2584 C  CD  . LYS B 1 51  ? 2.817   18.632  19.447  1.00 49.92 ? 86  LYS B CD  1 
ATOM   2585 C  CE  . LYS B 1 51  ? 3.288   19.800  18.635  1.00 58.67 ? 86  LYS B CE  1 
ATOM   2586 N  NZ  . LYS B 1 51  ? 2.437   20.982  18.802  1.00 58.55 ? 86  LYS B NZ  1 
ATOM   2587 N  N   . SER B 1 52  ? 3.854   12.994  19.625  1.00 35.61 ? 87  SER B N   1 
ATOM   2588 C  CA  . SER B 1 52  ? 3.418   11.830  20.437  1.00 38.18 ? 87  SER B CA  1 
ATOM   2589 C  C   . SER B 1 52  ? 4.491   10.747  20.307  1.00 29.25 ? 87  SER B C   1 
ATOM   2590 O  O   . SER B 1 52  ? 4.196   9.593   20.642  1.00 35.66 ? 87  SER B O   1 
ATOM   2591 C  CB  . SER B 1 52  ? 2.056   11.372  20.010  1.00 38.54 ? 87  SER B CB  1 
ATOM   2592 O  OG  . SER B 1 52  ? 1.044   12.218  20.533  1.00 45.58 ? 87  SER B OG  1 
ATOM   2593 N  N   . PHE B 1 53  ? 5.654   11.123  19.778  1.00 36.56 ? 88  PHE B N   1 
ATOM   2594 C  CA  . PHE B 1 53  ? 6.804   10.230  19.666  1.00 34.82 ? 88  PHE B CA  1 
ATOM   2595 C  C   . PHE B 1 53  ? 6.528   9.046   18.732  1.00 38.31 ? 88  PHE B C   1 
ATOM   2596 O  O   . PHE B 1 53  ? 6.932   7.910   18.996  1.00 42.42 ? 88  PHE B O   1 
ATOM   2597 C  CB  . PHE B 1 53  ? 7.266   9.771   21.056  1.00 34.88 ? 88  PHE B CB  1 
ATOM   2598 C  CG  . PHE B 1 53  ? 7.561   10.921  22.023  1.00 37.01 ? 88  PHE B CG  1 
ATOM   2599 C  CD1 . PHE B 1 53  ? 6.568   11.461  22.823  1.00 31.94 ? 88  PHE B CD1 1 
ATOM   2600 C  CD2 . PHE B 1 53  ? 8.838   11.451  22.112  1.00 30.45 ? 88  PHE B CD2 1 
ATOM   2601 C  CE1 . PHE B 1 53  ? 6.863   12.484  23.709  1.00 30.31 ? 88  PHE B CE1 1 
ATOM   2602 C  CE2 . PHE B 1 53  ? 9.127   12.490  22.979  1.00 32.44 ? 88  PHE B CE2 1 
ATOM   2603 C  CZ  . PHE B 1 53  ? 8.140   13.012  23.774  1.00 31.00 ? 88  PHE B CZ  1 
ATOM   2604 N  N   . GLN B 1 54  ? 5.886   9.342   17.593  1.00 29.90 ? 89  GLN B N   1 
ATOM   2605 C  CA  . GLN B 1 54  ? 5.612   8.393   16.516  1.00 32.15 ? 89  GLN B CA  1 
ATOM   2606 C  C   . GLN B 1 54  ? 6.165   8.979   15.223  1.00 26.73 ? 89  GLN B C   1 
ATOM   2607 O  O   . GLN B 1 54  ? 6.387   10.187  15.139  1.00 33.55 ? 89  GLN B O   1 
ATOM   2608 C  CB  . GLN B 1 54  ? 4.100   8.115   16.391  1.00 35.41 ? 89  GLN B CB  1 
ATOM   2609 C  CG  . GLN B 1 54  ? 3.385   7.867   17.729  1.00 34.70 ? 89  GLN B CG  1 
ATOM   2610 C  CD  . GLN B 1 54  ? 1.850   7.810   17.633  1.00 40.07 ? 89  GLN B CD  1 
ATOM   2611 O  OE1 . GLN B 1 54  ? 1.256   8.171   16.618  1.00 44.67 ? 89  GLN B OE1 1 
ATOM   2612 N  NE2 . GLN B 1 54  ? 1.214   7.327   18.693  1.00 46.14 ? 89  GLN B NE2 1 
ATOM   2613 N  N   . LYS B 1 55  ? 6.385   8.143   14.202  1.00 28.79 ? 90  LYS B N   1 
ATOM   2614 C  CA  . LYS B 1 55  ? 6.820   8.706   12.919  1.00 39.07 ? 90  LYS B CA  1 
ATOM   2615 C  C   . LYS B 1 55  ? 6.606   7.664   11.821  1.00 44.11 ? 90  LYS B C   1 
ATOM   2616 O  O   . LYS B 1 55  ? 6.145   6.548   12.086  1.00 46.28 ? 90  LYS B O   1 
ATOM   2617 C  CB  . LYS B 1 55  ? 8.293   9.184   12.967  1.00 52.95 ? 90  LYS B CB  1 
ATOM   2618 C  CG  . LYS B 1 55  ? 8.799   9.918   11.693  1.00 60.46 ? 90  LYS B CG  1 
ATOM   2619 C  CD  . LYS B 1 55  ? 10.239  10.460  11.772  1.00 71.32 ? 90  LYS B CD  1 
ATOM   2620 C  CE  . LYS B 1 55  ? 10.606  11.162  10.445  1.00 68.39 ? 90  LYS B CE  1 
ATOM   2621 N  NZ  . LYS B 1 55  ? 11.985  11.741  10.396  1.00 74.09 ? 90  LYS B NZ  1 
ATOM   2622 N  N   . ALA B 1 56  ? 6.883   8.079   10.552  1.00 53.63 ? 91  ALA B N   1 
ATOM   2623 C  CA  . ALA B 1 56  ? 7.079   7.238   9.368   1.00 32.30 ? 91  ALA B CA  1 
ATOM   2624 C  C   . ALA B 1 56  ? 5.788   6.453   9.223   1.00 31.88 ? 91  ALA B C   1 
ATOM   2625 O  O   . ALA B 1 56  ? 4.763   6.930   9.730   1.00 42.30 ? 91  ALA B O   1 
ATOM   2626 C  CB  . ALA B 1 56  ? 8.341   6.377   9.518   1.00 50.69 ? 91  ALA B CB  1 
ATOM   2627 N  N   . PRO B 1 57  ? 5.727   5.317   8.524   1.00 32.18 ? 92  PRO B N   1 
ATOM   2628 C  CA  . PRO B 1 57  ? 4.566   4.446   8.731   1.00 30.35 ? 92  PRO B CA  1 
ATOM   2629 C  C   . PRO B 1 57  ? 4.382   4.173   10.218  1.00 29.55 ? 92  PRO B C   1 
ATOM   2630 O  O   . PRO B 1 57  ? 5.348   3.963   10.957  1.00 29.09 ? 92  PRO B O   1 
ATOM   2631 C  CB  . PRO B 1 57  ? 4.931   3.182   7.957   1.00 28.79 ? 92  PRO B CB  1 
ATOM   2632 C  CG  . PRO B 1 57  ? 5.693   3.707   6.784   1.00 32.02 ? 92  PRO B CG  1 
ATOM   2633 C  CD  . PRO B 1 57  ? 6.428   4.950   7.271   1.00 37.82 ? 92  PRO B CD  1 
ATOM   2634 N  N   . LEU B 1 58  ? 3.138   4.206   10.660  1.00 22.66 ? 93  LEU B N   1 
ATOM   2635 C  CA  . LEU B 1 58  ? 2.813   4.111   12.072  1.00 21.88 ? 93  LEU B CA  1 
ATOM   2636 C  C   . LEU B 1 58  ? 2.272   2.725   12.409  1.00 19.91 ? 93  LEU B C   1 
ATOM   2637 O  O   . LEU B 1 58  ? 1.259   2.286   11.835  1.00 19.44 ? 93  LEU B O   1 
ATOM   2638 C  CB  . LEU B 1 58  ? 1.775   5.167   12.438  1.00 24.15 ? 93  LEU B CB  1 
ATOM   2639 C  CG  . LEU B 1 58  ? 1.196   5.126   13.856  1.00 28.51 ? 93  LEU B CG  1 
ATOM   2640 C  CD1 . LEU B 1 58  ? 2.328   5.087   14.897  1.00 27.66 ? 93  LEU B CD1 1 
ATOM   2641 C  CD2 . LEU B 1 58  ? 0.227   6.305   14.061  1.00 36.26 ? 93  LEU B CD2 1 
ATOM   2642 N  N   . GLU B 1 59  ? 2.886   2.070   13.397  1.00 19.62 ? 94  GLU B N   1 
ATOM   2643 C  CA  . GLU B 1 59  ? 2.376   0.770   13.842  1.00 18.77 ? 94  GLU B CA  1 
ATOM   2644 C  C   . GLU B 1 59  ? 1.027   0.957   14.528  1.00 21.21 ? 94  GLU B C   1 
ATOM   2645 O  O   . GLU B 1 59  ? 0.936   1.583   15.591  1.00 22.74 ? 94  GLU B O   1 
ATOM   2646 C  CB  . GLU B 1 59  ? 3.370   0.094   14.783  1.00 20.60 ? 94  GLU B CB  1 
ATOM   2647 C  CG  . GLU B 1 59  ? 2.815   -1.115  15.510  1.00 19.37 ? 94  GLU B CG  1 
ATOM   2648 C  CD  . GLU B 1 59  ? 3.894   -1.959  16.203  1.00 30.66 ? 94  GLU B CD  1 
ATOM   2649 O  OE1 . GLU B 1 59  ? 4.995   -1.440  16.493  1.00 26.08 ? 94  GLU B OE1 1 
ATOM   2650 O  OE2 . GLU B 1 59  ? 3.634   -3.147  16.480  1.00 19.83 ? 94  GLU B OE2 1 
ATOM   2651 N  N   . THR B 1 60  ? -0.023  0.426   13.930  1.00 17.17 ? 95  THR B N   1 
ATOM   2652 C  CA  . THR B 1 60  ? -1.389  0.703   14.347  1.00 16.28 ? 95  THR B CA  1 
ATOM   2653 C  C   . THR B 1 60  ? -2.038  -0.583  14.845  1.00 15.70 ? 95  THR B C   1 
ATOM   2654 O  O   . THR B 1 60  ? -1.982  -1.597  14.156  1.00 16.05 ? 95  THR B O   1 
ATOM   2655 C  CB  . THR B 1 60  ? -2.179  1.284   13.176  1.00 16.55 ? 95  THR B CB  1 
ATOM   2656 O  OG1 . THR B 1 60  ? -1.459  2.400   12.640  1.00 17.37 ? 95  THR B OG1 1 
ATOM   2657 C  CG2 . THR B 1 60  ? -3.574  1.732   13.631  1.00 15.81 ? 95  THR B CG2 1 
ATOM   2658 N  N   . SER B 1 61  ? -2.586  -0.549  16.061  1.00 14.99 ? 96  SER B N   1 
ATOM   2659 C  CA  . SER B 1 61  ? -3.348  -1.672  16.580  1.00 14.59 ? 96  SER B CA  1 
ATOM   2660 C  C   . SER B 1 61  ? -4.621  -1.898  15.753  1.00 14.53 ? 96  SER B C   1 
ATOM   2661 O  O   . SER B 1 61  ? -5.202  -0.975  15.170  1.00 14.53 ? 96  SER B O   1 
ATOM   2662 C  CB  . SER B 1 61  ? -3.735  -1.432  18.054  1.00 14.58 ? 96  SER B CB  1 
ATOM   2663 O  OG  . SER B 1 61  ? -2.628  -1.163  18.902  1.00 14.09 ? 96  SER B OG  1 
ATOM   2664 N  N   . VAL B 1 62  ? -5.067  -3.153  15.712  1.00 19.30 ? 97  VAL B N   1 
ATOM   2665 C  CA  . VAL B 1 62  ? -6.386  -3.528  15.189  1.00 14.63 ? 97  VAL B CA  1 
ATOM   2666 C  C   . VAL B 1 62  ? -7.050  -4.362  16.274  1.00 16.38 ? 97  VAL B C   1 
ATOM   2667 O  O   . VAL B 1 62  ? -6.468  -5.362  16.705  1.00 14.67 ? 97  VAL B O   1 
ATOM   2668 C  CB  . VAL B 1 62  ? -6.273  -4.331  13.876  1.00 15.30 ? 97  VAL B CB  1 
ATOM   2669 C  CG1 . VAL B 1 62  ? -7.657  -4.787  13.355  1.00 16.22 ? 97  VAL B CG1 1 
ATOM   2670 C  CG2 . VAL B 1 62  ? -5.508  -3.545  12.818  1.00 15.71 ? 97  VAL B CG2 1 
ATOM   2671 N  N   . THR B 1 63  ? -8.244  -3.950  16.736  1.00 14.13 ? 98  THR B N   1 
ATOM   2672 C  CA  . THR B 1 63  ? -8.856  -4.534  17.929  1.00 14.04 ? 98  THR B CA  1 
ATOM   2673 C  C   . THR B 1 63  ? -10.341 -4.803  17.707  1.00 15.87 ? 98  THR B C   1 
ATOM   2674 O  O   . THR B 1 63  ? -11.025 -4.049  17.006  1.00 15.95 ? 98  THR B O   1 
ATOM   2675 C  CB  . THR B 1 63  ? -8.661  -3.581  19.132  1.00 13.55 ? 98  THR B CB  1 
ATOM   2676 O  OG1 . THR B 1 63  ? -7.261  -3.279  19.281  1.00 17.91 ? 98  THR B OG1 1 
ATOM   2677 C  CG2 . THR B 1 63  ? -9.177  -4.170  20.471  1.00 13.60 ? 98  THR B CG2 1 
ATOM   2678 N  N   . GLY B 1 64  ? -10.824 -5.916  18.284  1.00 15.18 ? 99  GLY B N   1 
ATOM   2679 C  CA  . GLY B 1 64  ? -12.247 -6.182  18.405  1.00 15.10 ? 99  GLY B CA  1 
ATOM   2680 C  C   . GLY B 1 64  ? -12.626 -6.220  19.887  1.00 17.62 ? 99  GLY B C   1 
ATOM   2681 O  O   . GLY B 1 64  ? -11.761 -6.310  20.759  1.00 17.29 ? 99  GLY B O   1 
ATOM   2682 N  N   . TYR B 1 65  ? -13.922 -6.156  20.187  1.00 15.50 ? 100 TYR B N   1 
ATOM   2683 C  CA  . TYR B 1 65  ? -14.294 -6.101  21.601  1.00 16.55 ? 100 TYR B CA  1 
ATOM   2684 C  C   . TYR B 1 65  ? -15.348 -7.132  21.942  1.00 24.85 ? 100 TYR B C   1 
ATOM   2685 O  O   . TYR B 1 65  ? -16.454 -7.090  21.399  1.00 18.13 ? 100 TYR B O   1 
ATOM   2686 C  CB  . TYR B 1 65  ? -14.756 -4.707  21.989  1.00 15.21 ? 100 TYR B CB  1 
ATOM   2687 C  CG  . TYR B 1 65  ? -13.613 -3.701  21.830  1.00 14.37 ? 100 TYR B CG  1 
ATOM   2688 C  CD1 . TYR B 1 65  ? -13.383 -3.089  20.618  1.00 16.54 ? 100 TYR B CD1 1 
ATOM   2689 C  CD2 . TYR B 1 65  ? -12.798 -3.381  22.892  1.00 16.67 ? 100 TYR B CD2 1 
ATOM   2690 C  CE1 . TYR B 1 65  ? -12.365 -2.171  20.444  1.00 14.82 ? 100 TYR B CE1 1 
ATOM   2691 C  CE2 . TYR B 1 65  ? -11.743 -2.429  22.745  1.00 13.56 ? 100 TYR B CE2 1 
ATOM   2692 C  CZ  . TYR B 1 65  ? -11.543 -1.837  21.508  1.00 14.98 ? 100 TYR B CZ  1 
ATOM   2693 O  OH  . TYR B 1 65  ? -10.531 -0.875  21.300  1.00 14.64 ? 100 TYR B OH  1 
ATOM   2694 N  N   . LEU B 1 66  ? -15.020 -8.016  22.884  1.00 17.12 ? 101 LEU B N   1 
ATOM   2695 C  CA  . LEU B 1 66  ? -15.931 -9.057  23.347  1.00 18.34 ? 101 LEU B CA  1 
ATOM   2696 C  C   . LEU B 1 66  ? -16.689 -8.575  24.574  1.00 23.14 ? 101 LEU B C   1 
ATOM   2697 O  O   . LEU B 1 66  ? -16.077 -8.115  25.540  1.00 22.96 ? 101 LEU B O   1 
ATOM   2698 C  CB  . LEU B 1 66  ? -15.112 -10.300 23.680  1.00 19.35 ? 101 LEU B CB  1 
ATOM   2699 C  CG  . LEU B 1 66  ? -15.889 -11.557 23.939  1.00 21.47 ? 101 LEU B CG  1 
ATOM   2700 C  CD1 . LEU B 1 66  ? -16.508 -12.047 22.635  1.00 20.91 ? 101 LEU B CD1 1 
ATOM   2701 C  CD2 . LEU B 1 66  ? -14.904 -12.591 24.507  1.00 31.82 ? 101 LEU B CD2 1 
ATOM   2702 N  N   . VAL B 1 67  ? -18.015 -8.675  24.533  1.00 24.12 ? 102 VAL B N   1 
ATOM   2703 C  CA  . VAL B 1 67  ? -18.904 -8.269  25.615  1.00 20.44 ? 102 VAL B CA  1 
ATOM   2704 C  C   . VAL B 1 67  ? -19.639 -9.521  26.098  1.00 25.68 ? 102 VAL B C   1 
ATOM   2705 O  O   . VAL B 1 67  ? -20.364 -10.158 25.331  1.00 23.24 ? 102 VAL B O   1 
ATOM   2706 C  CB  . VAL B 1 67  ? -19.899 -7.180  25.159  1.00 20.12 ? 102 VAL B CB  1 
ATOM   2707 C  CG1 . VAL B 1 67  ? -20.757 -6.677  26.319  1.00 25.05 ? 102 VAL B CG1 1 
ATOM   2708 C  CG2 . VAL B 1 67  ? -19.152 -5.976  24.451  1.00 19.40 ? 102 VAL B CG2 1 
ATOM   2709 N  N   . ASN B 1 68  ? -19.444 -9.870  27.360  1.00 25.73 ? 103 ASN B N   1 
ATOM   2710 C  CA  . ASN B 1 68  ? -20.195 -10.929 28.007  1.00 29.94 ? 103 ASN B CA  1 
ATOM   2711 C  C   . ASN B 1 68  ? -21.180 -10.245 28.937  1.00 31.35 ? 103 ASN B C   1 
ATOM   2712 O  O   . ASN B 1 68  ? -20.776 -9.709  29.983  1.00 29.86 ? 103 ASN B O   1 
ATOM   2713 C  CB  . ASN B 1 68  ? -19.262 -11.875 28.764  1.00 31.09 ? 103 ASN B CB  1 
ATOM   2714 C  CG  . ASN B 1 68  ? -19.961 -13.130 29.192  1.00 35.45 ? 103 ASN B CG  1 
ATOM   2715 O  OD1 . ASN B 1 68  ? -21.172 -13.131 29.363  1.00 29.87 ? 103 ASN B OD1 1 
ATOM   2716 N  ND2 . ASN B 1 68  ? -19.207 -14.210 29.367  1.00 46.60 ? 103 ASN B ND2 1 
ATOM   2717 N  N   . THR B 1 69  ? -22.468 -10.249 28.542  1.00 32.08 ? 104 THR B N   1 
ATOM   2718 C  CA  . THR B 1 69  ? -23.534 -9.592  29.291  1.00 33.82 ? 104 THR B CA  1 
ATOM   2719 C  C   . THR B 1 69  ? -24.075 -10.462 30.409  1.00 34.29 ? 104 THR B C   1 
ATOM   2720 O  O   . THR B 1 69  ? -24.969 -10.019 31.137  1.00 35.58 ? 104 THR B O   1 
ATOM   2721 C  CB  . THR B 1 69  ? -24.689 -9.197  28.376  1.00 29.83 ? 104 THR B CB  1 
ATOM   2722 O  OG1 . THR B 1 69  ? -25.500 -10.349 28.074  1.00 30.93 ? 104 THR B OG1 1 
ATOM   2723 C  CG2 . THR B 1 69  ? -24.128 -8.625  27.061  1.00 28.62 ? 104 THR B CG2 1 
ATOM   2724 N  N   . GLY B 1 70  ? -23.529 -11.668 30.574  1.00 38.16 ? 105 GLY B N   1 
ATOM   2725 C  CA  . GLY B 1 70  ? -24.006 -12.638 31.536  1.00 36.51 ? 105 GLY B CA  1 
ATOM   2726 C  C   . GLY B 1 70  ? -25.035 -13.594 30.982  1.00 36.95 ? 105 GLY B C   1 
ATOM   2727 O  O   . GLY B 1 70  ? -25.261 -14.656 31.570  1.00 45.52 ? 105 GLY B O   1 
ATOM   2728 N  N   . SER B 1 71  ? -25.653 -13.241 29.865  1.00 35.45 ? 106 SER B N   1 
ATOM   2729 C  CA  . SER B 1 71  ? -26.600 -14.089 29.164  1.00 36.81 ? 106 SER B CA  1 
ATOM   2730 C  C   . SER B 1 71  ? -26.315 -14.203 27.673  1.00 37.33 ? 106 SER B C   1 
ATOM   2731 O  O   . SER B 1 71  ? -26.852 -15.112 27.037  1.00 34.37 ? 106 SER B O   1 
ATOM   2732 C  CB  . SER B 1 71  ? -28.026 -13.563 29.344  1.00 41.17 ? 106 SER B CB  1 
ATOM   2733 O  OG  . SER B 1 71  ? -28.166 -12.321 28.693  1.00 45.19 ? 106 SER B OG  1 
ATOM   2734 N  N   . LYS B 1 72  ? -25.501 -13.315 27.094  1.00 37.47 ? 107 LYS B N   1 
ATOM   2735 C  CA  . LYS B 1 72  ? -25.072 -13.414 25.706  1.00 35.55 ? 107 LYS B CA  1 
ATOM   2736 C  C   . LYS B 1 72  ? -23.580 -13.107 25.609  1.00 31.21 ? 107 LYS B C   1 
ATOM   2737 O  O   . LYS B 1 72  ? -23.022 -12.373 26.430  1.00 28.47 ? 107 LYS B O   1 
ATOM   2738 C  CB  . LYS B 1 72  ? -25.887 -12.472 24.790  1.00 30.96 ? 107 LYS B CB  1 
ATOM   2739 C  CG  . LYS B 1 72  ? -27.363 -12.860 24.651  1.00 36.58 ? 107 LYS B CG  1 
ATOM   2740 C  CD  . LYS B 1 72  ? -27.499 -14.181 23.891  1.00 27.81 ? 107 LYS B CD  1 
ATOM   2741 C  CE  . LYS B 1 72  ? -28.967 -14.505 23.541  1.00 35.31 ? 107 LYS B CE  1 
ATOM   2742 N  NZ  . LYS B 1 72  ? -29.105 -15.713 22.668  1.00 38.54 ? 107 LYS B NZ  1 
ATOM   2743 N  N   . LEU B 1 73  ? -22.927 -13.722 24.631  1.00 29.08 ? 108 LEU B N   1 
ATOM   2744 C  CA  . LEU B 1 73  ? -21.527 -13.438 24.330  1.00 22.31 ? 108 LEU B CA  1 
ATOM   2745 C  C   . LEU B 1 73  ? -21.468 -12.817 22.945  1.00 26.77 ? 108 LEU B C   1 
ATOM   2746 O  O   . LEU B 1 73  ? -21.681 -13.500 21.934  1.00 24.88 ? 108 LEU B O   1 
ATOM   2747 C  CB  . LEU B 1 73  ? -20.665 -14.694 24.413  1.00 27.74 ? 108 LEU B CB  1 
ATOM   2748 C  CG  . LEU B 1 73  ? -19.160 -14.376 24.361  1.00 24.57 ? 108 LEU B CG  1 
ATOM   2749 C  CD1 . LEU B 1 73  ? -18.735 -13.600 25.580  1.00 23.45 ? 108 LEU B CD1 1 
ATOM   2750 C  CD2 . LEU B 1 73  ? -18.362 -15.671 24.255  1.00 29.42 ? 108 LEU B CD2 1 
ATOM   2751 N  N   . VAL B 1 74  ? -21.129 -11.536 22.901  1.00 27.60 ? 109 VAL B N   1 
ATOM   2752 C  CA  . VAL B 1 74  ? -21.170 -10.740 21.686  1.00 23.66 ? 109 VAL B CA  1 
ATOM   2753 C  C   . VAL B 1 74  ? -19.761 -10.259 21.368  1.00 17.58 ? 109 VAL B C   1 
ATOM   2754 O  O   . VAL B 1 74  ? -19.027 -9.838  22.263  1.00 17.98 ? 109 VAL B O   1 
ATOM   2755 C  CB  . VAL B 1 74  ? -22.138 -9.550  21.849  1.00 22.92 ? 109 VAL B CB  1 
ATOM   2756 C  CG1 . VAL B 1 74  ? -22.196 -8.729  20.562  1.00 24.07 ? 109 VAL B CG1 1 
ATOM   2757 C  CG2 . VAL B 1 74  ? -23.521 -10.037 22.188  1.00 20.03 ? 109 VAL B CG2 1 
ATOM   2758 N  N   . LEU B 1 75  ? -19.385 -10.320 20.096  1.00 18.80 ? 110 LEU B N   1 
ATOM   2759 C  CA  . LEU B 1 75  ? -18.110 -9.813  19.623  1.00 19.54 ? 110 LEU B CA  1 
ATOM   2760 C  C   . LEU B 1 75  ? -18.368 -8.653  18.676  1.00 17.95 ? 110 LEU B C   1 
ATOM   2761 O  O   . LEU B 1 75  ? -19.111 -8.804  17.711  1.00 18.33 ? 110 LEU B O   1 
ATOM   2762 C  CB  . LEU B 1 75  ? -17.363 -10.909 18.876  1.00 24.25 ? 110 LEU B CB  1 
ATOM   2763 C  CG  . LEU B 1 75  ? -16.053 -10.537 18.214  1.00 18.83 ? 110 LEU B CG  1 
ATOM   2764 C  CD1 . LEU B 1 75  ? -15.050 -10.076 19.276  1.00 18.68 ? 110 LEU B CD1 1 
ATOM   2765 C  CD2 . LEU B 1 75  ? -15.539 -11.755 17.437  1.00 18.27 ? 110 LEU B CD2 1 
ATOM   2766 N  N   . VAL B 1 76  ? -17.737 -7.518  18.924  1.00 20.95 ? 111 VAL B N   1 
ATOM   2767 C  CA  . VAL B 1 76  ? -17.840 -6.345  18.064  1.00 21.43 ? 111 VAL B CA  1 
ATOM   2768 C  C   . VAL B 1 76  ? -16.534 -6.279  17.277  1.00 15.48 ? 111 VAL B C   1 
ATOM   2769 O  O   . VAL B 1 76  ? -15.465 -6.090  17.858  1.00 14.47 ? 111 VAL B O   1 
ATOM   2770 C  CB  . VAL B 1 76  ? -18.080 -5.064  18.886  1.00 20.86 ? 111 VAL B CB  1 
ATOM   2771 C  CG1 . VAL B 1 76  ? -18.158 -3.869  17.994  1.00 18.76 ? 111 VAL B CG1 1 
ATOM   2772 C  CG2 . VAL B 1 76  ? -19.371 -5.189  19.716  1.00 18.07 ? 111 VAL B CG2 1 
ATOM   2773 N  N   . ASP B 1 77  ? -16.629 -6.469  15.955  1.00 15.70 ? 112 ASP B N   1 
ATOM   2774 C  CA  . ASP B 1 77  ? -15.534 -6.546  15.002  1.00 14.62 ? 112 ASP B CA  1 
ATOM   2775 C  C   . ASP B 1 77  ? -14.613 -7.746  15.232  1.00 17.34 ? 112 ASP B C   1 
ATOM   2776 O  O   . ASP B 1 77  ? -14.564 -8.331  16.326  1.00 14.24 ? 112 ASP B O   1 
ATOM   2777 C  CB  . ASP B 1 77  ? -14.741 -5.225  14.971  1.00 16.42 ? 112 ASP B CB  1 
ATOM   2778 C  CG  . ASP B 1 77  ? -15.599 -4.043  14.470  1.00 16.13 ? 112 ASP B CG  1 
ATOM   2779 O  OD1 . ASP B 1 77  ? -16.701 -4.265  13.911  1.00 15.07 ? 112 ASP B OD1 1 
ATOM   2780 O  OD2 . ASP B 1 77  ? -15.148 -2.871  14.591  1.00 15.74 ? 112 ASP B OD2 1 
ATOM   2781 N  N   . THR B 1 78  ? -13.932 -8.164  14.166  1.00 14.17 ? 113 THR B N   1 
ATOM   2782 C  CA  . THR B 1 78  ? -13.341 -9.502  14.127  1.00 15.80 ? 113 THR B CA  1 
ATOM   2783 C  C   . THR B 1 78  ? -11.897 -9.476  13.628  1.00 15.27 ? 113 THR B C   1 
ATOM   2784 O  O   . THR B 1 78  ? -11.323 -10.539 13.399  1.00 18.67 ? 113 THR B O   1 
ATOM   2785 C  CB  . THR B 1 78  ? -14.159 -10.466 13.247  1.00 16.89 ? 113 THR B CB  1 
ATOM   2786 O  OG1 . THR B 1 78  ? -14.018 -10.145 11.848  1.00 19.61 ? 113 THR B OG1 1 
ATOM   2787 C  CG2 . THR B 1 78  ? -15.678 -10.408 13.618  1.00 16.66 ? 113 THR B CG2 1 
ATOM   2788 N  N   . GLY B 1 79  ? -11.306 -8.293  13.433  1.00 17.24 ? 114 GLY B N   1 
ATOM   2789 C  CA  . GLY B 1 79  ? -9.957  -8.195  12.896  1.00 14.89 ? 114 GLY B CA  1 
ATOM   2790 C  C   . GLY B 1 79  ? -9.970  -8.595  11.420  1.00 22.22 ? 114 GLY B C   1 
ATOM   2791 O  O   . GLY B 1 79  ? -11.016 -8.703  10.793  1.00 19.10 ? 114 GLY B O   1 
ATOM   2792 N  N   . ALA B 1 80  ? -8.773  -8.861  10.884  1.00 17.57 ? 115 ALA B N   1 
ATOM   2793 C  CA  . ALA B 1 80  ? -8.585  -9.018  9.437   1.00 20.46 ? 115 ALA B CA  1 
ATOM   2794 C  C   . ALA B 1 80  ? -8.405  -10.457 8.962   1.00 20.90 ? 115 ALA B C   1 
ATOM   2795 O  O   . ALA B 1 80  ? -8.373  -10.686 7.739   1.00 20.67 ? 115 ALA B O   1 
ATOM   2796 C  CB  . ALA B 1 80  ? -7.353  -8.228  8.978   1.00 20.89 ? 115 ALA B CB  1 
ATOM   2797 N  N   . ALA B 1 81  ? -8.252  -11.417 9.872   1.00 18.95 ? 116 ALA B N   1 
ATOM   2798 C  CA  . ALA B 1 81  ? -7.802  -12.757 9.486   1.00 30.37 ? 116 ALA B CA  1 
ATOM   2799 C  C   . ALA B 1 81  ? -6.568  -12.596 8.603   1.00 27.57 ? 116 ALA B C   1 
ATOM   2800 O  O   . ALA B 1 81  ? -5.623  -11.898 8.989   1.00 30.00 ? 116 ALA B O   1 
ATOM   2801 C  CB  . ALA B 1 81  ? -8.918  -13.554 8.784   1.00 24.31 ? 116 ALA B CB  1 
ATOM   2802 N  N   . GLY B 1 82  ? -6.577  -13.169 7.403   1.00 29.23 ? 117 GLY B N   1 
ATOM   2803 C  CA  . GLY B 1 82  ? -5.449  -13.059 6.496   1.00 26.86 ? 117 GLY B CA  1 
ATOM   2804 C  C   . GLY B 1 82  ? -5.622  -12.046 5.384   1.00 32.10 ? 117 GLY B C   1 
ATOM   2805 O  O   . GLY B 1 82  ? -4.821  -12.033 4.443   1.00 28.97 ? 117 GLY B O   1 
ATOM   2806 N  N   . LEU B 1 83  ? -6.639  -11.191 5.465   1.00 24.12 ? 118 LEU B N   1 
ATOM   2807 C  CA  . LEU B 1 83  ? -6.967  -10.292 4.366   1.00 26.35 ? 118 LEU B CA  1 
ATOM   2808 C  C   . LEU B 1 83  ? -5.998  -9.128  4.224   1.00 33.60 ? 118 LEU B C   1 
ATOM   2809 O  O   . LEU B 1 83  ? -5.959  -8.499  3.163   1.00 34.27 ? 118 LEU B O   1 
ATOM   2810 C  CB  . LEU B 1 83  ? -8.356  -9.713  4.564   1.00 25.73 ? 118 LEU B CB  1 
ATOM   2811 C  CG  . LEU B 1 83  ? -9.607  -10.573 4.483   1.00 27.81 ? 118 LEU B CG  1 
ATOM   2812 C  CD1 . LEU B 1 83  ? -10.788 -9.625  4.666   1.00 23.59 ? 118 LEU B CD1 1 
ATOM   2813 C  CD2 . LEU B 1 83  ? -9.659  -11.212 3.132   1.00 28.71 ? 118 LEU B CD2 1 
ATOM   2814 N  N   . PHE B 1 84  ? -5.237  -8.802  5.259   1.00 33.52 ? 119 PHE B N   1 
ATOM   2815 C  CA  . PHE B 1 84  ? -4.594  -7.504  5.267   1.00 31.81 ? 119 PHE B CA  1 
ATOM   2816 C  C   . PHE B 1 84  ? -3.151  -7.676  5.723   1.00 34.03 ? 119 PHE B C   1 
ATOM   2817 O  O   . PHE B 1 84  ? -2.626  -6.897  6.524   1.00 31.43 ? 119 PHE B O   1 
ATOM   2818 C  CB  . PHE B 1 84  ? -5.374  -6.553  6.175   1.00 29.95 ? 119 PHE B CB  1 
ATOM   2819 C  CG  . PHE B 1 84  ? -5.198  -5.108  5.853   1.00 39.65 ? 119 PHE B CG  1 
ATOM   2820 C  CD1 . PHE B 1 84  ? -3.951  -4.487  5.837   1.00 43.44 ? 119 PHE B CD1 1 
ATOM   2821 C  CD2 . PHE B 1 84  ? -6.320  -4.364  5.530   1.00 42.00 ? 119 PHE B CD2 1 
ATOM   2822 C  CE1 . PHE B 1 84  ? -3.829  -3.142  5.518   1.00 51.90 ? 119 PHE B CE1 1 
ATOM   2823 C  CE2 . PHE B 1 84  ? -6.218  -3.022  5.214   1.00 52.35 ? 119 PHE B CE2 1 
ATOM   2824 C  CZ  . PHE B 1 84  ? -4.970  -2.405  5.207   1.00 61.09 ? 119 PHE B CZ  1 
ATOM   2825 N  N   . GLY B 1 85  ? -2.517  -8.760  5.278   1.00 30.75 ? 120 GLY B N   1 
ATOM   2826 C  CA  . GLY B 1 85  ? -1.120  -9.015  5.547   1.00 35.42 ? 120 GLY B CA  1 
ATOM   2827 C  C   . GLY B 1 85  ? -0.874  -10.009 6.663   1.00 28.64 ? 120 GLY B C   1 
ATOM   2828 O  O   . GLY B 1 85  ? -1.796  -10.412 7.384   1.00 32.52 ? 120 GLY B O   1 
ATOM   2829 N  N   . PRO B 1 86  ? 0.384   -10.439 6.829   1.00 31.50 ? 121 PRO B N   1 
ATOM   2830 C  CA  . PRO B 1 86  ? 0.669   -11.500 7.810   1.00 23.62 ? 121 PRO B CA  1 
ATOM   2831 C  C   . PRO B 1 86  ? 0.783   -11.022 9.253   1.00 30.41 ? 121 PRO B C   1 
ATOM   2832 O  O   . PRO B 1 86  ? 0.731   -11.873 10.157  1.00 24.78 ? 121 PRO B O   1 
ATOM   2833 C  CB  . PRO B 1 86  ? 1.992   -12.098 7.298   1.00 36.43 ? 121 PRO B CB  1 
ATOM   2834 C  CG  . PRO B 1 86  ? 2.681   -10.969 6.680   1.00 29.53 ? 121 PRO B CG  1 
ATOM   2835 C  CD  . PRO B 1 86  ? 1.570   -10.131 6.013   1.00 35.00 ? 121 PRO B CD  1 
ATOM   2836 N  N   . THR B 1 87  ? 0.886   -9.707  9.506   1.00 22.42 ? 122 THR B N   1 
ATOM   2837 C  CA  . THR B 1 87  ? 0.991   -9.210  10.878  1.00 23.14 ? 122 THR B CA  1 
ATOM   2838 C  C   . THR B 1 87  ? -0.350  -9.178  11.607  1.00 23.91 ? 122 THR B C   1 
ATOM   2839 O  O   . THR B 1 87  ? -0.371  -8.887  12.809  1.00 22.36 ? 122 THR B O   1 
ATOM   2840 C  CB  . THR B 1 87  ? 1.579   -7.781  10.946  1.00 30.72 ? 122 THR B CB  1 
ATOM   2841 O  OG1 . THR B 1 87  ? 0.703   -6.814  10.323  1.00 23.00 ? 122 THR B OG1 1 
ATOM   2842 C  CG2 . THR B 1 87  ? 2.943   -7.743  10.264  1.00 31.61 ? 122 THR B CG2 1 
ATOM   2843 N  N   . LEU B 1 88  ? -1.467  -9.431  10.928  1.00 19.78 ? 123 LEU B N   1 
ATOM   2844 C  CA  . LEU B 1 88  ? -2.776  -9.360  11.567  1.00 18.06 ? 123 LEU B CA  1 
ATOM   2845 C  C   . LEU B 1 88  ? -3.385  -10.766 11.598  1.00 23.33 ? 123 LEU B C   1 
ATOM   2846 O  O   . LEU B 1 88  ? -2.711  -11.762 11.300  1.00 20.33 ? 123 LEU B O   1 
ATOM   2847 C  CB  . LEU B 1 88  ? -3.664  -8.343  10.851  1.00 18.56 ? 123 LEU B CB  1 
ATOM   2848 C  CG  . LEU B 1 88  ? -3.227  -6.873  10.905  1.00 25.87 ? 123 LEU B CG  1 
ATOM   2849 C  CD1 . LEU B 1 88  ? -4.258  -5.993  10.154  1.00 20.35 ? 123 LEU B CD1 1 
ATOM   2850 C  CD2 . LEU B 1 88  ? -3.073  -6.388  12.353  1.00 20.35 ? 123 LEU B CD2 1 
ATOM   2851 N  N   . GLY B 1 89  ? -4.651  -10.859 11.990  1.00 19.47 ? 124 GLY B N   1 
ATOM   2852 C  CA  . GLY B 1 89  ? -5.280  -12.169 12.110  1.00 17.24 ? 124 GLY B CA  1 
ATOM   2853 C  C   . GLY B 1 89  ? -5.088  -12.852 13.445  1.00 20.37 ? 124 GLY B C   1 
ATOM   2854 O  O   . GLY B 1 89  ? -5.321  -14.066 13.549  1.00 27.49 ? 124 GLY B O   1 
ATOM   2855 N  N   . ARG B 1 90  ? -4.685  -12.128 14.472  1.00 15.53 ? 125 ARG B N   1 
ATOM   2856 C  CA  . ARG B 1 90  ? -4.444  -12.742 15.770  1.00 21.42 ? 125 ARG B CA  1 
ATOM   2857 C  C   . ARG B 1 90  ? -5.681  -12.847 16.653  1.00 19.05 ? 125 ARG B C   1 
ATOM   2858 O  O   . ARG B 1 90  ? -5.630  -13.558 17.660  1.00 23.57 ? 125 ARG B O   1 
ATOM   2859 C  CB  . ARG B 1 90  ? -3.351  -11.973 16.502  1.00 20.49 ? 125 ARG B CB  1 
ATOM   2860 C  CG  . ARG B 1 90  ? -2.045  -12.021 15.716  1.00 25.67 ? 125 ARG B CG  1 
ATOM   2861 C  CD  . ARG B 1 90  ? -0.920  -11.227 16.335  1.00 36.22 ? 125 ARG B CD  1 
ATOM   2862 N  NE  . ARG B 1 90  ? 0.260   -11.343 15.481  1.00 50.74 ? 125 ARG B NE  1 
ATOM   2863 C  CZ  . ARG B 1 90  ? 1.474   -11.678 15.901  1.00 58.22 ? 125 ARG B CZ  1 
ATOM   2864 N  NH1 . ARG B 1 90  ? 1.711   -11.987 17.169  1.00 47.56 ? 125 ARG B NH1 1 
ATOM   2865 N  NH2 . ARG B 1 90  ? 2.474   -11.724 15.021  1.00 53.85 ? 125 ARG B NH2 1 
ATOM   2866 N  N   . LEU B 1 91  ? -6.796  -12.210 16.282  1.00 18.29 ? 126 LEU B N   1 
ATOM   2867 C  CA  . LEU B 1 91  ? -7.952  -12.159 17.177  1.00 25.47 ? 126 LEU B CA  1 
ATOM   2868 C  C   . LEU B 1 91  ? -8.458  -13.553 17.553  1.00 19.21 ? 126 LEU B C   1 
ATOM   2869 O  O   . LEU B 1 91  ? -8.826  -13.786 18.704  1.00 22.37 ? 126 LEU B O   1 
ATOM   2870 C  CB  . LEU B 1 91  ? -9.071  -11.318 16.546  1.00 17.04 ? 126 LEU B CB  1 
ATOM   2871 C  CG  . LEU B 1 91  ? -10.283 -11.139 17.447  1.00 22.00 ? 126 LEU B CG  1 
ATOM   2872 C  CD1 . LEU B 1 91  ? -10.762 -9.674  17.406  1.00 15.92 ? 126 LEU B CD1 1 
ATOM   2873 C  CD2 . LEU B 1 91  ? -11.426 -12.140 17.012  1.00 20.86 ? 126 LEU B CD2 1 
ATOM   2874 N  N   . ALA B 1 92  ? -8.457  -14.500 16.625  1.00 19.87 ? 127 ALA B N   1 
ATOM   2875 C  CA  . ALA B 1 92  ? -8.943  -15.847 16.971  1.00 27.01 ? 127 ALA B CA  1 
ATOM   2876 C  C   . ALA B 1 92  ? -8.160  -16.459 18.140  1.00 25.59 ? 127 ALA B C   1 
ATOM   2877 O  O   . ALA B 1 92  ? -8.746  -16.957 19.126  1.00 25.55 ? 127 ALA B O   1 
ATOM   2878 C  CB  . ALA B 1 92  ? -8.852  -16.752 15.746  1.00 23.48 ? 127 ALA B CB  1 
ATOM   2879 N  N   . ALA B 1 93  ? -6.822  -16.440 18.039  1.00 22.70 ? 128 ALA B N   1 
ATOM   2880 C  CA  . ALA B 1 93  ? -5.990  -17.021 19.079  1.00 23.97 ? 128 ALA B CA  1 
ATOM   2881 C  C   . ALA B 1 93  ? -6.179  -16.299 20.400  1.00 25.59 ? 128 ALA B C   1 
ATOM   2882 O  O   . ALA B 1 93  ? -6.200  -16.939 21.462  1.00 24.64 ? 128 ALA B O   1 
ATOM   2883 C  CB  . ALA B 1 93  ? -4.520  -16.998 18.661  1.00 33.94 ? 128 ALA B CB  1 
ATOM   2884 N  N   . ASN B 1 94  ? -6.287  -14.951 20.356  1.00 22.32 ? 129 ASN B N   1 
ATOM   2885 C  CA  . ASN B 1 94  ? -6.467  -14.159 21.568  1.00 24.44 ? 129 ASN B CA  1 
ATOM   2886 C  C   . ASN B 1 94  ? -7.857  -14.328 22.182  1.00 28.17 ? 129 ASN B C   1 
ATOM   2887 O  O   . ASN B 1 94  ? -8.005  -14.266 23.408  1.00 23.97 ? 129 ASN B O   1 
ATOM   2888 C  CB  . ASN B 1 94  ? -6.172  -12.685 21.263  1.00 22.24 ? 129 ASN B CB  1 
ATOM   2889 C  CG  . ASN B 1 94  ? -4.697  -12.443 21.092  1.00 20.66 ? 129 ASN B CG  1 
ATOM   2890 O  OD1 . ASN B 1 94  ? -3.914  -13.075 21.790  1.00 25.04 ? 129 ASN B OD1 1 
ATOM   2891 N  ND2 . ASN B 1 94  ? -4.305  -11.479 20.236  1.00 19.68 ? 129 ASN B ND2 1 
ATOM   2892 N  N   . LEU B 1 95  ? -8.885  -14.544 21.360  1.00 25.39 ? 130 LEU B N   1 
ATOM   2893 C  CA  . LEU B 1 95  ? -10.166 -14.989 21.883  1.00 27.62 ? 130 LEU B CA  1 
ATOM   2894 C  C   . LEU B 1 95  ? -10.004 -16.276 22.688  1.00 23.51 ? 130 LEU B C   1 
ATOM   2895 O  O   . LEU B 1 95  ? -10.475 -16.371 23.828  1.00 25.00 ? 130 LEU B O   1 
ATOM   2896 C  CB  . LEU B 1 95  ? -11.160 -15.195 20.733  1.00 26.97 ? 130 LEU B CB  1 
ATOM   2897 C  CG  . LEU B 1 95  ? -12.502 -15.816 21.119  1.00 37.02 ? 130 LEU B CG  1 
ATOM   2898 C  CD1 . LEU B 1 95  ? -13.052 -14.987 22.239  1.00 36.16 ? 130 LEU B CD1 1 
ATOM   2899 C  CD2 . LEU B 1 95  ? -13.478 -15.858 19.928  1.00 35.76 ? 130 LEU B CD2 1 
ATOM   2900 N  N   . LYS B 1 96  ? -9.307  -17.271 22.132  1.00 27.22 ? 131 LYS B N   1 
ATOM   2901 C  CA  . LYS B 1 96  ? -9.128  -18.505 22.909  1.00 26.30 ? 131 LYS B CA  1 
ATOM   2902 C  C   . LYS B 1 96  ? -8.271  -18.282 24.157  1.00 28.38 ? 131 LYS B C   1 
ATOM   2903 O  O   . LYS B 1 96  ? -8.593  -18.811 25.229  1.00 28.08 ? 131 LYS B O   1 
ATOM   2904 C  CB  . LYS B 1 96  ? -8.559  -19.622 22.031  1.00 29.85 ? 131 LYS B CB  1 
ATOM   2905 C  CG  . LYS B 1 96  ? -9.367  -19.810 20.745  1.00 29.08 ? 131 LYS B CG  1 
ATOM   2906 C  CD  . LYS B 1 96  ? -8.973  -21.045 19.997  1.00 40.54 ? 131 LYS B CD  1 
ATOM   2907 C  CE  . LYS B 1 96  ? -7.596  -20.812 19.409  1.00 44.33 ? 131 LYS B CE  1 
ATOM   2908 N  NZ  . LYS B 1 96  ? -7.635  -20.354 17.976  1.00 47.73 ? 131 LYS B NZ  1 
ATOM   2909 N  N   . ALA B 1 97  ? -7.193  -17.490 24.052  1.00 30.46 ? 132 ALA B N   1 
ATOM   2910 C  CA  . ALA B 1 97  ? -6.336  -17.250 25.210  1.00 30.17 ? 132 ALA B CA  1 
ATOM   2911 C  C   . ALA B 1 97  ? -7.075  -16.492 26.304  1.00 28.32 ? 132 ALA B C   1 
ATOM   2912 O  O   . ALA B 1 97  ? -6.743  -16.620 27.487  1.00 29.25 ? 132 ALA B O   1 
ATOM   2913 C  CB  . ALA B 1 97  ? -5.073  -16.501 24.789  1.00 28.32 ? 132 ALA B CB  1 
ATOM   2914 N  N   . ALA B 1 98  ? -8.079  -15.710 25.938  1.00 25.15 ? 133 ALA B N   1 
ATOM   2915 C  CA  . ALA B 1 98  ? -8.956  -15.063 26.904  1.00 32.67 ? 133 ALA B CA  1 
ATOM   2916 C  C   . ALA B 1 98  ? -9.972  -16.018 27.528  1.00 30.84 ? 133 ALA B C   1 
ATOM   2917 O  O   . ALA B 1 98  ? -10.826 -15.551 28.286  1.00 29.38 ? 133 ALA B O   1 
ATOM   2918 C  CB  . ALA B 1 98  ? -9.707  -13.890 26.248  1.00 27.08 ? 133 ALA B CB  1 
ATOM   2919 N  N   . GLY B 1 99  ? -9.928  -17.318 27.209  1.00 29.44 ? 134 GLY B N   1 
ATOM   2920 C  CA  . GLY B 1 99  ? -10.766 -18.312 27.869  1.00 29.65 ? 134 GLY B CA  1 
ATOM   2921 C  C   . GLY B 1 99  ? -12.136 -18.533 27.274  1.00 36.42 ? 134 GLY B C   1 
ATOM   2922 O  O   . GLY B 1 99  ? -13.043 -18.972 27.987  1.00 39.17 ? 134 GLY B O   1 
ATOM   2923 N  N   . TYR B 1 100 ? -12.322 -18.241 25.996  1.00 31.58 ? 135 TYR B N   1 
ATOM   2924 C  CA  . TYR B 1 100 ? -13.586 -18.429 25.304  1.00 31.52 ? 135 TYR B CA  1 
ATOM   2925 C  C   . TYR B 1 100 ? -13.328 -19.191 24.017  1.00 33.31 ? 135 TYR B C   1 
ATOM   2926 O  O   . TYR B 1 100 ? -12.241 -19.106 23.444  1.00 36.06 ? 135 TYR B O   1 
ATOM   2927 C  CB  . TYR B 1 100 ? -14.249 -17.095 24.965  1.00 31.00 ? 135 TYR B CB  1 
ATOM   2928 C  CG  . TYR B 1 100 ? -14.792 -16.281 26.122  1.00 33.86 ? 135 TYR B CG  1 
ATOM   2929 C  CD1 . TYR B 1 100 ? -15.993 -16.629 26.720  1.00 37.95 ? 135 TYR B CD1 1 
ATOM   2930 C  CD2 . TYR B 1 100 ? -14.106 -15.178 26.624  1.00 31.87 ? 135 TYR B CD2 1 
ATOM   2931 C  CE1 . TYR B 1 100 ? -16.519 -15.892 27.756  1.00 35.71 ? 135 TYR B CE1 1 
ATOM   2932 C  CE2 . TYR B 1 100 ? -14.629 -14.435 27.681  1.00 33.15 ? 135 TYR B CE2 1 
ATOM   2933 C  CZ  . TYR B 1 100 ? -15.836 -14.810 28.246  1.00 34.74 ? 135 TYR B CZ  1 
ATOM   2934 O  OH  . TYR B 1 100 ? -16.389 -14.110 29.299  1.00 35.12 ? 135 TYR B OH  1 
ATOM   2935 N  N   . GLN B 1 101 ? -14.382 -19.973 23.543  1.00 28.05 ? 136 GLN B N   1 
ATOM   2936 C  CA  . GLN B 1 101 ? -14.183 -20.524 22.215  1.00 30.58 ? 136 GLN B CA  1 
ATOM   2937 C  C   . GLN B 1 101 ? -15.033 -19.772 21.195  1.00 29.33 ? 136 GLN B C   1 
ATOM   2938 O  O   . GLN B 1 101 ? -16.069 -19.189 21.544  1.00 30.75 ? 136 GLN B O   1 
ATOM   2939 C  CB  . GLN B 1 101 ? -14.523 -22.028 22.154  1.00 34.93 ? 136 GLN B CB  1 
ATOM   2940 C  CG  . GLN B 1 101 ? -13.542 -22.914 22.919  1.00 45.39 ? 136 GLN B CG  1 
ATOM   2941 C  CD  . GLN B 1 101 ? -12.117 -22.847 22.357  1.00 45.04 ? 136 GLN B CD  1 
ATOM   2942 O  OE1 . GLN B 1 101 ? -11.884 -23.007 21.158  1.00 39.94 ? 136 GLN B OE1 1 
ATOM   2943 N  NE2 . GLN B 1 101 ? -11.153 -22.630 23.246  1.00 53.80 ? 136 GLN B NE2 1 
ATOM   2944 N  N   . PRO B 1 102 ? -14.605 -19.753 19.930  1.00 27.16 ? 137 PRO B N   1 
ATOM   2945 C  CA  . PRO B 1 102 ? -15.388 -19.037 18.915  1.00 24.71 ? 137 PRO B CA  1 
ATOM   2946 C  C   . PRO B 1 102 ? -16.818 -19.536 18.828  1.00 28.00 ? 137 PRO B C   1 
ATOM   2947 O  O   . PRO B 1 102 ? -17.743 -18.730 18.644  1.00 28.68 ? 137 PRO B O   1 
ATOM   2948 C  CB  . PRO B 1 102 ? -14.620 -19.323 17.621  1.00 30.54 ? 137 PRO B CB  1 
ATOM   2949 C  CG  . PRO B 1 102 ? -13.238 -19.652 18.059  1.00 36.73 ? 137 PRO B CG  1 
ATOM   2950 C  CD  . PRO B 1 102 ? -13.371 -20.334 19.372  1.00 37.97 ? 137 PRO B CD  1 
ATOM   2951 N  N   . GLU B 1 103 ? -17.015 -20.850 18.977  1.00 29.16 ? 138 GLU B N   1 
ATOM   2952 C  CA  . GLU B 1 103 ? -18.351 -21.432 18.924  1.00 31.65 ? 138 GLU B CA  1 
ATOM   2953 C  C   . GLU B 1 103 ? -19.253 -20.876 20.011  1.00 28.15 ? 138 GLU B C   1 
ATOM   2954 O  O   . GLU B 1 103 ? -20.478 -21.027 19.918  1.00 32.74 ? 138 GLU B O   1 
ATOM   2955 C  CB  . GLU B 1 103 ? -18.278 -22.964 19.057  1.00 31.49 ? 138 GLU B CB  1 
ATOM   2956 C  CG  . GLU B 1 103 ? -17.481 -23.712 17.996  1.00 30.67 ? 138 GLU B CG  1 
ATOM   2957 C  CD  . GLU B 1 103 ? -15.964 -23.593 18.168  1.00 45.12 ? 138 GLU B CD  1 
ATOM   2958 O  OE1 . GLU B 1 103 ? -15.478 -23.028 19.179  1.00 41.98 ? 138 GLU B OE1 1 
ATOM   2959 O  OE2 . GLU B 1 103 ? -15.247 -24.093 17.282  1.00 44.33 ? 138 GLU B OE2 1 
ATOM   2960 N  N   . GLN B 1 104 ? -18.681 -20.272 21.053  1.00 27.79 ? 139 GLN B N   1 
ATOM   2961 C  CA  . GLN B 1 104 ? -19.499 -19.767 22.147  1.00 32.28 ? 139 GLN B CA  1 
ATOM   2962 C  C   . GLN B 1 104 ? -20.068 -18.387 21.868  1.00 27.61 ? 139 GLN B C   1 
ATOM   2963 O  O   . GLN B 1 104 ? -20.862 -17.889 22.667  1.00 30.97 ? 139 GLN B O   1 
ATOM   2964 C  CB  . GLN B 1 104 ? -18.704 -19.735 23.463  1.00 28.59 ? 139 GLN B CB  1 
ATOM   2965 C  CG  . GLN B 1 104 ? -18.199 -21.107 23.907  1.00 30.71 ? 139 GLN B CG  1 
ATOM   2966 C  CD  . GLN B 1 104 ? -17.496 -21.071 25.249  1.00 37.86 ? 139 GLN B CD  1 
ATOM   2967 O  OE1 . GLN B 1 104 ? -16.446 -20.452 25.389  1.00 36.43 ? 139 GLN B OE1 1 
ATOM   2968 N  NE2 . GLN B 1 104 ? -18.075 -21.749 26.247  1.00 32.86 ? 139 GLN B NE2 1 
ATOM   2969 N  N   . VAL B 1 105 ? -19.688 -17.757 20.766  1.00 27.54 ? 140 VAL B N   1 
ATOM   2970 C  CA  . VAL B 1 105 ? -20.167 -16.412 20.485  1.00 23.91 ? 140 VAL B CA  1 
ATOM   2971 C  C   . VAL B 1 105 ? -21.584 -16.489 19.937  1.00 24.34 ? 140 VAL B C   1 
ATOM   2972 O  O   . VAL B 1 105 ? -21.848 -17.211 18.974  1.00 30.14 ? 140 VAL B O   1 
ATOM   2973 C  CB  . VAL B 1 105 ? -19.237 -15.694 19.503  1.00 23.32 ? 140 VAL B CB  1 
ATOM   2974 C  CG1 . VAL B 1 105 ? -19.855 -14.341 19.103  1.00 26.25 ? 140 VAL B CG1 1 
ATOM   2975 C  CG2 . VAL B 1 105 ? -17.830 -15.507 20.125  1.00 24.89 ? 140 VAL B CG2 1 
ATOM   2976 N  N   . ASP B 1 106 ? -22.487 -15.725 20.549  1.00 25.64 ? 141 ASP B N   1 
ATOM   2977 C  CA  . ASP B 1 106 ? -23.889 -15.681 20.174  1.00 25.32 ? 141 ASP B CA  1 
ATOM   2978 C  C   . ASP B 1 106 ? -24.134 -14.737 19.010  1.00 23.85 ? 141 ASP B C   1 
ATOM   2979 O  O   . ASP B 1 106 ? -24.951 -15.038 18.131  1.00 24.91 ? 141 ASP B O   1 
ATOM   2980 C  CB  . ASP B 1 106 ? -24.714 -15.255 21.378  1.00 26.10 ? 141 ASP B CB  1 
ATOM   2981 C  CG  . ASP B 1 106 ? -24.682 -16.278 22.493  1.00 35.94 ? 141 ASP B CG  1 
ATOM   2982 O  OD1 . ASP B 1 106 ? -24.980 -17.474 22.231  1.00 32.02 ? 141 ASP B OD1 1 
ATOM   2983 O  OD2 . ASP B 1 106 ? -24.319 -15.890 23.631  1.00 29.66 ? 141 ASP B OD2 1 
ATOM   2984 N  N   . GLU B 1 107 ? -23.502 -13.572 19.026  1.00 25.74 ? 142 GLU B N   1 
ATOM   2985 C  CA  . GLU B 1 107 ? -23.691 -12.573 17.985  1.00 21.56 ? 142 GLU B CA  1 
ATOM   2986 C  C   . GLU B 1 107 ? -22.361 -11.891 17.719  1.00 20.23 ? 142 GLU B C   1 
ATOM   2987 O  O   . GLU B 1 107 ? -21.521 -11.740 18.619  1.00 20.07 ? 142 GLU B O   1 
ATOM   2988 C  CB  . GLU B 1 107 ? -24.764 -11.539 18.364  1.00 21.85 ? 142 GLU B CB  1 
ATOM   2989 C  CG  . GLU B 1 107 ? -25.999 -12.241 18.874  1.00 23.43 ? 142 GLU B CG  1 
ATOM   2990 C  CD  . GLU B 1 107 ? -27.282 -11.467 18.834  1.00 28.91 ? 142 GLU B CD  1 
ATOM   2991 O  OE1 . GLU B 1 107 ? -27.264 -10.240 18.732  1.00 23.39 ? 142 GLU B OE1 1 
ATOM   2992 O  OE2 . GLU B 1 107 ? -28.351 -12.129 18.927  1.00 30.74 ? 142 GLU B OE2 1 
ATOM   2993 N  N   . VAL B 1 108 ? -22.183 -11.502 16.457  1.00 19.41 ? 143 VAL B N   1 
ATOM   2994 C  CA  . VAL B 1 108 ? -21.077 -10.655 16.030  1.00 22.54 ? 143 VAL B CA  1 
ATOM   2995 C  C   . VAL B 1 108 ? -21.670 -9.376  15.457  1.00 17.71 ? 143 VAL B C   1 
ATOM   2996 O  O   . VAL B 1 108 ? -22.476 -9.441  14.521  1.00 18.54 ? 143 VAL B O   1 
ATOM   2997 C  CB  . VAL B 1 108 ? -20.217 -11.354 14.976  1.00 17.92 ? 143 VAL B CB  1 
ATOM   2998 C  CG1 . VAL B 1 108 ? -19.114 -10.420 14.503  1.00 17.26 ? 143 VAL B CG1 1 
ATOM   2999 C  CG2 . VAL B 1 108 ? -19.648 -12.626 15.536  1.00 18.66 ? 143 VAL B CG2 1 
ATOM   3000 N  N   . TYR B 1 109 ? -21.268 -8.215  15.990  1.00 19.28 ? 144 TYR B N   1 
ATOM   3001 C  CA  . TYR B 1 109 ? -21.711 -6.912  15.475  1.00 18.66 ? 144 TYR B CA  1 
ATOM   3002 C  C   . TYR B 1 109 ? -20.549 -6.254  14.754  1.00 20.19 ? 144 TYR B C   1 
ATOM   3003 O  O   . TYR B 1 109 ? -19.435 -6.224  15.279  1.00 18.82 ? 144 TYR B O   1 
ATOM   3004 C  CB  . TYR B 1 109 ? -22.184 -5.960  16.585  1.00 17.77 ? 144 TYR B CB  1 
ATOM   3005 C  CG  . TYR B 1 109 ? -23.367 -6.451  17.401  1.00 20.56 ? 144 TYR B CG  1 
ATOM   3006 C  CD1 . TYR B 1 109 ? -24.206 -7.465  16.933  1.00 20.07 ? 144 TYR B CD1 1 
ATOM   3007 C  CD2 . TYR B 1 109 ? -23.551 -5.995  18.696  1.00 19.06 ? 144 TYR B CD2 1 
ATOM   3008 C  CE1 . TYR B 1 109 ? -25.255 -7.931  17.689  1.00 20.36 ? 144 TYR B CE1 1 
ATOM   3009 C  CE2 . TYR B 1 109 ? -24.580 -6.490  19.480  1.00 20.33 ? 144 TYR B CE2 1 
ATOM   3010 C  CZ  . TYR B 1 109 ? -25.425 -7.448  18.954  1.00 20.96 ? 144 TYR B CZ  1 
ATOM   3011 O  OH  . TYR B 1 109 ? -26.429 -7.929  19.729  1.00 22.36 ? 144 TYR B OH  1 
ATOM   3012 N  N   . LEU B 1 110 ? -20.812 -5.676  13.583  1.00 17.51 ? 145 LEU B N   1 
ATOM   3013 C  CA  . LEU B 1 110 ? -19.765 -5.065  12.779  1.00 14.79 ? 145 LEU B CA  1 
ATOM   3014 C  C   . LEU B 1 110 ? -19.955 -3.546  12.793  1.00 17.13 ? 145 LEU B C   1 
ATOM   3015 O  O   . LEU B 1 110 ? -21.030 -3.063  12.439  1.00 17.46 ? 145 LEU B O   1 
ATOM   3016 C  CB  . LEU B 1 110 ? -19.826 -5.601  11.350  1.00 15.00 ? 145 LEU B CB  1 
ATOM   3017 C  CG  . LEU B 1 110 ? -19.655 -7.140  11.231  1.00 15.27 ? 145 LEU B CG  1 
ATOM   3018 C  CD1 . LEU B 1 110 ? -19.943 -7.634  9.789   1.00 15.43 ? 145 LEU B CD1 1 
ATOM   3019 C  CD2 . LEU B 1 110 ? -18.262 -7.539  11.657  1.00 15.54 ? 145 LEU B CD2 1 
ATOM   3020 N  N   . THR B 1 111 ? -18.919 -2.793  13.208  1.00 14.22 ? 146 THR B N   1 
ATOM   3021 C  CA  . THR B 1 111 ? -18.993 -1.335  13.070  1.00 14.22 ? 146 THR B CA  1 
ATOM   3022 C  C   . THR B 1 111 ? -19.058 -0.946  11.594  1.00 14.09 ? 146 THR B C   1 
ATOM   3023 O  O   . THR B 1 111 ? -19.831 -0.049  11.209  1.00 17.16 ? 146 THR B O   1 
ATOM   3024 C  CB  . THR B 1 111 ? -17.803 -0.625  13.746  1.00 13.87 ? 146 THR B CB  1 
ATOM   3025 O  OG1 . THR B 1 111 ? -16.564 -1.047  13.163  1.00 13.31 ? 146 THR B OG1 1 
ATOM   3026 C  CG2 . THR B 1 111 ? -17.788 -0.837  15.291  1.00 14.19 ? 146 THR B CG2 1 
ATOM   3027 N  N   . HIS B 1 112 ? -18.313 -1.650  10.748  1.00 13.70 ? 147 HIS B N   1 
ATOM   3028 C  CA  . HIS B 1 112 ? -18.335 -1.443  9.300   1.00 13.70 ? 147 HIS B CA  1 
ATOM   3029 C  C   . HIS B 1 112 ? -17.585 -2.604  8.653   1.00 14.71 ? 147 HIS B C   1 
ATOM   3030 O  O   . HIS B 1 112 ? -17.066 -3.504  9.340   1.00 13.90 ? 147 HIS B O   1 
ATOM   3031 C  CB  . HIS B 1 112 ? -17.757 -0.076  8.899   1.00 13.61 ? 147 HIS B CB  1 
ATOM   3032 C  CG  . HIS B 1 112 ? -16.288 0.084   9.175   1.00 14.39 ? 147 HIS B CG  1 
ATOM   3033 N  ND1 . HIS B 1 112 ? -15.756 -0.025  10.446  1.00 13.69 ? 147 HIS B ND1 1 
ATOM   3034 C  CD2 . HIS B 1 112 ? -15.255 0.413   8.355   1.00 13.01 ? 147 HIS B CD2 1 
ATOM   3035 C  CE1 . HIS B 1 112 ? -14.455 0.235   10.397  1.00 12.71 ? 147 HIS B CE1 1 
ATOM   3036 N  NE2 . HIS B 1 112 ? -14.122 0.471   9.139   1.00 12.74 ? 147 HIS B NE2 1 
ATOM   3037 N  N   . MET B 1 113 ? -17.589 -2.631  7.315   1.00 16.53 ? 148 MET B N   1 
ATOM   3038 C  CA  . MET B 1 113 ? -17.131 -3.842  6.648   1.00 15.34 ? 148 MET B CA  1 
ATOM   3039 C  C   . MET B 1 113 ? -15.814 -3.648  5.916   1.00 15.31 ? 148 MET B C   1 
ATOM   3040 O  O   . MET B 1 113 ? -15.514 -4.397  4.980   1.00 14.28 ? 148 MET B O   1 
ATOM   3041 C  CB  . MET B 1 113 ? -18.184 -4.401  5.690   1.00 14.28 ? 148 MET B CB  1 
ATOM   3042 C  CG  . MET B 1 113 ? -19.476 -4.775  6.400   1.00 19.01 ? 148 MET B CG  1 
ATOM   3043 S  SD  . MET B 1 113 ? -20.792 -5.249  5.256   1.00 21.24 ? 148 MET B SD  1 
ATOM   3044 C  CE  . MET B 1 113 ? -22.044 -5.618  6.479   1.00 22.09 ? 148 MET B CE  1 
ATOM   3045 N  N   . HIS B 1 114 ? -14.981 -2.699  6.367   1.00 13.26 ? 149 HIS B N   1 
ATOM   3046 C  CA  . HIS B 1 114 ? -13.591 -2.693  5.920   1.00 16.34 ? 149 HIS B CA  1 
ATOM   3047 C  C   . HIS B 1 114 ? -12.909 -4.018  6.293   1.00 16.70 ? 149 HIS B C   1 
ATOM   3048 O  O   . HIS B 1 114 ? -13.319 -4.682  7.244   1.00 16.16 ? 149 HIS B O   1 
ATOM   3049 C  CB  . HIS B 1 114 ? -12.842 -1.508  6.528   1.00 15.95 ? 149 HIS B CB  1 
ATOM   3050 C  CG  . HIS B 1 114 ? -13.050 -0.221  5.756   1.00 18.24 ? 149 HIS B CG  1 
ATOM   3051 N  ND1 . HIS B 1 114 ? -12.693 1.026   6.243   1.00 15.30 ? 149 HIS B ND1 1 
ATOM   3052 C  CD2 . HIS B 1 114 ? -13.617 -0.000  4.543   1.00 17.72 ? 149 HIS B CD2 1 
ATOM   3053 C  CE1 . HIS B 1 114 ? -13.004 1.950   5.349   1.00 20.63 ? 149 HIS B CE1 1 
ATOM   3054 N  NE2 . HIS B 1 114 ? -13.578 1.358   4.314   1.00 19.36 ? 149 HIS B NE2 1 
ATOM   3055 N  N   . PRO B 1 115 ? -11.867 -4.421  5.559   1.00 13.96 ? 150 PRO B N   1 
ATOM   3056 C  CA  . PRO B 1 115 ? -11.319 -5.792  5.730   1.00 19.07 ? 150 PRO B CA  1 
ATOM   3057 C  C   . PRO B 1 115 ? -10.799 -6.104  7.121   1.00 19.05 ? 150 PRO B C   1 
ATOM   3058 O  O   . PRO B 1 115 ? -10.966 -7.242  7.586   1.00 16.81 ? 150 PRO B O   1 
ATOM   3059 C  CB  . PRO B 1 115 ? -10.193 -5.864  4.685   1.00 19.41 ? 150 PRO B CB  1 
ATOM   3060 C  CG  . PRO B 1 115 ? -10.499 -4.775  3.708   1.00 29.32 ? 150 PRO B CG  1 
ATOM   3061 C  CD  . PRO B 1 115 ? -11.179 -3.680  4.483   1.00 22.17 ? 150 PRO B CD  1 
ATOM   3062 N  N   . ASP B 1 116 ? -10.180 -5.112  7.815   1.00 14.55 ? 151 ASP B N   1 
ATOM   3063 C  CA  . ASP B 1 116 ? -9.626  -5.262  9.156   1.00 13.44 ? 151 ASP B CA  1 
ATOM   3064 C  C   . ASP B 1 116 ? -10.662 -5.334  10.238  1.00 17.59 ? 151 ASP B C   1 
ATOM   3065 O  O   . ASP B 1 116 ? -10.280 -5.358  11.442  1.00 13.20 ? 151 ASP B O   1 
ATOM   3066 C  CB  . ASP B 1 116 ? -8.639  -4.102  9.425   1.00 14.16 ? 151 ASP B CB  1 
ATOM   3067 C  CG  . ASP B 1 116 ? -9.251  -2.730  9.154   1.00 14.90 ? 151 ASP B CG  1 
ATOM   3068 O  OD1 . ASP B 1 116 ? -9.808  -2.514  8.066   1.00 17.48 ? 151 ASP B OD1 1 
ATOM   3069 O  OD2 . ASP B 1 116 ? -9.121  -1.861  10.021  1.00 14.79 ? 151 ASP B OD2 1 
ATOM   3070 N  N   . HIS B 1 117 ? -11.945 -5.408  9.848   1.00 15.15 ? 152 HIS B N   1 
ATOM   3071 C  CA  . HIS B 1 117 ? -13.047 -5.586  10.773  1.00 14.58 ? 152 HIS B CA  1 
ATOM   3072 C  C   . HIS B 1 117 ? -13.876 -6.816  10.483  1.00 13.64 ? 152 HIS B C   1 
ATOM   3073 O  O   . HIS B 1 117 ? -14.462 -7.370  11.411  1.00 15.59 ? 152 HIS B O   1 
ATOM   3074 C  CB  . HIS B 1 117 ? -13.950 -4.354  10.738  1.00 14.65 ? 152 HIS B CB  1 
ATOM   3075 C  CG  . HIS B 1 117 ? -13.203 -3.130  11.166  1.00 12.63 ? 152 HIS B CG  1 
ATOM   3076 N  ND1 . HIS B 1 117 ? -13.357 -2.583  12.411  1.00 14.47 ? 152 HIS B ND1 1 
ATOM   3077 C  CD2 . HIS B 1 117 ? -12.220 -2.429  10.555  1.00 13.32 ? 152 HIS B CD2 1 
ATOM   3078 C  CE1 . HIS B 1 117 ? -12.531 -1.553  12.542  1.00 15.92 ? 152 HIS B CE1 1 
ATOM   3079 N  NE2 . HIS B 1 117 ? -11.829 -1.439  11.425  1.00 12.39 ? 152 HIS B NE2 1 
ATOM   3080 N  N   . VAL B 1 118 ? -13.925 -7.264  9.232   1.00 18.06 ? 153 VAL B N   1 
ATOM   3081 C  CA  . VAL B 1 118 ? -14.771 -8.394  8.876   1.00 17.58 ? 153 VAL B CA  1 
ATOM   3082 C  C   . VAL B 1 118 ? -13.960 -9.632  8.541   1.00 18.25 ? 153 VAL B C   1 
ATOM   3083 O  O   . VAL B 1 118 ? -14.538 -10.731 8.485   1.00 20.89 ? 153 VAL B O   1 
ATOM   3084 C  CB  . VAL B 1 118 ? -15.715 -8.038  7.706   1.00 17.18 ? 153 VAL B CB  1 
ATOM   3085 C  CG1 . VAL B 1 118 ? -16.516 -6.817  8.094   1.00 22.29 ? 153 VAL B CG1 1 
ATOM   3086 C  CG2 . VAL B 1 118 ? -15.001 -7.867  6.329   1.00 16.09 ? 153 VAL B CG2 1 
ATOM   3087 N  N   . GLY B 1 119 ? -12.642 -9.511  8.334   1.00 18.15 ? 154 GLY B N   1 
ATOM   3088 C  CA  . GLY B 1 119 ? -11.868 -10.675 7.907   1.00 20.95 ? 154 GLY B CA  1 
ATOM   3089 C  C   . GLY B 1 119 ? -12.032 -11.863 8.840   1.00 23.61 ? 154 GLY B C   1 
ATOM   3090 O  O   . GLY B 1 119 ? -12.224 -13.001 8.390   1.00 21.66 ? 154 GLY B O   1 
ATOM   3091 N  N   . GLY B 1 120 ? -12.014 -11.603 10.153  1.00 17.74 ? 155 GLY B N   1 
ATOM   3092 C  CA  . GLY B 1 120 ? -12.094 -12.612 11.193  1.00 17.02 ? 155 GLY B CA  1 
ATOM   3093 C  C   . GLY B 1 120 ? -13.347 -13.462 11.157  1.00 23.29 ? 155 GLY B C   1 
ATOM   3094 O  O   . GLY B 1 120 ? -13.387 -14.496 11.841  1.00 21.38 ? 155 GLY B O   1 
ATOM   3095 N  N   . LEU B 1 121 ? -14.348 -13.083 10.348  1.00 20.18 ? 156 LEU B N   1 
ATOM   3096 C  CA  . LEU B 1 121 ? -15.585 -13.862 10.256  1.00 23.06 ? 156 LEU B CA  1 
ATOM   3097 C  C   . LEU B 1 121 ? -15.370 -15.238 9.631   1.00 19.34 ? 156 LEU B C   1 
ATOM   3098 O  O   . LEU B 1 121 ? -16.268 -16.108 9.730   1.00 22.02 ? 156 LEU B O   1 
ATOM   3099 C  CB  . LEU B 1 121 ? -16.625 -13.125 9.426   1.00 21.19 ? 156 LEU B CB  1 
ATOM   3100 C  CG  . LEU B 1 121 ? -17.366 -11.975 10.146  1.00 18.69 ? 156 LEU B CG  1 
ATOM   3101 C  CD1 . LEU B 1 121 ? -18.234 -11.200 9.134   1.00 19.00 ? 156 LEU B CD1 1 
ATOM   3102 C  CD2 . LEU B 1 121 ? -18.181 -12.471 11.335  1.00 18.32 ? 156 LEU B CD2 1 
ATOM   3103 N  N   . MET B 1 122 ? -14.236 -15.449 8.951   1.00 22.43 ? 157 MET B N   1 
ATOM   3104 C  CA  . MET B 1 122 ? -14.048 -16.704 8.235   1.00 20.98 ? 157 MET B CA  1 
ATOM   3105 C  C   . MET B 1 122 ? -12.659 -17.266 8.525   1.00 25.59 ? 157 MET B C   1 
ATOM   3106 O  O   . MET B 1 122 ? -11.672 -16.517 8.586   1.00 30.34 ? 157 MET B O   1 
ATOM   3107 C  CB  . MET B 1 122 ? -14.181 -16.529 6.727   1.00 25.07 ? 157 MET B CB  1 
ATOM   3108 C  CG  . MET B 1 122 ? -15.560 -16.115 6.310   1.00 26.87 ? 157 MET B CG  1 
ATOM   3109 S  SD  . MET B 1 122 ? -16.816 -17.347 6.469   1.00 23.71 ? 157 MET B SD  1 
ATOM   3110 C  CE  . MET B 1 122 ? -16.188 -18.705 5.455   1.00 24.11 ? 157 MET B CE  1 
ATOM   3111 N  N   . VAL B 1 123 ? -12.595 -18.583 8.711   1.00 28.63 ? 158 VAL B N   1 
ATOM   3112 C  CA  . VAL B 1 123 ? -11.341 -19.339 8.763   1.00 34.15 ? 158 VAL B CA  1 
ATOM   3113 C  C   . VAL B 1 123 ? -11.353 -20.316 7.589   1.00 28.11 ? 158 VAL B C   1 
ATOM   3114 O  O   . VAL B 1 123 ? -12.058 -21.332 7.600   1.00 33.81 ? 158 VAL B O   1 
ATOM   3115 C  CB  . VAL B 1 123 ? -11.138 -20.036 10.115  1.00 30.72 ? 158 VAL B CB  1 
ATOM   3116 C  CG1 . VAL B 1 123 ? -12.284 -20.970 10.441  1.00 43.08 ? 158 VAL B CG1 1 
ATOM   3117 C  CG2 . VAL B 1 123 ? -9.823  -20.820 10.111  1.00 29.61 ? 158 VAL B CG2 1 
ATOM   3118 N  N   . GLY B 1 124 ? -10.581 -20.003 6.553   1.00 35.63 ? 159 GLY B N   1 
ATOM   3119 C  CA  . GLY B 1 124 ? -10.702 -20.746 5.315   1.00 36.21 ? 159 GLY B CA  1 
ATOM   3120 C  C   . GLY B 1 124 ? -12.107 -20.612 4.779   1.00 32.35 ? 159 GLY B C   1 
ATOM   3121 O  O   . GLY B 1 124 ? -12.709 -19.545 4.824   1.00 30.64 ? 159 GLY B O   1 
ATOM   3122 N  N   . GLU B 1 125 ? -12.667 -21.707 4.285   1.00 38.67 ? 160 GLU B N   1 
ATOM   3123 C  CA  . GLU B 1 125 ? -14.047 -21.668 3.825   1.00 37.49 ? 160 GLU B CA  1 
ATOM   3124 C  C   . GLU B 1 125 ? -15.039 -22.072 4.901   1.00 36.25 ? 160 GLU B C   1 
ATOM   3125 O  O   . GLU B 1 125 ? -16.177 -22.411 4.582   1.00 42.91 ? 160 GLU B O   1 
ATOM   3126 C  CB  . GLU B 1 125 ? -14.218 -22.518 2.568   1.00 41.24 ? 160 GLU B CB  1 
ATOM   3127 C  CG  . GLU B 1 125 ? -14.059 -21.703 1.298   1.00 52.04 ? 160 GLU B CG  1 
ATOM   3128 C  CD  . GLU B 1 125 ? -12.630 -21.601 0.805   1.00 70.88 ? 160 GLU B CD  1 
ATOM   3129 O  OE1 . GLU B 1 125 ? -11.713 -22.102 1.490   1.00 78.13 ? 160 GLU B OE1 1 
ATOM   3130 O  OE2 . GLU B 1 125 ? -12.423 -20.993 -0.266  1.00 89.62 ? 160 GLU B OE2 1 
ATOM   3131 N  N   . GLN B 1 126 ? -14.660 -21.979 6.166   1.00 35.52 ? 161 GLN B N   1 
ATOM   3132 C  CA  . GLN B 1 126 ? -15.556 -22.299 7.263   1.00 29.74 ? 161 GLN B CA  1 
ATOM   3133 C  C   . GLN B 1 126 ? -15.897 -21.048 8.058   1.00 32.57 ? 161 GLN B C   1 
ATOM   3134 O  O   . GLN B 1 126 ? -15.071 -20.143 8.192   1.00 29.00 ? 161 GLN B O   1 
ATOM   3135 C  CB  . GLN B 1 126 ? -14.949 -23.357 8.165   1.00 41.06 ? 161 GLN B CB  1 
ATOM   3136 C  CG  . GLN B 1 126 ? -14.405 -24.501 7.334   1.00 38.42 ? 161 GLN B CG  1 
ATOM   3137 C  CD  . GLN B 1 126 ? -15.521 -25.363 6.836   1.00 43.13 ? 161 GLN B CD  1 
ATOM   3138 O  OE1 . GLN B 1 126 ? -16.338 -25.853 7.611   1.00 56.70 ? 161 GLN B OE1 1 
ATOM   3139 N  NE2 . GLN B 1 126 ? -15.595 -25.527 5.514   1.00 48.24 ? 161 GLN B NE2 1 
ATOM   3140 N  N   . LEU B 1 127 ? -17.135 -20.989 8.546   1.00 25.94 ? 162 LEU B N   1 
ATOM   3141 C  CA  . LEU B 1 127 ? -17.546 -19.909 9.439   1.00 25.90 ? 162 LEU B CA  1 
ATOM   3142 C  C   . LEU B 1 127 ? -16.686 -19.943 10.699  1.00 27.31 ? 162 LEU B C   1 
ATOM   3143 O  O   . LEU B 1 127 ? -16.524 -21.003 11.317  1.00 25.80 ? 162 LEU B O   1 
ATOM   3144 C  CB  . LEU B 1 127 ? -19.020 -20.088 9.815   1.00 32.30 ? 162 LEU B CB  1 
ATOM   3145 C  CG  . LEU B 1 127 ? -20.057 -20.297 8.703   1.00 35.57 ? 162 LEU B CG  1 
ATOM   3146 C  CD1 . LEU B 1 127 ? -21.499 -20.387 9.254   1.00 36.93 ? 162 LEU B CD1 1 
ATOM   3147 C  CD2 . LEU B 1 127 ? -19.971 -19.281 7.586   1.00 24.03 ? 162 LEU B CD2 1 
ATOM   3148 N  N   . ALA B 1 128 ? -16.126 -18.784 11.079  1.00 27.01 ? 163 ALA B N   1 
ATOM   3149 C  CA  . ALA B 1 128 ? -15.314 -18.721 12.292  1.00 26.07 ? 163 ALA B CA  1 
ATOM   3150 C  C   . ALA B 1 128 ? -16.161 -18.639 13.554  1.00 26.33 ? 163 ALA B C   1 
ATOM   3151 O  O   . ALA B 1 128 ? -15.692 -19.019 14.632  1.00 25.19 ? 163 ALA B O   1 
ATOM   3152 C  CB  . ALA B 1 128 ? -14.344 -17.537 12.222  1.00 22.94 ? 163 ALA B CB  1 
ATOM   3153 N  N   . PHE B 1 129 ? -17.400 -18.171 13.444  1.00 23.11 ? 164 PHE B N   1 
ATOM   3154 C  CA  . PHE B 1 129 ? -18.332 -18.125 14.564  1.00 24.62 ? 164 PHE B CA  1 
ATOM   3155 C  C   . PHE B 1 129 ? -19.596 -18.825 14.121  1.00 26.70 ? 164 PHE B C   1 
ATOM   3156 O  O   . PHE B 1 129 ? -20.609 -18.169 13.848  1.00 25.14 ? 164 PHE B O   1 
ATOM   3157 C  CB  . PHE B 1 129 ? -18.619 -16.687 14.996  1.00 23.02 ? 164 PHE B CB  1 
ATOM   3158 C  CG  . PHE B 1 129 ? -17.394 -15.926 15.272  1.00 20.84 ? 164 PHE B CG  1 
ATOM   3159 C  CD1 . PHE B 1 129 ? -16.771 -16.011 16.507  1.00 20.89 ? 164 PHE B CD1 1 
ATOM   3160 C  CD2 . PHE B 1 129 ? -16.831 -15.142 14.284  1.00 25.54 ? 164 PHE B CD2 1 
ATOM   3161 C  CE1 . PHE B 1 129 ? -15.615 -15.316 16.730  1.00 20.13 ? 164 PHE B CE1 1 
ATOM   3162 C  CE2 . PHE B 1 129 ? -15.674 -14.445 14.516  1.00 23.57 ? 164 PHE B CE2 1 
ATOM   3163 C  CZ  . PHE B 1 129 ? -15.063 -14.545 15.736  1.00 23.91 ? 164 PHE B CZ  1 
ATOM   3164 N  N   . PRO B 1 130 ? -19.564 -20.167 14.043  1.00 26.28 ? 165 PRO B N   1 
ATOM   3165 C  CA  . PRO B 1 130 ? -20.671 -20.913 13.421  1.00 28.90 ? 165 PRO B CA  1 
ATOM   3166 C  C   . PRO B 1 130 ? -21.967 -20.787 14.164  1.00 28.19 ? 165 PRO B C   1 
ATOM   3167 O  O   . PRO B 1 130 ? -23.036 -21.077 13.603  1.00 32.94 ? 165 PRO B O   1 
ATOM   3168 C  CB  . PRO B 1 130 ? -20.169 -22.368 13.454  1.00 33.91 ? 165 PRO B CB  1 
ATOM   3169 C  CG  . PRO B 1 130 ? -19.236 -22.393 14.658  1.00 31.29 ? 165 PRO B CG  1 
ATOM   3170 C  CD  . PRO B 1 130 ? -18.526 -21.066 14.580  1.00 26.28 ? 165 PRO B CD  1 
ATOM   3171 N  N   . ASN B 1 131 ? -21.910 -20.364 15.410  1.00 27.19 ? 166 ASN B N   1 
ATOM   3172 C  CA  . ASN B 1 131 ? -23.066 -20.312 16.276  1.00 33.28 ? 166 ASN B CA  1 
ATOM   3173 C  C   . ASN B 1 131 ? -23.707 -18.929 16.335  1.00 26.25 ? 166 ASN B C   1 
ATOM   3174 O  O   . ASN B 1 131 ? -24.709 -18.745 17.028  1.00 26.90 ? 166 ASN B O   1 
ATOM   3175 C  CB  . ASN B 1 131 ? -22.620 -20.793 17.654  1.00 34.18 ? 166 ASN B CB  1 
ATOM   3176 C  CG  . ASN B 1 131 ? -22.337 -22.301 17.658  1.00 33.12 ? 166 ASN B CG  1 
ATOM   3177 O  OD1 . ASN B 1 131 ? -22.699 -23.007 16.710  1.00 38.83 ? 166 ASN B OD1 1 
ATOM   3178 N  ND2 . ASN B 1 131 ? -21.644 -22.775 18.670  1.00 35.95 ? 166 ASN B ND2 1 
ATOM   3179 N  N   . ALA B 1 132 ? -23.172 -17.957 15.614  1.00 26.86 ? 167 ALA B N   1 
ATOM   3180 C  CA  . ALA B 1 132 ? -23.535 -16.573 15.857  1.00 23.69 ? 167 ALA B CA  1 
ATOM   3181 C  C   . ALA B 1 132 ? -24.456 -16.055 14.764  1.00 23.96 ? 167 ALA B C   1 
ATOM   3182 O  O   . ALA B 1 132 ? -24.524 -16.614 13.669  1.00 25.01 ? 167 ALA B O   1 
ATOM   3183 C  CB  . ALA B 1 132 ? -22.284 -15.683 15.938  1.00 28.42 ? 167 ALA B CB  1 
ATOM   3184 N  N   . VAL B 1 133 ? -25.189 -14.992 15.084  1.00 23.12 ? 168 VAL B N   1 
ATOM   3185 C  CA  . VAL B 1 133 ? -25.840 -14.169 14.071  1.00 22.65 ? 168 VAL B CA  1 
ATOM   3186 C  C   . VAL B 1 133 ? -25.008 -12.897 13.941  1.00 21.19 ? 168 VAL B C   1 
ATOM   3187 O  O   . VAL B 1 133 ? -24.533 -12.350 14.945  1.00 20.82 ? 168 VAL B O   1 
ATOM   3188 C  CB  . VAL B 1 133 ? -27.308 -13.847 14.415  1.00 24.56 ? 168 VAL B CB  1 
ATOM   3189 C  CG1 . VAL B 1 133 ? -28.094 -15.136 14.596  1.00 25.22 ? 168 VAL B CG1 1 
ATOM   3190 C  CG2 . VAL B 1 133 ? -27.416 -12.982 15.646  1.00 29.56 ? 168 VAL B CG2 1 
ATOM   3191 N  N   . VAL B 1 134 ? -24.776 -12.470 12.701  1.00 21.10 ? 169 VAL B N   1 
ATOM   3192 C  CA  . VAL B 1 134 ? -23.980 -11.286 12.412  1.00 19.47 ? 169 VAL B CA  1 
ATOM   3193 C  C   . VAL B 1 134 ? -24.941 -10.142 12.156  1.00 19.23 ? 169 VAL B C   1 
ATOM   3194 O  O   . VAL B 1 134 ? -25.941 -10.315 11.458  1.00 20.22 ? 169 VAL B O   1 
ATOM   3195 C  CB  . VAL B 1 134 ? -23.054 -11.507 11.204  1.00 23.42 ? 169 VAL B CB  1 
ATOM   3196 C  CG1 . VAL B 1 134 ? -22.301 -10.233 10.915  1.00 20.39 ? 169 VAL B CG1 1 
ATOM   3197 C  CG2 . VAL B 1 134 ? -22.067 -12.651 11.475  1.00 24.19 ? 169 VAL B CG2 1 
ATOM   3198 N  N   . ARG B 1 135 ? -24.686 -8.999  12.771  1.00 18.70 ? 170 ARG B N   1 
ATOM   3199 C  CA  . ARG B 1 135 ? -25.537 -7.831  12.597  1.00 21.59 ? 170 ARG B CA  1 
ATOM   3200 C  C   . ARG B 1 135 ? -24.703 -6.649  12.126  1.00 19.63 ? 170 ARG B C   1 
ATOM   3201 O  O   . ARG B 1 135 ? -23.569 -6.428  12.581  1.00 17.33 ? 170 ARG B O   1 
ATOM   3202 C  CB  . ARG B 1 135 ? -26.233 -7.504  13.915  1.00 19.63 ? 170 ARG B CB  1 
ATOM   3203 C  CG  . ARG B 1 135 ? -27.020 -8.722  14.453  1.00 20.80 ? 170 ARG B CG  1 
ATOM   3204 C  CD  . ARG B 1 135 ? -28.297 -8.300  15.173  1.00 26.48 ? 170 ARG B CD  1 
ATOM   3205 N  NE  . ARG B 1 135 ? -29.294 -7.632  14.345  1.00 22.51 ? 170 ARG B NE  1 
ATOM   3206 C  CZ  . ARG B 1 135 ? -30.465 -7.229  14.816  1.00 27.97 ? 170 ARG B CZ  1 
ATOM   3207 N  NH1 . ARG B 1 135 ? -30.784 -7.403  16.096  1.00 24.68 ? 170 ARG B NH1 1 
ATOM   3208 N  NH2 . ARG B 1 135 ? -31.336 -6.643  13.985  1.00 24.32 ? 170 ARG B NH2 1 
ATOM   3209 N  N   . ALA B 1 136 ? -25.237 -5.911  11.176  1.00 17.94 ? 171 ALA B N   1 
ATOM   3210 C  CA  . ALA B 1 136 ? -24.659 -4.603  10.877  1.00 22.63 ? 171 ALA B CA  1 
ATOM   3211 C  C   . ALA B 1 136 ? -25.753 -3.772  10.257  1.00 23.30 ? 171 ALA B C   1 
ATOM   3212 O  O   . ALA B 1 136 ? -26.847 -4.269  9.983   1.00 20.14 ? 171 ALA B O   1 
ATOM   3213 C  CB  . ALA B 1 136 ? -23.460 -4.674  9.935   1.00 20.90 ? 171 ALA B CB  1 
ATOM   3214 N  N   . ASP B 1 137 ? -25.447 -2.500  10.016  1.00 20.65 ? 172 ASP B N   1 
ATOM   3215 C  CA  . ASP B 1 137 ? -26.477 -1.662  9.448   1.00 18.60 ? 172 ASP B CA  1 
ATOM   3216 C  C   . ASP B 1 137 ? -26.790 -2.070  8.011   1.00 18.76 ? 172 ASP B C   1 
ATOM   3217 O  O   . ASP B 1 137 ? -25.905 -2.415  7.230   1.00 18.05 ? 172 ASP B O   1 
ATOM   3218 C  CB  . ASP B 1 137 ? -26.077 -0.181  9.506   1.00 18.51 ? 172 ASP B CB  1 
ATOM   3219 C  CG  . ASP B 1 137 ? -27.252 0.702   9.219   1.00 20.98 ? 172 ASP B CG  1 
ATOM   3220 O  OD1 . ASP B 1 137 ? -27.589 0.798   8.021   1.00 25.72 ? 172 ASP B OD1 1 
ATOM   3221 O  OD2 . ASP B 1 137 ? -27.885 1.220   10.170  1.00 21.45 ? 172 ASP B OD2 1 
ATOM   3222 N  N   . GLN B 1 138 ? -28.079 -2.005  7.668   1.00 20.65 ? 173 GLN B N   1 
ATOM   3223 C  CA  . GLN B 1 138 ? -28.547 -2.264  6.312   1.00 21.93 ? 173 GLN B CA  1 
ATOM   3224 C  C   . GLN B 1 138 ? -27.717 -1.526  5.276   1.00 19.77 ? 173 GLN B C   1 
ATOM   3225 O  O   . GLN B 1 138 ? -27.448 -2.043  4.187   1.00 19.64 ? 173 GLN B O   1 
ATOM   3226 C  CB  . GLN B 1 138 ? -29.973 -1.737  6.157   1.00 24.21 ? 173 GLN B CB  1 
ATOM   3227 C  CG  . GLN B 1 138 ? -30.723 -2.230  4.977   1.00 28.83 ? 173 GLN B CG  1 
ATOM   3228 C  CD  . GLN B 1 138 ? -31.841 -3.175  5.400   1.00 51.27 ? 173 GLN B CD  1 
ATOM   3229 O  OE1 . GLN B 1 138 ? -32.749 -2.728  6.113   1.00 36.58 ? 173 GLN B OE1 1 
ATOM   3230 N  NE2 . GLN B 1 138 ? -31.820 -4.445  4.952   1.00 33.22 ? 173 GLN B NE2 1 
ATOM   3231 N  N   . LYS B 1 139 ? -27.420 -0.247  5.549   1.00 19.71 ? 174 LYS B N   1 
ATOM   3232 C  CA  . LYS B 1 139 ? -26.760 0.575   4.545   1.00 19.49 ? 174 LYS B CA  1 
ATOM   3233 C  C   . LYS B 1 139 ? -25.327 0.112   4.322   1.00 18.30 ? 174 LYS B C   1 
ATOM   3234 O  O   . LYS B 1 139 ? -24.808 0.182   3.200   1.00 18.19 ? 174 LYS B O   1 
ATOM   3235 C  CB  . LYS B 1 139 ? -26.773 2.042   4.948   1.00 19.89 ? 174 LYS B CB  1 
ATOM   3236 C  CG  . LYS B 1 139 ? -28.144 2.610   5.192   1.00 24.00 ? 174 LYS B CG  1 
ATOM   3237 C  CD  . LYS B 1 139 ? -28.088 3.735   6.202   1.00 34.75 ? 174 LYS B CD  1 
ATOM   3238 C  CE  . LYS B 1 139 ? -28.657 3.294   7.568   1.00 38.47 ? 174 LYS B CE  1 
ATOM   3239 N  NZ  . LYS B 1 139 ? -29.961 2.543   7.634   1.00 29.66 ? 174 LYS B NZ  1 
ATOM   3240 N  N   . GLU B 1 140 ? -24.693 -0.380  5.378   1.00 17.57 ? 175 GLU B N   1 
ATOM   3241 C  CA  . GLU B 1 140 ? -23.362 -0.990  5.242   1.00 16.62 ? 175 GLU B CA  1 
ATOM   3242 C  C   . GLU B 1 140 ? -23.401 -2.212  4.323   1.00 17.72 ? 175 GLU B C   1 
ATOM   3243 O  O   . GLU B 1 140 ? -22.668 -2.288  3.329   1.00 18.33 ? 175 GLU B O   1 
ATOM   3244 C  CB  . GLU B 1 140 ? -22.849 -1.339  6.637   1.00 16.08 ? 175 GLU B CB  1 
ATOM   3245 C  CG  . GLU B 1 140 ? -21.369 -1.731  6.721   1.00 15.39 ? 175 GLU B CG  1 
ATOM   3246 C  CD  . GLU B 1 140 ? -20.433 -0.580  6.463   1.00 20.97 ? 175 GLU B CD  1 
ATOM   3247 O  OE1 . GLU B 1 140 ? -20.892 0.569   6.510   1.00 15.78 ? 175 GLU B OE1 1 
ATOM   3248 O  OE2 . GLU B 1 140 ? -19.240 -0.832  6.201   1.00 14.71 ? 175 GLU B OE2 1 
ATOM   3249 N  N   . ALA B 1 141 ? -24.280 -3.171  4.620   1.00 17.19 ? 176 ALA B N   1 
ATOM   3250 C  CA  . ALA B 1 141 ? -24.361 -4.373  3.799   1.00 17.47 ? 176 ALA B CA  1 
ATOM   3251 C  C   . ALA B 1 141 ? -24.780 -4.038  2.380   1.00 18.08 ? 176 ALA B C   1 
ATOM   3252 O  O   . ALA B 1 141 ? -24.305 -4.649  1.412   1.00 18.52 ? 176 ALA B O   1 
ATOM   3253 C  CB  . ALA B 1 141 ? -25.352 -5.353  4.419   1.00 18.10 ? 176 ALA B CB  1 
ATOM   3254 N  N   . ASP B 1 142 ? -25.665 -3.058  2.227   1.00 18.68 ? 177 ASP B N   1 
ATOM   3255 C  CA  . ASP B 1 142 ? -26.167 -2.799  0.895   1.00 22.27 ? 177 ASP B CA  1 
ATOM   3256 C  C   . ASP B 1 142 ? -25.107 -2.171  0.038   1.00 19.09 ? 177 ASP B C   1 
ATOM   3257 O  O   . ASP B 1 142 ? -25.084 -2.393  -1.182  1.00 20.58 ? 177 ASP B O   1 
ATOM   3258 C  CB  . ASP B 1 142 ? -27.421 -1.937  0.948   1.00 20.44 ? 177 ASP B CB  1 
ATOM   3259 C  CG  . ASP B 1 142 ? -28.593 -2.685  1.546   1.00 28.64 ? 177 ASP B CG  1 
ATOM   3260 O  OD1 . ASP B 1 142 ? -28.530 -3.942  1.639   1.00 29.37 ? 177 ASP B OD1 1 
ATOM   3261 O  OD2 . ASP B 1 142 ? -29.575 -2.020  1.889   1.00 27.72 ? 177 ASP B OD2 1 
ATOM   3262 N  N   . PHE B 1 143 ? -24.219 -1.389  0.650   1.00 21.55 ? 178 PHE B N   1 
ATOM   3263 C  CA  . PHE B 1 143 ? -23.109 -0.848  -0.110  1.00 22.03 ? 178 PHE B CA  1 
ATOM   3264 C  C   . PHE B 1 143 ? -22.033 -1.909  -0.390  1.00 20.46 ? 178 PHE B C   1 
ATOM   3265 O  O   . PHE B 1 143 ? -21.650 -2.115  -1.546  1.00 22.54 ? 178 PHE B O   1 
ATOM   3266 C  CB  . PHE B 1 143 ? -22.518 0.336   0.648   1.00 18.00 ? 178 PHE B CB  1 
ATOM   3267 C  CG  . PHE B 1 143 ? -21.344 0.964   -0.037  1.00 18.13 ? 178 PHE B CG  1 
ATOM   3268 C  CD1 . PHE B 1 143 ? -21.530 1.794   -1.127  1.00 18.57 ? 178 PHE B CD1 1 
ATOM   3269 C  CD2 . PHE B 1 143 ? -20.040 0.668   0.381   1.00 18.79 ? 178 PHE B CD2 1 
ATOM   3270 C  CE1 . PHE B 1 143 ? -20.442 2.381   -1.760  1.00 24.61 ? 178 PHE B CE1 1 
ATOM   3271 C  CE2 . PHE B 1 143 ? -18.952 1.254   -0.238  1.00 20.63 ? 178 PHE B CE2 1 
ATOM   3272 C  CZ  . PHE B 1 143 ? -19.155 2.111   -1.322  1.00 22.01 ? 178 PHE B CZ  1 
ATOM   3273 N  N   . TRP B 1 144 ? -21.523 -2.597  0.643   1.00 16.89 ? 179 TRP B N   1 
ATOM   3274 C  CA  . TRP B 1 144 ? -20.303 -3.405  0.435   1.00 18.31 ? 179 TRP B CA  1 
ATOM   3275 C  C   . TRP B 1 144 ? -20.569 -4.726  -0.278  1.00 17.87 ? 179 TRP B C   1 
ATOM   3276 O  O   . TRP B 1 144 ? -19.672 -5.238  -0.958  1.00 17.64 ? 179 TRP B O   1 
ATOM   3277 C  CB  . TRP B 1 144 ? -19.586 -3.681  1.770   1.00 15.76 ? 179 TRP B CB  1 
ATOM   3278 C  CG  . TRP B 1 144 ? -18.946 -2.407  2.304   1.00 18.48 ? 179 TRP B CG  1 
ATOM   3279 C  CD1 . TRP B 1 144 ? -19.348 -1.698  3.403   1.00 19.78 ? 179 TRP B CD1 1 
ATOM   3280 C  CD2 . TRP B 1 144 ? -17.816 -1.694  1.762   1.00 20.35 ? 179 TRP B CD2 1 
ATOM   3281 N  NE1 . TRP B 1 144 ? -18.543 -0.602  3.580   1.00 16.97 ? 179 TRP B NE1 1 
ATOM   3282 C  CE2 . TRP B 1 144 ? -17.594 -0.575  2.589   1.00 18.78 ? 179 TRP B CE2 1 
ATOM   3283 C  CE3 . TRP B 1 144 ? -16.956 -1.913  0.679   1.00 20.38 ? 179 TRP B CE3 1 
ATOM   3284 C  CZ2 . TRP B 1 144 ? -16.540 0.342   2.363   1.00 15.19 ? 179 TRP B CZ2 1 
ATOM   3285 C  CZ3 . TRP B 1 144 ? -15.922 -0.985  0.442   1.00 19.99 ? 179 TRP B CZ3 1 
ATOM   3286 C  CH2 . TRP B 1 144 ? -15.729 0.113   1.289   1.00 20.23 ? 179 TRP B CH2 1 
ATOM   3287 N  N   . LEU B 1 145 ? -21.784 -5.282  -0.175  1.00 22.71 ? 180 LEU B N   1 
ATOM   3288 C  CA  . LEU B 1 145 ? -22.091 -6.591  -0.754  1.00 21.86 ? 180 LEU B CA  1 
ATOM   3289 C  C   . LEU B 1 145 ? -22.715 -6.482  -2.140  1.00 22.97 ? 180 LEU B C   1 
ATOM   3290 O  O   . LEU B 1 145 ? -23.278 -7.463  -2.652  1.00 22.74 ? 180 LEU B O   1 
ATOM   3291 C  CB  . LEU B 1 145 ? -23.015 -7.367  0.177   1.00 15.10 ? 180 LEU B CB  1 
ATOM   3292 C  CG  . LEU B 1 145 ? -22.492 -7.414  1.611   1.00 18.64 ? 180 LEU B CG  1 
ATOM   3293 C  CD1 . LEU B 1 145 ? -23.464 -8.132  2.536   1.00 18.01 ? 180 LEU B CD1 1 
ATOM   3294 C  CD2 . LEU B 1 145 ? -21.049 -8.027  1.698   1.00 18.36 ? 180 LEU B CD2 1 
ATOM   3295 N  N   . SER B 1 146 ? -22.641 -5.305  -2.741  1.00 22.23 ? 181 SER B N   1 
ATOM   3296 C  CA  . SER B 1 146 ? -23.233 -5.017  -4.043  1.00 21.56 ? 181 SER B CA  1 
ATOM   3297 C  C   . SER B 1 146 ? -22.272 -5.432  -5.144  1.00 23.76 ? 181 SER B C   1 
ATOM   3298 O  O   . SER B 1 146 ? -21.195 -4.852  -5.285  1.00 23.66 ? 181 SER B O   1 
ATOM   3299 C  CB  . SER B 1 146 ? -23.564 -3.527  -4.133  1.00 25.33 ? 181 SER B CB  1 
ATOM   3300 O  OG  . SER B 1 146 ? -23.742 -3.115  -5.469  1.00 26.70 ? 181 SER B OG  1 
ATOM   3301 N  N   . GLN B 1 147 ? -22.662 -6.442  -5.923  1.00 26.10 ? 182 GLN B N   1 
ATOM   3302 C  CA  . GLN B 1 147 ? -21.882 -6.809  -7.101  1.00 24.77 ? 182 GLN B CA  1 
ATOM   3303 C  C   . GLN B 1 147 ? -21.678 -5.636  -8.051  1.00 25.94 ? 182 GLN B C   1 
ATOM   3304 O  O   . GLN B 1 147 ? -20.598 -5.490  -8.629  1.00 24.57 ? 182 GLN B O   1 
ATOM   3305 C  CB  . GLN B 1 147 ? -22.544 -7.962  -7.842  1.00 29.37 ? 182 GLN B CB  1 
ATOM   3306 C  CG  . GLN B 1 147 ? -21.680 -8.516  -8.954  1.00 29.94 ? 182 GLN B CG  1 
ATOM   3307 C  CD  . GLN B 1 147 ? -20.332 -8.984  -8.480  1.00 34.90 ? 182 GLN B CD  1 
ATOM   3308 O  OE1 . GLN B 1 147 ? -20.201 -9.546  -7.396  1.00 43.60 ? 182 GLN B OE1 1 
ATOM   3309 N  NE2 . GLN B 1 147 ? -19.317 -8.768  -9.301  1.00 35.73 ? 182 GLN B NE2 1 
ATOM   3310 N  N   . THR B 1 148 ? -22.705 -4.811  -8.267  1.00 24.11 ? 183 THR B N   1 
ATOM   3311 C  CA  . THR B 1 148 ? -22.510 -3.703  -9.199  1.00 27.33 ? 183 THR B CA  1 
ATOM   3312 C  C   . THR B 1 148 ? -21.471 -2.707  -8.675  1.00 24.95 ? 183 THR B C   1 
ATOM   3313 O  O   . THR B 1 148 ? -20.654 -2.191  -9.452  1.00 26.21 ? 183 THR B O   1 
ATOM   3314 C  CB  . THR B 1 148 ? -23.842 -3.017  -9.526  1.00 30.35 ? 183 THR B CB  1 
ATOM   3315 O  OG1 . THR B 1 148 ? -24.254 -2.188  -8.437  1.00 37.46 ? 183 THR B OG1 1 
ATOM   3316 C  CG2 . THR B 1 148 ? -24.907 -4.028  -9.847  1.00 28.36 ? 183 THR B CG2 1 
ATOM   3317 N  N   . ASN B 1 149 ? -21.455 -2.451  -7.360  1.00 24.98 ? 184 ASN B N   1 
ATOM   3318 C  CA  . ASN B 1 149 ? -20.463 -1.524  -6.833  1.00 24.50 ? 184 ASN B CA  1 
ATOM   3319 C  C   . ASN B 1 149 ? -19.067 -2.088  -7.030  1.00 25.66 ? 184 ASN B C   1 
ATOM   3320 O  O   . ASN B 1 149 ? -18.145 -1.356  -7.401  1.00 23.92 ? 184 ASN B O   1 
ATOM   3321 C  CB  . ASN B 1 149 ? -20.713 -1.236  -5.353  1.00 21.76 ? 184 ASN B CB  1 
ATOM   3322 C  CG  . ASN B 1 149 ? -21.923 -0.368  -5.127  1.00 30.44 ? 184 ASN B CG  1 
ATOM   3323 O  OD1 . ASN B 1 149 ? -22.386 0.323   -6.034  1.00 30.35 ? 184 ASN B OD1 1 
ATOM   3324 N  ND2 . ASN B 1 149 ? -22.437 -0.382  -3.905  1.00 26.93 ? 184 ASN B ND2 1 
ATOM   3325 N  N   . LEU B 1 150 ? -18.911 -3.401  -6.814  1.00 21.38 ? 185 LEU B N   1 
ATOM   3326 C  CA  . LEU B 1 150 ? -17.622 -4.055  -7.022  1.00 24.62 ? 185 LEU B CA  1 
ATOM   3327 C  C   . LEU B 1 150 ? -17.169 -3.923  -8.466  1.00 31.36 ? 185 LEU B C   1 
ATOM   3328 O  O   . LEU B 1 150 ? -16.029 -3.523  -8.733  1.00 27.60 ? 185 LEU B O   1 
ATOM   3329 C  CB  . LEU B 1 150 ? -17.704 -5.530  -6.634  1.00 21.45 ? 185 LEU B CB  1 
ATOM   3330 C  CG  . LEU B 1 150 ? -16.546 -6.393  -7.154  1.00 28.50 ? 185 LEU B CG  1 
ATOM   3331 C  CD1 . LEU B 1 150 ? -15.187 -5.846  -6.690  1.00 30.71 ? 185 LEU B CD1 1 
ATOM   3332 C  CD2 . LEU B 1 150 ? -16.682 -7.880  -6.823  1.00 27.72 ? 185 LEU B CD2 1 
ATOM   3333 N  N   . ASP B 1 151 ? -18.038 -4.269  -9.424  1.00 26.71 ? 186 ASP B N   1 
ATOM   3334 C  CA  . ASP B 1 151 ? -17.565 -4.213  -10.807 1.00 30.43 ? 186 ASP B CA  1 
ATOM   3335 C  C   . ASP B 1 151 ? -17.331 -2.791  -11.295 1.00 33.35 ? 186 ASP B C   1 
ATOM   3336 O  O   . ASP B 1 151 ? -16.630 -2.601  -12.293 1.00 38.80 ? 186 ASP B O   1 
ATOM   3337 C  CB  . ASP B 1 151 ? -18.515 -4.952  -11.745 1.00 29.44 ? 186 ASP B CB  1 
ATOM   3338 C  CG  . ASP B 1 151 ? -18.617 -6.418  -11.394 1.00 37.22 ? 186 ASP B CG  1 
ATOM   3339 O  OD1 . ASP B 1 151 ? -17.553 -7.003  -11.075 1.00 42.75 ? 186 ASP B OD1 1 
ATOM   3340 O  OD2 . ASP B 1 151 ? -19.722 -6.994  -11.455 1.00 44.84 ? 186 ASP B OD2 1 
ATOM   3341 N  N   . LYS B 1 152 ? -17.852 -1.790  -10.603 1.00 28.56 ? 187 LYS B N   1 
ATOM   3342 C  CA  . LYS B 1 152 ? -17.616 -0.419  -11.009 1.00 37.24 ? 187 LYS B CA  1 
ATOM   3343 C  C   . LYS B 1 152 ? -16.467 0.233   -10.241 1.00 33.69 ? 187 LYS B C   1 
ATOM   3344 O  O   . LYS B 1 152 ? -16.057 1.340   -10.592 1.00 31.92 ? 187 LYS B O   1 
ATOM   3345 C  CB  . LYS B 1 152 ? -18.923 0.360   -10.862 1.00 40.91 ? 187 LYS B CB  1 
ATOM   3346 C  CG  . LYS B 1 152 ? -19.851 0.042   -12.049 1.00 42.27 ? 187 LYS B CG  1 
ATOM   3347 C  CD  . LYS B 1 152 ? -21.279 -0.265  -11.614 1.00 46.34 ? 187 LYS B CD  1 
ATOM   3348 C  CE  . LYS B 1 152 ? -22.294 -0.202  -12.763 1.00 45.02 ? 187 LYS B CE  1 
ATOM   3349 N  NZ  . LYS B 1 152 ? -23.034 1.088   -12.851 1.00 49.66 ? 187 LYS B NZ  1 
ATOM   3350 N  N   . ALA B 1 153 ? -15.893 -0.462  -9.259  1.00 35.35 ? 188 ALA B N   1 
ATOM   3351 C  CA  . ALA B 1 153 ? -14.840 0.124   -8.435  1.00 36.95 ? 188 ALA B CA  1 
ATOM   3352 C  C   . ALA B 1 153 ? -13.648 0.502   -9.307  1.00 39.53 ? 188 ALA B C   1 
ATOM   3353 O  O   . ALA B 1 153 ? -13.224 -0.300  -10.150 1.00 39.28 ? 188 ALA B O   1 
ATOM   3354 C  CB  . ALA B 1 153 ? -14.401 -0.847  -7.334  1.00 30.96 ? 188 ALA B CB  1 
ATOM   3355 N  N   . PRO B 1 154 ? -13.123 1.728   -9.178  1.00 42.23 ? 189 PRO B N   1 
ATOM   3356 C  CA  . PRO B 1 154 ? -12.055 2.189   -10.070 1.00 40.85 ? 189 PRO B CA  1 
ATOM   3357 C  C   . PRO B 1 154 ? -10.624 1.933   -9.596  1.00 49.05 ? 189 PRO B C   1 
ATOM   3358 O  O   . PRO B 1 154 ? -9.800  2.843   -9.743  1.00 58.38 ? 189 PRO B O   1 
ATOM   3359 C  CB  . PRO B 1 154 ? -12.339 3.688   -10.135 1.00 46.46 ? 189 PRO B CB  1 
ATOM   3360 C  CG  . PRO B 1 154 ? -12.729 4.000   -8.691  1.00 55.32 ? 189 PRO B CG  1 
ATOM   3361 C  CD  . PRO B 1 154 ? -13.514 2.775   -8.214  1.00 40.41 ? 189 PRO B CD  1 
ATOM   3362 N  N   . ASP B 1 155 ? -10.309 0.754   -9.043  1.00 40.58 ? 190 ASP B N   1 
ATOM   3363 C  CA  . ASP B 1 155 ? -8.930  0.333   -8.766  1.00 42.09 ? 190 ASP B CA  1 
ATOM   3364 C  C   . ASP B 1 155 ? -8.954  -1.009  -8.041  1.00 32.57 ? 190 ASP B C   1 
ATOM   3365 O  O   . ASP B 1 155 ? -9.941  -1.351  -7.396  1.00 30.14 ? 190 ASP B O   1 
ATOM   3366 C  CB  . ASP B 1 155 ? -8.186  1.366   -7.927  1.00 37.66 ? 190 ASP B CB  1 
ATOM   3367 C  CG  . ASP B 1 155 ? -8.763  1.498   -6.553  1.00 42.68 ? 190 ASP B CG  1 
ATOM   3368 O  OD1 . ASP B 1 155 ? -9.736  2.275   -6.395  1.00 46.21 ? 190 ASP B OD1 1 
ATOM   3369 O  OD2 . ASP B 1 155 ? -8.209  0.866   -5.627  1.00 39.92 ? 190 ASP B OD2 1 
ATOM   3370 N  N   . ASP B 1 156 ? -7.819  -1.724  -8.083  1.00 33.91 ? 191 ASP B N   1 
ATOM   3371 C  CA  . ASP B 1 156 ? -7.723  -3.023  -7.414  1.00 32.49 ? 191 ASP B CA  1 
ATOM   3372 C  C   . ASP B 1 156 ? -7.847  -2.926  -5.890  1.00 31.43 ? 191 ASP B C   1 
ATOM   3373 O  O   . ASP B 1 156 ? -8.397  -3.839  -5.274  1.00 27.52 ? 191 ASP B O   1 
ATOM   3374 C  CB  . ASP B 1 156 ? -6.416  -3.733  -7.800  1.00 38.37 ? 191 ASP B CB  1 
ATOM   3375 C  CG  . ASP B 1 156 ? -6.519  -4.452  -9.139  1.00 38.80 ? 191 ASP B CG  1 
ATOM   3376 O  OD1 . ASP B 1 156 ? -7.608  -4.432  -9.744  1.00 45.49 ? 191 ASP B OD1 1 
ATOM   3377 O  OD2 . ASP B 1 156 ? -5.517  -5.033  -9.596  1.00 41.23 ? 191 ASP B OD2 1 
ATOM   3378 N  N   . GLU B 1 157 ? -7.356  -1.857  -5.250  1.00 34.12 ? 192 GLU B N   1 
ATOM   3379 C  CA  . GLU B 1 157 ? -7.537  -1.758  -3.793  1.00 33.90 ? 192 GLU B CA  1 
ATOM   3380 C  C   . GLU B 1 157 ? -9.011  -1.582  -3.414  1.00 29.37 ? 192 GLU B C   1 
ATOM   3381 O  O   . GLU B 1 157 ? -9.521  -2.250  -2.490  1.00 31.60 ? 192 GLU B O   1 
ATOM   3382 C  CB  . GLU B 1 157 ? -6.678  -0.620  -3.229  1.00 39.87 ? 192 GLU B CB  1 
ATOM   3383 C  CG  . GLU B 1 157 ? -6.921  -0.293  -1.736  1.00 45.08 ? 192 GLU B CG  1 
ATOM   3384 C  CD  . GLU B 1 157 ? -6.538  1.144   -1.346  1.00 52.63 ? 192 GLU B CD  1 
ATOM   3385 O  OE1 . GLU B 1 157 ? -5.344  1.502   -1.477  1.00 52.05 ? 192 GLU B OE1 1 
ATOM   3386 O  OE2 . GLU B 1 157 ? -7.420  1.914   -0.904  1.00 55.52 ? 192 GLU B OE2 1 
ATOM   3387 N  N   . SER B 1 158 ? -9.732  -0.724  -4.134  1.00 31.49 ? 193 SER B N   1 
ATOM   3388 C  CA  . SER B 1 158 ? -11.165 -0.580  -3.855  1.00 28.33 ? 193 SER B CA  1 
ATOM   3389 C  C   . SER B 1 158 ? -11.898 -1.890  -4.109  1.00 23.81 ? 193 SER B C   1 
ATOM   3390 O  O   . SER B 1 158 ? -12.734 -2.330  -3.297  1.00 25.39 ? 193 SER B O   1 
ATOM   3391 C  CB  . SER B 1 158 ? -11.756 0.529   -4.724  1.00 32.63 ? 193 SER B CB  1 
ATOM   3392 O  OG  . SER B 1 158 ? -11.064 1.742   -4.503  1.00 41.62 ? 193 SER B OG  1 
ATOM   3393 N  N   . LYS B 1 159 ? -11.607 -2.514  -5.261  1.00 25.82 ? 194 LYS B N   1 
ATOM   3394 C  CA  . LYS B 1 159 ? -12.241 -3.788  -5.581  1.00 23.00 ? 194 LYS B CA  1 
ATOM   3395 C  C   . LYS B 1 159 ? -11.970 -4.785  -4.481  1.00 22.45 ? 194 LYS B C   1 
ATOM   3396 O  O   . LYS B 1 159 ? -12.825 -5.612  -4.162  1.00 22.40 ? 194 LYS B O   1 
ATOM   3397 C  CB  . LYS B 1 159 ? -11.720 -4.356  -6.905  1.00 25.21 ? 194 LYS B CB  1 
ATOM   3398 C  CG  . LYS B 1 159 ? -12.029 -3.545  -8.135  1.00 30.79 ? 194 LYS B CG  1 
ATOM   3399 C  CD  . LYS B 1 159 ? -11.891 -4.378  -9.403  1.00 42.19 ? 194 LYS B CD  1 
ATOM   3400 C  CE  . LYS B 1 159 ? -12.386 -3.599  -10.625 1.00 35.83 ? 194 LYS B CE  1 
ATOM   3401 N  NZ  . LYS B 1 159 ? -13.793 -3.949  -10.963 1.00 39.90 ? 194 LYS B NZ  1 
ATOM   3402 N  N   . GLY B 1 160 ? -10.757 -4.751  -3.923  1.00 22.22 ? 195 GLY B N   1 
ATOM   3403 C  CA  . GLY B 1 160 ? -10.396 -5.684  -2.870  1.00 23.92 ? 195 GLY B CA  1 
ATOM   3404 C  C   . GLY B 1 160 ? -11.190 -5.483  -1.596  1.00 27.34 ? 195 GLY B C   1 
ATOM   3405 O  O   . GLY B 1 160 ? -11.478 -6.450  -0.885  1.00 20.99 ? 195 GLY B O   1 
ATOM   3406 N  N   . PHE B 1 161 ? -11.549 -4.235  -1.284  1.00 24.78 ? 196 PHE B N   1 
ATOM   3407 C  CA  . PHE B 1 161 ? -12.424 -3.990  -0.131  1.00 18.51 ? 196 PHE B CA  1 
ATOM   3408 C  C   . PHE B 1 161 ? -13.790 -4.653  -0.345  1.00 19.45 ? 196 PHE B C   1 
ATOM   3409 O  O   . PHE B 1 161 ? -14.336 -5.324  0.555   1.00 16.54 ? 196 PHE B O   1 
ATOM   3410 C  CB  . PHE B 1 161 ? -12.595 -2.484  0.065   1.00 18.09 ? 196 PHE B CB  1 
ATOM   3411 C  CG  . PHE B 1 161 ? -11.496 -1.839  0.905   1.00 18.65 ? 196 PHE B CG  1 
ATOM   3412 C  CD1 . PHE B 1 161 ? -10.176 -2.181  0.720   1.00 31.08 ? 196 PHE B CD1 1 
ATOM   3413 C  CD2 . PHE B 1 161 ? -11.798 -0.836  1.810   1.00 27.03 ? 196 PHE B CD2 1 
ATOM   3414 C  CE1 . PHE B 1 161 ? -9.175  -1.559  1.455   1.00 31.89 ? 196 PHE B CE1 1 
ATOM   3415 C  CE2 . PHE B 1 161 ? -10.812 -0.220  2.554   1.00 28.81 ? 196 PHE B CE2 1 
ATOM   3416 C  CZ  . PHE B 1 161 ? -9.497  -0.574  2.360   1.00 31.42 ? 196 PHE B CZ  1 
ATOM   3417 N  N   . PHE B 1 162 ? -14.346 -4.497  -1.552  1.00 16.55 ? 197 PHE B N   1 
ATOM   3418 C  CA  . PHE B 1 162 ? -15.618 -5.174  -1.844  1.00 15.92 ? 197 PHE B CA  1 
ATOM   3419 C  C   . PHE B 1 162 ? -15.489 -6.694  -1.779  1.00 18.08 ? 197 PHE B C   1 
ATOM   3420 O  O   . PHE B 1 162 ? -16.363 -7.383  -1.213  1.00 18.55 ? 197 PHE B O   1 
ATOM   3421 C  CB  . PHE B 1 162 ? -16.147 -4.785  -3.221  1.00 17.11 ? 197 PHE B CB  1 
ATOM   3422 C  CG  . PHE B 1 162 ? -16.669 -3.402  -3.283  1.00 17.45 ? 197 PHE B CG  1 
ATOM   3423 C  CD1 . PHE B 1 162 ? -17.947 -3.105  -2.846  1.00 22.21 ? 197 PHE B CD1 1 
ATOM   3424 C  CD2 . PHE B 1 162 ? -15.870 -2.387  -3.760  1.00 19.11 ? 197 PHE B CD2 1 
ATOM   3425 C  CE1 . PHE B 1 162 ? -18.415 -1.788  -2.899  1.00 20.34 ? 197 PHE B CE1 1 
ATOM   3426 C  CE2 . PHE B 1 162 ? -16.327 -1.089  -3.809  1.00 25.58 ? 197 PHE B CE2 1 
ATOM   3427 C  CZ  . PHE B 1 162 ? -17.601 -0.799  -3.376  1.00 18.92 ? 197 PHE B CZ  1 
ATOM   3428 N  N   . LYS B 1 163 ? -14.425 -7.241  -2.392  1.00 20.79 ? 198 LYS B N   1 
ATOM   3429 C  CA  . LYS B 1 163 ? -14.239 -8.688  -2.387  1.00 17.45 ? 198 LYS B CA  1 
ATOM   3430 C  C   . LYS B 1 163 ? -14.092 -9.218  -0.974  1.00 18.81 ? 198 LYS B C   1 
ATOM   3431 O  O   . LYS B 1 163 ? -14.650 -10.270 -0.645  1.00 16.43 ? 198 LYS B O   1 
ATOM   3432 C  CB  . LYS B 1 163 ? -13.022 -9.089  -3.231  1.00 21.48 ? 198 LYS B CB  1 
ATOM   3433 C  CG  . LYS B 1 163 ? -13.164 -8.803  -4.724  1.00 28.97 ? 198 LYS B CG  1 
ATOM   3434 C  CD  . LYS B 1 163 ? -12.035 -9.449  -5.508  1.00 26.50 ? 198 LYS B CD  1 
ATOM   3435 C  CE  . LYS B 1 163 ? -11.702 -8.704  -6.804  1.00 39.68 ? 198 LYS B CE  1 
ATOM   3436 N  NZ  . LYS B 1 163 ? -10.811 -9.503  -7.723  1.00 46.33 ? 198 LYS B NZ  1 
ATOM   3437 N  N   . GLY B 1 164 ? -13.280 -8.543  -0.155  1.00 16.31 ? 199 GLY B N   1 
ATOM   3438 C  CA  . GLY B 1 164 ? -13.109 -8.938  1.232   1.00 16.49 ? 199 GLY B CA  1 
ATOM   3439 C  C   . GLY B 1 164 ? -14.404 -8.956  2.010   1.00 18.13 ? 199 GLY B C   1 
ATOM   3440 O  O   . GLY B 1 164 ? -14.666 -9.898  2.767   1.00 24.94 ? 199 GLY B O   1 
ATOM   3441 N  N   . ALA B 1 165 ? -15.254 -7.927  1.825   1.00 18.33 ? 200 ALA B N   1 
ATOM   3442 C  CA  . ALA B 1 165 ? -16.554 -7.934  2.498   1.00 19.96 ? 200 ALA B CA  1 
ATOM   3443 C  C   . ALA B 1 165 ? -17.429 -9.100  2.036   1.00 17.05 ? 200 ALA B C   1 
ATOM   3444 O  O   . ALA B 1 165 ? -18.109 -9.742  2.841   1.00 15.21 ? 200 ALA B O   1 
ATOM   3445 C  CB  . ALA B 1 165 ? -17.298 -6.614  2.264   1.00 16.25 ? 200 ALA B CB  1 
ATOM   3446 N  N   . MET B 1 166 ? -17.455 -9.352  0.738   1.00 18.10 ? 201 MET B N   1 
ATOM   3447 C  CA  . MET B 1 166 ? -18.253 -10.431 0.198   1.00 18.17 ? 201 MET B CA  1 
ATOM   3448 C  C   . MET B 1 166 ? -17.768 -11.789 0.702   1.00 19.89 ? 201 MET B C   1 
ATOM   3449 O  O   . MET B 1 166 ? -18.563 -12.600 1.181   1.00 16.81 ? 201 MET B O   1 
ATOM   3450 C  CB  . MET B 1 166 ? -18.191 -10.332 -1.320  1.00 21.44 ? 201 MET B CB  1 
ATOM   3451 C  CG  . MET B 1 166 ? -18.944 -9.124  -1.852  1.00 21.94 ? 201 MET B CG  1 
ATOM   3452 S  SD  . MET B 1 166 ? -18.755 -8.957  -3.647  1.00 27.29 ? 201 MET B SD  1 
ATOM   3453 C  CE  . MET B 1 166 ? -19.721 -7.447  -3.864  1.00 23.00 ? 201 MET B CE  1 
ATOM   3454 N  N   . ALA B 1 167 ? -16.452 -12.021 0.651   1.00 16.63 ? 202 ALA B N   1 
ATOM   3455 C  CA  . ALA B 1 167 ? -15.902 -13.295 1.091   1.00 21.98 ? 202 ALA B CA  1 
ATOM   3456 C  C   . ALA B 1 167 ? -16.161 -13.514 2.568   1.00 21.95 ? 202 ALA B C   1 
ATOM   3457 O  O   . ALA B 1 167 ? -16.372 -14.670 2.991   1.00 19.36 ? 202 ALA B O   1 
ATOM   3458 C  CB  . ALA B 1 167 ? -14.397 -13.358 0.813   1.00 21.11 ? 202 ALA B CB  1 
ATOM   3459 N  N   . SER B 1 168 ? -16.195 -12.411 3.353   1.00 18.45 ? 203 SER B N   1 
ATOM   3460 C  CA  . SER B 1 168 ? -16.356 -12.517 4.804   1.00 19.47 ? 203 SER B CA  1 
ATOM   3461 C  C   . SER B 1 168 ? -17.814 -12.621 5.255   1.00 17.11 ? 203 SER B C   1 
ATOM   3462 O  O   . SER B 1 168 ? -18.099 -13.315 6.229   1.00 22.11 ? 203 SER B O   1 
ATOM   3463 C  CB  . SER B 1 168 ? -15.664 -11.337 5.494   1.00 22.85 ? 203 SER B CB  1 
ATOM   3464 O  OG  . SER B 1 168 ? -14.273 -11.286 5.144   1.00 15.39 ? 203 SER B OG  1 
ATOM   3465 N  N   . LEU B 1 169 ? -18.747 -11.934 4.598   1.00 17.17 ? 204 LEU B N   1 
ATOM   3466 C  CA  . LEU B 1 169 ? -20.140 -11.957 5.031   1.00 24.04 ? 204 LEU B CA  1 
ATOM   3467 C  C   . LEU B 1 169 ? -21.065 -12.849 4.228   1.00 17.04 ? 204 LEU B C   1 
ATOM   3468 O  O   . LEU B 1 169 ? -22.073 -13.312 4.773   1.00 18.88 ? 204 LEU B O   1 
ATOM   3469 C  CB  . LEU B 1 169 ? -20.773 -10.574 5.006   1.00 24.37 ? 204 LEU B CB  1 
ATOM   3470 C  CG  . LEU B 1 169 ? -20.876 -9.875  6.346   1.00 35.35 ? 204 LEU B CG  1 
ATOM   3471 C  CD1 . LEU B 1 169 ? -21.815 -8.798  6.100   1.00 31.69 ? 204 LEU B CD1 1 
ATOM   3472 C  CD2 . LEU B 1 169 ? -21.501 -10.827 7.350   1.00 22.62 ? 204 LEU B CD2 1 
ATOM   3473 N  N   . ASN B 1 170 ? -20.850 -12.973 2.924   1.00 17.43 ? 205 ASN B N   1 
ATOM   3474 C  CA  . ASN B 1 170 ? -21.798 -13.707 2.119   1.00 18.59 ? 205 ASN B CA  1 
ATOM   3475 C  C   . ASN B 1 170 ? -21.988 -15.154 2.581   1.00 18.97 ? 205 ASN B C   1 
ATOM   3476 O  O   . ASN B 1 170 ? -23.111 -15.668 2.415   1.00 20.50 ? 205 ASN B O   1 
ATOM   3477 C  CB  . ASN B 1 170 ? -21.358 -13.618 0.656   1.00 21.92 ? 205 ASN B CB  1 
ATOM   3478 C  CG  . ASN B 1 170 ? -21.817 -12.351 0.001   1.00 21.00 ? 205 ASN B CG  1 
ATOM   3479 O  OD1 . ASN B 1 170 ? -22.634 -11.592 0.562   1.00 27.79 ? 205 ASN B OD1 1 
ATOM   3480 N  ND2 . ASN B 1 170 ? -21.382 -12.147 -1.235  1.00 22.58 ? 205 ASN B ND2 1 
ATOM   3481 N  N   . PRO B 1 171 ? -21.001 -15.846 3.164   1.00 21.64 ? 206 PRO B N   1 
ATOM   3482 C  CA  . PRO B 1 171 ? -21.285 -17.162 3.765   1.00 23.49 ? 206 PRO B CA  1 
ATOM   3483 C  C   . PRO B 1 171 ? -22.338 -17.121 4.862   1.00 28.47 ? 206 PRO B C   1 
ATOM   3484 O  O   . PRO B 1 171 ? -23.131 -18.066 4.998   1.00 24.10 ? 206 PRO B O   1 
ATOM   3485 C  CB  . PRO B 1 171 ? -19.914 -17.591 4.316   1.00 22.57 ? 206 PRO B CB  1 
ATOM   3486 C  CG  . PRO B 1 171 ? -18.940 -16.968 3.414   1.00 24.32 ? 206 PRO B CG  1 
ATOM   3487 C  CD  . PRO B 1 171 ? -19.544 -15.577 3.153   1.00 18.25 ? 206 PRO B CD  1 
ATOM   3488 N  N   . TYR B 1 172 ? -22.354 -16.046 5.662   1.00 22.80 ? 207 TYR B N   1 
ATOM   3489 C  CA  . TYR B 1 172 ? -23.372 -15.911 6.693   1.00 21.80 ? 207 TYR B CA  1 
ATOM   3490 C  C   . TYR B 1 172 ? -24.717 -15.524 6.083   1.00 25.47 ? 207 TYR B C   1 
ATOM   3491 O  O   . TYR B 1 172 ? -25.757 -16.090 6.452   1.00 25.25 ? 207 TYR B O   1 
ATOM   3492 C  CB  . TYR B 1 172 ? -22.910 -14.883 7.730   1.00 18.81 ? 207 TYR B CB  1 
ATOM   3493 C  CG  . TYR B 1 172 ? -21.720 -15.342 8.544   1.00 18.65 ? 207 TYR B CG  1 
ATOM   3494 C  CD1 . TYR B 1 172 ? -20.429 -15.194 8.056   1.00 21.50 ? 207 TYR B CD1 1 
ATOM   3495 C  CD2 . TYR B 1 172 ? -21.880 -15.875 9.822   1.00 19.90 ? 207 TYR B CD2 1 
ATOM   3496 C  CE1 . TYR B 1 172 ? -19.313 -15.597 8.817   1.00 22.52 ? 207 TYR B CE1 1 
ATOM   3497 C  CE2 . TYR B 1 172 ? -20.774 -16.276 10.587  1.00 23.98 ? 207 TYR B CE2 1 
ATOM   3498 C  CZ  . TYR B 1 172 ? -19.490 -16.140 10.071  1.00 23.47 ? 207 TYR B CZ  1 
ATOM   3499 O  OH  . TYR B 1 172 ? -18.379 -16.527 10.816  1.00 27.53 ? 207 TYR B OH  1 
ATOM   3500 N  N   . VAL B 1 173 ? -24.713 -14.591 5.121   1.00 22.55 ? 208 VAL B N   1 
ATOM   3501 C  CA  . VAL B 1 173 ? -25.953 -14.229 4.425   1.00 23.04 ? 208 VAL B CA  1 
ATOM   3502 C  C   . VAL B 1 173 ? -26.599 -15.467 3.825   1.00 27.33 ? 208 VAL B C   1 
ATOM   3503 O  O   . VAL B 1 173 ? -27.798 -15.731 4.017   1.00 25.39 ? 208 VAL B O   1 
ATOM   3504 C  CB  . VAL B 1 173 ? -25.678 -13.171 3.337   1.00 23.05 ? 208 VAL B CB  1 
ATOM   3505 C  CG1 . VAL B 1 173 ? -26.954 -12.807 2.580   1.00 25.39 ? 208 VAL B CG1 1 
ATOM   3506 C  CG2 . VAL B 1 173 ? -25.029 -11.930 3.929   1.00 21.40 ? 208 VAL B CG2 1 
ATOM   3507 N  N   . LYS B 1 174 ? -25.806 -16.268 3.106   1.00 24.58 ? 209 LYS B N   1 
ATOM   3508 C  CA  . LYS B 1 174 ? -26.368 -17.445 2.460   1.00 29.36 ? 209 LYS B CA  1 
ATOM   3509 C  C   . LYS B 1 174 ? -26.780 -18.513 3.454   1.00 28.62 ? 209 LYS B C   1 
ATOM   3510 O  O   . LYS B 1 174 ? -27.606 -19.355 3.115   1.00 31.49 ? 209 LYS B O   1 
ATOM   3511 C  CB  . LYS B 1 174 ? -25.385 -18.054 1.459   1.00 33.72 ? 209 LYS B CB  1 
ATOM   3512 C  CG  . LYS B 1 174 ? -25.237 -17.296 0.160   1.00 38.80 ? 209 LYS B CG  1 
ATOM   3513 C  CD  . LYS B 1 174 ? -24.065 -17.850 -0.635  1.00 41.97 ? 209 LYS B CD  1 
ATOM   3514 C  CE  . LYS B 1 174 ? -23.760 -17.002 -1.849  1.00 54.02 ? 209 LYS B CE  1 
ATOM   3515 N  NZ  . LYS B 1 174 ? -22.334 -17.129 -2.254  1.00 63.95 ? 209 LYS B NZ  1 
ATOM   3516 N  N   . ALA B 1 175 ? -26.234 -18.494 4.671   1.00 29.12 ? 210 ALA B N   1 
ATOM   3517 C  CA  . ALA B 1 175 ? -26.637 -19.452 5.692   1.00 32.79 ? 210 ALA B CA  1 
ATOM   3518 C  C   . ALA B 1 175 ? -27.819 -18.973 6.529   1.00 28.28 ? 210 ALA B C   1 
ATOM   3519 O  O   . ALA B 1 175 ? -28.190 -19.654 7.492   1.00 31.45 ? 210 ALA B O   1 
ATOM   3520 C  CB  . ALA B 1 175 ? -25.453 -19.778 6.606   1.00 29.43 ? 210 ALA B CB  1 
ATOM   3521 N  N   . GLY B 1 176 ? -28.412 -17.830 6.192   1.00 25.65 ? 211 GLY B N   1 
ATOM   3522 C  CA  . GLY B 1 176 ? -29.491 -17.283 6.993   1.00 27.18 ? 211 GLY B CA  1 
ATOM   3523 C  C   . GLY B 1 176 ? -29.049 -16.734 8.337   1.00 30.24 ? 211 GLY B C   1 
ATOM   3524 O  O   . GLY B 1 176 ? -29.856 -16.675 9.276   1.00 24.66 ? 211 GLY B O   1 
ATOM   3525 N  N   . LYS B 1 177 ? -27.786 -16.317 8.462   1.00 24.59 ? 212 LYS B N   1 
ATOM   3526 C  CA  . LYS B 1 177 ? -27.260 -15.891 9.752   1.00 24.97 ? 212 LYS B CA  1 
ATOM   3527 C  C   . LYS B 1 177 ? -26.940 -14.408 9.794   1.00 22.38 ? 212 LYS B C   1 
ATOM   3528 O  O   . LYS B 1 177 ? -26.359 -13.947 10.772  1.00 24.55 ? 212 LYS B O   1 
ATOM   3529 C  CB  . LYS B 1 177 ? -26.004 -16.685 10.132  1.00 23.15 ? 212 LYS B CB  1 
ATOM   3530 C  CG  . LYS B 1 177 ? -26.280 -18.156 10.543  1.00 26.75 ? 212 LYS B CG  1 
ATOM   3531 C  CD  . LYS B 1 177 ? -25.058 -19.029 10.239  1.00 32.95 ? 212 LYS B CD  1 
ATOM   3532 C  CE  . LYS B 1 177 ? -25.095 -20.302 11.073  1.00 37.32 ? 212 LYS B CE  1 
ATOM   3533 N  NZ  . LYS B 1 177 ? -25.150 -19.873 12.516  1.00 33.75 ? 212 LYS B NZ  1 
ATOM   3534 N  N   . PHE B 1 178 ? -27.304 -13.647 8.773   1.00 20.61 ? 213 PHE B N   1 
ATOM   3535 C  CA  . PHE B 1 178 ? -27.073 -12.199 8.796   1.00 19.55 ? 213 PHE B CA  1 
ATOM   3536 C  C   . PHE B 1 178 ? -28.368 -11.466 9.095   1.00 19.98 ? 213 PHE B C   1 
ATOM   3537 O  O   . PHE B 1 178 ? -29.345 -11.611 8.353   1.00 21.86 ? 213 PHE B O   1 
ATOM   3538 C  CB  . PHE B 1 178 ? -26.515 -11.702 7.479   1.00 19.02 ? 213 PHE B CB  1 
ATOM   3539 C  CG  . PHE B 1 178 ? -26.289 -10.211 7.475   1.00 18.12 ? 213 PHE B CG  1 
ATOM   3540 C  CD1 . PHE B 1 178 ? -25.389 -9.643  8.358   1.00 19.85 ? 213 PHE B CD1 1 
ATOM   3541 C  CD2 . PHE B 1 178 ? -27.022 -9.393  6.619   1.00 18.31 ? 213 PHE B CD2 1 
ATOM   3542 C  CE1 . PHE B 1 178 ? -25.179 -8.248  8.372   1.00 23.14 ? 213 PHE B CE1 1 
ATOM   3543 C  CE2 . PHE B 1 178 ? -26.810 -8.009  6.603   1.00 17.69 ? 213 PHE B CE2 1 
ATOM   3544 C  CZ  . PHE B 1 178 ? -25.892 -7.432  7.504   1.00 16.78 ? 213 PHE B CZ  1 
ATOM   3545 N  N   . LYS B 1 179 ? -28.373 -10.674 10.166  1.00 20.44 ? 214 LYS B N   1 
ATOM   3546 C  CA  . LYS B 1 179 ? -29.578 -9.957  10.599  1.00 24.43 ? 214 LYS B CA  1 
ATOM   3547 C  C   . LYS B 1 179 ? -29.312 -8.457  10.679  1.00 25.10 ? 214 LYS B C   1 
ATOM   3548 O  O   . LYS B 1 179 ? -28.869 -7.946  11.726  1.00 19.16 ? 214 LYS B O   1 
ATOM   3549 C  CB  . LYS B 1 179 ? -30.065 -10.480 11.948  1.00 26.17 ? 214 LYS B CB  1 
ATOM   3550 C  CG  . LYS B 1 179 ? -31.402 -9.891  12.360  1.00 22.10 ? 214 LYS B CG  1 
ATOM   3551 C  CD  . LYS B 1 179 ? -31.905 -10.492 13.666  1.00 36.24 ? 214 LYS B CD  1 
ATOM   3552 C  CE  . LYS B 1 179 ? -33.259 -9.910  14.055  1.00 37.86 ? 214 LYS B CE  1 
ATOM   3553 N  NZ  . LYS B 1 179 ? -33.761 -10.474 15.339  1.00 42.86 ? 214 LYS B NZ  1 
ATOM   3554 N  N   . PRO B 1 180 ? -29.584 -7.703  9.617   1.00 21.48 ? 215 PRO B N   1 
ATOM   3555 C  CA  . PRO B 1 180 ? -29.234 -6.278  9.641   1.00 18.58 ? 215 PRO B CA  1 
ATOM   3556 C  C   . PRO B 1 180 ? -30.228 -5.514  10.494  1.00 19.91 ? 215 PRO B C   1 
ATOM   3557 O  O   . PRO B 1 180 ? -31.301 -6.009  10.863  1.00 20.33 ? 215 PRO B O   1 
ATOM   3558 C  CB  . PRO B 1 180 ? -29.314 -5.854  8.169   1.00 21.43 ? 215 PRO B CB  1 
ATOM   3559 C  CG  . PRO B 1 180 ? -30.311 -6.742  7.614   1.00 29.42 ? 215 PRO B CG  1 
ATOM   3560 C  CD  . PRO B 1 180 ? -30.102 -8.101  8.298   1.00 20.67 ? 215 PRO B CD  1 
ATOM   3561 N  N   . PHE B 1 181 ? -29.830 -4.304  10.840  1.00 19.67 ? 216 PHE B N   1 
ATOM   3562 C  CA  . PHE B 1 181 ? -30.673 -3.335  11.519  1.00 21.88 ? 216 PHE B CA  1 
ATOM   3563 C  C   . PHE B 1 181 ? -30.561 -2.045  10.724  1.00 19.39 ? 216 PHE B C   1 
ATOM   3564 O  O   . PHE B 1 181 ? -29.759 -1.946  9.795   1.00 22.98 ? 216 PHE B O   1 
ATOM   3565 C  CB  . PHE B 1 181 ? -30.249 -3.149  12.983  1.00 19.27 ? 216 PHE B CB  1 
ATOM   3566 C  CG  . PHE B 1 181 ? -28.821 -2.707  13.131  1.00 18.06 ? 216 PHE B CG  1 
ATOM   3567 C  CD1 . PHE B 1 181 ? -28.442 -1.372  12.937  1.00 19.03 ? 216 PHE B CD1 1 
ATOM   3568 C  CD2 . PHE B 1 181 ? -27.854 -3.630  13.443  1.00 18.02 ? 216 PHE B CD2 1 
ATOM   3569 C  CE1 . PHE B 1 181 ? -27.117 -0.998  13.066  1.00 19.01 ? 216 PHE B CE1 1 
ATOM   3570 C  CE2 . PHE B 1 181 ? -26.553 -3.280  13.574  1.00 16.73 ? 216 PHE B CE2 1 
ATOM   3571 C  CZ  . PHE B 1 181 ? -26.156 -1.957  13.390  1.00 19.78 ? 216 PHE B CZ  1 
ATOM   3572 N  N   . SER B 1 182 ? -31.369 -1.050  11.071  1.00 20.03 ? 217 SER B N   1 
ATOM   3573 C  CA  . SER B 1 182 ? -31.284 0.254   10.405  1.00 24.02 ? 217 SER B CA  1 
ATOM   3574 C  C   . SER B 1 182 ? -31.217 1.366   11.443  1.00 29.53 ? 217 SER B C   1 
ATOM   3575 O  O   . SER B 1 182 ? -32.165 1.551   12.206  1.00 26.11 ? 217 SER B O   1 
ATOM   3576 C  CB  . SER B 1 182 ? -32.466 0.479   9.461   1.00 29.89 ? 217 SER B CB  1 
ATOM   3577 O  OG  . SER B 1 182 ? -32.392 1.789   8.892   1.00 35.38 ? 217 SER B OG  1 
ATOM   3578 N  N   . GLY B 1 183 ? -30.107 2.114   11.463  1.00 20.43 ? 218 GLY B N   1 
ATOM   3579 C  CA  . GLY B 1 183 ? -30.077 3.225   12.402  1.00 20.95 ? 218 GLY B CA  1 
ATOM   3580 C  C   . GLY B 1 183 ? -30.082 2.771   13.865  1.00 26.95 ? 218 GLY B C   1 
ATOM   3581 O  O   . GLY B 1 183 ? -29.881 1.597   14.173  1.00 24.99 ? 218 GLY B O   1 
ATOM   3582 N  N   . ASN B 1 184 ? -30.374 3.728   14.769  1.00 25.55 ? 219 ASN B N   1 
ATOM   3583 C  CA  . ASN B 1 184 ? -30.403 3.480   16.213  1.00 22.09 ? 219 ASN B CA  1 
ATOM   3584 C  C   . ASN B 1 184 ? -31.335 2.316   16.559  1.00 31.07 ? 219 ASN B C   1 
ATOM   3585 O  O   . ASN B 1 184 ? -32.538 2.373   16.284  1.00 23.78 ? 219 ASN B O   1 
ATOM   3586 C  CB  . ASN B 1 184 ? -30.872 4.741   16.949  1.00 23.97 ? 219 ASN B CB  1 
ATOM   3587 C  CG  . ASN B 1 184 ? -29.928 5.940   16.746  1.00 26.10 ? 219 ASN B CG  1 
ATOM   3588 O  OD1 . ASN B 1 184 ? -28.845 5.809   16.193  1.00 27.26 ? 219 ASN B OD1 1 
ATOM   3589 N  ND2 . ASN B 1 184 ? -30.347 7.102   17.222  1.00 34.50 ? 219 ASN B ND2 1 
ATOM   3590 N  N   . THR B 1 185 ? -30.799 1.276   17.197  1.00 21.99 ? 220 THR B N   1 
ATOM   3591 C  CA  . THR B 1 185 ? -31.579 0.047   17.383  1.00 25.76 ? 220 THR B CA  1 
ATOM   3592 C  C   . THR B 1 185 ? -31.143 -0.653  18.660  1.00 25.47 ? 220 THR B C   1 
ATOM   3593 O  O   . THR B 1 185 ? -29.939 -0.788  18.907  1.00 25.82 ? 220 THR B O   1 
ATOM   3594 C  CB  . THR B 1 185 ? -31.371 -0.937  16.227  1.00 22.11 ? 220 THR B CB  1 
ATOM   3595 O  OG1 . THR B 1 185 ? -31.647 -0.305  14.974  1.00 25.78 ? 220 THR B OG1 1 
ATOM   3596 C  CG2 . THR B 1 185 ? -32.278 -2.186  16.401  1.00 26.60 ? 220 THR B CG2 1 
ATOM   3597 N  N   . ASP B 1 186 ? -32.103 -1.155  19.436  1.00 25.43 ? 221 ASP B N   1 
ATOM   3598 C  CA  . ASP B 1 186 ? -31.730 -1.996  20.563  1.00 28.10 ? 221 ASP B CA  1 
ATOM   3599 C  C   . ASP B 1 186 ? -31.347 -3.367  20.029  1.00 31.65 ? 221 ASP B C   1 
ATOM   3600 O  O   . ASP B 1 186 ? -32.126 -4.004  19.312  1.00 29.72 ? 221 ASP B O   1 
ATOM   3601 C  CB  . ASP B 1 186 ? -32.873 -2.151  21.551  1.00 29.59 ? 221 ASP B CB  1 
ATOM   3602 C  CG  . ASP B 1 186 ? -33.221 -0.865  22.261  1.00 26.46 ? 221 ASP B CG  1 
ATOM   3603 O  OD1 . ASP B 1 186 ? -32.482 0.112   22.106  1.00 29.66 ? 221 ASP B OD1 1 
ATOM   3604 O  OD2 . ASP B 1 186 ? -34.293 -0.840  22.929  1.00 29.33 ? 221 ASP B OD2 1 
ATOM   3605 N  N   . LEU B 1 187 ? -30.136 -3.797  20.339  1.00 24.11 ? 222 LEU B N   1 
ATOM   3606 C  CA  . LEU B 1 187 ? -29.686 -5.154  20.083  1.00 25.63 ? 222 LEU B CA  1 
ATOM   3607 C  C   . LEU B 1 187 ? -29.865 -5.981  21.355  1.00 26.59 ? 222 LEU B C   1 
ATOM   3608 O  O   . LEU B 1 187 ? -30.818 -5.760  22.116  1.00 35.25 ? 222 LEU B O   1 
ATOM   3609 C  CB  . LEU B 1 187 ? -28.246 -5.142  19.559  1.00 25.99 ? 222 LEU B CB  1 
ATOM   3610 C  CG  . LEU B 1 187 ? -28.111 -4.244  18.308  1.00 19.33 ? 222 LEU B CG  1 
ATOM   3611 C  CD1 . LEU B 1 187 ? -26.677 -4.186  17.787  1.00 18.64 ? 222 LEU B CD1 1 
ATOM   3612 C  CD2 . LEU B 1 187 ? -29.125 -4.632  17.186  1.00 22.43 ? 222 LEU B CD2 1 
ATOM   3613 N  N   . VAL B 1 188 ? -29.041 -7.012  21.513  1.00 31.38 ? 223 VAL B N   1 
ATOM   3614 C  CA  . VAL B 1 188 ? -28.924 -7.769  22.759  1.00 27.78 ? 223 VAL B CA  1 
ATOM   3615 C  C   . VAL B 1 188 ? -29.129 -6.840  23.951  1.00 29.53 ? 223 VAL B C   1 
ATOM   3616 O  O   . VAL B 1 188 ? -28.576 -5.735  23.965  1.00 30.26 ? 223 VAL B O   1 
ATOM   3617 C  CB  . VAL B 1 188 ? -27.547 -8.456  22.834  1.00 36.88 ? 223 VAL B CB  1 
ATOM   3618 C  CG1 . VAL B 1 188 ? -27.120 -8.641  24.270  1.00 42.60 ? 223 VAL B CG1 1 
ATOM   3619 C  CG2 . VAL B 1 188 ? -27.590 -9.810  22.145  1.00 27.65 ? 223 VAL B CG2 1 
ATOM   3620 N  N   . PRO B 1 189 ? -29.947 -7.225  24.951  1.00 35.00 ? 224 PRO B N   1 
ATOM   3621 C  CA  . PRO B 1 189 ? -30.047 -6.423  26.176  1.00 27.10 ? 224 PRO B CA  1 
ATOM   3622 C  C   . PRO B 1 189 ? -28.701 -5.992  26.720  1.00 26.20 ? 224 PRO B C   1 
ATOM   3623 O  O   . PRO B 1 189 ? -27.872 -6.835  27.058  1.00 31.70 ? 224 PRO B O   1 
ATOM   3624 C  CB  . PRO B 1 189 ? -30.765 -7.367  27.144  1.00 35.99 ? 224 PRO B CB  1 
ATOM   3625 C  CG  . PRO B 1 189 ? -31.693 -8.151  26.215  1.00 29.45 ? 224 PRO B CG  1 
ATOM   3626 C  CD  . PRO B 1 189 ? -30.849 -8.392  24.984  1.00 30.56 ? 224 PRO B CD  1 
ATOM   3627 N  N   . GLY B 1 190 ? -28.481 -4.685  26.809  1.00 29.78 ? 225 GLY B N   1 
ATOM   3628 C  CA  . GLY B 1 190 ? -27.195 -4.143  27.227  1.00 24.89 ? 225 GLY B CA  1 
ATOM   3629 C  C   . GLY B 1 190 ? -26.383 -3.529  26.116  1.00 23.09 ? 225 GLY B C   1 
ATOM   3630 O  O   . GLY B 1 190 ? -25.390 -2.843  26.416  1.00 24.61 ? 225 GLY B O   1 
ATOM   3631 N  N   . ILE B 1 191 ? -26.744 -3.744  24.849  1.00 23.56 ? 226 ILE B N   1 
ATOM   3632 C  CA  . ILE B 1 191 ? -25.984 -3.209  23.721  1.00 20.78 ? 226 ILE B CA  1 
ATOM   3633 C  C   . ILE B 1 191 ? -26.946 -2.593  22.717  1.00 26.03 ? 226 ILE B C   1 
ATOM   3634 O  O   . ILE B 1 191 ? -27.946 -3.219  22.352  1.00 22.70 ? 226 ILE B O   1 
ATOM   3635 C  CB  . ILE B 1 191 ? -25.132 -4.295  23.044  1.00 19.87 ? 226 ILE B CB  1 
ATOM   3636 C  CG1 . ILE B 1 191 ? -24.312 -5.085  24.073  1.00 24.17 ? 226 ILE B CG1 1 
ATOM   3637 C  CG2 . ILE B 1 191 ? -24.239 -3.683  21.972  1.00 21.93 ? 226 ILE B CG2 1 
ATOM   3638 C  CD1 . ILE B 1 191 ? -23.585 -6.317  23.494  1.00 24.20 ? 226 ILE B CD1 1 
ATOM   3639 N  N   . LYS B 1 192 ? -26.648 -1.367  22.270  1.00 23.49 ? 227 LYS B N   1 
ATOM   3640 C  CA  . LYS B 1 192 ? -27.444 -0.721  21.230  1.00 23.64 ? 227 LYS B CA  1 
ATOM   3641 C  C   . LYS B 1 192 ? -26.572 -0.310  20.059  1.00 21.31 ? 227 LYS B C   1 
ATOM   3642 O  O   . LYS B 1 192 ? -25.409 0.079   20.228  1.00 21.80 ? 227 LYS B O   1 
ATOM   3643 C  CB  . LYS B 1 192 ? -28.178 0.568   21.678  1.00 24.64 ? 227 LYS B CB  1 
ATOM   3644 C  CG  . LYS B 1 192 ? -29.159 0.518   22.861  1.00 30.21 ? 227 LYS B CG  1 
ATOM   3645 C  CD  . LYS B 1 192 ? -28.511 -0.042  24.089  1.00 36.72 ? 227 LYS B CD  1 
ATOM   3646 C  CE  . LYS B 1 192 ? -27.725 1.074   24.762  1.00 43.28 ? 227 LYS B CE  1 
ATOM   3647 N  NZ  . LYS B 1 192 ? -26.796 0.604   25.812  1.00 29.18 ? 227 LYS B NZ  1 
ATOM   3648 N  N   . ALA B 1 193 ? -27.171 -0.323  18.876  1.00 21.38 ? 228 ALA B N   1 
ATOM   3649 C  CA  . ALA B 1 193 ? -26.560 0.285   17.706  1.00 20.20 ? 228 ALA B CA  1 
ATOM   3650 C  C   . ALA B 1 193 ? -26.868 1.771   17.669  1.00 18.09 ? 228 ALA B C   1 
ATOM   3651 O  O   . ALA B 1 193 ? -28.020 2.178   17.833  1.00 20.20 ? 228 ALA B O   1 
ATOM   3652 C  CB  . ALA B 1 193 ? -27.067 -0.369  16.426  1.00 17.54 ? 228 ALA B CB  1 
ATOM   3653 N  N   . LEU B 1 194 ? -25.840 2.578   17.416  1.00 21.61 ? 229 LEU B N   1 
ATOM   3654 C  CA  . LEU B 1 194 ? -25.952 4.028   17.303  1.00 21.67 ? 229 LEU B CA  1 
ATOM   3655 C  C   . LEU B 1 194 ? -25.341 4.471   15.981  1.00 20.53 ? 229 LEU B C   1 
ATOM   3656 O  O   . LEU B 1 194 ? -24.144 4.262   15.759  1.00 16.29 ? 229 LEU B O   1 
ATOM   3657 C  CB  . LEU B 1 194 ? -25.250 4.720   18.477  1.00 21.89 ? 229 LEU B CB  1 
ATOM   3658 C  CG  . LEU B 1 194 ? -25.284 6.241   18.506  1.00 20.23 ? 229 LEU B CG  1 
ATOM   3659 C  CD1 . LEU B 1 194 ? -26.569 6.784   19.098  1.00 23.86 ? 229 LEU B CD1 1 
ATOM   3660 C  CD2 . LEU B 1 194 ? -24.028 6.833   19.262  1.00 24.15 ? 229 LEU B CD2 1 
ATOM   3661 N  N   . ALA B 1 195 ? -26.161 5.096   15.126  1.00 24.53 ? 230 ALA B N   1 
ATOM   3662 C  CA  . ALA B 1 195 ? -25.767 5.470   13.768  1.00 17.28 ? 230 ALA B CA  1 
ATOM   3663 C  C   . ALA B 1 195 ? -24.658 6.501   13.818  1.00 18.27 ? 230 ALA B C   1 
ATOM   3664 O  O   . ALA B 1 195 ? -24.799 7.560   14.437  1.00 24.41 ? 230 ALA B O   1 
ATOM   3665 C  CB  . ALA B 1 195 ? -26.954 5.980   12.974  1.00 22.45 ? 230 ALA B CB  1 
ATOM   3666 N  N   . SER B 1 196 ? -23.544 6.187   13.184  1.00 19.19 ? 231 SER B N   1 
ATOM   3667 C  CA  . SER B 1 196 ? -22.426 7.122   13.082  1.00 16.32 ? 231 SER B CA  1 
ATOM   3668 C  C   . SER B 1 196 ? -21.842 7.069   11.669  1.00 17.42 ? 231 SER B C   1 
ATOM   3669 O  O   . SER B 1 196 ? -20.649 6.844   11.462  1.00 19.53 ? 231 SER B O   1 
ATOM   3670 C  CB  . SER B 1 196 ? -21.406 6.831   14.172  1.00 16.53 ? 231 SER B CB  1 
ATOM   3671 O  OG  . SER B 1 196 ? -20.860 5.539   14.054  1.00 22.43 ? 231 SER B OG  1 
ATOM   3672 N  N   . HIS B 1 197 ? -22.709 7.202   10.674  1.00 18.88 ? 232 HIS B N   1 
ATOM   3673 C  CA  . HIS B 1 197 ? -22.320 7.036   9.280   1.00 19.45 ? 232 HIS B CA  1 
ATOM   3674 C  C   . HIS B 1 197 ? -21.362 8.145   8.829   1.00 20.02 ? 232 HIS B C   1 
ATOM   3675 O  O   . HIS B 1 197 ? -21.408 9.280   9.317   1.00 22.65 ? 232 HIS B O   1 
ATOM   3676 C  CB  . HIS B 1 197 ? -23.563 7.050   8.378   1.00 19.14 ? 232 HIS B CB  1 
ATOM   3677 C  CG  . HIS B 1 197 ? -24.651 6.127   8.816   1.00 16.81 ? 232 HIS B CG  1 
ATOM   3678 N  ND1 . HIS B 1 197 ? -24.425 4.993   9.563   1.00 17.48 ? 232 HIS B ND1 1 
ATOM   3679 C  CD2 . HIS B 1 197 ? -25.982 6.141   8.555   1.00 17.69 ? 232 HIS B CD2 1 
ATOM   3680 C  CE1 . HIS B 1 197 ? -25.568 4.371   9.780   1.00 19.64 ? 232 HIS B CE1 1 
ATOM   3681 N  NE2 . HIS B 1 197 ? -26.528 5.050   9.181   1.00 17.89 ? 232 HIS B NE2 1 
ATOM   3682 N  N   . GLY B 1 198 ? -20.510 7.799   7.864   1.00 16.37 ? 233 GLY B N   1 
ATOM   3683 C  CA  . GLY B 1 198 ? -19.609 8.711   7.174   1.00 24.32 ? 233 GLY B CA  1 
ATOM   3684 C  C   . GLY B 1 198 ? -18.233 8.127   6.882   1.00 19.08 ? 233 GLY B C   1 
ATOM   3685 O  O   . GLY B 1 198 ? -17.786 8.213   5.735   1.00 22.03 ? 233 GLY B O   1 
ATOM   3686 N  N   . HIS B 1 199 ? -17.596 7.433   7.831   1.00 14.81 ? 234 HIS B N   1 
ATOM   3687 C  CA  . HIS B 1 199 ? -16.425 6.623   7.465   1.00 21.52 ? 234 HIS B CA  1 
ATOM   3688 C  C   . HIS B 1 199 ? -16.784 5.596   6.386   1.00 18.31 ? 234 HIS B C   1 
ATOM   3689 O  O   . HIS B 1 199 ? -16.039 5.417   5.409   1.00 16.49 ? 234 HIS B O   1 
ATOM   3690 C  CB  . HIS B 1 199 ? -15.875 5.919   8.700   1.00 13.79 ? 234 HIS B CB  1 
ATOM   3691 C  CG  . HIS B 1 199 ? -14.686 5.063   8.448   1.00 15.48 ? 234 HIS B CG  1 
ATOM   3692 N  ND1 . HIS B 1 199 ? -13.478 5.550   7.977   1.00 19.27 ? 234 HIS B ND1 1 
ATOM   3693 C  CD2 . HIS B 1 199 ? -14.511 3.741   8.653   1.00 12.87 ? 234 HIS B CD2 1 
ATOM   3694 C  CE1 . HIS B 1 199 ? -12.612 4.554   7.895   1.00 19.07 ? 234 HIS B CE1 1 
ATOM   3695 N  NE2 . HIS B 1 199 ? -13.220 3.442   8.291   1.00 12.91 ? 234 HIS B NE2 1 
ATOM   3696 N  N   . THR B 1 200 ? -17.939 4.959   6.527   1.00 16.18 ? 235 THR B N   1 
ATOM   3697 C  CA  . THR B 1 200 ? -18.585 4.121   5.524   1.00 18.33 ? 235 THR B CA  1 
ATOM   3698 C  C   . THR B 1 200 ? -20.062 4.474   5.560   1.00 15.15 ? 235 THR B C   1 
ATOM   3699 O  O   . THR B 1 200 ? -20.527 5.042   6.555   1.00 20.18 ? 235 THR B O   1 
ATOM   3700 C  CB  . THR B 1 200 ? -18.440 2.622   5.811   1.00 17.25 ? 235 THR B CB  1 
ATOM   3701 O  OG1 . THR B 1 200 ? -19.005 2.344   7.095   1.00 16.35 ? 235 THR B OG1 1 
ATOM   3702 C  CG2 . THR B 1 200 ? -16.930 2.145   5.793   1.00 15.19 ? 235 THR B CG2 1 
ATOM   3703 N  N   . PRO B 1 201 ? -20.825 4.101   4.526   1.00 18.57 ? 236 PRO B N   1 
ATOM   3704 C  CA  . PRO B 1 201 ? -22.242 4.507   4.498   1.00 17.67 ? 236 PRO B CA  1 
ATOM   3705 C  C   . PRO B 1 201 ? -23.046 3.990   5.676   1.00 20.52 ? 236 PRO B C   1 
ATOM   3706 O  O   . PRO B 1 201 ? -24.048 4.616   6.043   1.00 17.78 ? 236 PRO B O   1 
ATOM   3707 C  CB  . PRO B 1 201 ? -22.733 3.909   3.174   1.00 24.70 ? 236 PRO B CB  1 
ATOM   3708 C  CG  . PRO B 1 201 ? -21.510 3.962   2.292   1.00 19.17 ? 236 PRO B CG  1 
ATOM   3709 C  CD  . PRO B 1 201 ? -20.407 3.534   3.218   1.00 17.57 ? 236 PRO B CD  1 
ATOM   3710 N  N   . GLY B 1 202 ? -22.671 2.853   6.257   1.00 16.28 ? 237 GLY B N   1 
ATOM   3711 C  CA  . GLY B 1 202 ? -23.405 2.287   7.380   1.00 16.15 ? 237 GLY B CA  1 
ATOM   3712 C  C   . GLY B 1 202 ? -22.645 2.177   8.691   1.00 19.44 ? 237 GLY B C   1 
ATOM   3713 O  O   . GLY B 1 202 ? -23.053 1.415   9.581   1.00 15.33 ? 237 GLY B O   1 
ATOM   3714 N  N   . HIS B 1 203 ? -21.563 2.960   8.836   1.00 18.02 ? 238 HIS B N   1 
ATOM   3715 C  CA  . HIS B 1 203 ? -20.695 2.844   10.002  1.00 14.58 ? 238 HIS B CA  1 
ATOM   3716 C  C   . HIS B 1 203 ? -21.486 3.027   11.293  1.00 17.40 ? 238 HIS B C   1 
ATOM   3717 O  O   . HIS B 1 203 ? -22.285 3.966   11.425  1.00 16.63 ? 238 HIS B O   1 
ATOM   3718 C  CB  . HIS B 1 203 ? -19.555 3.878   9.964   1.00 13.53 ? 238 HIS B CB  1 
ATOM   3719 C  CG  . HIS B 1 203 ? -18.612 3.736   11.111  1.00 13.12 ? 238 HIS B CG  1 
ATOM   3720 N  ND1 . HIS B 1 203 ? -18.869 4.286   12.347  1.00 13.32 ? 238 HIS B ND1 1 
ATOM   3721 C  CD2 . HIS B 1 203 ? -17.383 3.150   11.204  1.00 12.68 ? 238 HIS B CD2 1 
ATOM   3722 C  CE1 . HIS B 1 203 ? -17.868 4.003   13.171  1.00 13.81 ? 238 HIS B CE1 1 
ATOM   3723 N  NE2 . HIS B 1 203 ? -16.957 3.306   12.503  1.00 13.20 ? 238 HIS B NE2 1 
ATOM   3724 N  N   . THR B 1 204 ? -21.253 2.119   12.248  1.00 15.49 ? 239 THR B N   1 
ATOM   3725 C  CA  . THR B 1 204 ? -22.077 2.028   13.438  1.00 15.07 ? 239 THR B CA  1 
ATOM   3726 C  C   . THR B 1 204 ? -21.276 1.979   14.723  1.00 13.90 ? 239 THR B C   1 
ATOM   3727 O  O   . THR B 1 204 ? -20.289 1.253   14.816  1.00 15.54 ? 239 THR B O   1 
ATOM   3728 C  CB  . THR B 1 204 ? -23.042 0.828   13.354  1.00 18.58 ? 239 THR B CB  1 
ATOM   3729 O  OG1 . THR B 1 204 ? -23.867 0.995   12.193  1.00 14.72 ? 239 THR B OG1 1 
ATOM   3730 C  CG2 . THR B 1 204 ? -24.000 0.820   14.561  1.00 15.09 ? 239 THR B CG2 1 
ATOM   3731 N  N   . THR B 1 205 ? -21.708 2.764   15.709  1.00 16.81 ? 240 THR B N   1 
ATOM   3732 C  CA  . THR B 1 205 ? -21.149 2.716   17.056  1.00 19.10 ? 240 THR B CA  1 
ATOM   3733 C  C   . THR B 1 205 ? -21.978 1.782   17.920  1.00 18.01 ? 240 THR B C   1 
ATOM   3734 O  O   . THR B 1 205 ? -23.195 1.721   17.776  1.00 20.54 ? 240 THR B O   1 
ATOM   3735 C  CB  . THR B 1 205 ? -21.114 4.134   17.650  1.00 17.39 ? 240 THR B CB  1 
ATOM   3736 O  OG1 . THR B 1 205 ? -20.194 4.937   16.900  1.00 20.27 ? 240 THR B OG1 1 
ATOM   3737 C  CG2 . THR B 1 205 ? -20.675 4.150   19.162  1.00 15.40 ? 240 THR B CG2 1 
ATOM   3738 N  N   . TYR B 1 206 ? -21.336 1.017   18.791  1.00 18.75 ? 241 TYR B N   1 
ATOM   3739 C  CA  . TYR B 1 206 ? -22.082 0.076   19.640  1.00 18.35 ? 241 TYR B CA  1 
ATOM   3740 C  C   . TYR B 1 206 ? -21.961 0.531   21.086  1.00 19.29 ? 241 TYR B C   1 
ATOM   3741 O  O   . TYR B 1 206 ? -20.857 0.703   21.601  1.00 17.69 ? 241 TYR B O   1 
ATOM   3742 C  CB  . TYR B 1 206 ? -21.595 -1.363  19.445  1.00 16.34 ? 241 TYR B CB  1 
ATOM   3743 C  CG  . TYR B 1 206 ? -21.978 -1.859  18.083  1.00 15.09 ? 241 TYR B CG  1 
ATOM   3744 C  CD1 . TYR B 1 206 ? -23.301 -2.288  17.814  1.00 21.66 ? 241 TYR B CD1 1 
ATOM   3745 C  CD2 . TYR B 1 206 ? -21.074 -1.802  17.022  1.00 17.51 ? 241 TYR B CD2 1 
ATOM   3746 C  CE1 . TYR B 1 206 ? -23.659 -2.700  16.543  1.00 15.38 ? 241 TYR B CE1 1 
ATOM   3747 C  CE2 . TYR B 1 206 ? -21.446 -2.204  15.752  1.00 14.01 ? 241 TYR B CE2 1 
ATOM   3748 C  CZ  . TYR B 1 206 ? -22.737 -2.635  15.522  1.00 14.59 ? 241 TYR B CZ  1 
ATOM   3749 O  OH  . TYR B 1 206 ? -23.059 -3.038  14.248  1.00 16.46 ? 241 TYR B OH  1 
ATOM   3750 N  N   . VAL B 1 207 ? -23.084 0.778   21.739  1.00 23.06 ? 242 VAL B N   1 
ATOM   3751 C  CA  . VAL B 1 207 ? -23.050 1.408   23.049  1.00 22.30 ? 242 VAL B CA  1 
ATOM   3752 C  C   . VAL B 1 207 ? -23.460 0.365   24.064  1.00 23.44 ? 242 VAL B C   1 
ATOM   3753 O  O   . VAL B 1 207 ? -24.584 -0.154  24.007  1.00 20.64 ? 242 VAL B O   1 
ATOM   3754 C  CB  . VAL B 1 207 ? -23.958 2.644   23.129  1.00 22.39 ? 242 VAL B CB  1 
ATOM   3755 C  CG1 . VAL B 1 207 ? -23.865 3.292   24.534  1.00 22.92 ? 242 VAL B CG1 1 
ATOM   3756 C  CG2 . VAL B 1 207 ? -23.634 3.637   22.050  1.00 22.70 ? 242 VAL B CG2 1 
ATOM   3757 N  N   . VAL B 1 208 ? -22.559 0.093   25.003  1.00 21.35 ? 243 VAL B N   1 
ATOM   3758 C  CA  . VAL B 1 208 ? -22.705 -0.935  26.019  1.00 22.94 ? 243 VAL B CA  1 
ATOM   3759 C  C   . VAL B 1 208 ? -23.028 -0.248  27.337  1.00 21.47 ? 243 VAL B C   1 
ATOM   3760 O  O   . VAL B 1 208 ? -22.324 0.682   27.744  1.00 23.81 ? 243 VAL B O   1 
ATOM   3761 C  CB  . VAL B 1 208 ? -21.415 -1.772  26.138  1.00 23.73 ? 243 VAL B CB  1 
ATOM   3762 C  CG1 . VAL B 1 208 ? -21.600 -2.906  27.085  1.00 20.64 ? 243 VAL B CG1 1 
ATOM   3763 C  CG2 . VAL B 1 208 ? -20.951 -2.274  24.760  1.00 20.23 ? 243 VAL B CG2 1 
ATOM   3764 N  N   . GLU B 1 209 ? -24.063 -0.719  28.019  1.00 22.81 ? 244 GLU B N   1 
ATOM   3765 C  CA  . GLU B 1 209 ? -24.516 -0.051  29.228  1.00 24.35 ? 244 GLU B CA  1 
ATOM   3766 C  C   . GLU B 1 209 ? -24.942 -1.093  30.250  1.00 26.68 ? 244 GLU B C   1 
ATOM   3767 O  O   . GLU B 1 209 ? -25.768 -1.971  29.949  1.00 26.13 ? 244 GLU B O   1 
ATOM   3768 C  CB  . GLU B 1 209 ? -25.680 0.889   28.908  1.00 30.39 ? 244 GLU B CB  1 
ATOM   3769 C  CG  . GLU B 1 209 ? -25.240 2.195   28.246  1.00 30.68 ? 244 GLU B CG  1 
ATOM   3770 C  CD  . GLU B 1 209 ? -26.341 3.248   28.185  1.00 35.62 ? 244 GLU B CD  1 
ATOM   3771 O  OE1 . GLU B 1 209 ? -27.118 3.239   27.203  1.00 43.29 ? 244 GLU B OE1 1 
ATOM   3772 O  OE2 . GLU B 1 209 ? -26.473 4.039   29.138  1.00 35.60 ? 244 GLU B OE2 1 
ATOM   3773 N  N   . SER B 1 210 ? -24.391 -0.978  31.457  1.00 26.66 ? 245 SER B N   1 
ATOM   3774 C  CA  . SER B 1 210 ? -24.779 -1.876  32.543  1.00 28.31 ? 245 SER B CA  1 
ATOM   3775 C  C   . SER B 1 210 ? -24.645 -1.153  33.872  1.00 30.29 ? 245 SER B C   1 
ATOM   3776 O  O   . SER B 1 210 ? -23.562 -0.655  34.193  1.00 29.35 ? 245 SER B O   1 
ATOM   3777 C  CB  . SER B 1 210 ? -23.929 -3.152  32.550  1.00 29.20 ? 245 SER B CB  1 
ATOM   3778 O  OG  . SER B 1 210 ? -24.247 -3.952  33.686  1.00 34.94 ? 245 SER B OG  1 
ATOM   3779 N  N   . GLN B 1 211 ? -25.743 -1.134  34.643  1.00 31.70 ? 246 GLN B N   1 
ATOM   3780 C  CA  . GLN B 1 211 ? -25.787 -0.547  35.990  1.00 33.55 ? 246 GLN B CA  1 
ATOM   3781 C  C   . GLN B 1 211 ? -25.314 0.909   35.988  1.00 33.12 ? 246 GLN B C   1 
ATOM   3782 O  O   . GLN B 1 211 ? -24.652 1.368   36.923  1.00 35.23 ? 246 GLN B O   1 
ATOM   3783 C  CB  . GLN B 1 211 ? -24.985 -1.387  36.990  1.00 34.36 ? 246 GLN B CB  1 
ATOM   3784 C  CG  . GLN B 1 211 ? -25.422 -2.843  37.106  1.00 35.90 ? 246 GLN B CG  1 
ATOM   3785 C  CD  . GLN B 1 211 ? -26.775 -3.011  37.772  1.00 51.43 ? 246 GLN B CD  1 
ATOM   3786 O  OE1 . GLN B 1 211 ? -27.141 -2.247  38.669  1.00 49.18 ? 246 GLN B OE1 1 
ATOM   3787 N  NE2 . GLN B 1 211 ? -27.530 -4.022  37.335  1.00 49.56 ? 246 GLN B NE2 1 
ATOM   3788 N  N   . GLY B 1 212 ? -25.643 1.643   34.921  1.00 31.99 ? 247 GLY B N   1 
ATOM   3789 C  CA  . GLY B 1 212 ? -25.248 3.037   34.805  1.00 33.82 ? 247 GLY B CA  1 
ATOM   3790 C  C   . GLY B 1 212 ? -23.832 3.280   34.327  1.00 36.03 ? 247 GLY B C   1 
ATOM   3791 O  O   . GLY B 1 212 ? -23.376 4.432   34.353  1.00 35.77 ? 247 GLY B O   1 
ATOM   3792 N  N   . GLN B 1 213 ? -23.125 2.241   33.898  1.00 30.58 ? 248 GLN B N   1 
ATOM   3793 C  CA  . GLN B 1 213 ? -21.775 2.376   33.369  1.00 27.17 ? 248 GLN B CA  1 
ATOM   3794 C  C   . GLN B 1 213 ? -21.866 2.205   31.865  1.00 26.49 ? 248 GLN B C   1 
ATOM   3795 O  O   . GLN B 1 213 ? -22.455 1.229   31.396  1.00 27.84 ? 248 GLN B O   1 
ATOM   3796 C  CB  . GLN B 1 213 ? -20.837 1.326   33.961  1.00 32.71 ? 248 GLN B CB  1 
ATOM   3797 C  CG  . GLN B 1 213 ? -20.831 1.321   35.459  1.00 36.00 ? 248 GLN B CG  1 
ATOM   3798 C  CD  . GLN B 1 213 ? -20.123 2.532   35.999  1.00 43.68 ? 248 GLN B CD  1 
ATOM   3799 O  OE1 . GLN B 1 213 ? -18.894 2.614   35.969  1.00 54.67 ? 248 GLN B OE1 1 
ATOM   3800 N  NE2 . GLN B 1 213 ? -20.895 3.497   36.475  1.00 53.16 ? 248 GLN B NE2 1 
ATOM   3801 N  N   . LYS B 1 214 ? -21.317 3.167   31.124  1.00 24.96 ? 249 LYS B N   1 
ATOM   3802 C  CA  . LYS B 1 214 ? -21.426 3.249   29.672  1.00 23.30 ? 249 LYS B CA  1 
ATOM   3803 C  C   . LYS B 1 214 ? -20.066 3.109   28.998  1.00 26.08 ? 249 LYS B C   1 
ATOM   3804 O  O   . LYS B 1 214 ? -19.061 3.634   29.492  1.00 27.53 ? 249 LYS B O   1 
ATOM   3805 C  CB  . LYS B 1 214 ? -22.033 4.581   29.248  1.00 25.10 ? 249 LYS B CB  1 
ATOM   3806 C  CG  . LYS B 1 214 ? -22.612 4.571   27.862  1.00 31.83 ? 249 LYS B CG  1 
ATOM   3807 C  CD  . LYS B 1 214 ? -22.961 5.982   27.397  1.00 31.66 ? 249 LYS B CD  1 
ATOM   3808 C  CE  . LYS B 1 214 ? -24.101 6.562   28.185  1.00 39.80 ? 249 LYS B CE  1 
ATOM   3809 N  NZ  . LYS B 1 214 ? -25.367 6.217   27.528  1.00 42.24 ? 249 LYS B NZ  1 
ATOM   3810 N  N   . LEU B 1 215 ? -20.068 2.439   27.844  1.00 22.13 ? 250 LEU B N   1 
ATOM   3811 C  CA  . LEU B 1 215 ? -18.888 2.239   27.000  1.00 21.71 ? 250 LEU B CA  1 
ATOM   3812 C  C   . LEU B 1 215 ? -19.326 2.378   25.550  1.00 21.78 ? 250 LEU B C   1 
ATOM   3813 O  O   . LEU B 1 215 ? -20.147 1.589   25.075  1.00 22.08 ? 250 LEU B O   1 
ATOM   3814 C  CB  . LEU B 1 215 ? -18.258 0.852   27.227  1.00 21.84 ? 250 LEU B CB  1 
ATOM   3815 C  CG  . LEU B 1 215 ? -17.180 0.443   26.220  1.00 17.75 ? 250 LEU B CG  1 
ATOM   3816 C  CD1 . LEU B 1 215 ? -15.994 1.466   26.278  1.00 18.15 ? 250 LEU B CD1 1 
ATOM   3817 C  CD2 . LEU B 1 215 ? -16.696 -0.992  26.407  1.00 21.34 ? 250 LEU B CD2 1 
ATOM   3818 N  N   . ALA B 1 216 ? -18.795 3.364   24.831  1.00 22.36 ? 251 ALA B N   1 
ATOM   3819 C  CA  . ALA B 1 216 ? -19.154 3.555   23.425  1.00 21.78 ? 251 ALA B CA  1 
ATOM   3820 C  C   . ALA B 1 216 ? -18.039 2.979   22.552  1.00 17.99 ? 251 ALA B C   1 
ATOM   3821 O  O   . ALA B 1 216 ? -16.905 3.486   22.575  1.00 18.14 ? 251 ALA B O   1 
ATOM   3822 C  CB  . ALA B 1 216 ? -19.409 5.031   23.115  1.00 20.78 ? 251 ALA B CB  1 
ATOM   3823 N  N   . LEU B 1 217 ? -18.349 1.913   21.796  1.00 15.29 ? 252 LEU B N   1 
ATOM   3824 C  CA  . LEU B 1 217 ? -17.382 1.286   20.883  1.00 17.06 ? 252 LEU B CA  1 
ATOM   3825 C  C   . LEU B 1 217 ? -17.518 2.000   19.542  1.00 14.68 ? 252 LEU B C   1 
ATOM   3826 O  O   . LEU B 1 217 ? -18.486 1.785   18.816  1.00 17.23 ? 252 LEU B O   1 
ATOM   3827 C  CB  . LEU B 1 217 ? -17.611 -0.225  20.735  1.00 20.24 ? 252 LEU B CB  1 
ATOM   3828 C  CG  . LEU B 1 217 ? -17.664 -1.066  22.003  1.00 16.57 ? 252 LEU B CG  1 
ATOM   3829 C  CD1 . LEU B 1 217 ? -17.963 -2.509  21.646  1.00 20.82 ? 252 LEU B CD1 1 
ATOM   3830 C  CD2 . LEU B 1 217 ? -16.348 -0.936  22.791  1.00 22.05 ? 252 LEU B CD2 1 
ATOM   3831 N  N   . LEU B 1 218 ? -16.565 2.900   19.255  1.00 17.03 ? 253 LEU B N   1 
ATOM   3832 C  CA  . LEU B 1 218 ? -16.642 3.856   18.161  1.00 16.83 ? 253 LEU B CA  1 
ATOM   3833 C  C   . LEU B 1 218 ? -16.157 3.300   16.822  1.00 16.23 ? 253 LEU B C   1 
ATOM   3834 O  O   . LEU B 1 218 ? -16.280 4.005   15.814  1.00 17.03 ? 253 LEU B O   1 
ATOM   3835 C  CB  . LEU B 1 218 ? -15.839 5.132   18.493  1.00 17.12 ? 253 LEU B CB  1 
ATOM   3836 C  CG  . LEU B 1 218 ? -16.095 5.817   19.839  1.00 17.72 ? 253 LEU B CG  1 
ATOM   3837 C  CD1 . LEU B 1 218 ? -15.254 7.085   19.928  1.00 17.91 ? 253 LEU B CD1 1 
ATOM   3838 C  CD2 . LEU B 1 218 ? -17.582 6.207   20.034  1.00 19.56 ? 253 LEU B CD2 1 
ATOM   3839 N  N   . GLY B 1 219 ? -15.683 2.056   16.763  1.00 16.41 ? 254 GLY B N   1 
ATOM   3840 C  CA  . GLY B 1 219 ? -15.216 1.525   15.487  1.00 15.65 ? 254 GLY B CA  1 
ATOM   3841 C  C   . GLY B 1 219 ? -14.126 2.427   14.919  1.00 18.34 ? 254 GLY B C   1 
ATOM   3842 O  O   . GLY B 1 219 ? -13.125 2.693   15.574  1.00 16.58 ? 254 GLY B O   1 
ATOM   3843 N  N   . ASP B 1 220 ? -14.316 2.926   13.696  1.00 15.37 ? 255 ASP B N   1 
ATOM   3844 C  CA  . ASP B 1 220 ? -13.317 3.749   13.026  1.00 15.27 ? 255 ASP B CA  1 
ATOM   3845 C  C   . ASP B 1 220 ? -13.717 5.229   13.003  1.00 15.55 ? 255 ASP B C   1 
ATOM   3846 O  O   . ASP B 1 220 ? -13.363 5.952   12.078  1.00 15.68 ? 255 ASP B O   1 
ATOM   3847 C  CB  . ASP B 1 220 ? -13.053 3.217   11.615  1.00 15.30 ? 255 ASP B CB  1 
ATOM   3848 C  CG  . ASP B 1 220 ? -12.042 2.042   11.624  1.00 15.22 ? 255 ASP B CG  1 
ATOM   3849 O  OD1 . ASP B 1 220 ? -11.700 1.645   12.746  1.00 15.11 ? 255 ASP B OD1 1 
ATOM   3850 O  OD2 . ASP B 1 220 ? -11.641 1.547   10.555  1.00 15.42 ? 255 ASP B OD2 1 
ATOM   3851 N  N   . LEU B 1 221 ? -14.442 5.697   14.021  1.00 17.82 ? 256 LEU B N   1 
ATOM   3852 C  CA  . LEU B 1 221 ? -14.697 7.135   14.101  1.00 24.42 ? 256 LEU B CA  1 
ATOM   3853 C  C   . LEU B 1 221 ? -13.441 7.948   14.286  1.00 26.46 ? 256 LEU B C   1 
ATOM   3854 O  O   . LEU B 1 221 ? -13.452 9.156   14.001  1.00 32.18 ? 256 LEU B O   1 
ATOM   3855 C  CB  . LEU B 1 221 ? -15.668 7.513   15.215  1.00 22.10 ? 256 LEU B CB  1 
ATOM   3856 C  CG  . LEU B 1 221 ? -17.138 7.497   14.826  1.00 29.38 ? 256 LEU B CG  1 
ATOM   3857 C  CD1 . LEU B 1 221 ? -18.079 7.823   15.983  1.00 27.27 ? 256 LEU B CD1 1 
ATOM   3858 C  CD2 . LEU B 1 221 ? -17.334 8.538   13.701  1.00 21.27 ? 256 LEU B CD2 1 
ATOM   3859 N  N   . ILE B 1 222 ? -12.377 7.339   14.782  1.00 21.04 ? 257 ILE B N   1 
ATOM   3860 C  CA  . ILE B 1 222 ? -11.064 7.962   14.834  1.00 21.53 ? 257 ILE B CA  1 
ATOM   3861 C  C   . ILE B 1 222 ? -10.040 6.933   14.384  1.00 26.70 ? 257 ILE B C   1 
ATOM   3862 O  O   . ILE B 1 222 ? -10.145 5.753   14.722  1.00 26.96 ? 257 ILE B O   1 
ATOM   3863 C  CB  . ILE B 1 222 ? -10.744 8.524   16.237  1.00 24.58 ? 257 ILE B CB  1 
ATOM   3864 C  CG1 . ILE B 1 222 ? -9.476  9.377   16.163  1.00 22.62 ? 257 ILE B CG1 1 
ATOM   3865 C  CG2 . ILE B 1 222 ? -10.655 7.418   17.294  1.00 31.55 ? 257 ILE B CG2 1 
ATOM   3866 C  CD1 . ILE B 1 222 ? -9.130  10.081  17.474  1.00 29.70 ? 257 ILE B CD1 1 
ATOM   3867 N  N   . LEU B 1 223 ? -9.083  7.371   13.572  1.00 21.91 ? 258 LEU B N   1 
ATOM   3868 C  CA  . LEU B 1 223 ? -8.105  6.481   12.973  1.00 21.75 ? 258 LEU B CA  1 
ATOM   3869 C  C   . LEU B 1 223 ? -6.692  6.764   13.433  1.00 25.09 ? 258 LEU B C   1 
ATOM   3870 O  O   . LEU B 1 223 ? -5.881  5.843   13.512  1.00 20.64 ? 258 LEU B O   1 
ATOM   3871 C  CB  . LEU B 1 223 ? -8.184  6.580   11.436  1.00 21.30 ? 258 LEU B CB  1 
ATOM   3872 C  CG  . LEU B 1 223 ? -9.528  6.128   10.829  1.00 25.89 ? 258 LEU B CG  1 
ATOM   3873 C  CD1 . LEU B 1 223 ? -9.684  6.486   9.323   1.00 23.28 ? 258 LEU B CD1 1 
ATOM   3874 C  CD2 . LEU B 1 223 ? -9.759  4.624   11.092  1.00 20.29 ? 258 LEU B CD2 1 
ATOM   3875 N  N   . VAL B 1 224 ? -6.372  8.018   13.747  1.00 17.54 ? 259 VAL B N   1 
ATOM   3876 C  CA  . VAL B 1 224 ? -5.014  8.419   14.096  1.00 16.56 ? 259 VAL B CA  1 
ATOM   3877 C  C   . VAL B 1 224 ? -5.127  9.317   15.315  1.00 25.74 ? 259 VAL B C   1 
ATOM   3878 O  O   . VAL B 1 224 ? -5.377  10.523  15.182  1.00 18.85 ? 259 VAL B O   1 
ATOM   3879 C  CB  . VAL B 1 224 ? -4.323  9.134   12.932  1.00 22.18 ? 259 VAL B CB  1 
ATOM   3880 C  CG1 . VAL B 1 224 ? -2.876  9.485   13.266  1.00 20.86 ? 259 VAL B CG1 1 
ATOM   3881 C  CG2 . VAL B 1 224 ? -4.351  8.195   11.762  1.00 17.77 ? 259 VAL B CG2 1 
ATOM   3882 N  N   . ALA B 1 225 ? -4.946  8.730   16.499  1.00 18.74 ? 260 ALA B N   1 
ATOM   3883 C  CA  . ALA B 1 225 ? -5.105  9.476   17.751  1.00 17.26 ? 260 ALA B CA  1 
ATOM   3884 C  C   . ALA B 1 225 ? -4.205  10.706  17.818  1.00 26.04 ? 260 ALA B C   1 
ATOM   3885 O  O   . ALA B 1 225 ? -4.621  11.764  18.317  1.00 21.54 ? 260 ALA B O   1 
ATOM   3886 C  CB  . ALA B 1 225 ? -4.820  8.540   18.927  1.00 24.25 ? 260 ALA B CB  1 
ATOM   3887 N  N   . ALA B 1 226 ? -2.962  10.587  17.356  1.00 22.80 ? 261 ALA B N   1 
ATOM   3888 C  CA  . ALA B 1 226 ? -2.025  11.697  17.495  1.00 27.47 ? 261 ALA B CA  1 
ATOM   3889 C  C   . ALA B 1 226 ? -2.406  12.910  16.640  1.00 26.54 ? 261 ALA B C   1 
ATOM   3890 O  O   . ALA B 1 226 ? -1.787  13.966  16.782  1.00 32.37 ? 261 ALA B O   1 
ATOM   3891 C  CB  . ALA B 1 226 ? -0.611  11.205  17.174  1.00 27.34 ? 261 ALA B CB  1 
ATOM   3892 N  N   . VAL B 1 227 ? -3.407  12.793  15.765  1.00 26.35 ? 262 VAL B N   1 
ATOM   3893 C  CA  . VAL B 1 227 ? -3.869  13.898  14.925  1.00 25.55 ? 262 VAL B CA  1 
ATOM   3894 C  C   . VAL B 1 227 ? -5.294  14.311  15.273  1.00 28.73 ? 262 VAL B C   1 
ATOM   3895 O  O   . VAL B 1 227 ? -5.571  15.496  15.494  1.00 24.71 ? 262 VAL B O   1 
ATOM   3896 C  CB  . VAL B 1 227 ? -3.744  13.543  13.425  1.00 25.78 ? 262 VAL B CB  1 
ATOM   3897 C  CG1 . VAL B 1 227 ? -4.171  14.694  12.546  1.00 29.57 ? 262 VAL B CG1 1 
ATOM   3898 C  CG2 . VAL B 1 227 ? -2.307  13.260  13.101  1.00 20.56 ? 262 VAL B CG2 1 
ATOM   3899 N  N   . GLN B 1 228 ? -6.196  13.335  15.372  1.00 21.61 ? 263 GLN B N   1 
ATOM   3900 C  CA  . GLN B 1 228 ? -7.634  13.548  15.351  1.00 24.74 ? 263 GLN B CA  1 
ATOM   3901 C  C   . GLN B 1 228 ? -8.256  13.780  16.726  1.00 23.72 ? 263 GLN B C   1 
ATOM   3902 O  O   . GLN B 1 228 ? -9.431  14.177  16.794  1.00 19.87 ? 263 GLN B O   1 
ATOM   3903 C  CB  . GLN B 1 228 ? -8.282  12.349  14.638  1.00 20.21 ? 263 GLN B CB  1 
ATOM   3904 C  CG  . GLN B 1 228 ? -7.814  12.220  13.169  1.00 18.75 ? 263 GLN B CG  1 
ATOM   3905 C  CD  . GLN B 1 228 ? -8.451  11.043  12.443  1.00 21.39 ? 263 GLN B CD  1 
ATOM   3906 O  OE1 . GLN B 1 228 ? -8.408  9.920   12.946  1.00 21.20 ? 263 GLN B OE1 1 
ATOM   3907 N  NE2 . GLN B 1 228 ? -8.942  11.265  11.222  1.00 20.91 ? 263 GLN B NE2 1 
ATOM   3908 N  N   . PHE B 1 229 ? -7.520  13.554  17.813  1.00 19.55 ? 264 PHE B N   1 
ATOM   3909 C  CA  . PHE B 1 229 ? -7.993  14.056  19.103  1.00 22.93 ? 264 PHE B CA  1 
ATOM   3910 C  C   . PHE B 1 229 ? -7.793  15.558  19.201  1.00 27.45 ? 264 PHE B C   1 
ATOM   3911 O  O   . PHE B 1 229 ? -8.717  16.301  19.550  1.00 28.71 ? 264 PHE B O   1 
ATOM   3912 C  CB  . PHE B 1 229 ? -7.279  13.343  20.251  1.00 20.19 ? 264 PHE B CB  1 
ATOM   3913 C  CG  . PHE B 1 229 ? -7.896  12.007  20.557  1.00 24.33 ? 264 PHE B CG  1 
ATOM   3914 C  CD1 . PHE B 1 229 ? -9.257  11.921  20.838  1.00 22.59 ? 264 PHE B CD1 1 
ATOM   3915 C  CD2 . PHE B 1 229 ? -7.132  10.834  20.511  1.00 19.61 ? 264 PHE B CD2 1 
ATOM   3916 C  CE1 . PHE B 1 229 ? -9.876  10.677  21.084  1.00 26.57 ? 264 PHE B CE1 1 
ATOM   3917 C  CE2 . PHE B 1 229 ? -7.732  9.568   20.773  1.00 21.89 ? 264 PHE B CE2 1 
ATOM   3918 C  CZ  . PHE B 1 229 ? -9.113  9.497   21.064  1.00 24.26 ? 264 PHE B CZ  1 
ATOM   3919 N  N   . ASP B 1 230 ? -6.593  16.023  18.874  1.00 22.00 ? 265 ASP B N   1 
ATOM   3920 C  CA  . ASP B 1 230 ? -6.341  17.459  18.848  1.00 33.15 ? 265 ASP B CA  1 
ATOM   3921 C  C   . ASP B 1 230 ? -7.156  18.154  17.759  1.00 33.11 ? 265 ASP B C   1 
ATOM   3922 O  O   . ASP B 1 230 ? -7.676  19.257  17.972  1.00 28.24 ? 265 ASP B O   1 
ATOM   3923 C  CB  . ASP B 1 230 ? -4.856  17.696  18.648  1.00 29.52 ? 265 ASP B CB  1 
ATOM   3924 C  CG  . ASP B 1 230 ? -4.061  17.369  19.884  1.00 32.56 ? 265 ASP B CG  1 
ATOM   3925 O  OD1 . ASP B 1 230 ? -4.473  17.796  20.983  1.00 51.96 ? 265 ASP B OD1 1 
ATOM   3926 O  OD2 . ASP B 1 230 ? -3.004  16.722  19.749  1.00 50.12 ? 265 ASP B OD2 1 
ATOM   3927 N  N   . ASP B 1 231 ? -7.289  17.524  16.586  1.00 27.17 ? 266 ASP B N   1 
ATOM   3928 C  CA  . ASP B 1 231 ? -8.014  18.117  15.462  1.00 32.16 ? 266 ASP B CA  1 
ATOM   3929 C  C   . ASP B 1 231 ? -9.018  17.131  14.880  1.00 26.83 ? 266 ASP B C   1 
ATOM   3930 O  O   . ASP B 1 231 ? -8.760  16.506  13.840  1.00 22.67 ? 266 ASP B O   1 
ATOM   3931 C  CB  . ASP B 1 231 ? -7.052  18.600  14.381  1.00 32.36 ? 266 ASP B CB  1 
ATOM   3932 C  CG  . ASP B 1 231 ? -7.732  19.475  13.357  1.00 32.36 ? 266 ASP B CG  1 
ATOM   3933 O  OD1 . ASP B 1 231 ? -8.986  19.536  13.356  1.00 31.05 ? 266 ASP B OD1 1 
ATOM   3934 O  OD2 . ASP B 1 231 ? -7.022  20.094  12.543  1.00 29.59 ? 266 ASP B OD2 1 
ATOM   3935 N  N   . PRO B 1 232 ? -10.206 17.024  15.481  1.00 25.10 ? 267 PRO B N   1 
ATOM   3936 C  CA  . PRO B 1 232 ? -11.214 16.090  14.965  1.00 21.34 ? 267 PRO B CA  1 
ATOM   3937 C  C   . PRO B 1 232 ? -11.703 16.428  13.565  1.00 25.45 ? 267 PRO B C   1 
ATOM   3938 O  O   . PRO B 1 232 ? -12.494 15.656  13.012  1.00 27.79 ? 267 PRO B O   1 
ATOM   3939 C  CB  . PRO B 1 232 ? -12.353 16.209  15.984  1.00 27.42 ? 267 PRO B CB  1 
ATOM   3940 C  CG  . PRO B 1 232 ? -11.690 16.706  17.232  1.00 34.13 ? 267 PRO B CG  1 
ATOM   3941 C  CD  . PRO B 1 232 ? -10.634 17.656  16.746  1.00 23.73 ? 267 PRO B CD  1 
ATOM   3942 N  N   . SER B 1 233 ? -11.281 17.559  12.977  1.00 26.51 ? 268 SER B N   1 
ATOM   3943 C  CA  . SER B 1 233 ? -11.708 17.893  11.618  1.00 27.13 ? 268 SER B CA  1 
ATOM   3944 C  C   . SER B 1 233 ? -10.882 17.193  10.540  1.00 24.73 ? 268 SER B C   1 
ATOM   3945 O  O   . SER B 1 233 ? -11.316 17.147  9.389   1.00 24.86 ? 268 SER B O   1 
ATOM   3946 C  CB  . SER B 1 233 ? -11.648 19.408  11.354  1.00 26.02 ? 268 SER B CB  1 
ATOM   3947 O  OG  . SER B 1 233 ? -10.303 19.874  11.330  1.00 33.88 ? 268 SER B OG  1 
ATOM   3948 N  N   . VAL B 1 234 ? -9.697  16.670  10.856  1.00 22.05 ? 269 VAL B N   1 
ATOM   3949 C  CA  . VAL B 1 234 ? -8.895  16.029  9.817   1.00 21.07 ? 269 VAL B CA  1 
ATOM   3950 C  C   . VAL B 1 234 ? -9.519  14.685  9.455   1.00 20.05 ? 269 VAL B C   1 
ATOM   3951 O  O   . VAL B 1 234 ? -9.793  13.859  10.335  1.00 20.72 ? 269 VAL B O   1 
ATOM   3952 C  CB  . VAL B 1 234 ? -7.438  15.861  10.274  1.00 21.90 ? 269 VAL B CB  1 
ATOM   3953 C  CG1 . VAL B 1 234 ? -6.625  15.160  9.183   1.00 20.66 ? 269 VAL B CG1 1 
ATOM   3954 C  CG2 . VAL B 1 234 ? -6.827  17.238  10.668  1.00 22.14 ? 269 VAL B CG2 1 
ATOM   3955 N  N   . THR B 1 235 ? -9.724  14.447  8.153   1.00 20.14 ? 270 THR B N   1 
ATOM   3956 C  CA  . THR B 1 235 ? -10.286 13.185  7.672   1.00 19.75 ? 270 THR B CA  1 
ATOM   3957 C  C   . THR B 1 235 ? -9.246  12.430  6.831   1.00 25.64 ? 270 THR B C   1 
ATOM   3958 O  O   . THR B 1 235 ? -8.069  12.811  6.764   1.00 21.56 ? 270 THR B O   1 
ATOM   3959 C  CB  . THR B 1 235 ? -11.587 13.448  6.906   1.00 27.04 ? 270 THR B CB  1 
ATOM   3960 O  OG1 . THR B 1 235 ? -11.280 14.162  5.702   1.00 24.60 ? 270 THR B OG1 1 
ATOM   3961 C  CG2 . THR B 1 235 ? -12.573 14.237  7.759   1.00 20.22 ? 270 THR B CG2 1 
ATOM   3962 N  N   . THR B 1 236 ? -9.678  11.329  6.217   1.00 25.74 ? 271 THR B N   1 
ATOM   3963 C  CA  . THR B 1 236 ? -8.798  10.501  5.404   1.00 24.42 ? 271 THR B CA  1 
ATOM   3964 C  C   . THR B 1 236 ? -9.436  10.185  4.057   1.00 25.20 ? 271 THR B C   1 
ATOM   3965 O  O   . THR B 1 236 ? -10.660 10.287  3.867   1.00 22.20 ? 271 THR B O   1 
ATOM   3966 C  CB  . THR B 1 236 ? -8.427  9.182   6.112   1.00 26.23 ? 271 THR B CB  1 
ATOM   3967 O  OG1 . THR B 1 236 ? -9.558  8.286   6.110   1.00 25.09 ? 271 THR B OG1 1 
ATOM   3968 C  CG2 . THR B 1 236 ? -8.011  9.445   7.541   1.00 24.54 ? 271 THR B CG2 1 
ATOM   3969 N  N   . ASP B 1 237 ? -8.583  9.766   3.118   1.00 20.99 ? 272 ASP B N   1 
ATOM   3970 C  CA  . ASP B 1 237 ? -9.103  9.279   1.845   1.00 26.33 ? 272 ASP B CA  1 
ATOM   3971 C  C   . ASP B 1 237 ? -9.820  7.928   1.957   1.00 27.74 ? 272 ASP B C   1 
ATOM   3972 O  O   . ASP B 1 237 ? -10.324 7.424   0.948   1.00 32.10 ? 272 ASP B O   1 
ATOM   3973 C  CB  . ASP B 1 237 ? -7.975  9.201   0.824   1.00 32.35 ? 272 ASP B CB  1 
ATOM   3974 C  CG  . ASP B 1 237 ? -6.822  8.324   1.288   1.00 35.42 ? 272 ASP B CG  1 
ATOM   3975 O  OD1 . ASP B 1 237 ? -6.979  7.590   2.275   1.00 34.26 ? 272 ASP B OD1 1 
ATOM   3976 O  OD2 . ASP B 1 237 ? -5.752  8.372   0.653   1.00 48.25 ? 272 ASP B OD2 1 
ATOM   3977 N  N   . LEU B 1 238 ? -9.882  7.328   3.133   1.00 22.47 ? 273 LEU B N   1 
ATOM   3978 C  CA  . LEU B 1 238 ? -10.691 6.126   3.307   1.00 27.77 ? 273 LEU B CA  1 
ATOM   3979 C  C   . LEU B 1 238 ? -12.088 6.415   3.833   1.00 30.29 ? 273 LEU B C   1 
ATOM   3980 O  O   . LEU B 1 238 ? -12.882 5.474   3.992   1.00 28.24 ? 273 LEU B O   1 
ATOM   3981 C  CB  . LEU B 1 238 ? -10.005 5.153   4.247   1.00 22.74 ? 273 LEU B CB  1 
ATOM   3982 C  CG  . LEU B 1 238 ? -8.862  4.403   3.544   1.00 34.53 ? 273 LEU B CG  1 
ATOM   3983 C  CD1 . LEU B 1 238 ? -8.359  3.233   4.393   1.00 42.10 ? 273 LEU B CD1 1 
ATOM   3984 C  CD2 . LEU B 1 238 ? -9.223  3.984   2.107   1.00 31.16 ? 273 LEU B CD2 1 
ATOM   3985 N  N   . ASP B 1 239 ? -12.402 7.675   4.137   1.00 20.94 ? 274 ASP B N   1 
ATOM   3986 C  CA  . ASP B 1 239 ? -13.741 8.020   4.595   1.00 23.85 ? 274 ASP B CA  1 
ATOM   3987 C  C   . ASP B 1 239 ? -14.669 8.206   3.400   1.00 23.81 ? 274 ASP B C   1 
ATOM   3988 O  O   . ASP B 1 239 ? -14.354 8.964   2.476   1.00 29.56 ? 274 ASP B O   1 
ATOM   3989 C  CB  . ASP B 1 239 ? -13.712 9.294   5.450   1.00 18.70 ? 274 ASP B CB  1 
ATOM   3990 C  CG  . ASP B 1 239 ? -12.888 9.148   6.741   1.00 24.48 ? 274 ASP B CG  1 
ATOM   3991 O  OD1 . ASP B 1 239 ? -13.231 8.277   7.564   1.00 21.30 ? 274 ASP B OD1 1 
ATOM   3992 O  OD2 . ASP B 1 239 ? -11.933 9.948   6.979   1.00 31.44 ? 274 ASP B OD2 1 
ATOM   3993 N  N   . SER B 1 240 ? -15.830 7.532   3.432   1.00 22.38 ? 275 SER B N   1 
ATOM   3994 C  CA  . SER B 1 240 ? -16.805 7.667   2.353   1.00 24.94 ? 275 SER B CA  1 
ATOM   3995 C  C   . SER B 1 240 ? -17.375 9.078   2.276   1.00 26.82 ? 275 SER B C   1 
ATOM   3996 O  O   . SER B 1 240 ? -17.612 9.600   1.179   1.00 29.33 ? 275 SER B O   1 
ATOM   3997 C  CB  . SER B 1 240 ? -17.943 6.659   2.538   1.00 23.09 ? 275 SER B CB  1 
ATOM   3998 O  OG  . SER B 1 240 ? -17.434 5.332   2.658   1.00 37.13 ? 275 SER B OG  1 
ATOM   3999 N  N   . ASP B 1 241 ? -17.655 9.690   3.425   1.00 26.92 ? 276 ASP B N   1 
ATOM   4000 C  CA  . ASP B 1 241 ? -18.189 11.056  3.486   1.00 21.26 ? 276 ASP B CA  1 
ATOM   4001 C  C   . ASP B 1 241 ? -17.411 11.815  4.554   1.00 20.78 ? 276 ASP B C   1 
ATOM   4002 O  O   . ASP B 1 241 ? -17.756 11.757  5.742   1.00 21.17 ? 276 ASP B O   1 
ATOM   4003 C  CB  . ASP B 1 241 ? -19.692 11.051  3.772   1.00 26.63 ? 276 ASP B CB  1 
ATOM   4004 C  CG  . ASP B 1 241 ? -20.311 12.441  3.733   1.00 25.08 ? 276 ASP B CG  1 
ATOM   4005 O  OD1 . ASP B 1 241 ? -19.580 13.456  3.825   1.00 30.91 ? 276 ASP B OD1 1 
ATOM   4006 O  OD2 . ASP B 1 241 ? -21.550 12.524  3.637   1.00 28.81 ? 276 ASP B OD2 1 
ATOM   4007 N  N   . SER B 1 242 ? -16.391 12.556  4.099   1.00 23.99 ? 277 SER B N   1 
ATOM   4008 C  CA  . SER B 1 242 ? -15.521 13.343  4.983   1.00 24.89 ? 277 SER B CA  1 
ATOM   4009 C  C   . SER B 1 242 ? -16.297 14.286  5.904   1.00 23.48 ? 277 SER B C   1 
ATOM   4010 O  O   . SER B 1 242 ? -16.048 14.340  7.118   1.00 24.67 ? 277 SER B O   1 
ATOM   4011 C  CB  . SER B 1 242 ? -14.536 14.157  4.148   1.00 30.83 ? 277 SER B CB  1 
ATOM   4012 O  OG  . SER B 1 242 ? -13.470 13.352  3.701   1.00 42.57 ? 277 SER B OG  1 
ATOM   4013 N  N   . LYS B 1 243 ? -17.224 15.067  5.352   1.00 31.71 ? 278 LYS B N   1 
ATOM   4014 C  CA  . LYS B 1 243 ? -17.859 16.046  6.227   1.00 29.05 ? 278 LYS B CA  1 
ATOM   4015 C  C   . LYS B 1 243 ? -18.752 15.352  7.250   1.00 27.15 ? 278 LYS B C   1 
ATOM   4016 O  O   . LYS B 1 243 ? -18.804 15.765  8.421   1.00 24.65 ? 278 LYS B O   1 
ATOM   4017 C  CB  . LYS B 1 243 ? -18.628 17.094  5.425   1.00 39.04 ? 278 LYS B CB  1 
ATOM   4018 C  CG  . LYS B 1 243 ? -19.849 17.548  6.187   1.00 55.90 ? 278 LYS B CG  1 
ATOM   4019 C  CD  . LYS B 1 243 ? -20.470 18.836  5.682   1.00 58.48 ? 278 LYS B CD  1 
ATOM   4020 C  CE  . LYS B 1 243 ? -21.979 18.671  5.720   1.00 53.05 ? 278 LYS B CE  1 
ATOM   4021 N  NZ  . LYS B 1 243 ? -22.490 18.799  7.124   1.00 54.39 ? 278 LYS B NZ  1 
ATOM   4022 N  N   . ALA B 1 244 ? -19.396 14.252  6.845   1.00 24.03 ? 279 ALA B N   1 
ATOM   4023 C  CA  . ALA B 1 244 ? -20.184 13.460  7.786   1.00 30.97 ? 279 ALA B CA  1 
ATOM   4024 C  C   . ALA B 1 244 ? -19.320 12.867  8.882   1.00 26.36 ? 279 ALA B C   1 
ATOM   4025 O  O   . ALA B 1 244 ? -19.724 12.825  10.052  1.00 23.82 ? 279 ALA B O   1 
ATOM   4026 C  CB  . ALA B 1 244 ? -20.911 12.329  7.063   1.00 23.84 ? 279 ALA B CB  1 
ATOM   4027 N  N   . VAL B 1 245 ? -18.155 12.332  8.518   1.00 24.35 ? 280 VAL B N   1 
ATOM   4028 C  CA  . VAL B 1 245 ? -17.348 11.711  9.546   1.00 24.60 ? 280 VAL B CA  1 
ATOM   4029 C  C   . VAL B 1 245 ? -16.858 12.768  10.526  1.00 21.85 ? 280 VAL B C   1 
ATOM   4030 O  O   . VAL B 1 245 ? -16.829 12.524  11.732  1.00 21.20 ? 280 VAL B O   1 
ATOM   4031 C  CB  . VAL B 1 245 ? -16.206 10.867  8.932   1.00 23.81 ? 280 VAL B CB  1 
ATOM   4032 C  CG1 . VAL B 1 245 ? -15.005 11.689  8.626   1.00 25.33 ? 280 VAL B CG1 1 
ATOM   4033 C  CG2 . VAL B 1 245 ? -15.843 9.765   9.889   1.00 23.61 ? 280 VAL B CG2 1 
ATOM   4034 N  N   . ALA B 1 246 ? -16.536 13.981  10.045  1.00 21.71 ? 281 ALA B N   1 
ATOM   4035 C  CA  . ALA B 1 246 ? -16.087 15.022  10.971  1.00 24.77 ? 281 ALA B CA  1 
ATOM   4036 C  C   . ALA B 1 246 ? -17.208 15.421  11.926  1.00 29.23 ? 281 ALA B C   1 
ATOM   4037 O  O   . ALA B 1 246 ? -16.993 15.531  13.146  1.00 25.68 ? 281 ALA B O   1 
ATOM   4038 C  CB  . ALA B 1 246 ? -15.560 16.225  10.194  1.00 25.93 ? 281 ALA B CB  1 
ATOM   4039 N  N   . VAL B 1 247 ? -18.431 15.568  11.399  1.00 24.48 ? 282 VAL B N   1 
ATOM   4040 C  CA  . VAL B 1 247 ? -19.582 15.842  12.258  1.00 29.78 ? 282 VAL B CA  1 
ATOM   4041 C  C   . VAL B 1 247 ? -19.761 14.732  13.300  1.00 28.58 ? 282 VAL B C   1 
ATOM   4042 O  O   . VAL B 1 247 ? -19.834 15.003  14.506  1.00 27.27 ? 282 VAL B O   1 
ATOM   4043 C  CB  . VAL B 1 247 ? -20.856 16.021  11.410  1.00 25.30 ? 282 VAL B CB  1 
ATOM   4044 C  CG1 . VAL B 1 247 ? -22.084 15.979  12.304  1.00 29.96 ? 282 VAL B CG1 1 
ATOM   4045 C  CG2 . VAL B 1 247 ? -20.798 17.327  10.623  1.00 36.70 ? 282 VAL B CG2 1 
ATOM   4046 N  N   . GLU B 1 248 ? -19.814 13.467  12.859  1.00 22.19 ? 283 GLU B N   1 
ATOM   4047 C  CA  . GLU B 1 248 ? -20.082 12.370  13.804  1.00 26.44 ? 283 GLU B CA  1 
ATOM   4048 C  C   . GLU B 1 248 ? -18.937 12.188  14.807  1.00 26.46 ? 283 GLU B C   1 
ATOM   4049 O  O   . GLU B 1 248 ? -19.178 11.865  15.985  1.00 21.70 ? 283 GLU B O   1 
ATOM   4050 C  CB  . GLU B 1 248 ? -20.355 11.057  13.052  1.00 24.29 ? 283 GLU B CB  1 
ATOM   4051 C  CG  . GLU B 1 248 ? -21.660 11.066  12.312  1.00 23.24 ? 283 GLU B CG  1 
ATOM   4052 C  CD  . GLU B 1 248 ? -22.809 11.351  13.238  1.00 36.55 ? 283 GLU B CD  1 
ATOM   4053 O  OE1 . GLU B 1 248 ? -22.835 10.736  14.331  1.00 36.23 ? 283 GLU B OE1 1 
ATOM   4054 O  OE2 . GLU B 1 248 ? -23.629 12.243  12.905  1.00 35.07 ? 283 GLU B OE2 1 
ATOM   4055 N  N   . ARG B 1 249 ? -17.697 12.437  14.387  1.00 24.73 ? 284 ARG B N   1 
ATOM   4056 C  CA  . ARG B 1 249 ? -16.586 12.354  15.327  1.00 22.40 ? 284 ARG B CA  1 
ATOM   4057 C  C   . ARG B 1 249 ? -16.723 13.411  16.411  1.00 27.17 ? 284 ARG B C   1 
ATOM   4058 O  O   . ARG B 1 249 ? -16.654 13.085  17.605  1.00 20.55 ? 284 ARG B O   1 
ATOM   4059 C  CB  . ARG B 1 249 ? -15.247 12.491  14.615  1.00 23.51 ? 284 ARG B CB  1 
ATOM   4060 C  CG  . ARG B 1 249 ? -14.040 12.588  15.601  1.00 20.72 ? 284 ARG B CG  1 
ATOM   4061 C  CD  . ARG B 1 249 ? -12.747 12.700  14.852  1.00 24.28 ? 284 ARG B CD  1 
ATOM   4062 N  NE  . ARG B 1 249 ? -12.668 11.623  13.893  1.00 29.41 ? 284 ARG B NE  1 
ATOM   4063 C  CZ  . ARG B 1 249 ? -12.198 11.726  12.663  1.00 30.87 ? 284 ARG B CZ  1 
ATOM   4064 N  NH1 . ARG B 1 249 ? -11.848 12.898  12.150  1.00 25.76 ? 284 ARG B NH1 1 
ATOM   4065 N  NH2 . ARG B 1 249 ? -12.068 10.622  11.930  1.00 19.96 ? 284 ARG B NH2 1 
ATOM   4066 N  N   . LYS B 1 250 ? -16.918 14.685  16.010  1.00 24.21 ? 285 LYS B N   1 
ATOM   4067 C  CA  . LYS B 1 250 ? -17.061 15.759  16.989  1.00 24.56 ? 285 LYS B CA  1 
ATOM   4068 C  C   . LYS B 1 250 ? -18.251 15.496  17.907  1.00 31.81 ? 285 LYS B C   1 
ATOM   4069 O  O   . LYS B 1 250 ? -18.185 15.754  19.117  1.00 26.48 ? 285 LYS B O   1 
ATOM   4070 C  CB  . LYS B 1 250 ? -17.208 17.106  16.275  1.00 39.05 ? 285 LYS B CB  1 
ATOM   4071 C  CG  . LYS B 1 250 ? -16.041 17.430  15.347  1.00 41.58 ? 285 LYS B CG  1 
ATOM   4072 C  CD  . LYS B 1 250 ? -16.053 18.871  14.829  1.00 47.79 ? 285 LYS B CD  1 
ATOM   4073 C  CE  . LYS B 1 250 ? -14.880 19.106  13.885  1.00 38.83 ? 285 LYS B CE  1 
ATOM   4074 N  NZ  . LYS B 1 250 ? -15.336 19.582  12.531  1.00 38.86 ? 285 LYS B NZ  1 
ATOM   4075 N  N   . LYS B 1 251 ? -19.336 14.938  17.355  1.00 29.16 ? 286 LYS B N   1 
ATOM   4076 C  CA  . LYS B 1 251 ? -20.492 14.580  18.169  1.00 31.27 ? 286 LYS B CA  1 
ATOM   4077 C  C   . LYS B 1 251 ? -20.111 13.581  19.252  1.00 26.70 ? 286 LYS B C   1 
ATOM   4078 O  O   . LYS B 1 251 ? -20.419 13.785  20.436  1.00 26.58 ? 286 LYS B O   1 
ATOM   4079 C  CB  . LYS B 1 251 ? -21.601 14.030  17.267  1.00 24.16 ? 286 LYS B CB  1 
ATOM   4080 C  CG  . LYS B 1 251 ? -22.955 13.833  17.913  1.00 37.37 ? 286 LYS B CG  1 
ATOM   4081 C  CD  . LYS B 1 251 ? -23.910 13.185  16.910  1.00 33.21 ? 286 LYS B CD  1 
ATOM   4082 C  CE  . LYS B 1 251 ? -24.259 14.199  15.814  1.00 38.34 ? 286 LYS B CE  1 
ATOM   4083 N  NZ  . LYS B 1 251 ? -25.229 13.719  14.789  1.00 38.02 ? 286 LYS B NZ  1 
ATOM   4084 N  N   . ALA B 1 252 ? -19.425 12.499  18.869  1.00 26.56 ? 287 ALA B N   1 
ATOM   4085 C  CA  . ALA B 1 252 ? -19.106 11.455  19.839  1.00 26.61 ? 287 ALA B CA  1 
ATOM   4086 C  C   . ALA B 1 252 ? -18.104 11.958  20.873  1.00 26.68 ? 287 ALA B C   1 
ATOM   4087 O  O   . ALA B 1 252 ? -18.213 11.650  22.065  1.00 23.57 ? 287 ALA B O   1 
ATOM   4088 C  CB  . ALA B 1 252 ? -18.576 10.202  19.130  1.00 26.75 ? 287 ALA B CB  1 
ATOM   4089 N  N   . PHE B 1 253 ? -17.129 12.749  20.443  1.00 23.23 ? 288 PHE B N   1 
ATOM   4090 C  CA  . PHE B 1 253 ? -16.166 13.295  21.397  1.00 25.96 ? 288 PHE B CA  1 
ATOM   4091 C  C   . PHE B 1 253 ? -16.826 14.244  22.398  1.00 29.04 ? 288 PHE B C   1 
ATOM   4092 O  O   . PHE B 1 253 ? -16.544 14.183  23.607  1.00 27.89 ? 288 PHE B O   1 
ATOM   4093 C  CB  . PHE B 1 253 ? -15.041 14.005  20.649  1.00 24.61 ? 288 PHE B CB  1 
ATOM   4094 C  CG  . PHE B 1 253 ? -14.101 13.054  19.939  1.00 25.06 ? 288 PHE B CG  1 
ATOM   4095 C  CD1 . PHE B 1 253 ? -14.326 11.688  19.978  1.00 21.59 ? 288 PHE B CD1 1 
ATOM   4096 C  CD2 . PHE B 1 253 ? -12.994 13.526  19.253  1.00 24.44 ? 288 PHE B CD2 1 
ATOM   4097 C  CE1 . PHE B 1 253 ? -13.474 10.830  19.341  1.00 26.30 ? 288 PHE B CE1 1 
ATOM   4098 C  CE2 . PHE B 1 253 ? -12.140 12.658  18.609  1.00 23.87 ? 288 PHE B CE2 1 
ATOM   4099 C  CZ  . PHE B 1 253 ? -12.380 11.303  18.662  1.00 23.33 ? 288 PHE B CZ  1 
ATOM   4100 N  N   . ALA B 1 254 ? -17.695 15.144  21.922  1.00 25.39 ? 289 ALA B N   1 
ATOM   4101 C  CA  . ALA B 1 254 ? -18.333 16.063  22.858  1.00 27.46 ? 289 ALA B CA  1 
ATOM   4102 C  C   . ALA B 1 254 ? -19.269 15.316  23.803  1.00 26.33 ? 289 ALA B C   1 
ATOM   4103 O  O   . ALA B 1 254 ? -19.285 15.585  25.013  1.00 28.78 ? 289 ALA B O   1 
ATOM   4104 C  CB  . ALA B 1 254 ? -19.069 17.180  22.105  1.00 28.81 ? 289 ALA B CB  1 
ATOM   4105 N  N   . ASP B 1 255 ? -20.020 14.343  23.291  1.00 26.80 ? 290 ASP B N   1 
ATOM   4106 C  CA  . ASP B 1 255 ? -20.928 13.608  24.168  1.00 33.27 ? 290 ASP B CA  1 
ATOM   4107 C  C   . ASP B 1 255 ? -20.168 12.790  25.209  1.00 26.78 ? 290 ASP B C   1 
ATOM   4108 O  O   . ASP B 1 255 ? -20.572 12.746  26.381  1.00 28.66 ? 290 ASP B O   1 
ATOM   4109 C  CB  . ASP B 1 255 ? -21.858 12.718  23.344  1.00 27.98 ? 290 ASP B CB  1 
ATOM   4110 C  CG  . ASP B 1 255 ? -22.996 12.157  24.166  1.00 27.12 ? 290 ASP B CG  1 
ATOM   4111 O  OD1 . ASP B 1 255 ? -23.989 12.870  24.340  1.00 32.91 ? 290 ASP B OD1 1 
ATOM   4112 O  OD2 . ASP B 1 255 ? -22.914 10.996  24.630  1.00 34.57 ? 290 ASP B OD2 1 
ATOM   4113 N  N   . ALA B 1 256 ? -19.045 12.167  24.816  1.00 27.01 ? 291 ALA B N   1 
ATOM   4114 C  CA  . ALA B 1 256 ? -18.289 11.353  25.765  1.00 27.57 ? 291 ALA B CA  1 
ATOM   4115 C  C   . ALA B 1 256 ? -17.577 12.221  26.797  1.00 34.34 ? 291 ALA B C   1 
ATOM   4116 O  O   . ALA B 1 256 ? -17.464 11.822  27.969  1.00 25.74 ? 291 ALA B O   1 
ATOM   4117 C  CB  . ALA B 1 256 ? -17.290 10.452  25.022  1.00 27.20 ? 291 ALA B CB  1 
ATOM   4118 N  N   . ALA B 1 257 ? -17.107 13.413  26.396  1.00 26.57 ? 292 ALA B N   1 
ATOM   4119 C  CA  . ALA B 1 257 ? -16.517 14.315  27.375  1.00 29.04 ? 292 ALA B CA  1 
ATOM   4120 C  C   . ALA B 1 257 ? -17.571 14.845  28.344  1.00 36.24 ? 292 ALA B C   1 
ATOM   4121 O  O   . ALA B 1 257 ? -17.302 14.961  29.547  1.00 32.94 ? 292 ALA B O   1 
ATOM   4122 C  CB  . ALA B 1 257 ? -15.781 15.454  26.671  1.00 27.42 ? 292 ALA B CB  1 
ATOM   4123 N  N   . LYS B 1 258 ? -18.781 15.154  27.849  1.00 29.40 ? 293 LYS B N   1 
ATOM   4124 C  CA  . LYS B 1 258 ? -19.817 15.676  28.737  1.00 38.83 ? 293 LYS B CA  1 
ATOM   4125 C  C   . LYS B 1 258 ? -20.259 14.622  29.743  1.00 37.87 ? 293 LYS B C   1 
ATOM   4126 O  O   . LYS B 1 258 ? -20.320 14.894  30.950  1.00 33.15 ? 293 LYS B O   1 
ATOM   4127 C  CB  . LYS B 1 258 ? -21.027 16.177  27.944  1.00 34.15 ? 293 LYS B CB  1 
ATOM   4128 C  CG  . LYS B 1 258 ? -22.101 16.714  28.874  1.00 44.30 ? 293 LYS B CG  1 
ATOM   4129 C  CD  . LYS B 1 258 ? -23.101 17.645  28.200  1.00 41.72 ? 293 LYS B CD  1 
ATOM   4130 C  CE  . LYS B 1 258 ? -24.426 17.604  28.957  1.00 43.21 ? 293 LYS B CE  1 
ATOM   4131 N  NZ  . LYS B 1 258 ? -25.605 18.055  28.157  1.00 53.93 ? 293 LYS B NZ  1 
ATOM   4132 N  N   . GLY B 1 259 ? -20.561 13.406  29.266  1.00 33.33 ? 294 GLY B N   1 
ATOM   4133 C  CA  . GLY B 1 259 ? -21.016 12.341  30.150  1.00 30.58 ? 294 GLY B CA  1 
ATOM   4134 C  C   . GLY B 1 259 ? -19.926 11.644  30.944  1.00 35.26 ? 294 GLY B C   1 
ATOM   4135 O  O   . GLY B 1 259 ? -20.230 10.982  31.942  1.00 36.32 ? 294 GLY B O   1 
ATOM   4136 N  N   . GLY B 1 260 ? -18.671 11.777  30.530  1.00 33.33 ? 295 GLY B N   1 
ATOM   4137 C  CA  . GLY B 1 260 ? -17.567 11.201  31.273  1.00 27.43 ? 295 GLY B CA  1 
ATOM   4138 C  C   . GLY B 1 260 ? -17.533 9.690   31.272  1.00 33.06 ? 295 GLY B C   1 
ATOM   4139 O  O   . GLY B 1 260 ? -17.150 9.078   32.280  1.00 29.52 ? 295 GLY B O   1 
ATOM   4140 N  N   . TYR B 1 261 ? -17.894 9.075   30.156  1.00 27.98 ? 296 TYR B N   1 
ATOM   4141 C  CA  . TYR B 1 261 ? -17.950 7.628   30.048  1.00 27.80 ? 296 TYR B CA  1 
ATOM   4142 C  C   . TYR B 1 261 ? -16.832 7.128   29.133  1.00 25.61 ? 296 TYR B C   1 
ATOM   4143 O  O   . TYR B 1 261 ? -16.206 7.891   28.388  1.00 23.89 ? 296 TYR B O   1 
ATOM   4144 C  CB  . TYR B 1 261 ? -19.343 7.187   29.573  1.00 26.95 ? 296 TYR B CB  1 
ATOM   4145 C  CG  . TYR B 1 261 ? -19.824 7.761   28.246  1.00 23.53 ? 296 TYR B CG  1 
ATOM   4146 C  CD1 . TYR B 1 261 ? -19.332 7.263   27.039  1.00 25.83 ? 296 TYR B CD1 1 
ATOM   4147 C  CD2 . TYR B 1 261 ? -20.805 8.745   28.199  1.00 24.87 ? 296 TYR B CD2 1 
ATOM   4148 C  CE1 . TYR B 1 261 ? -19.779 7.744   25.831  1.00 23.40 ? 296 TYR B CE1 1 
ATOM   4149 C  CE2 . TYR B 1 261 ? -21.264 9.252   26.985  1.00 24.67 ? 296 TYR B CE2 1 
ATOM   4150 C  CZ  . TYR B 1 261 ? -20.739 8.744   25.801  1.00 23.94 ? 296 TYR B CZ  1 
ATOM   4151 O  OH  . TYR B 1 261 ? -21.154 9.203   24.569  1.00 22.96 ? 296 TYR B OH  1 
ATOM   4152 N  N   . LEU B 1 262 ? -16.550 5.835   29.240  1.00 24.36 ? 297 LEU B N   1 
ATOM   4153 C  CA  . LEU B 1 262 ? -15.487 5.220   28.465  1.00 19.64 ? 297 LEU B CA  1 
ATOM   4154 C  C   . LEU B 1 262 ? -15.835 5.173   26.984  1.00 18.84 ? 297 LEU B C   1 
ATOM   4155 O  O   . LEU B 1 262 ? -16.987 4.939   26.612  1.00 19.89 ? 297 LEU B O   1 
ATOM   4156 C  CB  . LEU B 1 262 ? -15.245 3.794   28.968  1.00 26.27 ? 297 LEU B CB  1 
ATOM   4157 C  CG  . LEU B 1 262 ? -14.692 3.782   30.393  1.00 27.70 ? 297 LEU B CG  1 
ATOM   4158 C  CD1 . LEU B 1 262 ? -14.779 2.384   30.997  1.00 24.92 ? 297 LEU B CD1 1 
ATOM   4159 C  CD2 . LEU B 1 262 ? -13.269 4.340   30.366  1.00 19.59 ? 297 LEU B CD2 1 
ATOM   4160 N  N   . ILE B 1 263 ? -14.831 5.383   26.130  1.00 19.80 ? 298 ILE B N   1 
ATOM   4161 C  CA  . ILE B 1 263 ? -14.949 5.055   24.715  1.00 17.13 ? 298 ILE B CA  1 
ATOM   4162 C  C   . ILE B 1 263 ? -13.868 4.032   24.368  1.00 21.26 ? 298 ILE B C   1 
ATOM   4163 O  O   . ILE B 1 263 ? -12.903 3.810   25.113  1.00 19.23 ? 298 ILE B O   1 
ATOM   4164 C  CB  . ILE B 1 263 ? -14.870 6.291   23.793  1.00 17.18 ? 298 ILE B CB  1 
ATOM   4165 C  CG1 . ILE B 1 263 ? -13.482 6.914   23.835  1.00 20.02 ? 298 ILE B CG1 1 
ATOM   4166 C  CG2 . ILE B 1 263 ? -15.853 7.366   24.254  1.00 18.35 ? 298 ILE B CG2 1 
ATOM   4167 C  CD1 . ILE B 1 263 ? -13.332 8.117   22.921  1.00 25.33 ? 298 ILE B CD1 1 
ATOM   4168 N  N   . ALA B 1 264 ? -14.054 3.378   23.230  1.00 19.00 ? 299 ALA B N   1 
ATOM   4169 C  CA  . ALA B 1 264 ? -13.004 2.549   22.656  1.00 22.85 ? 299 ALA B CA  1 
ATOM   4170 C  C   . ALA B 1 264 ? -13.044 2.738   21.146  1.00 23.19 ? 299 ALA B C   1 
ATOM   4171 O  O   . ALA B 1 264 ? -14.081 3.107   20.572  1.00 16.38 ? 299 ALA B O   1 
ATOM   4172 C  CB  . ALA B 1 264 ? -13.165 1.048   23.053  1.00 15.26 ? 299 ALA B CB  1 
ATOM   4173 N  N   . ALA B 1 265 ? -11.907 2.502   20.500  1.00 17.61 ? 300 ALA B N   1 
ATOM   4174 C  CA  . ALA B 1 265 ? -11.907 2.491   19.046  1.00 14.58 ? 300 ALA B CA  1 
ATOM   4175 C  C   . ALA B 1 265 ? -10.871 1.511   18.562  1.00 14.52 ? 300 ALA B C   1 
ATOM   4176 O  O   . ALA B 1 265 ? -9.844  1.287   19.222  1.00 15.60 ? 300 ALA B O   1 
ATOM   4177 C  CB  . ALA B 1 265 ? -11.634 3.866   18.449  1.00 20.27 ? 300 ALA B CB  1 
ATOM   4178 N  N   . SER B 1 266 ? -11.129 0.994   17.359  1.00 15.14 ? 301 SER B N   1 
ATOM   4179 C  CA  . SER B 1 266 ? -10.433 -0.178  16.841  1.00 16.93 ? 301 SER B CA  1 
ATOM   4180 C  C   . SER B 1 266 ? -8.949  0.075   16.674  1.00 18.51 ? 301 SER B C   1 
ATOM   4181 O  O   . SER B 1 266 ? -8.125  -0.849  16.766  1.00 16.59 ? 301 SER B O   1 
ATOM   4182 C  CB  . SER B 1 266 ? -11.050 -0.558  15.492  1.00 18.31 ? 301 SER B CB  1 
ATOM   4183 O  OG  . SER B 1 266 ? -12.457 -0.511  15.550  1.00 19.50 ? 301 SER B OG  1 
ATOM   4184 N  N   . HIS B 1 267 ? -8.574  1.317   16.407  1.00 16.62 ? 302 HIS B N   1 
ATOM   4185 C  CA  . HIS B 1 267 ? -7.189  1.584   16.066  1.00 13.76 ? 302 HIS B CA  1 
ATOM   4186 C  C   . HIS B 1 267 ? -6.522  2.528   17.037  1.00 13.79 ? 302 HIS B C   1 
ATOM   4187 O  O   . HIS B 1 267 ? -5.500  3.135   16.693  1.00 14.08 ? 302 HIS B O   1 
ATOM   4188 C  CB  . HIS B 1 267 ? -7.083  2.109   14.634  1.00 15.87 ? 302 HIS B CB  1 
ATOM   4189 C  CG  . HIS B 1 267 ? -7.658  1.169   13.628  1.00 14.23 ? 302 HIS B CG  1 
ATOM   4190 N  ND1 . HIS B 1 267 ? -7.181  -0.123  13.474  1.00 14.38 ? 302 HIS B ND1 1 
ATOM   4191 C  CD2 . HIS B 1 267 ? -8.672  1.310   12.735  1.00 14.39 ? 302 HIS B CD2 1 
ATOM   4192 C  CE1 . HIS B 1 267 ? -7.869  -0.733  12.524  1.00 14.65 ? 302 HIS B CE1 1 
ATOM   4193 N  NE2 . HIS B 1 267 ? -8.786  0.104   12.078  1.00 15.52 ? 302 HIS B NE2 1 
ATOM   4194 N  N   . LEU B 1 268 ? -7.077  2.680   18.231  1.00 13.89 ? 303 LEU B N   1 
ATOM   4195 C  CA  . LEU B 1 268 ? -6.315  3.296   19.295  1.00 14.39 ? 303 LEU B CA  1 
ATOM   4196 C  C   . LEU B 1 268 ? -5.396  2.236   19.876  1.00 14.38 ? 303 LEU B C   1 
ATOM   4197 O  O   . LEU B 1 268 ? -5.672  1.033   19.767  1.00 15.30 ? 303 LEU B O   1 
ATOM   4198 C  CB  . LEU B 1 268 ? -7.230  3.883   20.366  1.00 14.81 ? 303 LEU B CB  1 
ATOM   4199 C  CG  . LEU B 1 268 ? -8.249  4.926   19.875  1.00 16.03 ? 303 LEU B CG  1 
ATOM   4200 C  CD1 . LEU B 1 268 ? -9.071  5.309   21.088  1.00 20.86 ? 303 LEU B CD1 1 
ATOM   4201 C  CD2 . LEU B 1 268 ? -7.520  6.181   19.321  1.00 14.99 ? 303 LEU B CD2 1 
ATOM   4202 N  N   . SER B 1 269 ? -4.265  2.683   20.410  1.00 14.82 ? 304 SER B N   1 
ATOM   4203 C  CA  . SER B 1 269 ? -3.242  1.751   20.897  1.00 15.20 ? 304 SER B CA  1 
ATOM   4204 C  C   . SER B 1 269 ? -3.857  0.735   21.838  1.00 15.22 ? 304 SER B C   1 
ATOM   4205 O  O   . SER B 1 269 ? -4.489  1.112   22.831  1.00 18.08 ? 304 SER B O   1 
ATOM   4206 C  CB  . SER B 1 269 ? -2.127  2.514   21.624  1.00 17.25 ? 304 SER B CB  1 
ATOM   4207 O  OG  . SER B 1 269 ? -1.112  1.607   22.086  1.00 18.30 ? 304 SER B OG  1 
ATOM   4208 N  N   . PHE B 1 270 ? -3.650  -0.555  21.527  1.00 14.49 ? 305 PHE B N   1 
ATOM   4209 C  CA  . PHE B 1 270 ? -4.352  -1.627  22.226  1.00 14.18 ? 305 PHE B CA  1 
ATOM   4210 C  C   . PHE B 1 270 ? -4.149  -1.469  23.732  1.00 14.43 ? 305 PHE B C   1 
ATOM   4211 O  O   . PHE B 1 270 ? -3.025  -1.194  24.177  1.00 16.21 ? 305 PHE B O   1 
ATOM   4212 C  CB  . PHE B 1 270 ? -3.813  -2.989  21.755  1.00 17.26 ? 305 PHE B CB  1 
ATOM   4213 C  CG  . PHE B 1 270 ? -4.386  -4.157  22.490  1.00 17.27 ? 305 PHE B CG  1 
ATOM   4214 C  CD1 . PHE B 1 270 ? -5.614  -4.690  22.097  1.00 14.70 ? 305 PHE B CD1 1 
ATOM   4215 C  CD2 . PHE B 1 270 ? -3.719  -4.701  23.565  1.00 18.51 ? 305 PHE B CD2 1 
ATOM   4216 C  CE1 . PHE B 1 270 ? -6.185  -5.741  22.772  1.00 20.55 ? 305 PHE B CE1 1 
ATOM   4217 C  CE2 . PHE B 1 270 ? -4.262  -5.772  24.257  1.00 22.29 ? 305 PHE B CE2 1 
ATOM   4218 C  CZ  . PHE B 1 270 ? -5.511  -6.299  23.854  1.00 19.38 ? 305 PHE B CZ  1 
ATOM   4219 N  N   . PRO B 1 271 ? -5.188  -1.649  24.559  1.00 17.88 ? 306 PRO B N   1 
ATOM   4220 C  CA  . PRO B 1 271 ? -6.552  -2.117  24.280  1.00 14.44 ? 306 PRO B CA  1 
ATOM   4221 C  C   . PRO B 1 271 ? -7.510  -1.043  23.722  1.00 16.61 ? 306 PRO B C   1 
ATOM   4222 O  O   . PRO B 1 271 ? -8.658  -1.335  23.376  1.00 14.94 ? 306 PRO B O   1 
ATOM   4223 C  CB  . PRO B 1 271 ? -7.029  -2.589  25.666  1.00 18.70 ? 306 PRO B CB  1 
ATOM   4224 C  CG  . PRO B 1 271 ? -6.346  -1.585  26.613  1.00 19.97 ? 306 PRO B CG  1 
ATOM   4225 C  CD  . PRO B 1 271 ? -4.964  -1.450  26.010  1.00 14.95 ? 306 PRO B CD  1 
ATOM   4226 N  N   . GLY B 1 272 ? -7.062  0.203   23.628  1.00 14.09 ? 307 GLY B N   1 
ATOM   4227 C  CA  . GLY B 1 272 ? -7.841  1.239   22.966  1.00 18.36 ? 307 GLY B CA  1 
ATOM   4228 C  C   . GLY B 1 272 ? -9.036  1.762   23.729  1.00 15.52 ? 307 GLY B C   1 
ATOM   4229 O  O   . GLY B 1 272 ? -9.991  2.231   23.105  1.00 14.33 ? 307 GLY B O   1 
ATOM   4230 N  N   . ILE B 1 273 ? -8.995  1.729   25.063  1.00 18.16 ? 308 ILE B N   1 
ATOM   4231 C  CA  . ILE B 1 273 ? -10.134 2.053   25.925  1.00 16.83 ? 308 ILE B CA  1 
ATOM   4232 C  C   . ILE B 1 273 ? -9.761  3.208   26.832  1.00 17.23 ? 308 ILE B C   1 
ATOM   4233 O  O   . ILE B 1 273 ? -8.708  3.175   27.477  1.00 17.72 ? 308 ILE B O   1 
ATOM   4234 C  CB  . ILE B 1 273 ? -10.582 0.862   26.798  1.00 20.03 ? 308 ILE B CB  1 
ATOM   4235 C  CG1 . ILE B 1 273 ? -10.911 -0.375  25.952  1.00 16.67 ? 308 ILE B CG1 1 
ATOM   4236 C  CG2 . ILE B 1 273 ? -11.703 1.300   27.770  1.00 20.49 ? 308 ILE B CG2 1 
ATOM   4237 C  CD1 . ILE B 1 273 ? -11.139 -1.597  26.772  1.00 24.81 ? 308 ILE B CD1 1 
ATOM   4238 N  N   . GLY B 1 274 ? -10.643 4.180   26.949  1.00 16.25 ? 309 GLY B N   1 
ATOM   4239 C  CA  . GLY B 1 274 ? -10.338 5.253   27.889  1.00 19.89 ? 309 GLY B CA  1 
ATOM   4240 C  C   . GLY B 1 274 ? -11.402 6.323   27.862  1.00 19.35 ? 309 GLY B C   1 
ATOM   4241 O  O   . GLY B 1 274 ? -12.436 6.188   27.205  1.00 19.42 ? 309 GLY B O   1 
ATOM   4242 N  N   . HIS B 1 275 ? -11.143 7.383   28.620  1.00 24.42 ? 310 HIS B N   1 
ATOM   4243 C  CA  . HIS B 1 275 ? -12.038 8.531   28.737  1.00 21.38 ? 310 HIS B CA  1 
ATOM   4244 C  C   . HIS B 1 275 ? -11.577 9.630   27.780  1.00 26.43 ? 310 HIS B C   1 
ATOM   4245 O  O   . HIS B 1 275 ? -10.489 9.569   27.211  1.00 25.64 ? 310 HIS B O   1 
ATOM   4246 C  CB  . HIS B 1 275 ? -12.036 9.067   30.170  1.00 23.19 ? 310 HIS B CB  1 
ATOM   4247 C  CG  . HIS B 1 275 ? -12.681 8.163   31.159  1.00 21.73 ? 310 HIS B CG  1 
ATOM   4248 N  ND1 . HIS B 1 275 ? -14.043 8.123   31.357  1.00 27.90 ? 310 HIS B ND1 1 
ATOM   4249 C  CD2 . HIS B 1 275 ? -12.150 7.230   31.985  1.00 23.06 ? 310 HIS B CD2 1 
ATOM   4250 C  CE1 . HIS B 1 275 ? -14.323 7.219   32.279  1.00 32.32 ? 310 HIS B CE1 1 
ATOM   4251 N  NE2 . HIS B 1 275 ? -13.191 6.662   32.676  1.00 32.96 ? 310 HIS B NE2 1 
ATOM   4252 N  N   . ILE B 1 276 ? -12.394 10.669  27.631  1.00 26.83 ? 311 ILE B N   1 
ATOM   4253 C  CA  . ILE B 1 276 ? -12.010 11.789  26.777  1.00 24.17 ? 311 ILE B CA  1 
ATOM   4254 C  C   . ILE B 1 276 ? -12.403 13.076  27.473  1.00 27.06 ? 311 ILE B C   1 
ATOM   4255 O  O   . ILE B 1 276 ? -13.481 13.165  28.062  1.00 24.90 ? 311 ILE B O   1 
ATOM   4256 C  CB  . ILE B 1 276 ? -12.671 11.672  25.390  1.00 33.48 ? 311 ILE B CB  1 
ATOM   4257 C  CG1 . ILE B 1 276 ? -12.446 12.920  24.556  1.00 29.83 ? 311 ILE B CG1 1 
ATOM   4258 C  CG2 . ILE B 1 276 ? -14.152 11.506  25.543  1.00 30.37 ? 311 ILE B CG2 1 
ATOM   4259 C  CD1 . ILE B 1 276 ? -12.551 12.648  23.073  1.00 29.94 ? 311 ILE B CD1 1 
ATOM   4260 N  N   . ARG B 1 277 ? -11.519 14.066  27.414  1.00 25.69 ? 312 ARG B N   1 
ATOM   4261 C  CA  . ARG B 1 277 ? -11.709 15.359  28.072  1.00 33.58 ? 312 ARG B CA  1 
ATOM   4262 C  C   . ARG B 1 277 ? -11.500 16.451  27.034  1.00 28.03 ? 312 ARG B C   1 
ATOM   4263 O  O   . ARG B 1 277 ? -10.571 16.370  26.234  1.00 27.29 ? 312 ARG B O   1 
ATOM   4264 C  CB  . ARG B 1 277 ? -10.702 15.510  29.221  1.00 35.08 ? 312 ARG B CB  1 
ATOM   4265 C  CG  . ARG B 1 277 ? -10.520 16.886  29.778  1.00 44.54 ? 312 ARG B CG  1 
ATOM   4266 C  CD  . ARG B 1 277 ? -9.114  17.020  30.309  1.00 45.56 ? 312 ARG B CD  1 
ATOM   4267 N  NE  . ARG B 1 277 ? -8.719  15.832  31.049  1.00 51.08 ? 312 ARG B NE  1 
ATOM   4268 C  CZ  . ARG B 1 277 ? -7.460  15.505  31.309  1.00 59.35 ? 312 ARG B CZ  1 
ATOM   4269 N  NH1 . ARG B 1 277 ? -6.459  16.324  31.010  1.00 56.25 ? 312 ARG B NH1 1 
ATOM   4270 N  NH2 . ARG B 1 277 ? -7.201  14.337  31.897  1.00 57.95 ? 312 ARG B NH2 1 
ATOM   4271 N  N   . ALA B 1 278 ? -12.384 17.437  27.004  1.00 29.88 ? 313 ALA B N   1 
ATOM   4272 C  CA  . ALA B 1 278 ? -12.183 18.566  26.077  1.00 31.12 ? 313 ALA B CA  1 
ATOM   4273 C  C   . ALA B 1 278 ? -10.962 19.346  26.541  1.00 34.54 ? 313 ALA B C   1 
ATOM   4274 O  O   . ALA B 1 278 ? -10.922 19.779  27.705  1.00 38.30 ? 313 ALA B O   1 
ATOM   4275 C  CB  . ALA B 1 278 ? -13.411 19.446  26.009  1.00 36.61 ? 313 ALA B CB  1 
ATOM   4276 N  N   . GLU B 1 279 ? -9.995  19.470  25.651  1.00 32.31 ? 314 GLU B N   1 
ATOM   4277 C  CA  . GLU B 1 279 ? -8.780  20.228  25.995  1.00 44.87 ? 314 GLU B CA  1 
ATOM   4278 C  C   . GLU B 1 279 ? -8.416  21.137  24.822  1.00 35.41 ? 314 GLU B C   1 
ATOM   4279 O  O   . GLU B 1 279 ? -8.448  20.704  23.668  1.00 34.04 ? 314 GLU B O   1 
ATOM   4280 C  CB  . GLU B 1 279 ? -7.630  19.310  26.407  1.00 52.52 ? 314 GLU B CB  1 
ATOM   4281 C  CG  . GLU B 1 279 ? -6.921  19.803  27.663  1.00 62.59 ? 314 GLU B CG  1 
ATOM   4282 C  CD  . GLU B 1 279 ? -6.027  18.753  28.283  1.00 64.01 ? 314 GLU B CD  1 
ATOM   4283 O  OE1 . GLU B 1 279 ? -6.256  18.400  29.452  1.00 57.68 ? 314 GLU B OE1 1 
ATOM   4284 O  OE2 . GLU B 1 279 ? -5.109  18.288  27.586  1.00 69.84 ? 314 GLU B OE2 1 
ATOM   4285 N  N   . GLY B 1 280 ? -8.086  22.380  25.149  1.00 50.86 ? 315 GLY B N   1 
ATOM   4286 C  CA  . GLY B 1 280 ? -7.757  23.375  24.136  1.00 48.36 ? 315 GLY B CA  1 
ATOM   4287 C  C   . GLY B 1 280 ? -8.642  23.403  22.896  1.00 46.74 ? 315 GLY B C   1 
ATOM   4288 O  O   . GLY B 1 280 ? -9.857  23.584  23.002  1.00 39.84 ? 315 GLY B O   1 
ATOM   4289 N  N   . LYS B 1 281 ? -8.032  23.206  21.719  1.00 48.18 ? 316 LYS B N   1 
ATOM   4290 C  CA  . LYS B 1 281 ? -8.731  23.206  20.434  1.00 46.33 ? 316 LYS B CA  1 
ATOM   4291 C  C   . LYS B 1 281 ? -9.542  21.939  20.197  1.00 37.16 ? 316 LYS B C   1 
ATOM   4292 O  O   . LYS B 1 281 ? -10.406 21.916  19.313  1.00 38.95 ? 316 LYS B O   1 
ATOM   4293 C  CB  . LYS B 1 281 ? -7.715  23.329  19.298  1.00 56.30 ? 316 LYS B CB  1 
ATOM   4294 C  CG  . LYS B 1 281 ? -6.787  22.099  19.234  1.00 57.86 ? 316 LYS B CG  1 
ATOM   4295 C  CD  . LYS B 1 281 ? -5.728  22.153  18.141  1.00 51.91 ? 316 LYS B CD  1 
ATOM   4296 C  CE  . LYS B 1 281 ? -6.353  21.971  16.758  1.00 46.71 ? 316 LYS B CE  1 
ATOM   4297 N  NZ  . LYS B 1 281 ? -5.316  21.873  15.687  1.00 48.13 ? 316 LYS B NZ  1 
ATOM   4298 N  N   . GLY B 1 282 ? -9.245  20.877  20.921  1.00 37.87 ? 317 GLY B N   1 
ATOM   4299 C  CA  . GLY B 1 282 ? -9.848  19.589  20.659  1.00 39.29 ? 317 GLY B CA  1 
ATOM   4300 C  C   . GLY B 1 282 ? -10.057 18.791  21.925  1.00 29.85 ? 317 GLY B C   1 
ATOM   4301 O  O   . GLY B 1 282 ? -10.670 19.244  22.900  1.00 31.65 ? 317 GLY B O   1 
ATOM   4302 N  N   . TYR B 1 283 ? -9.536  17.577  21.915  1.00 27.95 ? 318 TYR B N   1 
ATOM   4303 C  CA  . TYR B 1 283 ? -9.772  16.659  23.011  1.00 26.64 ? 318 TYR B CA  1 
ATOM   4304 C  C   . TYR B 1 283 ? -8.474  15.984  23.423  1.00 27.01 ? 318 TYR B C   1 
ATOM   4305 O  O   . TYR B 1 283 ? -7.486  15.954  22.672  1.00 28.76 ? 318 TYR B O   1 
ATOM   4306 C  CB  . TYR B 1 283 ? -10.836 15.639  22.610  1.00 25.13 ? 318 TYR B CB  1 
ATOM   4307 C  CG  . TYR B 1 283 ? -12.181 16.297  22.350  1.00 27.19 ? 318 TYR B CG  1 
ATOM   4308 C  CD1 . TYR B 1 283 ? -12.507 16.811  21.103  1.00 26.89 ? 318 TYR B CD1 1 
ATOM   4309 C  CD2 . TYR B 1 283 ? -13.099 16.438  23.376  1.00 26.85 ? 318 TYR B CD2 1 
ATOM   4310 C  CE1 . TYR B 1 283 ? -13.740 17.422  20.886  1.00 28.58 ? 318 TYR B CE1 1 
ATOM   4311 C  CE2 . TYR B 1 283 ? -14.319 17.027  23.171  1.00 32.38 ? 318 TYR B CE2 1 
ATOM   4312 C  CZ  . TYR B 1 283 ? -14.626 17.531  21.942  1.00 28.76 ? 318 TYR B CZ  1 
ATOM   4313 O  OH  . TYR B 1 283 ? -15.845 18.094  21.789  1.00 30.90 ? 318 TYR B OH  1 
ATOM   4314 N  N   . ARG B 1 284 ? -8.481  15.491  24.657  1.00 25.45 ? 319 ARG B N   1 
ATOM   4315 C  CA  . ARG B 1 284 ? -7.422  14.651  25.193  1.00 26.67 ? 319 ARG B CA  1 
ATOM   4316 C  C   . ARG B 1 284 ? -8.005  13.282  25.521  1.00 25.44 ? 319 ARG B C   1 
ATOM   4317 O  O   . ARG B 1 284 ? -9.079  13.193  26.109  1.00 24.43 ? 319 ARG B O   1 
ATOM   4318 C  CB  . ARG B 1 284 ? -6.770  15.263  26.445  1.00 30.18 ? 319 ARG B CB  1 
ATOM   4319 C  CG  . ARG B 1 284 ? -5.802  14.301  27.111  1.00 33.43 ? 319 ARG B CG  1 
ATOM   4320 C  CD  . ARG B 1 284 ? -4.457  14.324  26.387  1.00 43.49 ? 319 ARG B CD  1 
ATOM   4321 N  NE  . ARG B 1 284 ? -4.601  13.931  24.984  1.00 46.17 ? 319 ARG B NE  1 
ATOM   4322 C  CZ  . ARG B 1 284 ? -4.358  12.746  24.449  1.00 38.24 ? 319 ARG B CZ  1 
ATOM   4323 N  NH1 . ARG B 1 284 ? -3.870  11.744  25.166  1.00 47.19 ? 319 ARG B NH1 1 
ATOM   4324 N  NH2 . ARG B 1 284 ? -4.613  12.565  23.156  1.00 30.50 ? 319 ARG B NH2 1 
ATOM   4325 N  N   . PHE B 1 285 ? -7.301  12.228  25.119  1.00 21.62 ? 320 PHE B N   1 
ATOM   4326 C  CA  . PHE B 1 285 ? -7.680  10.844  25.415  1.00 27.35 ? 320 PHE B CA  1 
ATOM   4327 C  C   . PHE B 1 285 ? -6.935  10.378  26.656  1.00 25.30 ? 320 PHE B C   1 
ATOM   4328 O  O   . PHE B 1 285 ? -5.730  10.603  26.791  1.00 26.11 ? 320 PHE B O   1 
ATOM   4329 C  CB  . PHE B 1 285 ? -7.364  9.948   24.218  1.00 20.50 ? 320 PHE B CB  1 
ATOM   4330 C  CG  . PHE B 1 285 ? -7.748  8.505   24.397  1.00 21.08 ? 320 PHE B CG  1 
ATOM   4331 C  CD1 . PHE B 1 285 ? -9.067  8.121   24.537  1.00 22.75 ? 320 PHE B CD1 1 
ATOM   4332 C  CD2 . PHE B 1 285 ? -6.749  7.512   24.378  1.00 24.49 ? 320 PHE B CD2 1 
ATOM   4333 C  CE1 . PHE B 1 285 ? -9.403  6.765   24.689  1.00 20.13 ? 320 PHE B CE1 1 
ATOM   4334 C  CE2 . PHE B 1 285 ? -7.078  6.146   24.523  1.00 19.77 ? 320 PHE B CE2 1 
ATOM   4335 C  CZ  . PHE B 1 285 ? -8.392  5.785   24.688  1.00 21.73 ? 320 PHE B CZ  1 
ATOM   4336 N  N   . VAL B 1 286 ? -7.674  9.771   27.581  1.00 19.71 ? 321 VAL B N   1 
ATOM   4337 C  CA  . VAL B 1 286 ? -7.139  9.341   28.853  1.00 26.75 ? 321 VAL B CA  1 
ATOM   4338 C  C   . VAL B 1 286 ? -7.345  7.829   28.957  1.00 18.66 ? 321 VAL B C   1 
ATOM   4339 O  O   . VAL B 1 286 ? -8.395  7.348   29.286  1.00 18.41 ? 321 VAL B O   1 
ATOM   4340 C  CB  . VAL B 1 286 ? -7.884  10.049  30.022  1.00 22.48 ? 321 VAL B CB  1 
ATOM   4341 C  CG1 . VAL B 1 286 ? -7.300  9.681   31.354  1.00 21.93 ? 321 VAL B CG1 1 
ATOM   4342 C  CG2 . VAL B 1 286 ? -7.859  11.543  29.792  1.00 31.40 ? 321 VAL B CG2 1 
ATOM   4343 N  N   . PRO B 1 287 ? -6.268  7.060   28.680  1.00 18.13 ? 322 PRO B N   1 
ATOM   4344 C  CA  . PRO B 1 287 ? -6.417  5.594   28.741  1.00 17.16 ? 322 PRO B CA  1 
ATOM   4345 C  C   . PRO B 1 287 ? -6.911  5.113   30.094  1.00 19.26 ? 322 PRO B C   1 
ATOM   4346 O  O   . PRO B 1 287 ? -6.568  5.662   31.148  1.00 18.90 ? 322 PRO B O   1 
ATOM   4347 C  CB  . PRO B 1 287 ? -4.991  5.085   28.471  1.00 17.25 ? 322 PRO B CB  1 
ATOM   4348 C  CG  . PRO B 1 287 ? -4.298  6.178   27.741  1.00 22.08 ? 322 PRO B CG  1 
ATOM   4349 C  CD  . PRO B 1 287 ? -4.925  7.469   28.254  1.00 20.53 ? 322 PRO B CD  1 
ATOM   4350 N  N   . VAL B 1 288 ? -7.703  4.037   30.052  1.00 16.83 ? 323 VAL B N   1 
ATOM   4351 C  CA  . VAL B 1 288 ? -8.293  3.499   31.272  1.00 18.68 ? 323 VAL B CA  1 
ATOM   4352 C  C   . VAL B 1 288 ? -7.175  3.100   32.223  1.00 24.55 ? 323 VAL B C   1 
ATOM   4353 O  O   . VAL B 1 288 ? -6.113  2.624   31.797  1.00 20.72 ? 323 VAL B O   1 
ATOM   4354 C  CB  . VAL B 1 288 ? -9.220  2.305   30.962  1.00 22.77 ? 323 VAL B CB  1 
ATOM   4355 C  CG1 . VAL B 1 288 ? -8.502  1.259   30.130  1.00 21.38 ? 323 VAL B CG1 1 
ATOM   4356 C  CG2 . VAL B 1 288 ? -9.808  1.703   32.238  1.00 31.02 ? 323 VAL B CG2 1 
ATOM   4357 N  N   . ASN B 1 289 ? -7.377  3.378   33.510  1.00 22.52 ? 324 ASN B N   1 
ATOM   4358 C  CA  . ASN B 1 289 ? -6.440  2.953   34.548  1.00 22.33 ? 324 ASN B CA  1 
ATOM   4359 C  C   . ASN B 1 289 ? -6.425  1.426   34.610  1.00 23.37 ? 324 ASN B C   1 
ATOM   4360 O  O   . ASN B 1 289 ? -7.488  0.805   34.652  1.00 21.12 ? 324 ASN B O   1 
ATOM   4361 C  CB  . ASN B 1 289 ? -6.894  3.523   35.893  1.00 21.88 ? 324 ASN B CB  1 
ATOM   4362 C  CG  . ASN B 1 289 ? -5.903  3.299   37.013  1.00 29.73 ? 324 ASN B CG  1 
ATOM   4363 O  OD1 . ASN B 1 289 ? -4.688  3.398   36.824  1.00 33.32 ? 324 ASN B OD1 1 
ATOM   4364 N  ND2 . ASN B 1 289 ? -6.424  2.952   38.199  1.00 29.45 ? 324 ASN B ND2 1 
ATOM   4365 N  N   . TYR B 1 290 ? -5.227  0.822   34.628  1.00 18.90 ? 325 TYR B N   1 
ATOM   4366 C  CA  . TYR B 1 290 ? -5.119  -0.623  34.760  1.00 20.95 ? 325 TYR B CA  1 
ATOM   4367 C  C   . TYR B 1 290 ? -5.821  -1.062  36.029  1.00 19.74 ? 325 TYR B C   1 
ATOM   4368 O  O   . TYR B 1 290 ? -5.598  -0.503  37.109  1.00 20.94 ? 325 TYR B O   1 
ATOM   4369 C  CB  . TYR B 1 290 ? -3.654  -1.059  34.819  1.00 21.58 ? 325 TYR B CB  1 
ATOM   4370 C  CG  . TYR B 1 290 ? -3.440  -2.568  34.942  1.00 23.23 ? 325 TYR B CG  1 
ATOM   4371 C  CD1 . TYR B 1 290 ? -3.583  -3.406  33.847  1.00 26.10 ? 325 TYR B CD1 1 
ATOM   4372 C  CD2 . TYR B 1 290 ? -3.127  -3.150  36.166  1.00 26.12 ? 325 TYR B CD2 1 
ATOM   4373 C  CE1 . TYR B 1 290 ? -3.382  -4.780  33.956  1.00 24.03 ? 325 TYR B CE1 1 
ATOM   4374 C  CE2 . TYR B 1 290 ? -2.956  -4.531  36.291  1.00 23.31 ? 325 TYR B CE2 1 
ATOM   4375 C  CZ  . TYR B 1 290 ? -3.070  -5.329  35.189  1.00 24.95 ? 325 TYR B CZ  1 
ATOM   4376 O  OH  . TYR B 1 290 ? -2.888  -6.691  35.321  1.00 28.36 ? 325 TYR B OH  1 
ATOM   4377 N  N   . SER B 1 291 ? -6.689  -2.066  35.888  1.00 19.60 ? 326 SER B N   1 
ATOM   4378 C  CA  . SER B 1 291 ? -7.485  -2.583  36.987  1.00 22.78 ? 326 SER B CA  1 
ATOM   4379 C  C   . SER B 1 291 ? -7.442  -4.091  36.920  1.00 25.37 ? 326 SER B C   1 
ATOM   4380 O  O   . SER B 1 291 ? -7.580  -4.667  35.836  1.00 28.71 ? 326 SER B O   1 
ATOM   4381 C  CB  . SER B 1 291 ? -8.951  -2.129  36.906  1.00 21.25 ? 326 SER B CB  1 
ATOM   4382 O  OG  . SER B 1 291 ? -9.613  -2.523  38.078  1.00 25.91 ? 326 SER B OG  1 
ATOM   4383 N  N   . VAL B 1 292 ? -7.233  -4.727  38.048  1.00 27.00 ? 327 VAL B N   1 
ATOM   4384 C  CA  . VAL B 1 292 ? -7.237  -6.183  38.069  1.00 23.56 ? 327 VAL B CA  1 
ATOM   4385 C  C   . VAL B 1 292 ? -8.672  -6.642  38.240  1.00 37.42 ? 327 VAL B C   1 
ATOM   4386 O  O   . VAL B 1 292 ? -9.420  -6.108  39.072  1.00 36.87 ? 327 VAL B O   1 
ATOM   4387 C  CB  . VAL B 1 292 ? -6.329  -6.751  39.180  1.00 28.14 ? 327 VAL B CB  1 
ATOM   4388 C  CG1 . VAL B 1 292 ? -6.428  -8.301  39.207  1.00 33.01 ? 327 VAL B CG1 1 
ATOM   4389 C  CG2 . VAL B 1 292 ? -4.886  -6.336  38.971  1.00 27.00 ? 327 VAL B CG2 1 
ATOM   4390 N  N   . VAL B 1 293 ? -9.058  -7.636  37.445  1.00 32.76 ? 328 VAL B N   1 
ATOM   4391 C  CA  . VAL B 1 293 ? -10.413 -8.175  37.428  1.00 39.50 ? 328 VAL B CA  1 
ATOM   4392 C  C   . VAL B 1 293 ? -10.367 -9.531  38.106  1.00 39.82 ? 328 VAL B C   1 
ATOM   4393 O  O   . VAL B 1 293 ? -9.612  -10.412 37.677  1.00 42.94 ? 328 VAL B O   1 
ATOM   4394 C  CB  . VAL B 1 293 ? -10.938 -8.313  35.995  1.00 39.55 ? 328 VAL B CB  1 
ATOM   4395 C  CG1 . VAL B 1 293 ? -12.224 -9.090  35.999  1.00 43.17 ? 328 VAL B CG1 1 
ATOM   4396 C  CG2 . VAL B 1 293 ? -11.103 -6.962  35.366  1.00 29.42 ? 328 VAL B CG2 1 
ATOM   4397 N  N   . ASN B 1 294 ? -11.146 -9.700  39.169  1.00 43.50 ? 329 ASN B N   1 
ATOM   4398 C  CA  . ASN B 1 294 ? -11.159 -10.981 39.866  1.00 48.43 ? 329 ASN B CA  1 
ATOM   4399 C  C   . ASN B 1 294 ? -12.504 -11.689 39.684  1.00 44.77 ? 329 ASN B C   1 
ATOM   4400 O  O   . ASN B 1 294 ? -13.554 -11.164 40.056  1.00 55.23 ? 329 ASN B O   1 
ATOM   4401 C  CB  . ASN B 1 294 ? -10.850 -10.804 41.358  1.00 43.83 ? 329 ASN B CB  1 
ATOM   4402 C  CG  . ASN B 1 294 ? -9.480  -10.189 41.611  1.00 49.61 ? 329 ASN B CG  1 
ATOM   4403 O  OD1 . ASN B 1 294 ? -9.373  -9.062  42.106  1.00 45.03 ? 329 ASN B OD1 1 
ATOM   4404 N  ND2 . ASN B 1 294 ? -8.426  -10.925 41.270  1.00 46.69 ? 329 ASN B ND2 1 
HETATM 4405 ZN ZN  . ZN  C 2 .   ? 8.203   3.945   47.766  1.00 24.04 ? 401 ZN  A ZN  1 
HETATM 4406 ZN ZN  . ZN  D 2 .   ? 6.501   1.976   45.948  1.00 22.88 ? 402 ZN  A ZN  1 
HETATM 4407 ZN ZN  . ZN  E 2 .   ? -12.167 1.440   8.413   1.00 19.41 ? 401 ZN  B ZN  1 
HETATM 4408 ZN ZN  . ZN  F 2 .   ? -10.257 -0.137  10.434  1.00 18.45 ? 402 ZN  B ZN  1 
HETATM 4409 O  O   . HOH G 3 .   ? -4.492  15.249  49.408  1.00 45.95 ? 501 HOH A O   1 
HETATM 4410 O  O   . HOH G 3 .   ? 29.565  5.116   42.240  1.00 45.24 ? 502 HOH A O   1 
HETATM 4411 O  O   . HOH G 3 .   ? 8.047   14.079  53.231  1.00 36.54 ? 503 HOH A O   1 
HETATM 4412 O  O   . HOH G 3 .   ? -3.443  -6.215  48.983  1.00 41.99 ? 504 HOH A O   1 
HETATM 4413 O  O   . HOH G 3 .   ? 27.532  5.676   35.572  1.00 36.48 ? 505 HOH A O   1 
HETATM 4414 O  O   . HOH G 3 .   ? 24.643  -7.362  29.683  1.00 35.67 ? 506 HOH A O   1 
HETATM 4415 O  O   . HOH G 3 .   ? 15.794  -6.087  21.222  1.00 33.43 ? 507 HOH A O   1 
HETATM 4416 O  O   . HOH G 3 .   ? 3.102   5.587   56.659  1.00 54.89 ? 508 HOH A O   1 
HETATM 4417 O  O   . HOH G 3 .   ? 12.911  -9.279  29.709  1.00 20.19 ? 509 HOH A O   1 
HETATM 4418 O  O   . HOH G 3 .   ? -0.047  -8.209  24.035  1.00 23.21 ? 510 HOH A O   1 
HETATM 4419 O  O   . HOH G 3 .   ? 22.362  8.889   30.126  1.00 46.14 ? 511 HOH A O   1 
HETATM 4420 O  O   . HOH G 3 .   ? -2.157  1.450   31.901  1.00 19.74 ? 512 HOH A O   1 
HETATM 4421 O  O   . HOH G 3 .   ? 20.343  4.984   64.632  1.00 30.08 ? 513 HOH A O   1 
HETATM 4422 O  O   . HOH G 3 .   ? 23.615  -21.951 41.182  1.00 38.79 ? 514 HOH A O   1 
HETATM 4423 O  O   . HOH G 3 .   ? 4.898   -1.154  23.432  1.00 24.44 ? 515 HOH A O   1 
HETATM 4424 O  O   . HOH G 3 .   ? 13.627  10.491  45.411  1.00 25.08 ? 516 HOH A O   1 
HETATM 4425 O  O   . HOH G 3 .   ? 31.702  1.273   32.751  1.00 31.61 ? 517 HOH A O   1 
HETATM 4426 O  O   . HOH G 3 .   ? -0.238  -14.352 36.747  1.00 42.71 ? 518 HOH A O   1 
HETATM 4427 O  O   . HOH G 3 .   ? 23.188  -3.424  23.150  1.00 24.29 ? 519 HOH A O   1 
HETATM 4428 O  O   . HOH G 3 .   ? 22.004  6.032   44.077  1.00 25.43 ? 520 HOH A O   1 
HETATM 4429 O  O   . HOH G 3 .   ? 26.688  -5.363  39.046  1.00 29.89 ? 521 HOH A O   1 
HETATM 4430 O  O   . HOH G 3 .   ? 6.155   12.348  45.983  1.00 35.37 ? 522 HOH A O   1 
HETATM 4431 O  O   . HOH G 3 .   ? 5.153   6.911   24.143  1.00 31.65 ? 523 HOH A O   1 
HETATM 4432 O  O   . HOH G 3 .   ? -7.406  -6.395  33.463  1.00 31.23 ? 524 HOH A O   1 
HETATM 4433 O  O   . HOH G 3 .   ? 20.257  10.815  50.876  1.00 34.14 ? 525 HOH A O   1 
HETATM 4434 O  O   . HOH G 3 .   ? 25.952  -11.153 37.351  1.00 39.12 ? 526 HOH A O   1 
HETATM 4435 O  O   . HOH G 3 .   ? 6.282   5.019   40.663  1.00 18.62 ? 527 HOH A O   1 
HETATM 4436 O  O   . HOH G 3 .   ? 6.446   -9.601  44.689  1.00 17.65 ? 528 HOH A O   1 
HETATM 4437 O  O   . HOH G 3 .   ? -0.915  15.073  36.589  1.00 29.44 ? 529 HOH A O   1 
HETATM 4438 O  O   . HOH G 3 .   ? -4.060  -7.273  42.472  1.00 32.67 ? 530 HOH A O   1 
HETATM 4439 O  O   . HOH G 3 .   ? 16.178  9.864   37.855  1.00 22.09 ? 531 HOH A O   1 
HETATM 4440 O  O   . HOH G 3 .   ? 8.914   -16.740 39.993  1.00 29.72 ? 532 HOH A O   1 
HETATM 4441 O  O   . HOH G 3 .   ? 28.106  4.067   54.244  1.00 29.57 ? 533 HOH A O   1 
HETATM 4442 O  O   . HOH G 3 .   ? 17.729  -2.723  70.086  1.00 49.30 ? 534 HOH A O   1 
HETATM 4443 O  O   . HOH G 3 .   ? 25.443  9.112   47.193  1.00 36.32 ? 535 HOH A O   1 
HETATM 4444 O  O   . HOH G 3 .   ? 4.279   -6.159  23.507  1.00 26.15 ? 536 HOH A O   1 
HETATM 4445 O  O   . HOH G 3 .   ? 15.292  19.903  39.496  1.00 38.70 ? 537 HOH A O   1 
HETATM 4446 O  O   . HOH G 3 .   ? 3.555   19.327  48.429  1.00 36.26 ? 538 HOH A O   1 
HETATM 4447 O  O   . HOH G 3 .   ? -1.728  -7.620  37.565  1.00 28.04 ? 539 HOH A O   1 
HETATM 4448 O  O   . HOH G 3 .   ? 1.472   -8.153  49.664  1.00 35.47 ? 540 HOH A O   1 
HETATM 4449 O  O   . HOH G 3 .   ? 0.803   3.568   31.657  1.00 24.78 ? 541 HOH A O   1 
HETATM 4450 O  O   . HOH G 3 .   ? 18.763  14.118  45.802  1.00 26.22 ? 542 HOH A O   1 
HETATM 4451 O  O   . HOH G 3 .   ? 0.754   -6.660  28.797  1.00 34.24 ? 543 HOH A O   1 
HETATM 4452 O  O   . HOH G 3 .   ? 7.968   10.319  45.049  1.00 31.82 ? 544 HOH A O   1 
HETATM 4453 O  O   . HOH G 3 .   ? 26.122  6.479   48.320  1.00 28.22 ? 545 HOH A O   1 
HETATM 4454 O  O   . HOH G 3 .   ? 25.221  -5.569  27.815  1.00 40.43 ? 546 HOH A O   1 
HETATM 4455 O  O   . HOH G 3 .   ? 1.399   -16.090 28.600  1.00 27.64 ? 547 HOH A O   1 
HETATM 4456 O  O   . HOH G 3 .   ? 11.893  -22.428 39.662  1.00 40.12 ? 548 HOH A O   1 
HETATM 4457 O  O   . HOH G 3 .   ? 1.025   0.455   25.605  1.00 20.20 ? 549 HOH A O   1 
HETATM 4458 O  O   . HOH G 3 .   ? 3.974   0.502   36.295  1.00 18.46 ? 550 HOH A O   1 
HETATM 4459 O  O   . HOH G 3 .   ? -10.361 0.880   40.610  1.00 38.50 ? 551 HOH A O   1 
HETATM 4460 O  O   . HOH G 3 .   ? 2.865   -18.355 36.222  1.00 29.96 ? 552 HOH A O   1 
HETATM 4461 O  O   . HOH G 3 .   ? -1.792  -2.385  30.491  1.00 28.44 ? 553 HOH A O   1 
HETATM 4462 O  O   . HOH G 3 .   ? 3.077   -17.914 29.578  1.00 36.42 ? 554 HOH A O   1 
HETATM 4463 O  O   . HOH G 3 .   ? 4.333   -6.425  56.124  1.00 38.28 ? 555 HOH A O   1 
HETATM 4464 O  O   . HOH G 3 .   ? 10.400  -0.457  39.645  1.00 24.59 ? 556 HOH A O   1 
HETATM 4465 O  O   . HOH G 3 .   ? 16.481  12.668  38.674  1.00 27.59 ? 557 HOH A O   1 
HETATM 4466 O  O   . HOH G 3 .   ? 17.566  18.387  50.450  1.00 45.52 ? 558 HOH A O   1 
HETATM 4467 O  O   . HOH G 3 .   ? 18.341  -16.074 40.695  1.00 25.40 ? 559 HOH A O   1 
HETATM 4468 O  O   . HOH G 3 .   ? 22.990  8.553   27.192  1.00 41.31 ? 560 HOH A O   1 
HETATM 4469 O  O   . HOH G 3 .   ? 24.645  -0.343  25.659  1.00 33.74 ? 561 HOH A O   1 
HETATM 4470 O  O   . HOH G 3 .   ? -1.617  18.602  39.623  1.00 32.43 ? 562 HOH A O   1 
HETATM 4471 O  O   . HOH G 3 .   ? 23.733  -6.502  62.468  1.00 35.05 ? 563 HOH A O   1 
HETATM 4472 O  O   . HOH G 3 .   ? -11.489 10.446  50.137  1.00 50.00 ? 564 HOH A O   1 
HETATM 4473 O  O   . HOH G 3 .   ? -0.747  6.039   35.962  1.00 29.58 ? 565 HOH A O   1 
HETATM 4474 O  O   . HOH G 3 .   ? -3.544  17.726  37.712  1.00 32.61 ? 566 HOH A O   1 
HETATM 4475 O  O   . HOH G 3 .   ? 0.502   20.315  32.705  1.00 44.09 ? 567 HOH A O   1 
HETATM 4476 O  O   . HOH G 3 .   ? 5.992   -15.761 27.898  1.00 27.23 ? 568 HOH A O   1 
HETATM 4477 O  O   . HOH G 3 .   ? 8.176   -4.228  18.625  1.00 28.97 ? 569 HOH A O   1 
HETATM 4478 O  O   . HOH G 3 .   ? 10.411  11.439  26.732  1.00 21.55 ? 570 HOH A O   1 
HETATM 4479 O  O   . HOH G 3 .   ? 30.343  -2.138  33.713  1.00 32.22 ? 571 HOH A O   1 
HETATM 4480 O  O   . HOH G 3 .   ? 10.914  7.020   52.896  1.00 39.12 ? 572 HOH A O   1 
HETATM 4481 O  O   . HOH G 3 .   ? 9.642   -8.259  17.390  1.00 30.54 ? 573 HOH A O   1 
HETATM 4482 O  O   . HOH G 3 .   ? 6.300   -3.494  22.894  1.00 18.14 ? 574 HOH A O   1 
HETATM 4483 O  O   . HOH G 3 .   ? 17.940  9.573   32.773  1.00 37.04 ? 575 HOH A O   1 
HETATM 4484 O  O   . HOH G 3 .   ? 3.079   -14.629 42.252  1.00 25.43 ? 576 HOH A O   1 
HETATM 4485 O  O   . HOH G 3 .   ? 0.361   24.719  33.282  1.00 52.88 ? 577 HOH A O   1 
HETATM 4486 O  O   . HOH G 3 .   ? 26.979  -13.702 30.069  1.00 42.03 ? 578 HOH A O   1 
HETATM 4487 O  O   . HOH G 3 .   ? 9.494   -13.023 43.750  1.00 32.23 ? 579 HOH A O   1 
HETATM 4488 O  O   . HOH G 3 .   ? 12.845  -20.504 31.581  1.00 40.76 ? 580 HOH A O   1 
HETATM 4489 O  O   . HOH G 3 .   ? 8.736   -3.327  21.558  1.00 21.90 ? 581 HOH A O   1 
HETATM 4490 O  O   . HOH G 3 .   ? 20.298  12.230  44.422  1.00 34.24 ? 582 HOH A O   1 
HETATM 4491 O  O   . HOH G 3 .   ? 0.418   7.091   23.260  1.00 40.95 ? 583 HOH A O   1 
HETATM 4492 O  O   . HOH G 3 .   ? 6.238   1.032   20.603  1.00 23.22 ? 584 HOH A O   1 
HETATM 4493 O  O   . HOH G 3 .   ? -3.198  8.972   39.013  1.00 29.34 ? 585 HOH A O   1 
HETATM 4494 O  O   . HOH G 3 .   ? 20.321  7.464   24.349  1.00 44.16 ? 586 HOH A O   1 
HETATM 4495 O  O   . HOH G 3 .   ? 27.247  11.638  50.781  1.00 45.89 ? 587 HOH A O   1 
HETATM 4496 O  O   . HOH G 3 .   ? -9.016  1.425   38.654  1.00 32.37 ? 588 HOH A O   1 
HETATM 4497 O  O   . HOH G 3 .   ? 20.395  8.027   20.999  1.00 35.26 ? 589 HOH A O   1 
HETATM 4498 O  O   . HOH G 3 .   ? 22.046  6.387   54.596  1.00 30.17 ? 590 HOH A O   1 
HETATM 4499 O  O   . HOH G 3 .   ? 9.963   -10.563 51.987  1.00 25.52 ? 591 HOH A O   1 
HETATM 4500 O  O   . HOH G 3 .   ? 19.696  -5.504  60.012  1.00 30.54 ? 592 HOH A O   1 
HETATM 4501 O  O   . HOH G 3 .   ? 15.242  -2.670  18.379  1.00 37.59 ? 593 HOH A O   1 
HETATM 4502 O  O   . HOH G 3 .   ? 27.573  -0.206  30.230  1.00 37.29 ? 594 HOH A O   1 
HETATM 4503 O  O   . HOH G 3 .   ? -1.140  2.876   38.902  1.00 18.93 ? 595 HOH A O   1 
HETATM 4504 O  O   . HOH G 3 .   ? 14.422  0.015   20.147  1.00 31.15 ? 596 HOH A O   1 
HETATM 4505 O  O   . HOH G 3 .   ? 11.108  16.518  53.809  1.00 43.44 ? 597 HOH A O   1 
HETATM 4506 O  O   . HOH G 3 .   ? 14.641  10.836  33.193  1.00 22.91 ? 598 HOH A O   1 
HETATM 4507 O  O   . HOH G 3 .   ? 4.812   -13.706 45.840  1.00 31.11 ? 599 HOH A O   1 
HETATM 4508 O  O   . HOH G 3 .   ? 22.474  -6.778  57.785  1.00 34.89 ? 600 HOH A O   1 
HETATM 4509 O  O   . HOH G 3 .   ? 17.495  17.407  33.778  1.00 39.65 ? 601 HOH A O   1 
HETATM 4510 O  O   . HOH G 3 .   ? -5.430  15.103  36.228  1.00 37.69 ? 602 HOH A O   1 
HETATM 4511 O  O   . HOH G 3 .   ? 2.297   2.381   29.774  1.00 16.50 ? 603 HOH A O   1 
HETATM 4512 O  O   . HOH G 3 .   ? 29.516  0.948   31.535  1.00 40.66 ? 604 HOH A O   1 
HETATM 4513 O  O   . HOH G 3 .   ? 25.277  6.849   36.184  1.00 30.36 ? 605 HOH A O   1 
HETATM 4514 O  O   . HOH G 3 .   ? 27.356  -0.211  56.065  1.00 30.05 ? 606 HOH A O   1 
HETATM 4515 O  O   . HOH G 3 .   ? 10.076  -2.556  53.308  1.00 25.12 ? 607 HOH A O   1 
HETATM 4516 O  O   . HOH G 3 .   ? 20.109  -13.422 29.744  1.00 31.20 ? 608 HOH A O   1 
HETATM 4517 O  O   . HOH G 3 .   ? -0.119  4.424   23.722  1.00 31.40 ? 609 HOH A O   1 
HETATM 4518 O  O   . HOH G 3 .   ? 26.489  -9.227  51.067  1.00 32.35 ? 610 HOH A O   1 
HETATM 4519 O  O   . HOH G 3 .   ? 1.910   23.183  24.752  1.00 53.29 ? 611 HOH A O   1 
HETATM 4520 O  O   . HOH G 3 .   ? -1.331  6.244   42.992  1.00 29.53 ? 612 HOH A O   1 
HETATM 4521 O  O   . HOH G 3 .   ? 22.868  11.714  39.969  1.00 33.03 ? 613 HOH A O   1 
HETATM 4522 O  O   . HOH G 3 .   ? -1.237  -10.381 37.191  1.00 26.62 ? 614 HOH A O   1 
HETATM 4523 O  O   . HOH G 3 .   ? 13.430  5.173   24.043  1.00 27.10 ? 615 HOH A O   1 
HETATM 4524 O  O   . HOH G 3 .   ? 27.054  0.036   32.755  1.00 37.17 ? 616 HOH A O   1 
HETATM 4525 O  O   . HOH G 3 .   ? 12.736  21.517  45.941  1.00 37.88 ? 617 HOH A O   1 
HETATM 4526 O  O   . HOH G 3 .   ? -2.628  15.067  53.224  1.00 51.09 ? 618 HOH A O   1 
HETATM 4527 O  O   . HOH G 3 .   ? 6.604   -12.379 43.942  1.00 24.75 ? 619 HOH A O   1 
HETATM 4528 O  O   . HOH G 3 .   ? -6.105  -6.024  42.674  1.00 33.28 ? 620 HOH A O   1 
HETATM 4529 O  O   . HOH G 3 .   ? 11.247  -2.567  67.620  1.00 47.19 ? 621 HOH A O   1 
HETATM 4530 O  O   . HOH G 3 .   ? 22.970  3.157   30.581  1.00 21.23 ? 622 HOH A O   1 
HETATM 4531 O  O   . HOH G 3 .   ? 12.224  17.765  23.066  1.00 34.53 ? 623 HOH A O   1 
HETATM 4532 O  O   . HOH G 3 .   ? -0.033  6.842   38.932  1.00 25.70 ? 624 HOH A O   1 
HETATM 4533 O  O   . HOH G 3 .   ? 1.216   -3.519  37.949  1.00 24.89 ? 625 HOH A O   1 
HETATM 4534 O  O   . HOH G 3 .   ? 8.151   -3.339  42.570  1.00 17.25 ? 626 HOH A O   1 
HETATM 4535 O  O   . HOH G 3 .   ? 31.056  3.472   37.652  1.00 28.53 ? 627 HOH A O   1 
HETATM 4536 O  O   . HOH G 3 .   ? 18.887  1.901   46.110  1.00 24.23 ? 628 HOH A O   1 
HETATM 4537 O  O   . HOH G 3 .   ? 4.940   -18.754 40.826  1.00 31.56 ? 629 HOH A O   1 
HETATM 4538 O  O   . HOH G 3 .   ? 10.817  1.626   38.028  1.00 22.14 ? 630 HOH A O   1 
HETATM 4539 O  O   . HOH G 3 .   ? 5.637   5.062   21.580  1.00 26.61 ? 631 HOH A O   1 
HETATM 4540 O  O   . HOH G 3 .   ? -9.590  3.446   41.789  1.00 43.41 ? 632 HOH A O   1 
HETATM 4541 O  O   . HOH G 3 .   ? -6.604  -3.148  47.188  1.00 32.16 ? 633 HOH A O   1 
HETATM 4542 O  O   . HOH G 3 .   ? 3.200   -7.715  25.614  1.00 17.89 ? 634 HOH A O   1 
HETATM 4543 O  O   . HOH G 3 .   ? 9.513   16.747  24.091  1.00 38.49 ? 635 HOH A O   1 
HETATM 4544 O  O   . HOH G 3 .   ? -22.297 -21.379 24.720  1.00 35.28 ? 636 HOH A O   1 
HETATM 4545 O  O   . HOH G 3 .   ? 29.896  2.370   43.569  1.00 35.72 ? 637 HOH A O   1 
HETATM 4546 O  O   . HOH G 3 .   ? 22.441  -17.437 34.054  1.00 37.61 ? 638 HOH A O   1 
HETATM 4547 O  O   . HOH G 3 .   ? 16.311  -3.981  65.991  1.00 47.27 ? 639 HOH A O   1 
HETATM 4548 O  O   . HOH G 3 .   ? 26.358  10.307  42.517  1.00 30.53 ? 640 HOH A O   1 
HETATM 4549 O  O   . HOH G 3 .   ? -3.559  18.605  42.397  1.00 33.98 ? 641 HOH A O   1 
HETATM 4550 O  O   . HOH G 3 .   ? 13.705  -19.358 28.849  1.00 45.70 ? 642 HOH A O   1 
HETATM 4551 O  O   . HOH G 3 .   ? 29.702  -2.227  31.484  1.00 55.00 ? 643 HOH A O   1 
HETATM 4552 O  O   . HOH G 3 .   ? 5.785   -4.325  55.774  1.00 51.21 ? 644 HOH A O   1 
HETATM 4553 O  O   . HOH G 3 .   ? 5.099   -19.197 29.420  1.00 42.17 ? 645 HOH A O   1 
HETATM 4554 O  O   . HOH G 3 .   ? 10.671  0.700   21.551  1.00 40.86 ? 646 HOH A O   1 
HETATM 4555 O  O   . HOH G 3 .   ? 31.350  4.683   40.505  1.00 36.38 ? 647 HOH A O   1 
HETATM 4556 O  O   . HOH G 3 .   ? 24.212  -2.321  54.597  1.00 30.02 ? 648 HOH A O   1 
HETATM 4557 O  O   . HOH G 3 .   ? 17.438  12.897  36.026  1.00 25.83 ? 649 HOH A O   1 
HETATM 4558 O  O   . HOH G 3 .   ? 31.526  5.551   43.509  1.00 49.25 ? 650 HOH A O   1 
HETATM 4559 O  O   . HOH G 3 .   ? 9.664   -23.568 39.932  1.00 43.66 ? 651 HOH A O   1 
HETATM 4560 O  O   . HOH G 3 .   ? 30.322  -0.064  42.698  1.00 40.40 ? 652 HOH A O   1 
HETATM 4561 O  O   . HOH G 3 .   ? -6.784  -3.404  44.782  1.00 39.35 ? 653 HOH A O   1 
HETATM 4562 O  O   . HOH G 3 .   ? -2.110  7.003   40.024  1.00 47.77 ? 654 HOH A O   1 
HETATM 4563 O  O   . HOH G 3 .   ? 25.206  4.176   21.232  1.00 42.68 ? 655 HOH A O   1 
HETATM 4564 O  O   . HOH G 3 .   ? 23.134  7.885   32.451  1.00 42.67 ? 656 HOH A O   1 
HETATM 4565 O  O   . HOH G 3 .   ? 3.374   -20.001 34.085  1.00 35.77 ? 657 HOH A O   1 
HETATM 4566 O  O   . HOH G 3 .   ? 27.330  6.187   50.938  1.00 29.01 ? 658 HOH A O   1 
HETATM 4567 O  O   . HOH G 3 .   ? -0.054  6.856   33.714  1.00 36.74 ? 659 HOH A O   1 
HETATM 4568 O  O   . HOH G 3 .   ? 0.671   -7.104  26.479  1.00 30.22 ? 660 HOH A O   1 
HETATM 4569 O  O   . HOH G 3 .   ? 3.691   -17.048 43.323  1.00 37.89 ? 661 HOH A O   1 
HETATM 4570 O  O   . HOH G 3 .   ? 10.446  -15.052 41.919  1.00 34.68 ? 662 HOH A O   1 
HETATM 4571 O  O   . HOH G 3 .   ? -0.864  17.350  54.457  1.00 48.85 ? 663 HOH A O   1 
HETATM 4572 O  O   . HOH G 3 .   ? 10.022  -2.187  18.013  1.00 46.41 ? 664 HOH A O   1 
HETATM 4573 O  O   . HOH G 3 .   ? 8.445   -0.532  20.972  1.00 32.68 ? 665 HOH A O   1 
HETATM 4574 O  O   . HOH G 3 .   ? 24.438  6.991   55.007  1.00 30.13 ? 666 HOH A O   1 
HETATM 4575 O  O   . HOH G 3 .   ? 0.395   1.417   28.001  1.00 25.49 ? 667 HOH A O   1 
HETATM 4576 O  O   . HOH G 3 .   ? 16.845  19.717  34.636  1.00 40.25 ? 668 HOH A O   1 
HETATM 4577 O  O   . HOH G 3 .   ? 16.668  10.046  35.061  1.00 23.12 ? 669 HOH A O   1 
HETATM 4578 O  O   . HOH G 3 .   ? 23.913  -2.178  57.577  1.00 32.02 ? 670 HOH A O   1 
HETATM 4579 O  O   . HOH G 3 .   ? 0.141   -15.131 41.914  1.00 31.31 ? 671 HOH A O   1 
HETATM 4580 O  O   . HOH G 3 .   ? 27.324  -8.688  30.553  1.00 37.88 ? 672 HOH A O   1 
HETATM 4581 O  O   . HOH G 3 .   ? -1.783  4.138   30.359  1.00 26.80 ? 673 HOH A O   1 
HETATM 4582 O  O   . HOH G 3 .   ? 23.073  13.721  43.498  1.00 39.72 ? 674 HOH A O   1 
HETATM 4583 O  O   . HOH G 3 .   ? -1.199  -14.713 39.192  1.00 40.16 ? 675 HOH A O   1 
HETATM 4584 O  O   . HOH G 3 .   ? -1.438  -5.093  29.733  1.00 24.53 ? 676 HOH A O   1 
HETATM 4585 O  O   . HOH H 3 .   ? 1.023   -8.228  14.568  1.00 32.32 ? 501 HOH B O   1 
HETATM 4586 O  O   . HOH H 3 .   ? -6.773  -11.610 42.810  1.00 46.04 ? 502 HOH B O   1 
HETATM 4587 O  O   . HOH H 3 .   ? -29.922 -2.858  26.318  1.00 35.54 ? 503 HOH B O   1 
HETATM 4588 O  O   . HOH H 3 .   ? -29.834 -11.171 27.419  1.00 43.73 ? 504 HOH B O   1 
HETATM 4589 O  O   . HOH H 3 .   ? -5.151  21.968  13.284  1.00 42.49 ? 505 HOH B O   1 
HETATM 4590 O  O   . HOH H 3 .   ? -25.468 3.829   31.323  1.00 32.35 ? 506 HOH B O   1 
HETATM 4591 O  O   . HOH H 3 .   ? -27.647 -9.515  27.346  1.00 34.97 ? 507 HOH B O   1 
HETATM 4592 O  O   . HOH H 3 .   ? -3.990  19.907  16.154  1.00 37.04 ? 508 HOH B O   1 
HETATM 4593 O  O   . HOH H 3 .   ? -9.873  1.841   -1.131  1.00 38.24 ? 509 HOH B O   1 
HETATM 4594 O  O   . HOH H 3 .   ? -6.145  19.338  21.964  1.00 42.81 ? 510 HOH B O   1 
HETATM 4595 O  O   . HOH H 3 .   ? -10.202 3.367   15.414  1.00 18.56 ? 511 HOH B O   1 
HETATM 4596 O  O   . HOH H 3 .   ? -33.704 3.581   14.449  1.00 49.83 ? 512 HOH B O   1 
HETATM 4597 O  O   . HOH H 3 .   ? 0.634   14.519  18.756  1.00 28.15 ? 513 HOH B O   1 
HETATM 4598 O  O   . HOH H 3 .   ? -11.185 10.151  9.357   1.00 23.31 ? 514 HOH B O   1 
HETATM 4599 O  O   . HOH H 3 .   ? 4.968   7.011   20.287  1.00 43.88 ? 515 HOH B O   1 
HETATM 4600 O  O   . HOH H 3 .   ? -0.894  13.999  6.153   1.00 20.65 ? 516 HOH B O   1 
HETATM 4601 O  O   . HOH H 3 .   ? 3.508   -9.624  14.034  1.00 41.39 ? 517 HOH B O   1 
HETATM 4602 O  O   . HOH H 3 .   ? -10.061 -20.859 25.626  1.00 34.61 ? 518 HOH B O   1 
HETATM 4603 O  O   . HOH H 3 .   ? -15.506 -10.538 27.809  1.00 27.54 ? 519 HOH B O   1 
HETATM 4604 O  O   . HOH H 3 .   ? -18.224 7.489   10.306  1.00 23.66 ? 520 HOH B O   1 
HETATM 4605 O  O   . HOH H 3 .   ? -8.573  -1.406  33.108  1.00 31.18 ? 521 HOH B O   1 
HETATM 4606 O  O   . HOH H 3 .   ? 1.928   22.949  17.239  1.00 46.04 ? 522 HOH B O   1 
HETATM 4607 O  O   . HOH H 3 .   ? -26.208 -19.613 22.970  1.00 49.14 ? 523 HOH B O   1 
HETATM 4608 O  O   . HOH H 3 .   ? -12.134 21.363  22.926  1.00 34.02 ? 524 HOH B O   1 
HETATM 4609 O  O   . HOH H 3 .   ? -33.371 -7.455  10.270  1.00 31.91 ? 525 HOH B O   1 
HETATM 4610 O  O   . HOH H 3 .   ? -16.723 9.426   34.820  1.00 40.64 ? 526 HOH B O   1 
HETATM 4611 O  O   . HOH H 3 .   ? 9.344   6.993   18.631  1.00 47.65 ? 527 HOH B O   1 
HETATM 4612 O  O   . HOH H 3 .   ? 4.321   6.901   5.387   1.00 28.79 ? 528 HOH B O   1 
HETATM 4613 O  O   . HOH H 3 .   ? -4.359  -9.937  7.586   1.00 19.69 ? 529 HOH B O   1 
HETATM 4614 O  O   . HOH H 3 .   ? -0.285  -7.194  7.650   1.00 31.91 ? 530 HOH B O   1 
HETATM 4615 O  O   . HOH H 3 .   ? -8.239  -5.600  41.354  1.00 37.97 ? 531 HOH B O   1 
HETATM 4616 O  O   . HOH H 3 .   ? -13.118 11.265  2.147   1.00 35.40 ? 532 HOH B O   1 
HETATM 4617 O  O   . HOH H 3 .   ? -9.026  -11.591 12.682  1.00 18.73 ? 533 HOH B O   1 
HETATM 4618 O  O   . HOH H 3 .   ? -7.748  -15.764 30.087  1.00 39.28 ? 534 HOH B O   1 
HETATM 4619 O  O   . HOH H 3 .   ? -12.731 -13.383 5.582   1.00 23.36 ? 535 HOH B O   1 
HETATM 4620 O  O   . HOH H 3 .   ? -18.104 -0.851  36.127  1.00 35.36 ? 536 HOH B O   1 
HETATM 4621 O  O   . HOH H 3 .   ? -24.823 6.807   4.768   1.00 30.81 ? 537 HOH B O   1 
HETATM 4622 O  O   . HOH H 3 .   ? -1.389  8.214   16.819  1.00 25.06 ? 538 HOH B O   1 
HETATM 4623 O  O   . HOH H 3 .   ? -11.926 -3.816  38.219  1.00 39.42 ? 539 HOH B O   1 
HETATM 4624 O  O   . HOH H 3 .   ? -13.716 -2.418  16.912  1.00 21.38 ? 540 HOH B O   1 
HETATM 4625 O  O   . HOH H 3 .   ? 6.795   11.875  12.867  1.00 34.75 ? 541 HOH B O   1 
HETATM 4626 O  O   . HOH H 3 .   ? 21.271  -14.977 31.543  1.00 29.12 ? 542 HOH B O   1 
HETATM 4627 O  O   . HOH H 3 .   ? -31.770 -4.061  2.312   1.00 20.50 ? 543 HOH B O   1 
HETATM 4628 O  O   . HOH H 3 .   ? -17.664 19.313  11.249  1.00 37.46 ? 544 HOH B O   1 
HETATM 4629 O  O   . HOH H 3 .   ? -7.737  -0.605  20.211  1.00 16.04 ? 545 HOH B O   1 
HETATM 4630 O  O   . HOH H 3 .   ? -0.271  -12.392 12.582  1.00 32.47 ? 546 HOH B O   1 
HETATM 4631 O  O   . HOH H 3 .   ? -1.586  1.155   24.686  1.00 20.19 ? 547 HOH B O   1 
HETATM 4632 O  O   . HOH H 3 .   ? -4.952  3.047   24.630  1.00 23.83 ? 548 HOH B O   1 
HETATM 4633 O  O   . HOH H 3 .   ? -14.302 18.095  28.760  1.00 37.08 ? 549 HOH B O   1 
HETATM 4634 O  O   . HOH H 3 .   ? -4.572  14.454  18.058  1.00 30.40 ? 550 HOH B O   1 
HETATM 4635 O  O   . HOH H 3 .   ? -3.639  17.356  15.218  1.00 30.16 ? 551 HOH B O   1 
HETATM 4636 O  O   . HOH H 3 .   ? -15.059 10.256  29.042  1.00 24.72 ? 552 HOH B O   1 
HETATM 4637 O  O   . HOH H 3 .   ? 6.851   -17.452 24.474  1.00 44.49 ? 553 HOH B O   1 
HETATM 4638 O  O   . HOH H 3 .   ? -20.006 -18.943 17.148  1.00 24.53 ? 554 HOH B O   1 
HETATM 4639 O  O   . HOH H 3 .   ? -3.857  19.517  11.963  1.00 35.75 ? 555 HOH B O   1 
HETATM 4640 O  O   . HOH H 3 .   ? -14.673 3.675   2.985   1.00 27.65 ? 556 HOH B O   1 
HETATM 4641 O  O   . HOH H 3 .   ? -1.306  -8.317  19.549  1.00 19.80 ? 557 HOH B O   1 
HETATM 4642 O  O   . HOH H 3 .   ? -22.524 -10.078 -2.880  1.00 28.67 ? 558 HOH B O   1 
HETATM 4643 O  O   . HOH H 3 .   ? -32.866 7.510   18.197  1.00 43.98 ? 559 HOH B O   1 
HETATM 4644 O  O   . HOH H 3 .   ? -3.964  5.809   35.761  1.00 38.99 ? 560 HOH B O   1 
HETATM 4645 O  O   . HOH H 3 .   ? -2.843  1.829   17.395  1.00 14.78 ? 561 HOH B O   1 
HETATM 4646 O  O   . HOH H 3 .   ? -31.377 1.601   5.487   1.00 40.46 ? 562 HOH B O   1 
HETATM 4647 O  O   . HOH H 3 .   ? -31.760 2.055   20.315  1.00 30.16 ? 563 HOH B O   1 
HETATM 4648 O  O   . HOH H 3 .   ? -17.794 4.294   31.833  1.00 25.86 ? 564 HOH B O   1 
HETATM 4649 O  O   . HOH H 3 .   ? -0.389  0.359   18.433  1.00 16.44 ? 565 HOH B O   1 
HETATM 4650 O  O   . HOH H 3 .   ? -7.418  -8.728  0.837   1.00 37.64 ? 566 HOH B O   1 
HETATM 4651 O  O   . HOH H 3 .   ? -28.705 -0.966  27.032  1.00 36.25 ? 567 HOH B O   1 
HETATM 4652 O  O   . HOH H 3 .   ? -10.007 0.950   35.762  1.00 29.70 ? 568 HOH B O   1 
HETATM 4653 O  O   . HOH H 3 .   ? -22.986 -20.427 3.577   1.00 30.14 ? 569 HOH B O   1 
HETATM 4654 O  O   . HOH H 3 .   ? -4.769  0.414   30.834  1.00 25.12 ? 570 HOH B O   1 
HETATM 4655 O  O   . HOH H 3 .   ? -4.026  11.572  28.737  1.00 33.62 ? 571 HOH B O   1 
HETATM 4656 O  O   . HOH H 3 .   ? 5.406   2.856   14.237  1.00 33.21 ? 572 HOH B O   1 
HETATM 4657 O  O   . HOH H 3 .   ? -26.173 2.532   12.054  1.00 22.15 ? 573 HOH B O   1 
HETATM 4658 O  O   . HOH H 3 .   ? -2.952  -4.052  -9.160  1.00 28.29 ? 574 HOH B O   1 
HETATM 4659 O  O   . HOH H 3 .   ? -27.215 8.277   15.628  1.00 26.15 ? 575 HOH B O   1 
HETATM 4660 O  O   . HOH H 3 .   ? -20.568 7.470   18.014  1.00 21.40 ? 576 HOH B O   1 
HETATM 4661 O  O   . HOH H 3 .   ? -5.430  0.036   -5.965  1.00 30.60 ? 577 HOH B O   1 
HETATM 4662 O  O   . HOH H 3 .   ? -19.673 -13.984 -2.467  1.00 35.69 ? 578 HOH B O   1 
HETATM 4663 O  O   . HOH H 3 .   ? -22.552 15.476  21.076  1.00 34.88 ? 579 HOH B O   1 
HETATM 4664 O  O   . HOH H 3 .   ? -32.810 -6.180  17.596  1.00 28.43 ? 580 HOH B O   1 
HETATM 4665 O  O   . HOH H 3 .   ? -1.558  -10.939 20.052  1.00 24.92 ? 581 HOH B O   1 
HETATM 4666 O  O   . HOH H 3 .   ? -29.375 3.591   19.847  1.00 25.54 ? 582 HOH B O   1 
HETATM 4667 O  O   . HOH H 3 .   ? -3.456  1.032   38.091  1.00 21.08 ? 583 HOH B O   1 
HETATM 4668 O  O   . HOH H 3 .   ? 5.256   1.128   17.632  1.00 25.94 ? 584 HOH B O   1 
HETATM 4669 O  O   . HOH H 3 .   ? -17.013 19.369  24.021  1.00 29.95 ? 585 HOH B O   1 
HETATM 4670 O  O   . HOH H 3 .   ? -27.259 -16.638 18.431  1.00 32.76 ? 586 HOH B O   1 
HETATM 4671 O  O   . HOH H 3 .   ? -19.266 8.864   22.494  1.00 19.60 ? 587 HOH B O   1 
HETATM 4672 O  O   . HOH H 3 .   ? -20.481 -23.148 25.753  1.00 30.60 ? 588 HOH B O   1 
HETATM 4673 O  O   . HOH H 3 .   ? -25.982 1.925   1.305   1.00 21.24 ? 589 HOH B O   1 
HETATM 4674 O  O   . HOH H 3 .   ? -1.565  -2.505  26.218  1.00 25.09 ? 590 HOH B O   1 
HETATM 4675 O  O   . HOH H 3 .   ? -33.470 -1.375  12.946  1.00 23.31 ? 591 HOH B O   1 
HETATM 4676 O  O   . HOH H 3 .   ? 10.359  -17.884 22.577  1.00 36.09 ? 592 HOH B O   1 
HETATM 4677 O  O   . HOH H 3 .   ? -13.630 18.615  8.641   1.00 31.08 ? 593 HOH B O   1 
HETATM 4678 O  O   . HOH H 3 .   ? -29.627 -8.679  18.355  1.00 25.69 ? 594 HOH B O   1 
HETATM 4679 O  O   . HOH H 3 .   ? -9.769  -16.834 6.499   1.00 42.16 ? 595 HOH B O   1 
HETATM 4680 O  O   . HOH H 3 .   ? -3.328  5.311   19.868  1.00 28.07 ? 596 HOH B O   1 
HETATM 4681 O  O   . HOH H 3 .   ? -4.785  14.178  30.184  1.00 45.21 ? 597 HOH B O   1 
HETATM 4682 O  O   . HOH H 3 .   ? 20.387  -14.874 25.572  1.00 34.40 ? 598 HOH B O   1 
HETATM 4683 O  O   . HOH H 3 .   ? -13.408 -5.661  3.235   1.00 23.30 ? 599 HOH B O   1 
HETATM 4684 O  O   . HOH H 3 .   ? -1.546  16.978  17.305  1.00 33.28 ? 600 HOH B O   1 
HETATM 4685 O  O   . HOH H 3 .   ? -3.840  4.230   32.466  1.00 30.78 ? 601 HOH B O   1 
HETATM 4686 O  O   . HOH H 3 .   ? -7.664  -3.903  -1.070  1.00 26.80 ? 602 HOH B O   1 
HETATM 4687 O  O   . HOH H 3 .   ? -9.575  -7.627  0.908   1.00 37.65 ? 603 HOH B O   1 
HETATM 4688 O  O   . HOH H 3 .   ? -4.424  7.433   31.850  1.00 25.38 ? 604 HOH B O   1 
HETATM 4689 O  O   . HOH H 3 .   ? -5.281  -16.198 15.470  1.00 20.30 ? 605 HOH B O   1 
HETATM 4690 O  O   . HOH H 3 .   ? -4.732  -19.387 21.814  1.00 27.61 ? 606 HOH B O   1 
HETATM 4691 O  O   . HOH H 3 .   ? -6.655  -7.989  31.564  1.00 33.90 ? 607 HOH B O   1 
HETATM 4692 O  O   . HOH H 3 .   ? -22.210 6.979   23.063  1.00 26.91 ? 608 HOH B O   1 
HETATM 4693 O  O   . HOH H 3 .   ? -11.480 -15.253 13.877  1.00 22.30 ? 609 HOH B O   1 
HETATM 4694 O  O   . HOH H 3 .   ? -25.080 -10.738 -0.720  1.00 35.32 ? 610 HOH B O   1 
HETATM 4695 O  O   . HOH H 3 .   ? -23.336 -19.484 20.954  1.00 41.93 ? 611 HOH B O   1 
HETATM 4696 O  O   . HOH H 3 .   ? -6.188  2.007   26.665  1.00 20.48 ? 612 HOH B O   1 
HETATM 4697 O  O   . HOH H 3 .   ? -15.145 -12.261 -2.686  1.00 35.08 ? 613 HOH B O   1 
HETATM 4698 O  O   . HOH H 3 .   ? -12.146 -3.704  35.471  1.00 31.20 ? 614 HOH B O   1 
HETATM 4699 O  O   . HOH H 3 .   ? -9.607  5.002   34.415  1.00 32.03 ? 615 HOH B O   1 
HETATM 4700 O  O   . HOH H 3 .   ? -17.381 1.367   -6.715  1.00 37.24 ? 616 HOH B O   1 
HETATM 4701 O  O   . HOH H 3 .   ? -9.901  -3.489  33.959  1.00 28.16 ? 617 HOH B O   1 
HETATM 4702 O  O   . HOH H 3 .   ? -35.032 2.284   10.031  1.00 48.33 ? 618 HOH B O   1 
HETATM 4703 O  O   . HOH H 3 .   ? -15.803 -17.024 1.349   1.00 32.47 ? 619 HOH B O   1 
HETATM 4704 O  O   . HOH H 3 .   ? -3.222  4.468   39.121  1.00 43.08 ? 620 HOH B O   1 
HETATM 4705 O  O   . HOH H 3 .   ? -15.768 10.484  -0.922  1.00 49.19 ? 621 HOH B O   1 
HETATM 4706 O  O   . HOH H 3 .   ? -9.082  17.024  6.423   1.00 28.41 ? 622 HOH B O   1 
HETATM 4707 O  O   . HOH H 3 .   ? 4.954   -3.058  13.441  1.00 32.25 ? 623 HOH B O   1 
HETATM 4708 O  O   . HOH H 3 .   ? -22.690 -1.504  10.309  1.00 16.51 ? 624 HOH B O   1 
HETATM 4709 O  O   . HOH H 3 .   ? 17.843  -7.353  18.102  1.00 38.59 ? 625 HOH B O   1 
HETATM 4710 O  O   . HOH H 3 .   ? -29.894 -18.356 1.514   1.00 31.79 ? 626 HOH B O   1 
HETATM 4711 O  O   . HOH H 3 .   ? -17.650 18.497  8.606   1.00 38.61 ? 627 HOH B O   1 
HETATM 4712 O  O   . HOH H 3 .   ? -8.977  -14.174 13.714  1.00 19.55 ? 628 HOH B O   1 
HETATM 4713 O  O   . HOH H 3 .   ? -25.208 8.630   11.473  1.00 31.08 ? 629 HOH B O   1 
HETATM 4714 O  O   . HOH H 3 .   ? -25.432 -7.504  -5.502  1.00 29.31 ? 630 HOH B O   1 
HETATM 4715 O  O   . HOH H 3 .   ? -8.296  -14.648 5.438   1.00 38.03 ? 631 HOH B O   1 
HETATM 4716 O  O   . HOH H 3 .   ? -21.372 10.018  16.880  1.00 23.15 ? 632 HOH B O   1 
HETATM 4717 O  O   . HOH H 3 .   ? 6.657   8.665   5.879   1.00 46.90 ? 633 HOH B O   1 
HETATM 4718 O  O   . HOH H 3 .   ? 2.185   16.307  1.571   1.00 38.59 ? 634 HOH B O   1 
HETATM 4719 O  O   . HOH H 3 .   ? -2.786  5.040   13.234  1.00 25.16 ? 635 HOH B O   1 
HETATM 4720 O  O   . HOH H 3 .   ? 6.663   0.746   12.792  1.00 38.70 ? 636 HOH B O   1 
HETATM 4721 O  O   . HOH H 3 .   ? -29.220 -5.840  4.259   1.00 35.97 ? 637 HOH B O   1 
HETATM 4722 O  O   . HOH H 3 .   ? -11.615 -5.179  14.158  1.00 19.14 ? 638 HOH B O   1 
HETATM 4723 O  O   . HOH H 3 .   ? -14.572 -0.141  18.556  1.00 20.31 ? 639 HOH B O   1 
HETATM 4724 O  O   . HOH H 3 .   ? -29.206 -13.892 6.334   1.00 27.95 ? 640 HOH B O   1 
HETATM 4725 O  O   . HOH H 3 .   ? -2.348  17.659  12.748  1.00 29.57 ? 641 HOH B O   1 
HETATM 4726 O  O   . HOH H 3 .   ? -30.999 6.416   13.316  1.00 31.42 ? 642 HOH B O   1 
HETATM 4727 O  O   . HOH H 3 .   ? -3.602  -16.568 29.094  1.00 41.84 ? 643 HOH B O   1 
HETATM 4728 O  O   . HOH H 3 .   ? 0.418   5.511   21.127  1.00 32.97 ? 644 HOH B O   1 
HETATM 4729 O  O   . HOH H 3 .   ? 6.542   11.235  10.558  1.00 42.45 ? 645 HOH B O   1 
HETATM 4730 O  O   . HOH H 3 .   ? -19.962 5.639   32.628  1.00 37.04 ? 646 HOH B O   1 
HETATM 4731 O  O   . HOH H 3 .   ? 3.592   -6.588  14.241  1.00 39.78 ? 647 HOH B O   1 
HETATM 4732 O  O   . HOH H 3 .   ? -10.594 6.622   -2.188  1.00 47.58 ? 648 HOH B O   1 
HETATM 4733 O  O   . HOH H 3 .   ? -31.055 -11.083 17.281  1.00 30.62 ? 649 HOH B O   1 
HETATM 4734 O  O   . HOH H 3 .   ? -18.424 -20.754 2.759   1.00 35.13 ? 650 HOH B O   1 
HETATM 4735 O  O   . HOH H 3 .   ? 7.558   -2.507  14.432  1.00 47.23 ? 651 HOH B O   1 
HETATM 4736 O  O   . HOH H 3 .   ? 19.227  -14.083 23.397  1.00 39.30 ? 652 HOH B O   1 
HETATM 4737 O  O   . HOH H 3 .   ? 5.801   5.120   15.942  1.00 35.16 ? 653 HOH B O   1 
HETATM 4738 O  O   . HOH H 3 .   ? -9.382  -9.408  -0.573  1.00 48.19 ? 654 HOH B O   1 
HETATM 4739 O  O   . HOH H 3 .   ? -22.447 10.442  19.337  1.00 24.98 ? 655 HOH B O   1 
HETATM 4740 O  O   . HOH H 3 .   ? -22.872 9.262   5.442   1.00 38.32 ? 656 HOH B O   1 
HETATM 4741 O  O   . HOH H 3 .   ? -0.155  19.469  13.812  1.00 35.86 ? 657 HOH B O   1 
HETATM 4742 O  O   . HOH H 3 .   ? 2.050   -5.698  6.964   1.00 31.05 ? 658 HOH B O   1 
HETATM 4743 O  O   . HOH H 3 .   ? -23.470 -7.348  -12.089 1.00 38.83 ? 659 HOH B O   1 
HETATM 4744 O  O   . HOH H 3 .   ? -27.003 10.459  12.561  1.00 35.67 ? 660 HOH B O   1 
HETATM 4745 O  O   . HOH H 3 .   ? -12.312 -12.802 -6.353  1.00 45.80 ? 661 HOH B O   1 
HETATM 4746 O  O   . HOH H 3 .   ? -0.124  19.075  16.517  1.00 36.17 ? 662 HOH B O   1 
HETATM 4747 O  O   . HOH H 3 .   ? -12.038 -0.567  35.609  1.00 39.78 ? 663 HOH B O   1 
HETATM 4748 O  O   . HOH H 3 .   ? -21.261 7.999   20.609  1.00 23.96 ? 664 HOH B O   1 
HETATM 4749 O  O   . HOH H 3 .   ? -16.593 -19.468 1.690   1.00 34.00 ? 665 HOH B O   1 
HETATM 4750 O  O   . HOH H 3 .   ? -1.924  -0.717  28.178  1.00 20.91 ? 666 HOH B O   1 
HETATM 4751 O  O   . HOH H 3 .   ? -16.922 -14.748 -2.532  1.00 39.06 ? 667 HOH B O   1 
HETATM 4752 O  O   . HOH H 3 .   ? -25.210 7.509   23.503  1.00 36.64 ? 668 HOH B O   1 
HETATM 4753 O  O   . HOH H 3 .   ? -2.480  -16.167 15.875  1.00 26.93 ? 669 HOH B O   1 
HETATM 4754 O  O   . HOH H 3 .   ? 7.037   -18.030 26.693  1.00 41.53 ? 670 HOH B O   1 
HETATM 4755 O  O   . HOH H 3 .   ? -4.191  1.029   28.347  1.00 23.12 ? 671 HOH B O   1 
HETATM 4756 O  O   . HOH H 3 .   ? -33.782 5.814   13.294  1.00 53.13 ? 672 HOH B O   1 
HETATM 4757 O  O   . HOH H 3 .   ? -10.783 -12.062 -0.450  1.00 44.84 ? 673 HOH B O   1 
HETATM 4758 O  O   . HOH H 3 .   ? -27.962 8.678   10.927  1.00 38.28 ? 674 HOH B O   1 
HETATM 4759 O  O   . HOH H 3 .   ? -33.320 -9.798  8.912   1.00 26.56 ? 675 HOH B O   1 
HETATM 4760 O  O   . HOH H 3 .   ? -2.269  3.893   25.657  1.00 29.38 ? 676 HOH B O   1 
HETATM 4761 O  O   . HOH H 3 .   ? -29.711 6.002   21.495  1.00 37.45 ? 677 HOH B O   1 
HETATM 4762 O  O   . HOH H 3 .   ? -12.074 -12.979 -3.345  1.00 39.93 ? 678 HOH B O   1 
HETATM 4763 O  O   . HOH H 3 .   ? -22.191 18.097  19.805  1.00 50.70 ? 679 HOH B O   1 
HETATM 4764 O  O   . HOH H 3 .   ? -11.546 -14.844 3.628   1.00 36.10 ? 680 HOH B O   1 
HETATM 4765 O  O   . HOH H 3 .   ? -25.694 4.411   0.879   1.00 38.56 ? 681 HOH B O   1 
HETATM 4766 O  O   . HOH H 3 .   ? -31.150 2.625   2.798   1.00 37.82 ? 682 HOH B O   1 
HETATM 4767 O  O   . HOH H 3 .   ? -1.534  -5.148  27.062  1.00 24.07 ? 683 HOH B O   1 
HETATM 4768 O  O   . HOH H 3 .   ? -15.470 -11.938 -5.559  1.00 48.75 ? 684 HOH B O   1 
HETATM 4769 O  O   . HOH H 3 .   ? -23.423 5.226   -0.181  1.00 51.38 ? 685 HOH B O   1 
HETATM 4770 O  O   . HOH H 3 .   ? -2.115  3.067   28.033  1.00 28.15 ? 686 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   . ALA A 1   ? 0.6777 1.1452 1.1855 -0.4747 -0.1400 0.0481  36  ALA A N   
2    C CA  . ALA A 1   ? 0.6430 1.1305 1.1587 -0.4590 -0.1128 0.0485  36  ALA A CA  
3    C C   . ALA A 1   ? 0.6487 1.0738 1.0987 -0.4588 -0.1062 0.0569  36  ALA A C   
4    O O   . ALA A 1   ? 0.6762 1.0424 1.0751 -0.4668 -0.1240 0.0610  36  ALA A O   
5    C CB  . ALA A 1   ? 0.6532 1.1942 1.2130 -0.4740 -0.0913 0.0516  36  ALA A CB  
6    N N   . ALA A 2   ? 0.6242 1.0616 1.0752 -0.4477 -0.0814 0.0585  37  ALA A N   
7    C CA  . ALA A 2   ? 0.6332 1.0184 1.0274 -0.4497 -0.0709 0.0662  37  ALA A CA  
8    C C   . ALA A 2   ? 0.6116 1.0306 1.0250 -0.4414 -0.0413 0.0674  37  ALA A C   
9    O O   . ALA A 2   ? 0.5993 1.0686 1.0586 -0.4205 -0.0322 0.0601  37  ALA A O   
10   C CB  . ALA A 2   ? 0.6129 0.9478 0.9631 -0.4290 -0.0830 0.0632  37  ALA A CB  
11   N N   . PRO A 3   ? 0.6487 1.0410 1.0275 -0.4565 -0.0269 0.0762  38  PRO A N   
12   C CA  . PRO A 3   ? 0.6172 1.0276 0.9999 -0.4436 -0.0002 0.0771  38  PRO A CA  
13   C C   . PRO A 3   ? 0.5735 0.9634 0.9385 -0.4130 0.0006  0.0714  38  PRO A C   
14   O O   . PRO A 3   ? 0.5741 0.9117 0.8971 -0.4083 -0.0150 0.0708  38  PRO A O   
15   C CB  . PRO A 3   ? 0.6636 1.0325 0.9985 -0.4673 0.0084  0.0878  38  PRO A CB  
16   C CG  . PRO A 3   ? 0.7115 1.0719 1.0451 -0.4975 -0.0088 0.0930  38  PRO A CG  
17   C CD  . PRO A 3   ? 0.6960 1.0462 1.0351 -0.4873 -0.0345 0.0858  38  PRO A CD  
18   N N   . GLN A 4   ? 0.5378 0.9698 0.9353 -0.3918 0.0186  0.0670  39  GLN A N   
19   C CA  . GLN A 4   ? 0.4944 0.9161 0.8847 -0.3617 0.0185  0.0610  39  GLN A CA  
20   C C   . GLN A 4   ? 0.5026 0.8651 0.8335 -0.3616 0.0248  0.0659  39  GLN A C   
21   O O   . GLN A 4   ? 0.5596 0.9122 0.8710 -0.3731 0.0412  0.0719  39  GLN A O   
22   C CB  . GLN A 4   ? 0.4607 0.9398 0.8984 -0.3389 0.0352  0.0552  39  GLN A CB  
23   C CG  . GLN A 4   ? 0.4585 0.9962 0.9558 -0.3390 0.0291  0.0495  39  GLN A CG  
24   C CD  . GLN A 4   ? 0.4279 1.0168 0.9686 -0.3123 0.0419  0.0425  39  GLN A CD  
25   O OE1 . GLN A 4   ? 0.4130 0.9967 0.9395 -0.2971 0.0584  0.0432  39  GLN A OE1 
26   N NE2 . GLN A 4   ? 0.4222 1.0594 1.0152 -0.3060 0.0336  0.0356  39  GLN A NE2 
27   N N   . VAL A 5   ? 0.4877 0.8086 0.7876 -0.3491 0.0107  0.0634  40  VAL A N   
28   C CA  . VAL A 5   ? 0.4964 0.7589 0.7401 -0.3469 0.0148  0.0664  40  VAL A CA  
29   C C   . VAL A 5   ? 0.5426 0.8219 0.7941 -0.3270 0.0368  0.0648  40  VAL A C   
30   O O   . VAL A 5   ? 0.4860 0.7377 0.7047 -0.3321 0.0505  0.0688  40  VAL A O   
31   C CB  . VAL A 5   ? 0.4898 0.7070 0.7011 -0.3378 -0.0061 0.0636  40  VAL A CB  
32   C CG1 . VAL A 5   ? 0.5051 0.6577 0.6562 -0.3355 -0.0038 0.0653  40  VAL A CG1 
33   C CG2 . VAL A 5   ? 0.5202 0.7243 0.7260 -0.3552 -0.0286 0.0645  40  VAL A CG2 
34   N N   . ARG A 6   ? 0.4531 0.7764 0.7468 -0.3033 0.0391  0.0585  41  ARG A N   
35   C CA  . ARG A 6   ? 0.4125 0.7536 0.7166 -0.2799 0.0568  0.0557  41  ARG A CA  
36   C C   . ARG A 6   ? 0.4289 0.7136 0.6798 -0.2765 0.0628  0.0583  41  ARG A C   
37   O O   . ARG A 6   ? 0.4532 0.7331 0.6904 -0.2744 0.0813  0.0603  41  ARG A O   
38   C CB  . ARG A 6   ? 0.4320 0.8217 0.7690 -0.2813 0.0771  0.0563  41  ARG A CB  
39   C CG  . ARG A 6   ? 0.4129 0.8643 0.8098 -0.2734 0.0725  0.0504  41  ARG A CG  
40   C CD  . ARG A 6   ? 0.4320 0.9333 0.8619 -0.2713 0.0931  0.0501  41  ARG A CD  
41   N NE  . ARG A 6   ? 0.5215 1.0778 1.0076 -0.2611 0.0862  0.0431  41  ARG A NE  
42   C CZ  . ARG A 6   ? 0.4369 1.0449 0.9611 -0.2569 0.0999  0.0410  41  ARG A CZ  
43   N NH1 . ARG A 6   ? 0.5682 1.1835 1.0812 -0.2633 0.1228  0.0458  41  ARG A NH1 
44   N NH2 . ARG A 6   ? 0.3727 1.0252 0.9461 -0.2455 0.0901  0.0339  41  ARG A NH2 
45   N N   . THR A 7   ? 0.3971 0.6373 0.6163 -0.2751 0.0462  0.0578  42  THR A N   
46   C CA  . THR A 7   ? 0.4615 0.6473 0.6329 -0.2672 0.0488  0.0580  42  THR A CA  
47   C C   . THR A 7   ? 0.4283 0.6111 0.6053 -0.2477 0.0363  0.0543  42  THR A C   
48   O O   . THR A 7   ? 0.4575 0.6365 0.6370 -0.2514 0.0171  0.0538  42  THR A O   
49   C CB  . THR A 7   ? 0.6339 0.7532 0.7468 -0.2868 0.0399  0.0613  42  THR A CB  
50   O OG1 . THR A 7   ? 0.6345 0.7342 0.7374 -0.2931 0.0168  0.0603  42  THR A OG1 
51   C CG2 . THR A 7   ? 0.5120 0.6367 0.6212 -0.3093 0.0485  0.0666  42  THR A CG2 
52   N N   . SER A 8   ? 0.3608 0.5422 0.5377 -0.2225 0.0463  0.0513  43  SER A N   
53   C CA  . SER A 8   ? 0.4143 0.5842 0.5919 -0.1931 0.0348  0.0469  43  SER A CA  
54   C C   . SER A 8   ? 0.4461 0.5506 0.5709 -0.1927 0.0217  0.0460  43  SER A C   
55   O O   . SER A 8   ? 0.3682 0.4256 0.4488 -0.2049 0.0246  0.0469  43  SER A O   
56   C CB  . SER A 8   ? 0.3742 0.5497 0.5595 -0.1630 0.0476  0.0433  43  SER A CB  
57   O OG  . SER A 8   ? 0.3367 0.5746 0.5732 -0.1555 0.0554  0.0418  43  SER A OG  
58   N N   . ALA A 9   ? 0.3863 0.4879 0.5144 -0.1772 0.0070  0.0440  44  ALA A N   
59   C CA  . ALA A 9   ? 0.5075 0.5553 0.5904 -0.1684 -0.0042 0.0415  44  ALA A CA  
60   C C   . ALA A 9   ? 0.4737 0.4807 0.5222 -0.1533 0.0070  0.0384  44  ALA A C   
61   O O   . ALA A 9   ? 0.3807 0.4058 0.4471 -0.1418 0.0214  0.0381  44  ALA A O   
62   C CB  . ALA A 9   ? 0.3885 0.4519 0.4888 -0.1483 -0.0158 0.0404  44  ALA A CB  
63   N N   . PRO A 10  ? 0.4986 0.4508 0.4982 -0.1506 -0.0003 0.0350  45  PRO A N   
64   C CA  . PRO A 10  ? 0.5020 0.4180 0.4727 -0.1327 0.0084  0.0307  45  PRO A CA  
65   C C   . PRO A 10  ? 0.3958 0.3363 0.3946 -0.1046 0.0134  0.0296  45  PRO A C   
66   O O   . PRO A 10  ? 0.4313 0.3929 0.4496 -0.0949 0.0051  0.0305  45  PRO A O   
67   C CB  . PRO A 10  ? 0.5893 0.4502 0.5086 -0.1311 -0.0045 0.0256  45  PRO A CB  
68   C CG  . PRO A 10  ? 0.6609 0.5316 0.5842 -0.1424 -0.0204 0.0271  45  PRO A CG  
69   C CD  . PRO A 10  ? 0.5957 0.5244 0.5715 -0.1534 -0.0185 0.0331  45  PRO A CD  
70   N N   . GLY A 11  ? 0.4140 0.3493 0.4127 -0.0924 0.0261  0.0280  46  GLY A N   
71   C CA  . GLY A 11  ? 0.3535 0.3059 0.3756 -0.0665 0.0294  0.0271  46  GLY A CA  
72   C C   . GLY A 11  ? 0.3845 0.3034 0.3805 -0.0481 0.0235  0.0229  46  GLY A C   
73   O O   . GLY A 11  ? 0.3259 0.2209 0.3068 -0.0338 0.0294  0.0191  46  GLY A O   
74   N N   . TYR A 12  ? 0.2842 0.2023 0.2746 -0.0479 0.0121  0.0231  47  TYR A N   
75   C CA  . TYR A 12  ? 0.2757 0.1798 0.2548 -0.0277 0.0084  0.0203  47  TYR A CA  
76   C C   . TYR A 12  ? 0.3872 0.3206 0.3880 -0.0256 -0.0005 0.0250  47  TYR A C   
77   O O   . TYR A 12  ? 0.2939 0.2455 0.3058 -0.0406 -0.0071 0.0282  47  TYR A O   
78   C CB  . TYR A 12  ? 0.3546 0.2092 0.2838 -0.0260 0.0045  0.0127  47  TYR A CB  
79   C CG  . TYR A 12  ? 0.3358 0.1729 0.2375 -0.0405 -0.0071 0.0111  47  TYR A CG  
80   C CD1 . TYR A 12  ? 0.3661 0.1867 0.2510 -0.0633 -0.0099 0.0115  47  TYR A CD1 
81   C CD2 . TYR A 12  ? 0.3519 0.1889 0.2435 -0.0319 -0.0157 0.0094  47  TYR A CD2 
82   C CE1 . TYR A 12  ? 0.4618 0.2621 0.3196 -0.0765 -0.0232 0.0098  47  TYR A CE1 
83   C CE2 . TYR A 12  ? 0.3892 0.2067 0.2521 -0.0430 -0.0278 0.0069  47  TYR A CE2 
84   C CZ  . TYR A 12  ? 0.4107 0.2086 0.2569 -0.0650 -0.0326 0.0069  47  TYR A CZ  
85   O OH  . TYR A 12  ? 0.4347 0.2111 0.2523 -0.0764 -0.0472 0.0046  47  TYR A OH  
86   N N   . TYR A 13  ? 0.2989 0.2386 0.3082 -0.0074 -0.0008 0.0262  48  TYR A N   
87   C CA  . TYR A 13  ? 0.2995 0.2652 0.3278 -0.0037 -0.0087 0.0321  48  TYR A CA  
88   C C   . TYR A 13  ? 0.2212 0.1724 0.2298 0.0103  -0.0095 0.0306  48  TYR A C   
89   O O   . TYR A 13  ? 0.2382 0.1829 0.2491 0.0242  -0.0034 0.0290  48  TYR A O   
90   C CB  . TYR A 13  ? 0.2272 0.2275 0.2984 0.0031  -0.0081 0.0381  48  TYR A CB  
91   C CG  . TYR A 13  ? 0.1867 0.2107 0.2756 0.0046  -0.0185 0.0449  48  TYR A CG  
92   C CD1 . TYR A 13  ? 0.1690 0.1930 0.2576 0.0171  -0.0206 0.0491  48  TYR A CD1 
93   C CD2 . TYR A 13  ? 0.2125 0.2593 0.3185 -0.0075 -0.0272 0.0474  48  TYR A CD2 
94   C CE1 . TYR A 13  ? 0.1943 0.2367 0.2951 0.0171  -0.0308 0.0566  48  TYR A CE1 
95   C CE2 . TYR A 13  ? 0.1754 0.2398 0.2944 -0.0056 -0.0386 0.0535  48  TYR A CE2 
96   C CZ  . TYR A 13  ? 0.2511 0.3117 0.3659 0.0067  -0.0402 0.0585  48  TYR A CZ  
97   O OH  . TYR A 13  ? 0.2007 0.2750 0.3238 0.0074  -0.0521 0.0657  48  TYR A OH  
98   N N   . ARG A 14  ? 0.2372 0.1850 0.2270 0.0069  -0.0170 0.0308  49  ARG A N   
99   C CA  . ARG A 14  ? 0.2509 0.1866 0.2176 0.0193  -0.0163 0.0280  49  ARG A CA  
100  C C   . ARG A 14  ? 0.2392 0.2025 0.2261 0.0251  -0.0190 0.0372  49  ARG A C   
101  O O   . ARG A 14  ? 0.2257 0.2069 0.2256 0.0169  -0.0269 0.0437  49  ARG A O   
102  C CB  . ARG A 14  ? 0.2809 0.1913 0.2065 0.0143  -0.0227 0.0210  49  ARG A CB  
103  C CG  . ARG A 14  ? 0.3034 0.1963 0.2013 0.0304  -0.0190 0.0135  49  ARG A CG  
104  C CD  . ARG A 14  ? 0.3071 0.1674 0.1848 0.0351  -0.0151 0.0034  49  ARG A CD  
105  N NE  . ARG A 14  ? 0.3427 0.1713 0.1865 0.0228  -0.0232 -0.0029 49  ARG A NE  
106  C CZ  . ARG A 14  ? 0.3654 0.1582 0.1838 0.0210  -0.0237 -0.0108 49  ARG A CZ  
107  N NH1 . ARG A 14  ? 0.4096 0.1929 0.2318 0.0318  -0.0161 -0.0144 49  ARG A NH1 
108  N NH2 . ARG A 14  ? 0.4068 0.1688 0.1920 0.0079  -0.0337 -0.0153 49  ARG A NH2 
109  N N   . MET A 15  ? 0.2180 0.1832 0.2058 0.0385  -0.0133 0.0379  50  MET A N   
110  C CA  . MET A 15  ? 0.2055 0.1945 0.2101 0.0426  -0.0151 0.0481  50  MET A CA  
111  C C   . MET A 15  ? 0.2562 0.2426 0.2446 0.0541  -0.0086 0.0456  50  MET A C   
112  O O   . MET A 15  ? 0.2819 0.2567 0.2679 0.0636  -0.0022 0.0387  50  MET A O   
113  C CB  . MET A 15  ? 0.1994 0.2058 0.2424 0.0455  -0.0156 0.0558  50  MET A CB  
114  C CG  . MET A 15  ? 0.2368 0.2639 0.2957 0.0464  -0.0209 0.0681  50  MET A CG  
115  S SD  . MET A 15  ? 0.2096 0.2495 0.3091 0.0528  -0.0244 0.0757  50  MET A SD  
116  C CE  . MET A 15  ? 0.1913 0.2174 0.2810 0.0611  -0.0137 0.0661  50  MET A CE  
117  N N   . LEU A 16  ? 0.2771 0.2752 0.2542 0.0535  -0.0103 0.0510  51  LEU A N   
118  C CA  . LEU A 16  ? 0.3081 0.3130 0.2741 0.0638  -0.0028 0.0500  51  LEU A CA  
119  C C   . LEU A 16  ? 0.2727 0.2992 0.2716 0.0663  -0.0002 0.0615  51  LEU A C   
120  O O   . LEU A 16  ? 0.2476 0.2850 0.2698 0.0594  -0.0070 0.0725  51  LEU A O   
121  C CB  . LEU A 16  ? 0.2897 0.2994 0.2278 0.0615  -0.0048 0.0517  51  LEU A CB  
122  C CG  . LEU A 16  ? 0.2967 0.2809 0.1972 0.0603  -0.0096 0.0394  51  LEU A CG  
123  C CD1 . LEU A 16  ? 0.3191 0.3068 0.1882 0.0614  -0.0116 0.0399  51  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.3506 0.3122 0.2337 0.0715  -0.0046 0.0242  51  LEU A CD2 
125  N N   . LEU A 17  ? 0.2052 0.2366 0.2065 0.0766  0.0079  0.0582  52  LEU A N   
126  C CA  . LEU A 17  ? 0.1828 0.2345 0.2132 0.0776  0.0094  0.0698  52  LEU A CA  
127  C C   . LEU A 17  ? 0.2813 0.3488 0.3005 0.0844  0.0190  0.0680  52  LEU A C   
128  O O   . LEU A 17  ? 0.2483 0.3104 0.2648 0.0959  0.0248  0.0565  52  LEU A O   
129  C CB  . LEU A 17  ? 0.3085 0.3512 0.3635 0.0837  0.0087  0.0670  52  LEU A CB  
130  C CG  . LEU A 17  ? 0.1978 0.2531 0.2782 0.0786  0.0067  0.0738  52  LEU A CG  
131  C CD1 . LEU A 17  ? 0.2110 0.2670 0.3039 0.0664  -0.0031 0.0813  52  LEU A CD1 
132  C CD2 . LEU A 17  ? 0.1541 0.1918 0.2350 0.0780  0.0065  0.0564  52  LEU A CD2 
133  N N   . GLY A 18  ? 0.2519 0.3392 0.2640 0.0779  0.0205  0.0787  53  GLY A N   
134  C CA  . GLY A 18  ? 0.2167 0.3226 0.2138 0.0849  0.0316  0.0752  53  GLY A CA  
135  C C   . GLY A 18  ? 0.3163 0.4043 0.2788 0.0962  0.0346  0.0559  53  GLY A C   
136  O O   . GLY A 18  ? 0.2742 0.3437 0.2110 0.0928  0.0286  0.0514  53  GLY A O   
137  N N   . ASP A 19  ? 0.2484 0.3399 0.2099 0.1104  0.0421  0.0436  54  ASP A N   
138  C CA  . ASP A 19  ? 0.2628 0.3339 0.1905 0.1241  0.0429  0.0236  54  ASP A CA  
139  C C   . ASP A 19  ? 0.2616 0.2965 0.1875 0.1279  0.0359  0.0123  54  ASP A C   
140  O O   . ASP A 19  ? 0.3869 0.3960 0.2811 0.1375  0.0333  -0.0041 54  ASP A O   
141  C CB  . ASP A 19  ? 0.3148 0.4111 0.2421 0.1394  0.0539  0.0151  54  ASP A CB  
142  C CG  . ASP A 19  ? 0.3677 0.4911 0.2741 0.1400  0.0619  0.0185  54  ASP A CG  
143  O OD1 . ASP A 19  ? 0.3827 0.5040 0.2763 0.1274  0.0581  0.0295  54  ASP A OD1 
144  O OD2 . ASP A 19  ? 0.3734 0.5244 0.2800 0.1523  0.0725  0.0118  54  ASP A OD2 
145  N N   . PHE A 20  ? 0.2311 0.2619 0.1877 0.1211  0.0323  0.0203  55  PHE A N   
146  C CA  . PHE A 20  ? 0.2281 0.2258 0.1820 0.1237  0.0272  0.0109  55  PHE A CA  
147  C C   . PHE A 20  ? 0.3555 0.3329 0.2968 0.1107  0.0198  0.0130  55  PHE A C   
148  O O   . PHE A 20  ? 0.2866 0.2779 0.2357 0.0987  0.0167  0.0250  55  PHE A O   
149  C CB  . PHE A 20  ? 0.1999 0.2008 0.1896 0.1186  0.0255  0.0164  55  PHE A CB  
150  C CG  . PHE A 20  ? 0.2401 0.2566 0.2462 0.1180  0.0277  0.0131  55  PHE A CG  
151  C CD1 . PHE A 20  ? 0.2551 0.2829 0.2463 0.1291  0.0331  0.0051  55  PHE A CD1 
152  C CD2 . PHE A 20  ? 0.2276 0.2453 0.2628 0.1060  0.0222  0.0156  55  PHE A CD2 
153  C CE1 . PHE A 20  ? 0.3151 0.3585 0.3253 0.1284  0.0345  0.0027  55  PHE A CE1 
154  C CE2 . PHE A 20  ? 0.2927 0.3214 0.3433 0.1060  0.0224  0.0121  55  PHE A CE2 
155  C CZ  . PHE A 20  ? 0.2231 0.2655 0.2636 0.1171  0.0292  0.0068  55  PHE A CZ  
156  N N   . GLU A 21  ? 0.3533 0.2973 0.2765 0.1125  0.0162  0.0017  56  GLU A N   
157  C CA  . GLU A 21  ? 0.3110 0.2376 0.2280 0.0985  0.0099  0.0039  56  GLU A CA  
158  C C   . GLU A 21  ? 0.2810 0.1999 0.2218 0.0963  0.0103  0.0063  56  GLU A C   
159  O O   . GLU A 21  ? 0.2742 0.1809 0.2135 0.0990  0.0113  -0.0022 56  GLU A O   
160  C CB  . GLU A 21  ? 0.3385 0.2309 0.2121 0.0988  0.0047  -0.0095 56  GLU A CB  
161  C CG  . GLU A 21  ? 0.3430 0.2157 0.2105 0.0828  -0.0016 -0.0080 56  GLU A CG  
162  C CD  . GLU A 21  ? 0.3691 0.1977 0.1970 0.0841  -0.0068 -0.0218 56  GLU A CD  
163  O OE1 . GLU A 21  ? 0.3324 0.1408 0.1588 0.0895  -0.0047 -0.0275 56  GLU A OE1 
164  O OE2 . GLU A 21  ? 0.4154 0.2269 0.2116 0.0791  -0.0147 -0.0266 56  GLU A OE2 
165  N N   . ILE A 22  ? 0.2418 0.1747 0.2066 0.0847  0.0078  0.0172  57  ILE A N   
166  C CA  . ILE A 22  ? 0.2752 0.2043 0.2622 0.0828  0.0082  0.0196  57  ILE A CA  
167  C C   . ILE A 22  ? 0.2844 0.1999 0.2596 0.0692  0.0054  0.0176  57  ILE A C   
168  O O   . ILE A 22  ? 0.2355 0.1599 0.2062 0.0582  0.0005  0.0214  57  ILE A O   
169  C CB  . ILE A 22  ? 0.2487 0.2069 0.2743 0.0808  0.0062  0.0325  57  ILE A CB  
170  C CG1 . ILE A 22  ? 0.2442 0.2217 0.2792 0.0827  0.0064  0.0350  57  ILE A CG1 
171  C CG2 . ILE A 22  ? 0.2543 0.2126 0.2953 0.0720  0.0026  0.0260  57  ILE A CG2 
172  C CD1 . ILE A 22  ? 0.1878 0.1591 0.2209 0.0819  0.0071  0.0222  57  ILE A CD1 
173  N N   . THR A 23  ? 0.2589 0.1530 0.2288 0.0691  0.0080  0.0120  58  THR A N   
174  C CA  . THR A 23  ? 0.2834 0.1693 0.2476 0.0539  0.0070  0.0119  58  THR A CA  
175  C C   . THR A 23  ? 0.2721 0.1652 0.2617 0.0551  0.0118  0.0149  58  THR A C   
176  O O   . THR A 23  ? 0.2863 0.1623 0.2686 0.0616  0.0149  0.0088  58  THR A O   
177  C CB  . THR A 23  ? 0.2952 0.1415 0.2167 0.0496  0.0055  0.0015  58  THR A CB  
178  O OG1 . THR A 23  ? 0.3038 0.1406 0.1983 0.0535  0.0003  -0.0037 58  THR A OG1 
179  C CG2 . THR A 23  ? 0.3345 0.1774 0.2522 0.0292  0.0037  0.0039  58  THR A CG2 
180  N N   . ALA A 24  ? 0.2109 0.1330 0.2302 0.0476  0.0105  0.0227  59  ALA A N   
181  C CA  . ALA A 24  ? 0.2212 0.1502 0.2602 0.0482  0.0154  0.0236  59  ALA A CA  
182  C C   . ALA A 24  ? 0.3060 0.2146 0.3216 0.0343  0.0200  0.0187  59  ALA A C   
183  O O   . ALA A 24  ? 0.2505 0.1586 0.2541 0.0187  0.0164  0.0190  59  ALA A O   
184  C CB  . ALA A 24  ? 0.1586 0.1259 0.2356 0.0458  0.0113  0.0317  59  ALA A CB  
185  N N   . LEU A 25  ? 0.2636 0.1516 0.2692 0.0395  0.0269  0.0144  60  LEU A N   
186  C CA  . LEU A 25  ? 0.2586 0.1239 0.2392 0.0257  0.0322  0.0111  60  LEU A CA  
187  C C   . LEU A 25  ? 0.2825 0.1686 0.2861 0.0235  0.0408  0.0139  60  LEU A C   
188  O O   . LEU A 25  ? 0.2530 0.1360 0.2647 0.0391  0.0448  0.0124  60  LEU A O   
189  C CB  . LEU A 25  ? 0.3116 0.1291 0.2524 0.0337  0.0326  0.0028  60  LEU A CB  
190  C CG  . LEU A 25  ? 0.3480 0.1513 0.2657 0.0371  0.0235  -0.0027 60  LEU A CG  
191  C CD1 . LEU A 25  ? 0.2879 0.0929 0.1936 0.0395  0.0183  -0.0100 60  LEU A CD1 
192  C CD2 . LEU A 25  ? 0.3395 0.1311 0.2356 0.0183  0.0188  -0.0018 60  LEU A CD2 
193  N N   . SER A 26  ? 0.2795 0.1874 0.2933 0.0045  0.0435  0.0174  61  SER A N   
194  C CA  . SER A 26  ? 0.2297 0.1642 0.2669 0.0023  0.0531  0.0193  61  SER A CA  
195  C C   . SER A 26  ? 0.2577 0.1591 0.2631 -0.0019 0.0634  0.0160  61  SER A C   
196  O O   . SER A 26  ? 0.2898 0.1567 0.2582 -0.0165 0.0626  0.0145  61  SER A O   
197  C CB  . SER A 26  ? 0.2285 0.2016 0.2898 -0.0173 0.0527  0.0237  61  SER A CB  
198  O OG  . SER A 26  ? 0.2248 0.2258 0.3073 -0.0189 0.0638  0.0243  61  SER A OG  
199  N N   . ASP A 27  ? 0.2618 0.1694 0.2777 0.0117  0.0715  0.0147  62  ASP A N   
200  C CA  . ASP A 27  ? 0.3644 0.2459 0.3514 0.0062  0.0828  0.0127  62  ASP A CA  
201  C C   . ASP A 27  ? 0.3390 0.2575 0.3440 -0.0102 0.0951  0.0165  62  ASP A C   
202  O O   . ASP A 27  ? 0.3624 0.2627 0.3418 -0.0198 0.1064  0.0166  62  ASP A O   
203  C CB  . ASP A 27  ? 0.2846 0.1462 0.2660 0.0311  0.0848  0.0082  62  ASP A CB  
204  C CG  . ASP A 27  ? 0.3102 0.1285 0.2487 0.0274  0.0930  0.0051  62  ASP A CG  
205  O OD1 . ASP A 27  ? 0.3889 0.1657 0.2878 0.0158  0.0894  0.0035  62  ASP A OD1 
206  O OD2 . ASP A 27  ? 0.3712 0.1963 0.3135 0.0364  0.1025  0.0043  62  ASP A OD2 
207  N N   . GLY A 28  ? 0.2606 0.2301 0.3074 -0.0147 0.0927  0.0198  63  GLY A N   
208  C CA  . GLY A 28  ? 0.2600 0.2765 0.3345 -0.0264 0.1037  0.0222  63  GLY A CA  
209  C C   . GLY A 28  ? 0.2270 0.2869 0.3452 -0.0037 0.1026  0.0201  63  GLY A C   
210  O O   . GLY A 28  ? 0.2043 0.2593 0.3336 0.0162  0.0909  0.0189  63  GLY A O   
211  N N   . THR A 29  ? 0.2049 0.4453 0.2177 -0.0734 0.0292  0.0108  64  THR A N   
212  C CA  . THR A 29  ? 0.1885 0.4333 0.2130 -0.0593 0.0295  -0.0009 64  THR A CA  
213  C C   . THR A 29  ? 0.2114 0.4699 0.2245 -0.0464 0.0429  -0.0064 64  THR A C   
214  O O   . THR A 29  ? 0.2833 0.5525 0.2861 -0.0496 0.0537  0.0015  64  THR A O   
215  C CB  . THR A 29  ? 0.1797 0.4362 0.2347 -0.0601 0.0271  0.0039  64  THR A CB  
216  O OG1 . THR A 29  ? 0.1836 0.4653 0.2516 -0.0627 0.0380  0.0141  64  THR A OG1 
217  C CG2 . THR A 29  ? 0.2584 0.4990 0.3200 -0.0727 0.0146  0.0110  64  THR A CG2 
218  N N   . VAL A 30  ? 0.2434 0.4996 0.2561 -0.0312 0.0427  -0.0199 65  VAL A N   
219  C CA  . VAL A 30  ? 0.2555 0.5235 0.2561 -0.0163 0.0561  -0.0257 65  VAL A CA  
220  C C   . VAL A 30  ? 0.2485 0.5230 0.2657 -0.0015 0.0565  -0.0350 65  VAL A C   
221  O O   . VAL A 30  ? 0.2441 0.5038 0.2687 0.0004  0.0442  -0.0432 65  VAL A O   
222  C CB  . VAL A 30  ? 0.2585 0.5086 0.2241 -0.0095 0.0547  -0.0358 65  VAL A CB  
223  C CG1 . VAL A 30  ? 0.2742 0.5016 0.2374 -0.0069 0.0387  -0.0488 65  VAL A CG1 
224  C CG2 . VAL A 30  ? 0.3801 0.6384 0.3283 0.0078  0.0685  -0.0421 65  VAL A CG2 
225  N N   . ASP A 31  ? 0.2615 0.5574 0.2845 0.0093  0.0714  -0.0337 66  ASP A N   
226  C CA  . ASP A 31  ? 0.2706 0.5728 0.3084 0.0251  0.0722  -0.0428 66  ASP A CA  
227  C C   . ASP A 31  ? 0.3551 0.6388 0.3654 0.0422  0.0702  -0.0599 66  ASP A C   
228  O O   . ASP A 31  ? 0.3547 0.6368 0.3380 0.0496  0.0795  -0.0626 66  ASP A O   
229  C CB  . ASP A 31  ? 0.2962 0.6300 0.3533 0.0316  0.0895  -0.0351 66  ASP A CB  
230  C CG  . ASP A 31  ? 0.3817 0.7348 0.4688 0.0149  0.0901  -0.0189 66  ASP A CG  
231  O OD1 . ASP A 31  ? 0.3859 0.7321 0.4914 0.0061  0.0758  -0.0168 66  ASP A OD1 
232  O OD2 . ASP A 31  ? 0.4922 0.8666 0.5842 0.0109  0.1048  -0.0080 66  ASP A OD2 
233  N N   . LEU A 32  ? 0.3718 0.6393 0.3876 0.0488  0.0574  -0.0716 67  LEU A N   
234  C CA  . LEU A 32  ? 0.3314 0.5774 0.3228 0.0638  0.0515  -0.0889 67  LEU A CA  
235  C C   . LEU A 32  ? 0.3855 0.6344 0.3854 0.0825  0.0534  -0.0985 67  LEU A C   
236  O O   . LEU A 32  ? 0.3876 0.6421 0.4147 0.0805  0.0489  -0.0958 67  LEU A O   
237  C CB  . LEU A 32  ? 0.3130 0.5310 0.2995 0.0547  0.0325  -0.0961 67  LEU A CB  
238  C CG  . LEU A 32  ? 0.3565 0.5679 0.3324 0.0381  0.0286  -0.0888 67  LEU A CG  
239  C CD1 . LEU A 32  ? 0.3858 0.5721 0.3615 0.0300  0.0112  -0.0959 67  LEU A CD1 
240  C CD2 . LEU A 32  ? 0.3595 0.5721 0.3044 0.0449  0.0378  -0.0905 67  LEU A CD2 
241  N N   . PRO A 33  ? 0.3688 0.6126 0.3440 0.1020  0.0599  -0.1100 68  PRO A N   
242  C CA  . PRO A 33  ? 0.4135 0.6560 0.3920 0.1221  0.0609  -0.1210 68  PRO A CA  
243  C C   . PRO A 33  ? 0.5068 0.7184 0.4812 0.1245  0.0409  -0.1356 68  PRO A C   
244  O O   . PRO A 33  ? 0.4615 0.6517 0.4103 0.1385  0.0351  -0.1508 68  PRO A O   
245  C CB  . PRO A 33  ? 0.4684 0.7135 0.4161 0.1410  0.0756  -0.1267 68  PRO A CB  
246  C CG  . PRO A 33  ? 0.4514 0.6823 0.3712 0.1326  0.0723  -0.1268 68  PRO A CG  
247  C CD  . PRO A 33  ? 0.4444 0.6847 0.3857 0.1076  0.0687  -0.1118 68  PRO A CD  
248  N N   . VAL A 34  ? 0.3946 0.6019 0.3941 0.1101  0.0296  -0.1305 69  VAL A N   
249  C CA  . VAL A 34  ? 0.4027 0.5802 0.4019 0.1085  0.0112  -0.1418 69  VAL A CA  
250  C C   . VAL A 34  ? 0.4892 0.6545 0.4813 0.1300  0.0083  -0.1567 69  VAL A C   
251  O O   . VAL A 34  ? 0.4942 0.6311 0.4740 0.1340  -0.0056 -0.1705 69  VAL A O   
252  C CB  . VAL A 34  ? 0.4767 0.6532 0.5037 0.0912  0.0030  -0.1317 69  VAL A CB  
253  C CG1 . VAL A 34  ? 0.5622 0.7491 0.5931 0.0714  0.0059  -0.1172 69  VAL A CG1 
254  C CG2 . VAL A 34  ? 0.4845 0.6781 0.5353 0.0984  0.0082  -0.1267 69  VAL A CG2 
255  N N   . ASP A 35  ? 0.4566 0.6431 0.4574 0.1443  0.0211  -0.1544 70  ASP A N   
256  C CA  . ASP A 35  ? 0.4922 0.6674 0.4853 0.1666  0.0192  -0.1682 70  ASP A CA  
257  C C   . ASP A 35  ? 0.5640 0.7216 0.5198 0.1827  0.0194  -0.1828 70  ASP A C   
258  O O   . ASP A 35  ? 0.6277 0.7609 0.5698 0.1973  0.0095  -0.1982 70  ASP A O   
259  C CB  . ASP A 35  ? 0.4835 0.6891 0.4962 0.1788  0.0345  -0.1614 70  ASP A CB  
260  C CG  . ASP A 35  ? 0.4818 0.7167 0.4894 0.1816  0.0553  -0.1521 70  ASP A CG  
261  O OD1 . ASP A 35  ? 0.5626 0.8016 0.5642 0.1657  0.0577  -0.1436 70  ASP A OD1 
262  O OD2 . ASP A 35  ? 0.6373 0.8907 0.6467 0.2001  0.0699  -0.1528 70  ASP A OD2 
263  N N   . LYS A 36  ? 0.5133 0.6809 0.4506 0.1811  0.0299  -0.1783 71  LYS A N   
264  C CA  . LYS A 36  ? 0.6332 0.7812 0.5310 0.1959  0.0287  -0.1918 71  LYS A CA  
265  C C   . LYS A 36  ? 0.5932 0.7109 0.4774 0.1852  0.0083  -0.2013 71  LYS A C   
266  O O   . LYS A 36  ? 0.7185 0.8122 0.5724 0.1989  0.0003  -0.2167 71  LYS A O   
267  C CB  . LYS A 36  ? 0.6319 0.8008 0.5128 0.1990  0.0486  -0.1826 71  LYS A CB  
268  C CG  . LYS A 36  ? 0.5928 0.7890 0.4798 0.2157  0.0708  -0.1769 71  LYS A CG  
269  C CD  . LYS A 36  ? 0.6766 0.9053 0.5747 0.2045  0.0906  -0.1580 71  LYS A CD  
270  C CE  . LYS A 36  ? 0.7490 0.9732 0.6083 0.2112  0.1022  -0.1581 71  LYS A CE  
271  N NZ  . LYS A 36  ? 0.7899 0.9872 0.6259 0.2001  0.0854  -0.1640 71  LYS A NZ  
272  N N   . ARG A 37  ? 0.5802 0.6979 0.4861 0.1620  -0.0006 -0.1928 72  ARG A N   
273  C CA  . ARG A 37  ? 0.5882 0.6824 0.4830 0.1513  -0.0172 -0.2001 72  ARG A CA  
274  C C   . ARG A 37  ? 0.5506 0.6195 0.4596 0.1458  -0.0365 -0.2095 72  ARG A C   
275  O O   . ARG A 37  ? 0.5280 0.5724 0.4239 0.1452  -0.0518 -0.2219 72  ARG A O   
276  C CB  . ARG A 37  ? 0.6359 0.7441 0.5407 0.1295  -0.0140 -0.1850 72  ARG A CB  
277  C CG  . ARG A 37  ? 0.6366 0.7698 0.5302 0.1316  0.0056  -0.1733 72  ARG A CG  
278  C CD  . ARG A 37  ? 0.6878 0.8133 0.5425 0.1510  0.0116  -0.1833 72  ARG A CD  
279  N NE  . ARG A 37  ? 0.8203 0.9286 0.6508 0.1466  0.0014  -0.1891 72  ARG A NE  
280  C CZ  . ARG A 37  ? 0.7826 0.8706 0.5777 0.1633  -0.0040 -0.2039 72  ARG A CZ  
281  N NH1 . ARG A 37  ? 0.8672 0.9462 0.6493 0.1825  -0.0006 -0.2107 72  ARG A NH1 
282  N NH2 . ARG A 37  ? 0.7771 0.8499 0.5579 0.1551  -0.0141 -0.2035 72  ARG A NH2 
283  N N   . LEU A 38  ? 0.4744 0.5478 0.4102 0.1417  -0.0365 -0.2037 73  LEU A N   
284  C CA  . LEU A 38  ? 0.4690 0.5165 0.4174 0.1368  -0.0532 -0.2116 73  LEU A CA  
285  C C   . LEU A 38  ? 0.5463 0.5696 0.4752 0.1576  -0.0618 -0.2306 73  LEU A C   
286  O O   . LEU A 38  ? 0.5714 0.6025 0.4876 0.1778  -0.0520 -0.2345 73  LEU A O   
287  C CB  . LEU A 38  ? 0.4468 0.5038 0.4247 0.1292  -0.0503 -0.2001 73  LEU A CB  
288  C CG  . LEU A 38  ? 0.4291 0.4973 0.4285 0.1059  -0.0490 -0.1835 73  LEU A CG  
289  C CD1 . LEU A 38  ? 0.3937 0.4751 0.4167 0.1040  -0.0437 -0.1724 73  LEU A CD1 
290  C CD2 . LEU A 38  ? 0.4274 0.4708 0.4325 0.0904  -0.0639 -0.1868 73  LEU A CD2 
291  N N   . ASN A 39  ? 0.5567 0.5500 0.4844 0.1526  -0.0803 -0.2423 74  ASN A N   
292  C CA  . ASN A 39  ? 0.5625 0.5274 0.4701 0.1706  -0.0922 -0.2616 74  ASN A CA  
293  C C   . ASN A 39  ? 0.5706 0.5240 0.4922 0.1768  -0.0955 -0.2639 74  ASN A C   
294  O O   . ASN A 39  ? 0.6072 0.5335 0.5374 0.1707  -0.1110 -0.2712 74  ASN A O   
295  C CB  . ASN A 39  ? 0.5725 0.5121 0.4763 0.1601  -0.1108 -0.2697 74  ASN A CB  
296  C CG  . ASN A 39  ? 0.6151 0.5631 0.5006 0.1580  -0.1084 -0.2670 74  ASN A CG  
297  O OD1 . ASN A 39  ? 0.6634 0.6231 0.5253 0.1729  -0.0966 -0.2665 74  ASN A OD1 
298  N ND2 . ASN A 39  ? 0.5911 0.5326 0.4877 0.1398  -0.1189 -0.2638 74  ASN A ND2 
299  N N   . GLN A 40  ? 0.5701 0.5445 0.4940 0.1899  -0.0806 -0.2578 75  GLN A N   
300  C CA  . GLN A 40  ? 0.5782 0.5452 0.5145 0.1984  -0.0822 -0.2590 75  GLN A CA  
301  C C   . GLN A 40  ? 0.5868 0.5796 0.5181 0.2190  -0.0645 -0.2559 75  GLN A C   
302  O O   . GLN A 40  ? 0.5768 0.5969 0.5030 0.2203  -0.0495 -0.2480 75  GLN A O   
303  C CB  . GLN A 40  ? 0.5815 0.5527 0.5498 0.1775  -0.0841 -0.2450 75  GLN A CB  
304  C CG  . GLN A 40  ? 0.5118 0.5203 0.4981 0.1711  -0.0677 -0.2268 75  GLN A CG  
305  C CD  . GLN A 40  ? 0.5442 0.5515 0.5574 0.1552  -0.0712 -0.2149 75  GLN A CD  
306  O OE1 . GLN A 40  ? 0.5219 0.5002 0.5397 0.1506  -0.0841 -0.2201 75  GLN A OE1 
307  N NE2 . GLN A 40  ? 0.4574 0.4943 0.4876 0.1466  -0.0600 -0.1987 75  GLN A NE2 
308  N N   . PRO A 41  ? 0.6071 0.5915 0.5400 0.2355  -0.0657 -0.2619 76  PRO A N   
309  C CA  . PRO A 41  ? 0.6156 0.6272 0.5473 0.2560  -0.0479 -0.2587 76  PRO A CA  
310  C C   . PRO A 41  ? 0.5891 0.6410 0.5498 0.2433  -0.0329 -0.2387 76  PRO A C   
311  O O   . PRO A 41  ? 0.5630 0.6169 0.5485 0.2242  -0.0383 -0.2283 76  PRO A O   
312  C CB  . PRO A 41  ? 0.6405 0.6325 0.5739 0.2724  -0.0555 -0.2679 76  PRO A CB  
313  C CG  . PRO A 41  ? 0.6586 0.6072 0.5814 0.2651  -0.0772 -0.2799 76  PRO A CG  
314  C CD  . PRO A 41  ? 0.6570 0.6046 0.5891 0.2387  -0.0832 -0.2736 76  PRO A CD  
315  N N   . ALA A 42  ? 0.5771 0.6597 0.5335 0.2542  -0.0138 -0.2332 77  ALA A N   
316  C CA  . ALA A 42  ? 0.5948 0.7171 0.5800 0.2438  0.0009  -0.2147 77  ALA A CA  
317  C C   . ALA A 42  ? 0.5577 0.6886 0.5740 0.2434  -0.0020 -0.2085 77  ALA A C   
318  O O   . ALA A 42  ? 0.5254 0.6744 0.5677 0.2249  -0.0007 -0.1938 77  ALA A O   
319  C CB  . ALA A 42  ? 0.6725 0.8251 0.6487 0.2594  0.0231  -0.2111 77  ALA A CB  
320  N N   . PRO A 43  ? 0.5570 0.6753 0.5711 0.2636  -0.0060 -0.2187 78  PRO A N   
321  C CA  . PRO A 43  ? 0.5770 0.6998 0.6194 0.2628  -0.0111 -0.2131 78  PRO A CA  
322  C C   . PRO A 43  ? 0.5197 0.6242 0.5756 0.2382  -0.0260 -0.2064 78  PRO A C   
323  O O   . PRO A 43  ? 0.4943 0.6155 0.5771 0.2276  -0.0256 -0.1936 78  PRO A O   
324  C CB  . PRO A 43  ? 0.5841 0.6807 0.6104 0.2872  -0.0185 -0.2294 78  PRO A CB  
325  C CG  . PRO A 43  ? 0.6124 0.7147 0.6122 0.3073  -0.0064 -0.2382 78  PRO A CG  
326  C CD  . PRO A 43  ? 0.6182 0.7220 0.6037 0.2910  -0.0037 -0.2347 78  PRO A CD  
327  N N   . LYS A 44  ? 0.5287 0.5981 0.5660 0.2293  -0.0394 -0.2150 79  LYS A N   
328  C CA  . LYS A 44  ? 0.5078 0.5584 0.5564 0.2060  -0.0517 -0.2086 79  LYS A CA  
329  C C   . LYS A 44  ? 0.4718 0.5493 0.5361 0.1851  -0.0440 -0.1918 79  LYS A C   
330  O O   . LYS A 44  ? 0.4476 0.5285 0.5320 0.1717  -0.0472 -0.1802 79  LYS A O   
331  C CB  . LYS A 44  ? 0.5268 0.5395 0.5548 0.2004  -0.0655 -0.2210 79  LYS A CB  
332  C CG  . LYS A 44  ? 0.6020 0.5761 0.6261 0.2063  -0.0807 -0.2316 79  LYS A CG  
333  C CD  . LYS A 44  ? 0.6388 0.5790 0.6531 0.1919  -0.0949 -0.2390 79  LYS A CD  
334  C CE  . LYS A 44  ? 0.6718 0.5770 0.6927 0.1868  -0.1084 -0.2415 79  LYS A CE  
335  N NZ  . LYS A 44  ? 0.5914 0.5065 0.6351 0.1708  -0.1055 -0.2244 79  LYS A NZ  
336  N N   . THR A 45  ? 0.4648 0.5596 0.5177 0.1831  -0.0341 -0.1903 80  THR A N   
337  C CA  . THR A 45  ? 0.4317 0.5480 0.4957 0.1629  -0.0277 -0.1751 80  THR A CA  
338  C C   . THR A 45  ? 0.4117 0.5627 0.5019 0.1620  -0.0173 -0.1609 80  THR A C   
339  O O   . THR A 45  ? 0.4015 0.5587 0.5087 0.1441  -0.0198 -0.1481 80  THR A O   
340  C CB  . THR A 45  ? 0.4358 0.5600 0.4783 0.1628  -0.0196 -0.1775 80  THR A CB  
341  O OG1 . THR A 45  ? 0.4525 0.5442 0.4738 0.1612  -0.0323 -0.1904 80  THR A OG1 
342  C CG2 . THR A 45  ? 0.4037 0.5488 0.4559 0.1424  -0.0130 -0.1617 80  THR A CG2 
343  N N   . GLN A 46  ? 0.4330 0.6067 0.5275 0.1816  -0.0057 -0.1630 81  GLN A N   
344  C CA  . GLN A 46  ? 0.4463 0.6541 0.5708 0.1816  0.0027  -0.1504 81  GLN A CA  
345  C C   . GLN A 46  ? 0.4125 0.6072 0.5559 0.1762  -0.0108 -0.1468 81  GLN A C   
346  O O   . GLN A 46  ? 0.4489 0.6600 0.6146 0.1631  -0.0113 -0.1334 81  GLN A O   
347  C CB  . GLN A 46  ? 0.4283 0.6607 0.5574 0.2060  0.0164  -0.1546 81  GLN A CB  
348  C CG  . GLN A 46  ? 0.5266 0.7338 0.6406 0.2280  0.0094  -0.1709 81  GLN A CG  
349  C CD  . GLN A 46  ? 0.7206 0.9519 0.8498 0.2518  0.0194  -0.1729 81  GLN A CD  
350  O OE1 . GLN A 46  ? 0.7469 1.0066 0.8762 0.2639  0.0373  -0.1713 81  GLN A OE1 
351  N NE2 . GLN A 46  ? 0.5774 0.7958 0.7186 0.2593  0.0078  -0.1766 81  GLN A NE2 
352  N N   . SER A 47  ? 0.4973 0.6605 0.6304 0.1869  -0.0224 -0.1589 82  SER A N   
353  C CA  . SER A 47  ? 0.5047 0.6493 0.6507 0.1824  -0.0356 -0.1560 82  SER A CA  
354  C C   . SER A 47  ? 0.3937 0.5270 0.5436 0.1567  -0.0426 -0.1449 82  SER A C   
355  O O   . SER A 47  ? 0.3763 0.5196 0.5454 0.1482  -0.0452 -0.1332 82  SER A O   
356  C CB  . SER A 47  ? 0.4503 0.5560 0.5785 0.1950  -0.0471 -0.1712 82  SER A CB  
357  O OG  . SER A 47  ? 0.5602 0.6449 0.6979 0.1916  -0.0593 -0.1683 82  SER A OG  
358  N N   . ALA A 48  ? 0.3927 0.5057 0.5242 0.1450  -0.0458 -0.1484 83  ALA A N   
359  C CA  . ALA A 48  ? 0.3881 0.4871 0.5213 0.1219  -0.0522 -0.1388 83  ALA A CA  
360  C C   . ALA A 48  ? 0.4079 0.5380 0.5556 0.1090  -0.0442 -0.1231 83  ALA A C   
361  O O   . ALA A 48  ? 0.3273 0.4534 0.4857 0.0958  -0.0495 -0.1120 83  ALA A O   
362  C CB  . ALA A 48  ? 0.3945 0.4714 0.5078 0.1136  -0.0558 -0.1464 83  ALA A CB  
363  N N   . LEU A 49  ? 0.3392 0.4985 0.4857 0.1130  -0.0315 -0.1220 84  LEU A N   
364  C CA  . LEU A 49  ? 0.3817 0.5700 0.5415 0.1003  -0.0236 -0.1073 84  LEU A CA  
365  C C   . LEU A 49  ? 0.3724 0.5797 0.5591 0.1028  -0.0247 -0.0985 84  LEU A C   
366  O O   . LEU A 49  ? 0.3511 0.5630 0.5495 0.0879  -0.0284 -0.0861 84  LEU A O   
367  C CB  . LEU A 49  ? 0.3819 0.5961 0.5340 0.1061  -0.0085 -0.1083 84  LEU A CB  
368  C CG  . LEU A 49  ? 0.4586 0.6610 0.5855 0.0985  -0.0068 -0.1122 84  LEU A CG  
369  C CD1 . LEU A 49  ? 0.4906 0.7220 0.6128 0.1013  0.0094  -0.1078 84  LEU A CD1 
370  C CD2 . LEU A 49  ? 0.4815 0.6667 0.6057 0.0766  -0.0154 -0.1046 84  LEU A CD2 
371  N N   . ALA A 50  ? 0.3231 0.5401 0.5194 0.1225  -0.0227 -0.1052 85  ALA A N   
372  C CA  . ALA A 50  ? 0.3172 0.5528 0.5413 0.1264  -0.0254 -0.0979 85  ALA A CA  
373  C C   . ALA A 50  ? 0.3157 0.5212 0.5409 0.1188  -0.0418 -0.0949 85  ALA A C   
374  O O   . ALA A 50  ? 0.3038 0.5196 0.5481 0.1127  -0.0469 -0.0846 85  ALA A O   
375  C CB  . ALA A 50  ? 0.3376 0.5889 0.5710 0.1509  -0.0198 -0.1067 85  ALA A CB  
376  N N   . LYS A 51  ? 0.4027 0.5697 0.6072 0.1190  -0.0502 -0.1035 86  LYS A N   
377  C CA  . LYS A 51  ? 0.3621 0.4968 0.5639 0.1108  -0.0638 -0.0998 86  LYS A CA  
378  C C   . LYS A 51  ? 0.3077 0.4433 0.5114 0.0892  -0.0653 -0.0859 86  LYS A C   
379  O O   . LYS A 51  ? 0.3477 0.4746 0.5589 0.0838  -0.0738 -0.0774 86  LYS A O   
380  C CB  . LYS A 51  ? 0.3906 0.4850 0.5703 0.1117  -0.0703 -0.1107 86  LYS A CB  
381  C CG  . LYS A 51  ? 0.5467 0.6042 0.7221 0.1068  -0.0828 -0.1080 86  LYS A CG  
382  C CD  . LYS A 51  ? 0.6005 0.6199 0.7567 0.1060  -0.0879 -0.1185 86  LYS A CD  
383  C CE  . LYS A 51  ? 0.6804 0.6624 0.8305 0.0950  -0.0971 -0.1124 86  LYS A CE  
384  N NZ  . LYS A 51  ? 0.6710 0.6253 0.8074 0.0833  -0.0984 -0.1169 86  LYS A NZ  
385  N N   . SER A 52  ? 0.3034 0.4477 0.4981 0.0778  -0.0575 -0.0836 87  SER A N   
386  C CA  . SER A 52  ? 0.3335 0.4805 0.5283 0.0583  -0.0577 -0.0706 87  SER A CA  
387  C C   . SER A 52  ? 0.3124 0.4982 0.5261 0.0553  -0.0506 -0.0606 87  SER A C   
388  O O   . SER A 52  ? 0.2433 0.4348 0.4552 0.0396  -0.0489 -0.0505 87  SER A O   
389  C CB  . SER A 52  ? 0.3284 0.4625 0.5036 0.0473  -0.0543 -0.0730 87  SER A CB  
390  O OG  . SER A 52  ? 0.4707 0.5674 0.6338 0.0432  -0.0629 -0.0769 87  SER A OG  
391  N N   . PHE A 53  ? 0.2633 0.4755 0.4960 0.0700  -0.0465 -0.0631 88  PHE A N   
392  C CA  . PHE A 53  ? 0.2649 0.5164 0.5216 0.0679  -0.0395 -0.0536 88  PHE A CA  
393  C C   . PHE A 53  ? 0.3125 0.5853 0.5627 0.0611  -0.0251 -0.0509 88  PHE A C   
394  O O   . PHE A 53  ? 0.3243 0.6204 0.5876 0.0504  -0.0206 -0.0397 88  PHE A O   
395  C CB  . PHE A 53  ? 0.2831 0.5322 0.5520 0.0547  -0.0503 -0.0409 88  PHE A CB  
396  C CG  . PHE A 53  ? 0.2497 0.4762 0.5224 0.0622  -0.0648 -0.0429 88  PHE A CG  
397  C CD1 . PHE A 53  ? 0.2557 0.5027 0.5542 0.0753  -0.0683 -0.0434 88  PHE A CD1 
398  C CD2 . PHE A 53  ? 0.2922 0.4763 0.5426 0.0572  -0.0742 -0.0447 88  PHE A CD2 
399  C CE1 . PHE A 53  ? 0.2734 0.4980 0.5734 0.0836  -0.0823 -0.0456 88  PHE A CE1 
400  C CE2 . PHE A 53  ? 0.3119 0.4724 0.5629 0.0650  -0.0869 -0.0462 88  PHE A CE2 
401  C CZ  . PHE A 53  ? 0.2786 0.4587 0.5532 0.0786  -0.0915 -0.0469 88  PHE A CZ  
402  N N   . GLN A 54  ? 0.2650 0.5286 0.4942 0.0679  -0.0185 -0.0612 89  GLN A N   
403  C CA  . GLN A 54  ? 0.3630 0.6417 0.5804 0.0634  -0.0054 -0.0599 89  GLN A CA  
404  C C   . GLN A 54  ? 0.3805 0.6797 0.5985 0.0827  0.0078  -0.0684 89  GLN A C   
405  O O   . GLN A 54  ? 0.3644 0.6589 0.5857 0.0999  0.0055  -0.0780 89  GLN A O   
406  C CB  . GLN A 54  ? 0.3782 0.6274 0.5667 0.0545  -0.0091 -0.0647 89  GLN A CB  
407  C CG  . GLN A 54  ? 0.3850 0.6170 0.5692 0.0342  -0.0178 -0.0547 89  GLN A CG  
408  C CD  . GLN A 54  ? 0.5185 0.7208 0.6781 0.0278  -0.0223 -0.0611 89  GLN A CD  
409  O OE1 . GLN A 54  ? 0.4873 0.6709 0.6369 0.0375  -0.0259 -0.0736 89  GLN A OE1 
410  N NE2 . GLN A 54  ? 0.4933 0.6913 0.6443 0.0115  -0.0226 -0.0526 89  GLN A NE2 
411  N N   . LYS A 55  ? 0.4015 0.7219 0.6142 0.0805  0.0223  -0.0645 90  LYS A N   
412  C CA  . LYS A 55  ? 0.4872 0.8281 0.6971 0.0984  0.0380  -0.0706 90  LYS A CA  
413  C C   . LYS A 55  ? 0.4873 0.8147 0.6629 0.0991  0.0446  -0.0771 90  LYS A C   
414  O O   . LYS A 55  ? 0.5278 0.8335 0.6858 0.0853  0.0369  -0.0765 90  LYS A O   
415  C CB  . LYS A 55  ? 0.5364 0.9194 0.7759 0.0975  0.0516  -0.0586 90  LYS A CB  
416  C CG  . LYS A 55  ? 0.5885 0.9831 0.8358 0.0749  0.0530  -0.0432 90  LYS A CG  
417  C CD  . LYS A 55  ? 0.5482 0.9840 0.8179 0.0753  0.0713  -0.0331 90  LYS A CD  
418  C CE  . LYS A 55  ? 0.5570 0.9977 0.8011 0.0812  0.0896  -0.0354 90  LYS A CE  
419  N NZ  . LYS A 55  ? 0.4240 0.9046 0.6902 0.0841  0.1102  -0.0257 90  LYS A NZ  
420  N N   . ALA A 56  ? 0.5565 0.8967 0.7222 0.1167  0.0590  -0.0835 91  ALA A N   
421  C CA  . ALA A 56  ? 0.5335 0.8541 0.6624 0.1243  0.0620  -0.0945 91  ALA A CA  
422  C C   . ALA A 56  ? 0.5195 0.8380 0.6304 0.1086  0.0658  -0.0875 91  ALA A C   
423  O O   . ALA A 56  ? 0.5245 0.8150 0.6104 0.1044  0.0561  -0.0951 91  ALA A O   
424  C CB  . ALA A 56  ? 0.6593 0.9947 0.7806 0.1484  0.0778  -0.1018 91  ALA A CB  
425  N N   . PRO A 57  ? 0.5530 0.8985 0.6748 0.0995  0.0790  -0.0736 92  PRO A N   
426  C CA  . PRO A 57  ? 0.5001 0.8392 0.6035 0.0833  0.0801  -0.0667 92  PRO A CA  
427  C C   . PRO A 57  ? 0.3734 0.6975 0.4862 0.0632  0.0636  -0.0606 92  PRO A C   
428  O O   . PRO A 57  ? 0.4240 0.7648 0.5612 0.0504  0.0637  -0.0474 92  PRO A O   
429  C CB  . PRO A 57  ? 0.5006 0.8734 0.6174 0.0795  0.0992  -0.0527 92  PRO A CB  
430  C CG  . PRO A 57  ? 0.5062 0.9024 0.6421 0.0981  0.1109  -0.0553 92  PRO A CG  
431  C CD  . PRO A 57  ? 0.5236 0.9067 0.6737 0.1043  0.0947  -0.0640 92  PRO A CD  
432  N N   . LEU A 58  ? 0.3572 0.6499 0.4526 0.0609  0.0492  -0.0701 93  LEU A N   
433  C CA  . LEU A 58  ? 0.2679 0.5445 0.3722 0.0440  0.0344  -0.0647 93  LEU A CA  
434  C C   . LEU A 58  ? 0.2710 0.5487 0.3662 0.0261  0.0361  -0.0535 93  LEU A C   
435  O O   . LEU A 58  ? 0.2523 0.5180 0.3219 0.0253  0.0370  -0.0580 93  LEU A O   
436  C CB  . LEU A 58  ? 0.4333 0.6772 0.5241 0.0471  0.0204  -0.0778 93  LEU A CB  
437  C CG  . LEU A 58  ? 0.3757 0.6004 0.4786 0.0354  0.0059  -0.0747 93  LEU A CG  
438  C CD1 . LEU A 58  ? 0.4564 0.6969 0.5867 0.0343  0.0055  -0.0655 93  LEU A CD1 
439  C CD2 . LEU A 58  ? 0.4169 0.6126 0.5112 0.0426  -0.0054 -0.0888 93  LEU A CD2 
440  N N   . GLU A 59  ? 0.2335 0.5244 0.3483 0.0125  0.0358  -0.0393 94  GLU A N   
441  C CA  . GLU A 59  ? 0.2139 0.5016 0.3186 -0.0048 0.0354  -0.0287 94  GLU A CA  
442  C C   . GLU A 59  ? 0.2073 0.4646 0.2987 -0.0129 0.0214  -0.0327 94  GLU A C   
443  O O   . GLU A 59  ? 0.2009 0.4465 0.3050 -0.0184 0.0108  -0.0305 94  GLU A O   
444  C CB  . GLU A 59  ? 0.2299 0.5355 0.3588 -0.0172 0.0359  -0.0134 94  GLU A CB  
445  C CG  . GLU A 59  ? 0.1858 0.4820 0.3036 -0.0355 0.0320  -0.0026 94  GLU A CG  
446  C CD  . GLU A 59  ? 0.2556 0.5718 0.3946 -0.0470 0.0345  0.0124  94  GLU A CD  
447  O OE1 . GLU A 59  ? 0.2346 0.5675 0.4016 -0.0429 0.0337  0.0144  94  GLU A OE1 
448  O OE2 . GLU A 59  ? 0.2069 0.5213 0.3348 -0.0601 0.0361  0.0218  94  GLU A OE2 
449  N N   . THR A 60  ? 0.2138 0.4578 0.2799 -0.0134 0.0214  -0.0384 95  THR A N   
450  C CA  . THR A 60  ? 0.2112 0.4280 0.2667 -0.0181 0.0091  -0.0450 95  THR A CA  
451  C C   . THR A 60  ? 0.1989 0.4092 0.2432 -0.0336 0.0072  -0.0354 95  THR A C   
452  O O   . THR A 60  ? 0.2033 0.4207 0.2311 -0.0348 0.0145  -0.0327 95  THR A O   
453  C CB  . THR A 60  ? 0.2306 0.4353 0.2674 -0.0053 0.0077  -0.0611 95  THR A CB  
454  O OG1 . THR A 60  ? 0.2454 0.4557 0.2895 0.0108  0.0104  -0.0700 95  THR A OG1 
455  C CG2 . THR A 60  ? 0.2281 0.4062 0.2599 -0.0110 -0.0055 -0.0680 95  THR A CG2 
456  N N   . SER A 61  ? 0.1857 0.3812 0.2370 -0.0447 -0.0023 -0.0300 96  SER A N   
457  C CA  . SER A 61  ? 0.1768 0.3659 0.2146 -0.0576 -0.0033 -0.0216 96  SER A CA  
458  C C   . SER A 61  ? 0.1829 0.3561 0.2019 -0.0562 -0.0074 -0.0312 96  SER A C   
459  O O   . SER A 61  ? 0.1928 0.3565 0.2112 -0.0475 -0.0118 -0.0442 96  SER A O   
460  C CB  . SER A 61  ? 0.3047 0.4847 0.3526 -0.0701 -0.0099 -0.0098 96  SER A CB  
461  O OG  . SER A 61  ? 0.2911 0.4592 0.3534 -0.0683 -0.0173 -0.0122 96  SER A OG  
462  N N   . VAL A 62  ? 0.1791 0.3503 0.1821 -0.0644 -0.0061 -0.0250 97  VAL A N   
463  C CA  . VAL A 62  ? 0.1846 0.3432 0.1696 -0.0638 -0.0103 -0.0327 97  VAL A CA  
464  C C   . VAL A 62  ? 0.2253 0.3731 0.2076 -0.0771 -0.0147 -0.0227 97  VAL A C   
465  O O   . VAL A 62  ? 0.1823 0.3361 0.1584 -0.0847 -0.0105 -0.0106 97  VAL A O   
466  C CB  . VAL A 62  ? 0.1983 0.3658 0.1609 -0.0574 -0.0028 -0.0351 97  VAL A CB  
467  C CG1 . VAL A 62  ? 0.2047 0.3581 0.1477 -0.0569 -0.0095 -0.0429 97  VAL A CG1 
468  C CG2 . VAL A 62  ? 0.2366 0.4156 0.1995 -0.0426 0.0041  -0.0437 97  VAL A CG2 
469  N N   . THR A 63  ? 0.2799 0.2848 0.2215 0.0239  0.0048  -0.0358 98  THR A N   
470  C CA  . THR A 63  ? 0.2063 0.2015 0.1556 0.0222  -0.0007 -0.0317 98  THR A CA  
471  C C   . THR A 63  ? 0.2362 0.2124 0.1787 0.0167  -0.0039 -0.0237 98  THR A C   
472  O O   . THR A 63  ? 0.2379 0.2033 0.1682 0.0169  -0.0051 -0.0229 98  THR A O   
473  C CB  . THR A 63  ? 0.2509 0.2418 0.1999 0.0349  -0.0042 -0.0372 98  THR A CB  
474  O OG1 . THR A 63  ? 0.1872 0.1992 0.1447 0.0424  -0.0029 -0.0447 98  THR A OG1 
475  C CG2 . THR A 63  ? 0.2282 0.2116 0.1817 0.0342  -0.0081 -0.0347 98  THR A CG2 
476  N N   . GLY A 64  ? 0.2418 0.2142 0.1925 0.0120  -0.0061 -0.0184 99  GLY A N   
477  C CA  . GLY A 64  ? 0.2617 0.2219 0.2123 0.0108  -0.0092 -0.0113 99  GLY A CA  
478  C C   . GLY A 64  ? 0.2557 0.2114 0.2111 0.0180  -0.0095 -0.0127 99  GLY A C   
479  O O   . GLY A 64  ? 0.1942 0.1532 0.1514 0.0218  -0.0092 -0.0186 99  GLY A O   
480  N N   . TYR A 65  ? 0.2456 0.1961 0.2030 0.0197  -0.0099 -0.0073 100 TYR A N   
481  C CA  . TYR A 65  ? 0.2340 0.1820 0.1923 0.0272  -0.0075 -0.0087 100 TYR A CA  
482  C C   . TYR A 65  ? 0.2563 0.2046 0.2242 0.0293  -0.0063 -0.0035 100 TYR A C   
483  O O   . TYR A 65  ? 0.2442 0.1969 0.2191 0.0262  -0.0074 0.0041  100 TYR A O   
484  C CB  . TYR A 65  ? 0.2036 0.1479 0.1538 0.0292  -0.0065 -0.0075 100 TYR A CB  
485  C CG  . TYR A 65  ? 0.2563 0.1972 0.1961 0.0321  -0.0084 -0.0142 100 TYR A CG  
486  C CD1 . TYR A 65  ? 0.2580 0.1986 0.1930 0.0399  -0.0089 -0.0201 100 TYR A CD1 
487  C CD2 . TYR A 65  ? 0.2444 0.1828 0.1784 0.0287  -0.0103 -0.0151 100 TYR A CD2 
488  C CE1 . TYR A 65  ? 0.2398 0.1806 0.1687 0.0455  -0.0115 -0.0259 100 TYR A CE1 
489  C CE2 . TYR A 65  ? 0.2611 0.1980 0.1866 0.0353  -0.0112 -0.0226 100 TYR A CE2 
490  C CZ  . TYR A 65  ? 0.2646 0.2042 0.1900 0.0442  -0.0119 -0.0274 100 TYR A CZ  
491  O OH  . TYR A 65  ? 0.2078 0.1491 0.1283 0.0533  -0.0136 -0.0343 100 TYR A OH  
492  N N   . LEU A 66  ? 0.2190 0.1626 0.1868 0.0355  -0.0047 -0.0080 101 LEU A N   
493  C CA  . LEU A 66  ? 0.2767 0.2181 0.2518 0.0422  -0.0026 -0.0057 101 LEU A CA  
494  C C   . LEU A 66  ? 0.3017 0.2482 0.2747 0.0507  0.0048  -0.0060 101 LEU A C   
495  O O   . LEU A 66  ? 0.2611 0.2040 0.2211 0.0534  0.0069  -0.0114 101 LEU A O   
496  C CB  . LEU A 66  ? 0.2475 0.1747 0.2187 0.0440  -0.0058 -0.0119 101 LEU A CB  
497  C CG  . LEU A 66  ? 0.3112 0.2274 0.2874 0.0520  -0.0063 -0.0105 101 LEU A CG  
498  C CD1 . LEU A 66  ? 0.3575 0.2747 0.3444 0.0476  -0.0114 -0.0001 101 LEU A CD1 
499  C CD2 . LEU A 66  ? 0.2276 0.1230 0.1936 0.0513  -0.0108 -0.0188 101 LEU A CD2 
500  N N   . VAL A 67  ? 0.2382 0.1957 0.2243 0.0549  0.0088  0.0008  102 VAL A N   
501  C CA  . VAL A 67  ? 0.2359 0.2044 0.2227 0.0619  0.0185  0.0025  102 VAL A CA  
502  C C   . VAL A 67  ? 0.2385 0.2100 0.2348 0.0755  0.0233  0.0011  102 VAL A C   
503  O O   . VAL A 67  ? 0.2517 0.2325 0.2667 0.0771  0.0203  0.0075  102 VAL A O   
504  C CB  . VAL A 67  ? 0.1913 0.1772 0.1890 0.0530  0.0202  0.0133  102 VAL A CB  
505  C CG1 . VAL A 67  ? 0.2324 0.2324 0.2306 0.0578  0.0322  0.0168  102 VAL A CG1 
506  C CG2 . VAL A 67  ? 0.2527 0.2287 0.2382 0.0410  0.0136  0.0137  102 VAL A CG2 
507  N N   . ASN A 68  ? 0.2317 0.1939 0.2135 0.0866  0.0297  -0.0079 103 ASN A N   
508  C CA  . ASN A 68  ? 0.2767 0.2400 0.2636 0.1035  0.0365  -0.0115 103 ASN A CA  
509  C C   . ASN A 68  ? 0.3039 0.2895 0.2914 0.1096  0.0514  -0.0085 103 ASN A C   
510  O O   . ASN A 68  ? 0.3199 0.2978 0.2840 0.1117  0.0572  -0.0144 103 ASN A O   
511  C CB  . ASN A 68  ? 0.3671 0.2996 0.3327 0.1115  0.0326  -0.0253 103 ASN A CB  
512  C CG  . ASN A 68  ? 0.3458 0.2734 0.3158 0.1281  0.0368  -0.0300 103 ASN A CG  
513  O OD1 . ASN A 68  ? 0.3205 0.2721 0.3047 0.1378  0.0474  -0.0257 103 ASN A OD1 
514  N ND2 . ASN A 68  ? 0.3475 0.2468 0.3070 0.1273  0.0277  -0.0380 103 ASN A ND2 
515  N N   . THR A 69  ? 0.2956 0.3110 0.3098 0.1112  0.0571  0.0020  104 THR A N   
516  C CA  . THR A 69  ? 0.3102 0.3535 0.3294 0.1142  0.0730  0.0075  104 THR A CA  
517  C C   . THR A 69  ? 0.3069 0.3531 0.3195 0.1368  0.0869  -0.0015 104 THR A C   
518  O O   . THR A 69  ? 0.3160 0.3864 0.3288 0.1408  0.1032  0.0020  104 THR A O   
519  C CB  . THR A 69  ? 0.3191 0.3992 0.3734 0.1059  0.0738  0.0226  104 THR A CB  
520  O OG1 . THR A 69  ? 0.2794 0.3741 0.3592 0.1216  0.0734  0.0229  104 THR A OG1 
521  C CG2 . THR A 69  ? 0.2486 0.3206 0.3059 0.0850  0.0583  0.0295  104 THR A CG2 
522  N N   . GLY A 70  ? 0.3408 0.3598 0.3444 0.1472  0.0792  -0.0133 105 GLY A N   
523  C CA  . GLY A 70  ? 0.3358 0.3509 0.3338 0.1604  0.0847  -0.0229 105 GLY A CA  
524  C C   . GLY A 70  ? 0.3601 0.3930 0.3893 0.1718  0.0844  -0.0194 105 GLY A C   
525  O O   . GLY A 70  ? 0.3934 0.4120 0.4180 0.1844  0.0843  -0.0291 105 GLY A O   
526  N N   . SER A 71  ? 0.3006 0.3620 0.3609 0.1671  0.0821  -0.0055 106 SER A N   
527  C CA  . SER A 71  ? 0.3771 0.4616 0.4715 0.1762  0.0789  0.0007  106 SER A CA  
528  C C   . SER A 71  ? 0.3120 0.3883 0.4204 0.1693  0.0614  0.0093  106 SER A C   
529  O O   . SER A 71  ? 0.2844 0.3632 0.4119 0.1780  0.0529  0.0116  106 SER A O   
530  C CB  . SER A 71  ? 0.3557 0.4941 0.4803 0.1744  0.0919  0.0125  106 SER A CB  
531  O OG  . SER A 71  ? 0.4109 0.5616 0.5296 0.1855  0.1080  0.0052  106 SER A OG  
532  N N   . LYS A 72  ? 0.2485 0.3151 0.3475 0.1546  0.0556  0.0146  107 LYS A N   
533  C CA  . LYS A 72  ? 0.2764 0.3311 0.3808 0.1407  0.0374  0.0220  107 LYS A CA  
534  C C   . LYS A 72  ? 0.3014 0.3197 0.3742 0.1257  0.0302  0.0151  107 LYS A C   
535  O O   . LYS A 72  ? 0.2804 0.2932 0.3340 0.1203  0.0374  0.0091  107 LYS A O   
536  C CB  . LYS A 72  ? 0.2325 0.3221 0.3618 0.1235  0.0328  0.0367  107 LYS A CB  
537  C CG  . LYS A 72  ? 0.2956 0.4292 0.4641 0.1354  0.0363  0.0461  107 LYS A CG  
538  C CD  . LYS A 72  ? 0.3391 0.4630 0.5205 0.1498  0.0223  0.0488  107 LYS A CD  
539  C CE  . LYS A 72  ? 0.3789 0.5432 0.5960 0.1586  0.0217  0.0545  107 LYS A CE  
540  N NZ  . LYS A 72  ? 0.4148 0.6193 0.6605 0.1407  0.0144  0.0704  107 LYS A NZ  
541  N N   . LEU A 73  ? 0.2703 0.2659 0.3386 0.1192  0.0160  0.0170  108 LEU A N   
542  C CA  . LEU A 73  ? 0.2216 0.1902 0.2666 0.1036  0.0087  0.0125  108 LEU A CA  
543  C C   . LEU A 73  ? 0.2688 0.2473 0.3206 0.0857  -0.0008 0.0229  108 LEU A C   
544  O O   . LEU A 73  ? 0.2714 0.2497 0.3334 0.0855  -0.0105 0.0310  108 LEU A O   
545  C CB  . LEU A 73  ? 0.2916 0.2237 0.3217 0.1095  0.0015  0.0056  108 LEU A CB  
546  C CG  . LEU A 73  ? 0.2833 0.1943 0.2918 0.0933  -0.0033 -0.0002 108 LEU A CG  
547  C CD1 . LEU A 73  ? 0.3433 0.2554 0.3370 0.0940  0.0051  -0.0106 108 LEU A CD1 
548  C CD2 . LEU A 73  ? 0.3093 0.1846 0.3054 0.0930  -0.0126 -0.0036 108 LEU A CD2 
549  N N   . VAL A 74  ? 0.2672 0.2523 0.3111 0.0721  0.0014  0.0227  109 VAL A N   
550  C CA  . VAL A 74  ? 0.2571 0.2499 0.3028 0.0559  -0.0061 0.0302  109 VAL A CA  
551  C C   . VAL A 74  ? 0.2781 0.2523 0.3020 0.0451  -0.0088 0.0240  109 VAL A C   
552  O O   . VAL A 74  ? 0.2181 0.1856 0.2297 0.0464  -0.0031 0.0160  109 VAL A O   
553  C CB  . VAL A 74  ? 0.2312 0.2481 0.2877 0.0496  -0.0016 0.0359  109 VAL A CB  
554  C CG1 . VAL A 74  ? 0.2051 0.2220 0.2578 0.0325  -0.0117 0.0415  109 VAL A CG1 
555  C CG2 . VAL A 74  ? 0.2041 0.2496 0.2885 0.0590  0.0020  0.0434  109 VAL A CG2 
556  N N   . LEU A 75  ? 0.2812 0.2496 0.3003 0.0349  -0.0174 0.0280  110 LEU A N   
557  C CA  . LEU A 75  ? 0.2187 0.1758 0.2202 0.0256  -0.0186 0.0227  110 LEU A CA  
558  C C   . LEU A 75  ? 0.2579 0.2210 0.2542 0.0152  -0.0221 0.0259  110 LEU A C   
559  O O   . LEU A 75  ? 0.2290 0.1984 0.2312 0.0104  -0.0292 0.0339  110 LEU A O   
560  C CB  . LEU A 75  ? 0.2631 0.2062 0.2579 0.0218  -0.0237 0.0240  110 LEU A CB  
561  C CG  . LEU A 75  ? 0.2695 0.2089 0.2498 0.0114  -0.0231 0.0198  110 LEU A CG  
562  C CD1 . LEU A 75  ? 0.3054 0.2448 0.2821 0.0148  -0.0172 0.0092  110 LEU A CD1 
563  C CD2 . LEU A 75  ? 0.2861 0.2149 0.2597 0.0037  -0.0273 0.0244  110 LEU A CD2 
564  N N   . VAL A 76  ? 0.2670 0.2266 0.2513 0.0125  -0.0188 0.0192  111 VAL A N   
565  C CA  . VAL A 76  ? 0.2000 0.1579 0.1743 0.0041  -0.0225 0.0198  111 VAL A CA  
566  C C   . VAL A 76  ? 0.2763 0.2268 0.2346 0.0009  -0.0225 0.0138  111 VAL A C   
567  O O   . VAL A 76  ? 0.2768 0.2255 0.2299 0.0053  -0.0176 0.0060  111 VAL A O   
568  C CB  . VAL A 76  ? 0.2668 0.2230 0.2377 0.0052  -0.0188 0.0175  111 VAL A CB  
569  C CG1 . VAL A 76  ? 0.2036 0.1504 0.1608 -0.0036 -0.0245 0.0174  111 VAL A CG1 
570  C CG2 . VAL A 76  ? 0.1705 0.1399 0.1586 0.0082  -0.0153 0.0242  111 VAL A CG2 
571  N N   . ASP A 77  ? 0.2505 0.1992 0.2010 -0.0066 -0.0282 0.0178  112 ASP A N   
572  C CA  . ASP A 77  ? 0.2641 0.2097 0.1986 -0.0107 -0.0266 0.0140  112 ASP A CA  
573  C C   . ASP A 77  ? 0.2540 0.2024 0.1937 -0.0103 -0.0226 0.0143  112 ASP A C   
574  O O   . ASP A 77  ? 0.2905 0.2393 0.2424 -0.0046 -0.0204 0.0129  112 ASP A O   
575  C CB  . ASP A 77  ? 0.2882 0.2304 0.2096 -0.0075 -0.0223 0.0038  112 ASP A CB  
576  C CG  . ASP A 77  ? 0.3397 0.2709 0.2490 -0.0110 -0.0284 0.0033  112 ASP A CG  
577  O OD1 . ASP A 77  ? 0.3000 0.2304 0.2114 -0.0186 -0.0366 0.0112  112 ASP A OD1 
578  O OD2 . ASP A 77  ? 0.2600 0.1824 0.1579 -0.0062 -0.0261 -0.0049 112 ASP A OD2 
579  N N   . THR A 78  ? 0.2636 0.2122 0.1919 -0.0176 -0.0220 0.0167  113 THR A N   
580  C CA  . THR A 78  ? 0.2498 0.1968 0.1816 -0.0224 -0.0211 0.0216  113 THR A CA  
581  C C   . THR A 78  ? 0.3102 0.2669 0.2343 -0.0290 -0.0133 0.0179  113 THR A C   
582  O O   . THR A 78  ? 0.2581 0.2128 0.1824 -0.0376 -0.0128 0.0240  113 THR A O   
583  C CB  . THR A 78  ? 0.3232 0.2605 0.2503 -0.0277 -0.0296 0.0342  113 THR A CB  
584  O OG1 . THR A 78  ? 0.3189 0.2566 0.2252 -0.0357 -0.0308 0.0371  113 THR A OG1 
585  C CG2 . THR A 78  ? 0.3636 0.2995 0.3039 -0.0203 -0.0370 0.0383  113 THR A CG2 
586  N N   . GLY A 79  ? 0.2427 0.2101 0.1607 -0.0251 -0.0071 0.0086  114 GLY A N   
587  C CA  . GLY A 79  ? 0.3015 0.2851 0.2149 -0.0299 0.0019  0.0053  114 GLY A CA  
588  C C   . GLY A 79  ? 0.3399 0.3215 0.2323 -0.0400 0.0032  0.0127  114 GLY A C   
589  O O   . GLY A 79  ? 0.3341 0.3006 0.2138 -0.0422 -0.0048 0.0191  114 GLY A O   
590  N N   . ALA A 80  ? 0.2676 0.2672 0.1566 -0.0470 0.0134  0.0126  115 ALA A N   
591  C CA  . ALA A 80  ? 0.3566 0.3590 0.2206 -0.0556 0.0189  0.0175  115 ALA A CA  
592  C C   . ALA A 80  ? 0.3793 0.3773 0.2382 -0.0726 0.0182  0.0330  115 ALA A C   
593  O O   . ALA A 80  ? 0.3282 0.3263 0.1623 -0.0814 0.0223  0.0397  115 ALA A O   
594  C CB  . ALA A 80  ? 0.3483 0.3779 0.2091 -0.0506 0.0340  0.0067  115 ALA A CB  
595  N N   . ALA A 81  ? 0.3741 0.3644 0.2521 -0.0774 0.0125  0.0389  116 ALA A N   
596  C CA  . ALA A 81  ? 0.3365 0.3214 0.2115 -0.0951 0.0128  0.0527  116 ALA A CA  
597  C C   . ALA A 81  ? 0.4377 0.4500 0.3032 -0.1069 0.0282  0.0543  116 ALA A C   
598  O O   . ALA A 81  ? 0.4349 0.4777 0.3166 -0.1030 0.0390  0.0437  116 ALA A O   
599  C CB  . ALA A 81  ? 0.4087 0.3631 0.2654 -0.0999 0.0006  0.0674  116 ALA A CB  
600  N N   . GLY A 82  ? 0.4456 0.4494 0.2846 -0.1202 0.0298  0.0678  117 GLY A N   
601  C CA  . GLY A 82  ? 0.4794 0.5114 0.3059 -0.1318 0.0470  0.0705  117 GLY A CA  
602  C C   . GLY A 82  ? 0.4747 0.5150 0.2726 -0.1227 0.0550  0.0631  117 GLY A C   
603  O O   . GLY A 82  ? 0.6259 0.6838 0.4095 -0.1292 0.0681  0.0658  117 GLY A O   
604  N N   . LEU A 83  ? 0.5004 0.5263 0.2932 -0.1052 0.0463  0.0519  118 LEU A N   
605  C CA  . LEU A 83  ? 0.5026 0.5276 0.2622 -0.0977 0.0509  0.0441  118 LEU A CA  
606  C C   . LEU A 83  ? 0.5156 0.5716 0.2790 -0.0850 0.0684  0.0266  118 LEU A C   
607  O O   . LEU A 83  ? 0.4912 0.5474 0.2287 -0.0777 0.0751  0.0198  118 LEU A O   
608  C CB  . LEU A 83  ? 0.3901 0.3863 0.1413 -0.0868 0.0335  0.0394  118 LEU A CB  
609  C CG  . LEU A 83  ? 0.5548 0.5238 0.3060 -0.0943 0.0148  0.0553  118 LEU A CG  
610  C CD1 . LEU A 83  ? 0.4766 0.4256 0.2202 -0.0853 -0.0014 0.0511  118 LEU A CD1 
611  C CD2 . LEU A 83  ? 0.5563 0.5187 0.2853 -0.1079 0.0149  0.0705  118 LEU A CD2 
612  N N   . PHE A 84  ? 0.4891 0.5684 0.2886 -0.0780 0.0736  0.0186  119 PHE A N   
613  C CA  . PHE A 84  ? 0.5729 0.6779 0.3783 -0.0601 0.0864  0.0006  119 PHE A CA  
614  C C   . PHE A 84  ? 0.5005 0.6507 0.3395 -0.0641 0.1004  0.0004  119 PHE A C   
615  O O   . PHE A 84  ? 0.4935 0.6636 0.3587 -0.0488 0.1025  -0.0120 119 PHE A O   
616  C CB  . PHE A 84  ? 0.5704 0.6554 0.3849 -0.0409 0.0744  -0.0125 119 PHE A CB  
617  C CG  . PHE A 84  ? 0.6499 0.7393 0.4495 -0.0205 0.0824  -0.0305 119 PHE A CG  
618  C CD1 . PHE A 84  ? 0.6683 0.7913 0.4910 -0.0060 0.0942  -0.0419 119 PHE A CD1 
619  C CD2 . PHE A 84  ? 0.7480 0.8061 0.5096 -0.0150 0.0765  -0.0366 119 PHE A CD2 
620  C CE1 . PHE A 84  ? 0.7811 0.8991 0.5916 0.0161  0.0995  -0.0578 119 PHE A CE1 
621  C CE2 . PHE A 84  ? 0.8081 0.8595 0.5542 0.0053  0.0818  -0.0534 119 PHE A CE2 
622  C CZ  . PHE A 84  ? 0.8144 0.8920 0.5861 0.0211  0.0933  -0.0634 119 PHE A CZ  
623  N N   . GLY A 85  ? 0.4479 0.6139 0.2874 -0.0857 0.1082  0.0153  120 GLY A N   
624  C CA  . GLY A 85  ? 0.4010 0.6111 0.2730 -0.0913 0.1209  0.0162  120 GLY A CA  
625  C C   . GLY A 85  ? 0.5315 0.7493 0.4349 -0.1092 0.1135  0.0254  120 GLY A C   
626  O O   . GLY A 85  ? 0.5082 0.6888 0.4142 -0.1087 0.0953  0.0277  120 GLY A O   
627  N N   . PRO A 86  ? 0.4349 0.6902 0.3681 -0.1194 0.1216  0.0288  121 PRO A N   
628  C CA  . PRO A 86  ? 0.4151 0.6715 0.3755 -0.1398 0.1119  0.0382  121 PRO A CA  
629  C C   . PRO A 86  ? 0.3992 0.6633 0.3912 -0.1276 0.1015  0.0260  121 PRO A C   
630  O O   . PRO A 86  ? 0.4463 0.6989 0.4557 -0.1422 0.0891  0.0318  121 PRO A O   
631  C CB  . PRO A 86  ? 0.4614 0.7531 0.4398 -0.1543 0.1228  0.0455  121 PRO A CB  
632  C CG  . PRO A 86  ? 0.4448 0.7689 0.4188 -0.1343 0.1406  0.0348  121 PRO A CG  
633  C CD  . PRO A 86  ? 0.4736 0.7729 0.4212 -0.1096 0.1383  0.0216  121 PRO A CD  
634  N N   . THR A 87  ? 0.3588 0.6330 0.3558 -0.0997 0.1028  0.0091  122 THR A N   
635  C CA  . THR A 87  ? 0.3206 0.5944 0.3436 -0.0863 0.0897  -0.0013 122 THR A CA  
636  C C   . THR A 87  ? 0.3405 0.5598 0.3465 -0.0766 0.0725  -0.0033 122 THR A C   
637  O O   . THR A 87  ? 0.2882 0.5014 0.3101 -0.0667 0.0613  -0.0105 122 THR A O   
638  C CB  . THR A 87  ? 0.3390 0.6471 0.3767 -0.0594 0.0970  -0.0176 122 THR A CB  
639  O OG1 . THR A 87  ? 0.2758 0.5614 0.2812 -0.0402 0.1019  -0.0253 122 THR A OG1 
640  C CG2 . THR A 87  ? 0.3609 0.7336 0.4253 -0.0657 0.1142  -0.0171 122 THR A CG2 
641  N N   . LEU A 88  ? 0.3537 0.5361 0.3281 -0.0784 0.0702  0.0029  123 LEU A N   
642  C CA  . LEU A 88  ? 0.2941 0.4321 0.2567 -0.0693 0.0552  0.0017  123 LEU A CA  
643  C C   . LEU A 88  ? 0.3394 0.4463 0.2943 -0.0874 0.0458  0.0162  123 LEU A C   
644  O O   . LEU A 88  ? 0.4094 0.5244 0.3666 -0.1079 0.0494  0.0271  123 LEU A O   
645  C CB  . LEU A 88  ? 0.3078 0.4281 0.2431 -0.0544 0.0567  -0.0039 123 LEU A CB  
646  C CG  . LEU A 88  ? 0.3205 0.4613 0.2599 -0.0329 0.0638  -0.0195 123 LEU A CG  
647  C CD1 . LEU A 88  ? 0.4203 0.5338 0.3286 -0.0198 0.0621  -0.0260 123 LEU A CD1 
648  C CD2 . LEU A 88  ? 0.2876 0.4358 0.2537 -0.0213 0.0562  -0.0276 123 LEU A CD2 
649  N N   . GLY A 89  ? 0.2939 0.3646 0.2397 -0.0798 0.0336  0.0169  124 GLY A N   
650  C CA  . GLY A 89  ? 0.3409 0.3798 0.2807 -0.0917 0.0234  0.0291  124 GLY A CA  
651  C C   . GLY A 89  ? 0.3967 0.4253 0.3549 -0.0944 0.0144  0.0271  124 GLY A C   
652  O O   . GLY A 89  ? 0.3463 0.3479 0.2996 -0.1054 0.0065  0.0367  124 GLY A O   
653  N N   . ARG A 90  ? 0.3199 0.3652 0.2958 -0.0836 0.0139  0.0146  125 ARG A N   
654  C CA  . ARG A 90  ? 0.3461 0.3811 0.3355 -0.0864 0.0045  0.0111  125 ARG A CA  
655  C C   . ARG A 90  ? 0.3019 0.3016 0.2836 -0.0733 -0.0052 0.0088  125 ARG A C   
656  O O   . ARG A 90  ? 0.3084 0.2915 0.2945 -0.0745 -0.0133 0.0057  125 ARG A O   
657  C CB  . ARG A 90  ? 0.2546 0.3223 0.2642 -0.0795 0.0061  -0.0007 125 ARG A CB  
658  C CG  . ARG A 90  ? 0.3446 0.4493 0.3735 -0.0968 0.0110  0.0013  125 ARG A CG  
659  C CD  . ARG A 90  ? 0.3682 0.4835 0.3886 -0.1128 0.0219  0.0131  125 ARG A CD  
660  N NE  . ARG A 90  ? 0.4540 0.6206 0.4953 -0.1220 0.0330  0.0126  125 ARG A NE  
661  C CZ  . ARG A 90  ? 0.3902 0.5813 0.4255 -0.1297 0.0479  0.0192  125 ARG A CZ  
662  N NH1 . ARG A 90  ? 0.4133 0.5793 0.4194 -0.1302 0.0519  0.0269  125 ARG A NH1 
663  N NH2 . ARG A 90  ? 0.4336 0.6780 0.4927 -0.1364 0.0593  0.0179  125 ARG A NH2 
664  N N   . LEU A 91  ? 0.2640 0.2622 0.2574 -0.0573 -0.0065 0.0288  126 LEU A N   
665  C CA  . LEU A 91  ? 0.2844 0.2604 0.2678 -0.0400 -0.0100 0.0246  126 LEU A CA  
666  C C   . LEU A 91  ? 0.3352 0.2743 0.3055 -0.0394 -0.0175 0.0287  126 LEU A C   
667  O O   . LEU A 91  ? 0.3382 0.2596 0.3026 -0.0290 -0.0231 0.0210  126 LEU A O   
668  C CB  . LEU A 91  ? 0.2621 0.2491 0.2430 -0.0288 -0.0036 0.0259  126 LEU A CB  
669  C CG  . LEU A 91  ? 0.2403 0.2143 0.2144 -0.0129 -0.0050 0.0220  126 LEU A CG  
670  C CD1 . LEU A 91  ? 0.2173 0.2086 0.1960 -0.0045 0.0001  0.0182  126 LEU A CD1 
671  C CD2 . LEU A 91  ? 0.2895 0.2446 0.2531 -0.0082 -0.0070 0.0286  126 LEU A CD2 
672  N N   . ALA A 92  ? 0.3366 0.2626 0.3002 -0.0494 -0.0182 0.0405  127 ALA A N   
673  C CA  . ALA A 92  ? 0.3777 0.2629 0.3276 -0.0470 -0.0275 0.0446  127 ALA A CA  
674  C C   . ALA A 92  ? 0.3899 0.2533 0.3403 -0.0521 -0.0372 0.0360  127 ALA A C   
675  O O   . ALA A 92  ? 0.3941 0.2324 0.3354 -0.0378 -0.0445 0.0273  127 ALA A O   
676  C CB  . ALA A 92  ? 0.3512 0.2246 0.2930 -0.0610 -0.0280 0.0613  127 ALA A CB  
677  N N   . ALA A 93  ? 0.4158 0.2922 0.3776 -0.0721 -0.0376 0.0369  128 ALA A N   
678  C CA  . ALA A 93  ? 0.4194 0.2759 0.3830 -0.0802 -0.0487 0.0283  128 ALA A CA  
679  C C   . ALA A 93  ? 0.4195 0.2846 0.3845 -0.0633 -0.0511 0.0116  128 ALA A C   
680  O O   . ALA A 93  ? 0.3602 0.1989 0.3173 -0.0583 -0.0619 0.0014  128 ALA A O   
681  C CB  . ALA A 93  ? 0.4353 0.3128 0.4150 -0.1070 -0.0479 0.0329  128 ALA A CB  
682  N N   . ASN A 94  ? 0.3045 0.2049 0.2774 -0.0540 -0.0420 0.0085  129 ASN A N   
683  C CA  . ASN A 94  ? 0.3372 0.2454 0.3086 -0.0389 -0.0443 -0.0043 129 ASN A CA  
684  C C   . ASN A 94  ? 0.3101 0.1994 0.2650 -0.0181 -0.0442 -0.0077 129 ASN A C   
685  O O   . ASN A 94  ? 0.3431 0.2267 0.2900 -0.0070 -0.0491 -0.0183 129 ASN A O   
686  C CB  . ASN A 94  ? 0.2758 0.2223 0.2599 -0.0360 -0.0365 -0.0054 129 ASN A CB  
687  C CG  . ASN A 94  ? 0.2926 0.2645 0.2951 -0.0520 -0.0387 -0.0080 129 ASN A CG  
688  O OD1 . ASN A 94  ? 0.3263 0.2887 0.3318 -0.0625 -0.0483 -0.0133 129 ASN A OD1 
689  N ND2 . ASN A 94  ? 0.2348 0.2405 0.2505 -0.0534 -0.0307 -0.0062 129 ASN A ND2 
690  N N   . LEU A 95  ? 0.3380 0.2217 0.2877 -0.0121 -0.0386 0.0007  130 LEU A N   
691  C CA  . LEU A 95  ? 0.3358 0.2022 0.2719 0.0065  -0.0399 -0.0032 130 LEU A CA  
692  C C   . LEU A 95  ? 0.4131 0.2434 0.3381 0.0085  -0.0524 -0.0111 130 LEU A C   
693  O O   . LEU A 95  ? 0.3812 0.2024 0.2952 0.0245  -0.0560 -0.0226 130 LEU A O   
694  C CB  . LEU A 95  ? 0.3339 0.2003 0.2687 0.0105  -0.0347 0.0073  130 LEU A CB  
695  C CG  . LEU A 95  ? 0.3973 0.2518 0.3221 0.0301  -0.0357 0.0046  130 LEU A CG  
696  C CD1 . LEU A 95  ? 0.4240 0.2982 0.3473 0.0445  -0.0299 -0.0039 130 LEU A CD1 
697  C CD2 . LEU A 95  ? 0.4546 0.3152 0.3812 0.0315  -0.0319 0.0158  130 LEU A CD2 
698  N N   . LYS A 96  ? 0.3701 0.1793 0.2969 -0.0083 -0.0594 -0.0054 131 LYS A N   
699  C CA  . LYS A 96  ? 0.4051 0.1733 0.3207 -0.0074 -0.0737 -0.0141 131 LYS A CA  
700  C C   . LYS A 96  ? 0.4736 0.2454 0.3899 -0.0087 -0.0808 -0.0297 131 LYS A C   
701  O O   . LYS A 96  ? 0.4504 0.2002 0.3529 0.0055  -0.0895 -0.0440 131 LYS A O   
702  C CB  . LYS A 96  ? 0.4905 0.2306 0.4067 -0.0283 -0.0806 -0.0022 131 LYS A CB  
703  C CG  . LYS A 96  ? 0.5168 0.2432 0.4255 -0.0226 -0.0780 0.0119  131 LYS A CG  
704  C CD  . LYS A 96  ? 0.5274 0.2260 0.4342 -0.0466 -0.0844 0.0273  131 LYS A CD  
705  C CE  . LYS A 96  ? 0.5916 0.2704 0.4862 -0.0390 -0.0850 0.0420  131 LYS A CE  
706  N NZ  . LYS A 96  ? 0.6529 0.3749 0.5558 -0.0450 -0.0703 0.0546  131 LYS A NZ  
707  N N   . ALA A 97  ? 0.4021 0.2039 0.3337 -0.0238 -0.0778 -0.0285 132 ALA A N   
708  C CA  . ALA A 97  ? 0.3916 0.2026 0.3244 -0.0235 -0.0852 -0.0429 132 ALA A CA  
709  C C   . ALA A 97  ? 0.3831 0.2025 0.3017 0.0012  -0.0823 -0.0529 132 ALA A C   
710  O O   . ALA A 97  ? 0.4025 0.2137 0.3106 0.0085  -0.0918 -0.0676 132 ALA A O   
711  C CB  . ALA A 97  ? 0.4280 0.2777 0.3817 -0.0390 -0.0810 -0.0392 132 ALA A CB  
712  N N   . ALA A 98  ? 0.3575 0.1940 0.2746 0.0133  -0.0695 -0.0450 133 ALA A N   
713  C CA  . ALA A 98  ? 0.3753 0.2242 0.2798 0.0336  -0.0641 -0.0505 133 ALA A CA  
714  C C   . ALA A 98  ? 0.4579 0.2837 0.3444 0.0515  -0.0679 -0.0601 133 ALA A C   
715  O O   . ALA A 98  ? 0.4112 0.2513 0.2867 0.0683  -0.0615 -0.0642 133 ALA A O   
716  C CB  . ALA A 98  ? 0.3166 0.1910 0.2281 0.0369  -0.0498 -0.0382 133 ALA A CB  
717  N N   . GLY A 99  ? 0.4223 0.2136 0.3054 0.0486  -0.0779 -0.0635 134 GLY A N   
718  C CA  . GLY A 99  ? 0.4418 0.2081 0.3076 0.0686  -0.0840 -0.0760 134 GLY A CA  
719  C C   . GLY A 99  ? 0.4514 0.2133 0.3165 0.0813  -0.0781 -0.0689 134 GLY A C   
720  O O   . GLY A 99  ? 0.5553 0.3000 0.4071 0.1017  -0.0830 -0.0806 134 GLY A O   
721  N N   . TYR A 100 ? 0.4286 0.2052 0.3072 0.0711  -0.0693 -0.0517 135 TYR A N   
722  C CA  . TYR A 100 ? 0.5398 0.3174 0.4189 0.0833  -0.0645 -0.0447 135 TYR A CA  
723  C C   . TYR A 100 ? 0.5654 0.3174 0.4485 0.0698  -0.0704 -0.0314 135 TYR A C   
724  O O   . TYR A 100 ? 0.5271 0.2757 0.4176 0.0470  -0.0720 -0.0232 135 TYR A O   
725  C CB  . TYR A 100 ? 0.3705 0.1910 0.2597 0.0851  -0.0489 -0.0357 135 TYR A CB  
726  C CG  . TYR A 100 ? 0.4389 0.2852 0.3220 0.0986  -0.0415 -0.0447 135 TYR A CG  
727  C CD1 . TYR A 100 ? 0.4515 0.3033 0.3259 0.1211  -0.0397 -0.0542 135 TYR A CD1 
728  C CD2 . TYR A 100 ? 0.3564 0.2230 0.2416 0.0895  -0.0366 -0.0433 135 TYR A CD2 
729  C CE1 . TYR A 100 ? 0.4209 0.2999 0.2877 0.1316  -0.0314 -0.0608 135 TYR A CE1 
730  C CE2 . TYR A 100 ? 0.3388 0.2268 0.2150 0.1002  -0.0301 -0.0485 135 TYR A CE2 
731  C CZ  . TYR A 100 ? 0.3584 0.2542 0.2252 0.1199  -0.0265 -0.0563 135 TYR A CZ  
732  O OH  . TYR A 100 ? 0.3865 0.3071 0.2425 0.1289  -0.0185 -0.0599 135 TYR A OH  
733  N N   . GLN A 101 ? 0.5093 0.2476 0.3876 0.0847  -0.0729 -0.0284 136 GLN A N   
734  C CA  . GLN A 101 ? 0.5300 0.2493 0.4096 0.0739  -0.0768 -0.0121 136 GLN A CA  
735  C C   . GLN A 101 ? 0.5493 0.3048 0.4384 0.0764  -0.0649 -0.0003 136 GLN A C   
736  O O   . GLN A 101 ? 0.4549 0.2402 0.3481 0.0926  -0.0570 -0.0063 136 GLN A O   
737  C CB  . GLN A 101 ? 0.5775 0.2493 0.4430 0.0889  -0.0918 -0.0156 136 GLN A CB  
738  C CG  . GLN A 101 ? 0.6391 0.2647 0.4940 0.0829  -0.1070 -0.0262 136 GLN A CG  
739  C CD  . GLN A 101 ? 0.7083 0.3230 0.5691 0.0494  -0.1093 -0.0139 136 GLN A CD  
740  O OE1 . GLN A 101 ? 0.7833 0.3849 0.6442 0.0343  -0.1104 0.0048  136 GLN A OE1 
741  N NE2 . GLN A 101 ? 0.7364 0.3583 0.6015 0.0377  -0.1104 -0.0244 136 GLN A NE2 
742  N N   . PRO A 102 ? 0.5074 0.2620 0.3996 0.0599  -0.0638 0.0163  137 PRO A N   
743  C CA  . PRO A 102 ? 0.3957 0.1819 0.2950 0.0632  -0.0552 0.0257  137 PRO A CA  
744  C C   . PRO A 102 ? 0.5164 0.3013 0.4120 0.0882  -0.0591 0.0227  137 PRO A C   
745  O O   . PRO A 102 ? 0.4685 0.2899 0.3737 0.0958  -0.0509 0.0231  137 PRO A O   
746  C CB  . PRO A 102 ? 0.4852 0.2600 0.3816 0.0431  -0.0572 0.0432  137 PRO A CB  
747  C CG  . PRO A 102 ? 0.6076 0.3611 0.5025 0.0241  -0.0615 0.0431  137 PRO A CG  
748  C CD  . PRO A 102 ? 0.5342 0.2591 0.4222 0.0376  -0.0711 0.0274  137 PRO A CD  
749  N N   . GLU A 103 ? 0.4860 0.2295 0.3689 0.1014  -0.0727 0.0192  138 GLU A N   
750  C CA  . GLU A 103 ? 0.5664 0.3109 0.4472 0.1291  -0.0777 0.0141  138 GLU A CA  
751  C C   . GLU A 103 ? 0.5127 0.2951 0.4022 0.1471  -0.0686 -0.0022 138 GLU A C   
752  O O   . GLU A 103 ? 0.4711 0.2758 0.3662 0.1679  -0.0677 -0.0060 138 GLU A O   
753  C CB  . GLU A 103 ? 0.5740 0.2703 0.4416 0.1379  -0.0933 0.0108  138 GLU A CB  
754  C CG  . GLU A 103 ? 0.6299 0.2957 0.4896 0.1202  -0.1007 0.0300  138 GLU A CG  
755  C CD  . GLU A 103 ? 0.7637 0.4039 0.6188 0.0922  -0.1024 0.0365  138 GLU A CD  
756  O OE1 . GLU A 103 ? 0.6473 0.2878 0.5047 0.0895  -0.1007 0.0236  138 GLU A OE1 
757  O OE2 . GLU A 103 ? 0.9171 0.5409 0.7670 0.0725  -0.1049 0.0545  138 GLU A OE2 
758  N N   . GLN A 104 ? 0.4784 0.2722 0.3696 0.1392  -0.0615 -0.0109 139 GLN A N   
759  C CA  . GLN A 104 ? 0.4833 0.3119 0.3789 0.1551  -0.0524 -0.0244 139 GLN A CA  
760  C C   . GLN A 104 ? 0.3840 0.2633 0.2954 0.1477  -0.0374 -0.0175 139 GLN A C   
761  O O   . GLN A 104 ? 0.3781 0.2915 0.2952 0.1606  -0.0290 -0.0250 139 GLN A O   
762  C CB  . GLN A 104 ? 0.4139 0.2324 0.3006 0.1520  -0.0526 -0.0366 139 GLN A CB  
763  C CG  . GLN A 104 ? 0.4863 0.2564 0.3567 0.1640  -0.0684 -0.0497 139 GLN A CG  
764  C CD  . GLN A 104 ? 0.5927 0.3570 0.4541 0.1600  -0.0695 -0.0631 139 GLN A CD  
765  O OE1 . GLN A 104 ? 0.4716 0.2284 0.3350 0.1371  -0.0703 -0.0575 139 GLN A OE1 
766  N NE2 . GLN A 104 ? 0.6207 0.3979 0.4745 0.1792  -0.0686 -0.0797 139 GLN A NE2 
767  N N   . VAL A 105 ? 0.3912 0.2764 0.3095 0.1268  -0.0340 -0.0039 140 VAL A N   
768  C CA  . VAL A 105 ? 0.3370 0.2638 0.2695 0.1177  -0.0218 0.0015  140 VAL A CA  
769  C C   . VAL A 105 ? 0.3251 0.2791 0.2676 0.1312  -0.0206 0.0027  140 VAL A C   
770  O O   . VAL A 105 ? 0.4283 0.3704 0.3693 0.1356  -0.0288 0.0088  140 VAL A O   
771  C CB  . VAL A 105 ? 0.2900 0.2139 0.2256 0.0948  -0.0203 0.0128  140 VAL A CB  
772  C CG1 . VAL A 105 ? 0.2525 0.2141 0.2022 0.0866  -0.0104 0.0173  140 VAL A CG1 
773  C CG2 . VAL A 105 ? 0.3693 0.2748 0.2992 0.0820  -0.0214 0.0104  140 VAL A CG2 
774  N N   . ASP A 106 ? 0.2825 0.2748 0.2353 0.1373  -0.0106 -0.0025 141 ASP A N   
775  C CA  . ASP A 106 ? 0.3097 0.3374 0.2765 0.1494  -0.0086 -0.0032 141 ASP A CA  
776  C C   . ASP A 106 ? 0.3399 0.3920 0.3207 0.1329  -0.0047 0.0066  141 ASP A C   
777  O O   . ASP A 106 ? 0.2529 0.3208 0.2424 0.1397  -0.0094 0.0090  141 ASP A O   
778  C CB  . ASP A 106 ? 0.3603 0.4237 0.3332 0.1601  0.0018  -0.0126 141 ASP A CB  
779  C CG  . ASP A 106 ? 0.3871 0.4326 0.3459 0.1815  -0.0026 -0.0261 141 ASP A CG  
780  O OD1 . ASP A 106 ? 0.3310 0.3554 0.2849 0.1999  -0.0142 -0.0310 141 ASP A OD1 
781  O OD2 . ASP A 106 ? 0.3597 0.4084 0.3099 0.1803  0.0042  -0.0320 141 ASP A OD2 
782  N N   . GLU A 107 ? 0.2595 0.3163 0.2426 0.1130  0.0028  0.0108  142 GLU A N   
783  C CA  . GLU A 107 ? 0.2086 0.2860 0.2039 0.0973  0.0061  0.0173  142 GLU A CA  
784  C C   . GLU A 107 ? 0.3078 0.3650 0.2965 0.0794  0.0071  0.0215  142 GLU A C   
785  O O   . GLU A 107 ? 0.2824 0.3245 0.2631 0.0764  0.0096  0.0194  142 GLU A O   
786  C CB  . GLU A 107 ? 0.2760 0.3936 0.2872 0.0935  0.0159  0.0159  142 GLU A CB  
787  C CG  . GLU A 107 ? 0.2628 0.4089 0.2819 0.1123  0.0180  0.0093  142 GLU A CG  
788  C CD  . GLU A 107 ? 0.3096 0.5038 0.3508 0.1063  0.0251  0.0103  142 GLU A CD  
789  O OE1 . GLU A 107 ? 0.1919 0.3945 0.2410 0.0860  0.0292  0.0158  142 GLU A OE1 
790  O OE2 . GLU A 107 ? 0.3130 0.5380 0.3646 0.1225  0.0260  0.0045  142 GLU A OE2 
791  N N   . VAL A 108 ? 0.2215 0.2820 0.2140 0.0689  0.0048  0.0264  143 VAL A N   
792  C CA  . VAL A 108 ? 0.1969 0.2463 0.1861 0.0537  0.0062  0.0286  143 VAL A CA  
793  C C   . VAL A 108 ? 0.2774 0.3489 0.2787 0.0433  0.0098  0.0283  143 VAL A C   
794  O O   . VAL A 108 ? 0.2313 0.3199 0.2397 0.0434  0.0067  0.0288  143 VAL A O   
795  C CB  . VAL A 108 ? 0.2495 0.2812 0.2289 0.0501  0.0000  0.0336  143 VAL A CB  
796  C CG1 . VAL A 108 ? 0.2292 0.2603 0.2088 0.0355  0.0031  0.0337  143 VAL A CG1 
797  C CG2 . VAL A 108 ? 0.2230 0.2264 0.1904 0.0563  -0.0048 0.0346  143 VAL A CG2 
798  N N   . TYR A 109 ? 0.1888 0.2578 0.1916 0.0345  0.0146  0.0271  144 TYR A N   
799  C CA  . TYR A 109 ? 0.2192 0.3012 0.2321 0.0237  0.0164  0.0264  144 TYR A CA  
800  C C   . TYR A 109 ? 0.2032 0.2722 0.2118 0.0162  0.0140  0.0243  144 TYR A C   
801  O O   . TYR A 109 ? 0.1882 0.2415 0.1893 0.0164  0.0146  0.0239  144 TYR A O   
802  C CB  . TYR A 109 ? 0.2169 0.3040 0.2336 0.0197  0.0226  0.0279  144 TYR A CB  
803  C CG  . TYR A 109 ? 0.2443 0.3533 0.2669 0.0268  0.0273  0.0290  144 TYR A CG  
804  C CD1 . TYR A 109 ? 0.1867 0.3119 0.2152 0.0367  0.0242  0.0271  144 TYR A CD1 
805  C CD2 . TYR A 109 ? 0.2168 0.3312 0.2371 0.0257  0.0345  0.0316  144 TYR A CD2 
806  C CE1 . TYR A 109 ? 0.2631 0.4128 0.2985 0.0465  0.0284  0.0259  144 TYR A CE1 
807  C CE2 . TYR A 109 ? 0.1807 0.3209 0.2060 0.0338  0.0402  0.0312  144 TYR A CE2 
808  C CZ  . TYR A 109 ? 0.2010 0.3600 0.2352 0.0449  0.0372  0.0273  144 TYR A CZ  
809  O OH  . TYR A 109 ? 0.2400 0.4294 0.2813 0.0557  0.0426  0.0248  144 TYR A OH  
810  N N   . LEU A 110 ? 0.1570 0.2355 0.1706 0.0105  0.0109  0.0215  145 LEU A N   
811  C CA  . LEU A 110 ? 0.1954 0.2668 0.2050 0.0056  0.0090  0.0169  145 LEU A CA  
812  C C   . LEU A 110 ? 0.1801 0.2489 0.1967 -0.0016 0.0083  0.0121  145 LEU A C   
813  O O   . LEU A 110 ? 0.1995 0.2790 0.2249 -0.0070 0.0061  0.0104  145 LEU A O   
814  C CB  . LEU A 110 ? 0.1861 0.2685 0.1921 0.0059  0.0049  0.0157  145 LEU A CB  
815  C CG  . LEU A 110 ? 0.1749 0.2537 0.1714 0.0123  0.0037  0.0229  145 LEU A CG  
816  C CD1 . LEU A 110 ? 0.1619 0.2524 0.1520 0.0126  -0.0011 0.0241  145 LEU A CD1 
817  C CD2 . LEU A 110 ? 0.2051 0.2681 0.1932 0.0111  0.0062  0.0252  145 LEU A CD2 
818  N N   . THR A 111 ? 0.1675 0.2211 0.1805 -0.0018 0.0087  0.0096  146 THR A N   
819  C CA  . THR A 111 ? 0.1574 0.2018 0.1745 -0.0071 0.0055  0.0043  146 THR A CA  
820  C C   . THR A 111 ? 0.1613 0.2136 0.1801 -0.0090 0.0005  -0.0054 146 THR A C   
821  O O   . THR A 111 ? 0.2113 0.2617 0.2363 -0.0155 -0.0040 -0.0099 146 THR A O   
822  C CB  . THR A 111 ? 0.1793 0.2058 0.1916 -0.0034 0.0048  0.0027  146 THR A CB  
823  O OG1 . THR A 111 ? 0.1781 0.2096 0.1869 0.0020  0.0047  -0.0028 146 THR A OG1 
824  C CG2 . THR A 111 ? 0.1621 0.1818 0.1701 -0.0015 0.0089  0.0120  146 THR A CG2 
825  N N   . HIS A 112 ? 0.1573 0.2195 0.1697 -0.0045 0.0011  -0.0082 147 HIS A N   
826  C CA  . HIS A 112 ? 0.1672 0.2415 0.1770 -0.0047 -0.0028 -0.0175 147 HIS A CA  
827  C C   . HIS A 112 ? 0.1872 0.2739 0.1871 -0.0013 0.0004  -0.0138 147 HIS A C   
828  O O   . HIS A 112 ? 0.2069 0.2891 0.2040 0.0002  0.0045  -0.0053 147 HIS A O   
829  C CB  . HIS A 112 ? 0.1745 0.2393 0.1848 -0.0032 -0.0069 -0.0307 147 HIS A CB  
830  C CG  . HIS A 112 ? 0.1729 0.2346 0.1799 0.0035  -0.0038 -0.0336 147 HIS A CG  
831  N ND1 . HIS A 112 ? 0.1673 0.2173 0.1757 0.0052  -0.0010 -0.0261 147 HIS A ND1 
832  C CD2 . HIS A 112 ? 0.2256 0.2969 0.2295 0.0096  -0.0040 -0.0453 147 HIS A CD2 
833  C CE1 . HIS A 112 ? 0.1753 0.2285 0.1833 0.0115  -0.0004 -0.0325 147 HIS A CE1 
834  N NE2 . HIS A 112 ? 0.2044 0.2719 0.2103 0.0144  -0.0015 -0.0442 147 HIS A NE2 
835  N N   . MET A 113 ? 0.2174 0.3190 0.2106 -0.0008 -0.0018 -0.0206 148 MET A N   
836  C CA  . MET A 113 ? 0.2007 0.3152 0.1819 -0.0001 0.0008  -0.0132 148 MET A CA  
837  C C   . MET A 113 ? 0.2091 0.3350 0.1828 0.0006  0.0054  -0.0181 148 MET A C   
838  O O   . MET A 113 ? 0.1871 0.3279 0.1483 -0.0009 0.0075  -0.0131 148 MET A O   
839  C CB  . MET A 113 ? 0.2172 0.3455 0.1934 -0.0002 -0.0050 -0.0139 148 MET A CB  
840  C CG  . MET A 113 ? 0.2949 0.4192 0.2789 0.0002  -0.0077 -0.0051 148 MET A CG  
841  S SD  . MET A 113 ? 0.2631 0.4065 0.2436 0.0024  -0.0161 -0.0035 148 MET A SD  
842  C CE  . MET A 113 ? 0.2723 0.4142 0.2700 0.0041  -0.0169 0.0030  148 MET A CE  
843  N N   . HIS A 114 ? 0.1822 0.3041 0.1631 0.0033  0.0070  -0.0276 149 HIS A N   
844  C CA  . HIS A 114 ? 0.2150 0.3545 0.1925 0.0048  0.0125  -0.0326 149 HIS A CA  
845  C C   . HIS A 114 ? 0.2141 0.3558 0.1883 -0.0015 0.0183  -0.0173 149 HIS A C   
846  O O   . HIS A 114 ? 0.2067 0.3299 0.1831 -0.0037 0.0170  -0.0065 149 HIS A O   
847  C CB  . HIS A 114 ? 0.2366 0.3702 0.2246 0.0114  0.0112  -0.0452 149 HIS A CB  
848  C CG  . HIS A 114 ? 0.2859 0.4211 0.2740 0.0187  0.0057  -0.0639 149 HIS A CG  
849  N ND1 . HIS A 114 ? 0.2002 0.3209 0.1964 0.0268  0.0009  -0.0758 149 HIS A ND1 
850  C CD2 . HIS A 114 ? 0.3809 0.5272 0.3606 0.0199  0.0024  -0.0735 149 HIS A CD2 
851  C CE1 . HIS A 114 ? 0.2718 0.3917 0.2652 0.0326  -0.0053 -0.0926 149 HIS A CE1 
852  N NE2 . HIS A 114 ? 0.2474 0.3845 0.2309 0.0283  -0.0043 -0.0925 149 HIS A NE2 
853  N N   . PRO A 115 ? 0.2556 0.4203 0.2243 -0.0051 0.0246  -0.0164 150 PRO A N   
854  C CA  . PRO A 115 ? 0.2213 0.3859 0.1843 -0.0150 0.0289  0.0004  150 PRO A CA  
855  C C   . PRO A 115 ? 0.2570 0.4043 0.2308 -0.0177 0.0285  0.0053  150 PRO A C   
856  O O   . PRO A 115 ? 0.2098 0.3417 0.1786 -0.0244 0.0277  0.0191  150 PRO A O   
857  C CB  . PRO A 115 ? 0.2722 0.4709 0.2299 -0.0199 0.0369  -0.0016 150 PRO A CB  
858  C CG  . PRO A 115 ? 0.3878 0.6042 0.3420 -0.0106 0.0360  -0.0183 150 PRO A CG  
859  C CD  . PRO A 115 ? 0.4168 0.6103 0.3831 -0.0009 0.0281  -0.0306 150 PRO A CD  
860  N N   . ASP A 116 ? 0.1806 0.3288 0.1675 -0.0117 0.0278  -0.0063 151 ASP A N   
861  C CA  . ASP A 116 ? 0.1617 0.2971 0.1582 -0.0126 0.0262  -0.0044 151 ASP A CA  
862  C C   . ASP A 116 ? 0.2214 0.3267 0.2173 -0.0085 0.0208  -0.0002 151 ASP A C   
863  O O   . ASP A 116 ? 0.1727 0.2658 0.1739 -0.0071 0.0185  0.0000  151 ASP A O   
864  C CB  . ASP A 116 ? 0.2379 0.3889 0.2472 -0.0052 0.0262  -0.0187 151 ASP A CB  
865  C CG  . ASP A 116 ? 0.1856 0.3329 0.1959 0.0066  0.0222  -0.0321 151 ASP A CG  
866  O OD1 . ASP A 116 ? 0.2380 0.3966 0.2411 0.0076  0.0235  -0.0368 151 ASP A OD1 
867  O OD2 . ASP A 116 ? 0.1901 0.3209 0.2068 0.0146  0.0167  -0.0378 151 ASP A OD2 
868  N N   . HIS A 117 ? 0.1578 0.2548 0.1472 -0.0065 0.0188  0.0027  152 HIS A N   
869  C CA  . HIS A 117 ? 0.2339 0.3105 0.2232 -0.0033 0.0154  0.0073  152 HIS A CA  
870  C C   . HIS A 117 ? 0.2400 0.3112 0.2206 -0.0047 0.0141  0.0177  152 HIS A C   
871  O O   . HIS A 117 ? 0.2405 0.2966 0.2206 -0.0016 0.0121  0.0226  152 HIS A O   
872  C CB  . HIS A 117 ? 0.2384 0.3126 0.2325 0.0013  0.0127  -0.0007 152 HIS A CB  
873  C CG  . HIS A 117 ? 0.1795 0.2509 0.1803 0.0054  0.0114  -0.0100 152 HIS A CG  
874  N ND1 . HIS A 117 ? 0.2069 0.2612 0.2104 0.0083  0.0091  -0.0087 152 HIS A ND1 
875  C CD2 . HIS A 117 ? 0.1742 0.2581 0.1782 0.0089  0.0113  -0.0209 152 HIS A CD2 
876  C CE1 . HIS A 117 ? 0.2201 0.2728 0.2278 0.0134  0.0064  -0.0172 152 HIS A CE1 
877  N NE2 . HIS A 117 ? 0.1724 0.2437 0.1819 0.0148  0.0076  -0.0258 152 HIS A NE2 
878  N N   . VAL A 118 ? 0.2068 0.2906 0.1791 -0.0079 0.0147  0.0208  153 VAL A N   
879  C CA  . VAL A 118 ? 0.2541 0.3316 0.2163 -0.0072 0.0114  0.0315  153 VAL A CA  
880  C C   . VAL A 118 ? 0.2646 0.3365 0.2156 -0.0147 0.0124  0.0436  153 VAL A C   
881  O O   . VAL A 118 ? 0.2910 0.3488 0.2322 -0.0128 0.0078  0.0541  153 VAL A O   
882  C CB  . VAL A 118 ? 0.2534 0.3467 0.2109 -0.0047 0.0088  0.0284  153 VAL A CB  
883  C CG1 . VAL A 118 ? 0.3575 0.4534 0.3269 -0.0010 0.0069  0.0174  153 VAL A CG1 
884  C CG2 . VAL A 118 ? 0.2414 0.3555 0.1896 -0.0096 0.0123  0.0261  153 VAL A CG2 
885  N N   . GLY A 119 ? 0.2477 0.3304 0.2003 -0.0233 0.0176  0.0428  154 GLY A N   
886  C CA  . GLY A 119 ? 0.2587 0.3381 0.2007 -0.0347 0.0191  0.0563  154 GLY A CA  
887  C C   . GLY A 119 ? 0.2870 0.3331 0.2250 -0.0354 0.0130  0.0661  154 GLY A C   
888  O O   . GLY A 119 ? 0.2870 0.3175 0.2105 -0.0394 0.0093  0.0800  154 GLY A O   
889  N N   . GLY A 120 ? 0.2961 0.3287 0.2447 -0.0302 0.0109  0.0586  155 GLY A N   
890  C CA  . GLY A 120 ? 0.2973 0.2986 0.2422 -0.0296 0.0047  0.0636  155 GLY A CA  
891  C C   . GLY A 120 ? 0.3849 0.3661 0.3207 -0.0177 -0.0020 0.0685  155 GLY A C   
892  O O   . GLY A 120 ? 0.3356 0.2882 0.2663 -0.0143 -0.0085 0.0714  155 GLY A O   
893  N N   . LEU A 121 ? 0.2928 0.2892 0.2267 -0.0103 -0.0019 0.0682  156 LEU A N   
894  C CA  . LEU A 121 ? 0.3611 0.3438 0.2878 0.0020  -0.0093 0.0732  156 LEU A CA  
895  C C   . LEU A 121 ? 0.3830 0.3417 0.2916 -0.0020 -0.0159 0.0889  156 LEU A C   
896  O O   . LEU A 121 ? 0.3463 0.2849 0.2477 0.0103  -0.0246 0.0933  156 LEU A O   
897  C CB  . LEU A 121 ? 0.3530 0.3614 0.2834 0.0088  -0.0089 0.0689  156 LEU A CB  
898  C CG  . LEU A 121 ? 0.2746 0.2965 0.2215 0.0158  -0.0061 0.0562  156 LEU A CG  
899  C CD1 . LEU A 121 ? 0.3045 0.3525 0.2569 0.0175  -0.0062 0.0512  156 LEU A CD1 
900  C CD2 . LEU A 121 ? 0.2893 0.2975 0.2393 0.0284  -0.0098 0.0548  156 LEU A CD2 
901  N N   . MET A 122 ? 0.3867 0.3474 0.2878 -0.0188 -0.0122 0.0979  157 MET A N   
902  C CA  . MET A 122 ? 0.4218 0.3612 0.3029 -0.0267 -0.0175 0.1165  157 MET A CA  
903  C C   . MET A 122 ? 0.5053 0.4305 0.3860 -0.0463 -0.0151 0.1231  157 MET A C   
904  O O   . MET A 122 ? 0.5661 0.5184 0.4580 -0.0583 -0.0058 0.1174  157 MET A O   
905  C CB  . MET A 122 ? 0.4207 0.3873 0.2901 -0.0303 -0.0140 0.1238  157 MET A CB  
906  C CG  . MET A 122 ? 0.3944 0.3734 0.2631 -0.0126 -0.0193 0.1186  157 MET A CG  
907  S SD  . MET A 122 ? 0.5241 0.4678 0.3803 0.0057  -0.0351 0.1286  157 MET A SD  
908  C CE  . MET A 122 ? 0.5931 0.5067 0.4212 -0.0100 -0.0393 0.1542  157 MET A CE  
909  N N   . VAL A 123 ? 0.5623 0.4451 0.4314 -0.0491 -0.0248 0.1341  158 VAL A N   
910  C CA  . VAL A 123 ? 0.5982 0.4628 0.4654 -0.0713 -0.0250 0.1432  158 VAL A CA  
911  C C   . VAL A 123 ? 0.7623 0.6036 0.6055 -0.0830 -0.0300 0.1674  158 VAL A C   
912  O O   . VAL A 123 ? 0.8012 0.6121 0.6316 -0.0677 -0.0404 0.1725  158 VAL A O   
913  C CB  . VAL A 123 ? 0.6978 0.5260 0.5713 -0.0673 -0.0338 0.1341  158 VAL A CB  
914  C CG1 . VAL A 123 ? 0.7230 0.5157 0.5860 -0.0438 -0.0463 0.1326  158 VAL A CG1 
915  C CG2 . VAL A 123 ? 0.5790 0.3811 0.4481 -0.0926 -0.0375 0.1461  158 VAL A CG2 
916  N N   . GLY A 124 ? 0.8832 0.7477 0.7282 -0.1040 -0.0200 0.1742  159 GLY A N   
917  C CA  . GLY A 124 ? 0.8060 0.6673 0.6336 -0.1087 -0.0194 0.1896  159 GLY A CA  
918  C C   . GLY A 124 ? 0.7820 0.6669 0.5993 -0.0919 -0.0181 0.1888  159 GLY A C   
919  O O   . GLY A 124 ? 0.7645 0.6886 0.5912 -0.0879 -0.0106 0.1774  159 GLY A O   
920  N N   . GLU A 125 ? 0.7958 0.6571 0.5940 -0.0810 -0.0265 0.1999  160 GLU A N   
921  C CA  . GLU A 125 ? 0.8394 0.7189 0.6289 -0.0619 -0.0294 0.1971  160 GLU A CA  
922  C C   . GLU A 125 ? 0.8437 0.6895 0.6325 -0.0389 -0.0443 0.1943  160 GLU A C   
923  O O   . GLU A 125 ? 0.8754 0.7124 0.6509 -0.0228 -0.0529 0.2002  160 GLU A O   
924  C CB  . GLU A 125 ? 0.8739 0.7639 0.6419 -0.0651 -0.0269 0.2102  160 GLU A CB  
925  C CG  . GLU A 125 ? 1.0151 0.9468 0.7789 -0.0544 -0.0239 0.2016  160 GLU A CG  
926  C CD  . GLU A 125 ? 1.1642 1.0889 0.9223 -0.0300 -0.0371 0.1983  160 GLU A CD  
927  O OE1 . GLU A 125 ? 1.2323 1.1198 0.9809 -0.0177 -0.0491 0.2074  160 GLU A OE1 
928  O OE2 . GLU A 125 ? 1.0120 0.9722 0.7784 -0.0224 -0.0356 0.1850  160 GLU A OE2 
929  N N   . GLN A 126 ? 0.8254 0.6530 0.6289 -0.0359 -0.0478 0.1841  161 GLN A N   
930  C CA  . GLN A 126 ? 0.7201 0.5160 0.5250 -0.0129 -0.0612 0.1782  161 GLN A CA  
931  C C   . GLN A 126 ? 0.6663 0.4761 0.4914 -0.0031 -0.0590 0.1583  161 GLN A C   
932  O O   . GLN A 126 ? 0.5547 0.3832 0.3945 -0.0166 -0.0484 0.1492  161 GLN A O   
933  C CB  . GLN A 126 ? 0.9554 0.7038 0.7548 -0.0176 -0.0686 0.1847  161 GLN A CB  
934  C CG  . GLN A 126 ? 0.9974 0.7130 0.7984 0.0063  -0.0820 0.1769  161 GLN A CG  
935  C CD  . GLN A 126 ? 0.9820 0.6558 0.7695 0.0029  -0.0906 0.1897  161 GLN A CD  
936  O OE1 . GLN A 126 ? 1.1085 0.7818 0.8841 -0.0163 -0.0860 0.2062  161 GLN A OE1 
937  N NE2 . GLN A 126 ? 1.2680 0.9083 1.0563 0.0220  -0.1031 0.1822  161 GLN A NE2 
938  N N   . LEU A 127 ? 0.5668 0.3761 0.3979 0.0224  -0.0661 0.1477  162 LEU A N   
939  C CA  . LEU A 127 ? 0.5382 0.3752 0.3930 0.0339  -0.0595 0.1259  162 LEU A CA  
940  C C   . LEU A 127 ? 0.5227 0.3417 0.3867 0.0287  -0.0572 0.1155  162 LEU A C   
941  O O   . LEU A 127 ? 0.4972 0.2747 0.3532 0.0346  -0.0674 0.1163  162 LEU A O   
942  C CB  . LEU A 127 ? 0.5603 0.3998 0.4193 0.0614  -0.0681 0.1183  162 LEU A CB  
943  C CG  . LEU A 127 ? 0.7496 0.6055 0.6009 0.0729  -0.0749 0.1261  162 LEU A CG  
944  C CD1 . LEU A 127 ? 0.6501 0.5185 0.5140 0.1001  -0.0816 0.1139  162 LEU A CD1 
945  C CD2 . LEU A 127 ? 0.5658 0.4662 0.4231 0.0598  -0.0642 0.1245  162 LEU A CD2 
946  N N   . ALA A 128 ? 0.4638 0.3137 0.3443 0.0202  -0.0453 0.1041  163 ALA A N   
947  C CA  . ALA A 128 ? 0.5010 0.3389 0.3897 0.0153  -0.0436 0.0937  163 ALA A CA  
948  C C   . ALA A 128 ? 0.4452 0.2781 0.3404 0.0369  -0.0470 0.0787  163 ALA A C   
949  O O   . ALA A 128 ? 0.5137 0.3225 0.4078 0.0381  -0.0511 0.0713  163 ALA A O   
950  C CB  . ALA A 128 ? 0.4042 0.2764 0.3069 0.0008  -0.0313 0.0873  163 ALA A CB  
951  N N   . PHE A 129 ? 0.4018 0.2599 0.3040 0.0533  -0.0452 0.0734  164 PHE A N   
952  C CA  . PHE A 129 ? 0.3882 0.2536 0.2986 0.0727  -0.0451 0.0591  164 PHE A CA  
953  C C   . PHE A 129 ? 0.4192 0.2817 0.3258 0.0937  -0.0540 0.0610  164 PHE A C   
954  O O   . PHE A 129 ? 0.4252 0.3227 0.3429 0.1026  -0.0506 0.0578  164 PHE A O   
955  C CB  . PHE A 129 ? 0.3129 0.2192 0.2398 0.0701  -0.0329 0.0502  164 PHE A CB  
956  C CG  . PHE A 129 ? 0.3049 0.2154 0.2354 0.0516  -0.0258 0.0489  164 PHE A CG  
957  C CD1 . PHE A 129 ? 0.2897 0.1871 0.2197 0.0511  -0.0258 0.0407  164 PHE A CD1 
958  C CD2 . PHE A 129 ? 0.3747 0.3048 0.3090 0.0370  -0.0201 0.0543  164 PHE A CD2 
959  C CE1 . PHE A 129 ? 0.3681 0.2723 0.3028 0.0360  -0.0209 0.0390  164 PHE A CE1 
960  C CE2 . PHE A 129 ? 0.3622 0.2995 0.3016 0.0234  -0.0144 0.0515  164 PHE A CE2 
961  C CZ  . PHE A 129 ? 0.3878 0.3124 0.3282 0.0228  -0.0151 0.0444  164 PHE A CZ  
962  N N   . PRO A 130 ? 0.5088 0.3288 0.4003 0.1023  -0.0670 0.0659  165 PRO A N   
963  C CA  . PRO A 130 ? 0.5071 0.3202 0.3923 0.1229  -0.0783 0.0705  165 PRO A CA  
964  C C   . PRO A 130 ? 0.4680 0.3101 0.3672 0.1487  -0.0777 0.0554  165 PRO A C   
965  O O   . PRO A 130 ? 0.5951 0.4495 0.4966 0.1646  -0.0845 0.0574  165 PRO A O   
966  C CB  . PRO A 130 ? 0.5139 0.2698 0.3814 0.1241  -0.0917 0.0762  165 PRO A CB  
967  C CG  . PRO A 130 ? 0.4877 0.2253 0.3556 0.1182  -0.0894 0.0652  165 PRO A CG  
968  C CD  . PRO A 130 ? 0.5199 0.2944 0.4001 0.0959  -0.0737 0.0652  165 PRO A CD  
969  N N   . ASN A 131 ? 0.4591 0.3169 0.3688 0.1522  -0.0692 0.0405  166 ASN A N   
970  C CA  . ASN A 131 ? 0.4600 0.3517 0.3836 0.1751  -0.0662 0.0266  166 ASN A CA  
971  C C   . ASN A 131 ? 0.4607 0.4080 0.4044 0.1660  -0.0517 0.0238  166 ASN A C   
972  O O   . ASN A 131 ? 0.4317 0.4143 0.3893 0.1807  -0.0469 0.0136  166 ASN A O   
973  C CB  . ASN A 131 ? 0.4618 0.3371 0.3811 0.1872  -0.0663 0.0113  166 ASN A CB  
974  C CG  . ASN A 131 ? 0.5966 0.4298 0.5033 0.1953  -0.0792 0.0081  166 ASN A CG  
975  O OD1 . ASN A 131 ? 0.6725 0.4649 0.5665 0.1873  -0.0844 0.0068  166 ASN A OD1 
976  N ND2 . ASN A 131 ? 0.6044 0.4462 0.5148 0.2102  -0.0856 0.0080  166 ASN A ND2 
977  N N   . ALA A 132 ? 0.3644 0.3206 0.3103 0.1423  -0.0450 0.0323  167 ALA A N   
978  C CA  . ALA A 132 ? 0.2959 0.2924 0.2580 0.1303  -0.0319 0.0287  167 ALA A CA  
979  C C   . ALA A 132 ? 0.3707 0.4026 0.3455 0.1287  -0.0319 0.0323  167 ALA A C   
980  O O   . ALA A 132 ? 0.4256 0.4489 0.3928 0.1282  -0.0402 0.0409  167 ALA A O   
981  C CB  . ALA A 132 ? 0.3174 0.3020 0.2751 0.1071  -0.0254 0.0326  167 ALA A CB  
982  N N   . VAL A 133 ? 0.2966 0.3683 0.2895 0.1269  -0.0232 0.0263  168 VAL A N   
983  C CA  . VAL A 133 ? 0.2815 0.3867 0.2883 0.1171  -0.0219 0.0285  168 VAL A CA  
984  C C   . VAL A 133 ? 0.2624 0.3636 0.2684 0.0940  -0.0143 0.0308  168 VAL A C   
985  O O   . VAL A 133 ? 0.3000 0.3914 0.3039 0.0878  -0.0068 0.0284  168 VAL A O   
986  C CB  . VAL A 133 ? 0.2231 0.3752 0.2526 0.1246  -0.0172 0.0213  168 VAL A CB  
987  C CG1 . VAL A 133 ? 0.2606 0.4439 0.3055 0.1080  -0.0150 0.0224  168 VAL A CG1 
988  C CG2 . VAL A 133 ? 0.3631 0.5263 0.3962 0.1504  -0.0271 0.0179  168 VAL A CG2 
989  N N   . VAL A 134 ? 0.2647 0.3722 0.2704 0.0832  -0.0172 0.0346  169 VAL A N   
990  C CA  . VAL A 134 ? 0.2421 0.3475 0.2476 0.0643  -0.0115 0.0345  169 VAL A CA  
991  C C   . VAL A 134 ? 0.2738 0.4122 0.2978 0.0560  -0.0089 0.0297  169 VAL A C   
992  O O   . VAL A 134 ? 0.2223 0.3842 0.2547 0.0601  -0.0149 0.0286  169 VAL A O   
993  C CB  . VAL A 134 ? 0.2905 0.3800 0.2807 0.0576  -0.0162 0.0404  169 VAL A CB  
994  C CG1 . VAL A 134 ? 0.2793 0.3721 0.2713 0.0416  -0.0107 0.0370  169 VAL A CG1 
995  C CG2 . VAL A 134 ? 0.2668 0.3221 0.2398 0.0611  -0.0188 0.0470  169 VAL A CG2 
996  N N   . ARG A 135 ? 0.2171 0.3558 0.2471 0.0436  -0.0013 0.0270  170 ARG A N   
997  C CA  . ARG A 135 ? 0.2168 0.3799 0.2638 0.0322  0.0008  0.0234  170 ARG A CA  
998  C C   . ARG A 135 ? 0.2342 0.3822 0.2767 0.0180  0.0011  0.0211  170 ARG A C   
999  O O   . ARG A 135 ? 0.1687 0.2934 0.2007 0.0164  0.0046  0.0221  170 ARG A O   
1000 C CB  . ARG A 135 ? 0.1978 0.3737 0.2557 0.0301  0.0096  0.0236  170 ARG A CB  
1001 C CG  . ARG A 135 ? 0.2288 0.4236 0.2921 0.0458  0.0126  0.0232  170 ARG A CG  
1002 C CD  . ARG A 135 ? 0.2935 0.5234 0.3727 0.0539  0.0076  0.0207  170 ARG A CD  
1003 N NE  . ARG A 135 ? 0.1730 0.4359 0.2736 0.0389  0.0081  0.0191  170 ARG A NE  
1004 C CZ  . ARG A 135 ? 0.2545 0.5508 0.3739 0.0318  0.0158  0.0191  170 ARG A CZ  
1005 N NH1 . ARG A 135 ? 0.2366 0.5411 0.3549 0.0393  0.0256  0.0203  170 ARG A NH1 
1006 N NH2 . ARG A 135 ? 0.1451 0.4705 0.2850 0.0167  0.0132  0.0175  170 ARG A NH2 
1007 N N   . ALA A 136 ? 0.2498 0.4123 0.3012 0.0088  -0.0034 0.0164  171 ALA A N   
1008 C CA  . ALA A 136 ? 0.1941 0.3437 0.2439 -0.0033 -0.0041 0.0111  171 ALA A CA  
1009 C C   . ALA A 136 ? 0.1644 0.3337 0.2304 -0.0145 -0.0091 0.0054  171 ALA A C   
1010 O O   . ALA A 136 ? 0.1529 0.3498 0.2316 -0.0129 -0.0121 0.0055  171 ALA A O   
1011 C CB  . ALA A 136 ? 0.1843 0.3217 0.2183 -0.0009 -0.0077 0.0081  171 ALA A CB  
1012 N N   . ASP A 137 ? 0.2013 0.3563 0.2678 -0.0256 -0.0113 -0.0007 172 ASP A N   
1013 C CA  . ASP A 137 ? 0.1679 0.3379 0.2501 -0.0387 -0.0178 -0.0069 172 ASP A CA  
1014 C C   . ASP A 137 ? 0.1720 0.3595 0.2517 -0.0347 -0.0276 -0.0150 172 ASP A C   
1015 O O   . ASP A 137 ? 0.1733 0.3524 0.2354 -0.0259 -0.0295 -0.0176 172 ASP A O   
1016 C CB  . ASP A 137 ? 0.1814 0.3254 0.2639 -0.0515 -0.0202 -0.0124 172 ASP A CB  
1017 C CG  . ASP A 137 ? 0.2669 0.4226 0.3686 -0.0696 -0.0265 -0.0163 172 ASP A CG  
1018 O OD1 . ASP A 137 ? 0.2795 0.4445 0.3846 -0.0734 -0.0369 -0.0278 172 ASP A OD1 
1019 O OD2 . ASP A 137 ? 0.2237 0.3816 0.3371 -0.0813 -0.0211 -0.0076 172 ASP A OD2 
1020 N N   . GLN A 138 ? 0.1762 0.3913 0.2737 -0.0423 -0.0340 -0.0188 173 GLN A N   
1021 C CA  . GLN A 138 ? 0.1944 0.4292 0.2892 -0.0384 -0.0453 -0.0270 173 GLN A CA  
1022 C C   . GLN A 138 ? 0.1965 0.4126 0.2768 -0.0415 -0.0519 -0.0395 173 GLN A C   
1023 O O   . GLN A 138 ? 0.2018 0.4247 0.2660 -0.0323 -0.0573 -0.0437 173 GLN A O   
1024 C CB  . GLN A 138 ? 0.1871 0.4570 0.3070 -0.0483 -0.0526 -0.0310 173 GLN A CB  
1025 C CG  . GLN A 138 ? 0.2294 0.5252 0.3460 -0.0404 -0.0654 -0.0381 173 GLN A CG  
1026 C CD  . GLN A 138 ? 0.3057 0.6225 0.4200 -0.0216 -0.0652 -0.0287 173 GLN A CD  
1027 O OE1 . GLN A 138 ? 0.2713 0.6093 0.4041 -0.0191 -0.0606 -0.0228 173 GLN A OE1 
1028 N NE2 . GLN A 138 ? 0.3055 0.6155 0.3955 -0.0076 -0.0702 -0.0270 173 GLN A NE2 
1029 N N   . LYS A 139 ? 0.2244 0.4170 0.3088 -0.0536 -0.0521 -0.0457 174 LYS A N   
1030 C CA  . LYS A 139 ? 0.2838 0.4569 0.3538 -0.0529 -0.0584 -0.0602 174 LYS A CA  
1031 C C   . LYS A 139 ? 0.2333 0.3980 0.2807 -0.0378 -0.0519 -0.0577 174 LYS A C   
1032 O O   . LYS A 139 ? 0.2354 0.4054 0.2671 -0.0313 -0.0564 -0.0675 174 LYS A O   
1033 C CB  . LYS A 139 ? 0.3134 0.4534 0.3879 -0.0638 -0.0593 -0.0655 174 LYS A CB  
1034 C CG  . LYS A 139 ? 0.4212 0.5540 0.5109 -0.0820 -0.0704 -0.0755 174 LYS A CG  
1035 C CD  . LYS A 139 ? 0.4204 0.5741 0.5347 -0.0988 -0.0706 -0.0670 174 LYS A CD  
1036 C CE  . LYS A 139 ? 0.3919 0.5188 0.5165 -0.1195 -0.0806 -0.0754 174 LYS A CE  
1037 N NZ  . LYS A 139 ? 0.4414 0.5792 0.5899 -0.1415 -0.0778 -0.0633 174 LYS A NZ  
1038 N N   . GLU A 140 ? 0.2128 0.3656 0.2582 -0.0332 -0.0411 -0.0449 175 GLU A N   
1039 C CA  . GLU A 140 ? 0.2354 0.3798 0.2626 -0.0222 -0.0345 -0.0415 175 GLU A CA  
1040 C C   . GLU A 140 ? 0.2651 0.4296 0.2787 -0.0139 -0.0362 -0.0374 175 GLU A C   
1041 O O   . GLU A 140 ? 0.2642 0.4319 0.2612 -0.0093 -0.0367 -0.0430 175 GLU A O   
1042 C CB  . GLU A 140 ? 0.2137 0.3440 0.2432 -0.0201 -0.0247 -0.0287 175 GLU A CB  
1043 C CG  . GLU A 140 ? 0.1856 0.3040 0.2010 -0.0127 -0.0185 -0.0271 175 GLU A CG  
1044 C CD  . GLU A 140 ? 0.2229 0.3265 0.2355 -0.0128 -0.0201 -0.0398 175 GLU A CD  
1045 O OE1 . GLU A 140 ? 0.2162 0.3092 0.2366 -0.0188 -0.0264 -0.0488 175 GLU A OE1 
1046 O OE2 . GLU A 140 ? 0.2171 0.3200 0.2202 -0.0066 -0.0156 -0.0412 175 GLU A OE2 
1047 N N   . ALA A 141 ? 0.2199 0.3992 0.2397 -0.0111 -0.0374 -0.0275 176 ALA A N   
1048 C CA  . ALA A 141 ? 0.2411 0.4349 0.2464 -0.0021 -0.0411 -0.0211 176 ALA A CA  
1049 C C   . ALA A 141 ? 0.2123 0.4245 0.2099 -0.0028 -0.0516 -0.0327 176 ALA A C   
1050 O O   . ALA A 141 ? 0.2673 0.4852 0.2432 0.0030  -0.0530 -0.0310 176 ALA A O   
1051 C CB  . ALA A 141 ? 0.2197 0.4251 0.2355 0.0038  -0.0426 -0.0106 176 ALA A CB  
1052 N N   . ASP A 142 ? 0.2368 0.4595 0.2511 -0.0109 -0.0596 -0.0442 177 ASP A N   
1053 C CA  . ASP A 142 ? 0.2340 0.4751 0.2410 -0.0115 -0.0717 -0.0574 177 ASP A CA  
1054 C C   . ASP A 142 ? 0.3059 0.5376 0.2917 -0.0093 -0.0703 -0.0688 177 ASP A C   
1055 O O   . ASP A 142 ? 0.2634 0.5112 0.2294 -0.0037 -0.0761 -0.0736 177 ASP A O   
1056 C CB  . ASP A 142 ? 0.2945 0.5453 0.3255 -0.0240 -0.0811 -0.0694 177 ASP A CB  
1057 C CG  . ASP A 142 ? 0.2699 0.5459 0.3219 -0.0245 -0.0842 -0.0608 177 ASP A CG  
1058 O OD1 . ASP A 142 ? 0.2473 0.5289 0.2937 -0.0124 -0.0799 -0.0464 177 ASP A OD1 
1059 O OD2 . ASP A 142 ? 0.2717 0.5624 0.3459 -0.0368 -0.0919 -0.0692 177 ASP A OD2 
1060 N N   . PHE A 143 ? 0.2426 0.4505 0.2315 -0.0125 -0.0630 -0.0736 178 PHE A N   
1061 C CA  . PHE A 143 ? 0.3080 0.5106 0.2799 -0.0081 -0.0615 -0.0871 178 PHE A CA  
1062 C C   . PHE A 143 ? 0.2667 0.4757 0.2175 0.0000  -0.0513 -0.0756 178 PHE A C   
1063 O O   . PHE A 143 ? 0.3025 0.5282 0.2325 0.0051  -0.0524 -0.0819 178 PHE A O   
1064 C CB  . PHE A 143 ? 0.2659 0.4411 0.2491 -0.0119 -0.0590 -0.0962 178 PHE A CB  
1065 C CG  . PHE A 143 ? 0.2984 0.4698 0.2668 -0.0040 -0.0575 -0.1124 178 PHE A CG  
1066 C CD1 . PHE A 143 ? 0.2956 0.4715 0.2565 -0.0021 -0.0683 -0.1352 178 PHE A CD1 
1067 C CD2 . PHE A 143 ? 0.3085 0.4757 0.2707 0.0025  -0.0458 -0.1063 178 PHE A CD2 
1068 C CE1 . PHE A 143 ? 0.3796 0.5560 0.3268 0.0082  -0.0667 -0.1526 178 PHE A CE1 
1069 C CE2 . PHE A 143 ? 0.3197 0.4906 0.2709 0.0113  -0.0438 -0.1225 178 PHE A CE2 
1070 C CZ  . PHE A 143 ? 0.3045 0.4806 0.2477 0.0153  -0.0539 -0.1460 178 PHE A CZ  
1071 N N   . TRP A 144 ? 0.2500 0.4474 0.2050 0.0004  -0.0416 -0.0585 179 TRP A N   
1072 C CA  . TRP A 144 ? 0.2858 0.4865 0.2231 0.0044  -0.0320 -0.0481 179 TRP A CA  
1073 C C   . TRP A 144 ? 0.2475 0.4619 0.1671 0.0073  -0.0342 -0.0330 179 TRP A C   
1074 O O   . TRP A 144 ? 0.2586 0.4810 0.1582 0.0084  -0.0282 -0.0261 179 TRP A O   
1075 C CB  . TRP A 144 ? 0.2657 0.4468 0.2131 0.0028  -0.0224 -0.0372 179 TRP A CB  
1076 C CG  . TRP A 144 ? 0.2413 0.4086 0.2000 0.0022  -0.0202 -0.0503 179 TRP A CG  
1077 C CD1 . TRP A 144 ? 0.2427 0.3905 0.2190 -0.0012 -0.0214 -0.0511 179 TRP A CD1 
1078 C CD2 . TRP A 144 ? 0.2795 0.4521 0.2317 0.0064  -0.0168 -0.0640 179 TRP A CD2 
1079 N NE1 . TRP A 144 ? 0.2096 0.3453 0.1895 0.0009  -0.0208 -0.0636 179 TRP A NE1 
1080 C CE2 . TRP A 144 ? 0.2891 0.4407 0.2558 0.0068  -0.0181 -0.0728 179 TRP A CE2 
1081 C CE3 . TRP A 144 ? 0.3293 0.5244 0.2645 0.0104  -0.0125 -0.0693 179 TRP A CE3 
1082 C CZ2 . TRP A 144 ? 0.2989 0.4496 0.2648 0.0137  -0.0169 -0.0883 179 TRP A CZ2 
1083 C CZ3 . TRP A 144 ? 0.3867 0.5866 0.3224 0.0166  -0.0094 -0.0858 179 TRP A CZ3 
1084 C CH2 . TRP A 144 ? 0.3492 0.5261 0.3008 0.0194  -0.0124 -0.0958 179 TRP A CH2 
1085 N N   . LEU A 145 ? 0.2616 0.4108 0.1652 0.0113  -0.0331 -0.0383 180 LEU A N   
1086 C CA  . LEU A 145 ? 0.3203 0.4660 0.1986 0.0113  -0.0376 -0.0236 180 LEU A CA  
1087 C C   . LEU A 145 ? 0.3341 0.4858 0.1823 0.0144  -0.0462 -0.0304 180 LEU A C   
1088 O O   . LEU A 145 ? 0.3412 0.4897 0.1664 0.0157  -0.0535 -0.0180 180 LEU A O   
1089 C CB  . LEU A 145 ? 0.3124 0.4490 0.2060 0.0137  -0.0480 -0.0128 180 LEU A CB  
1090 C CG  . LEU A 145 ? 0.2774 0.4061 0.1946 0.0111  -0.0399 -0.0074 180 LEU A CG  
1091 C CD1 . LEU A 145 ? 0.2907 0.4108 0.2218 0.0160  -0.0475 0.0009  180 LEU A CD1 
1092 C CD2 . LEU A 145 ? 0.3449 0.4688 0.2494 0.0047  -0.0274 0.0025  180 LEU A CD2 
1093 N N   . SER A 146 ? 0.3814 0.5392 0.2272 0.0164  -0.0467 -0.0502 181 SER A N   
1094 C CA  . SER A 146 ? 0.3770 0.5389 0.1917 0.0195  -0.0568 -0.0611 181 SER A CA  
1095 C C   . SER A 146 ? 0.4956 0.6653 0.2715 0.0200  -0.0429 -0.0573 181 SER A C   
1096 O O   . SER A 146 ? 0.4578 0.6359 0.2329 0.0214  -0.0268 -0.0672 181 SER A O   
1097 C CB  . SER A 146 ? 0.4171 0.5772 0.2434 0.0214  -0.0632 -0.0857 181 SER A CB  
1098 O OG  . SER A 146 ? 0.4367 0.5990 0.2276 0.0248  -0.0709 -0.1005 181 SER A OG  
1099 N N   . GLN A 147 ? 0.4822 0.6509 0.2261 0.0195  -0.0489 -0.0421 182 GLN A N   
1100 C CA  . GLN A 147 ? 0.5328 0.7054 0.2388 0.0181  -0.0357 -0.0354 182 GLN A CA  
1101 C C   . GLN A 147 ? 0.5732 0.7498 0.2653 0.0228  -0.0305 -0.0589 182 GLN A C   
1102 O O   . GLN A 147 ? 0.5991 0.7852 0.2754 0.0231  -0.0114 -0.0601 182 GLN A O   
1103 C CB  . GLN A 147 ? 0.6165 0.7764 0.2934 0.0175  -0.0483 -0.0178 182 GLN A CB  
1104 C CG  . GLN A 147 ? 0.6057 0.7554 0.2893 0.0152  -0.0536 0.0074  182 GLN A CG  
1105 C CD  . GLN A 147 ? 0.7542 0.8992 0.4624 0.0209  -0.0756 0.0062  182 GLN A CD  
1106 O OE1 . GLN A 147 ? 0.6395 0.7926 0.3779 0.0227  -0.0808 -0.0105 182 GLN A OE1 
1107 N NE2 . GLN A 147 ? 0.4944 0.6263 0.1904 0.0239  -0.0891 0.0237  182 GLN A NE2 
1108 N N   . THR A 148 ? 0.5013 0.6701 0.2003 0.0263  -0.0477 -0.0772 183 THR A N   
1109 C CA  . THR A 148 ? 0.5430 0.7087 0.2266 0.0312  -0.0464 -0.1007 183 THR A CA  
1110 C C   . THR A 148 ? 0.5762 0.7499 0.2801 0.0362  -0.0293 -0.1162 183 THR A C   
1111 O O   . THR A 148 ? 0.5500 0.7288 0.2358 0.0419  -0.0152 -0.1270 183 THR A O   
1112 C CB  . THR A 148 ? 0.5252 0.6779 0.2175 0.0306  -0.0706 -0.1152 183 THR A CB  
1113 O OG1 . THR A 148 ? 0.7725 0.9229 0.4661 0.0263  -0.0882 -0.0983 183 THR A OG1 
1114 C CG2 . THR A 148 ? 0.5760 0.7214 0.2348 0.0336  -0.0727 -0.1302 183 THR A CG2 
1115 N N   . ASN A 149 ? 0.4768 0.6514 0.2189 0.0353  -0.0315 -0.1185 184 ASN A N   
1116 C CA  . ASN A 149 ? 0.5632 0.7445 0.3280 0.0409  -0.0171 -0.1318 184 ASN A CA  
1117 C C   . ASN A 149 ? 0.5278 0.7300 0.2864 0.0408  0.0079  -0.1197 184 ASN A C   
1118 O O   . ASN A 149 ? 0.6032 0.8149 0.3650 0.0485  0.0228  -0.1321 184 ASN A O   
1119 C CB  . ASN A 149 ? 0.4545 0.6275 0.2636 0.0371  -0.0242 -0.1288 184 ASN A CB  
1120 C CG  . ASN A 149 ? 0.4600 0.6145 0.2821 0.0360  -0.0465 -0.1431 184 ASN A CG  
1121 O OD1 . ASN A 149 ? 0.5052 0.6512 0.3053 0.0385  -0.0569 -0.1585 184 ASN A OD1 
1122 N ND2 . ASN A 149 ? 0.4288 0.5748 0.2890 0.0301  -0.0531 -0.1346 184 ASN A ND2 
1123 N N   . LEU A 150 ? 0.5217 0.7306 0.2737 0.0318  0.0122  -0.0945 185 LEU A N   
1124 C CA  . LEU A 150 ? 0.5154 0.7424 0.2599 0.0273  0.0343  -0.0790 185 LEU A CA  
1125 C C   . LEU A 150 ? 0.6075 0.8396 0.3201 0.0325  0.0443  -0.0864 185 LEU A C   
1126 O O   . LEU A 150 ? 0.6255 0.8749 0.3460 0.0378  0.0623  -0.0947 185 LEU A O   
1127 C CB  . LEU A 150 ? 0.5210 0.7436 0.2553 0.0155  0.0322  -0.0497 185 LEU A CB  
1128 C CG  . LEU A 150 ? 0.5260 0.7625 0.2498 0.0068  0.0527  -0.0302 185 LEU A CG  
1129 C CD1 . LEU A 150 ? 0.5384 0.7993 0.2946 0.0063  0.0723  -0.0351 185 LEU A CD1 
1130 C CD2 . LEU A 150 ? 0.5404 0.7635 0.2564 -0.0055 0.0475  -0.0009 185 LEU A CD2 
1131 N N   . ASP A 151 ? 0.5313 0.7494 0.2079 0.0318  0.0323  -0.0836 186 ASP A N   
1132 C CA  . ASP A 151 ? 0.6328 0.8550 0.2730 0.0360  0.0424  -0.0896 186 ASP A CA  
1133 C C   . ASP A 151 ? 0.6015 0.8230 0.2446 0.0489  0.0443  -0.1201 186 ASP A C   
1134 O O   . ASP A 151 ? 0.7494 0.9803 0.3701 0.0547  0.0591  -0.1277 186 ASP A O   
1135 C CB  . ASP A 151 ? 0.6839 0.8890 0.2832 0.0326  0.0266  -0.0803 186 ASP A CB  
1136 C CG  . ASP A 151 ? 0.8546 1.0559 0.4487 0.0218  0.0249  -0.0491 186 ASP A CG  
1137 O OD1 . ASP A 151 ? 0.8769 1.0916 0.4777 0.0150  0.0441  -0.0325 186 ASP A OD1 
1138 O OD2 . ASP A 151 ? 0.8992 1.0835 0.4847 0.0201  0.0038  -0.0409 186 ASP A OD2 
1139 N N   . LYS A 152 ? 0.5730 0.7826 0.2437 0.0536  0.0306  -0.1371 187 LYS A N   
1140 C CA  . LYS A 152 ? 0.6113 0.8118 0.2871 0.0657  0.0285  -0.1658 187 LYS A CA  
1141 C C   . LYS A 152 ? 0.7268 0.9420 0.4399 0.0736  0.0443  -0.1734 187 LYS A C   
1142 O O   . LYS A 152 ? 0.8203 1.0282 0.5380 0.0859  0.0454  -0.1959 187 LYS A O   
1143 C CB  . LYS A 152 ? 0.7176 0.8917 0.4023 0.0639  0.0012  -0.1780 187 LYS A CB  
1144 C CG  . LYS A 152 ? 0.8840 1.0376 0.5682 0.0729  -0.0081 -0.2066 187 LYS A CG  
1145 C CD  . LYS A 152 ? 0.9083 1.0399 0.6151 0.0658  -0.0339 -0.2109 187 LYS A CD  
1146 C CE  . LYS A 152 ? 1.0047 1.1113 0.7225 0.0724  -0.0439 -0.2368 187 LYS A CE  
1147 N NZ  . LYS A 152 ? 0.7795 0.8655 0.5188 0.0615  -0.0691 -0.2378 187 LYS A NZ  
1148 N N   . ALA A 153 ? 0.6542 0.8889 0.3930 0.0670  0.0560  -0.1546 188 ALA A N   
1149 C CA  . ALA A 153 ? 0.6007 0.8494 0.3802 0.0734  0.0671  -0.1600 188 ALA A CA  
1150 C C   . ALA A 153 ? 0.7054 0.9724 0.4806 0.0851  0.0867  -0.1705 188 ALA A C   
1151 O O   . ALA A 153 ? 0.7449 1.0257 0.4908 0.0822  0.0997  -0.1621 188 ALA A O   
1152 C CB  . ALA A 153 ? 0.5719 0.8389 0.3761 0.0611  0.0752  -0.1357 188 ALA A CB  
1153 N N   . PRO A 154 ? 0.7193 0.9859 0.5227 0.0991  0.0889  -0.1887 189 PRO A N   
1154 C CA  . PRO A 154 ? 0.7523 1.0348 0.5509 0.1130  0.1062  -0.2012 189 PRO A CA  
1155 C C   . PRO A 154 ? 0.6786 1.0012 0.4916 0.1086  0.1303  -0.1833 189 PRO A C   
1156 O O   . PRO A 154 ? 0.7122 1.0518 0.4990 0.1097  0.1464  -0.1812 189 PRO A O   
1157 C CB  . PRO A 154 ? 0.7596 1.0259 0.5880 0.1289  0.0982  -0.2227 189 PRO A CB  
1158 C CG  . PRO A 154 ? 0.7747 1.0187 0.6254 0.1205  0.0778  -0.2184 189 PRO A CG  
1159 C CD  . PRO A 154 ? 0.7175 0.9761 0.5620 0.1019  0.0802  -0.1927 189 PRO A CD  
1160 N N   . ASP A 155 ? 0.7068 1.0442 0.5609 0.1022  0.1325  -0.1698 190 ASP A N   
1161 C CA  . ASP A 155 ? 0.7044 1.0795 0.5811 0.0951  0.1524  -0.1516 190 ASP A CA  
1162 C C   . ASP A 155 ? 0.6559 1.0360 0.5348 0.0724  0.1511  -0.1234 190 ASP A C   
1163 O O   . ASP A 155 ? 0.5936 0.9499 0.4635 0.0646  0.1349  -0.1186 190 ASP A O   
1164 C CB  . ASP A 155 ? 0.6635 1.0530 0.5892 0.1062  0.1553  -0.1586 190 ASP A CB  
1165 C CG  . ASP A 155 ? 0.7525 1.1208 0.7065 0.1043  0.1363  -0.1590 190 ASP A CG  
1166 O OD1 . ASP A 155 ? 0.6790 1.0353 0.6269 0.0891  0.1264  -0.1455 190 ASP A OD1 
1167 O OD2 . ASP A 155 ? 0.7529 1.1165 0.7360 0.1187  0.1315  -0.1721 190 ASP A OD2 
1168 N N   . ASP A 156 ? 0.6289 1.0398 0.5221 0.0617  0.1681  -0.1045 191 ASP A N   
1169 C CA  . ASP A 156 ? 0.6343 1.0464 0.5282 0.0389  0.1670  -0.0768 191 ASP A CA  
1170 C C   . ASP A 156 ? 0.6157 1.0262 0.5518 0.0319  0.1570  -0.0700 191 ASP A C   
1171 O O   . ASP A 156 ? 0.5811 0.9823 0.5168 0.0144  0.1507  -0.0504 191 ASP A O   
1172 C CB  . ASP A 156 ? 0.5999 1.0417 0.4906 0.0272  0.1878  -0.0581 191 ASP A CB  
1173 C CG  . ASP A 156 ? 0.7632 1.1989 0.6470 0.0022  0.1858  -0.0280 191 ASP A CG  
1174 O OD1 . ASP A 156 ? 0.7452 1.1544 0.6247 -0.0051 0.1691  -0.0214 191 ASP A OD1 
1175 O OD2 . ASP A 156 ? 0.7514 1.2076 0.6331 -0.0101 0.2013  -0.0107 191 ASP A OD2 
1176 N N   . GLU A 157 ? 0.5811 0.9969 0.5518 0.0460  0.1542  -0.0857 192 GLU A N   
1177 C CA  . GLU A 157 ? 0.6001 1.0087 0.6058 0.0413  0.1416  -0.0815 192 GLU A CA  
1178 C C   . GLU A 157 ? 0.4660 0.8412 0.4534 0.0398  0.1239  -0.0853 192 GLU A C   
1179 O O   . GLU A 157 ? 0.4501 0.8171 0.4424 0.0250  0.1168  -0.0698 192 GLU A O   
1180 C CB  . GLU A 157 ? 0.5964 1.0136 0.6387 0.0591  0.1404  -0.0977 192 GLU A CB  
1181 C CG  . GLU A 157 ? 0.8107 1.2658 0.8786 0.0597  0.1573  -0.0918 192 GLU A CG  
1182 C CD  . GLU A 157 ? 0.9799 1.4431 1.0825 0.0799  0.1556  -0.1074 192 GLU A CD  
1183 O OE1 . GLU A 157 ? 0.9658 1.4013 1.0676 0.0946  0.1420  -0.1242 192 GLU A OE1 
1184 O OE2 . GLU A 157 ? 0.8958 1.3923 1.0266 0.0809  0.1676  -0.1022 192 GLU A OE2 
1185 N N   . SER A 158 ? 0.5264 0.8810 0.4910 0.0543  0.1164  -0.1059 193 SER A N   
1186 C CA  . SER A 158 ? 0.5283 0.8529 0.4738 0.0524  0.0993  -0.1100 193 SER A CA  
1187 C C   . SER A 158 ? 0.3656 0.6847 0.2769 0.0368  0.0985  -0.0909 193 SER A C   
1188 O O   . SER A 158 ? 0.3718 0.6640 0.2843 0.0270  0.0830  -0.0786 193 SER A O   
1189 C CB  . SER A 158 ? 0.5888 0.8910 0.5167 0.0688  0.0897  -0.1358 193 SER A CB  
1190 O OG  . SER A 158 ? 0.6551 0.9672 0.5587 0.0758  0.1012  -0.1425 193 SER A OG  
1191 N N   . LYS A 159 ? 0.4556 0.7853 0.3398 0.0339  0.1101  -0.0838 194 LYS A N   
1192 C CA  . LYS A 159 ? 0.4937 0.8145 0.3456 0.0194  0.1080  -0.0626 194 LYS A CA  
1193 C C   . LYS A 159 ? 0.4306 0.7535 0.3022 0.0019  0.1080  -0.0387 194 LYS A C   
1194 O O   . LYS A 159 ? 0.3850 0.6816 0.2440 -0.0064 0.0942  -0.0257 194 LYS A O   
1195 C CB  . LYS A 159 ? 0.5395 0.8737 0.3633 0.0178  0.1230  -0.0560 194 LYS A CB  
1196 C CG  . LYS A 159 ? 0.6457 0.9748 0.4424 0.0341  0.1230  -0.0791 194 LYS A CG  
1197 C CD  . LYS A 159 ? 0.6305 0.9639 0.3853 0.0294  0.1331  -0.0683 194 LYS A CD  
1198 C CE  . LYS A 159 ? 0.7110 1.0390 0.4358 0.0454  0.1337  -0.0924 194 LYS A CE  
1199 N NZ  . LYS A 159 ? 0.7142 1.0145 0.4368 0.0552  0.1118  -0.1139 194 LYS A NZ  
1200 N N   . GLY A 160 ? 0.4758 0.8219 0.3825 -0.0034 0.1195  -0.0327 195 GLY A N   
1201 C CA  . GLY A 160 ? 0.3505 0.6950 0.2797 -0.0209 0.1168  -0.0123 195 GLY A CA  
1202 C C   . GLY A 160 ? 0.3462 0.6544 0.2927 -0.0185 0.0952  -0.0160 195 GLY A C   
1203 O O   . GLY A 160 ? 0.3837 0.6681 0.3302 -0.0306 0.0852  0.0002  195 GLY A O   
1204 N N   . PHE A 161 ? 0.3939 0.6964 0.3545 -0.0027 0.0881  -0.0371 196 PHE A N   
1205 C CA  . PHE A 161 ? 0.2822 0.5520 0.2558 -0.0014 0.0689  -0.0390 196 PHE A CA  
1206 C C   . PHE A 161 ? 0.3577 0.5989 0.3018 -0.0046 0.0563  -0.0320 196 PHE A C   
1207 O O   . PHE A 161 ? 0.2943 0.5132 0.2436 -0.0112 0.0454  -0.0208 196 PHE A O   
1208 C CB  . PHE A 161 ? 0.3376 0.6032 0.3273 0.0146  0.0628  -0.0610 196 PHE A CB  
1209 C CG  . PHE A 161 ? 0.3599 0.6484 0.3849 0.0206  0.0701  -0.0670 196 PHE A CG  
1210 C CD1 . PHE A 161 ? 0.3404 0.6455 0.3886 0.0091  0.0749  -0.0521 196 PHE A CD1 
1211 C CD2 . PHE A 161 ? 0.4628 0.7547 0.4987 0.0382  0.0701  -0.0881 196 PHE A CD2 
1212 C CE1 . PHE A 161 ? 0.3537 0.6840 0.4375 0.0151  0.0796  -0.0571 196 PHE A CE1 
1213 C CE2 . PHE A 161 ? 0.4212 0.7349 0.4917 0.0464  0.0752  -0.0932 196 PHE A CE2 
1214 C CZ  . PHE A 161 ? 0.3379 0.6733 0.4333 0.0349  0.0799  -0.0772 196 PHE A CZ  
1215 N N   . PHE A 162 ? 0.3285 0.5711 0.2410 0.0016  0.0571  -0.0397 197 PHE A N   
1216 C CA  . PHE A 162 ? 0.3101 0.5288 0.1978 0.0001  0.0426  -0.0334 197 PHE A CA  
1217 C C   . PHE A 162 ? 0.3146 0.5255 0.1883 -0.0126 0.0437  -0.0088 197 PHE A C   
1218 O O   . PHE A 162 ? 0.3775 0.5646 0.2507 -0.0147 0.0305  0.0007  197 PHE A O   
1219 C CB  . PHE A 162 ? 0.3668 0.5881 0.2197 0.0082  0.0402  -0.0459 197 PHE A CB  
1220 C CG  . PHE A 162 ? 0.3446 0.5633 0.2062 0.0203  0.0341  -0.0713 197 PHE A CG  
1221 C CD1 . PHE A 162 ? 0.4294 0.6666 0.2979 0.0294  0.0472  -0.0879 197 PHE A CD1 
1222 C CD2 . PHE A 162 ? 0.3354 0.5326 0.2049 0.0223  0.0151  -0.0779 197 PHE A CD2 
1223 C CE1 . PHE A 162 ? 0.3914 0.6193 0.2670 0.0413  0.0398  -0.1118 197 PHE A CE1 
1224 C CE2 . PHE A 162 ? 0.3856 0.5756 0.2647 0.0306  0.0078  -0.0998 197 PHE A CE2 
1225 C CZ  . PHE A 162 ? 0.4240 0.6258 0.3047 0.0406  0.0194  -0.1173 197 PHE A CZ  
1226 N N   . LYS A 163 ? 0.3795 0.6102 0.2418 -0.0208 0.0597  0.0022  198 LYS A N   
1227 C CA  . LYS A 163 ? 0.3488 0.5677 0.1961 -0.0350 0.0603  0.0276  198 LYS A CA  
1228 C C   . LYS A 163 ? 0.3784 0.5793 0.2546 -0.0435 0.0535  0.0370  198 LYS A C   
1229 O O   . LYS A 163 ? 0.3336 0.5065 0.1991 -0.0492 0.0434  0.0522  198 LYS A O   
1230 C CB  . LYS A 163 ? 0.3783 0.6256 0.2114 -0.0452 0.0806  0.0391  198 LYS A CB  
1231 C CG  . LYS A 163 ? 0.4091 0.6778 0.2092 -0.0357 0.0903  0.0280  198 LYS A CG  
1232 C CD  . LYS A 163 ? 0.4532 0.7267 0.2313 -0.0466 0.1028  0.0473  198 LYS A CD  
1233 C CE  . LYS A 163 ? 0.4529 0.7583 0.2601 -0.0536 0.1228  0.0492  198 LYS A CE  
1234 N NZ  . LYS A 163 ? 0.5600 0.8715 0.3448 -0.0642 0.1359  0.0676  198 LYS A NZ  
1235 N N   . GLY A 164 ? 0.3486 0.5639 0.2599 -0.0433 0.0578  0.0277  199 GLY A N   
1236 C CA  . GLY A 164 ? 0.3295 0.5277 0.2648 -0.0511 0.0501  0.0347  199 GLY A CA  
1237 C C   . GLY A 164 ? 0.3548 0.5219 0.2890 -0.0427 0.0331  0.0305  199 GLY A C   
1238 O O   . GLY A 164 ? 0.3773 0.5182 0.3084 -0.0482 0.0246  0.0416  199 GLY A O   
1239 N N   . ALA A 165 ? 0.3395 0.5090 0.2753 -0.0293 0.0281  0.0143  200 ALA A N   
1240 C CA  . ALA A 165 ? 0.3147 0.4623 0.2530 -0.0218 0.0137  0.0107  200 ALA A CA  
1241 C C   . ALA A 165 ? 0.3421 0.4708 0.2542 -0.0209 0.0054  0.0223  200 ALA A C   
1242 O O   . ALA A 165 ? 0.3338 0.4417 0.2485 -0.0185 -0.0042 0.0276  200 ALA A O   
1243 C CB  . ALA A 165 ? 0.2948 0.4508 0.2410 -0.0109 0.0102  -0.0076 200 ALA A CB  
1244 N N   . MET A 166 ? 0.3924 0.5288 0.2777 -0.0212 0.0088  0.0259  201 MET A N   
1245 C CA  . MET A 166 ? 0.3944 0.5133 0.2525 -0.0198 -0.0004 0.0392  201 MET A CA  
1246 C C   . MET A 166 ? 0.4304 0.5262 0.2841 -0.0293 -0.0010 0.0586  201 MET A C   
1247 O O   . MET A 166 ? 0.4106 0.4813 0.2609 -0.0241 -0.0129 0.0656  201 MET A O   
1248 C CB  . MET A 166 ? 0.4052 0.5393 0.2321 -0.0197 0.0049  0.0397  201 MET A CB  
1249 C CG  . MET A 166 ? 0.3464 0.4924 0.1719 -0.0088 -0.0013 0.0198  201 MET A CG  
1250 S SD  . MET A 166 ? 0.4368 0.6000 0.2193 -0.0072 0.0046  0.0166  201 MET A SD  
1251 C CE  . MET A 166 ? 0.4942 0.6718 0.2922 0.0026  0.0038  -0.0143 201 MET A CE  
1252 N N   . ALA A 167 ? 0.3729 0.4773 0.2293 -0.0431 0.0115  0.0668  202 ALA A N   
1253 C CA  . ALA A 167 ? 0.4010 0.4810 0.2533 -0.0558 0.0100  0.0855  202 ALA A CA  
1254 C C   . ALA A 167 ? 0.3819 0.4391 0.2557 -0.0532 0.0005  0.0808  202 ALA A C   
1255 O O   . ALA A 167 ? 0.3949 0.4188 0.2592 -0.0559 -0.0082 0.0925  202 ALA A O   
1256 C CB  . ALA A 167 ? 0.3709 0.4722 0.2284 -0.0736 0.0257  0.0943  202 ALA A CB  
1257 N N   . SER A 168 ? 0.3300 0.4021 0.2297 -0.0468 0.0013  0.0637  203 SER A N   
1258 C CA  . SER A 168 ? 0.4310 0.4844 0.3476 -0.0449 -0.0062 0.0591  203 SER A CA  
1259 C C   . SER A 168 ? 0.4152 0.4521 0.3290 -0.0288 -0.0173 0.0537  203 SER A C   
1260 O O   . SER A 168 ? 0.3439 0.3540 0.2568 -0.0261 -0.0245 0.0561  203 SER A O   
1261 C CB  . SER A 168 ? 0.2751 0.3515 0.2196 -0.0465 -0.0008 0.0465  203 SER A CB  
1262 O OG  . SER A 168 ? 0.3210 0.4187 0.2734 -0.0602 0.0099  0.0516  203 SER A OG  
1263 N N   . LEU A 169 ? 0.4003 0.4534 0.3133 -0.0179 -0.0190 0.0457  204 LEU A N   
1264 C CA  . LEU A 169 ? 0.3335 0.3797 0.2495 -0.0036 -0.0289 0.0413  204 LEU A CA  
1265 C C   . LEU A 169 ? 0.3929 0.4269 0.2882 0.0042  -0.0378 0.0510  204 LEU A C   
1266 O O   . LEU A 169 ? 0.3722 0.3933 0.2707 0.0159  -0.0460 0.0515  204 LEU A O   
1267 C CB  . LEU A 169 ? 0.3505 0.4206 0.2829 0.0028  -0.0292 0.0273  204 LEU A CB  
1268 C CG  . LEU A 169 ? 0.4420 0.5179 0.3983 0.0032  -0.0268 0.0177  204 LEU A CG  
1269 C CD1 . LEU A 169 ? 0.4375 0.5325 0.4040 0.0068  -0.0284 0.0076  204 LEU A CD1 
1270 C CD2 . LEU A 169 ? 0.4306 0.4919 0.3902 0.0119  -0.0324 0.0197  204 LEU A CD2 
1271 N N   . ASN A 170 ? 0.4263 0.4671 0.3006 0.0005  -0.0369 0.0578  205 ASN A N   
1272 C CA  . ASN A 170 ? 0.3536 0.3837 0.2073 0.0095  -0.0482 0.0676  205 ASN A CA  
1273 C C   . ASN A 170 ? 0.4405 0.4349 0.2857 0.0140  -0.0559 0.0807  205 ASN A C   
1274 O O   . ASN A 170 ? 0.4561 0.4432 0.2991 0.0291  -0.0679 0.0831  205 ASN A O   
1275 C CB  . ASN A 170 ? 0.4094 0.4498 0.2349 0.0028  -0.0451 0.0750  205 ASN A CB  
1276 C CG  . ASN A 170 ? 0.4827 0.5532 0.3117 0.0058  -0.0440 0.0588  205 ASN A CG  
1277 O OD1 . ASN A 170 ? 0.4967 0.5774 0.3482 0.0134  -0.0496 0.0456  205 ASN A OD1 
1278 N ND2 . ASN A 170 ? 0.4419 0.5261 0.2481 -0.0004 -0.0365 0.0594  205 ASN A ND2 
1279 N N   . PRO A 171 ? 0.4384 0.4094 0.2801 0.0025  -0.0512 0.0887  206 PRO A N   
1280 C CA  . PRO A 171 ? 0.5119 0.4422 0.3457 0.0088  -0.0608 0.0977  206 PRO A CA  
1281 C C   . PRO A 171 ? 0.4823 0.4095 0.3348 0.0273  -0.0668 0.0850  206 PRO A C   
1282 O O   . PRO A 171 ? 0.5006 0.4029 0.3456 0.0424  -0.0774 0.0901  206 PRO A O   
1283 C CB  . PRO A 171 ? 0.4837 0.3955 0.3174 -0.0105 -0.0543 0.1032  206 PRO A CB  
1284 C CG  . PRO A 171 ? 0.4610 0.4019 0.2915 -0.0268 -0.0422 0.1072  206 PRO A CG  
1285 C CD  . PRO A 171 ? 0.4452 0.4244 0.2892 -0.0170 -0.0385 0.0909  206 PRO A CD  
1286 N N   . TYR A 172 ? 0.4532 0.4048 0.3295 0.0273  -0.0598 0.0693  207 TYR A N   
1287 C CA  . TYR A 172 ? 0.3723 0.3275 0.2656 0.0440  -0.0627 0.0584  207 TYR A CA  
1288 C C   . TYR A 172 ? 0.4195 0.4011 0.3216 0.0580  -0.0687 0.0561  207 TYR A C   
1289 O O   . TYR A 172 ? 0.4167 0.3959 0.3261 0.0759  -0.0750 0.0546  207 TYR A O   
1290 C CB  . TYR A 172 ? 0.3261 0.2979 0.2392 0.0381  -0.0538 0.0454  207 TYR A CB  
1291 C CG  . TYR A 172 ? 0.3748 0.3220 0.2830 0.0264  -0.0510 0.0455  207 TYR A CG  
1292 C CD1 . TYR A 172 ? 0.4220 0.3698 0.3259 0.0072  -0.0464 0.0517  207 TYR A CD1 
1293 C CD2 . TYR A 172 ? 0.4326 0.3587 0.3409 0.0344  -0.0533 0.0387  207 TYR A CD2 
1294 C CE1 . TYR A 172 ? 0.4221 0.3512 0.3255 -0.0058 -0.0458 0.0522  207 TYR A CE1 
1295 C CE2 . TYR A 172 ? 0.4062 0.3089 0.3089 0.0221  -0.0536 0.0375  207 TYR A CE2 
1296 C CZ  . TYR A 172 ? 0.4047 0.3097 0.3069 0.0010  -0.0507 0.0448  207 TYR A CZ  
1297 O OH  . TYR A 172 ? 0.4541 0.3401 0.3547 -0.0133 -0.0528 0.0442  207 TYR A OH  
1298 N N   . VAL A 173 ? 0.3651 0.3732 0.2673 0.0507  -0.0675 0.0550  208 VAL A N   
1299 C CA  . VAL A 173 ? 0.3950 0.4270 0.3039 0.0614  -0.0766 0.0532  208 VAL A CA  
1300 C C   . VAL A 173 ? 0.3950 0.4084 0.2881 0.0753  -0.0895 0.0657  208 VAL A C   
1301 O O   . VAL A 173 ? 0.4476 0.4723 0.3557 0.0921  -0.0979 0.0639  208 VAL A O   
1302 C CB  . VAL A 173 ? 0.4228 0.4776 0.3253 0.0507  -0.0754 0.0496  208 VAL A CB  
1303 C CG1 . VAL A 173 ? 0.3631 0.4404 0.2710 0.0602  -0.0884 0.0475  208 VAL A CG1 
1304 C CG2 . VAL A 173 ? 0.3526 0.4236 0.2730 0.0402  -0.0645 0.0367  208 VAL A CG2 
1305 N N   . LYS A 174 ? 0.4932 0.4788 0.3571 0.0686  -0.0914 0.0798  209 LYS A N   
1306 C CA  . LYS A 174 ? 0.4647 0.4273 0.3100 0.0818  -0.1056 0.0944  209 LYS A CA  
1307 C C   . LYS A 174 ? 0.5152 0.4496 0.3683 0.0988  -0.1103 0.0944  209 LYS A C   
1308 O O   . LYS A 174 ? 0.6166 0.5412 0.4664 0.1178  -0.1237 0.1016  209 LYS A O   
1309 C CB  . LYS A 174 ? 0.5107 0.4475 0.3202 0.0682  -0.1059 0.1126  209 LYS A CB  
1310 C CG  . LYS A 174 ? 0.5860 0.5463 0.3835 0.0492  -0.0953 0.1114  209 LYS A CG  
1311 C CD  . LYS A 174 ? 0.6530 0.6355 0.4336 0.0535  -0.1047 0.1140  209 LYS A CD  
1312 C CE  . LYS A 174 ? 0.6629 0.6789 0.4438 0.0413  -0.0940 0.1008  209 LYS A CE  
1313 N NZ  . LYS A 174 ? 0.5807 0.6260 0.3944 0.0473  -0.0954 0.0802  209 LYS A NZ  
1314 N N   . ALA A 175 ? 0.5299 0.4511 0.3925 0.0942  -0.1005 0.0857  210 ALA A N   
1315 C CA  . ALA A 175 ? 0.5453 0.4400 0.4131 0.1118  -0.1039 0.0813  210 ALA A CA  
1316 C C   . ALA A 175 ? 0.5185 0.4483 0.4167 0.1298  -0.1015 0.0670  210 ALA A C   
1317 O O   . ALA A 175 ? 0.5166 0.4312 0.4204 0.1478  -0.1021 0.0607  210 ALA A O   
1318 C CB  . ALA A 175 ? 0.5056 0.3693 0.3662 0.0983  -0.0962 0.0774  210 ALA A CB  
1319 N N   . GLY A 176 ? 0.4079 0.3840 0.3254 0.1254  -0.0990 0.0619  211 GLY A N   
1320 C CA  . GLY A 176 ? 0.4261 0.4401 0.3754 0.1374  -0.0954 0.0507  211 GLY A CA  
1321 C C   . GLY A 176 ? 0.4371 0.4579 0.3986 0.1300  -0.0810 0.0388  211 GLY A C   
1322 O O   . GLY A 176 ? 0.4178 0.4611 0.4008 0.1424  -0.0759 0.0310  211 GLY A O   
1323 N N   . LYS A 177 ? 0.3977 0.4023 0.3461 0.1101  -0.0740 0.0381  212 LYS A N   
1324 C CA  . LYS A 177 ? 0.3823 0.3853 0.3365 0.1038  -0.0631 0.0285  212 LYS A CA  
1325 C C   . LYS A 177 ? 0.3488 0.3816 0.3178 0.0872  -0.0554 0.0235  212 LYS A C   
1326 O O   . LYS A 177 ? 0.3823 0.4144 0.3550 0.0810  -0.0475 0.0172  212 LYS A O   
1327 C CB  . LYS A 177 ? 0.3983 0.3574 0.3291 0.0950  -0.0631 0.0309  212 LYS A CB  
1328 C CG  . LYS A 177 ? 0.5324 0.4524 0.4472 0.1116  -0.0712 0.0336  212 LYS A CG  
1329 C CD  . LYS A 177 ? 0.5954 0.4699 0.4888 0.0997  -0.0728 0.0349  212 LYS A CD  
1330 C CE  . LYS A 177 ? 0.6612 0.4995 0.5438 0.1199  -0.0776 0.0276  212 LYS A CE  
1331 N NZ  . LYS A 177 ? 0.6843 0.4809 0.5490 0.1071  -0.0796 0.0240  212 LYS A NZ  
1332 N N   . PHE A 178 ? 0.3209 0.3765 0.2961 0.0800  -0.0587 0.0256  213 PHE A N   
1333 C CA  . PHE A 178 ? 0.3318 0.4116 0.3217 0.0667  -0.0530 0.0195  213 PHE A CA  
1334 C C   . PHE A 178 ? 0.3832 0.4968 0.4000 0.0728  -0.0537 0.0155  213 PHE A C   
1335 O O   . PHE A 178 ? 0.3326 0.4640 0.3573 0.0789  -0.0624 0.0178  213 PHE A O   
1336 C CB  . PHE A 178 ? 0.3052 0.3888 0.2849 0.0548  -0.0557 0.0211  213 PHE A CB  
1337 C CG  . PHE A 178 ? 0.3252 0.4276 0.3189 0.0436  -0.0511 0.0131  213 PHE A CG  
1338 C CD1 . PHE A 178 ? 0.3115 0.4077 0.3091 0.0357  -0.0427 0.0094  213 PHE A CD1 
1339 C CD2 . PHE A 178 ? 0.3481 0.4731 0.3526 0.0419  -0.0572 0.0088  213 PHE A CD2 
1340 C CE1 . PHE A 178 ? 0.2583 0.3681 0.2692 0.0275  -0.0398 0.0027  213 PHE A CE1 
1341 C CE2 . PHE A 178 ? 0.3241 0.4601 0.3411 0.0321  -0.0544 0.0007  213 PHE A CE2 
1342 C CZ  . PHE A 178 ? 0.2755 0.4029 0.2958 0.0259  -0.0454 -0.0018 213 PHE A CZ  
1343 N N   . LYS A 179 ? 0.2480 0.3722 0.2790 0.0700  -0.0451 0.0108  214 LYS A N   
1344 C CA  . LYS A 179 ? 0.3346 0.4931 0.3932 0.0725  -0.0438 0.0094  214 LYS A CA  
1345 C C   . LYS A 179 ? 0.2203 0.3890 0.2899 0.0556  -0.0406 0.0064  214 LYS A C   
1346 O O   . LYS A 179 ? 0.2052 0.3696 0.2755 0.0509  -0.0323 0.0053  214 LYS A O   
1347 C CB  . LYS A 179 ? 0.2981 0.4622 0.3630 0.0860  -0.0355 0.0085  214 LYS A CB  
1348 C CG  . LYS A 179 ? 0.4269 0.5745 0.4799 0.1058  -0.0394 0.0097  214 LYS A CG  
1349 C CD  . LYS A 179 ? 0.4604 0.6283 0.5269 0.1169  -0.0499 0.0138  214 LYS A CD  
1350 C CE  . LYS A 179 ? 0.4498 0.5949 0.5029 0.1391  -0.0544 0.0153  214 LYS A CE  
1351 N NZ  . LYS A 179 ? 0.5718 0.7360 0.6376 0.1520  -0.0673 0.0208  214 LYS A NZ  
1352 N N   . PRO A 180 ? 0.2149 0.3948 0.2914 0.0468  -0.0484 0.0046  215 PRO A N   
1353 C CA  . PRO A 180 ? 0.1763 0.3599 0.2626 0.0322  -0.0470 0.0007  215 PRO A CA  
1354 C C   . PRO A 180 ? 0.2026 0.4097 0.3153 0.0283  -0.0432 0.0033  215 PRO A C   
1355 O O   . PRO A 180 ? 0.2231 0.4533 0.3516 0.0362  -0.0425 0.0071  215 PRO A O   
1356 C CB  . PRO A 180 ? 0.1727 0.3602 0.2563 0.0266  -0.0582 -0.0039 215 PRO A CB  
1357 C CG  . PRO A 180 ? 0.3669 0.5690 0.4535 0.0370  -0.0665 0.0000  215 PRO A CG  
1358 C CD  . PRO A 180 ? 0.2340 0.4212 0.3072 0.0504  -0.0603 0.0055  215 PRO A CD  
1359 N N   . PHE A 181 ? 0.2182 0.4201 0.3364 0.0162  -0.0405 0.0022  216 PHE A N   
1360 C CA  . PHE A 181 ? 0.2369 0.4579 0.3794 0.0067  -0.0386 0.0066  216 PHE A CA  
1361 C C   . PHE A 181 ? 0.2006 0.4155 0.3512 -0.0076 -0.0481 0.0019  216 PHE A C   
1362 O O   . PHE A 181 ? 0.2358 0.4329 0.3711 -0.0078 -0.0538 -0.0063 216 PHE A O   
1363 C CB  . PHE A 181 ? 0.1144 0.3295 0.2526 0.0063  -0.0268 0.0120  216 PHE A CB  
1364 C CG  . PHE A 181 ? 0.1645 0.3504 0.2833 0.0038  -0.0259 0.0086  216 PHE A CG  
1365 C CD1 . PHE A 181 ? 0.1528 0.3271 0.2763 -0.0072 -0.0307 0.0067  216 PHE A CD1 
1366 C CD2 . PHE A 181 ? 0.1568 0.3268 0.2547 0.0129  -0.0217 0.0069  216 PHE A CD2 
1367 C CE1 . PHE A 181 ? 0.2054 0.3577 0.3151 -0.0071 -0.0301 0.0034  216 PHE A CE1 
1368 C CE2 . PHE A 181 ? 0.1519 0.3006 0.2365 0.0097  -0.0217 0.0043  216 PHE A CE2 
1369 C CZ  . PHE A 181 ? 0.2319 0.3745 0.3239 0.0006  -0.0255 0.0028  216 PHE A CZ  
1370 N N   . SER A 182 ? 0.1488 0.3781 0.3231 -0.0199 -0.0495 0.0069  217 SER A N   
1371 C CA  . SER A 182 ? 0.2325 0.4502 0.4151 -0.0344 -0.0603 0.0018  217 SER A CA  
1372 C C   . SER A 182 ? 0.3092 0.5183 0.5013 -0.0458 -0.0555 0.0101  217 SER A C   
1373 O O   . SER A 182 ? 0.2903 0.5218 0.5025 -0.0534 -0.0508 0.0215  217 SER A O   
1374 C CB  . SER A 182 ? 0.2847 0.5254 0.4892 -0.0426 -0.0728 0.0003  217 SER A CB  
1375 O OG  . SER A 182 ? 0.2792 0.5040 0.4895 -0.0569 -0.0855 -0.0069 217 SER A OG  
1376 N N   . GLY A 183 ? 0.2807 0.4594 0.4595 -0.0470 -0.0573 0.0052  218 GLY A N   
1377 C CA  . GLY A 183 ? 0.2604 0.4249 0.4454 -0.0568 -0.0557 0.0138  218 GLY A CA  
1378 C C   . GLY A 183 ? 0.1969 0.3728 0.3776 -0.0532 -0.0418 0.0271  218 GLY A C   
1379 O O   . GLY A 183 ? 0.2586 0.4413 0.4247 -0.0400 -0.0337 0.0256  218 GLY A O   
1380 N N   . ASN A 184 ? 0.1464 0.3221 0.3375 -0.0655 -0.0397 0.0403  219 ASN A N   
1381 C CA  . ASN A 184 ? 0.1477 0.3338 0.3310 -0.0635 -0.0265 0.0538  219 ASN A CA  
1382 C C   . ASN A 184 ? 0.2152 0.4380 0.4043 -0.0559 -0.0156 0.0561  219 ASN A C   
1383 O O   . ASN A 184 ? 0.2223 0.4732 0.4365 -0.0638 -0.0163 0.0602  219 ASN A O   
1384 C CB  . ASN A 184 ? 0.2072 0.3896 0.4021 -0.0811 -0.0267 0.0703  219 ASN A CB  
1385 C CG  . ASN A 184 ? 0.2907 0.4325 0.4796 -0.0860 -0.0384 0.0691  219 ASN A CG  
1386 O OD1 . ASN A 184 ? 0.2610 0.3813 0.4371 -0.0748 -0.0441 0.0557  219 ASN A OD1 
1387 N ND2 . ASN A 184 ? 0.2841 0.4163 0.4835 -0.1026 -0.0417 0.0840  219 ASN A ND2 
1388 N N   . THR A 185 ? 0.1619 0.3844 0.3292 -0.0404 -0.0065 0.0532  220 THR A N   
1389 C CA  . THR A 185 ? 0.2515 0.5011 0.4195 -0.0270 0.0027  0.0512  220 THR A CA  
1390 C C   . THR A 185 ? 0.1821 0.4295 0.3256 -0.0159 0.0152  0.0536  220 THR A C   
1391 O O   . THR A 185 ? 0.2055 0.4246 0.3245 -0.0110 0.0127  0.0487  220 THR A O   
1392 C CB  . THR A 185 ? 0.1806 0.4231 0.3429 -0.0150 -0.0049 0.0377  220 THR A CB  
1393 O OG1 . THR A 185 ? 0.2560 0.4997 0.4359 -0.0247 -0.0175 0.0338  220 THR A OG1 
1394 C CG2 . THR A 185 ? 0.1867 0.4544 0.3518 0.0007  0.0025  0.0363  220 THR A CG2 
1395 N N   . ASP A 186 ? 0.1792 0.4586 0.3295 -0.0120 0.0284  0.0606  221 ASP A N   
1396 C CA  . ASP A 186 ? 0.2352 0.5142 0.3588 0.0024  0.0405  0.0590  221 ASP A CA  
1397 C C   . ASP A 186 ? 0.2722 0.5418 0.3834 0.0222  0.0384  0.0445  221 ASP A C   
1398 O O   . ASP A 186 ? 0.2375 0.5295 0.3670 0.0310  0.0389  0.0412  221 ASP A O   
1399 C CB  . ASP A 186 ? 0.1796 0.4994 0.3138 0.0024  0.0575  0.0701  221 ASP A CB  
1400 C CG  . ASP A 186 ? 0.3032 0.6247 0.4374 -0.0171 0.0617  0.0876  221 ASP A CG  
1401 O OD1 . ASP A 186 ? 0.3144 0.6031 0.4419 -0.0289 0.0497  0.0903  221 ASP A OD1 
1402 O OD2 . ASP A 186 ? 0.2965 0.6532 0.4380 -0.0200 0.0774  0.0995  221 ASP A OD2 
1403 N N   . LEU A 187 ? 0.2452 0.4807 0.3270 0.0282  0.0342  0.0367  222 LEU A N   
1404 C CA  . LEU A 187 ? 0.2804 0.4980 0.3454 0.0445  0.0313  0.0245  222 LEU A CA  
1405 C C   . LEU A 187 ? 0.3693 0.5898 0.4116 0.0598  0.0430  0.0205  222 LEU A C   
1406 O O   . LEU A 187 ? 0.4717 0.7238 0.5220 0.0624  0.0561  0.0266  222 LEU A O   
1407 C CB  . LEU A 187 ? 0.2640 0.4449 0.3131 0.0393  0.0194  0.0188  222 LEU A CB  
1408 C CG  . LEU A 187 ? 0.1980 0.3769 0.2663 0.0255  0.0098  0.0213  222 LEU A CG  
1409 C CD1 . LEU A 187 ? 0.2283 0.3777 0.2828 0.0218  0.0009  0.0159  222 LEU A CD1 
1410 C CD2 . LEU A 187 ? 0.2750 0.4720 0.3643 0.0281  0.0062  0.0198  222 LEU A CD2 
1411 N N   . VAL A 188 ? 0.3525 0.5421 0.3679 0.0708  0.0388  0.0095  223 VAL A N   
1412 C CA  . VAL A 188 ? 0.2852 0.4659 0.2701 0.0843  0.0467  0.0023  223 VAL A CA  
1413 C C   . VAL A 188 ? 0.3416 0.5390 0.3176 0.0762  0.0567  0.0116  223 VAL A C   
1414 O O   . VAL A 188 ? 0.3149 0.5067 0.2951 0.0586  0.0507  0.0210  223 VAL A O   
1415 C CB  . VAL A 188 ? 0.3479 0.4836 0.3042 0.0854  0.0349  -0.0080 223 VAL A CB  
1416 C CG1 . VAL A 188 ? 0.4511 0.5719 0.3719 0.0895  0.0380  -0.0136 223 VAL A CG1 
1417 C CG2 . VAL A 188 ? 0.4297 0.5478 0.3840 0.1003  0.0298  -0.0176 223 VAL A CG2 
1418 N N   . PRO A 189 ? 0.3266 0.5464 0.2906 0.0893  0.0727  0.0103  224 PRO A N   
1419 C CA  . PRO A 189 ? 0.3435 0.5756 0.2897 0.0818  0.0826  0.0201  224 PRO A CA  
1420 C C   . PRO A 189 ? 0.2934 0.4891 0.2110 0.0713  0.0699  0.0200  224 PRO A C   
1421 O O   . PRO A 189 ? 0.3154 0.4790 0.2056 0.0797  0.0616  0.0061  224 PRO A O   
1422 C CB  . PRO A 189 ? 0.3517 0.5987 0.2747 0.1042  0.0991  0.0102  224 PRO A CB  
1423 C CG  . PRO A 189 ? 0.3689 0.6362 0.3213 0.1196  0.1026  0.0038  224 PRO A CG  
1424 C CD  . PRO A 189 ? 0.2852 0.5193 0.2492 0.1134  0.0824  -0.0005 224 PRO A CD  
1425 N N   . GLY A 190 ? 0.3713 0.5708 0.2962 0.0529  0.0669  0.0357  225 GLY A N   
1426 C CA  . GLY A 190 ? 0.2923 0.4616 0.1961 0.0434  0.0532  0.0376  225 GLY A CA  
1427 C C   . GLY A 190 ? 0.2723 0.4242 0.2003 0.0316  0.0371  0.0389  225 GLY A C   
1428 O O   . GLY A 190 ? 0.2833 0.4171 0.2028 0.0229  0.0258  0.0434  225 GLY A O   
1429 N N   . ILE A 191 ? 0.2366 0.3941 0.1929 0.0325  0.0353  0.0345  226 ILE A N   
1430 C CA  . ILE A 191 ? 0.2461 0.3889 0.2222 0.0229  0.0219  0.0341  226 ILE A CA  
1431 C C   . ILE A 191 ? 0.2632 0.4272 0.2738 0.0156  0.0242  0.0409  226 ILE A C   
1432 O O   . ILE A 191 ? 0.2331 0.4182 0.2567 0.0225  0.0316  0.0387  226 ILE A O   
1433 C CB  . ILE A 191 ? 0.2395 0.3613 0.2097 0.0300  0.0138  0.0201  226 ILE A CB  
1434 C CG1 . ILE A 191 ? 0.2972 0.3961 0.2339 0.0348  0.0090  0.0123  226 ILE A CG1 
1435 C CG2 . ILE A 191 ? 0.2675 0.3784 0.2556 0.0199  0.0022  0.0204  226 ILE A CG2 
1436 C CD1 . ILE A 191 ? 0.2354 0.3124 0.1647 0.0407  0.0022  -0.0002 226 ILE A CD1 
1437 N N   . LYS A 192 ? 0.2131 0.3708 0.2386 0.0025  0.0163  0.0485  227 LYS A N   
1438 C CA  . LYS A 192 ? 0.2045 0.3755 0.2608 -0.0073 0.0147  0.0538  227 LYS A CA  
1439 C C   . LYS A 192 ? 0.3004 0.4523 0.3672 -0.0108 0.0018  0.0464  227 LYS A C   
1440 O O   . LYS A 192 ? 0.2219 0.3533 0.2787 -0.0114 -0.0056 0.0445  227 LYS A O   
1441 C CB  . LYS A 192 ? 0.2319 0.4093 0.2952 -0.0210 0.0170  0.0706  227 LYS A CB  
1442 C CG  . LYS A 192 ? 0.3247 0.5274 0.3798 -0.0205 0.0323  0.0813  227 LYS A CG  
1443 C CD  . LYS A 192 ? 0.3625 0.5640 0.4214 -0.0374 0.0322  0.1012  227 LYS A CD  
1444 C CE  . LYS A 192 ? 0.4546 0.6926 0.5267 -0.0457 0.0475  0.1162  227 LYS A CE  
1445 N NZ  . LYS A 192 ? 0.4589 0.6888 0.5209 -0.0607 0.0483  0.1377  227 LYS A NZ  
1446 N N   . ALA A 193 ? 0.2041 0.3653 0.2911 -0.0126 -0.0010 0.0420  228 ALA A N   
1447 C CA  . ALA A 193 ? 0.1703 0.3165 0.2669 -0.0167 -0.0117 0.0352  228 ALA A CA  
1448 C C   . ALA A 193 ? 0.2042 0.3461 0.3172 -0.0297 -0.0172 0.0429  228 ALA A C   
1449 O O   . ALA A 193 ? 0.1985 0.3575 0.3271 -0.0383 -0.0143 0.0512  228 ALA A O   
1450 C CB  . ALA A 193 ? 0.1793 0.3343 0.2840 -0.0122 -0.0141 0.0260  228 ALA A CB  
1451 N N   . LEU A 194 ? 0.1671 0.2863 0.2782 -0.0312 -0.0255 0.0408  229 LEU A N   
1452 C CA  . LEU A 194 ? 0.2416 0.3467 0.3664 -0.0415 -0.0336 0.0458  229 LEU A CA  
1453 C C   . LEU A 194 ? 0.1978 0.2885 0.3294 -0.0384 -0.0429 0.0311  229 LEU A C   
1454 O O   . LEU A 194 ? 0.1766 0.2584 0.2999 -0.0293 -0.0445 0.0231  229 LEU A O   
1455 C CB  . LEU A 194 ? 0.2296 0.3184 0.3443 -0.0429 -0.0358 0.0573  229 LEU A CB  
1456 C CG  . LEU A 194 ? 0.3458 0.4121 0.4729 -0.0518 -0.0464 0.0632  229 LEU A CG  
1457 C CD1 . LEU A 194 ? 0.3044 0.3807 0.4424 -0.0678 -0.0428 0.0792  229 LEU A CD1 
1458 C CD2 . LEU A 194 ? 0.2928 0.3384 0.4088 -0.0467 -0.0527 0.0694  229 LEU A CD2 
1459 N N   . ALA A 195 ? 0.1845 0.2737 0.3312 -0.0464 -0.0493 0.0275  230 ALA A N   
1460 C CA  . ALA A 195 ? 0.1895 0.2661 0.3384 -0.0424 -0.0575 0.0111  230 ALA A CA  
1461 C C   . ALA A 195 ? 0.1934 0.2428 0.3421 -0.0384 -0.0646 0.0081  230 ALA A C   
1462 O O   . ALA A 195 ? 0.2486 0.2805 0.4043 -0.0461 -0.0706 0.0177  230 ALA A O   
1463 C CB  . ALA A 195 ? 0.2571 0.3369 0.4205 -0.0531 -0.0651 0.0073  230 ALA A CB  
1464 N N   . SER A 196 ? 0.1894 0.2362 0.3310 -0.0260 -0.0638 -0.0041 231 SER A N   
1465 C CA  . SER A 196 ? 0.2569 0.2835 0.4013 -0.0177 -0.0700 -0.0098 231 SER A CA  
1466 C C   . SER A 196 ? 0.2545 0.2807 0.3972 -0.0085 -0.0709 -0.0299 231 SER A C   
1467 O O   . SER A 196 ? 0.2235 0.2552 0.3641 0.0030  -0.0672 -0.0373 231 SER A O   
1468 C CB  . SER A 196 ? 0.2500 0.2806 0.3892 -0.0109 -0.0667 -0.0020 231 SER A CB  
1469 O OG  . SER A 196 ? 0.2238 0.2749 0.3543 -0.0059 -0.0582 -0.0066 231 SER A OG  
1470 N N   . HIS A 197 ? 0.2869 0.3104 0.4302 -0.0143 -0.0754 -0.0384 232 HIS A N   
1471 C CA  . HIS A 197 ? 0.2881 0.3147 0.4231 -0.0064 -0.0752 -0.0575 232 HIS A CA  
1472 C C   . HIS A 197 ? 0.3246 0.3320 0.4617 0.0062  -0.0794 -0.0717 232 HIS A C   
1473 O O   . HIS A 197 ? 0.2486 0.2287 0.3949 0.0053  -0.0893 -0.0711 232 HIS A O   
1474 C CB  . HIS A 197 ? 0.2529 0.2785 0.3867 -0.0158 -0.0828 -0.0643 232 HIS A CB  
1475 C CG  . HIS A 197 ? 0.2644 0.3121 0.4011 -0.0262 -0.0798 -0.0513 232 HIS A CG  
1476 N ND1 . HIS A 197 ? 0.2105 0.2782 0.3420 -0.0230 -0.0688 -0.0405 232 HIS A ND1 
1477 C CD2 . HIS A 197 ? 0.2007 0.2554 0.3454 -0.0381 -0.0869 -0.0493 232 HIS A CD2 
1478 C CE1 . HIS A 197 ? 0.2061 0.2911 0.3422 -0.0303 -0.0682 -0.0326 232 HIS A CE1 
1479 N NE2 . HIS A 197 ? 0.2718 0.3525 0.4178 -0.0398 -0.0788 -0.0369 232 HIS A NE2 
1480 N N   . GLY A 198 ? 0.2220 0.2436 0.3502 0.0181  -0.0717 -0.0848 233 GLY A N   
1481 C CA  . GLY A 198 ? 0.3315 0.3402 0.4598 0.0327  -0.0740 -0.1036 233 GLY A CA  
1482 C C   . GLY A 198 ? 0.2704 0.3028 0.3985 0.0469  -0.0616 -0.1091 233 GLY A C   
1483 O O   . GLY A 198 ? 0.2861 0.3228 0.4066 0.0588  -0.0574 -0.1273 233 GLY A O   
1484 N N   . HIS A 199 ? 0.2126 0.2628 0.3479 0.0449  -0.0553 -0.0938 234 HIS A N   
1485 C CA  . HIS A 199 ? 0.2629 0.3430 0.3982 0.0522  -0.0426 -0.0962 234 HIS A CA  
1486 C C   . HIS A 199 ? 0.2102 0.3065 0.3253 0.0480  -0.0341 -0.1014 234 HIS A C   
1487 O O   . HIS A 199 ? 0.2306 0.3446 0.3396 0.0566  -0.0244 -0.1123 234 HIS A O   
1488 C CB  . HIS A 199 ? 0.2102 0.3034 0.3540 0.0463  -0.0404 -0.0784 234 HIS A CB  
1489 C CG  . HIS A 199 ? 0.2113 0.3351 0.3581 0.0490  -0.0290 -0.0781 234 HIS A CG  
1490 N ND1 . HIS A 199 ? 0.2370 0.3780 0.3973 0.0627  -0.0234 -0.0887 234 HIS A ND1 
1491 C CD2 . HIS A 199 ? 0.1474 0.2880 0.2868 0.0392  -0.0221 -0.0682 234 HIS A CD2 
1492 C CE1 . HIS A 199 ? 0.2016 0.3724 0.3646 0.0589  -0.0130 -0.0838 234 HIS A CE1 
1493 N NE2 . HIS A 199 ? 0.1867 0.3544 0.3360 0.0441  -0.0129 -0.0713 234 HIS A NE2 
1494 N N   . THR A 200 ? 0.1936 0.2862 0.2983 0.0356  -0.0372 -0.0924 235 THR A N   
1495 C CA  . THR A 200 ? 0.1944 0.2950 0.2785 0.0312  -0.0346 -0.0960 235 THR A CA  
1496 C C   . THR A 200 ? 0.2218 0.3058 0.3048 0.0231  -0.0465 -0.0959 235 THR A C   
1497 O O   . THR A 200 ? 0.2405 0.3105 0.3379 0.0174  -0.0538 -0.0878 235 THR A O   
1498 C CB  . THR A 200 ? 0.1973 0.3154 0.2741 0.0246  -0.0265 -0.0815 235 THR A CB  
1499 O OG1 . THR A 200 ? 0.2161 0.3273 0.3013 0.0168  -0.0311 -0.0671 235 THR A OG1 
1500 C CG2 . THR A 200 ? 0.1652 0.3026 0.2473 0.0290  -0.0152 -0.0799 235 THR A CG2 
1501 N N   . PRO A 201 ? 0.2410 0.3269 0.3072 0.0206  -0.0501 -0.1034 236 PRO A N   
1502 C CA  . PRO A 201 ? 0.3205 0.3944 0.3901 0.0112  -0.0636 -0.1041 236 PRO A CA  
1503 C C   . PRO A 201 ? 0.2529 0.3322 0.3364 0.0007  -0.0651 -0.0850 236 PRO A C   
1504 O O   . PRO A 201 ? 0.2419 0.3125 0.3378 -0.0085 -0.0750 -0.0822 236 PRO A O   
1505 C CB  . PRO A 201 ? 0.3056 0.3882 0.3521 0.0117  -0.0662 -0.1135 236 PRO A CB  
1506 C CG  . PRO A 201 ? 0.2504 0.3374 0.2809 0.0244  -0.0561 -0.1274 236 PRO A CG  
1507 C CD  . PRO A 201 ? 0.2453 0.3439 0.2887 0.0273  -0.0433 -0.1147 236 PRO A CD  
1508 N N   . GLY A 202 ? 0.2390 0.3320 0.3207 0.0016  -0.0555 -0.0721 237 GLY A N   
1509 C CA  . GLY A 202 ? 0.2257 0.3242 0.3175 -0.0051 -0.0551 -0.0565 237 GLY A CA  
1510 C C   . GLY A 202 ? 0.2231 0.3210 0.3202 -0.0036 -0.0480 -0.0458 237 GLY A C   
1511 O O   . GLY A 202 ? 0.1670 0.2721 0.2641 -0.0058 -0.0445 -0.0345 237 GLY A O   
1512 N N   . HIS A 203 ? 0.1973 0.2873 0.2987 0.0015  -0.0468 -0.0502 238 HIS A N   
1513 C CA  . HIS A 203 ? 0.1929 0.2834 0.2990 0.0028  -0.0428 -0.0407 238 HIS A CA  
1514 C C   . HIS A 203 ? 0.1967 0.2821 0.3089 -0.0040 -0.0456 -0.0279 238 HIS A C   
1515 O O   . HIS A 203 ? 0.2059 0.2807 0.3272 -0.0091 -0.0521 -0.0266 238 HIS A O   
1516 C CB  . HIS A 203 ? 0.1503 0.2340 0.2658 0.0103  -0.0444 -0.0471 238 HIS A CB  
1517 C CG  . HIS A 203 ? 0.2039 0.2909 0.3247 0.0116  -0.0429 -0.0377 238 HIS A CG  
1518 N ND1 . HIS A 203 ? 0.2281 0.3045 0.3533 0.0080  -0.0482 -0.0264 238 HIS A ND1 
1519 C CD2 . HIS A 203 ? 0.1563 0.2567 0.2794 0.0156  -0.0382 -0.0381 238 HIS A CD2 
1520 C CE1 . HIS A 203 ? 0.1787 0.2609 0.3055 0.0104  -0.0478 -0.0209 238 HIS A CE1 
1521 N NE2 . HIS A 203 ? 0.1393 0.2365 0.2673 0.0144  -0.0424 -0.0281 238 HIS A NE2 
1522 N N   . THR A 204 ? 0.2120 0.3320 0.2526 0.0240  -0.0575 -0.0104 239 THR A N   
1523 C CA  . THR A 204 ? 0.1657 0.3008 0.2277 0.0151  -0.0550 -0.0052 239 THR A CA  
1524 C C   . THR A 204 ? 0.1584 0.2802 0.2194 0.0125  -0.0434 0.0053  239 THR A C   
1525 O O   . THR A 204 ? 0.1721 0.2810 0.2173 0.0211  -0.0371 0.0098  239 THR A O   
1526 C CB  . THR A 204 ? 0.2293 0.3895 0.2944 0.0245  -0.0582 -0.0048 239 THR A CB  
1527 O OG1 . THR A 204 ? 0.1793 0.3535 0.2456 0.0278  -0.0713 -0.0160 239 THR A OG1 
1528 C CG2 . THR A 204 ? 0.1527 0.3354 0.2417 0.0163  -0.0545 -0.0006 239 THR A CG2 
1529 N N   . THR A 205 ? 0.1629 0.2879 0.2405 0.0000  -0.0409 0.0090  240 THR A N   
1530 C CA  . THR A 205 ? 0.1405 0.2571 0.2181 -0.0025 -0.0313 0.0185  240 THR A CA  
1531 C C   . THR A 205 ? 0.1858 0.3260 0.2714 0.0007  -0.0270 0.0233  240 THR A C   
1532 O O   . THR A 205 ? 0.1735 0.3382 0.2743 -0.0031 -0.0307 0.0203  240 THR A O   
1533 C CB  . THR A 205 ? 0.1729 0.2779 0.2603 -0.0172 -0.0315 0.0207  240 THR A CB  
1534 O OG1 . THR A 205 ? 0.2113 0.2927 0.2904 -0.0173 -0.0366 0.0144  240 THR A OG1 
1535 C CG2 . THR A 205 ? 0.1904 0.2895 0.2762 -0.0192 -0.0225 0.0312  240 THR A CG2 
1536 N N   . TYR A 206 ? 0.1433 0.2780 0.2201 0.0082  -0.0198 0.0293  241 TYR A N   
1537 C CA  . TYR A 206 ? 0.1203 0.2763 0.2030 0.0136  -0.0156 0.0324  241 TYR A CA  
1538 C C   . TYR A 206 ? 0.1181 0.2730 0.2039 0.0069  -0.0078 0.0395  241 TYR A C   
1539 O O   . TYR A 206 ? 0.1545 0.2877 0.2294 0.0079  -0.0048 0.0426  241 TYR A O   
1540 C CB  . TYR A 206 ? 0.1391 0.2892 0.2072 0.0299  -0.0154 0.0321  241 TYR A CB  
1541 C CG  . TYR A 206 ? 0.1278 0.2809 0.1901 0.0374  -0.0232 0.0270  241 TYR A CG  
1542 C CD1 . TYR A 206 ? 0.1304 0.3112 0.2036 0.0419  -0.0292 0.0224  241 TYR A CD1 
1543 C CD2 . TYR A 206 ? 0.1593 0.2907 0.2056 0.0401  -0.0248 0.0262  241 TYR A CD2 
1544 C CE1 . TYR A 206 ? 0.1745 0.3575 0.2395 0.0505  -0.0380 0.0174  241 TYR A CE1 
1545 C CE2 . TYR A 206 ? 0.1520 0.2858 0.1884 0.0481  -0.0319 0.0221  241 TYR A CE2 
1546 C CZ  . TYR A 206 ? 0.1496 0.3079 0.1944 0.0538  -0.0393 0.0178  241 TYR A CZ  
1547 O OH  . TYR A 206 ? 0.1702 0.3306 0.2027 0.0635  -0.0479 0.0135  241 TYR A OH  
1548 N N   . VAL A 207 ? 0.1373 0.3172 0.2384 -0.0004 -0.0045 0.0420  242 VAL A N   
1549 C CA  . VAL A 207 ? 0.1550 0.3357 0.2569 -0.0079 0.0037  0.0504  242 VAL A CA  
1550 C C   . VAL A 207 ? 0.1474 0.3492 0.2476 0.0037  0.0099  0.0514  242 VAL A C   
1551 O O   . VAL A 207 ? 0.1834 0.4168 0.2967 0.0070  0.0104  0.0481  242 VAL A O   
1552 C CB  . VAL A 207 ? 0.2233 0.4163 0.3427 -0.0267 0.0051  0.0543  242 VAL A CB  
1553 C CG1 . VAL A 207 ? 0.2145 0.4091 0.3308 -0.0336 0.0154  0.0658  242 VAL A CG1 
1554 C CG2 . VAL A 207 ? 0.2713 0.4393 0.3911 -0.0365 -0.0031 0.0511  242 VAL A CG2 
1555 N N   . VAL A 208 ? 0.1646 0.3501 0.2492 0.0111  0.0136  0.0542  243 VAL A N   
1556 C CA  . VAL A 208 ? 0.1810 0.3797 0.2594 0.0250  0.0179  0.0529  243 VAL A CA  
1557 C C   . VAL A 208 ? 0.1600 0.3701 0.2369 0.0191  0.0271  0.0606  243 VAL A C   
1558 O O   . VAL A 208 ? 0.1354 0.3250 0.2043 0.0107  0.0283  0.0672  243 VAL A O   
1559 C CB  . VAL A 208 ? 0.1189 0.2901 0.1804 0.0370  0.0145  0.0493  243 VAL A CB  
1560 C CG1 . VAL A 208 ? 0.1265 0.3084 0.1814 0.0522  0.0168  0.0456  243 VAL A CG1 
1561 C CG2 . VAL A 208 ? 0.1197 0.2771 0.1798 0.0405  0.0074  0.0446  243 VAL A CG2 
1562 N N   . GLU A 209 ? 0.1307 0.3731 0.2132 0.0251  0.0335  0.0601  244 GLU A N   
1563 C CA  . GLU A 209 ? 0.1425 0.3972 0.2211 0.0188  0.0440  0.0692  244 GLU A CA  
1564 C C   . GLU A 209 ? 0.1467 0.4283 0.2205 0.0351  0.0500  0.0648  244 GLU A C   
1565 O O   . GLU A 209 ? 0.1427 0.4546 0.2307 0.0421  0.0501  0.0581  244 GLU A O   
1566 C CB  . GLU A 209 ? 0.1692 0.4448 0.2672 -0.0018 0.0498  0.0772  244 GLU A CB  
1567 C CG  . GLU A 209 ? 0.2584 0.5461 0.3502 -0.0104 0.0629  0.0899  244 GLU A CG  
1568 C CD  . GLU A 209 ? 0.4667 0.7580 0.5738 -0.0353 0.0673  0.1001  244 GLU A CD  
1569 O OE1 . GLU A 209 ? 0.4153 0.7109 0.5435 -0.0457 0.0608  0.0956  244 GLU A OE1 
1570 O OE2 . GLU A 209 ? 0.5717 0.8563 0.6675 -0.0436 0.0756  0.1111  244 GLU A OE2 
1571 N N   . SER A 210 ? 0.1578 0.4303 0.2117 0.0418  0.0543  0.0678  245 SER A N   
1572 C CA  . SER A 210 ? 0.1666 0.4644 0.2126 0.0586  0.0603  0.0627  245 SER A CA  
1573 C C   . SER A 210 ? 0.1864 0.4860 0.2152 0.0550  0.0695  0.0722  245 SER A C   
1574 O O   . SER A 210 ? 0.1923 0.4634 0.2041 0.0526  0.0674  0.0779  245 SER A O   
1575 C CB  . SER A 210 ? 0.1844 0.4612 0.2166 0.0791  0.0507  0.0500  245 SER A CB  
1576 O OG  . SER A 210 ? 0.1890 0.4826 0.2093 0.0951  0.0541  0.0436  245 SER A OG  
1577 N N   . GLN A 211 ? 0.2022 0.5283 0.2336 0.0550  0.0764  0.0723  246 GLN A N   
1578 C CA  . GLN A 211 ? 0.2270 0.5571 0.2419 0.0521  0.0856  0.0813  246 GLN A CA  
1579 C C   . GLN A 211 ? 0.2629 0.5701 0.2724 0.0326  0.0889  0.0975  246 GLN A C   
1580 O O   . GLN A 211 ? 0.3142 0.6049 0.3003 0.0345  0.0912  0.1048  246 GLN A O   
1581 C CB  . GLN A 211 ? 0.2373 0.5586 0.2264 0.0739  0.0824  0.0736  246 GLN A CB  
1582 C CG  . GLN A 211 ? 0.2363 0.5716 0.2262 0.0951  0.0766  0.0566  246 GLN A CG  
1583 C CD  . GLN A 211 ? 0.2502 0.6214 0.2504 0.0960  0.0836  0.0544  246 GLN A CD  
1584 O OE1 . GLN A 211 ? 0.2621 0.6503 0.2693 0.0804  0.0944  0.0655  246 GLN A OE1 
1585 N NE2 . GLN A 211 ? 0.2533 0.6344 0.2530 0.1147  0.0774  0.0399  246 GLN A NE2 
1586 N N   . GLY A 212 ? 0.2718 0.5748 0.3018 0.0147  0.0873  0.1022  247 GLY A N   
1587 C CA  . GLY A 212 ? 0.2536 0.5314 0.2800 -0.0046 0.0889  0.1168  247 GLY A CA  
1588 C C   . GLY A 212 ? 0.3563 0.5978 0.3704 -0.0027 0.0799  0.1194  247 GLY A C   
1589 O O   . GLY A 212 ? 0.3134 0.5288 0.3238 -0.0173 0.0786  0.1306  247 GLY A O   
1590 N N   . GLN A 213 ? 0.2271 0.4573 0.2351 0.0148  0.0703  0.1058  248 GLN A N   
1591 C CA  . GLN A 213 ? 0.2374 0.4276 0.2380 0.0170  0.0575  0.1016  248 GLN A CA  
1592 C C   . GLN A 213 ? 0.2230 0.4083 0.2448 0.0116  0.0498  0.0936  248 GLN A C   
1593 O O   . GLN A 213 ? 0.2188 0.4223 0.2513 0.0199  0.0484  0.0838  248 GLN A O   
1594 C CB  . GLN A 213 ? 0.2319 0.4115 0.2150 0.0370  0.0512  0.0909  248 GLN A CB  
1595 C CG  . GLN A 213 ? 0.3540 0.5507 0.3168 0.0482  0.0590  0.0935  248 GLN A CG  
1596 C CD  . GLN A 213 ? 0.4044 0.5881 0.3476 0.0410  0.0635  0.1090  248 GLN A CD  
1597 O OE1 . GLN A 213 ? 0.4856 0.6395 0.4269 0.0325  0.0570  0.1146  248 GLN A OE1 
1598 N NE2 . GLN A 213 ? 0.5189 0.7236 0.4476 0.0445  0.0744  0.1157  248 GLN A NE2 
1599 N N   . LYS A 214 ? 0.2109 0.3707 0.2364 -0.0004 0.0442  0.0973  249 LYS A N   
1600 C CA  . LYS A 214 ? 0.1954 0.3510 0.2385 -0.0066 0.0373  0.0906  249 LYS A CA  
1601 C C   . LYS A 214 ? 0.2814 0.4062 0.3174 0.0002  0.0271  0.0832  249 LYS A C   
1602 O O   . LYS A 214 ? 0.2617 0.3640 0.2836 0.0033  0.0243  0.0856  249 LYS A O   
1603 C CB  . LYS A 214 ? 0.2645 0.4187 0.3203 -0.0269 0.0389  0.0991  249 LYS A CB  
1604 C CG  . LYS A 214 ? 0.3039 0.4592 0.3786 -0.0335 0.0314  0.0908  249 LYS A CG  
1605 C CD  . LYS A 214 ? 0.3691 0.5177 0.4559 -0.0545 0.0310  0.0978  249 LYS A CD  
1606 C CE  . LYS A 214 ? 0.4526 0.6360 0.5555 -0.0673 0.0414  0.1053  249 LYS A CE  
1607 N NZ  . LYS A 214 ? 0.4513 0.6258 0.5697 -0.0903 0.0395  0.1107  249 LYS A NZ  
1608 N N   . LEU A 215 ? 0.1872 0.3135 0.2330 0.0032  0.0219  0.0740  250 LEU A N   
1609 C CA  . LEU A 215 ? 0.1697 0.2726 0.2122 0.0076  0.0143  0.0672  250 LEU A CA  
1610 C C   . LEU A 215 ? 0.1492 0.2545 0.2039 0.0016  0.0102  0.0627  250 LEU A C   
1611 O O   . LEU A 215 ? 0.1647 0.2901 0.2273 0.0046  0.0106  0.0592  250 LEU A O   
1612 C CB  . LEU A 215 ? 0.1343 0.2362 0.1703 0.0219  0.0129  0.0599  250 LEU A CB  
1613 C CG  . LEU A 215 ? 0.1343 0.2193 0.1703 0.0252  0.0075  0.0532  250 LEU A CG  
1614 C CD1 . LEU A 215 ? 0.1982 0.2617 0.2300 0.0224  0.0041  0.0532  250 LEU A CD1 
1615 C CD2 . LEU A 215 ? 0.1696 0.2541 0.2011 0.0367  0.0069  0.0475  250 LEU A CD2 
1616 N N   . ALA A 216 ? 0.1477 0.2333 0.2030 -0.0050 0.0052  0.0618  251 ALA A N   
1617 C CA  . ALA A 216 ? 0.1759 0.2625 0.2400 -0.0094 -0.0001 0.0557  251 ALA A CA  
1618 C C   . ALA A 216 ? 0.1579 0.2310 0.2149 -0.0004 -0.0038 0.0484  251 ALA A C   
1619 O O   . ALA A 216 ? 0.2301 0.2842 0.2814 0.0008  -0.0057 0.0471  251 ALA A O   
1620 C CB  . ALA A 216 ? 0.1935 0.2677 0.2632 -0.0228 -0.0037 0.0581  251 ALA A CB  
1621 N N   . LEU A 217 ? 0.1578 0.2418 0.2151 0.0061  -0.0045 0.0441  252 LEU A N   
1622 C CA  . LEU A 217 ? 0.1502 0.2243 0.1999 0.0134  -0.0060 0.0392  252 LEU A CA  
1623 C C   . LEU A 217 ? 0.2105 0.2811 0.2617 0.0093  -0.0114 0.0338  252 LEU A C   
1624 O O   . LEU A 217 ? 0.1987 0.2823 0.2534 0.0094  -0.0151 0.0309  252 LEU A O   
1625 C CB  . LEU A 217 ? 0.1402 0.2239 0.1861 0.0227  -0.0049 0.0389  252 LEU A CB  
1626 C CG  . LEU A 217 ? 0.1747 0.2626 0.2187 0.0287  -0.0011 0.0417  252 LEU A CG  
1627 C CD1 . LEU A 217 ? 0.1593 0.2536 0.1991 0.0393  -0.0022 0.0404  252 LEU A CD1 
1628 C CD2 . LEU A 217 ? 0.2434 0.3138 0.2815 0.0303  0.0007  0.0417  252 LEU A CD2 
1629 N N   . LEU A 218 ? 0.2079 0.2619 0.2566 0.0072  -0.0130 0.0312  253 LEU A N   
1630 C CA  . LEU A 218 ? 0.1394 0.1859 0.1881 0.0045  -0.0190 0.0242  253 LEU A CA  
1631 C C   . LEU A 218 ? 0.2217 0.2692 0.2610 0.0122  -0.0196 0.0180  253 LEU A C   
1632 O O   . LEU A 218 ? 0.1839 0.2276 0.2213 0.0119  -0.0253 0.0103  253 LEU A O   
1633 C CB  . LEU A 218 ? 0.2423 0.2696 0.2903 0.0025  -0.0207 0.0234  253 LEU A CB  
1634 C CG  . LEU A 218 ? 0.3184 0.3379 0.3730 -0.0081 -0.0241 0.0279  253 LEU A CG  
1635 C CD1 . LEU A 218 ? 0.3385 0.3683 0.3970 -0.0131 -0.0188 0.0381  253 LEU A CD1 
1636 C CD2 . LEU A 218 ? 0.2161 0.2130 0.2658 -0.0057 -0.0268 0.0270  253 LEU A CD2 
1637 N N   . GLY A 219 ? 0.1985 0.2496 0.2305 0.0192  -0.0141 0.0211  254 GLY A N   
1638 C CA  . GLY A 219 ? 0.1803 0.2311 0.2004 0.0257  -0.0132 0.0175  254 GLY A CA  
1639 C C   . GLY A 219 ? 0.2245 0.2663 0.2418 0.0268  -0.0124 0.0113  254 GLY A C   
1640 O O   . GLY A 219 ? 0.2212 0.2570 0.2426 0.0264  -0.0083 0.0123  254 GLY A O   
1641 N N   . ASP A 220 ? 0.2180 0.2604 0.2283 0.0295  -0.0171 0.0032  255 ASP A N   
1642 C CA  . ASP A 220 ? 0.2648 0.3014 0.2708 0.0334  -0.0168 -0.0052 255 ASP A CA  
1643 C C   . ASP A 220 ? 0.3400 0.3669 0.3524 0.0301  -0.0269 -0.0141 255 ASP A C   
1644 O O   . ASP A 220 ? 0.2543 0.2778 0.2598 0.0354  -0.0312 -0.0251 255 ASP A O   
1645 C CB  . ASP A 220 ? 0.2169 0.2601 0.2058 0.0414  -0.0138 -0.0086 255 ASP A CB  
1646 C CG  . ASP A 220 ? 0.1822 0.2288 0.1646 0.0436  -0.0017 0.0000  255 ASP A CG  
1647 O OD1 . ASP A 220 ? 0.2197 0.2637 0.2120 0.0391  0.0023  0.0073  255 ASP A OD1 
1648 O OD2 . ASP A 220 ? 0.2243 0.2753 0.1910 0.0493  0.0038  -0.0001 255 ASP A OD2 
1649 N N   . LEU A 221 ? 0.3172 0.3384 0.3414 0.0214  -0.0309 -0.0095 256 LEU A N   
1650 C CA  . LEU A 221 ? 0.3242 0.3300 0.3539 0.0167  -0.0401 -0.0160 256 LEU A CA  
1651 C C   . LEU A 221 ? 0.3627 0.3541 0.3910 0.0226  -0.0399 -0.0203 256 LEU A C   
1652 O O   . LEU A 221 ? 0.4798 0.4543 0.5088 0.0224  -0.0486 -0.0281 256 LEU A O   
1653 C CB  . LEU A 221 ? 0.2967 0.2990 0.3384 0.0044  -0.0428 -0.0079 256 LEU A CB  
1654 C CG  . LEU A 221 ? 0.3533 0.3695 0.4025 -0.0034 -0.0473 -0.0080 256 LEU A CG  
1655 C CD1 . LEU A 221 ? 0.2179 0.2330 0.2804 -0.0168 -0.0467 0.0016  256 LEU A CD1 
1656 C CD2 . LEU A 221 ? 0.3393 0.3483 0.3868 -0.0033 -0.0584 -0.0219 256 LEU A CD2 
1657 N N   . ILE A 222 ? 0.3723 0.3697 0.4001 0.0278  -0.0313 -0.0159 257 ILE A N   
1658 C CA  . ILE A 222 ? 0.3328 0.3244 0.3610 0.0359  -0.0306 -0.0221 257 ILE A CA  
1659 C C   . ILE A 222 ? 0.2960 0.3055 0.3215 0.0421  -0.0198 -0.0226 257 ILE A C   
1660 O O   . ILE A 222 ? 0.3954 0.4146 0.4212 0.0386  -0.0126 -0.0137 257 ILE A O   
1661 C CB  . ILE A 222 ? 0.4006 0.3803 0.4353 0.0341  -0.0325 -0.0157 257 ILE A CB  
1662 C CG1 . ILE A 222 ? 0.2890 0.2637 0.3251 0.0450  -0.0346 -0.0248 257 ILE A CG1 
1663 C CG2 . ILE A 222 ? 0.2995 0.2906 0.3375 0.0306  -0.0247 -0.0049 257 ILE A CG2 
1664 C CD1 . ILE A 222 ? 0.4087 0.3664 0.4473 0.0460  -0.0405 -0.0204 257 ILE A CD1 
1665 N N   . LEU A 223 ? 0.3339 0.3474 0.3565 0.0512  -0.0186 -0.0334 258 LEU A N   
1666 C CA  . LEU A 223 ? 0.3244 0.3570 0.3450 0.0556  -0.0067 -0.0339 258 LEU A CA  
1667 C C   . LEU A 223 ? 0.3820 0.4222 0.4142 0.0613  -0.0030 -0.0388 258 LEU A C   
1668 O O   . LEU A 223 ? 0.2873 0.3432 0.3257 0.0593  0.0076  -0.0345 258 LEU A O   
1669 C CB  . LEU A 223 ? 0.3377 0.3773 0.3438 0.0625  -0.0056 -0.0428 258 LEU A CB  
1670 C CG  . LEU A 223 ? 0.4154 0.4522 0.4098 0.0584  -0.0100 -0.0391 258 LEU A CG  
1671 C CD1 . LEU A 223 ? 0.4204 0.4608 0.3985 0.0672  -0.0136 -0.0513 258 LEU A CD1 
1672 C CD2 . LEU A 223 ? 0.2715 0.3166 0.2623 0.0531  -0.0008 -0.0248 258 LEU A CD2 
1673 N N   . VAL A 224 ? 0.3035 0.3327 0.3399 0.0684  -0.0123 -0.0481 259 VAL A N   
1674 C CA  . VAL A 224 ? 0.2509 0.2892 0.2993 0.0769  -0.0112 -0.0552 259 VAL A CA  
1675 C C   . VAL A 224 ? 0.3178 0.3348 0.3708 0.0778  -0.0230 -0.0532 259 VAL A C   
1676 O O   . VAL A 224 ? 0.3103 0.3071 0.3583 0.0840  -0.0341 -0.0602 259 VAL A O   
1677 C CB  . VAL A 224 ? 0.2669 0.3144 0.3125 0.0903  -0.0112 -0.0713 259 VAL A CB  
1678 C CG1 . VAL A 224 ? 0.3092 0.3752 0.3712 0.0995  -0.0082 -0.0791 259 VAL A CG1 
1679 C CG2 . VAL A 224 ? 0.3081 0.3727 0.3419 0.0897  -0.0003 -0.0718 259 VAL A CG2 
1680 N N   . ALA A 225 ? 0.2800 0.2994 0.3407 0.0723  -0.0212 -0.0439 260 ALA A N   
1681 C CA  . ALA A 225 ? 0.3151 0.3143 0.3758 0.0736  -0.0316 -0.0397 260 ALA A CA  
1682 C C   . ALA A 225 ? 0.3564 0.3480 0.4202 0.0884  -0.0411 -0.0513 260 ALA A C   
1683 O O   . ALA A 225 ? 0.3352 0.2989 0.3911 0.0913  -0.0525 -0.0496 260 ALA A O   
1684 C CB  . ALA A 225 ? 0.2741 0.2823 0.3418 0.0685  -0.0280 -0.0310 260 ALA A CB  
1685 N N   . ALA A 226 ? 0.3068 0.3225 0.3820 0.0981  -0.0366 -0.0628 261 ALA A N   
1686 C CA  . ALA A 226 ? 0.3247 0.3369 0.4048 0.1150  -0.0463 -0.0754 261 ALA A CA  
1687 C C   . ALA A 226 ? 0.3619 0.3490 0.4295 0.1236  -0.0562 -0.0842 261 ALA A C   
1688 O O   . ALA A 226 ? 0.4207 0.3940 0.4860 0.1351  -0.0668 -0.0911 261 ALA A O   
1689 C CB  . ALA A 226 ? 0.2527 0.3032 0.3510 0.1232  -0.0377 -0.0873 261 ALA A CB  
1690 N N   . VAL A 227 ? 0.3122 0.2932 0.3695 0.1156  -0.0530 -0.0831 262 VAL A N   
1691 C CA  . VAL A 227 ? 0.3339 0.2910 0.3797 0.1220  -0.0631 -0.0933 262 VAL A CA  
1692 C C   . VAL A 227 ? 0.3429 0.2659 0.3786 0.1085  -0.0713 -0.0822 262 VAL A C   
1693 O O   . VAL A 227 ? 0.3634 0.2524 0.3925 0.1122  -0.0848 -0.0844 262 VAL A O   
1694 C CB  . VAL A 227 ? 0.3844 0.3634 0.4260 0.1251  -0.0546 -0.1041 262 VAL A CB  
1695 C CG1 . VAL A 227 ? 0.4428 0.3964 0.4721 0.1329  -0.0671 -0.1175 262 VAL A CG1 
1696 C CG2 . VAL A 227 ? 0.4049 0.4211 0.4580 0.1372  -0.0442 -0.1145 262 VAL A CG2 
1697 N N   . GLN A 228 ? 0.3224 0.2543 0.3573 0.0925  -0.0633 -0.0700 263 GLN A N   
1698 C CA  . GLN A 228 ? 0.4125 0.3241 0.4410 0.0787  -0.0683 -0.0628 263 GLN A CA  
1699 C C   . GLN A 228 ? 0.4050 0.2972 0.4333 0.0679  -0.0715 -0.0464 263 GLN A C   
1700 O O   . GLN A 228 ? 0.4112 0.2880 0.4371 0.0547  -0.0750 -0.0395 263 GLN A O   
1701 C CB  . GLN A 228 ? 0.3160 0.2515 0.3438 0.0698  -0.0583 -0.0595 263 GLN A CB  
1702 C CG  . GLN A 228 ? 0.3685 0.3090 0.3886 0.0759  -0.0603 -0.0740 263 GLN A CG  
1703 C CD  . GLN A 228 ? 0.3889 0.3592 0.4057 0.0740  -0.0476 -0.0714 263 GLN A CD  
1704 O OE1 . GLN A 228 ? 0.3666 0.3526 0.3885 0.0691  -0.0373 -0.0602 263 GLN A OE1 
1705 N NE2 . GLN A 228 ? 0.3511 0.3264 0.3575 0.0780  -0.0494 -0.0815 263 GLN A NE2 
1706 N N   . PHE A 229 ? 0.3100 0.2053 0.3412 0.0726  -0.0699 -0.0402 264 PHE A N   
1707 C CA  . PHE A 229 ? 0.3576 0.2297 0.3834 0.0658  -0.0747 -0.0259 264 PHE A CA  
1708 C C   . PHE A 229 ? 0.4302 0.2648 0.4479 0.0741  -0.0889 -0.0298 264 PHE A C   
1709 O O   . PHE A 229 ? 0.4589 0.2639 0.4694 0.0635  -0.0945 -0.0198 264 PHE A O   
1710 C CB  . PHE A 229 ? 0.3882 0.2762 0.4170 0.0689  -0.0694 -0.0182 264 PHE A CB  
1711 C CG  . PHE A 229 ? 0.3399 0.2527 0.3731 0.0575  -0.0575 -0.0094 264 PHE A CG  
1712 C CD1 . PHE A 229 ? 0.3794 0.2878 0.4093 0.0429  -0.0546 0.0020  264 PHE A CD1 
1713 C CD2 . PHE A 229 ? 0.3262 0.2666 0.3681 0.0616  -0.0498 -0.0130 264 PHE A CD2 
1714 C CE1 . PHE A 229 ? 0.3528 0.2835 0.3862 0.0356  -0.0450 0.0087  264 PHE A CE1 
1715 C CE2 . PHE A 229 ? 0.3611 0.3190 0.4056 0.0526  -0.0406 -0.0054 264 PHE A CE2 
1716 C CZ  . PHE A 229 ? 0.3062 0.2589 0.3454 0.0411  -0.0386 0.0050  264 PHE A CZ  
1717 N N   . ASP A 230 ? 0.4174 0.2526 0.4366 0.0930  -0.0947 -0.0443 265 ASP A N   
1718 C CA  . ASP A 230 ? 0.5300 0.3306 0.5397 0.1020  -0.1083 -0.0493 265 ASP A CA  
1719 C C   . ASP A 230 ? 0.5099 0.2891 0.5157 0.0975  -0.1153 -0.0582 265 ASP A C   
1720 O O   . ASP A 230 ? 0.4960 0.2429 0.4925 0.0947  -0.1247 -0.0557 265 ASP A O   
1721 C CB  . ASP A 230 ? 0.5110 0.3307 0.5239 0.1199  -0.1096 -0.0623 265 ASP A CB  
1722 C CG  . ASP A 230 ? 0.6526 0.4879 0.6682 0.1241  -0.1067 -0.0550 265 ASP A CG  
1723 O OD1 . ASP A 230 ? 0.6740 0.4876 0.6790 0.1189  -0.1103 -0.0404 265 ASP A OD1 
1724 O OD2 . ASP A 230 ? 0.7353 0.6051 0.7633 0.1327  -0.1012 -0.0646 265 ASP A OD2 
1725 N N   . ASP A 231 ? 0.4287 0.2286 0.4404 0.0966  -0.1102 -0.0691 266 ASP A N   
1726 C CA  . ASP A 231 ? 0.5008 0.2832 0.5086 0.0935  -0.1182 -0.0807 266 ASP A CA  
1727 C C   . ASP A 231 ? 0.4222 0.2294 0.4342 0.0776  -0.1089 -0.0771 266 ASP A C   
1728 O O   . ASP A 231 ? 0.5116 0.3465 0.5241 0.0839  -0.1029 -0.0885 266 ASP A O   
1729 C CB  . ASP A 231 ? 0.5025 0.2959 0.5076 0.1120  -0.1215 -0.1010 266 ASP A CB  
1730 C CG  . ASP A 231 ? 0.5709 0.3406 0.5691 0.1096  -0.1330 -0.1121 266 ASP A CG  
1731 O OD1 . ASP A 231 ? 0.5496 0.2995 0.5481 0.0923  -0.1373 -0.1063 266 ASP A OD1 
1732 O OD2 . ASP A 231 ? 0.5432 0.3151 0.5370 0.1242  -0.1383 -0.1267 266 ASP A OD2 
1733 N N   . PRO A 232 ? 0.4463 0.2453 0.4607 0.0576  -0.1074 -0.0611 267 PRO A N   
1734 C CA  . PRO A 232 ? 0.4291 0.2529 0.4488 0.0438  -0.1001 -0.0582 267 PRO A CA  
1735 C C   . PRO A 232 ? 0.4736 0.2964 0.4910 0.0454  -0.1077 -0.0755 267 PRO A C   
1736 O O   . PRO A 232 ? 0.4242 0.2717 0.4440 0.0389  -0.1024 -0.0758 267 PRO A O   
1737 C CB  . PRO A 232 ? 0.4904 0.3001 0.5144 0.0234  -0.1002 -0.0402 267 PRO A CB  
1738 C CG  . PRO A 232 ? 0.4907 0.2807 0.5092 0.0279  -0.1008 -0.0288 267 PRO A CG  
1739 C CD  . PRO A 232 ? 0.4727 0.2428 0.4845 0.0476  -0.1110 -0.0440 267 PRO A CD  
1740 N N   . SER A 233 ? 0.5025 0.2967 0.5142 0.0551  -0.1210 -0.0906 268 SER A N   
1741 C CA  . SER A 233 ? 0.4795 0.2728 0.4878 0.0571  -0.1296 -0.1089 268 SER A CA  
1742 C C   . SER A 233 ? 0.4966 0.3216 0.4972 0.0756  -0.1228 -0.1237 268 SER A C   
1743 O O   . SER A 233 ? 0.5194 0.3508 0.5139 0.0784  -0.1279 -0.1380 268 SER A O   
1744 C CB  . SER A 233 ? 0.5014 0.2487 0.5055 0.0604  -0.1483 -0.1217 268 SER A CB  
1745 O OG  . SER A 233 ? 0.6644 0.4104 0.6616 0.0803  -0.1482 -0.1272 268 SER A OG  
1746 N N   . VAL A 234 ? 0.4978 0.3441 0.4983 0.0878  -0.1113 -0.1208 269 VAL A N   
1747 C CA  . VAL A 234 ? 0.4713 0.3496 0.4651 0.1036  -0.1025 -0.1334 269 VAL A CA  
1748 C C   . VAL A 234 ? 0.4587 0.3680 0.4508 0.0942  -0.0905 -0.1244 269 VAL A C   
1749 O O   . VAL A 234 ? 0.3838 0.3032 0.3833 0.0819  -0.0818 -0.1064 269 VAL A O   
1750 C CB  . VAL A 234 ? 0.5477 0.4419 0.5462 0.1176  -0.0938 -0.1334 269 VAL A CB  
1751 C CG1 . VAL A 234 ? 0.4540 0.3856 0.4471 0.1309  -0.0816 -0.1442 269 VAL A CG1 
1752 C CG2 . VAL A 234 ? 0.4469 0.3098 0.4454 0.1303  -0.1076 -0.1430 269 VAL A CG2 
1753 N N   . THR A 235 ? 0.4246 0.3482 0.4047 0.1016  -0.0907 -0.1373 270 THR A N   
1754 C CA  . THR A 235 ? 0.4109 0.3614 0.3855 0.0952  -0.0806 -0.1287 270 THR A CA  
1755 C C   . THR A 235 ? 0.3913 0.3720 0.3542 0.1091  -0.0664 -0.1331 270 THR A C   
1756 O O   . THR A 235 ? 0.4972 0.4832 0.4597 0.1230  -0.0631 -0.1431 270 THR A O   
1757 C CB  . THR A 235 ? 0.4144 0.3576 0.3831 0.0891  -0.0931 -0.1364 270 THR A CB  
1758 O OG1 . THR A 235 ? 0.4388 0.3798 0.3925 0.1048  -0.1013 -0.1588 270 THR A OG1 
1759 C CG2 . THR A 235 ? 0.4724 0.3866 0.4554 0.0730  -0.1061 -0.1322 270 THR A CG2 
1760 N N   . THR A 236 ? 0.4386 0.4400 0.3921 0.1055  -0.0573 -0.1248 271 THR A N   
1761 C CA  . THR A 236 ? 0.3934 0.4225 0.3335 0.1158  -0.0418 -0.1251 271 THR A CA  
1762 C C   . THR A 236 ? 0.4404 0.4778 0.3574 0.1221  -0.0451 -0.1330 271 THR A C   
1763 O O   . THR A 236 ? 0.4416 0.4674 0.3567 0.1160  -0.0584 -0.1353 271 THR A O   
1764 C CB  . THR A 236 ? 0.4158 0.4611 0.3631 0.1063  -0.0253 -0.1043 271 THR A CB  
1765 O OG1 . THR A 236 ? 0.4893 0.5355 0.4294 0.0974  -0.0258 -0.0929 271 THR A OG1 
1766 C CG2 . THR A 236 ? 0.4091 0.4431 0.3784 0.0979  -0.0263 -0.0959 271 THR A CG2 
1767 N N   . ASP A 237 ? 0.4497 0.5092 0.3491 0.1349  -0.0330 -0.1376 272 ASP A N   
1768 C CA  . ASP A 237 ? 0.4286 0.4991 0.3005 0.1429  -0.0335 -0.1425 272 ASP A CA  
1769 C C   . ASP A 237 ? 0.4900 0.5649 0.3563 0.1322  -0.0292 -0.1232 272 ASP A C   
1770 O O   . ASP A 237 ? 0.5533 0.6330 0.3974 0.1379  -0.0342 -0.1261 272 ASP A O   
1771 C CB  . ASP A 237 ? 0.5329 0.6287 0.3867 0.1578  -0.0171 -0.1476 272 ASP A CB  
1772 C CG  . ASP A 237 ? 0.6149 0.7296 0.4699 0.1499  0.0051  -0.1254 272 ASP A CG  
1773 O OD1 . ASP A 237 ? 0.7773 0.8986 0.6121 0.1480  0.0116  -0.1130 272 ASP A OD1 
1774 O OD2 . ASP A 237 ? 0.6792 0.8006 0.5556 0.1456  0.0149  -0.1205 272 ASP A OD2 
1775 N N   . LEU A 238 ? 0.4290 0.5025 0.3133 0.1188  -0.0209 -0.1044 273 LEU A N   
1776 C CA  . LEU A 238 ? 0.4398 0.5147 0.3204 0.1099  -0.0184 -0.0870 273 LEU A CA  
1777 C C   . LEU A 238 ? 0.5085 0.5702 0.4004 0.1014  -0.0358 -0.0887 273 LEU A C   
1778 O O   . LEU A 238 ? 0.5080 0.5732 0.3957 0.0972  -0.0366 -0.0777 273 LEU A O   
1779 C CB  . LEU A 238 ? 0.4791 0.5564 0.3752 0.0995  -0.0043 -0.0684 273 LEU A CB  
1780 C CG  . LEU A 238 ? 0.5817 0.6741 0.4759 0.1012  0.0153  -0.0613 273 LEU A CG  
1781 C CD1 . LEU A 238 ? 0.3701 0.4580 0.2869 0.0880  0.0214  -0.0463 273 LEU A CD1 
1782 C CD2 . LEU A 238 ? 0.5885 0.6926 0.4531 0.1074  0.0261  -0.0539 273 LEU A CD2 
1783 N N   . ASP A 239 ? 0.3356 0.3823 0.2429 0.0983  -0.0493 -0.1013 274 ASP A N   
1784 C CA  . ASP A 239 ? 0.4542 0.4905 0.3759 0.0870  -0.0642 -0.1019 274 ASP A CA  
1785 C C   . ASP A 239 ? 0.4509 0.4903 0.3580 0.0935  -0.0789 -0.1169 274 ASP A C   
1786 O O   . ASP A 239 ? 0.4493 0.4847 0.3440 0.1044  -0.0859 -0.1351 274 ASP A O   
1787 C CB  . ASP A 239 ? 0.3702 0.3856 0.3136 0.0787  -0.0722 -0.1066 274 ASP A CB  
1788 C CG  . ASP A 239 ? 0.4723 0.4852 0.4294 0.0732  -0.0603 -0.0925 274 ASP A CG  
1789 O OD1 . ASP A 239 ? 0.4189 0.4382 0.3838 0.0642  -0.0539 -0.0765 274 ASP A OD1 
1790 O OD2 . ASP A 239 ? 0.4589 0.4637 0.4195 0.0790  -0.0588 -0.0986 274 ASP A OD2 
1791 N N   . SER A 240 ? 0.4183 0.4664 0.3269 0.0882  -0.0845 -0.1107 275 SER A N   
1792 C CA  . SER A 240 ? 0.3687 0.4231 0.2650 0.0945  -0.1004 -0.1254 275 SER A CA  
1793 C C   . SER A 240 ? 0.5482 0.5870 0.4594 0.0887  -0.1189 -0.1448 275 SER A C   
1794 O O   . SER A 240 ? 0.5282 0.5665 0.4244 0.0989  -0.1317 -0.1645 275 SER A O   
1795 C CB  . SER A 240 ? 0.3666 0.4351 0.2675 0.0896  -0.1041 -0.1152 275 SER A CB  
1796 O OG  . SER A 240 ? 0.5194 0.5970 0.4025 0.0965  -0.0888 -0.0980 275 SER A OG  
1797 N N   . ASP A 241 ? 0.4779 0.5024 0.4171 0.0723  -0.1211 -0.1396 276 ASP A N   
1798 C CA  . ASP A 241 ? 0.5338 0.5383 0.4899 0.0626  -0.1385 -0.1547 276 ASP A CA  
1799 C C   . ASP A 241 ? 0.4932 0.4739 0.4628 0.0557  -0.1329 -0.1484 276 ASP A C   
1800 O O   . ASP A 241 ? 0.4015 0.3801 0.3896 0.0416  -0.1262 -0.1316 276 ASP A O   
1801 C CB  . ASP A 241 ? 0.5034 0.5167 0.4818 0.0462  -0.1497 -0.1532 276 ASP A CB  
1802 C CG  . ASP A 241 ? 0.5495 0.5423 0.5460 0.0338  -0.1686 -0.1694 276 ASP A CG  
1803 O OD1 . ASP A 241 ? 0.5142 0.4796 0.5077 0.0364  -0.1724 -0.1785 276 ASP A OD1 
1804 O OD2 . ASP A 241 ? 0.5598 0.5635 0.5750 0.0212  -0.1804 -0.1736 276 ASP A OD2 
1805 N N   . SER A 242 ? 0.4327 0.3963 0.3915 0.0674  -0.1362 -0.1627 277 SER A N   
1806 C CA  . SER A 242 ? 0.5319 0.4734 0.4995 0.0659  -0.1315 -0.1579 277 SER A CA  
1807 C C   . SER A 242 ? 0.5602 0.4751 0.5505 0.0465  -0.1421 -0.1540 277 SER A C   
1808 O O   . SER A 242 ? 0.5652 0.4703 0.5667 0.0381  -0.1343 -0.1380 277 SER A O   
1809 C CB  . SER A 242 ? 0.5375 0.4677 0.4891 0.0851  -0.1354 -0.1772 277 SER A CB  
1810 O OG  . SER A 242 ? 0.6418 0.5959 0.5775 0.1002  -0.1186 -0.1736 277 SER A OG  
1811 N N   . LYS A 243 ? 0.5096 0.4120 0.5062 0.0389  -0.1600 -0.1685 278 LYS A N   
1812 C CA  . LYS A 243 ? 0.5717 0.4482 0.5907 0.0174  -0.1694 -0.1637 278 LYS A CA  
1813 C C   . LYS A 243 ? 0.5279 0.4235 0.5652 -0.0007 -0.1587 -0.1410 278 LYS A C   
1814 O O   . LYS A 243 ? 0.4845 0.3633 0.5345 -0.0143 -0.1544 -0.1259 278 LYS A O   
1815 C CB  . LYS A 243 ? 0.5113 0.3770 0.5362 0.0111  -0.1885 -0.1823 278 LYS A CB  
1816 C CG  . LYS A 243 ? 0.7066 0.5536 0.7155 0.0286  -0.1951 -0.1990 278 LYS A CG  
1817 C CD  . LYS A 243 ? 0.7380 0.6118 0.7239 0.0508  -0.1936 -0.2128 278 LYS A CD  
1818 C CE  . LYS A 243 ? 0.8291 0.6876 0.7998 0.0701  -0.1976 -0.2276 278 LYS A CE  
1819 N NZ  . LYS A 243 ? 0.7329 0.6196 0.6793 0.0925  -0.1923 -0.2378 278 LYS A NZ  
1820 N N   . ALA A 244 ? 0.4540 0.3845 0.4905 0.0007  -0.1547 -0.1385 279 ALA A N   
1821 C CA  . ALA A 244 ? 0.4500 0.4026 0.5029 -0.0130 -0.1448 -0.1193 279 ALA A CA  
1822 C C   . ALA A 244 ? 0.4221 0.3751 0.4708 -0.0096 -0.1268 -0.0999 279 ALA A C   
1823 O O   . ALA A 244 ? 0.3915 0.3433 0.4549 -0.0235 -0.1203 -0.0840 279 ALA A O   
1824 C CB  . ALA A 244 ? 0.4597 0.4478 0.5087 -0.0069 -0.1455 -0.1223 279 ALA A CB  
1825 N N   . VAL A 245 ? 0.3294 0.2861 0.3584 0.0086  -0.1184 -0.1013 280 VAL A N   
1826 C CA  . VAL A 245 ? 0.3710 0.3312 0.3988 0.0109  -0.1025 -0.0842 280 VAL A CA  
1827 C C   . VAL A 245 ? 0.4865 0.4172 0.5211 0.0051  -0.1038 -0.0796 280 VAL A C   
1828 O O   . VAL A 245 ? 0.4255 0.3558 0.4674 -0.0023 -0.0953 -0.0633 280 VAL A O   
1829 C CB  . VAL A 245 ? 0.3620 0.3352 0.3705 0.0290  -0.0920 -0.0858 280 VAL A CB  
1830 C CG1 . VAL A 245 ? 0.4934 0.4555 0.4882 0.0429  -0.0987 -0.1043 280 VAL A CG1 
1831 C CG2 . VAL A 245 ? 0.4870 0.4604 0.4978 0.0302  -0.0782 -0.0714 280 VAL A CG2 
1832 N N   . ALA A 246 ? 0.3964 0.3004 0.4268 0.0094  -0.1156 -0.0941 281 ALA A N   
1833 C CA  . ALA A 246 ? 0.4874 0.3580 0.5222 0.0047  -0.1194 -0.0894 281 ALA A CA  
1834 C C   . ALA A 246 ? 0.4883 0.3506 0.5397 -0.0179 -0.1201 -0.0745 281 ALA A C   
1835 O O   . ALA A 246 ? 0.4306 0.2850 0.4843 -0.0230 -0.1125 -0.0580 281 ALA A O   
1836 C CB  . ALA A 246 ? 0.4607 0.3007 0.4886 0.0128  -0.1349 -0.1093 281 ALA A CB  
1837 N N   . VAL A 247 ? 0.4529 0.3198 0.5163 -0.0318 -0.1291 -0.0804 282 VAL A N   
1838 C CA  . VAL A 247 ? 0.4258 0.2899 0.5083 -0.0555 -0.1287 -0.0668 282 VAL A CA  
1839 C C   . VAL A 247 ? 0.4609 0.3548 0.5483 -0.0592 -0.1121 -0.0474 282 VAL A C   
1840 O O   . VAL A 247 ? 0.4485 0.3338 0.5419 -0.0712 -0.1056 -0.0307 282 VAL A O   
1841 C CB  . VAL A 247 ? 0.4338 0.3072 0.5321 -0.0688 -0.1411 -0.0792 282 VAL A CB  
1842 C CG1 . VAL A 247 ? 0.4221 0.3069 0.5439 -0.0939 -0.1365 -0.0638 282 VAL A CG1 
1843 C CG2 . VAL A 247 ? 0.5393 0.3744 0.6348 -0.0691 -0.1594 -0.0975 282 VAL A CG2 
1844 N N   . GLU A 248 ? 0.3714 0.2988 0.4543 -0.0485 -0.1055 -0.0493 283 GLU A N   
1845 C CA  . GLU A 248 ? 0.3328 0.2876 0.4213 -0.0516 -0.0920 -0.0333 283 GLU A CA  
1846 C C   . GLU A 248 ? 0.3856 0.3308 0.4634 -0.0438 -0.0811 -0.0209 283 GLU A C   
1847 O O   . GLU A 248 ? 0.2882 0.2400 0.3714 -0.0514 -0.0722 -0.0056 283 GLU A O   
1848 C CB  . GLU A 248 ? 0.3279 0.3158 0.4126 -0.0412 -0.0897 -0.0386 283 GLU A CB  
1849 C CG  . GLU A 248 ? 0.3870 0.3953 0.4868 -0.0503 -0.0994 -0.0473 283 GLU A CG  
1850 C CD  . GLU A 248 ? 0.4027 0.4247 0.5267 -0.0704 -0.0962 -0.0362 283 GLU A CD  
1851 O OE1 . GLU A 248 ? 0.4417 0.4698 0.5840 -0.0841 -0.1064 -0.0441 283 GLU A OE1 
1852 O OE2 . GLU A 248 ? 0.4483 0.4772 0.5738 -0.0726 -0.0834 -0.0203 283 GLU A OE2 
1853 N N   . ARG A 249 ? 0.3922 0.3242 0.4554 -0.0282 -0.0817 -0.0282 284 ARG A N   
1854 C CA  . ARG A 249 ? 0.3875 0.3114 0.4432 -0.0206 -0.0737 -0.0188 284 ARG A CA  
1855 C C   . ARG A 249 ? 0.3853 0.2810 0.4434 -0.0307 -0.0766 -0.0089 284 ARG A C   
1856 O O   . ARG A 249 ? 0.3438 0.2418 0.4010 -0.0333 -0.0685 0.0056  284 ARG A O   
1857 C CB  . ARG A 249 ? 0.3760 0.2939 0.4196 -0.0027 -0.0748 -0.0305 284 ARG A CB  
1858 C CG  . ARG A 249 ? 0.3589 0.2680 0.3978 0.0056  -0.0694 -0.0237 284 ARG A CG  
1859 C CD  . ARG A 249 ? 0.4035 0.3147 0.4349 0.0228  -0.0694 -0.0366 284 ARG A CD  
1860 N NE  . ARG A 249 ? 0.4488 0.3845 0.4762 0.0278  -0.0645 -0.0435 284 ARG A NE  
1861 C CZ  . ARG A 249 ? 0.4575 0.3962 0.4769 0.0396  -0.0669 -0.0583 284 ARG A CZ  
1862 N NH1 . ARG A 249 ? 0.4992 0.4186 0.5155 0.0486  -0.0750 -0.0701 284 ARG A NH1 
1863 N NH2 . ARG A 249 ? 0.4096 0.3706 0.4220 0.0435  -0.0612 -0.0613 284 ARG A NH2 
1864 N N   . LYS A 250 ? 0.4004 0.2669 0.4596 -0.0361 -0.0887 -0.0165 285 LYS A N   
1865 C CA  . LYS A 250 ? 0.4096 0.2429 0.4682 -0.0462 -0.0921 -0.0053 285 LYS A CA  
1866 C C   . LYS A 250 ? 0.4379 0.2840 0.5080 -0.0662 -0.0843 0.0118  285 LYS A C   
1867 O O   . LYS A 250 ? 0.4227 0.2567 0.4876 -0.0708 -0.0786 0.0281  285 LYS A O   
1868 C CB  . LYS A 250 ? 0.5043 0.3012 0.5625 -0.0493 -0.1078 -0.0176 285 LYS A CB  
1869 C CG  . LYS A 250 ? 0.5095 0.2908 0.5547 -0.0271 -0.1156 -0.0348 285 LYS A CG  
1870 C CD  . LYS A 250 ? 0.6214 0.3698 0.6668 -0.0295 -0.1327 -0.0510 285 LYS A CD  
1871 C CE  . LYS A 250 ? 0.6446 0.3845 0.6775 -0.0053 -0.1401 -0.0715 285 LYS A CE  
1872 N NZ  . LYS A 250 ? 0.6314 0.3323 0.6615 -0.0057 -0.1567 -0.0845 285 LYS A NZ  
1873 N N   . LYS A 251 ? 0.3864 0.2611 0.4715 -0.0765 -0.0833 0.0082  286 LYS A N   
1874 C CA  . LYS A 251 ? 0.3246 0.2204 0.4240 -0.0944 -0.0746 0.0227  286 LYS A CA  
1875 C C   . LYS A 251 ? 0.3309 0.2499 0.4235 -0.0864 -0.0602 0.0356  286 LYS A C   
1876 O O   . LYS A 251 ? 0.3603 0.2789 0.4530 -0.0958 -0.0520 0.0519  286 LYS A O   
1877 C CB  . LYS A 251 ? 0.3495 0.2757 0.4675 -0.1027 -0.0785 0.0124  286 LYS A CB  
1878 C CG  . LYS A 251 ? 0.5364 0.4631 0.6764 -0.1282 -0.0816 0.0166  286 LYS A CG  
1879 C CD  . LYS A 251 ? 0.5481 0.5195 0.7085 -0.1330 -0.0825 0.0082  286 LYS A CD  
1880 C CE  . LYS A 251 ? 0.4534 0.4177 0.6207 -0.1341 -0.0999 -0.0130 286 LYS A CE  
1881 N NZ  . LYS A 251 ? 0.5214 0.5284 0.7002 -0.1292 -0.1034 -0.0248 286 LYS A NZ  
1882 N N   . ALA A 252 ? 0.3381 0.2763 0.4236 -0.0691 -0.0571 0.0284  287 ALA A N   
1883 C CA  . ALA A 252 ? 0.2862 0.2429 0.3652 -0.0606 -0.0455 0.0380  287 ALA A CA  
1884 C C   . ALA A 252 ? 0.3662 0.2981 0.4311 -0.0556 -0.0435 0.0475  287 ALA A C   
1885 O O   . ALA A 252 ? 0.2977 0.2373 0.3586 -0.0571 -0.0350 0.0604  287 ALA A O   
1886 C CB  . ALA A 252 ? 0.2700 0.2446 0.3435 -0.0444 -0.0440 0.0282  287 ALA A CB  
1887 N N   . PHE A 253 ? 0.3259 0.2288 0.3821 -0.0476 -0.0521 0.0402  288 PHE A N   
1888 C CA  . PHE A 253 ? 0.3343 0.2145 0.3766 -0.0395 -0.0524 0.0474  288 PHE A CA  
1889 C C   . PHE A 253 ? 0.4272 0.2857 0.4661 -0.0540 -0.0518 0.0636  288 PHE A C   
1890 O O   . PHE A 253 ? 0.4089 0.2668 0.4375 -0.0521 -0.0455 0.0769  288 PHE A O   
1891 C CB  . PHE A 253 ? 0.3758 0.2327 0.4113 -0.0257 -0.0626 0.0341  288 PHE A CB  
1892 C CG  . PHE A 253 ? 0.3470 0.2261 0.3827 -0.0104 -0.0600 0.0214  288 PHE A CG  
1893 C CD1 . PHE A 253 ? 0.3363 0.2477 0.3763 -0.0098 -0.0503 0.0233  288 PHE A CD1 
1894 C CD2 . PHE A 253 ? 0.3851 0.2523 0.4164 0.0037  -0.0667 0.0081  288 PHE A CD2 
1895 C CE1 . PHE A 253 ? 0.3069 0.2351 0.3463 0.0020  -0.0471 0.0141  288 PHE A CE1 
1896 C CE2 . PHE A 253 ? 0.3395 0.2297 0.3717 0.0159  -0.0619 -0.0019 288 PHE A CE2 
1897 C CZ  . PHE A 253 ? 0.3320 0.2508 0.3680 0.0139  -0.0520 0.0021  288 PHE A CZ  
1898 N N   . ALA A 254 ? 0.4339 0.2748 0.4811 -0.0694 -0.0581 0.0630  289 ALA A N   
1899 C CA  . ALA A 254 ? 0.4388 0.2577 0.4838 -0.0866 -0.0562 0.0804  289 ALA A CA  
1900 C C   . ALA A 254 ? 0.4058 0.2582 0.4561 -0.0967 -0.0414 0.0951  289 ALA A C   
1901 O O   . ALA A 254 ? 0.4150 0.2572 0.4526 -0.1004 -0.0348 0.1125  289 ALA A O   
1902 C CB  . ALA A 254 ? 0.4476 0.2447 0.5052 -0.1042 -0.0658 0.0755  289 ALA A CB  
1903 N N   . ASP A 255 ? 0.4251 0.3185 0.4916 -0.0986 -0.0361 0.0880  290 ASP A N   
1904 C CA  . ASP A 255 ? 0.4014 0.3296 0.4748 -0.1067 -0.0225 0.0998  290 ASP A CA  
1905 C C   . ASP A 255 ? 0.3899 0.3279 0.4458 -0.0906 -0.0144 0.1062  290 ASP A C   
1906 O O   . ASP A 255 ? 0.3370 0.2841 0.3866 -0.0958 -0.0042 0.1212  290 ASP A O   
1907 C CB  . ASP A 255 ? 0.3135 0.2820 0.4083 -0.1096 -0.0212 0.0887  290 ASP A CB  
1908 C CG  . ASP A 255 ? 0.3726 0.3778 0.4808 -0.1219 -0.0085 0.0996  290 ASP A CG  
1909 O OD1 . ASP A 255 ? 0.3473 0.3496 0.4674 -0.1432 -0.0058 0.1090  290 ASP A OD1 
1910 O OD2 . ASP A 255 ? 0.3328 0.3695 0.4402 -0.1107 -0.0009 0.0987  290 ASP A OD2 
1911 N N   . ALA A 256 ? 0.3402 0.2781 0.3883 -0.0713 -0.0187 0.0947  291 ALA A N   
1912 C CA  . ALA A 256 ? 0.2937 0.2401 0.3274 -0.0570 -0.0130 0.0989  291 ALA A CA  
1913 C C   . ALA A 256 ? 0.3866 0.3012 0.3998 -0.0536 -0.0153 0.1102  291 ALA A C   
1914 O O   . ALA A 256 ? 0.3705 0.2926 0.3704 -0.0486 -0.0086 0.1200  291 ALA A O   
1915 C CB  . ALA A 256 ? 0.3239 0.2791 0.3576 -0.0402 -0.0166 0.0841  291 ALA A CB  
1916 N N   . ALA A 257 ? 0.3391 0.2174 0.3477 -0.0548 -0.0255 0.1087  292 ALA A N   
1917 C CA  . ALA A 257 ? 0.3738 0.2185 0.3609 -0.0505 -0.0292 0.1206  292 ALA A CA  
1918 C C   . ALA A 257 ? 0.4859 0.3236 0.4665 -0.0682 -0.0207 0.1417  292 ALA A C   
1919 O O   . ALA A 257 ? 0.4841 0.3095 0.4427 -0.0633 -0.0177 0.1557  292 ALA A O   
1920 C CB  . ALA A 257 ? 0.4650 0.2710 0.4486 -0.0450 -0.0435 0.1124  292 ALA A CB  
1921 N N   . LYS A 258 ? 0.3956 0.2414 0.3947 -0.0891 -0.0169 0.1443  293 LYS A N   
1922 C CA  . LYS A 258 ? 0.4788 0.3286 0.4758 -0.1066 -0.0050 0.1615  293 LYS A CA  
1923 C C   . LYS A 258 ? 0.4744 0.3642 0.4672 -0.1029 0.0094  0.1693  293 LYS A C   
1924 O O   . LYS A 258 ? 0.4610 0.3474 0.4343 -0.1023 0.0188  0.1815  293 LYS A O   
1925 C CB  . LYS A 258 ? 0.5185 0.3777 0.5418 -0.1286 -0.0040 0.1574  293 LYS A CB  
1926 C CG  . LYS A 258 ? 0.7425 0.5606 0.7685 -0.1337 -0.0176 0.1493  293 LYS A CG  
1927 C CD  . LYS A 258 ? 0.5727 0.4037 0.6264 -0.1551 -0.0179 0.1429  293 LYS A CD  
1928 C CE  . LYS A 258 ? 0.7803 0.5683 0.8341 -0.1576 -0.0327 0.1327  293 LYS A CE  
1929 N NZ  . LYS A 258 ? 0.7645 0.5611 0.8448 -0.1773 -0.0359 0.1234  293 LYS A NZ  
1930 N N   . GLY A 259 ? 0.3955 0.3239 0.4045 -0.0969 0.0118  0.1577  294 GLY A N   
1931 C CA  . GLY A 259 ? 0.3418 0.3113 0.3506 -0.0928 0.0250  0.1614  294 GLY A CA  
1932 C C   . GLY A 259 ? 0.4182 0.3871 0.4039 -0.0704 0.0244  0.1596  294 GLY A C   
1933 O O   . GLY A 259 ? 0.3996 0.3930 0.3760 -0.0655 0.0348  0.1659  294 GLY A O   
1934 N N   . GLY A 260 ? 0.3513 0.2944 0.3286 -0.0564 0.0120  0.1499  295 GLY A N   
1935 C CA  . GLY A 260 ? 0.3948 0.3386 0.3542 -0.0358 0.0094  0.1456  295 GLY A CA  
1936 C C   . GLY A 260 ? 0.3511 0.3311 0.3191 -0.0262 0.0141  0.1343  295 GLY A C   
1937 O O   . GLY A 260 ? 0.3891 0.3791 0.3421 -0.0139 0.0168  0.1350  295 GLY A O   
1938 N N   . TYR A 261 ? 0.3246 0.3226 0.3149 -0.0304 0.0140  0.1234  296 TYR A N   
1939 C CA  . TYR A 261 ? 0.2845 0.3110 0.2822 -0.0202 0.0166  0.1122  296 TYR A CA  
1940 C C   . TYR A 261 ? 0.2951 0.3117 0.2980 -0.0102 0.0073  0.0974  296 TYR A C   
1941 O O   . TYR A 261 ? 0.2186 0.2122 0.2224 -0.0113 -0.0005 0.0943  296 TYR A O   
1942 C CB  . TYR A 261 ? 0.2309 0.2885 0.2478 -0.0305 0.0241  0.1121  296 TYR A CB  
1943 C CG  . TYR A 261 ? 0.2186 0.2712 0.2541 -0.0436 0.0192  0.1082  296 TYR A CG  
1944 C CD1 . TYR A 261 ? 0.2012 0.2515 0.2451 -0.0373 0.0114  0.0943  296 TYR A CD1 
1945 C CD2 . TYR A 261 ? 0.3188 0.3685 0.3628 -0.0626 0.0221  0.1181  296 TYR A CD2 
1946 C CE1 . TYR A 261 ? 0.1994 0.2452 0.2571 -0.0470 0.0057  0.0889  296 TYR A CE1 
1947 C CE2 . TYR A 261 ? 0.2835 0.3277 0.3451 -0.0741 0.0153  0.1118  296 TYR A CE2 
1948 C CZ  . TYR A 261 ? 0.3034 0.3464 0.3706 -0.0647 0.0067  0.0963  296 TYR A CZ  
1949 O OH  . TYR A 261 ? 0.2870 0.3253 0.3682 -0.0730 -0.0013 0.0879  296 TYR A OH  
1950 N N   . LEU A 262 ? 0.2475 0.2815 0.2531 0.0002  0.0083  0.0884  297 LEU A N   
1951 C CA  . LEU A 262 ? 0.2139 0.2405 0.2237 0.0086  0.0018  0.0762  297 LEU A CA  
1952 C C   . LEU A 262 ? 0.2185 0.2492 0.2428 0.0030  0.0003  0.0699  297 LEU A C   
1953 O O   . LEU A 262 ? 0.2161 0.2636 0.2492 -0.0034 0.0041  0.0715  297 LEU A O   
1954 C CB  . LEU A 262 ? 0.2613 0.3004 0.2681 0.0202  0.0030  0.0696  297 LEU A CB  
1955 C CG  . LEU A 262 ? 0.2911 0.3257 0.2827 0.0300  0.0011  0.0703  297 LEU A CG  
1956 C CD1 . LEU A 262 ? 0.2726 0.3207 0.2634 0.0397  0.0021  0.0624  297 LEU A CD1 
1957 C CD2 . LEU A 262 ? 0.2184 0.2344 0.2086 0.0346  -0.0074 0.0651  297 LEU A CD2 
1958 N N   . ILE A 263 ? 0.1722 0.1898 0.1988 0.0065  -0.0054 0.0620  298 ILE A N   
1959 C CA  . ILE A 263 ? 0.1884 0.2096 0.2241 0.0049  -0.0070 0.0545  298 ILE A CA  
1960 C C   . ILE A 263 ? 0.1776 0.2010 0.2131 0.0140  -0.0068 0.0470  298 ILE A C   
1961 O O   . ILE A 263 ? 0.1812 0.1999 0.2127 0.0202  -0.0078 0.0456  298 ILE A O   
1962 C CB  . ILE A 263 ? 0.2211 0.2248 0.2589 0.0002  -0.0131 0.0515  298 ILE A CB  
1963 C CG1 . ILE A 263 ? 0.2977 0.2858 0.3306 0.0087  -0.0175 0.0465  298 ILE A CG1 
1964 C CG2 . ILE A 263 ? 0.2047 0.1997 0.2425 -0.0110 -0.0139 0.0602  298 ILE A CG2 
1965 C CD1 . ILE A 263 ? 0.3289 0.3007 0.3631 0.0088  -0.0241 0.0401  298 ILE A CD1 
1966 N N   . ALA A 264 ? 0.1552 0.1852 0.1948 0.0144  -0.0060 0.0423  299 ALA A N   
1967 C CA  . ALA A 264 ? 0.2038 0.2327 0.2434 0.0202  -0.0049 0.0366  299 ALA A CA  
1968 C C   . ALA A 264 ? 0.2341 0.2629 0.2745 0.0190  -0.0056 0.0321  299 ALA A C   
1969 O O   . ALA A 264 ? 0.2466 0.2803 0.2880 0.0153  -0.0073 0.0325  299 ALA A O   
1970 C CB  . ALA A 264 ? 0.1633 0.1998 0.2012 0.0245  -0.0015 0.0374  299 ALA A CB  
1971 N N   . ALA A 265 ? 0.1679 0.1935 0.2085 0.0223  -0.0043 0.0270  300 ALA A N   
1972 C CA  . ALA A 265 ? 0.2302 0.2574 0.2682 0.0229  -0.0039 0.0226  300 ALA A CA  
1973 C C   . ALA A 265 ? 0.1553 0.1856 0.1916 0.0258  0.0023  0.0215  300 ALA A C   
1974 O O   . ALA A 265 ? 0.1930 0.2227 0.2350 0.0265  0.0046  0.0204  300 ALA A O   
1975 C CB  . ALA A 265 ? 0.2733 0.2927 0.3123 0.0232  -0.0087 0.0162  300 ALA A CB  
1976 N N   . SER A 266 ? 0.1817 0.2153 0.2101 0.0272  0.0047  0.0215  301 SER A N   
1977 C CA  . SER A 266 ? 0.1508 0.1854 0.1742 0.0283  0.0122  0.0241  301 SER A CA  
1978 C C   . SER A 266 ? 0.2210 0.2587 0.2514 0.0278  0.0174  0.0198  301 SER A C   
1979 O O   . SER A 266 ? 0.1783 0.2167 0.2123 0.0252  0.0238  0.0227  301 SER A O   
1980 C CB  . SER A 266 ? 0.2422 0.2791 0.2516 0.0315  0.0130  0.0250  301 SER A CB  
1981 O OG  . SER A 266 ? 0.3267 0.3657 0.3326 0.0328  0.0065  0.0266  301 SER A OG  
1982 N N   . HIS A 267 ? 0.1502 0.1904 0.1837 0.0303  0.0146  0.0121  302 HIS A N   
1983 C CA  . HIS A 267 ? 0.1862 0.2348 0.2277 0.0320  0.0196  0.0058  302 HIS A CA  
1984 C C   . HIS A 267 ? 0.1858 0.2333 0.2400 0.0344  0.0136  -0.0001 302 HIS A C   
1985 O O   . HIS A 267 ? 0.1968 0.2538 0.2594 0.0383  0.0157  -0.0079 302 HIS A O   
1986 C CB  . HIS A 267 ? 0.1954 0.2498 0.2275 0.0370  0.0219  -0.0003 302 HIS A CB  
1987 C CG  . HIS A 267 ? 0.2596 0.3144 0.2754 0.0366  0.0268  0.0060  302 HIS A CG  
1988 N ND1 . HIS A 267 ? 0.2329 0.2895 0.2453 0.0326  0.0366  0.0147  302 HIS A ND1 
1989 C CD2 . HIS A 267 ? 0.2640 0.3159 0.2653 0.0399  0.0219  0.0053  302 HIS A CD2 
1990 C CE1 . HIS A 267 ? 0.2054 0.2589 0.1991 0.0349  0.0379  0.0201  302 HIS A CE1 
1991 N NE2 . HIS A 267 ? 0.2083 0.2608 0.1956 0.0399  0.0285  0.0137  302 HIS A NE2 
1992 N N   . LEU A 268 ? 0.1521 0.1901 0.2074 0.0332  0.0066  0.0034  303 LEU A N   
1993 C CA  . LEU A 268 ? 0.1555 0.1926 0.2206 0.0362  0.0017  -0.0004 303 LEU A CA  
1994 C C   . LEU A 268 ? 0.1391 0.1859 0.2152 0.0336  0.0065  -0.0005 303 LEU A C   
1995 O O   . LEU A 268 ? 0.1985 0.2458 0.2724 0.0283  0.0123  0.0051  303 LEU A O   
1996 C CB  . LEU A 268 ? 0.1908 0.2150 0.2506 0.0358  -0.0060 0.0047  303 LEU A CB  
1997 C CG  . LEU A 268 ? 0.2238 0.2356 0.2759 0.0352  -0.0119 0.0057  303 LEU A CG  
1998 C CD1 . LEU A 268 ? 0.2140 0.2163 0.2619 0.0323  -0.0161 0.0136  303 LEU A CD1 
1999 C CD2 . LEU A 268 ? 0.1821 0.1883 0.2366 0.0423  -0.0172 -0.0034 303 LEU A CD2 
2000 N N   . SER A 269 ? 0.1260 0.1798 0.2146 0.0376  0.0032  -0.0076 304 SER A N   
2001 C CA  . SER A 269 ? 0.1418 0.2069 0.2451 0.0340  0.0062  -0.0101 304 SER A CA  
2002 C C   . SER A 269 ? 0.1766 0.2323 0.2750 0.0295  0.0048  -0.0036 304 SER A C   
2003 O O   . SER A 269 ? 0.1761 0.2227 0.2671 0.0333  -0.0026 -0.0016 304 SER A O   
2004 C CB  . SER A 269 ? 0.2214 0.2950 0.3382 0.0413  -0.0015 -0.0198 304 SER A CB  
2005 O OG  . SER A 269 ? 0.1695 0.2578 0.3048 0.0369  0.0004  -0.0246 304 SER A OG  
2006 N N   . PHE A 270 ? 0.1267 0.1840 0.2289 0.0220  0.0121  -0.0005 305 PHE A N   
2007 C CA  . PHE A 270 ? 0.1499 0.1955 0.2451 0.0195  0.0105  0.0048  305 PHE A CA  
2008 C C   . PHE A 270 ? 0.1603 0.2046 0.2594 0.0240  0.0009  -0.0003 305 PHE A C   
2009 O O   . PHE A 270 ? 0.1398 0.1943 0.2542 0.0246  -0.0027 -0.0087 305 PHE A O   
2010 C CB  . PHE A 270 ? 0.2016 0.2459 0.3031 0.0106  0.0182  0.0073  305 PHE A CB  
2011 C CG  . PHE A 270 ? 0.1452 0.1742 0.2393 0.0099  0.0153  0.0111  305 PHE A CG  
2012 C CD1 . PHE A 270 ? 0.1807 0.1988 0.2572 0.0127  0.0166  0.0190  305 PHE A CD1 
2013 C CD2 . PHE A 270 ? 0.1359 0.1621 0.2408 0.0076  0.0101  0.0051  305 PHE A CD2 
2014 C CE1 . PHE A 270 ? 0.2361 0.2406 0.3051 0.0150  0.0131  0.0212  305 PHE A CE1 
2015 C CE2 . PHE A 270 ? 0.2348 0.2448 0.3311 0.0091  0.0063  0.0067  305 PHE A CE2 
2016 C CZ  . PHE A 270 ? 0.2446 0.2437 0.3228 0.0134  0.0081  0.0148  305 PHE A CZ  
2017 N N   . PRO A 271 ? 0.1444 0.1791 0.2300 0.0280  -0.0036 0.0037  306 PRO A N   
2018 C CA  . PRO A 271 ? 0.1361 0.1629 0.2075 0.0278  -0.0003 0.0119  306 PRO A CA  
2019 C C   . PRO A 271 ? 0.1960 0.2233 0.2585 0.0292  0.0003  0.0166  306 PRO A C   
2020 O O   . PRO A 271 ? 0.1733 0.1984 0.2271 0.0290  0.0024  0.0220  306 PRO A O   
2021 C CB  . PRO A 271 ? 0.1963 0.2187 0.2607 0.0329  -0.0059 0.0113  306 PRO A CB  
2022 C CG  . PRO A 271 ? 0.1826 0.2093 0.2497 0.0377  -0.0130 0.0062  306 PRO A CG  
2023 C CD  . PRO A 271 ? 0.1200 0.1541 0.2044 0.0341  -0.0126 -0.0008 306 PRO A CD  
2024 N N   . GLY A 272 ? 0.2088 0.2383 0.2743 0.0312  -0.0027 0.0136  307 GLY A N   
2025 C CA  . GLY A 272 ? 0.2240 0.2506 0.2826 0.0313  -0.0033 0.0166  307 GLY A CA  
2026 C C   . GLY A 272 ? 0.2113 0.2330 0.2607 0.0316  -0.0066 0.0227  307 GLY A C   
2027 O O   . GLY A 272 ? 0.1285 0.1487 0.1739 0.0287  -0.0063 0.0260  307 GLY A O   
2028 N N   . ILE A 273 ? 0.2378 0.2582 0.2838 0.0349  -0.0099 0.0240  308 ILE A N   
2029 C CA  . ILE A 273 ? 0.1657 0.1850 0.2019 0.0347  -0.0104 0.0312  308 ILE A CA  
2030 C C   . ILE A 273 ? 0.1920 0.2030 0.2223 0.0382  -0.0160 0.0329  308 ILE A C   
2031 O O   . ILE A 273 ? 0.2047 0.2149 0.2368 0.0441  -0.0207 0.0274  308 ILE A O   
2032 C CB  . ILE A 273 ? 0.1473 0.1729 0.1794 0.0379  -0.0086 0.0319  308 ILE A CB  
2033 C CG1 . ILE A 273 ? 0.1797 0.2088 0.2153 0.0368  -0.0047 0.0305  308 ILE A CG1 
2034 C CG2 . ILE A 273 ? 0.2305 0.2599 0.2522 0.0388  -0.0075 0.0393  308 ILE A CG2 
2035 C CD1 . ILE A 273 ? 0.1357 0.1664 0.1673 0.0426  -0.0053 0.0283  308 ILE A CD1 
2036 N N   . GLY A 274 ? 0.2284 0.1693 0.2449 -0.0059 -0.0032 0.0063  309 GLY A N   
2037 C CA  . GLY A 274 ? 0.2191 0.1730 0.2684 -0.0030 -0.0159 0.0128  309 GLY A CA  
2038 C C   . GLY A 274 ? 0.2311 0.1792 0.2693 -0.0116 -0.0309 0.0265  309 GLY A C   
2039 O O   . GLY A 274 ? 0.2399 0.1833 0.2535 -0.0194 -0.0323 0.0296  309 GLY A O   
2040 N N   . HIS A 275 ? 0.2481 0.1934 0.3030 -0.0108 -0.0447 0.0345  310 HIS A N   
2041 C CA  . HIS A 275 ? 0.2590 0.1905 0.3001 -0.0226 -0.0578 0.0479  310 HIS A CA  
2042 C C   . HIS A 275 ? 0.3432 0.2365 0.3911 -0.0216 -0.0581 0.0386  310 HIS A C   
2043 O O   . HIS A 275 ? 0.3487 0.2309 0.4189 -0.0107 -0.0477 0.0208  310 HIS A O   
2044 C CB  . HIS A 275 ? 0.2684 0.2041 0.3074 -0.0256 -0.0746 0.0646  310 HIS A CB  
2045 C CG  . HIS A 275 ? 0.3201 0.2906 0.3477 -0.0299 -0.0721 0.0728  310 HIS A CG  
2046 N ND1 . HIS A 275 ? 0.2952 0.2837 0.3328 -0.0184 -0.0708 0.0687  310 HIS A ND1 
2047 C CD2 . HIS A 275 ? 0.3392 0.3320 0.3506 -0.0446 -0.0688 0.0812  310 HIS A CD2 
2048 C CE1 . HIS A 275 ? 0.3982 0.4143 0.4208 -0.0249 -0.0667 0.0753  310 HIS A CE1 
2049 N NE2 . HIS A 275 ? 0.3626 0.3850 0.3730 -0.0403 -0.0641 0.0815  310 HIS A NE2 
2050 N N   . ILE A 276 ? 0.3223 0.1953 0.3533 -0.0343 -0.0687 0.0490  311 ILE A N   
2051 C CA  . ILE A 276 ? 0.3535 0.1854 0.3858 -0.0344 -0.0699 0.0401  311 ILE A CA  
2052 C C   . ILE A 276 ? 0.4657 0.2719 0.4876 -0.0431 -0.0906 0.0568  311 ILE A C   
2053 O O   . ILE A 276 ? 0.4432 0.2607 0.4430 -0.0606 -0.0965 0.0738  311 ILE A O   
2054 C CB  . ILE A 276 ? 0.4109 0.2296 0.4178 -0.0457 -0.0596 0.0320  311 ILE A CB  
2055 C CG1 . ILE A 276 ? 0.4971 0.2694 0.5020 -0.0457 -0.0573 0.0190  311 ILE A CG1 
2056 C CG2 . ILE A 276 ? 0.4289 0.2615 0.4147 -0.0643 -0.0695 0.0465  311 ILE A CG2 
2057 C CD1 . ILE A 276 ? 0.5314 0.2944 0.5681 -0.0279 -0.0443 -0.0014 311 ILE A CD1 
2058 N N   . ARG A 277 ? 0.4085 0.1779 0.4462 -0.0314 -0.1013 0.0506  312 ARG A N   
2059 C CA  . ARG A 277 ? 0.5563 0.2833 0.5726 -0.0407 -0.1229 0.0664  312 ARG A CA  
2060 C C   . ARG A 277 ? 0.4945 0.1748 0.5174 -0.0350 -0.1248 0.0520  312 ARG A C   
2061 O O   . ARG A 277 ? 0.4866 0.1666 0.5419 -0.0174 -0.1123 0.0278  312 ARG A O   
2062 C CB  . ARG A 277 ? 0.5285 0.2417 0.5458 -0.0306 -0.1472 0.0797  312 ARG A CB  
2063 C CG  . ARG A 277 ? 0.5506 0.2707 0.6158 -0.0011 -0.1539 0.0619  312 ARG A CG  
2064 C CD  . ARG A 277 ? 0.5432 0.2475 0.5992 0.0073  -0.1838 0.0750  312 ARG A CD  
2065 N NE  . ARG A 277 ? 0.6143 0.3118 0.7132 0.0335  -0.1979 0.0544  312 ARG A NE  
2066 C CZ  . ARG A 277 ? 0.6538 0.3842 0.8004 0.0530  -0.2009 0.0378  312 ARG A CZ  
2067 N NH1 . ARG A 277 ? 0.5887 0.3558 0.7428 0.0513  -0.1906 0.0400  312 ARG A NH1 
2068 N NH2 . ARG A 277 ? 0.8232 0.5523 1.0127 0.0736  -0.2144 0.0172  312 ARG A NH2 
2069 N N   . ALA A 278 ? 0.5374 0.1844 0.5277 -0.0520 -0.1352 0.0644  313 ALA A N   
2070 C CA  . ALA A 278 ? 0.6180 0.2274 0.6080 -0.0460 -0.1359 0.0513  313 ALA A CA  
2071 C C   . ALA A 278 ? 0.6140 0.2088 0.6365 -0.0172 -0.1494 0.0407  313 ALA A C   
2072 O O   . ALA A 278 ? 0.7099 0.3051 0.7311 -0.0103 -0.1701 0.0536  313 ALA A O   
2073 C CB  . ALA A 278 ? 0.7189 0.3028 0.6671 -0.0702 -0.1446 0.0677  313 ALA A CB  
2074 N N   . GLU A 279 ? 0.6137 0.1973 0.6645 -0.0012 -0.1374 0.0150  314 GLU A N   
2075 C CA  . GLU A 279 ? 0.6366 0.2114 0.7261 0.0263  -0.1502 0.0004  314 GLU A CA  
2076 C C   . GLU A 279 ? 0.7399 0.2840 0.8333 0.0309  -0.1370 -0.0203 314 GLU A C   
2077 O O   . GLU A 279 ? 0.6600 0.2124 0.7612 0.0287  -0.1072 -0.0414 314 GLU A O   
2078 C CB  . GLU A 279 ? 0.5921 0.2122 0.7363 0.0460  -0.1415 -0.0179 314 GLU A CB  
2079 C CG  . GLU A 279 ? 0.7718 0.3971 0.9602 0.0719  -0.1637 -0.0288 314 GLU A CG  
2080 C CD  . GLU A 279 ? 0.8368 0.4663 1.0090 0.0717  -0.1949 -0.0052 314 GLU A CD  
2081 O OE1 . GLU A 279 ? 0.6882 0.3556 0.8994 0.0843  -0.1992 -0.0140 314 GLU A OE1 
2082 O OE2 . GLU A 279 ? 0.8573 0.4509 0.9733 0.0560  -0.2131 0.0210  314 GLU A OE2 
2083 N N   . GLY A 280 ? 0.7339 0.2370 0.8133 0.0351  -0.1581 -0.0141 315 GLY A N   
2084 C CA  . GLY A 280 ? 0.7766 0.2472 0.8589 0.0402  -0.1459 -0.0341 315 GLY A CA  
2085 C C   . GLY A 280 ? 0.7743 0.2326 0.8181 0.0143  -0.1215 -0.0353 315 GLY A C   
2086 O O   . GLY A 280 ? 0.7673 0.2290 0.7733 -0.0107 -0.1261 -0.0135 315 GLY A O   
2087 N N   . LYS A 281 ? 0.7921 0.2374 0.8447 0.0194  -0.0954 -0.0630 316 LYS A N   
2088 C CA  . LYS A 281 ? 0.7944 0.2281 0.8112 -0.0040 -0.0710 -0.0700 316 LYS A CA  
2089 C C   . LYS A 281 ? 0.7677 0.2384 0.7751 -0.0176 -0.0566 -0.0668 316 LYS A C   
2090 O O   . LYS A 281 ? 0.7406 0.2088 0.7183 -0.0385 -0.0463 -0.0674 316 LYS A O   
2091 C CB  . LYS A 281 ? 0.8351 0.2417 0.8539 0.0046  -0.0428 -0.1028 316 LYS A CB  
2092 C CG  . LYS A 281 ? 0.9277 0.2939 0.9579 0.0206  -0.0529 -0.1124 316 LYS A CG  
2093 C CD  . LYS A 281 ? 0.9301 0.2653 0.9314 0.0039  -0.0772 -0.0893 316 LYS A CD  
2094 C CE  . LYS A 281 ? 1.0983 0.3844 1.0881 0.0038  -0.0665 -0.1080 316 LYS A CE  
2095 N NZ  . LYS A 281 ? 1.0412 0.2911 1.0023 -0.0104 -0.0927 -0.0879 316 LYS A NZ  
2096 N N   . GLY A 282 ? 0.7019 0.2094 0.7381 -0.0049 -0.0584 -0.0652 317 GLY A N   
2097 C CA  . GLY A 282 ? 0.6950 0.2325 0.7207 -0.0164 -0.0445 -0.0637 317 GLY A CA  
2098 C C   . GLY A 282 ? 0.6200 0.1936 0.6592 -0.0152 -0.0638 -0.0411 317 GLY A C   
2099 O O   . GLY A 282 ? 0.6104 0.1802 0.6346 -0.0231 -0.0884 -0.0161 317 GLY A O   
2100 N N   . TYR A 283 ? 0.5637 0.1709 0.6287 -0.0066 -0.0503 -0.0510 318 TYR A N   
2101 C CA  . TYR A 283 ? 0.5190 0.1603 0.5924 -0.0081 -0.0628 -0.0323 318 TYR A CA  
2102 C C   . TYR A 283 ? 0.5310 0.2077 0.6567 0.0123  -0.0516 -0.0499 318 TYR A C   
2103 O O   . TYR A 283 ? 0.5342 0.2172 0.6795 0.0195  -0.0246 -0.0774 318 TYR A O   
2104 C CB  . TYR A 283 ? 0.4972 0.1558 0.5293 -0.0289 -0.0522 -0.0228 318 TYR A CB  
2105 C CG  . TYR A 283 ? 0.6242 0.2605 0.6128 -0.0515 -0.0657 -0.0067 318 TYR A CG  
2106 C CD1 . TYR A 283 ? 0.6066 0.2594 0.5833 -0.0646 -0.0850 0.0196  318 TYR A CD1 
2107 C CD2 . TYR A 283 ? 0.5601 0.1624 0.5206 -0.0615 -0.0564 -0.0200 318 TYR A CD2 
2108 C CE1 . TYR A 283 ? 0.5783 0.2170 0.5239 -0.0884 -0.0945 0.0309  318 TYR A CE1 
2109 C CE2 . TYR A 283 ? 0.6405 0.2342 0.5697 -0.0817 -0.0686 -0.0075 318 TYR A CE2 
2110 C CZ  . TYR A 283 ? 0.6029 0.2169 0.5282 -0.0952 -0.0871 0.0168  318 TYR A CZ  
2111 O OH  . TYR A 283 ? 0.6900 0.3010 0.5920 -0.1174 -0.0967 0.0256  318 TYR A OH  
2112 N N   . ARG A 284 ? 0.5072 0.2083 0.6510 0.0192  -0.0720 -0.0335 319 ARG A N   
2113 C CA  . ARG A 284 ? 0.4717 0.2166 0.6557 0.0314  -0.0613 -0.0454 319 ARG A CA  
2114 C C   . ARG A 284 ? 0.4541 0.2341 0.6057 0.0174  -0.0522 -0.0291 319 ARG A C   
2115 O O   . ARG A 284 ? 0.3802 0.1647 0.4979 0.0062  -0.0689 -0.0026 319 ARG A O   
2116 C CB  . ARG A 284 ? 0.5199 0.2809 0.7457 0.0516  -0.0890 -0.0426 319 ARG A CB  
2117 C CG  . ARG A 284 ? 0.7433 0.5188 1.0261 0.0727  -0.0918 -0.0680 319 ARG A CG  
2118 C CD  . ARG A 284 ? 0.7420 0.5666 1.0762 0.0777  -0.0659 -0.0947 319 ARG A CD  
2119 N NE  . ARG A 284 ? 0.8907 0.7192 1.1984 0.0607  -0.0267 -0.1025 319 ARG A NE  
2120 C CZ  . ARG A 284 ? 0.9179 0.7250 1.2012 0.0505  0.0014  -0.1161 319 ARG A CZ  
2121 N NH1 . ARG A 284 ? 1.1195 0.9220 1.4323 0.0594  0.0072  -0.1366 319 ARG A NH1 
2122 N NH2 . ARG A 284 ? 0.7551 0.5447 0.9825 0.0313  0.0222  -0.1100 319 ARG A NH2 
2123 N N   . PHE A 285 ? 0.3899 0.1939 0.5556 0.0185  -0.0252 -0.0472 320 PHE A N   
2124 C CA  . PHE A 285 ? 0.3280 0.1642 0.4736 0.0116  -0.0178 -0.0369 320 PHE A CA  
2125 C C   . PHE A 285 ? 0.3085 0.1771 0.4932 0.0246  -0.0312 -0.0351 320 PHE A C   
2126 O O   . PHE A 285 ? 0.3295 0.2067 0.5686 0.0386  -0.0286 -0.0567 320 PHE A O   
2127 C CB  . PHE A 285 ? 0.3701 0.2019 0.5009 0.0039  0.0174  -0.0575 320 PHE A CB  
2128 C CG  . PHE A 285 ? 0.3847 0.2375 0.4888 -0.0022 0.0250  -0.0493 320 PHE A CG  
2129 C CD1 . PHE A 285 ? 0.3566 0.2127 0.4161 -0.0106 0.0121  -0.0276 320 PHE A CD1 
2130 C CD2 . PHE A 285 ? 0.2979 0.1662 0.4249 0.0001  0.0466  -0.0671 320 PHE A CD2 
2131 C CE1 . PHE A 285 ? 0.2913 0.1636 0.3288 -0.0124 0.0175  -0.0230 320 PHE A CE1 
2132 C CE2 . PHE A 285 ? 0.3354 0.2151 0.4338 -0.0051 0.0532  -0.0605 320 PHE A CE2 
2133 C CZ  . PHE A 285 ? 0.3270 0.2067 0.3794 -0.0095 0.0376  -0.0383 320 PHE A CZ  
2134 N N   . VAL A 286 ? 0.2842 0.1722 0.4438 0.0198  -0.0451 -0.0123 321 VAL A N   
2135 C CA  . VAL A 286 ? 0.2666 0.1808 0.4495 0.0294  -0.0596 -0.0084 321 VAL A CA  
2136 C C   . VAL A 286 ? 0.2376 0.1792 0.4038 0.0233  -0.0414 -0.0087 321 VAL A C   
2137 O O   . VAL A 286 ? 0.2295 0.1790 0.3565 0.0139  -0.0436 0.0090  321 VAL A O   
2138 C CB  . VAL A 286 ? 0.2840 0.1879 0.4439 0.0279  -0.0914 0.0176  321 VAL A CB  
2139 C CG1 . VAL A 286 ? 0.2766 0.1998 0.4534 0.0378  -0.1091 0.0201  321 VAL A CG1 
2140 C CG2 . VAL A 286 ? 0.3260 0.1885 0.4937 0.0337  -0.1120 0.0188  321 VAL A CG2 
2141 N N   . PRO A 287 ? 0.2260 0.1817 0.4230 0.0276  -0.0224 -0.0306 322 PRO A N   
2142 C CA  . PRO A 287 ? 0.2118 0.1834 0.3872 0.0214  -0.0057 -0.0314 322 PRO A CA  
2143 C C   . PRO A 287 ? 0.1921 0.1855 0.3533 0.0235  -0.0256 -0.0122 322 PRO A C   
2144 O O   . PRO A 287 ? 0.1949 0.1951 0.3757 0.0311  -0.0492 -0.0061 322 PRO A O   
2145 C CB  . PRO A 287 ? 0.2058 0.1881 0.4276 0.0242  0.0147  -0.0598 322 PRO A CB  
2146 C CG  . PRO A 287 ? 0.2254 0.1934 0.4865 0.0293  0.0199  -0.0787 322 PRO A CG  
2147 C CD  . PRO A 287 ? 0.2349 0.1904 0.4903 0.0371  -0.0132 -0.0588 322 PRO A CD  
2148 N N   . VAL A 288 ? 0.1833 0.1826 0.3059 0.0172  -0.0176 -0.0035 323 VAL A N   
2149 C CA  . VAL A 288 ? 0.1937 0.2138 0.3001 0.0179  -0.0312 0.0118  323 VAL A CA  
2150 C C   . VAL A 288 ? 0.2003 0.2361 0.3345 0.0252  -0.0379 0.0037  323 VAL A C   
2151 O O   . VAL A 288 ? 0.1605 0.1990 0.3209 0.0270  -0.0236 -0.0155 323 VAL A O   
2152 C CB  . VAL A 288 ? 0.1662 0.1915 0.2371 0.0139  -0.0204 0.0155  323 VAL A CB  
2153 C CG1 . VAL A 288 ? 0.1997 0.2131 0.2657 0.0144  0.0000  -0.0009 323 VAL A CG1 
2154 C CG2 . VAL A 288 ? 0.2368 0.2865 0.2949 0.0148  -0.0303 0.0272  323 VAL A CG2 
2155 N N   . ASN A 289 ? 0.1988 0.2415 0.3255 0.0271  -0.0601 0.0174  324 ASN A N   
2156 C CA  . ASN A 289 ? 0.1714 0.2262 0.3155 0.0334  -0.0730 0.0118  324 ASN A CA  
2157 C C   . ASN A 289 ? 0.1637 0.2333 0.2974 0.0315  -0.0549 0.0034  324 ASN A C   
2158 O O   . ASN A 289 ? 0.1511 0.2241 0.2492 0.0274  -0.0455 0.0121  324 ASN A O   
2159 C CB  . ASN A 289 ? 0.1950 0.2431 0.3082 0.0313  -0.0982 0.0315  324 ASN A CB  
2160 C CG  . ASN A 289 ? 0.2479 0.2995 0.3716 0.0381  -0.1199 0.0270  324 ASN A CG  
2161 O OD1 . ASN A 289 ? 0.2836 0.3371 0.4555 0.0483  -0.1323 0.0112  324 ASN A OD1 
2162 N ND2 . ASN A 289 ? 0.2401 0.2924 0.3207 0.0322  -0.1260 0.0387  324 ASN A ND2 
2163 N N   . TYR A 290 ? 0.1505 0.2285 0.3186 0.0346  -0.0509 -0.0154 325 TYR A N   
2164 C CA  . TYR A 290 ? 0.1440 0.2279 0.2986 0.0312  -0.0346 -0.0239 325 TYR A CA  
2165 C C   . TYR A 290 ? 0.1484 0.2402 0.2680 0.0324  -0.0479 -0.0106 325 TYR A C   
2166 O O   . TYR A 290 ? 0.1613 0.2557 0.2808 0.0349  -0.0718 -0.0033 325 TYR A O   
2167 C CB  . TYR A 290 ? 0.1429 0.2362 0.3453 0.0301  -0.0283 -0.0483 325 TYR A CB  
2168 C CG  . TYR A 290 ? 0.1447 0.2366 0.3271 0.0238  -0.0123 -0.0565 325 TYR A CG  
2169 C CD1 . TYR A 290 ? 0.1650 0.2348 0.3177 0.0157  0.0161  -0.0612 325 TYR A CD1 
2170 C CD2 . TYR A 290 ? 0.1625 0.2670 0.3489 0.0256  -0.0280 -0.0597 325 TYR A CD2 
2171 C CE1 . TYR A 290 ? 0.2189 0.2766 0.3457 0.0101  0.0287  -0.0679 325 TYR A CE1 
2172 C CE2 . TYR A 290 ? 0.1552 0.2530 0.3206 0.0193  -0.0134 -0.0682 325 TYR A CE2 
2173 C CZ  . TYR A 290 ? 0.2219 0.2953 0.3579 0.0120  0.0148  -0.0718 325 TYR A CZ  
2174 O OH  . TYR A 290 ? 0.2159 0.2728 0.3245 0.0062  0.0266  -0.0790 325 TYR A OH  
2175 N N   . SER A 291 ? 0.1473 0.2380 0.2329 0.0309  -0.0331 -0.0082 326 SER A N   
2176 C CA  . SER A 291 ? 0.1956 0.2955 0.2495 0.0321  -0.0394 0.0001  326 SER A CA  
2177 C C   . SER A 291 ? 0.2625 0.3582 0.3009 0.0341  -0.0249 -0.0107 326 SER A C   
2178 O O   . SER A 291 ? 0.2707 0.3506 0.3046 0.0336  -0.0093 -0.0173 326 SER A O   
2179 C CB  . SER A 291 ? 0.1818 0.2874 0.2114 0.0296  -0.0398 0.0157  326 SER A CB  
2180 O OG  . SER A 291 ? 0.2971 0.4142 0.2994 0.0281  -0.0422 0.0208  326 SER A OG  
2181 N N   . VAL A 292 ? 0.2230 0.3247 0.2469 0.0355  -0.0309 -0.0131 327 VAL A N   
2182 C CA  . VAL A 292 ? 0.2478 0.3398 0.2555 0.0379  -0.0195 -0.0244 327 VAL A CA  
2183 C C   . VAL A 292 ? 0.3114 0.4076 0.2890 0.0453  -0.0136 -0.0191 327 VAL A C   
2184 O O   . VAL A 292 ? 0.3026 0.4173 0.2708 0.0450  -0.0185 -0.0106 327 VAL A O   
2185 C CB  . VAL A 292 ? 0.2888 0.3835 0.2979 0.0356  -0.0302 -0.0329 327 VAL A CB  
2186 C CG1 . VAL A 292 ? 0.2910 0.3731 0.2725 0.0387  -0.0200 -0.0427 327 VAL A CG1 
2187 C CG2 . VAL A 292 ? 0.2017 0.2978 0.2555 0.0297  -0.0368 -0.0447 327 VAL A CG2 
2188 N N   . VAL A 293 ? 0.2773 0.3547 0.2404 0.0512  -0.0032 -0.0253 328 VAL A N   
2189 C CA  . VAL A 293 ? 0.3242 0.4075 0.2691 0.0629  -0.0018 -0.0251 328 VAL A CA  
2190 C C   . VAL A 293 ? 0.3792 0.4475 0.3034 0.0704  0.0012  -0.0370 328 VAL A C   
2191 O O   . VAL A 293 ? 0.3846 0.4192 0.2969 0.0679  0.0059  -0.0445 328 VAL A O   
2192 C CB  . VAL A 293 ? 0.2871 0.3527 0.2256 0.0684  -0.0009 -0.0229 328 VAL A CB  
2193 C CG1 . VAL A 293 ? 0.3088 0.3850 0.2396 0.0845  -0.0053 -0.0271 328 VAL A CG1 
2194 C CG2 . VAL A 293 ? 0.2130 0.2907 0.1699 0.0601  -0.0036 -0.0123 328 VAL A CG2 
2195 N N   . ASN A 294 ? 0.3747 0.4648 0.2923 0.0773  0.0010  -0.0404 329 ASN A N   
2196 C CA  . ASN A 294 ? 0.4619 0.5377 0.3589 0.0868  0.0038  -0.0539 329 ASN A CA  
2197 C C   . ASN A 294 ? 0.4094 0.4936 0.3053 0.1060  0.0047  -0.0613 329 ASN A C   
2198 O O   . ASN A 294 ? 0.4090 0.5295 0.3240 0.1077  0.0061  -0.0587 329 ASN A O   
2199 C CB  . ASN A 294 ? 0.4605 0.5518 0.3486 0.0797  0.0037  -0.0573 329 ASN A CB  
2200 C CG  . ASN A 294 ? 0.4879 0.5698 0.3818 0.0648  -0.0045 -0.0544 329 ASN A CG  
2201 O OD1 . ASN A 294 ? 0.4701 0.5278 0.3690 0.0610  -0.0038 -0.0603 329 ASN A OD1 
2202 N ND2 . ASN A 294 ? 0.4206 0.5198 0.3146 0.0555  -0.0130 -0.0463 329 ASN A ND2 
2203 N N   . ALA B 1   ? 0.5282 0.6055 0.4857 0.2459  -0.1418 -0.1643 36  ALA B N   
2204 C CA  . ALA B 1   ? 0.4365 0.4868 0.3605 0.2551  -0.1472 -0.1603 36  ALA B CA  
2205 C C   . ALA B 1   ? 0.4722 0.4885 0.3701 0.2516  -0.1476 -0.1476 36  ALA B C   
2206 O O   . ALA B 1   ? 0.5830 0.5754 0.4582 0.2547  -0.1496 -0.1419 36  ALA B O   
2207 C CB  . ALA B 1   ? 0.4687 0.5081 0.3672 0.2704  -0.1609 -0.1700 36  ALA B CB  
2208 N N   . ALA B 2   ? 0.4599 0.4743 0.3614 0.2450  -0.1460 -0.1433 37  ALA B N   
2209 C CA  . ALA B 2   ? 0.4348 0.4222 0.3186 0.2389  -0.1440 -0.1296 37  ALA B CA  
2210 C C   . ALA B 2   ? 0.4119 0.4078 0.3153 0.2292  -0.1330 -0.1236 37  ALA B C   
2211 O O   . ALA B 2   ? 0.4156 0.4427 0.3554 0.2210  -0.1236 -0.1268 37  ALA B O   
2212 C CB  . ALA B 2   ? 0.5103 0.5008 0.3981 0.2338  -0.1437 -0.1269 37  ALA B CB  
2213 N N   . PRO B 3   ? 0.4254 0.3936 0.3060 0.2293  -0.1337 -0.1149 38  PRO B N   
2214 C CA  . PRO B 3   ? 0.4411 0.4165 0.3378 0.2213  -0.1232 -0.1094 38  PRO B CA  
2215 C C   . PRO B 3   ? 0.3802 0.3631 0.2957 0.2067  -0.1144 -0.1021 38  PRO B C   
2216 O O   . PRO B 3   ? 0.3970 0.3661 0.2996 0.1995  -0.1168 -0.0960 38  PRO B O   
2217 C CB  . PRO B 3   ? 0.5761 0.5132 0.4378 0.2242  -0.1292 -0.1019 38  PRO B CB  
2218 C CG  . PRO B 3   ? 0.6535 0.5594 0.4838 0.2266  -0.1402 -0.0973 38  PRO B CG  
2219 C CD  . PRO B 3   ? 0.4994 0.4263 0.3384 0.2350  -0.1442 -0.1090 38  PRO B CD  
2220 N N   . GLN B 4   ? 0.3543 0.3610 0.2994 0.1972  -0.1022 -0.1013 39  GLN B N   
2221 C CA  . GLN B 4   ? 0.3338 0.3419 0.2912 0.1771  -0.0922 -0.0916 39  GLN B CA  
2222 C C   . GLN B 4   ? 0.3673 0.3407 0.2946 0.1690  -0.0921 -0.0789 39  GLN B C   
2223 O O   . GLN B 4   ? 0.4641 0.4219 0.3738 0.1766  -0.0951 -0.0780 39  GLN B O   
2224 C CB  . GLN B 4   ? 0.3181 0.3591 0.3147 0.1692  -0.0798 -0.0928 39  GLN B CB  
2225 C CG  . GLN B 4   ? 0.3078 0.3845 0.3405 0.1740  -0.0797 -0.1047 39  GLN B CG  
2226 C CD  . GLN B 4   ? 0.3562 0.4647 0.4304 0.1639  -0.0675 -0.1034 39  GLN B CD  
2227 O OE1 . GLN B 4   ? 0.4557 0.5629 0.5297 0.1578  -0.0587 -0.0948 39  GLN B OE1 
2228 N NE2 . GLN B 4   ? 0.2699 0.4046 0.3781 0.1594  -0.0667 -0.1102 39  GLN B NE2 
2229 N N   . VAL B 5   ? 0.3435 0.3053 0.2651 0.1546  -0.0896 -0.0701 40  VAL B N   
2230 C CA  . VAL B 5   ? 0.3906 0.3206 0.2865 0.1452  -0.0898 -0.0577 40  VAL B CA  
2231 C C   . VAL B 5   ? 0.4249 0.3624 0.3370 0.1329  -0.0787 -0.0524 40  VAL B C   
2232 O O   . VAL B 5   ? 0.3485 0.2673 0.2448 0.1332  -0.0794 -0.0477 40  VAL B O   
2233 C CB  . VAL B 5   ? 0.3725 0.2891 0.2545 0.1359  -0.0920 -0.0501 40  VAL B CB  
2234 C CG1 . VAL B 5   ? 0.4925 0.3769 0.3499 0.1255  -0.0928 -0.0368 40  VAL B CG1 
2235 C CG2 . VAL B 5   ? 0.4362 0.3474 0.3014 0.1497  -0.1030 -0.0550 40  VAL B CG2 
2236 N N   . ARG B 6   ? 0.3451 0.3098 0.2890 0.1227  -0.0694 -0.0535 41  ARG B N   
2237 C CA  . ARG B 6   ? 0.3780 0.3546 0.3420 0.1116  -0.0584 -0.0487 41  ARG B CA  
2238 C C   . ARG B 6   ? 0.3497 0.3005 0.2942 0.1005  -0.0567 -0.0377 41  ARG B C   
2239 O O   . ARG B 6   ? 0.3488 0.2977 0.2937 0.0986  -0.0520 -0.0341 41  ARG B O   
2240 C CB  . ARG B 6   ? 0.3789 0.3730 0.3554 0.1212  -0.0545 -0.0532 41  ARG B CB  
2241 C CG  . ARG B 6   ? 0.4123 0.4417 0.4229 0.1256  -0.0515 -0.0621 41  ARG B CG  
2242 C CD  . ARG B 6   ? 0.3924 0.4438 0.4205 0.1298  -0.0436 -0.0626 41  ARG B CD  
2243 N NE  . ARG B 6   ? 0.4534 0.5390 0.5147 0.1350  -0.0416 -0.0711 41  ARG B NE  
2244 C CZ  . ARG B 6   ? 0.4427 0.5578 0.5378 0.1293  -0.0313 -0.0688 41  ARG B CZ  
2245 N NH1 . ARG B 6   ? 0.3332 0.4479 0.4319 0.1190  -0.0217 -0.0581 41  ARG B NH1 
2246 N NH2 . ARG B 6   ? 0.3490 0.4948 0.4755 0.1341  -0.0308 -0.0769 41  ARG B NH2 
2247 N N   . THR B 7   ? 0.3207 0.2536 0.2493 0.0929  -0.0604 -0.0321 42  THR B N   
2248 C CA  . THR B 7   ? 0.3882 0.3023 0.3060 0.0791  -0.0576 -0.0217 42  THR B CA  
2249 C C   . THR B 7   ? 0.3506 0.2758 0.2821 0.0660  -0.0530 -0.0190 42  THR B C   
2250 O O   . THR B 7   ? 0.3927 0.3238 0.3229 0.0687  -0.0566 -0.0222 42  THR B O   
2251 C CB  . THR B 7   ? 0.4164 0.2949 0.2991 0.0820  -0.0673 -0.0157 42  THR B CB  
2252 O OG1 . THR B 7   ? 0.5244 0.3963 0.3940 0.0843  -0.0735 -0.0148 42  THR B OG1 
2253 C CG2 . THR B 7   ? 0.4391 0.3075 0.3089 0.0974  -0.0737 -0.0209 42  THR B CG2 
2254 N N   . SER B 8   ? 0.3633 0.2930 0.3079 0.0533  -0.0455 -0.0141 43  SER B N   
2255 C CA  . SER B 8   ? 0.3482 0.2874 0.3042 0.0417  -0.0421 -0.0123 43  SER B CA  
2256 C C   . SER B 8   ? 0.3567 0.2748 0.2857 0.0375  -0.0469 -0.0050 43  SER B C   
2257 O O   . SER B 8   ? 0.3608 0.2530 0.2650 0.0392  -0.0520 0.0011  43  SER B O   
2258 C CB  . SER B 8   ? 0.3050 0.2516 0.2796 0.0296  -0.0340 -0.0085 43  SER B CB  
2259 O OG  . SER B 8   ? 0.3023 0.2730 0.3064 0.0320  -0.0290 -0.0141 43  SER B OG  
2260 N N   . ALA B 9   ? 0.3606 0.2906 0.2950 0.0327  -0.0460 -0.0056 44  ALA B N   
2261 C CA  . ALA B 9   ? 0.3478 0.2622 0.2588 0.0268  -0.0485 0.0035  44  ALA B CA  
2262 C C   . ALA B 9   ? 0.3576 0.2568 0.2641 0.0135  -0.0450 0.0130  44  ALA B C   
2263 O O   . ALA B 9   ? 0.3136 0.2200 0.2379 0.0086  -0.0398 0.0112  44  ALA B O   
2264 C CB  . ALA B 9   ? 0.3505 0.2862 0.2703 0.0246  -0.0468 0.0002  44  ALA B CB  
2265 N N   . PRO B 10  ? 0.4072 0.2850 0.2907 0.0075  -0.0482 0.0235  45  PRO B N   
2266 C CA  . PRO B 10  ? 0.3679 0.2328 0.2499 -0.0057 -0.0456 0.0316  45  PRO B CA  
2267 C C   . PRO B 10  ? 0.3307 0.2194 0.2368 -0.0154 -0.0374 0.0289  45  PRO B C   
2268 O O   . PRO B 10  ? 0.3256 0.2357 0.2416 -0.0155 -0.0349 0.0250  45  PRO B O   
2269 C CB  . PRO B 10  ? 0.3996 0.2442 0.2574 -0.0115 -0.0500 0.0437  45  PRO B CB  
2270 C CG  . PRO B 10  ? 0.5233 0.3601 0.3639 0.0018  -0.0572 0.0424  45  PRO B CG  
2271 C CD  . PRO B 10  ? 0.4237 0.2886 0.2828 0.0120  -0.0545 0.0293  45  PRO B CD  
2272 N N   . GLY B 11  ? 0.3104 0.1962 0.2268 -0.0217 -0.0342 0.0295  46  GLY B N   
2273 C CA  . GLY B 11  ? 0.3575 0.2636 0.2977 -0.0296 -0.0275 0.0264  46  GLY B CA  
2274 C C   . GLY B 11  ? 0.3170 0.2227 0.2547 -0.0426 -0.0253 0.0332  46  GLY B C   
2275 O O   . GLY B 11  ? 0.3199 0.2178 0.2604 -0.0509 -0.0238 0.0369  46  GLY B O   
2276 N N   . TYR B 12  ? 0.3193 0.2345 0.2511 -0.0439 -0.0253 0.0350  47  TYR B N   
2277 C CA  . TYR B 12  ? 0.3482 0.2729 0.2828 -0.0554 -0.0216 0.0398  47  TYR B CA  
2278 C C   . TYR B 12  ? 0.3428 0.2950 0.2861 -0.0515 -0.0195 0.0333  47  TYR B C   
2279 O O   . TYR B 12  ? 0.3552 0.3120 0.2922 -0.0410 -0.0224 0.0293  47  TYR B O   
2280 C CB  . TYR B 12  ? 0.3309 0.2342 0.2427 -0.0632 -0.0241 0.0533  47  TYR B CB  
2281 C CG  . TYR B 12  ? 0.4313 0.3276 0.3215 -0.0575 -0.0279 0.0592  47  TYR B CG  
2282 C CD1 . TYR B 12  ? 0.3969 0.2699 0.2703 -0.0483 -0.0349 0.0605  47  TYR B CD1 
2283 C CD2 . TYR B 12  ? 0.4083 0.3219 0.2938 -0.0603 -0.0248 0.0635  47  TYR B CD2 
2284 C CE1 . TYR B 12  ? 0.3927 0.2579 0.2454 -0.0425 -0.0392 0.0665  47  TYR B CE1 
2285 C CE2 . TYR B 12  ? 0.4188 0.3263 0.2829 -0.0547 -0.0281 0.0703  47  TYR B CE2 
2286 C CZ  . TYR B 12  ? 0.4808 0.3630 0.3286 -0.0460 -0.0356 0.0720  47  TYR B CZ  
2287 O OH  . TYR B 12  ? 0.5167 0.3923 0.3426 -0.0401 -0.0395 0.0794  47  TYR B OH  
2288 N N   . TYR B 13  ? 0.2671 0.2381 0.2248 -0.0589 -0.0152 0.0312  48  TYR B N   
2289 C CA  . TYR B 13  ? 0.2625 0.2625 0.2309 -0.0544 -0.0139 0.0228  48  TYR B CA  
2290 C C   . TYR B 13  ? 0.2652 0.2783 0.2311 -0.0638 -0.0098 0.0282  48  TYR B C   
2291 O O   . TYR B 13  ? 0.2632 0.2771 0.2403 -0.0732 -0.0071 0.0294  48  TYR B O   
2292 C CB  . TYR B 13  ? 0.2447 0.2608 0.2423 -0.0508 -0.0139 0.0094  48  TYR B CB  
2293 C CG  . TYR B 13  ? 0.2479 0.2920 0.2588 -0.0438 -0.0151 -0.0022 48  TYR B CG  
2294 C CD1 . TYR B 13  ? 0.2210 0.2853 0.2402 -0.0484 -0.0127 -0.0052 48  TYR B CD1 
2295 C CD2 . TYR B 13  ? 0.2880 0.3401 0.3062 -0.0317 -0.0195 -0.0123 48  TYR B CD2 
2296 C CE1 . TYR B 13  ? 0.2603 0.3510 0.2916 -0.0402 -0.0151 -0.0179 48  TYR B CE1 
2297 C CE2 . TYR B 13  ? 0.2848 0.3626 0.3170 -0.0241 -0.0224 -0.0251 48  TYR B CE2 
2298 C CZ  . TYR B 13  ? 0.3081 0.4046 0.3462 -0.0279 -0.0205 -0.0282 48  TYR B CZ  
2299 O OH  . TYR B 13  ? 0.2996 0.4220 0.3514 -0.0185 -0.0247 -0.0427 48  TYR B OH  
2300 N N   . ARG B 14  ? 0.2840 0.3099 0.2360 -0.0604 -0.0092 0.0313  49  ARG B N   
2301 C CA  . ARG B 14  ? 0.2985 0.3375 0.2431 -0.0692 -0.0044 0.0399  49  ARG B CA  
2302 C C   . ARG B 14  ? 0.3415 0.4164 0.3023 -0.0645 -0.0023 0.0277  49  ARG B C   
2303 O O   . ARG B 14  ? 0.2783 0.3679 0.2437 -0.0518 -0.0056 0.0160  49  ARG B O   
2304 C CB  . ARG B 14  ? 0.3670 0.3985 0.2836 -0.0680 -0.0047 0.0533  49  ARG B CB  
2305 C CG  . ARG B 14  ? 0.4493 0.4847 0.3556 -0.0809 0.0005  0.0686  49  ARG B CG  
2306 C CD  . ARG B 14  ? 0.4553 0.4575 0.3535 -0.0927 -0.0013 0.0819  49  ARG B CD  
2307 N NE  . ARG B 14  ? 0.5556 0.5306 0.4312 -0.0875 -0.0070 0.0904  49  ARG B NE  
2308 C CZ  . ARG B 14  ? 0.5635 0.5044 0.4295 -0.0935 -0.0119 0.0997  49  ARG B CZ  
2309 N NH1 . ARG B 14  ? 0.4746 0.4042 0.3508 -0.1053 -0.0116 0.1024  49  ARG B NH1 
2310 N NH2 . ARG B 14  ? 0.5611 0.4784 0.4070 -0.0863 -0.0183 0.1052  49  ARG B NH2 
2311 N N   . MET B 15  ? 0.2935 0.3830 0.2630 -0.0740 0.0023  0.0295  50  MET B N   
2312 C CA  . MET B 15  ? 0.3147 0.4388 0.3004 -0.0691 0.0036  0.0166  50  MET B CA  
2313 C C   . MET B 15  ? 0.3206 0.4624 0.3027 -0.0790 0.0100  0.0251  50  MET B C   
2314 O O   . MET B 15  ? 0.3362 0.4647 0.3198 -0.0921 0.0125  0.0346  50  MET B O   
2315 C CB  . MET B 15  ? 0.3463 0.4727 0.3608 -0.0673 0.0002  0.0018  50  MET B CB  
2316 C CG  . MET B 15  ? 0.2611 0.4201 0.2952 -0.0582 -0.0022 -0.0156 50  MET B CG  
2317 S SD  . MET B 15  ? 0.2215 0.3800 0.2893 -0.0615 -0.0055 -0.0277 50  MET B SD  
2318 C CE  . MET B 15  ? 0.1733 0.3283 0.2396 -0.0776 0.0006  -0.0164 50  MET B CE  
2319 N N   . LEU B 16  ? 0.2658 0.4389 0.2430 -0.0723 0.0125  0.0218  51  LEU B N   
2320 C CA  . LEU B 16  ? 0.3495 0.5458 0.3262 -0.0810 0.0194  0.0287  51  LEU B CA  
2321 C C   . LEU B 16  ? 0.3470 0.5628 0.3511 -0.0810 0.0185  0.0132  51  LEU B C   
2322 O O   . LEU B 16  ? 0.3224 0.5453 0.3432 -0.0702 0.0126  -0.0045 51  LEU B O   
2323 C CB  . LEU B 16  ? 0.2842 0.5099 0.2437 -0.0729 0.0233  0.0319  51  LEU B CB  
2324 C CG  . LEU B 16  ? 0.4575 0.6651 0.3882 -0.0714 0.0235  0.0478  51  LEU B CG  
2325 C CD1 . LEU B 16  ? 0.4709 0.7113 0.3841 -0.0665 0.0295  0.0549  51  LEU B CD1 
2326 C CD2 . LEU B 16  ? 0.5493 0.7213 0.4708 -0.0877 0.0248  0.0673  51  LEU B CD2 
2327 N N   . LEU B 17  ? 0.2734 0.4958 0.2836 -0.0936 0.0234  0.0200  52  LEU B N   
2328 C CA  . LEU B 17  ? 0.2884 0.5326 0.3227 -0.0937 0.0229  0.0064  52  LEU B CA  
2329 C C   . LEU B 17  ? 0.3262 0.6006 0.3561 -0.1007 0.0310  0.0147  52  LEU B C   
2330 O O   . LEU B 17  ? 0.3067 0.5718 0.3356 -0.1158 0.0352  0.0281  52  LEU B O   
2331 C CB  . LEU B 17  ? 0.2936 0.5114 0.3431 -0.1025 0.0197  0.0056  52  LEU B CB  
2332 C CG  . LEU B 17  ? 0.2933 0.5292 0.3685 -0.1016 0.0173  -0.0092 52  LEU B CG  
2333 C CD1 . LEU B 17  ? 0.2727 0.5122 0.3649 -0.0877 0.0094  -0.0282 52  LEU B CD1 
2334 C CD2 . LEU B 17  ? 0.2029 0.4060 0.2813 -0.1091 0.0160  -0.0031 52  LEU B CD2 
2335 N N   . GLY B 18  ? 0.3534 0.6651 0.3809 -0.0896 0.0330  0.0067  53  GLY B N   
2336 C CA  . GLY B 18  ? 0.2169 0.5614 0.2383 -0.0955 0.0421  0.0162  53  GLY B CA  
2337 C C   . GLY B 18  ? 0.3468 0.6744 0.3445 -0.1074 0.0484  0.0419  53  GLY B C   
2338 O O   . GLY B 18  ? 0.3488 0.6624 0.3264 -0.1013 0.0470  0.0484  53  GLY B O   
2339 N N   . ASP B 19  ? 0.2873 0.6065 0.2872 -0.1213 0.0517  0.0550  54  ASP B N   
2340 C CA  . ASP B 19  ? 0.3539 0.6448 0.3356 -0.1301 0.0532  0.0769  54  ASP B CA  
2341 C C   . ASP B 19  ? 0.4015 0.6422 0.3824 -0.1381 0.0470  0.0829  54  ASP B C   
2342 O O   . ASP B 19  ? 0.4354 0.6487 0.4040 -0.1439 0.0462  0.0984  54  ASP B O   
2343 C CB  . ASP B 19  ? 0.3371 0.6407 0.3226 -0.1367 0.0576  0.0859  54  ASP B CB  
2344 C CG  . ASP B 19  ? 0.5055 0.8561 0.4858 -0.1278 0.0639  0.0840  54  ASP B CG  
2345 O OD1 . ASP B 19  ? 0.4902 0.8537 0.4551 -0.1171 0.0649  0.0833  54  ASP B OD1 
2346 O OD2 . ASP B 19  ? 0.4502 0.8248 0.4408 -0.1299 0.0672  0.0827  54  ASP B OD2 
2347 N N   . PHE B 20  ? 0.2756 0.5032 0.2703 -0.1369 0.0419  0.0700  55  PHE B N   
2348 C CA  . PHE B 20  ? 0.3313 0.5124 0.3237 -0.1409 0.0354  0.0738  55  PHE B CA  
2349 C C   . PHE B 20  ? 0.3730 0.5413 0.3521 -0.1367 0.0332  0.0750  55  PHE B C   
2350 O O   . PHE B 20  ? 0.3212 0.5085 0.3006 -0.1230 0.0324  0.0630  55  PHE B O   
2351 C CB  . PHE B 20  ? 0.2966 0.4658 0.3090 -0.1397 0.0305  0.0603  55  PHE B CB  
2352 C CG  . PHE B 20  ? 0.3252 0.5034 0.3498 -0.1425 0.0319  0.0581  55  PHE B CG  
2353 C CD1 . PHE B 20  ? 0.3021 0.4921 0.3214 -0.1485 0.0366  0.0696  55  PHE B CD1 
2354 C CD2 . PHE B 20  ? 0.2087 0.3819 0.2502 -0.1386 0.0282  0.0453  55  PHE B CD2 
2355 C CE1 . PHE B 20  ? 0.3248 0.5250 0.3568 -0.1516 0.0380  0.0673  55  PHE B CE1 
2356 C CE2 . PHE B 20  ? 0.2351 0.4165 0.2874 -0.1407 0.0293  0.0433  55  PHE B CE2 
2357 C CZ  . PHE B 20  ? 0.2275 0.4233 0.2755 -0.1478 0.0343  0.0540  55  PHE B CZ  
2358 N N   . GLU B 21  ? 0.2749 0.4012 0.2437 -0.1389 0.0278  0.0829  56  GLU B N   
2359 C CA  . GLU B 21  ? 0.3167 0.4215 0.2744 -0.1319 0.0231  0.0814  56  GLU B CA  
2360 C C   . GLU B 21  ? 0.3474 0.4269 0.3178 -0.1318 0.0173  0.0726  56  GLU B C   
2361 O O   . GLU B 21  ? 0.3502 0.4061 0.3238 -0.1343 0.0142  0.0746  56  GLU B O   
2362 C CB  . GLU B 21  ? 0.4045 0.4841 0.3377 -0.1345 0.0215  0.0988  56  GLU B CB  
2363 C CG  . GLU B 21  ? 0.4243 0.4752 0.3454 -0.1251 0.0147  0.0964  56  GLU B CG  
2364 C CD  . GLU B 21  ? 0.5920 0.6066 0.4965 -0.1288 0.0101  0.1105  56  GLU B CD  
2365 O OE1 . GLU B 21  ? 0.4816 0.4724 0.3953 -0.1305 0.0058  0.1078  56  GLU B OE1 
2366 O OE2 . GLU B 21  ? 0.6169 0.6285 0.5018 -0.1252 0.0100  0.1206  56  GLU B OE2 
2367 N N   . ILE B 22  ? 0.3217 0.4032 0.3006 -0.1192 0.0139  0.0578  57  ILE B N   
2368 C CA  . ILE B 22  ? 0.2987 0.3600 0.2895 -0.1175 0.0093  0.0500  57  ILE B CA  
2369 C C   . ILE B 22  ? 0.2985 0.3351 0.2752 -0.1093 0.0049  0.0517  57  ILE B C   
2370 O O   . ILE B 22  ? 0.3552 0.3996 0.3221 -0.1000 0.0043  0.0502  57  ILE B O   
2371 C CB  . ILE B 22  ? 0.2692 0.3520 0.2838 -0.1102 0.0085  0.0327  57  ILE B CB  
2372 C CG1 . ILE B 22  ? 0.2074 0.3221 0.2331 -0.1141 0.0126  0.0290  57  ILE B CG1 
2373 C CG2 . ILE B 22  ? 0.2737 0.3373 0.3015 -0.1111 0.0052  0.0279  57  ILE B CG2 
2374 C CD1 . ILE B 22  ? 0.2246 0.3312 0.2534 -0.1244 0.0143  0.0358  57  ILE B CD1 
2375 N N   . THR B 23  ? 0.2576 0.2656 0.2324 -0.1120 0.0014  0.0546  58  THR B N   
2376 C CA  . THR B 23  ? 0.2827 0.2686 0.2469 -0.1032 -0.0032 0.0541  58  THR B CA  
2377 C C   . THR B 23  ? 0.3126 0.2891 0.2914 -0.1009 -0.0050 0.0463  58  THR B C   
2378 O O   . THR B 23  ? 0.2889 0.2496 0.2677 -0.1047 -0.0061 0.0492  58  THR B O   
2379 C CB  . THR B 23  ? 0.2928 0.2499 0.2337 -0.1075 -0.0066 0.0681  58  THR B CB  
2380 O OG1 . THR B 23  ? 0.3000 0.2664 0.2283 -0.1124 -0.0039 0.0786  58  THR B OG1 
2381 C CG2 . THR B 23  ? 0.3538 0.2941 0.2834 -0.0951 -0.0115 0.0653  58  THR B CG2 
2382 N N   . ALA B 24  ? 0.2675 0.2561 0.2601 -0.0912 -0.0054 0.0351  59  ALA B N   
2383 C CA  . ALA B 24  ? 0.1861 0.1644 0.1898 -0.0878 -0.0069 0.0304  59  ALA B CA  
2384 C C   . ALA B 24  ? 0.2777 0.2294 0.2624 -0.0836 -0.0103 0.0363  59  ALA B C   
2385 O O   . ALA B 24  ? 0.2283 0.1767 0.1998 -0.0767 -0.0124 0.0374  59  ALA B O   
2386 C CB  . ALA B 24  ? 0.1688 0.1660 0.1926 -0.0789 -0.0070 0.0184  59  ALA B CB  
2387 N N   . LEU B 25  ? 0.2680 0.2016 0.2510 -0.0861 -0.0116 0.0391  60  LEU B N   
2388 C CA  . LEU B 25  ? 0.3260 0.2343 0.2912 -0.0811 -0.0160 0.0432  60  LEU B CA  
2389 C C   . LEU B 25  ? 0.2614 0.1693 0.2367 -0.0735 -0.0154 0.0376  60  LEU B C   
2390 O O   . LEU B 25  ? 0.2206 0.1328 0.2076 -0.0744 -0.0128 0.0354  60  LEU B O   
2391 C CB  . LEU B 25  ? 0.2822 0.1771 0.2375 -0.0826 -0.0179 0.0477  60  LEU B CB  
2392 C CG  . LEU B 25  ? 0.2806 0.1760 0.2273 -0.0891 -0.0182 0.0545  60  LEU B CG  
2393 C CD1 . LEU B 25  ? 0.3266 0.2146 0.2729 -0.0896 -0.0199 0.0556  60  LEU B CD1 
2394 C CD2 . LEU B 25  ? 0.3628 0.2423 0.2880 -0.0887 -0.0226 0.0622  60  LEU B CD2 
2395 N N   . SER B 26  ? 0.2300 0.1371 0.2017 -0.0627 -0.0168 0.0343  61  SER B N   
2396 C CA  . SER B 26  ? 0.2037 0.1145 0.1863 -0.0555 -0.0151 0.0301  61  SER B CA  
2397 C C   . SER B 26  ? 0.2449 0.1338 0.2117 -0.0523 -0.0182 0.0336  61  SER B C   
2398 O O   . SER B 26  ? 0.2881 0.1577 0.2340 -0.0488 -0.0238 0.0365  61  SER B O   
2399 C CB  . SER B 26  ? 0.2621 0.1840 0.2498 -0.0449 -0.0153 0.0243  61  SER B CB  
2400 O OG  . SER B 26  ? 0.2350 0.1618 0.2340 -0.0388 -0.0129 0.0219  61  SER B OG  
2401 N N   . ASP B 27  ? 0.2338 0.1253 0.2103 -0.0524 -0.0154 0.0332  62  ASP B N   
2402 C CA  . ASP B 27  ? 0.2799 0.1553 0.2428 -0.0460 -0.0181 0.0346  62  ASP B CA  
2403 C C   . ASP B 27  ? 0.2816 0.1653 0.2473 -0.0335 -0.0161 0.0312  62  ASP B C   
2404 O O   . ASP B 27  ? 0.3072 0.1810 0.2609 -0.0254 -0.0181 0.0312  62  ASP B O   
2405 C CB  . ASP B 27  ? 0.2307 0.1055 0.2000 -0.0515 -0.0161 0.0365  62  ASP B CB  
2406 C CG  . ASP B 27  ? 0.2722 0.1269 0.2228 -0.0457 -0.0213 0.0375  62  ASP B CG  
2407 O OD1 . ASP B 27  ? 0.3463 0.1840 0.2804 -0.0451 -0.0280 0.0378  62  ASP B OD1 
2408 O OD2 . ASP B 27  ? 0.2734 0.1332 0.2276 -0.0405 -0.0184 0.0373  62  ASP B OD2 
2409 N N   . GLY B 28  ? 0.2080 0.1108 0.1899 -0.0312 -0.0126 0.0277  63  GLY B N   
2410 C CA  . GLY B 28  ? 0.2521 0.1682 0.2431 -0.0211 -0.0097 0.0246  63  GLY B CA  
2411 C C   . GLY B 28  ? 0.2378 0.1758 0.2575 -0.0252 -0.0027 0.0247  63  GLY B C   
2412 O O   . GLY B 28  ? 0.2237 0.1675 0.2570 -0.0347 -0.0012 0.0252  63  GLY B O   
2413 N N   . THR B 29  ? 0.2134 0.1640 0.2432 -0.0178 0.0014  0.0246  64  THR B N   
2414 C CA  . THR B 29  ? 0.1889 0.1585 0.2466 -0.0220 0.0078  0.0270  64  THR B CA  
2415 C C   . THR B 29  ? 0.2259 0.1984 0.2803 -0.0159 0.0126  0.0324  64  THR B C   
2416 O O   . THR B 29  ? 0.2822 0.2463 0.3155 -0.0061 0.0107  0.0316  64  THR B O   
2417 C CB  . THR B 29  ? 0.2494 0.2399 0.3327 -0.0205 0.0091  0.0221  64  THR B CB  
2418 O OG1 . THR B 29  ? 0.2345 0.2312 0.3137 -0.0093 0.0100  0.0204  64  THR B OG1 
2419 C CG2 . THR B 29  ? 0.2444 0.2340 0.3278 -0.0233 0.0037  0.0154  64  THR B CG2 
2420 N N   . VAL B 30  ? 0.1940 0.1791 0.2693 -0.0211 0.0185  0.0379  65  VAL B N   
2421 C CA  . VAL B 30  ? 0.2108 0.2033 0.2850 -0.0153 0.0247  0.0449  65  VAL B CA  
2422 C C   . VAL B 30  ? 0.1738 0.1882 0.2818 -0.0205 0.0316  0.0506  65  VAL B C   
2423 O O   . VAL B 30  ? 0.1380 0.1548 0.2662 -0.0304 0.0304  0.0502  65  VAL B O   
2424 C CB  . VAL B 30  ? 0.2884 0.2641 0.3420 -0.0162 0.0232  0.0488  65  VAL B CB  
2425 C CG1 . VAL B 30  ? 0.2317 0.2042 0.2983 -0.0285 0.0225  0.0510  65  VAL B CG1 
2426 C CG2 . VAL B 30  ? 0.3091 0.2933 0.3578 -0.0082 0.0292  0.0557  65  VAL B CG2 
2427 N N   . ASP B 31  ? 0.1521 0.1835 0.2675 -0.0138 0.0384  0.0559  66  ASP B N   
2428 C CA  . ASP B 31  ? 0.1570 0.2097 0.3071 -0.0198 0.0451  0.0633  66  ASP B CA  
2429 C C   . ASP B 31  ? 0.2516 0.3027 0.4044 -0.0250 0.0495  0.0746  66  ASP B C   
2430 O O   . ASP B 31  ? 0.2880 0.3372 0.4201 -0.0177 0.0533  0.0804  66  ASP B O   
2431 C CB  . ASP B 31  ? 0.1733 0.2488 0.3339 -0.0116 0.0517  0.0661  66  ASP B CB  
2432 C CG  . ASP B 31  ? 0.2060 0.2884 0.3745 -0.0076 0.0474  0.0553  66  ASP B CG  
2433 O OD1 . ASP B 31  ? 0.2467 0.3197 0.4186 -0.0125 0.0401  0.0468  66  ASP B OD1 
2434 O OD2 . ASP B 31  ? 0.3383 0.4370 0.5085 0.0016  0.0512  0.0548  66  ASP B OD2 
2435 N N   . LEU B 32  ? 0.1564 0.2069 0.3296 -0.0350 0.0470  0.0754  67  LEU B N   
2436 C CA  . LEU B 32  ? 0.1747 0.2177 0.3390 -0.0367 0.0460  0.0801  67  LEU B CA  
2437 C C   . LEU B 32  ? 0.1972 0.2514 0.3789 -0.0381 0.0472  0.0842  67  LEU B C   
2438 O O   . LEU B 32  ? 0.2072 0.2652 0.4048 -0.0406 0.0428  0.0776  67  LEU B O   
2439 C CB  . LEU B 32  ? 0.1514 0.1773 0.3046 -0.0413 0.0367  0.0705  67  LEU B CB  
2440 C CG  . LEU B 32  ? 0.2237 0.2345 0.3573 -0.0416 0.0338  0.0663  67  LEU B CG  
2441 C CD1 . LEU B 32  ? 0.2488 0.2490 0.3728 -0.0457 0.0258  0.0565  67  LEU B CD1 
2442 C CD2 . LEU B 32  ? 0.2922 0.2952 0.4068 -0.0370 0.0389  0.0763  67  LEU B CD2 
2443 N N   . PRO B 33  ? 0.2903 0.2703 0.3086 0.0250  0.0646  0.0520  68  PRO B N   
2444 C CA  . PRO B 33  ? 0.2788 0.2852 0.3310 0.0199  0.0582  0.0717  68  PRO B CA  
2445 C C   . PRO B 33  ? 0.2904 0.2855 0.3457 0.0057  0.0468  0.0629  68  PRO B C   
2446 O O   . PRO B 33  ? 0.2669 0.2687 0.3203 0.0051  0.0498  0.0624  68  PRO B O   
2447 C CB  . PRO B 33  ? 0.3325 0.3623 0.3815 0.0338  0.0741  0.0820  68  PRO B CB  
2448 C CG  . PRO B 33  ? 0.2956 0.3031 0.3045 0.0396  0.0833  0.0594  68  PRO B CG  
2449 C CD  . PRO B 33  ? 0.3014 0.2809 0.2941 0.0372  0.0800  0.0444  68  PRO B CD  
2450 N N   . VAL B 34  ? 0.2687 0.2448 0.3266 -0.0051 0.0333  0.0551  69  VAL B N   
2451 C CA  . VAL B 34  ? 0.2646 0.2239 0.3201 -0.0168 0.0233  0.0425  69  VAL B CA  
2452 C C   . VAL B 34  ? 0.2674 0.2442 0.3528 -0.0230 0.0151  0.0575  69  VAL B C   
2453 O O   . VAL B 34  ? 0.2530 0.2238 0.3362 -0.0279 0.0124  0.0499  69  VAL B O   
2454 C CB  . VAL B 34  ? 0.3225 0.2581 0.3717 -0.0244 0.0115  0.0322  69  VAL B CB  
2455 C CG1 . VAL B 34  ? 0.4531 0.3769 0.5106 -0.0357 -0.0019 0.0260  69  VAL B CG1 
2456 C CG2 . VAL B 34  ? 0.3026 0.2150 0.3161 -0.0204 0.0211  0.0130  69  VAL B CG2 
2457 N N   . ASP B 35  ? 0.2541 0.2533 0.3700 -0.0228 0.0109  0.0801  70  ASP B N   
2458 C CA  . ASP B 35  ? 0.2634 0.2807 0.4109 -0.0289 0.0038  0.0981  70  ASP B CA  
2459 C C   . ASP B 35  ? 0.3243 0.3578 0.4656 -0.0217 0.0168  0.1031  70  ASP B C   
2460 O O   . ASP B 35  ? 0.3121 0.3501 0.4679 -0.0276 0.0110  0.1096  70  ASP B O   
2461 C CB  . ASP B 35  ? 0.2480 0.2888 0.4313 -0.0300 -0.0019 0.1231  70  ASP B CB  
2462 C CG  . ASP B 35  ? 0.3156 0.3806 0.4973 -0.0152 0.0154  0.1354  70  ASP B CG  
2463 O OD1 . ASP B 35  ? 0.2733 0.3262 0.4214 -0.0052 0.0276  0.1195  70  ASP B OD1 
2464 O OD2 . ASP B 35  ? 0.3585 0.4532 0.5735 -0.0136 0.0164  0.1608  70  ASP B OD2 
2465 N N   . LYS B 36  ? 0.2560 0.2965 0.3740 -0.0085 0.0337  0.0998  71  LYS B N   
2466 C CA  . LYS B 36  ? 0.3012 0.3535 0.4061 -0.0010 0.0450  0.1013  71  LYS B CA  
2467 C C   . LYS B 36  ? 0.3378 0.3675 0.4167 -0.0045 0.0434  0.0777  71  LYS B C   
2468 O O   . LYS B 36  ? 0.3600 0.3977 0.4324 -0.0017 0.0471  0.0789  71  LYS B O   
2469 C CB  . LYS B 36  ? 0.3364 0.4021 0.4229 0.0156  0.0630  0.1048  71  LYS B CB  
2470 C CG  . LYS B 36  ? 0.3831 0.4763 0.4968 0.0220  0.0678  0.1299  71  LYS B CG  
2471 C CD  . LYS B 36  ? 0.4058 0.5277 0.5512 0.0192  0.0668  0.1561  71  LYS B CD  
2472 C CE  . LYS B 36  ? 0.4672 0.6200 0.6443 0.0248  0.0723  0.1829  71  LYS B CE  
2473 N NZ  . LYS B 36  ? 0.3755 0.5570 0.5877 0.0202  0.0710  0.2112  71  LYS B NZ  
2474 N N   . ARG B 37  ? 0.2966 0.2998 0.3602 -0.0100 0.0384  0.0571  72  ARG B N   
2475 C CA  . ARG B 37  ? 0.3208 0.3060 0.3619 -0.0126 0.0388  0.0358  72  ARG B CA  
2476 C C   . ARG B 37  ? 0.2798 0.2529 0.3337 -0.0241 0.0257  0.0295  72  ARG B C   
2477 O O   . ARG B 37  ? 0.2891 0.2576 0.3345 -0.0255 0.0257  0.0190  72  ARG B O   
2478 C CB  . ARG B 37  ? 0.4177 0.3817 0.4305 -0.0101 0.0450  0.0163  72  ARG B CB  
2479 C CG  . ARG B 37  ? 0.5840 0.5591 0.5804 0.0028  0.0583  0.0197  72  ARG B CG  
2480 C CD  . ARG B 37  ? 0.6265 0.5835 0.5914 0.0077  0.0665  0.0011  72  ARG B CD  
2481 N NE  . ARG B 37  ? 0.7702 0.7352 0.7222 0.0125  0.0709  -0.0021 72  ARG B NE  
2482 C CZ  . ARG B 37  ? 0.8142 0.8011 0.7669 0.0226  0.0773  0.0123  72  ARG B CZ  
2483 N NH1 . ARG B 37  ? 0.6761 0.6812 0.6433 0.0301  0.0825  0.0314  72  ARG B NH1 
2484 N NH2 . ARG B 37  ? 0.8065 0.7985 0.7457 0.0256  0.0786  0.0082  72  ARG B NH2 
2485 N N   . LEU B 38  ? 0.2838 0.2520 0.3582 -0.0315 0.0140  0.0359  73  LEU B N   
2486 C CA  . LEU B 38  ? 0.2452 0.2008 0.3319 -0.0408 0.0010  0.0305  73  LEU B CA  
2487 C C   . LEU B 38  ? 0.2419 0.2141 0.3494 -0.0416 -0.0023 0.0456  73  LEU B C   
2488 O O   . LEU B 38  ? 0.2836 0.2786 0.4067 -0.0382 0.0009  0.0668  73  LEU B O   
2489 C CB  . LEU B 38  ? 0.2487 0.1926 0.3500 -0.0482 -0.0126 0.0332  73  LEU B CB  
2490 C CG  . LEU B 38  ? 0.3118 0.2341 0.3874 -0.0479 -0.0103 0.0150  73  LEU B CG  
2491 C CD1 . LEU B 38  ? 0.2913 0.2065 0.3778 -0.0527 -0.0226 0.0207  73  LEU B CD1 
2492 C CD2 . LEU B 38  ? 0.3852 0.2861 0.4423 -0.0507 -0.0099 -0.0072 73  LEU B CD2 
2493 N N   . ASN B 39  ? 0.2429 0.2041 0.3514 -0.0456 -0.0085 0.0357  74  ASN B N   
2494 C CA  . ASN B 39  ? 0.2407 0.2144 0.3677 -0.0463 -0.0128 0.0490  74  ASN B CA  
2495 C C   . ASN B 39  ? 0.2714 0.2397 0.4291 -0.0549 -0.0286 0.0612  74  ASN B C   
2496 O O   . ASN B 39  ? 0.2790 0.2335 0.4458 -0.0593 -0.0386 0.0556  74  ASN B O   
2497 C CB  . ASN B 39  ? 0.2406 0.2059 0.3551 -0.0452 -0.0120 0.0325  74  ASN B CB  
2498 C CG  . ASN B 39  ? 0.4041 0.3792 0.4929 -0.0373 0.0012  0.0252  74  ASN B CG  
2499 O OD1 . ASN B 39  ? 0.3382 0.3290 0.4196 -0.0309 0.0101  0.0358  74  ASN B OD1 
2500 N ND2 . ASN B 39  ? 0.3699 0.3349 0.4453 -0.0377 0.0022  0.0063  74  ASN B ND2 
2501 N N   . GLN B 40  ? 0.2440 0.2223 0.4187 -0.0572 -0.0314 0.0779  75  GLN B N   
2502 C CA  . GLN B 40  ? 0.2610 0.2370 0.4686 -0.0665 -0.0475 0.0932  75  GLN B CA  
2503 C C   . GLN B 40  ? 0.2467 0.2486 0.4748 -0.0659 -0.0441 0.1181  75  GLN B C   
2504 O O   . GLN B 40  ? 0.2428 0.2588 0.4555 -0.0574 -0.0298 0.1189  75  GLN B O   
2505 C CB  . GLN B 40  ? 0.2569 0.2028 0.4608 -0.0736 -0.0617 0.0755  75  GLN B CB  
2506 C CG  . GLN B 40  ? 0.2583 0.2025 0.4556 -0.0740 -0.0618 0.0738  75  GLN B CG  
2507 C CD  . GLN B 40  ? 0.2708 0.1847 0.4608 -0.0803 -0.0768 0.0570  75  GLN B CD  
2508 O OE1 . GLN B 40  ? 0.2805 0.1759 0.4702 -0.0830 -0.0868 0.0468  75  GLN B OE1 
2509 N NE2 . GLN B 40  ? 0.2737 0.1831 0.4502 -0.0793 -0.0760 0.0517  75  GLN B NE2 
2510 N N   . PRO B 41  ? 0.2506 0.2603 0.5151 -0.0743 -0.0564 0.1397  76  PRO B N   
2511 C CA  . PRO B 41  ? 0.2484 0.2882 0.5376 -0.0734 -0.0515 0.1666  76  PRO B CA  
2512 C C   . PRO B 41  ? 0.2468 0.2870 0.5272 -0.0708 -0.0490 0.1606  76  PRO B C   
2513 O O   . PRO B 41  ? 0.2515 0.2669 0.5240 -0.0763 -0.0611 0.1439  76  PRO B O   
2514 C CB  . PRO B 41  ? 0.2568 0.2967 0.5845 -0.0845 -0.0702 0.1840  76  PRO B CB  
2515 C CG  . PRO B 41  ? 0.2628 0.2813 0.5829 -0.0862 -0.0780 0.1716  76  PRO B CG  
2516 C CD  . PRO B 41  ? 0.2592 0.2515 0.5461 -0.0845 -0.0748 0.1421  76  PRO B CD  
2517 N N   . ALA B 42  ? 0.2428 0.3111 0.5236 -0.0611 -0.0330 0.1750  77  ALA B N   
2518 C CA  . ALA B 42  ? 0.2424 0.3127 0.5164 -0.0568 -0.0298 0.1712  77  ALA B CA  
2519 C C   . ALA B 42  ? 0.2468 0.3118 0.5505 -0.0687 -0.0501 0.1787  77  ALA B C   
2520 O O   . ALA B 42  ? 0.2500 0.2989 0.5381 -0.0684 -0.0549 0.1640  77  ALA B O   
2521 C CB  . ALA B 42  ? 0.2687 0.3726 0.5440 -0.0433 -0.0095 0.1888  77  ALA B CB  
2522 N N   . PRO B 43  ? 0.2814 0.3587 0.6272 -0.0794 -0.0631 0.2015  78  PRO B N   
2523 C CA  . PRO B 43  ? 0.2724 0.3399 0.6385 -0.0887 -0.0858 0.2025  78  PRO B CA  
2524 C C   . PRO B 43  ? 0.2868 0.3127 0.6287 -0.0948 -0.1030 0.1740  78  PRO B C   
2525 O O   . PRO B 43  ? 0.2808 0.2935 0.6218 -0.0987 -0.1180 0.1669  78  PRO B O   
2526 C CB  . PRO B 43  ? 0.2689 0.3542 0.6667 -0.0902 -0.0945 0.2240  78  PRO B CB  
2527 C CG  . PRO B 43  ? 0.2600 0.3765 0.6630 -0.0815 -0.0727 0.2427  78  PRO B CG  
2528 C CD  . PRO B 43  ? 0.2868 0.3897 0.6556 -0.0778 -0.0576 0.2251  78  PRO B CD  
2529 N N   . LYS B 44  ? 0.2710 0.2770 0.5916 -0.0941 -0.1008 0.1575  79  LYS B N   
2530 C CA  . LYS B 44  ? 0.2995 0.2684 0.5926 -0.0962 -0.1129 0.1292  79  LYS B CA  
2531 C C   . LYS B 44  ? 0.2808 0.2331 0.5449 -0.0946 -0.1068 0.1112  79  LYS B C   
2532 O O   . LYS B 44  ? 0.2944 0.2258 0.5431 -0.0962 -0.1190 0.0966  79  LYS B O   
2533 C CB  . LYS B 44  ? 0.2839 0.2402 0.5649 -0.0942 -0.1098 0.1183  79  LYS B CB  
2534 C CG  . LYS B 44  ? 0.3914 0.3175 0.6551 -0.0948 -0.1239 0.0968  79  LYS B CG  
2535 C CD  . LYS B 44  ? 0.3963 0.3140 0.6553 -0.0923 -0.1216 0.0900  79  LYS B CD  
2536 C CE  . LYS B 44  ? 0.4364 0.3263 0.6786 -0.0913 -0.1338 0.0700  79  LYS B CE  
2537 N NZ  . LYS B 44  ? 0.5597 0.4454 0.8131 -0.0905 -0.1387 0.0724  79  LYS B NZ  
2538 N N   . THR B 45  ? 0.2686 0.2338 0.5131 -0.0843 -0.0852 0.1088  80  THR B N   
2539 C CA  . THR B 45  ? 0.2696 0.2240 0.4800 -0.0770 -0.0762 0.0915  80  THR B CA  
2540 C C   . THR B 45  ? 0.2739 0.2373 0.4973 -0.0778 -0.0833 0.1025  80  THR B C   
2541 O O   . THR B 45  ? 0.2841 0.2269 0.4872 -0.0783 -0.0902 0.0883  80  THR B O   
2542 C CB  . THR B 45  ? 0.2590 0.2278 0.4485 -0.0649 -0.0525 0.0891  80  THR B CB  
2543 O OG1 . THR B 45  ? 0.2565 0.2151 0.4318 -0.0644 -0.0479 0.0764  80  THR B OG1 
2544 C CG2 . THR B 45  ? 0.2619 0.2202 0.4190 -0.0572 -0.0427 0.0742  80  THR B CG2 
2545 N N   . GLN B 46  ? 0.2676 0.2632 0.5254 -0.0773 -0.0814 0.1290  81  GLN B N   
2546 C CA  . GLN B 46  ? 0.3160 0.3265 0.5944 -0.0778 -0.0884 0.1435  81  GLN B CA  
2547 C C   . GLN B 46  ? 0.3070 0.2926 0.5904 -0.0898 -0.1150 0.1356  81  GLN B C   
2548 O O   . GLN B 46  ? 0.3171 0.2929 0.5866 -0.0881 -0.1210 0.1284  81  GLN B O   
2549 C CB  . GLN B 46  ? 0.3888 0.4385 0.7124 -0.0786 -0.0852 0.1756  81  GLN B CB  
2550 C CG  . GLN B 46  ? 0.4976 0.5685 0.8610 -0.0839 -0.0982 0.1977  81  GLN B CG  
2551 C CD  . GLN B 46  ? 0.6001 0.7148 1.0055 -0.0816 -0.0875 0.2307  81  GLN B CD  
2552 O OE1 . GLN B 46  ? 0.5841 0.7222 1.0271 -0.0848 -0.0960 0.2523  81  GLN B OE1 
2553 N NE2 . GLN B 46  ? 0.5546 0.6794 0.9515 -0.0753 -0.0698 0.2342  81  GLN B NE2 
2554 N N   . SER B 47  ? 0.3669 0.3399 0.6682 -0.1017 -0.1320 0.1365  82  SER B N   
2555 C CA  . SER B 47  ? 0.3580 0.3080 0.6521 -0.1060 -0.1555 0.1249  82  SER B CA  
2556 C C   . SER B 47  ? 0.3867 0.3002 0.6346 -0.1039 -0.1573 0.0950  82  SER B C   
2557 O O   . SER B 47  ? 0.3774 0.2762 0.6142 -0.1057 -0.1717 0.0879  82  SER B O   
2558 C CB  . SER B 47  ? 0.3376 0.2849 0.6450 -0.1081 -0.1660 0.1281  82  SER B CB  
2559 O OG  . SER B 47  ? 0.3444 0.2703 0.6248 -0.1050 -0.1605 0.1081  82  SER B OG  
2560 N N   . ALA B 48  ? 0.4052 0.3045 0.6250 -0.0993 -0.1428 0.0778  83  ALA B N   
2561 C CA  . ALA B 48  ? 0.3731 0.2415 0.5481 -0.0953 -0.1409 0.0506  83  ALA B CA  
2562 C C   . ALA B 48  ? 0.3453 0.2109 0.5042 -0.0925 -0.1365 0.0491  83  ALA B C   
2563 O O   . ALA B 48  ? 0.3661 0.2087 0.5020 -0.0936 -0.1476 0.0366  83  ALA B O   
2564 C CB  . ALA B 48  ? 0.3762 0.2363 0.5290 -0.0902 -0.1240 0.0355  83  ALA B CB  
2565 N N   . LEU B 49  ? 0.3184 0.2116 0.4838 -0.0842 -0.1176 0.0617  84  LEU B N   
2566 C CA  . LEU B 49  ? 0.3513 0.2489 0.5011 -0.0763 -0.1102 0.0624  84  LEU B CA  
2567 C C   . LEU B 49  ? 0.3362 0.2349 0.5044 -0.0821 -0.1322 0.0728  84  LEU B C   
2568 O O   . LEU B 49  ? 0.3722 0.2527 0.5153 -0.0803 -0.1384 0.0627  84  LEU B O   
2569 C CB  . LEU B 49  ? 0.3352 0.2644 0.4963 -0.0661 -0.0890 0.0776  84  LEU B CB  
2570 C CG  . LEU B 49  ? 0.3523 0.2800 0.4881 -0.0579 -0.0662 0.0660  84  LEU B CG  
2571 C CD1 . LEU B 49  ? 0.3802 0.3320 0.5169 -0.0454 -0.0471 0.0773  84  LEU B CD1 
2572 C CD2 . LEU B 49  ? 0.4146 0.3097 0.5088 -0.0574 -0.0632 0.0403  84  LEU B CD2 
2573 N N   . ALA B 50  ? 0.3501 0.2699 0.5629 -0.0900 -0.1456 0.0938  85  ALA B N   
2574 C CA  . ALA B 50  ? 0.3888 0.3134 0.6252 -0.0966 -0.1684 0.1058  85  ALA B CA  
2575 C C   . ALA B 50  ? 0.4321 0.3184 0.6458 -0.1051 -0.1927 0.0867  85  ALA B C   
2576 O O   . ALA B 50  ? 0.4424 0.3224 0.6516 -0.1063 -0.2082 0.0870  85  ALA B O   
2577 C CB  . ALA B 50  ? 0.3639 0.3197 0.6569 -0.1051 -0.1780 0.1333  85  ALA B CB  
2578 N N   . LYS B 51  ? 0.4268 0.2907 0.6219 -0.1067 -0.1939 0.0698  86  LYS B N   
2579 C CA  . LYS B 51  ? 0.5571 0.3895 0.7149 -0.1045 -0.2059 0.0482  86  LYS B CA  
2580 C C   . LYS B 51  ? 0.4534 0.2647 0.5711 -0.1004 -0.2018 0.0332  86  LYS B C   
2581 O O   . LYS B 51  ? 0.5543 0.3459 0.6481 -0.0997 -0.2161 0.0234  86  LYS B O   
2582 C CB  . LYS B 51  ? 0.5200 0.3374 0.6547 -0.0998 -0.1964 0.0304  86  LYS B CB  
2583 C CG  . LYS B 51  ? 0.5936 0.4208 0.7540 -0.1020 -0.1995 0.0384  86  LYS B CG  
2584 C CD  . LYS B 51  ? 0.6312 0.4552 0.8102 -0.1070 -0.2232 0.0466  86  LYS B CD  
2585 C CE  . LYS B 51  ? 0.7347 0.5630 0.9316 -0.1076 -0.2224 0.0508  86  LYS B CE  
2586 N NZ  . LYS B 51  ? 0.7107 0.5707 0.9433 -0.1098 -0.2116 0.0728  86  LYS B NZ  
2587 N N   . SER B 52  ? 0.4784 0.2925 0.5820 -0.0948 -0.1795 0.0300  87  SER B N   
2588 C CA  . SER B 52  ? 0.5303 0.3288 0.5916 -0.0864 -0.1693 0.0171  87  SER B CA  
2589 C C   . SER B 52  ? 0.4063 0.2268 0.4782 -0.0801 -0.1653 0.0336  87  SER B C   
2590 O O   . SER B 52  ? 0.5001 0.3132 0.5416 -0.0714 -0.1512 0.0269  87  SER B O   
2591 C CB  . SER B 52  ? 0.5466 0.3379 0.5798 -0.0794 -0.1433 0.0024  87  SER B CB  
2592 O OG  . SER B 52  ? 0.6513 0.4200 0.6606 -0.0802 -0.1448 -0.0168 87  SER B OG  
2593 N N   . PHE B 53  ? 0.3792 0.3392 0.6707 -0.0513 -0.0697 0.0564  88  PHE B N   
2594 C CA  . PHE B 53  ? 0.3406 0.3254 0.6571 -0.0547 -0.0631 0.0473  88  PHE B CA  
2595 C C   . PHE B 53  ? 0.3793 0.3857 0.6904 -0.0560 -0.0478 0.0461  88  PHE B C   
2596 O O   . PHE B 53  ? 0.4265 0.4447 0.7405 -0.0468 -0.0447 0.0332  88  PHE B O   
2597 C CB  . PHE B 53  ? 0.3410 0.3164 0.6677 -0.0406 -0.0755 0.0319  88  PHE B CB  
2598 C CG  . PHE B 53  ? 0.3731 0.3310 0.7020 -0.0364 -0.0907 0.0315  88  PHE B CG  
2599 C CD1 . PHE B 53  ? 0.3236 0.2609 0.6289 -0.0250 -0.1011 0.0319  88  PHE B CD1 
2600 C CD2 . PHE B 53  ? 0.2785 0.2471 0.6315 -0.0441 -0.0937 0.0294  88  PHE B CD2 
2601 C CE1 . PHE B 53  ? 0.3054 0.2333 0.6130 -0.0215 -0.1151 0.0297  88  PHE B CE1 
2602 C CE2 . PHE B 53  ? 0.3078 0.2608 0.6641 -0.0408 -0.1082 0.0286  88  PHE B CE2 
2603 C CZ  . PHE B 53  ? 0.3037 0.2361 0.6381 -0.0289 -0.1196 0.0289  88  PHE B CZ  
2604 N N   . GLN B 54  ? 0.2759 0.2874 0.5729 -0.0650 -0.0380 0.0590  89  GLN B N   
2605 C CA  . GLN B 54  ? 0.3011 0.3344 0.5860 -0.0656 -0.0225 0.0589  89  GLN B CA  
2606 C C   . GLN B 54  ? 0.2217 0.2779 0.5162 -0.0830 -0.0111 0.0714  89  GLN B C   
2607 O O   . GLN B 54  ? 0.3116 0.3574 0.6058 -0.0917 -0.0155 0.0810  89  GLN B O   
2608 C CB  . GLN B 54  ? 0.3581 0.3753 0.6119 -0.0579 -0.0219 0.0618  89  GLN B CB  
2609 C CG  . GLN B 54  ? 0.3616 0.3531 0.6038 -0.0431 -0.0341 0.0535  89  GLN B CG  
2610 C CD  . GLN B 54  ? 0.4434 0.4218 0.6575 -0.0374 -0.0342 0.0576  89  GLN B CD  
2611 O OE1 . GLN B 54  ? 0.5034 0.4875 0.7063 -0.0439 -0.0279 0.0676  89  GLN B OE1 
2612 N NE2 . GLN B 54  ? 0.5292 0.4920 0.7318 -0.0250 -0.0412 0.0496  89  GLN B NE2 
2613 N N   . LYS B 55  ? 0.2392 0.3236 0.5312 -0.0848 0.0036  0.0695  90  LYS B N   
2614 C CA  . LYS B 55  ? 0.3617 0.4676 0.6551 -0.0999 0.0156  0.0817  90  LYS B CA  
2615 C C   . LYS B 55  ? 0.4203 0.5523 0.7036 -0.0977 0.0305  0.0795  90  LYS B C   
2616 O O   . LYS B 55  ? 0.4527 0.5818 0.7238 -0.0840 0.0301  0.0669  90  LYS B O   
2617 C CB  . LYS B 55  ? 0.5238 0.6480 0.8402 -0.1092 0.0166  0.0791  90  LYS B CB  
2618 C CG  . LYS B 55  ? 0.6145 0.7568 0.9261 -0.1255 0.0287  0.0909  90  LYS B CG  
2619 C CD  . LYS B 55  ? 0.7378 0.8992 1.0729 -0.1371 0.0299  0.0885  90  LYS B CD  
2620 C CE  . LYS B 55  ? 0.6982 0.8750 1.0254 -0.1538 0.0434  0.1008  90  LYS B CE  
2621 N NZ  . LYS B 55  ? 0.7560 0.9535 1.1056 -0.1681 0.0467  0.0994  90  LYS B NZ  
2622 N N   . ALA B 56  ? 0.5364 0.6878 0.8133 -0.1091 0.0426  0.0897  91  ALA B N   
2623 C CA  . ALA B 56  ? 0.2571 0.4414 0.5288 -0.1091 0.0582  0.0873  91  ALA B CA  
2624 C C   . ALA B 56  ? 0.2644 0.4360 0.5110 -0.0975 0.0577  0.0840  91  ALA B C   
2625 O O   . ALA B 56  ? 0.4117 0.5524 0.6431 -0.0945 0.0480  0.0890  91  ALA B O   
2626 C CB  . ALA B 56  ? 0.4702 0.6876 0.7681 -0.1054 0.0632  0.0725  91  ALA B CB  
2627 N N   . PRO B 57  ? 0.2648 0.4563 0.5014 -0.0899 0.0667  0.0745  92  PRO B N   
2628 C CA  . PRO B 57  ? 0.2558 0.4287 0.4687 -0.0773 0.0623  0.0660  92  PRO B CA  
2629 C C   . PRO B 57  ? 0.2531 0.3992 0.4705 -0.0681 0.0487  0.0561  92  PRO B C   
2630 O O   . PRO B 57  ? 0.2389 0.3894 0.4768 -0.0652 0.0448  0.0472  92  PRO B O   
2631 C CB  . PRO B 57  ? 0.2287 0.4278 0.4375 -0.0702 0.0719  0.0535  92  PRO B CB  
2632 C CG  . PRO B 57  ? 0.2561 0.4878 0.4727 -0.0812 0.0851  0.0634  92  PRO B CG  
2633 C CD  . PRO B 57  ? 0.3225 0.5525 0.5620 -0.0941 0.0821  0.0748  92  PRO B CD  
2634 N N   . LEU B 58  ? 0.1809 0.3010 0.3790 -0.0633 0.0414  0.0578  93  LEU B N   
2635 C CA  . LEU B 58  ? 0.1797 0.2733 0.3785 -0.0553 0.0288  0.0511  93  LEU B CA  
2636 C C   . LEU B 58  ? 0.1621 0.2482 0.3462 -0.0443 0.0277  0.0375  93  LEU B C   
2637 O O   . LEU B 58  ? 0.1634 0.2481 0.3270 -0.0433 0.0310  0.0381  93  LEU B O   
2638 C CB  . LEU B 58  ? 0.2200 0.2902 0.4075 -0.0571 0.0207  0.0623  93  LEU B CB  
2639 C CG  . LEU B 58  ? 0.2855 0.3290 0.4688 -0.0478 0.0082  0.0565  93  LEU B CG  
2640 C CD1 . LEU B 58  ? 0.2687 0.3085 0.4737 -0.0444 0.0014  0.0485  93  LEU B CD1 
2641 C CD2 . LEU B 58  ? 0.3933 0.4183 0.5659 -0.0488 0.0005  0.0678  93  LEU B CD2 
2642 N N   . GLU B 59  ? 0.1580 0.2364 0.3511 -0.0362 0.0216  0.0254  94  GLU B N   
2643 C CA  . GLU B 59  ? 0.1572 0.2220 0.3340 -0.0265 0.0190  0.0135  94  GLU B CA  
2644 C C   . GLU B 59  ? 0.2022 0.2425 0.3612 -0.0251 0.0125  0.0177  94  GLU B C   
2645 O O   . GLU B 59  ? 0.2257 0.2493 0.3892 -0.0226 0.0036  0.0200  94  GLU B O   
2646 C CB  . GLU B 59  ? 0.1783 0.2376 0.3667 -0.0172 0.0129  0.0003  94  GLU B CB  
2647 C CG  . GLU B 59  ? 0.1769 0.2129 0.3461 -0.0076 0.0076  -0.0100 94  GLU B CG  
2648 C CD  . GLU B 59  ? 0.3186 0.3506 0.4957 0.0035  0.0021  -0.0243 94  GLU B CD  
2649 O OE1 . GLU B 59  ? 0.2489 0.2929 0.4491 0.0048  -0.0004 -0.0264 94  GLU B OE1 
2650 O OE2 . GLU B 59  ? 0.1927 0.2083 0.3524 0.0111  -0.0006 -0.0338 94  GLU B OE2 
2651 N N   . THR B 60  ? 0.1576 0.1979 0.2970 -0.0263 0.0165  0.0181  95  THR B N   
2652 C CA  . THR B 60  ? 0.1564 0.1820 0.2802 -0.0265 0.0122  0.0231  95  THR B CA  
2653 C C   . THR B 60  ? 0.1591 0.1710 0.2665 -0.0223 0.0105  0.0135  95  THR B C   
2654 O O   . THR B 60  ? 0.1639 0.1821 0.2638 -0.0225 0.0154  0.0065  95  THR B O   
2655 C CB  . THR B 60  ? 0.1584 0.1973 0.2731 -0.0330 0.0179  0.0326  95  THR B CB  
2656 O OG1 . THR B 60  ? 0.1607 0.2104 0.2889 -0.0383 0.0202  0.0424  95  THR B OG1 
2657 C CG2 . THR B 60  ? 0.1573 0.1848 0.2584 -0.0320 0.0124  0.0375  95  THR B CG2 
2658 N N   . SER B 61  ? 0.1584 0.1510 0.2602 -0.0185 0.0031  0.0130  96  SER B N   
2659 C CA  . SER B 61  ? 0.1640 0.1422 0.2482 -0.0171 0.0018  0.0066  96  SER B CA  
2660 C C   . SER B 61  ? 0.1649 0.1526 0.2346 -0.0237 0.0066  0.0093  96  SER B C   
2661 O O   . SER B 61  ? 0.1604 0.1608 0.2309 -0.0269 0.0082  0.0174  96  SER B O   
2662 C CB  . SER B 61  ? 0.1717 0.1303 0.2520 -0.0121 -0.0062 0.0074  96  SER B CB  
2663 O OG  . SER B 61  ? 0.1644 0.1135 0.2576 -0.0049 -0.0123 0.0044  96  SER B OG  
2664 N N   . VAL B 62  ? 0.2326 0.2126 0.2880 -0.0256 0.0078  0.0020  97  VAL B N   
2665 C CA  . VAL B 62  ? 0.1760 0.1624 0.2174 -0.0325 0.0105  0.0027  97  VAL B CA  
2666 C C   . VAL B 62  ? 0.2092 0.1758 0.2375 -0.0340 0.0069  -0.0008 97  VAL B C   
2667 O O   . VAL B 62  ? 0.1955 0.1438 0.2181 -0.0317 0.0049  -0.0080 97  VAL B O   
2668 C CB  . VAL B 62  ? 0.1827 0.1800 0.2185 -0.0358 0.0158  -0.0032 97  VAL B CB  
2669 C CG1 . VAL B 62  ? 0.1968 0.2007 0.2187 -0.0435 0.0174  -0.0040 97  VAL B CG1 
2670 C CG2 . VAL B 62  ? 0.1772 0.1950 0.2247 -0.0344 0.0206  0.0009  97  VAL B CG2 
2671 N N   . THR B 63  ? 0.1811 0.1517 0.2039 -0.0374 0.0060  0.0042  98  THR B N   
2672 C CA  . THR B 63  ? 0.1893 0.1435 0.2008 -0.0391 0.0033  0.0032  98  THR B CA  
2673 C C   . THR B 63  ? 0.2116 0.1783 0.2131 -0.0487 0.0060  0.0043  98  THR B C   
2674 O O   . THR B 63  ? 0.2037 0.1928 0.2094 -0.0501 0.0076  0.0079  98  THR B O   
2675 C CB  . THR B 63  ? 0.1833 0.1309 0.2008 -0.0307 -0.0018 0.0079  98  THR B CB  
2676 O OG1 . THR B 63  ? 0.2373 0.1764 0.2669 -0.0227 -0.0049 0.0062  98  THR B OG1 
2677 C CG2 . THR B 63  ? 0.1940 0.1243 0.1983 -0.0310 -0.0042 0.0074  98  THR B CG2 
2678 N N   . GLY B 64  ? 0.2124 0.1643 0.2003 -0.0558 0.0061  0.0011  99  GLY B N   
2679 C CA  . GLY B 64  ? 0.2100 0.1738 0.1898 -0.0662 0.0084  0.0025  99  GLY B CA  
2680 C C   . GLY B 64  ? 0.2483 0.2006 0.2208 -0.0657 0.0069  0.0060  99  GLY B C   
2681 O O   . GLY B 64  ? 0.2523 0.1820 0.2225 -0.0581 0.0035  0.0060  99  GLY B O   
2682 N N   . TYR B 65  ? 0.2169 0.1865 0.1854 -0.0733 0.0094  0.0086  100 TYR B N   
2683 C CA  . TYR B 65  ? 0.2350 0.1978 0.1961 -0.0718 0.0089  0.0125  100 TYR B CA  
2684 C C   . TYR B 65  ? 0.3442 0.3077 0.2921 -0.0881 0.0132  0.0128  100 TYR B C   
2685 O O   . TYR B 65  ? 0.2489 0.2400 0.2000 -0.0975 0.0165  0.0123  100 TYR B O   
2686 C CB  . TYR B 65  ? 0.2074 0.1928 0.1776 -0.0612 0.0072  0.0165  100 TYR B CB  
2687 C CG  . TYR B 65  ? 0.1953 0.1735 0.1773 -0.0466 0.0019  0.0172  100 TYR B CG  
2688 C CD1 . TYR B 65  ? 0.2146 0.2063 0.2074 -0.0447 0.0017  0.0171  100 TYR B CD1 
2689 C CD2 . TYR B 65  ? 0.2310 0.1895 0.2128 -0.0357 -0.0029 0.0182  100 TYR B CD2 
2690 C CE1 . TYR B 65  ? 0.1911 0.1772 0.1949 -0.0342 -0.0024 0.0188  100 TYR B CE1 
2691 C CE2 . TYR B 65  ? 0.1890 0.1422 0.1839 -0.0241 -0.0083 0.0186  100 TYR B CE2 
2692 C CZ  . TYR B 65  ? 0.1987 0.1659 0.2047 -0.0246 -0.0075 0.0194  100 TYR B CZ  
2693 O OH  . TYR B 65  ? 0.1913 0.1545 0.2105 -0.0160 -0.0121 0.0212  100 TYR B OH  
2694 N N   . LEU B 66  ? 0.2613 0.1950 0.1941 -0.0916 0.0127  0.0139  101 LEU B N   
2695 C CA  . LEU B 66  ? 0.2835 0.2120 0.2013 -0.1090 0.0168  0.0159  101 LEU B CA  
2696 C C   . LEU B 66  ? 0.3410 0.2835 0.2546 -0.1078 0.0197  0.0220  101 LEU B C   
2697 O O   . LEU B 66  ? 0.3445 0.2732 0.2548 -0.0941 0.0167  0.0245  101 LEU B O   
2698 C CB  . LEU B 66  ? 0.3171 0.2011 0.2171 -0.1127 0.0138  0.0142  101 LEU B CB  
2699 C CG  . LEU B 66  ? 0.3548 0.2244 0.2367 -0.1334 0.0168  0.0162  101 LEU B CG  
2700 C CD1 . LEU B 66  ? 0.3406 0.2256 0.2282 -0.1477 0.0182  0.0108  101 LEU B CD1 
2701 C CD2 . LEU B 66  ? 0.5096 0.3285 0.3709 -0.1312 0.0116  0.0154  101 LEU B CD2 
2702 N N   . VAL B 67  ? 0.3433 0.3155 0.2577 -0.1214 0.0254  0.0237  102 VAL B N   
2703 C CA  . VAL B 67  ? 0.2907 0.2843 0.2017 -0.1217 0.0296  0.0288  102 VAL B CA  
2704 C C   . VAL B 67  ? 0.3653 0.3506 0.2599 -0.1444 0.0357  0.0328  102 VAL B C   
2705 O O   . VAL B 67  ? 0.3292 0.3274 0.2264 -0.1626 0.0387  0.0305  102 VAL B O   
2706 C CB  . VAL B 67  ? 0.2646 0.3075 0.1925 -0.1170 0.0311  0.0269  102 VAL B CB  
2707 C CG1 . VAL B 67  ? 0.3197 0.3877 0.2444 -0.1135 0.0349  0.0308  102 VAL B CG1 
2708 C CG2 . VAL B 67  ? 0.2493 0.2959 0.1921 -0.0971 0.0243  0.0237  102 VAL B CG2 
2709 N N   . ASN B 68  ? 0.3792 0.3421 0.2562 -0.1438 0.0371  0.0388  103 ASN B N   
2710 C CA  . ASN B 68  ? 0.4408 0.3966 0.3000 -0.1655 0.0437  0.0450  103 ASN B CA  
2711 C C   . ASN B 68  ? 0.4452 0.4398 0.3061 -0.1637 0.0504  0.0497  103 ASN B C   
2712 O O   . ASN B 68  ? 0.4316 0.4184 0.2847 -0.1473 0.0490  0.0529  103 ASN B O   
2713 C CB  . ASN B 68  ? 0.4823 0.3824 0.3165 -0.1658 0.0404  0.0490  103 ASN B CB  
2714 C CG  . ASN B 68  ? 0.5464 0.4350 0.3656 -0.1848 0.0437  0.0528  103 ASN B CG  
2715 O OD1 . ASN B 68  ? 0.4615 0.3861 0.2875 -0.1956 0.0501  0.0547  103 ASN B OD1 
2716 N ND2 . ASN B 68  ? 0.7096 0.5504 0.5107 -0.1852 0.0380  0.0525  103 ASN B ND2 
2717 N N   . THR B 69  ? 0.3534 0.4849 0.3808 -0.1749 -0.0019 0.0147  104 THR B N   
2718 C CA  . THR B 69  ? 0.3677 0.5236 0.3938 -0.1817 0.0071  0.0078  104 THR B CA  
2719 C C   . THR B 69  ? 0.3705 0.5414 0.3909 -0.1953 0.0076  0.0184  104 THR B C   
2720 O O   . THR B 69  ? 0.3796 0.5739 0.3983 -0.2022 0.0155  0.0133  104 THR B O   
2721 C CB  . THR B 69  ? 0.3095 0.4700 0.3539 -0.1761 0.0100  -0.0016 104 THR B CB  
2722 O OG1 . THR B 69  ? 0.3189 0.4788 0.3773 -0.1799 0.0054  0.0052  104 THR B OG1 
2723 C CG2 . THR B 69  ? 0.2978 0.4406 0.3490 -0.1631 0.0069  -0.0081 104 THR B CG2 
2724 N N   . GLY B 70  ? 0.4244 0.5837 0.4418 -0.1997 -0.0002 0.0329  105 GLY B N   
2725 C CA  . GLY B 70  ? 0.4010 0.5714 0.4148 -0.2132 -0.0004 0.0461  105 GLY B CA  
2726 C C   . GLY B 70  ? 0.4014 0.5667 0.4358 -0.2154 -0.0015 0.0499  105 GLY B C   
2727 O O   . GLY B 70  ? 0.5094 0.6757 0.5443 -0.2260 -0.0032 0.0636  105 GLY B O   
2728 N N   . SER B 71  ? 0.3780 0.5388 0.4303 -0.2065 -0.0008 0.0383  106 SER B N   
2729 C CA  . SER B 71  ? 0.3889 0.5456 0.4640 -0.2080 -0.0030 0.0384  106 SER B CA  
2730 C C   . SER B 71  ? 0.3977 0.5343 0.4865 -0.1956 -0.0104 0.0307  106 SER B C   
2731 O O   . SER B 71  ? 0.3563 0.4860 0.4635 -0.1973 -0.0147 0.0306  106 SER B O   
2732 C CB  . SER B 71  ? 0.4316 0.6137 0.5188 -0.2121 0.0052  0.0301  106 SER B CB  
2733 O OG  . SER B 71  ? 0.4800 0.6677 0.5693 -0.2013 0.0076  0.0156  106 SER B OG  
2734 N N   . LYS B 72  ? 0.4048 0.5331 0.4859 -0.1841 -0.0117 0.0236  107 LYS B N   
2735 C CA  . LYS B 72  ? 0.3833 0.4935 0.4739 -0.1726 -0.0188 0.0174  107 LYS B CA  
2736 C C   . LYS B 72  ? 0.3387 0.4334 0.4136 -0.1655 -0.0214 0.0198  107 LYS B C   
2737 O O   . LYS B 72  ? 0.3071 0.4082 0.3665 -0.1670 -0.0169 0.0212  107 LYS B O   
2738 C CB  . LYS B 72  ? 0.3177 0.4380 0.4207 -0.1651 -0.0175 0.0040  107 LYS B CB  
2739 C CG  . LYS B 72  ? 0.3767 0.5133 0.4999 -0.1709 -0.0172 0.0001  107 LYS B CG  
2740 C CD  . LYS B 72  ? 0.2646 0.3878 0.4044 -0.1720 -0.0260 0.0006  107 LYS B CD  
2741 C CE  . LYS B 72  ? 0.3456 0.4858 0.5102 -0.1768 -0.0274 -0.0061 107 LYS B CE  
2742 N NZ  . LYS B 72  ? 0.3845 0.5123 0.5675 -0.1776 -0.0363 -0.0104 107 LYS B NZ  
2743 N N   . LEU B 73  ? 0.3165 0.3923 0.3960 -0.1586 -0.0289 0.0195  108 LEU B N   
2744 C CA  . LEU B 73  ? 0.2391 0.3011 0.3074 -0.1508 -0.0315 0.0206  108 LEU B CA  
2745 C C   . LEU B 73  ? 0.2951 0.3510 0.3709 -0.1394 -0.0331 0.0095  108 LEU B C   
2746 O O   . LEU B 73  ? 0.2706 0.3184 0.3563 -0.1359 -0.0393 0.0055  108 LEU B O   
2747 C CB  . LEU B 73  ? 0.3145 0.3608 0.3789 -0.1530 -0.0392 0.0312  108 LEU B CB  
2748 C CG  . LEU B 73  ? 0.2815 0.3181 0.3340 -0.1467 -0.0417 0.0338  108 LEU B CG  
2749 C CD1 . LEU B 73  ? 0.2678 0.3171 0.3060 -0.1519 -0.0366 0.0373  108 LEU B CD1 
2750 C CD2 . LEU B 73  ? 0.3485 0.3691 0.4003 -0.1477 -0.0513 0.0441  108 LEU B CD2 
2751 N N   . VAL B 74  ? 0.3065 0.3662 0.3761 -0.1345 -0.0279 0.0045  109 VAL B N   
2752 C CA  . VAL B 74  ? 0.2558 0.3126 0.3307 -0.1257 -0.0285 -0.0045 109 VAL B CA  
2753 C C   . VAL B 74  ? 0.1862 0.2300 0.2517 -0.1196 -0.0279 -0.0037 109 VAL B C   
2754 O O   . VAL B 74  ? 0.1940 0.2391 0.2500 -0.1220 -0.0233 -0.0003 109 VAL B O   
2755 C CB  . VAL B 74  ? 0.2398 0.3136 0.3173 -0.1271 -0.0215 -0.0115 109 VAL B CB  
2756 C CG1 . VAL B 74  ? 0.2538 0.3257 0.3349 -0.1196 -0.0226 -0.0200 109 VAL B CG1 
2757 C CG2 . VAL B 74  ? 0.1944 0.2839 0.2829 -0.1335 -0.0217 -0.0125 109 VAL B CG2 
2758 N N   . LEU B 75  ? 0.2045 0.2375 0.2724 -0.1125 -0.0329 -0.0074 110 LEU B N   
2759 C CA  . LEU B 75  ? 0.2201 0.2414 0.2809 -0.1072 -0.0318 -0.0069 110 LEU B CA  
2760 C C   . LEU B 75  ? 0.2000 0.2210 0.2611 -0.1039 -0.0289 -0.0139 110 LEU B C   
2761 O O   . LEU B 75  ? 0.2028 0.2254 0.2684 -0.1017 -0.0355 -0.0189 110 LEU B O   
2762 C CB  . LEU B 75  ? 0.2847 0.2921 0.3445 -0.1030 -0.0406 -0.0039 110 LEU B CB  
2763 C CG  . LEU B 75  ? 0.2222 0.2172 0.2762 -0.0973 -0.0410 -0.0030 110 LEU B CG  
2764 C CD1 . LEU B 75  ? 0.2208 0.2189 0.2700 -0.1000 -0.0341 0.0010  110 LEU B CD1 
2765 C CD2 . LEU B 75  ? 0.2191 0.2011 0.2737 -0.0925 -0.0521 -0.0005 110 LEU B CD2 
2766 N N   . VAL B 76  ? 0.2404 0.2594 0.2960 -0.1040 -0.0195 -0.0151 111 VAL B N   
2767 C CA  . VAL B 76  ? 0.2491 0.2630 0.3021 -0.0960 -0.0113 -0.0216 111 VAL B CA  
2768 C C   . VAL B 76  ? 0.1819 0.1775 0.2287 -0.0860 -0.0107 -0.0178 111 VAL B C   
2769 O O   . VAL B 76  ? 0.1708 0.1628 0.2160 -0.0935 -0.0070 -0.0151 111 VAL B O   
2770 C CB  . VAL B 76  ? 0.2391 0.2610 0.2925 -0.1003 0.0026  -0.0273 111 VAL B CB  
2771 C CG1 . VAL B 76  ? 0.2169 0.2277 0.2681 -0.0825 0.0126  -0.0311 111 VAL B CG1 
2772 C CG2 . VAL B 76  ? 0.1943 0.2380 0.2541 -0.1097 0.0026  -0.0312 111 VAL B CG2 
2773 N N   . ASP B 77  ? 0.1887 0.1755 0.2323 -0.0691 -0.0147 -0.0182 112 ASP B N   
2774 C CA  . ASP B 77  ? 0.1821 0.1541 0.2194 -0.0572 -0.0146 -0.0148 112 ASP B CA  
2775 C C   . ASP B 77  ? 0.2172 0.1851 0.2566 -0.0647 -0.0250 -0.0106 112 ASP B C   
2776 O O   . ASP B 77  ? 0.1741 0.1484 0.2185 -0.0810 -0.0300 -0.0077 112 ASP B O   
2777 C CB  . ASP B 77  ? 0.2090 0.1724 0.2427 -0.0530 0.0011  -0.0135 112 ASP B CB  
2778 C CG  . ASP B 77  ? 0.2067 0.1685 0.2377 -0.0403 0.0114  -0.0162 112 ASP B CG  
2779 O OD1 . ASP B 77  ? 0.1912 0.1598 0.2215 -0.0309 0.0053  -0.0190 112 ASP B OD1 
2780 O OD2 . ASP B 77  ? 0.2046 0.1579 0.2354 -0.0389 0.0254  -0.0157 112 ASP B OD2 
2781 N N   . THR B 78  ? 0.1818 0.1397 0.2170 -0.0515 -0.0287 -0.0098 113 THR B N   
2782 C CA  . THR B 78  ? 0.2027 0.1559 0.2416 -0.0542 -0.0414 -0.0078 113 THR B CA  
2783 C C   . THR B 78  ? 0.1997 0.1446 0.2357 -0.0463 -0.0380 -0.0051 113 THR B C   
2784 O O   . THR B 78  ? 0.2434 0.1833 0.2826 -0.0442 -0.0480 -0.0045 113 THR B O   
2785 C CB  . THR B 78  ? 0.2166 0.1685 0.2567 -0.0459 -0.0540 -0.0134 113 THR B CB  
2786 O OG1 . THR B 78  ? 0.2556 0.2032 0.2863 -0.0253 -0.0515 -0.0174 113 THR B OG1 
2787 C CG2 . THR B 78  ? 0.2079 0.1717 0.2533 -0.0528 -0.0564 -0.0173 113 THR B CG2 
2788 N N   . GLY B 79  ? 0.2266 0.1700 0.2586 -0.0416 -0.0236 -0.0037 114 GLY B N   
2789 C CA  . GLY B 79  ? 0.1987 0.1371 0.2300 -0.0343 -0.0184 -0.0013 114 GLY B CA  
2790 C C   . GLY B 79  ? 0.2960 0.2291 0.3190 -0.0145 -0.0212 -0.0037 114 GLY B C   
2791 O O   . GLY B 79  ? 0.2584 0.1919 0.2754 -0.0059 -0.0256 -0.0076 114 GLY B O   
2792 N N   . ALA B 80  ? 0.2379 0.1687 0.2612 -0.0072 -0.0193 -0.0025 115 ALA B N   
2793 C CA  . ALA B 80  ? 0.2788 0.2069 0.2917 0.0130  -0.0180 -0.0048 115 ALA B CA  
2794 C C   . ALA B 80  ? 0.2841 0.2109 0.2991 0.0198  -0.0335 -0.0111 115 ALA B C   
2795 O O   . ALA B 80  ? 0.2845 0.2111 0.2896 0.0373  -0.0341 -0.0157 115 ALA B O   
2796 C CB  . ALA B 80  ? 0.2847 0.2127 0.2962 0.0188  -0.0022 0.0003  115 ALA B CB  
2797 N N   . ALA B 81  ? 0.2559 0.1812 0.2829 0.0075  -0.0454 -0.0112 116 ALA B N   
2798 C CA  . ALA B 81  ? 0.4005 0.3210 0.4326 0.0140  -0.0586 -0.0164 116 ALA B CA  
2799 C C   . ALA B 81  ? 0.3651 0.2884 0.3939 0.0286  -0.0503 -0.0173 116 ALA B C   
2800 O O   . ALA B 81  ? 0.3928 0.3212 0.4258 0.0240  -0.0390 -0.0111 116 ALA B O   
2801 C CB  . ALA B 81  ? 0.3261 0.2427 0.3548 0.0213  -0.0711 -0.0261 116 ALA B CB  
2802 N N   . GLY B 82  ? 0.3891 0.3111 0.4106 0.0460  -0.0547 -0.0258 117 GLY B N   
2803 C CA  . GLY B 82  ? 0.3587 0.2859 0.3759 0.0610  -0.0459 -0.0273 117 GLY B CA  
2804 C C   . GLY B 82  ? 0.4293 0.3620 0.4282 0.0752  -0.0315 -0.0258 117 GLY B C   
2805 O O   . GLY B 82  ? 0.3900 0.3286 0.3822 0.0899  -0.0241 -0.0276 117 GLY B O   
2806 N N   . LEU B 83  ? 0.3315 0.2632 0.3218 0.0720  -0.0269 -0.0218 118 LEU B N   
2807 C CA  . LEU B 83  ? 0.3649 0.3002 0.3360 0.0876  -0.0151 -0.0190 118 LEU B CA  
2808 C C   . LEU B 83  ? 0.4570 0.3938 0.4258 0.0884  0.0063  -0.0074 118 LEU B C   
2809 O O   . LEU B 83  ? 0.4702 0.4098 0.4222 0.1039  0.0177  -0.0031 118 LEU B O   
2810 C CB  . LEU B 83  ? 0.3595 0.2932 0.3247 0.0847  -0.0170 -0.0177 118 LEU B CB  
2811 C CG  . LEU B 83  ? 0.3853 0.3207 0.3508 0.0855  -0.0354 -0.0287 118 LEU B CG  
2812 C CD1 . LEU B 83  ? 0.3328 0.2703 0.2932 0.0839  -0.0314 -0.0246 118 LEU B CD1 
2813 C CD2 . LEU B 83  ? 0.3993 0.3405 0.3512 0.1061  -0.0422 -0.0391 118 LEU B CD2 
2814 N N   . PHE B 84  ? 0.4509 0.3867 0.4361 0.0719  0.0122  -0.0021 119 PHE B N   
2815 C CA  . PHE B 84  ? 0.4291 0.3645 0.4151 0.0686  0.0330  0.0083  119 PHE B CA  
2816 C C   . PHE B 84  ? 0.4490 0.3915 0.4524 0.0603  0.0379  0.0091  119 PHE B C   
2817 O O   . PHE B 84  ? 0.4116 0.3546 0.4279 0.0456  0.0478  0.0140  119 PHE B O   
2818 C CB  . PHE B 84  ? 0.4068 0.3349 0.3963 0.0547  0.0375  0.0129  119 PHE B CB  
2819 C CG  . PHE B 84  ? 0.5332 0.4553 0.5181 0.0566  0.0587  0.0231  119 PHE B CG  
2820 C CD1 . PHE B 84  ? 0.5775 0.5013 0.5718 0.0518  0.0751  0.0290  119 PHE B CD1 
2821 C CD2 . PHE B 84  ? 0.5697 0.4844 0.5418 0.0637  0.0624  0.0271  119 PHE B CD2 
2822 C CE1 . PHE B 84  ? 0.6886 0.6035 0.6800 0.0526  0.0956  0.0394  119 PHE B CE1 
2823 C CE2 . PHE B 84  ? 0.7054 0.6105 0.6732 0.0667  0.0821  0.0380  119 PHE B CE2 
2824 C CZ  . PHE B 84  ? 0.8133 0.7170 0.7909 0.0605  0.0992  0.0445  119 PHE B CZ  
2825 N N   . GLY B 85  ? 0.4044 0.3538 0.4103 0.0695  0.0293  0.0024  120 GLY B N   
2826 C CA  . GLY B 85  ? 0.4544 0.4141 0.4773 0.0657  0.0331  0.0021  120 GLY B CA  
2827 C C   . GLY B 85  ? 0.3623 0.3233 0.4027 0.0543  0.0158  -0.0027 120 GLY B C   
2828 O O   . GLY B 85  ? 0.4143 0.3670 0.4544 0.0458  0.0024  -0.0043 120 GLY B O   
2829 N N   . PRO B 86  ? 0.3893 0.3618 0.4455 0.0545  0.0159  -0.0043 121 PRO B N   
2830 C CA  . PRO B 86  ? 0.2841 0.2576 0.3558 0.0472  -0.0020 -0.0075 121 PRO B CA  
2831 C C   . PRO B 86  ? 0.3646 0.3418 0.4490 0.0261  -0.0032 -0.0022 121 PRO B C   
2832 O O   . PRO B 86  ? 0.2911 0.2669 0.3836 0.0193  -0.0192 -0.0024 121 PRO B O   
2833 C CB  . PRO B 86  ? 0.4379 0.4249 0.5214 0.0591  -0.0007 -0.0118 121 PRO B CB  
2834 C CG  . PRO B 86  ? 0.3468 0.3452 0.4298 0.0609  0.0216  -0.0075 121 PRO B CG  
2835 C CD  . PRO B 86  ? 0.4278 0.4140 0.4881 0.0642  0.0311  -0.0036 121 PRO B CD  
2836 N N   . THR B 87  ? 0.2619 0.2427 0.3474 0.0157  0.0129  0.0023  122 THR B N   
2837 C CA  . THR B 87  ? 0.2653 0.2515 0.3623 -0.0043 0.0117  0.0044  122 THR B CA  
2838 C C   . THR B 87  ? 0.2822 0.2570 0.3693 -0.0139 0.0035  0.0054  122 THR B C   
2839 O O   . THR B 87  ? 0.2585 0.2388 0.3525 -0.0301 0.0007  0.0063  122 THR B O   
2840 C CB  . THR B 87  ? 0.3565 0.3495 0.4613 -0.0136 0.0321  0.0065  122 THR B CB  
2841 O OG1 . THR B 87  ? 0.2684 0.2472 0.3582 -0.0106 0.0453  0.0098  122 THR B OG1 
2842 C CG2 . THR B 87  ? 0.3585 0.3664 0.4761 -0.0062 0.0425  0.0060  122 THR B CG2 
2843 N N   . LEU B 88  ? 0.2395 0.2012 0.3109 -0.0047 -0.0001 0.0045  123 LEU B N   
2844 C CA  . LEU B 88  ? 0.2228 0.1767 0.2868 -0.0137 -0.0066 0.0050  123 LEU B CA  
2845 C C   . LEU B 88  ? 0.2924 0.2397 0.3543 -0.0099 -0.0257 0.0027  123 LEU B C   
2846 O O   . LEU B 88  ? 0.2522 0.2001 0.3201 -0.0017 -0.0345 0.0007  123 LEU B O   
2847 C CB  . LEU B 88  ? 0.2364 0.1822 0.2868 -0.0079 0.0058  0.0058  123 LEU B CB  
2848 C CG  . LEU B 88  ? 0.3275 0.2743 0.3810 -0.0134 0.0256  0.0091  123 LEU B CG  
2849 C CD1 . LEU B 88  ? 0.2663 0.2020 0.3049 -0.0046 0.0356  0.0115  123 LEU B CD1 
2850 C CD2 . LEU B 88  ? 0.2515 0.2047 0.3170 -0.0339 0.0259  0.0080  123 LEU B CD2 
2851 N N   . GLY B 89  ? 0.2476 0.1889 0.3034 -0.0163 -0.0319 0.0026  124 GLY B N   
2852 C CA  . GLY B 89  ? 0.2213 0.1554 0.2782 -0.0159 -0.0493 0.0009  124 GLY B CA  
2853 C C   . GLY B 89  ? 0.2570 0.1934 0.3235 -0.0307 -0.0603 0.0065  124 GLY B C   
2854 O O   . GLY B 89  ? 0.3486 0.2768 0.4192 -0.0300 -0.0746 0.0070  124 GLY B O   
2855 N N   . ARG B 90  ? 0.1909 0.1380 0.2611 -0.0438 -0.0543 0.0107  125 ARG B N   
2856 C CA  . ARG B 90  ? 0.2615 0.2141 0.3382 -0.0568 -0.0647 0.0172  125 ARG B CA  
2857 C C   . ARG B 90  ? 0.2335 0.1853 0.3052 -0.0706 -0.0692 0.0208  125 ARG B C   
2858 O O   . ARG B 90  ? 0.2890 0.2440 0.3626 -0.0792 -0.0784 0.0280  125 ARG B O   
2859 C CB  . ARG B 90  ? 0.2421 0.2110 0.3255 -0.0645 -0.0576 0.0184  125 ARG B CB  
2860 C CG  . ARG B 90  ? 0.3033 0.2765 0.3954 -0.0520 -0.0539 0.0157  125 ARG B CG  
2861 C CD  . ARG B 90  ? 0.4273 0.4191 0.5298 -0.0598 -0.0463 0.0150  125 ARG B CD  
2862 N NE  . ARG B 90  ? 0.6060 0.6033 0.7184 -0.0472 -0.0421 0.0123  125 ARG B NE  
2863 C CZ  . ARG B 90  ? 0.6906 0.7038 0.8176 -0.0471 -0.0470 0.0129  125 ARG B CZ  
2864 N NH1 . ARG B 90  ? 0.5502 0.5750 0.6819 -0.0579 -0.0579 0.0171  125 ARG B NH1 
2865 N NH2 . ARG B 90  ? 0.6298 0.6496 0.7665 -0.0349 -0.0411 0.0095  125 ARG B NH2 
2866 N N   . LEU B 91  ? 0.2226 0.1520 0.3205 -0.0251 -0.0603 0.0465  126 LEU B N   
2867 C CA  . LEU B 91  ? 0.3209 0.2403 0.4067 -0.0418 -0.0590 0.0516  126 LEU B CA  
2868 C C   . LEU B 91  ? 0.2510 0.1455 0.3335 -0.0463 -0.0693 0.0556  126 LEU B C   
2869 O O   . LEU B 91  ? 0.2974 0.1828 0.3700 -0.0607 -0.0731 0.0654  126 LEU B O   
2870 C CB  . LEU B 91  ? 0.2118 0.1406 0.2949 -0.0454 -0.0480 0.0436  126 LEU B CB  
2871 C CG  . LEU B 91  ? 0.2793 0.2044 0.3523 -0.0618 -0.0445 0.0471  126 LEU B CG  
2872 C CD1 . LEU B 91  ? 0.1975 0.1395 0.2679 -0.0651 -0.0329 0.0430  126 LEU B CD1 
2873 C CD2 . LEU B 91  ? 0.2693 0.1811 0.3423 -0.0652 -0.0476 0.0435  126 LEU B CD2 
2874 N N   . ALA B 92  ? 0.2613 0.1431 0.3504 -0.0352 -0.0745 0.0486  127 ALA B N   
2875 C CA  . ALA B 92  ? 0.3628 0.2164 0.4473 -0.0405 -0.0858 0.0528  127 ALA B CA  
2876 C C   . ALA B 92  ? 0.3500 0.1903 0.4321 -0.0438 -0.0980 0.0663  127 ALA B C   
2877 O O   . ALA B 92  ? 0.3581 0.1840 0.4285 -0.0596 -0.1037 0.0763  127 ALA B O   
2878 C CB  . ALA B 92  ? 0.3199 0.1602 0.4118 -0.0256 -0.0903 0.0414  127 ALA B CB  
2879 N N   . ALA B 93  ? 0.3073 0.1551 0.4003 -0.0291 -0.1021 0.0670  128 ALA B N   
2880 C CA  . ALA B 93  ? 0.3270 0.1638 0.4200 -0.0301 -0.1153 0.0803  128 ALA B CA  
2881 C C   . ALA B 93  ? 0.3491 0.1944 0.4288 -0.0498 -0.1131 0.0928  128 ALA B C   
2882 O O   . ALA B 93  ? 0.3448 0.1769 0.4146 -0.0603 -0.1228 0.1042  128 ALA B O   
2883 C CB  . ALA B 93  ? 0.4428 0.2936 0.5530 -0.0099 -0.1187 0.0776  128 ALA B CB  
2884 N N   . ASN B 94  ? 0.3000 0.1707 0.3774 -0.0543 -0.0993 0.0887  129 ASN B N   
2885 C CA  . ASN B 94  ? 0.3285 0.2081 0.3921 -0.0724 -0.0957 0.0977  129 ASN B CA  
2886 C C   . ASN B 94  ? 0.3827 0.2582 0.4296 -0.0881 -0.0904 0.0969  129 ASN B C   
2887 O O   . ASN B 94  ? 0.3328 0.2132 0.3648 -0.0997 -0.0903 0.1027  129 ASN B O   
2888 C CB  . ASN B 94  ? 0.2912 0.1971 0.3567 -0.0704 -0.0827 0.0912  129 ASN B CB  
2889 C CG  . ASN B 94  ? 0.2625 0.1825 0.3398 -0.0582 -0.0869 0.0932  129 ASN B CG  
2890 O OD1 . ASN B 94  ? 0.3194 0.2334 0.3987 -0.0578 -0.0990 0.1036  129 ASN B OD1 
2891 N ND2 . ASN B 94  ? 0.2408 0.1813 0.3255 -0.0500 -0.0774 0.0846  129 ASN B ND2 
2892 N N   . LEU B 95  ? 0.3482 0.2195 0.3968 -0.0867 -0.0848 0.0878  130 LEU B N   
2893 C CA  . LEU B 95  ? 0.3815 0.2513 0.4167 -0.0982 -0.0811 0.0866  130 LEU B CA  
2894 C C   . LEU B 95  ? 0.3380 0.1903 0.3651 -0.1030 -0.0944 0.0961  130 LEU B C   
2895 O O   . LEU B 95  ? 0.3603 0.2169 0.3728 -0.1159 -0.0935 0.1014  130 LEU B O   
2896 C CB  . LEU B 95  ? 0.3724 0.2389 0.4135 -0.0950 -0.0762 0.0765  130 LEU B CB  
2897 C CG  . LEU B 95  ? 0.5038 0.3684 0.5343 -0.1066 -0.0739 0.0760  130 LEU B CG  
2898 C CD1 . LEU B 95  ? 0.4903 0.3738 0.5097 -0.1179 -0.0637 0.0774  130 LEU B CD1 
2899 C CD2 . LEU B 95  ? 0.4853 0.3506 0.5229 -0.1041 -0.0688 0.0659  130 LEU B CD2 
2900 N N   . LYS B 96  ? 0.3885 0.2207 0.4253 -0.0920 -0.1073 0.0978  131 LYS B N   
2901 C CA  . LYS B 96  ? 0.3854 0.1994 0.4147 -0.0962 -0.1213 0.1070  131 LYS B CA  
2902 C C   . LYS B 96  ? 0.4114 0.2320 0.4347 -0.1022 -0.1274 0.1186  131 LYS B C   
2903 O O   . LYS B 96  ? 0.4137 0.2305 0.4229 -0.1149 -0.1329 0.1266  131 LYS B O   
2904 C CB  . LYS B 96  ? 0.4343 0.2244 0.4756 -0.0806 -0.1335 0.1041  131 LYS B CB  
2905 C CG  . LYS B 96  ? 0.4250 0.2091 0.4710 -0.0749 -0.1277 0.0913  131 LYS B CG  
2906 C CD  . LYS B 96  ? 0.5761 0.3350 0.6293 -0.0609 -0.1392 0.0865  131 LYS B CD  
2907 C CE  . LYS B 96  ? 0.6173 0.3784 0.6885 -0.0398 -0.1426 0.0826  131 LYS B CE  
2908 N NZ  . LYS B 96  ? 0.6545 0.4215 0.7375 -0.0260 -0.1345 0.0677  131 LYS B NZ  
2909 N N   . ALA B 97  ? 0.4307 0.2625 0.4641 -0.0943 -0.1270 0.1201  132 ALA B N   
2910 C CA  . ALA B 97  ? 0.4263 0.2659 0.4543 -0.1006 -0.1336 0.1312  132 ALA B CA  
2911 C C   . ALA B 97  ? 0.4039 0.2600 0.4120 -0.1183 -0.1235 0.1318  132 ALA B C   
2912 O O   . ALA B 97  ? 0.4186 0.2770 0.4156 -0.1283 -0.1304 0.1409  132 ALA B O   
2913 C CB  . ALA B 97  ? 0.3938 0.2447 0.4376 -0.0889 -0.1345 0.1326  132 ALA B CB  
2914 N N   . ALA B 98  ? 0.3613 0.2292 0.3652 -0.1213 -0.1076 0.1216  133 ALA B N   
2915 C CA  . ALA B 98  ? 0.4575 0.3399 0.4440 -0.1351 -0.0968 0.1192  133 ALA B CA  
2916 C C   . ALA B 98  ? 0.4413 0.3153 0.4151 -0.1465 -0.1000 0.1225  133 ALA B C   
2917 O O   . ALA B 98  ? 0.4230 0.3095 0.3836 -0.1575 -0.0906 0.1199  133 ALA B O   
2918 C CB  . ALA B 98  ? 0.3806 0.2782 0.3701 -0.1323 -0.0791 0.1064  133 ALA B CB  
2919 N N   . GLY B 99  ? 0.4292 0.2824 0.4069 -0.1440 -0.1127 0.1276  134 GLY B N   
2920 C CA  . GLY B 99  ? 0.4394 0.2831 0.4039 -0.1565 -0.1184 0.1330  134 GLY B CA  
2921 C C   . GLY B 99  ? 0.5252 0.3694 0.4891 -0.1598 -0.1095 0.1253  134 GLY B C   
2922 O O   . GLY B 99  ? 0.5639 0.4096 0.5147 -0.1736 -0.1093 0.1287  134 GLY B O   
2923 N N   . TYR B 100 ? 0.4592 0.3037 0.4372 -0.1485 -0.1027 0.1155  135 TYR B N   
2924 C CA  . TYR B 100 ? 0.4573 0.3033 0.4371 -0.1511 -0.0951 0.1079  135 TYR B CA  
2925 C C   . TYR B 100 ? 0.4824 0.3086 0.4745 -0.1390 -0.1026 0.1039  135 TYR B C   
2926 O O   . TYR B 100 ? 0.5160 0.3348 0.5191 -0.1255 -0.1079 0.1028  135 TYR B O   
2927 C CB  . TYR B 100 ? 0.4411 0.3111 0.4257 -0.1500 -0.0773 0.0973  135 TYR B CB  
2928 C CG  . TYR B 100 ? 0.4744 0.3647 0.4475 -0.1612 -0.0674 0.0974  135 TYR B CG  
2929 C CD1 . TYR B 100 ? 0.5271 0.4242 0.4908 -0.1746 -0.0639 0.0983  135 TYR B CD1 
2930 C CD2 . TYR B 100 ? 0.4458 0.3482 0.4168 -0.1589 -0.0619 0.0962  135 TYR B CD2 
2931 C CE1 . TYR B 100 ? 0.4958 0.4118 0.4492 -0.1845 -0.0547 0.0971  135 TYR B CE1 
2932 C CE2 . TYR B 100 ? 0.4603 0.3796 0.4197 -0.1688 -0.0530 0.0946  135 TYR B CE2 
2933 C CZ  . TYR B 100 ? 0.4811 0.4071 0.4319 -0.1814 -0.0494 0.0949  135 TYR B CZ  
2934 O OH  . TYR B 100 ? 0.4841 0.4272 0.4231 -0.1916 -0.0407 0.0926  135 TYR B OH  
2935 N N   . GLN B 101 ? 0.4194 0.2371 0.4095 -0.1441 -0.1033 0.1010  136 GLN B N   
2936 C CA  . GLN B 101 ? 0.4534 0.2539 0.4547 -0.1317 -0.1085 0.0940  136 GLN B CA  
2937 C C   . GLN B 101 ? 0.4296 0.2455 0.4392 -0.1294 -0.0954 0.0822  136 GLN B C   
2938 O O   . GLN B 101 ? 0.4421 0.2780 0.4481 -0.1396 -0.0845 0.0804  136 GLN B O   
2939 C CB  . GLN B 101 ? 0.5192 0.2938 0.5140 -0.1361 -0.1215 0.0979  136 GLN B CB  
2940 C CG  . GLN B 101 ? 0.6602 0.4142 0.6501 -0.1349 -0.1378 0.1088  136 GLN B CG  
2941 C CD  . GLN B 101 ? 0.6543 0.3987 0.6584 -0.1154 -0.1444 0.1062  136 GLN B CD  
2942 O OE1 . GLN B 101 ? 0.5891 0.3241 0.6043 -0.1013 -0.1446 0.0961  136 GLN B OE1 
2943 N NE2 . GLN B 101 ? 0.7642 0.5120 0.7678 -0.1148 -0.1500 0.1151  136 GLN B NE2 
2944 N N   . PRO B 102 ? 0.4009 0.2088 0.4223 -0.1155 -0.0969 0.0737  137 PRO B N   
2945 C CA  . PRO B 102 ? 0.3624 0.1848 0.3916 -0.1137 -0.0862 0.0629  137 PRO B CA  
2946 C C   . PRO B 102 ? 0.4048 0.2300 0.4289 -0.1261 -0.0837 0.0613  137 PRO B C   
2947 O O   . PRO B 102 ? 0.4047 0.2521 0.4328 -0.1310 -0.0726 0.0562  137 PRO B O   
2948 C CB  . PRO B 102 ? 0.4379 0.2448 0.4778 -0.0972 -0.0924 0.0548  137 PRO B CB  
2949 C CG  . PRO B 102 ? 0.5200 0.3137 0.5620 -0.0878 -0.1020 0.0608  137 PRO B CG  
2950 C CD  . PRO B 102 ? 0.5422 0.3292 0.5714 -0.1000 -0.1083 0.0728  137 PRO B CD  
2951 N N   . GLU B 103 ? 0.4294 0.2330 0.4456 -0.1313 -0.0946 0.0657  138 GLU B N   
2952 C CA  . GLU B 103 ? 0.4621 0.2674 0.4730 -0.1445 -0.0938 0.0654  138 GLU B CA  
2953 C C   . GLU B 103 ? 0.4113 0.2415 0.4169 -0.1591 -0.0844 0.0704  138 GLU B C   
2954 O O   . GLU B 103 ? 0.4659 0.3070 0.4710 -0.1698 -0.0804 0.0687  138 GLU B O   
2955 C CB  . GLU B 103 ? 0.4734 0.2485 0.4747 -0.1485 -0.1086 0.0712  138 GLU B CB  
2956 C CG  . GLU B 103 ? 0.4707 0.2181 0.4766 -0.1336 -0.1189 0.0646  138 GLU B CG  
2957 C CD  . GLU B 103 ? 0.6553 0.3927 0.6664 -0.1184 -0.1247 0.0665  138 GLU B CD  
2958 O OE1 . GLU B 103 ? 0.6122 0.3614 0.6215 -0.1210 -0.1226 0.0746  138 GLU B OE1 
2959 O OE2 . GLU B 103 ? 0.6497 0.3679 0.6668 -0.1035 -0.1316 0.0592  138 GLU B OE2 
2960 N N   . GLN B 104 ? 0.4050 0.2446 0.4062 -0.1600 -0.0813 0.0761  139 GLN B N   
2961 C CA  . GLN B 104 ? 0.4566 0.3189 0.4511 -0.1732 -0.0725 0.0796  139 GLN B CA  
2962 C C   . GLN B 104 ? 0.3843 0.2754 0.3895 -0.1704 -0.0571 0.0706  139 GLN B C   
2963 O O   . GLN B 104 ? 0.4209 0.3330 0.4229 -0.1799 -0.0486 0.0711  139 GLN B O   
2964 C CB  . GLN B 104 ? 0.4144 0.2745 0.3972 -0.1769 -0.0764 0.0893  139 GLN B CB  
2965 C CG  . GLN B 104 ? 0.4542 0.2867 0.4260 -0.1813 -0.0932 0.0999  139 GLN B CG  
2966 C CD  . GLN B 104 ? 0.5487 0.3813 0.5084 -0.1870 -0.0982 0.1100  139 GLN B CD  
2967 O OE1 . GLN B 104 ? 0.5287 0.3632 0.4922 -0.1778 -0.0981 0.1103  139 GLN B OE1 
2968 N NE2 . GLN B 104 ? 0.4909 0.3220 0.4355 -0.2034 -0.1034 0.1190  139 GLN B NE2 
2969 N N   . VAL B 105 ? 0.3788 0.2713 0.3964 -0.1576 -0.0540 0.0623  140 VAL B N   
2970 C CA  . VAL B 105 ? 0.3207 0.2388 0.3489 -0.1544 -0.0410 0.0544  140 VAL B CA  
2971 C C   . VAL B 105 ? 0.3188 0.2514 0.3546 -0.1610 -0.0367 0.0492  140 VAL B C   
2972 O O   . VAL B 105 ? 0.3950 0.3162 0.4340 -0.1601 -0.0430 0.0465  140 VAL B O   
2973 C CB  . VAL B 105 ? 0.3111 0.2260 0.3489 -0.1397 -0.0405 0.0485  140 VAL B CB  
2974 C CG1 . VAL B 105 ? 0.3361 0.2761 0.3853 -0.1370 -0.0286 0.0405  140 VAL B CG1 
2975 C CG2 . VAL B 105 ? 0.3362 0.2414 0.3681 -0.1337 -0.0443 0.0542  140 VAL B CG2 
2976 N N   . ASP B 106 ? 0.3257 0.2841 0.3644 -0.1675 -0.0264 0.0473  141 ASP B N   
2977 C CA  . ASP B 106 ? 0.3119 0.2902 0.3598 -0.1742 -0.0218 0.0430  141 ASP B CA  
2978 C C   . ASP B 106 ? 0.2829 0.2752 0.3480 -0.1645 -0.0168 0.0337  141 ASP B C   
2979 O O   . ASP B 106 ? 0.2914 0.2896 0.3653 -0.1664 -0.0188 0.0299  141 ASP B O   
2980 C CB  . ASP B 106 ? 0.3153 0.3169 0.3593 -0.1847 -0.0131 0.0449  141 ASP B CB  
2981 C CG  . ASP B 106 ? 0.4498 0.4401 0.4755 -0.1975 -0.0191 0.0547  141 ASP B CG  
2982 O OD1 . ASP B 106 ? 0.4069 0.3824 0.4274 -0.2047 -0.0282 0.0593  141 ASP B OD1 
2983 O OD2 . ASP B 106 ? 0.3724 0.3671 0.3875 -0.2009 -0.0156 0.0582  141 ASP B OD2 
2984 N N   . GLU B 107 ? 0.3031 0.3022 0.3728 -0.1552 -0.0107 0.0304  142 GLU B N   
2985 C CA  . GLU B 107 ? 0.2404 0.2534 0.3255 -0.1464 -0.0066 0.0226  142 GLU B CA  
2986 C C   . GLU B 107 ? 0.2279 0.2293 0.3113 -0.1353 -0.0072 0.0219  142 GLU B C   
2987 O O   . GLU B 107 ? 0.2319 0.2253 0.3052 -0.1348 -0.0063 0.0262  142 GLU B O   
2988 C CB  . GLU B 107 ? 0.2298 0.2748 0.3257 -0.1486 0.0043  0.0183  142 GLU B CB  
2989 C CG  . GLU B 107 ? 0.2455 0.3037 0.3409 -0.1608 0.0053  0.0204  142 GLU B CG  
2990 C CD  . GLU B 107 ? 0.2984 0.3909 0.4091 -0.1619 0.0142  0.0146  142 GLU B CD  
2991 O OE1 . GLU B 107 ? 0.2200 0.3283 0.3404 -0.1534 0.0217  0.0087  142 GLU B OE1 
2992 O OE2 . GLU B 107 ? 0.3167 0.4213 0.4299 -0.1716 0.0134  0.0159  142 GLU B OE2 
2993 N N   . VAL B 108 ? 0.2143 0.2158 0.3075 -0.1273 -0.0097 0.0170  143 VAL B N   
2994 C CA  . VAL B 108 ? 0.2552 0.2514 0.3497 -0.1153 -0.0094 0.0157  143 VAL B CA  
2995 C C   . VAL B 108 ? 0.1830 0.2010 0.2889 -0.1053 -0.0015 0.0082  143 VAL B C   
2996 O O   . VAL B 108 ? 0.1872 0.2147 0.3026 -0.1026 -0.0031 0.0038  143 VAL B O   
2997 C CB  . VAL B 108 ? 0.2040 0.1797 0.2970 -0.1054 -0.0189 0.0146  143 VAL B CB  
2998 C CG1 . VAL B 108 ? 0.1956 0.1710 0.2893 -0.0897 -0.0163 0.0119  143 VAL B CG1 
2999 C CG2 . VAL B 108 ? 0.2248 0.1770 0.3070 -0.1119 -0.0274 0.0212  143 VAL B CG2 
3000 N N   . TYR B 109 ? 0.2013 0.2255 0.3058 -0.0997 0.0059  0.0069  144 TYR B N   
3001 C CA  . TYR B 109 ? 0.1849 0.2247 0.2993 -0.0885 0.0122  0.0003  144 TYR B CA  
3002 C C   . TYR B 109 ? 0.2093 0.2376 0.3203 -0.0752 0.0098  -0.0001 144 TYR B C   
3003 O O   . TYR B 109 ? 0.1992 0.2153 0.3005 -0.0755 0.0090  0.0038  144 TYR B O   
3004 C CB  . TYR B 109 ? 0.1687 0.2231 0.2834 -0.0915 0.0225  -0.0026 144 TYR B CB  
3005 C CG  . TYR B 109 ? 0.1968 0.2692 0.3151 -0.1055 0.0273  -0.0030 144 TYR B CG  
3006 C CD1 . TYR B 109 ? 0.1862 0.2650 0.3112 -0.1135 0.0224  -0.0016 144 TYR B CD1 
3007 C CD2 . TYR B 109 ? 0.1765 0.2585 0.2890 -0.1131 0.0363  -0.0043 144 TYR B CD2 
3008 C CE1 . TYR B 109 ? 0.1831 0.2798 0.3105 -0.1275 0.0265  -0.0008 144 TYR B CE1 
3009 C CE2 . TYR B 109 ? 0.1862 0.2863 0.2998 -0.1265 0.0409  -0.0041 144 TYR B CE2 
3010 C CZ  . TYR B 109 ? 0.1899 0.2960 0.3106 -0.1313 0.0353  -0.0015 144 TYR B CZ  
3011 O OH  . TYR B 109 ? 0.2030 0.3243 0.3223 -0.1409 0.0385  -0.0002 144 TYR B OH  
3012 N N   . LEU B 110 ? 0.1707 0.2049 0.2898 -0.0647 0.0086  -0.0041 145 LEU B N   
3013 C CA  . LEU B 110 ? 0.1404 0.1660 0.2557 -0.0539 0.0062  -0.0038 145 LEU B CA  
3014 C C   . LEU B 110 ? 0.1667 0.1991 0.2851 -0.0466 0.0114  -0.0064 145 LEU B C   
3015 O O   . LEU B 110 ? 0.1630 0.2082 0.2920 -0.0430 0.0128  -0.0101 145 LEU B O   
3016 C CB  . LEU B 110 ? 0.1422 0.1668 0.2608 -0.0487 -0.0005 -0.0057 145 LEU B CB  
3017 C CG  . LEU B 110 ? 0.1505 0.1641 0.2654 -0.0548 -0.0068 -0.0048 145 LEU B CG  
3018 C CD1 . LEU B 110 ? 0.1516 0.1656 0.2691 -0.0505 -0.0128 -0.0090 145 LEU B CD1 
3019 C CD2 . LEU B 110 ? 0.1620 0.1605 0.2679 -0.0536 -0.0087 -0.0012 145 LEU B CD2 
3020 N N   . THR B 111 ? 0.1357 0.1592 0.2454 -0.0445 0.0133  -0.0043 146 THR B N   
3021 C CA  . THR B 111 ? 0.1351 0.1595 0.2458 -0.0371 0.0162  -0.0066 146 THR B CA  
3022 C C   . THR B 111 ? 0.1315 0.1572 0.2468 -0.0283 0.0109  -0.0064 146 THR B C   
3023 O O   . THR B 111 ? 0.1661 0.1972 0.2887 -0.0218 0.0111  -0.0089 146 THR B O   
3024 C CB  . THR B 111 ? 0.1386 0.1514 0.2371 -0.0386 0.0181  -0.0038 146 THR B CB  
3025 O OG1 . THR B 111 ? 0.1358 0.1418 0.2283 -0.0380 0.0130  0.0011  146 THR B OG1 
3026 C CG2 . THR B 111 ? 0.1451 0.1571 0.2368 -0.0484 0.0234  -0.0040 146 THR B CG2 
3027 N N   . HIS B 112 ? 0.1291 0.1509 0.2404 -0.0278 0.0058  -0.0039 147 HIS B N   
3028 C CA  . HIS B 112 ? 0.1277 0.1523 0.2406 -0.0215 0.0006  -0.0037 147 HIS B CA  
3029 C C   . HIS B 112 ? 0.1430 0.1647 0.2513 -0.0227 -0.0032 -0.0035 147 HIS B C   
3030 O O   . HIS B 112 ? 0.1356 0.1516 0.2410 -0.0271 -0.0028 -0.0030 147 HIS B O   
3031 C CB  . HIS B 112 ? 0.1300 0.1496 0.2374 -0.0167 0.0001  -0.0008 147 HIS B CB  
3032 C CG  . HIS B 112 ? 0.1462 0.1580 0.2426 -0.0192 0.0009  0.0030  147 HIS B CG  
3033 N ND1 . HIS B 112 ? 0.1405 0.1470 0.2325 -0.0245 0.0047  0.0039  147 HIS B ND1 
3034 C CD2 . HIS B 112 ? 0.1315 0.1423 0.2206 -0.0181 -0.0017 0.0066  147 HIS B CD2 
3035 C CE1 . HIS B 112 ? 0.1321 0.1348 0.2159 -0.0259 0.0039  0.0080  147 HIS B CE1 
3036 N NE2 . HIS B 112 ? 0.1318 0.1381 0.2142 -0.0222 0.0005  0.0095  147 HIS B NE2 
3037 N N   . MET B 113 ? 0.1649 0.1905 0.2726 -0.0186 -0.0076 -0.0044 148 MET B N   
3038 C CA  . MET B 113 ? 0.1516 0.1753 0.2560 -0.0189 -0.0109 -0.0072 148 MET B CA  
3039 C C   . MET B 113 ? 0.1538 0.1775 0.2502 -0.0151 -0.0114 -0.0063 148 MET B C   
3040 O O   . MET B 113 ? 0.1413 0.1666 0.2347 -0.0130 -0.0140 -0.0103 148 MET B O   
3041 C CB  . MET B 113 ? 0.1348 0.1645 0.2435 -0.0192 -0.0156 -0.0112 148 MET B CB  
3042 C CG  . MET B 113 ? 0.1901 0.2239 0.3083 -0.0245 -0.0152 -0.0122 148 MET B CG  
3043 S SD  . MET B 113 ? 0.2127 0.2571 0.3371 -0.0262 -0.0216 -0.0158 148 MET B SD  
3044 C CE  . MET B 113 ? 0.2170 0.2692 0.3533 -0.0343 -0.0188 -0.0158 148 MET B CE  
3045 N N   . HIS B 114 ? 0.1296 0.1521 0.2219 -0.0150 -0.0085 -0.0016 149 HIS B N   
3046 C CA  . HIS B 114 ? 0.1699 0.1953 0.2558 -0.0133 -0.0081 -0.0004 149 HIS B CA  
3047 C C   . HIS B 114 ? 0.1748 0.1972 0.2624 -0.0122 -0.0084 -0.0036 149 HIS B C   
3048 O O   . HIS B 114 ? 0.1695 0.1839 0.2607 -0.0150 -0.0088 -0.0037 149 HIS B O   
3049 C CB  . HIS B 114 ? 0.1668 0.1908 0.2482 -0.0158 -0.0056 0.0058  149 HIS B CB  
3050 C CG  . HIS B 114 ? 0.1969 0.2226 0.2735 -0.0158 -0.0071 0.0096  149 HIS B CG  
3051 N ND1 . HIS B 114 ? 0.1633 0.1830 0.2348 -0.0188 -0.0062 0.0150  149 HIS B ND1 
3052 C CD2 . HIS B 114 ? 0.1891 0.2197 0.2644 -0.0138 -0.0106 0.0091  149 HIS B CD2 
3053 C CE1 . HIS B 114 ? 0.2324 0.2518 0.2998 -0.0182 -0.0096 0.0183  149 HIS B CE1 
3054 N NE2 . HIS B 114 ? 0.2131 0.2399 0.2828 -0.0153 -0.0124 0.0153  149 HIS B NE2 
3055 N N   . PRO B 115 ? 0.1388 0.1676 0.2240 -0.0080 -0.0086 -0.0061 150 PRO B N   
3056 C CA  . PRO B 115 ? 0.2040 0.2282 0.2923 -0.0040 -0.0104 -0.0109 150 PRO B CA  
3057 C C   . PRO B 115 ? 0.2053 0.2218 0.2967 -0.0061 -0.0107 -0.0062 150 PRO B C   
3058 O O   . PRO B 115 ? 0.1797 0.1851 0.2740 -0.0056 -0.0142 -0.0082 150 PRO B O   
3059 C CB  . PRO B 115 ? 0.2047 0.2421 0.2907 0.0019  -0.0090 -0.0148 150 PRO B CB  
3060 C CG  . PRO B 115 ? 0.3290 0.3765 0.4085 -0.0008 -0.0076 -0.0129 150 PRO B CG  
3061 C CD  . PRO B 115 ? 0.2406 0.2818 0.3199 -0.0066 -0.0074 -0.0052 150 PRO B CD  
3062 N N   . ASP B 116 ? 0.1475 0.1682 0.2371 -0.0097 -0.0081 0.0006  151 ASP B N   
3063 C CA  . ASP B 116 ? 0.1350 0.1503 0.2255 -0.0132 -0.0088 0.0061  151 ASP B CA  
3064 C C   . ASP B 116 ? 0.1917 0.1956 0.2812 -0.0203 -0.0088 0.0083  151 ASP B C   
3065 O O   . ASP B 116 ? 0.1382 0.1376 0.2259 -0.0255 -0.0093 0.0136  151 ASP B O   
3066 C CB  . ASP B 116 ? 0.1422 0.1667 0.2292 -0.0163 -0.0063 0.0120  151 ASP B CB  
3067 C CG  . ASP B 116 ? 0.1534 0.1782 0.2345 -0.0205 -0.0035 0.0139  151 ASP B CG  
3068 O OD1 . ASP B 116 ? 0.1852 0.2133 0.2656 -0.0177 -0.0034 0.0106  151 ASP B OD1 
3069 O OD2 . ASP B 116 ? 0.1549 0.1757 0.2315 -0.0265 -0.0021 0.0186  151 ASP B OD2 
3070 N N   . HIS B 117 ? 0.1612 0.1626 0.2518 -0.0215 -0.0085 0.0046  152 HIS B N   
3071 C CA  . HIS B 117 ? 0.1560 0.1510 0.2471 -0.0285 -0.0078 0.0055  152 HIS B CA  
3072 C C   . HIS B 117 ? 0.1450 0.1340 0.2394 -0.0296 -0.0116 0.0017  152 HIS B C   
3073 O O   . HIS B 117 ? 0.1719 0.1545 0.2660 -0.0371 -0.0125 0.0039  152 HIS B O   
3074 C CB  . HIS B 117 ? 0.1549 0.1555 0.2462 -0.0301 -0.0034 0.0050  152 HIS B CB  
3075 C CG  . HIS B 117 ? 0.1307 0.1324 0.2168 -0.0309 -0.0004 0.0087  152 HIS B CG  
3076 N ND1 . HIS B 117 ? 0.1565 0.1545 0.2388 -0.0371 0.0029  0.0109  152 HIS B ND1 
3077 C CD2 . HIS B 117 ? 0.1393 0.1450 0.2219 -0.0279 -0.0007 0.0108  152 HIS B CD2 
3078 C CE1 . HIS B 117 ? 0.1770 0.1745 0.2534 -0.0376 0.0041  0.0138  152 HIS B CE1 
3079 N NE2 . HIS B 117 ? 0.1305 0.1331 0.2073 -0.0326 0.0018  0.0145  152 HIS B NE2 
3080 N N   . VAL B 118 ? 0.1999 0.1905 0.2957 -0.0237 -0.0142 -0.0039 153 VAL B N   
3081 C CA  . VAL B 118 ? 0.1957 0.1789 0.2931 -0.0259 -0.0187 -0.0082 153 VAL B CA  
3082 C C   . VAL B 118 ? 0.2085 0.1802 0.3047 -0.0207 -0.0241 -0.0118 153 VAL B C   
3083 O O   . VAL B 118 ? 0.2462 0.2056 0.3419 -0.0240 -0.0293 -0.0146 153 VAL B O   
3084 C CB  . VAL B 118 ? 0.1870 0.1794 0.2862 -0.0246 -0.0187 -0.0130 153 VAL B CB  
3085 C CG1 . VAL B 118 ? 0.2473 0.2499 0.3498 -0.0276 -0.0143 -0.0098 153 VAL B CG1 
3086 C CG2 . VAL B 118 ? 0.1723 0.1708 0.2681 -0.0162 -0.0192 -0.0178 153 VAL B CG2 
3087 N N   . GLY B 119 ? 0.2061 0.1814 0.3023 -0.0127 -0.0234 -0.0121 154 GLY B N   
3088 C CA  . GLY B 119 ? 0.2442 0.2103 0.3414 -0.0046 -0.0283 -0.0176 154 GLY B CA  
3089 C C   . GLY B 119 ? 0.2848 0.2301 0.3821 -0.0088 -0.0352 -0.0146 154 GLY B C   
3090 O O   . GLY B 119 ? 0.2656 0.1957 0.3619 -0.0062 -0.0411 -0.0207 154 GLY B O   
3091 N N   . GLY B 120 ? 0.2116 0.1543 0.3082 -0.0165 -0.0351 -0.0051 155 GLY B N   
3092 C CA  . GLY B 120 ? 0.2094 0.1332 0.3041 -0.0229 -0.0422 0.0008  155 GLY B CA  
3093 C C   . GLY B 120 ? 0.2946 0.2044 0.3860 -0.0321 -0.0465 -0.0008 155 GLY B C   
3094 O O   . GLY B 120 ? 0.2781 0.1680 0.3664 -0.0376 -0.0544 0.0038  155 GLY B O   
3095 N N   . LEU B 121 ? 0.2519 0.1712 0.3437 -0.0346 -0.0428 -0.0064 156 LEU B N   
3096 C CA  . LEU B 121 ? 0.2923 0.2020 0.3818 -0.0449 -0.0471 -0.0079 156 LEU B CA  
3097 C C   . LEU B 121 ? 0.2540 0.1405 0.3404 -0.0407 -0.0564 -0.0142 156 LEU B C   
3098 O O   . LEU B 121 ? 0.2940 0.1661 0.3767 -0.0514 -0.0625 -0.0138 156 LEU B O   
3099 C CB  . LEU B 121 ? 0.2617 0.1894 0.3541 -0.0468 -0.0421 -0.0127 156 LEU B CB  
3100 C CG  . LEU B 121 ? 0.2225 0.1692 0.3185 -0.0539 -0.0344 -0.0074 156 LEU B CG  
3101 C CD1 . LEU B 121 ? 0.2188 0.1833 0.3196 -0.0517 -0.0310 -0.0125 156 LEU B CD1 
3102 C CD2 . LEU B 121 ? 0.2197 0.1622 0.3141 -0.0691 -0.0356 -0.0009 156 LEU B CD2 
3103 N N   . MET B 122 ? 0.2936 0.1768 0.3816 -0.0258 -0.0576 -0.0207 157 MET B N   
3104 C CA  . MET B 122 ? 0.2837 0.1447 0.3687 -0.0196 -0.0657 -0.0297 157 MET B CA  
3105 C C   . MET B 122 ? 0.3449 0.1940 0.4334 -0.0064 -0.0702 -0.0300 157 MET B C   
3106 O O   . MET B 122 ? 0.3972 0.2643 0.4914 0.0027  -0.0646 -0.0286 157 MET B O   
3107 C CB  . MET B 122 ? 0.3325 0.2037 0.4161 -0.0121 -0.0625 -0.0426 157 MET B CB  
3108 C CG  . MET B 122 ? 0.3526 0.2345 0.4340 -0.0238 -0.0604 -0.0429 157 MET B CG  
3109 S SD  . MET B 122 ? 0.3224 0.1807 0.3978 -0.0392 -0.0703 -0.0430 157 MET B SD  
3110 C CE  . MET B 122 ? 0.3395 0.1692 0.4076 -0.0282 -0.0789 -0.0576 157 MET B CE  
3111 N N   . VAL B 123 ? 0.3946 0.2132 0.4800 -0.0057 -0.0812 -0.0314 158 VAL B N   
3112 C CA  . VAL B 123 ? 0.4679 0.2715 0.5582 0.0101  -0.0876 -0.0345 158 VAL B CA  
3113 C C   . VAL B 123 ? 0.3986 0.1837 0.4856 0.0200  -0.0924 -0.0507 158 VAL B C   
3114 O O   . VAL B 123 ? 0.4834 0.2387 0.5627 0.0123  -0.1019 -0.0522 158 VAL B O   
3115 C CB  . VAL B 123 ? 0.4326 0.2128 0.5219 0.0038  -0.0982 -0.0212 158 VAL B CB  
3116 C CG1 . VAL B 123 ? 0.6017 0.3552 0.6800 -0.0126 -0.1067 -0.0172 158 VAL B CG1 
3117 C CG2 . VAL B 123 ? 0.4209 0.1863 0.5179 0.0227  -0.1062 -0.0247 158 VAL B CG2 
3118 N N   . GLY B 124 ? 0.4863 0.2893 0.5780 0.0358  -0.0857 -0.0632 159 GLY B N   
3119 C CA  . GLY B 124 ? 0.4996 0.2903 0.5858 0.0438  -0.0877 -0.0807 159 GLY B CA  
3120 C C   . GLY B 124 ? 0.4544 0.2448 0.5301 0.0278  -0.0868 -0.0826 159 GLY B C   
3121 O O   . GLY B 124 ? 0.4244 0.2395 0.5002 0.0178  -0.0793 -0.0757 159 GLY B O   
3122 N N   . GLU B 125 ? 0.5471 0.3083 0.6137 0.0251  -0.0954 -0.0918 160 GLU B N   
3123 C CA  . GLU B 125 ? 0.5354 0.2965 0.5927 0.0082  -0.0963 -0.0927 160 GLU B CA  
3124 C C   . GLU B 125 ? 0.5261 0.2711 0.5799 -0.0115 -0.1034 -0.0782 160 GLU B C   
3125 O O   . GLU B 125 ? 0.6145 0.3559 0.6599 -0.0257 -0.1058 -0.0784 160 GLU B O   
3126 C CB  . GLU B 125 ? 0.5919 0.3363 0.6387 0.0129  -0.1003 -0.1109 160 GLU B CB  
3127 C CG  . GLU B 125 ? 0.7192 0.4942 0.7641 0.0198  -0.0901 -0.1224 160 GLU B CG  
3128 C CD  . GLU B 125 ? 0.9519 0.7389 1.0024 0.0415  -0.0837 -0.1331 160 GLU B CD  
3129 O OE1 . GLU B 125 ? 1.0456 0.8188 1.1043 0.0531  -0.0873 -0.1316 160 GLU B OE1 
3130 O OE2 . GLU B 125 ? 1.1817 0.9944 1.2289 0.0464  -0.0752 -0.1425 160 GLU B OE2 
3131 N N   . GLN B 126 ? 0.5158 0.2592 0.5746 -0.0137 -0.1045 -0.0639 161 GLN B N   
3132 C CA  . GLN B 126 ? 0.4462 0.1842 0.4996 -0.0328 -0.1075 -0.0484 161 GLN B CA  
3133 C C   . GLN B 126 ? 0.4711 0.2346 0.5319 -0.0426 -0.1004 -0.0372 161 GLN B C   
3134 O O   . GLN B 126 ? 0.4170 0.1987 0.4861 -0.0324 -0.0938 -0.0362 161 GLN B O   
3135 C CB  . GLN B 126 ? 0.5987 0.3130 0.6484 -0.0301 -0.1155 -0.0404 161 GLN B CB  
3136 C CG  . GLN B 126 ? 0.5748 0.2649 0.6199 -0.0165 -0.1217 -0.0531 161 GLN B CG  
3137 C CD  . GLN B 126 ? 0.6438 0.3185 0.6765 -0.0293 -0.1260 -0.0567 161 GLN B CD  
3138 O OE1 . GLN B 126 ? 0.8205 0.4873 0.8465 -0.0462 -0.1301 -0.0452 161 GLN B OE1 
3139 N NE2 . GLN B 126 ? 0.7105 0.3831 0.7395 -0.0224 -0.1246 -0.0732 161 GLN B NE2 
3140 N N   . LEU B 127 ? 0.3856 0.1578 0.4422 -0.0613 -0.0988 -0.0289 162 LEU B N   
3141 C CA  . LEU B 127 ? 0.3750 0.1719 0.4373 -0.0711 -0.0913 -0.0183 162 LEU B CA  
3142 C C   . LEU B 127 ? 0.3946 0.1862 0.4566 -0.0692 -0.0921 -0.0071 162 LEU B C   
3143 O O   . LEU B 127 ? 0.3850 0.1564 0.4390 -0.0718 -0.0992 -0.0013 162 LEU B O   
3144 C CB  . LEU B 127 ? 0.4542 0.2614 0.5118 -0.0902 -0.0894 -0.0124 162 LEU B CB  
3145 C CG  . LEU B 127 ? 0.4946 0.3061 0.5509 -0.0961 -0.0908 -0.0212 162 LEU B CG  
3146 C CD1 . LEU B 127 ? 0.5068 0.3343 0.5620 -0.1150 -0.0879 -0.0140 162 LEU B CD1 
3147 C CD2 . LEU B 127 ? 0.3397 0.1684 0.4050 -0.0876 -0.0874 -0.0312 162 LEU B CD2 
3148 N N   . ALA B 128 ? 0.3821 0.1917 0.4526 -0.0651 -0.0857 -0.0037 163 ALA B N   
3149 C CA  . ALA B 128 ? 0.3713 0.1786 0.4408 -0.0647 -0.0866 0.0074  163 ALA B CA  
3150 C C   . ALA B 128 ? 0.3738 0.1915 0.4352 -0.0822 -0.0826 0.0190  163 ALA B C   
3151 O O   . ALA B 128 ? 0.3638 0.1741 0.4192 -0.0852 -0.0862 0.0287  163 ALA B O   
3152 C CB  . ALA B 128 ? 0.3215 0.1511 0.3989 -0.0521 -0.0780 0.0062  163 ALA B CB  
3153 N N   . PHE B 129 ? 0.3268 0.1629 0.3884 -0.0932 -0.0756 0.0177  164 PHE B N   
3154 C CA  . PHE B 129 ? 0.3436 0.1928 0.3988 -0.1087 -0.0704 0.0258  164 PHE B CA  
3155 C C   . PHE B 129 ? 0.3710 0.2197 0.4236 -0.1188 -0.0721 0.0228  164 PHE B C   
3156 O O   . PHE B 129 ? 0.3417 0.2131 0.4004 -0.1249 -0.0649 0.0195  164 PHE B O   
3157 C CB  . PHE B 129 ? 0.3118 0.1899 0.3730 -0.1111 -0.0585 0.0265  164 PHE B CB  
3158 C CG  . PHE B 129 ? 0.2827 0.1621 0.3469 -0.1017 -0.0569 0.0286  164 PHE B CG  
3159 C CD1 . PHE B 129 ? 0.2871 0.1632 0.3434 -0.1046 -0.0577 0.0375  164 PHE B CD1 
3160 C CD2 . PHE B 129 ? 0.3368 0.2218 0.4117 -0.0897 -0.0553 0.0218  164 PHE B CD2 
3161 C CE1 . PHE B 129 ? 0.2757 0.1540 0.3351 -0.0967 -0.0570 0.0398  164 PHE B CE1 
3162 C CE2 . PHE B 129 ? 0.3095 0.2001 0.3859 -0.0793 -0.0521 0.0233  164 PHE B CE2 
3163 C CZ  . PHE B 129 ? 0.3178 0.2020 0.3886 -0.0851 -0.0549 0.0332  164 PHE B CZ  
3164 N N   . PRO B 130 ? 0.3770 0.2003 0.4212 -0.1209 -0.0821 0.0241  165 PRO B N   
3165 C CA  . PRO B 130 ? 0.4124 0.2319 0.4538 -0.1299 -0.0853 0.0202  165 PRO B CA  
3166 C C   . PRO B 130 ? 0.3964 0.2375 0.4371 -0.1466 -0.0793 0.0258  165 PRO B C   
3167 O O   . PRO B 130 ? 0.4538 0.3017 0.4962 -0.1548 -0.0797 0.0222  165 PRO B O   
3168 C CB  . PRO B 130 ? 0.4909 0.2757 0.5220 -0.1283 -0.0979 0.0223  165 PRO B CB  
3169 C CG  . PRO B 130 ? 0.4610 0.2394 0.4883 -0.1260 -0.1001 0.0325  165 PRO B CG  
3170 C CD  . PRO B 130 ? 0.3881 0.1850 0.4252 -0.1156 -0.0919 0.0299  165 PRO B CD  
3171 N N   . ASN B 131 ? 0.3806 0.2336 0.4189 -0.1517 -0.0740 0.0339  166 ASN B N   
3172 C CA  . ASN B 131 ? 0.4515 0.3248 0.4882 -0.1668 -0.0685 0.0392  166 ASN B CA  
3173 C C   . ASN B 131 ? 0.3466 0.2550 0.3956 -0.1668 -0.0555 0.0350  166 ASN B C   
3174 O O   . ASN B 131 ? 0.3474 0.2769 0.3977 -0.1777 -0.0496 0.0378  166 ASN B O   
3175 C CB  . ASN B 131 ? 0.4703 0.3338 0.4945 -0.1730 -0.0718 0.0503  166 ASN B CB  
3176 C CG  . ASN B 131 ? 0.4720 0.3022 0.4844 -0.1765 -0.0862 0.0555  166 ASN B CG  
3177 O OD1 . ASN B 131 ? 0.5486 0.3652 0.5613 -0.1767 -0.0921 0.0505  166 ASN B OD1 
3178 N ND2 . ASN B 131 ? 0.5160 0.3320 0.5180 -0.1784 -0.0925 0.0651  166 ASN B ND2 
3179 N N   . ALA B 132 ? 0.3490 0.2642 0.4074 -0.1547 -0.0515 0.0284  167 ALA B N   
3180 C CA  . ALA B 132 ? 0.2954 0.2404 0.3644 -0.1529 -0.0400 0.0257  167 ALA B CA  
3181 C C   . ALA B 132 ? 0.2877 0.2522 0.3706 -0.1521 -0.0376 0.0180  167 ALA B C   
3182 O O   . ALA B 132 ? 0.3045 0.2577 0.3880 -0.1502 -0.0449 0.0135  167 ALA B O   
3183 C CB  . ALA B 132 ? 0.3561 0.2977 0.4259 -0.1409 -0.0373 0.0252  167 ALA B CB  
3184 N N   . VAL B 133 ? 0.2632 0.2579 0.3574 -0.1533 -0.0279 0.0162  168 VAL B N   
3185 C CA  . VAL B 133 ? 0.2446 0.2613 0.3546 -0.1490 -0.0255 0.0094  168 VAL B CA  
3186 C C   . VAL B 133 ? 0.2225 0.2446 0.3379 -0.1376 -0.0206 0.0072  168 VAL B C   
3187 O O   . VAL B 133 ? 0.2186 0.2426 0.3299 -0.1365 -0.0142 0.0101  168 VAL B O   
3188 C CB  . VAL B 133 ? 0.2541 0.3030 0.3759 -0.1568 -0.0191 0.0088  168 VAL B CB  
3189 C CG1 . VAL B 133 ? 0.2668 0.3097 0.3818 -0.1698 -0.0245 0.0124  168 VAL B CG1 
3190 C CG2 . VAL B 133 ? 0.3110 0.3779 0.4344 -0.1571 -0.0083 0.0106  168 VAL B CG2 
3191 N N   . VAL B 134 ? 0.2187 0.2415 0.3413 -0.1276 -0.0242 0.0022  169 VAL B N   
3192 C CA  . VAL B 134 ? 0.1965 0.2222 0.3211 -0.1102 -0.0188 -0.0010 169 VAL B CA  
3193 C C   . VAL B 134 ? 0.1788 0.2340 0.3180 -0.1049 -0.0119 -0.0052 169 VAL B C   
3194 O O   . VAL B 134 ? 0.1833 0.2529 0.3320 -0.1078 -0.0148 -0.0078 169 VAL B O   
3195 C CB  . VAL B 134 ? 0.2541 0.2619 0.3740 -0.0975 -0.0253 -0.0047 169 VAL B CB  
3196 C CG1 . VAL B 134 ? 0.2131 0.2267 0.3348 -0.0825 -0.0198 -0.0067 169 VAL B CG1 
3197 C CG2 . VAL B 134 ? 0.2777 0.2561 0.3855 -0.1000 -0.0326 -0.0017 169 VAL B CG2 
3198 N N   . ARG B 135 ? 0.1683 0.2325 0.3097 -0.0979 -0.0034 -0.0058 170 ARG B N   
3199 C CA  . ARG B 135 ? 0.1917 0.2810 0.3476 -0.0904 0.0028  -0.0103 170 ARG B CA  
3200 C C   . ARG B 135 ? 0.1696 0.2523 0.3240 -0.0741 0.0045  -0.0122 170 ARG B C   
3201 O O   . ARG B 135 ? 0.1496 0.2162 0.2928 -0.0714 0.0060  -0.0100 170 ARG B O   
3202 C CB  . ARG B 135 ? 0.1591 0.2674 0.3194 -0.0988 0.0124  -0.0107 170 ARG B CB  
3203 C CG  . ARG B 135 ? 0.1718 0.2873 0.3314 -0.1184 0.0106  -0.0071 170 ARG B CG  
3204 C CD  . ARG B 135 ? 0.2276 0.3778 0.4009 -0.1250 0.0199  -0.0103 170 ARG B CD  
3205 N NE  . ARG B 135 ? 0.1619 0.3378 0.3558 -0.1152 0.0206  -0.0161 170 ARG B NE  
3206 C CZ  . ARG B 135 ? 0.2153 0.4234 0.4239 -0.1165 0.0279  -0.0196 170 ARG B CZ  
3207 N NH1 . ARG B 135 ? 0.1743 0.3885 0.3748 -0.1250 0.0353  -0.0177 170 ARG B NH1 
3208 N NH2 . ARG B 135 ? 0.1540 0.3864 0.3839 -0.1068 0.0268  -0.0244 170 ARG B NH2 
3209 N N   . ALA B 136 ? 0.1406 0.2354 0.3057 -0.0642 0.0030  -0.0154 171 ALA B N   
3210 C CA  . ALA B 136 ? 0.2015 0.2923 0.3661 -0.0505 0.0050  -0.0164 171 ALA B CA  
3211 C C   . ALA B 136 ? 0.1977 0.3087 0.3788 -0.0424 0.0044  -0.0195 171 ALA B C   
3212 O O   . ALA B 136 ? 0.1478 0.2768 0.3407 -0.0473 0.0021  -0.0207 171 ALA B O   
3213 C CB  . ALA B 136 ? 0.1898 0.2616 0.3429 -0.0445 -0.0009 -0.0143 171 ALA B CB  
3214 N N   . ASP B 137 ? 0.1651 0.2725 0.3471 -0.0302 0.0055  -0.0201 172 ASP B N   
3215 C CA  . ASP B 137 ? 0.1277 0.2526 0.3264 -0.0208 0.0035  -0.0223 172 ASP B CA  
3216 C C   . ASP B 137 ? 0.1275 0.2563 0.3292 -0.0198 -0.0068 -0.0200 172 ASP B C   
3217 O O   . ASP B 137 ? 0.1282 0.2411 0.3163 -0.0204 -0.0120 -0.0173 172 ASP B O   
3218 C CB  . ASP B 137 ? 0.1300 0.2455 0.3277 -0.0081 0.0052  -0.0230 172 ASP B CB  
3219 C CG  . ASP B 137 ? 0.1486 0.2824 0.3662 0.0028  0.0039  -0.0261 172 ASP B CG  
3220 O OD1 . ASP B 137 ? 0.2053 0.3434 0.4285 0.0075  -0.0054 -0.0228 172 ASP B OD1 
3221 O OD2 . ASP B 137 ? 0.1469 0.2929 0.3752 0.0063  0.0117  -0.0320 172 ASP B OD2 
3222 N N   . GLN B 138 ? 0.1374 0.2900 0.3574 -0.0183 -0.0096 -0.0216 173 GLN B N   
3223 C CA  . GLN B 138 ? 0.1497 0.3096 0.3738 -0.0175 -0.0201 -0.0194 173 GLN B CA  
3224 C C   . GLN B 138 ? 0.1317 0.2748 0.3445 -0.0087 -0.0265 -0.0156 173 GLN B C   
3225 O O   . GLN B 138 ? 0.1348 0.2729 0.3384 -0.0118 -0.0340 -0.0137 173 GLN B O   
3226 C CB  . GLN B 138 ? 0.1607 0.3498 0.4092 -0.0118 -0.0222 -0.0210 173 GLN B CB  
3227 C CG  . GLN B 138 ? 0.2122 0.4156 0.4677 -0.0151 -0.0330 -0.0188 173 GLN B CG  
3228 C CD  . GLN B 138 ? 0.4831 0.7122 0.7526 -0.0273 -0.0317 -0.0212 173 GLN B CD  
3229 O OE1 . GLN B 138 ? 0.2820 0.5362 0.5719 -0.0239 -0.0260 -0.0241 173 GLN B OE1 
3230 N NE2 . GLN B 138 ? 0.2595 0.4838 0.5190 -0.0416 -0.0370 -0.0204 173 GLN B NE2 
3231 N N   . LYS B 139 ? 0.1330 0.2690 0.3468 0.0022  -0.0240 -0.0147 174 LYS B N   
3232 C CA  . LYS B 139 ? 0.1382 0.2602 0.3420 0.0093  -0.0311 -0.0096 174 LYS B CA  
3233 C C   . LYS B 139 ? 0.1374 0.2389 0.3189 0.0035  -0.0301 -0.0077 174 LYS B C   
3234 O O   . LYS B 139 ? 0.1417 0.2371 0.3123 0.0038  -0.0367 -0.0039 174 LYS B O   
3235 C CB  . LYS B 139 ? 0.1439 0.2592 0.3528 0.0211  -0.0296 -0.0090 174 LYS B CB  
3236 C CG  . LYS B 139 ? 0.1808 0.3170 0.4141 0.0302  -0.0302 -0.0122 174 LYS B CG  
3237 C CD  . LYS B 139 ? 0.3184 0.4461 0.5557 0.0398  -0.0234 -0.0163 174 LYS B CD  
3238 C CE  . LYS B 139 ? 0.3565 0.5007 0.6044 0.0360  -0.0111 -0.0249 174 LYS B CE  
3239 N NZ  . LYS B 139 ? 0.2269 0.4043 0.4958 0.0325  -0.0102 -0.0283 174 LYS B NZ  
3240 N N   . GLU B 140 ? 0.1331 0.2263 0.3081 -0.0019 -0.0220 -0.0102 175 GLU B N   
3241 C CA  . GLU B 140 ? 0.1324 0.2096 0.2896 -0.0068 -0.0211 -0.0090 175 GLU B CA  
3242 C C   . GLU B 140 ? 0.1470 0.2266 0.2995 -0.0127 -0.0265 -0.0105 175 GLU B C   
3243 O O   . GLU B 140 ? 0.1607 0.2343 0.3016 -0.0120 -0.0306 -0.0093 175 GLU B O   
3244 C CB  . GLU B 140 ? 0.1291 0.1991 0.2828 -0.0117 -0.0128 -0.0107 175 GLU B CB  
3245 C CG  . GLU B 140 ? 0.1309 0.1851 0.2687 -0.0144 -0.0115 -0.0089 175 GLU B CG  
3246 C CD  . GLU B 140 ? 0.2075 0.2525 0.3367 -0.0093 -0.0116 -0.0051 175 GLU B CD  
3247 O OE1 . GLU B 140 ? 0.1399 0.1855 0.2739 -0.0038 -0.0118 -0.0040 175 GLU B OE1 
3248 O OE2 . GLU B 140 ? 0.1346 0.1719 0.2525 -0.0108 -0.0118 -0.0033 175 GLU B OE2 
3249 N N   . ALA B 141 ? 0.1344 0.2235 0.2952 -0.0195 -0.0268 -0.0136 176 ALA B N   
3250 C CA  . ALA B 141 ? 0.1403 0.2283 0.2954 -0.0260 -0.0326 -0.0161 176 ALA B CA  
3251 C C   . ALA B 141 ? 0.1452 0.2415 0.3001 -0.0230 -0.0410 -0.0151 176 ALA B C   
3252 O O   . ALA B 141 ? 0.1570 0.2473 0.2996 -0.0254 -0.0455 -0.0172 176 ALA B O   
3253 C CB  . ALA B 141 ? 0.1422 0.2389 0.3065 -0.0358 -0.0323 -0.0185 176 ALA B CB  
3254 N N   . ASP B 142 ? 0.1437 0.2542 0.3118 -0.0174 -0.0436 -0.0121 177 ASP B N   
3255 C CA  . ASP B 142 ? 0.1861 0.3058 0.3544 -0.0158 -0.0533 -0.0098 177 ASP B CA  
3256 C C   . ASP B 142 ? 0.1552 0.2631 0.3070 -0.0117 -0.0558 -0.0062 177 ASP B C   
3257 O O   . ASP B 142 ? 0.1764 0.2868 0.3187 -0.0143 -0.0630 -0.0057 177 ASP B O   
3258 C CB  . ASP B 142 ? 0.1496 0.2885 0.3385 -0.0098 -0.0570 -0.0069 177 ASP B CB  
3259 C CG  . ASP B 142 ? 0.2416 0.3994 0.4474 -0.0162 -0.0557 -0.0106 177 ASP B CG  
3260 O OD1 . ASP B 142 ? 0.2542 0.4084 0.4533 -0.0273 -0.0550 -0.0142 177 ASP B OD1 
3261 O OD2 . ASP B 142 ? 0.2169 0.3933 0.4429 -0.0104 -0.0557 -0.0098 177 ASP B OD2 
3262 N N   . PHE B 143 ? 0.1920 0.2880 0.3389 -0.0069 -0.0499 -0.0037 178 PHE B N   
3263 C CA  . PHE B 143 ? 0.2070 0.2930 0.3370 -0.0054 -0.0514 0.0002  178 PHE B CA  
3264 C C   . PHE B 143 ? 0.1946 0.2734 0.3095 -0.0106 -0.0482 -0.0048 178 PHE B C   
3265 O O   . PHE B 143 ? 0.2244 0.3050 0.3269 -0.0128 -0.0523 -0.0052 178 PHE B O   
3266 C CB  . PHE B 143 ? 0.1595 0.2351 0.2891 0.0000  -0.0469 0.0046  178 PHE B CB  
3267 C CG  . PHE B 143 ? 0.1699 0.2365 0.2824 -0.0006 -0.0483 0.0098  178 PHE B CG  
3268 C CD1 . PHE B 143 ? 0.1767 0.2450 0.2838 0.0007  -0.0570 0.0169  178 PHE B CD1 
3269 C CD2 . PHE B 143 ? 0.1847 0.2430 0.2862 -0.0034 -0.0414 0.0083  178 PHE B CD2 
3270 C CE1 . PHE B 143 ? 0.2613 0.3228 0.3511 -0.0022 -0.0582 0.0226  178 PHE B CE1 
3271 C CE2 . PHE B 143 ? 0.2143 0.2684 0.3010 -0.0053 -0.0421 0.0133  178 PHE B CE2 
3272 C CZ  . PHE B 143 ? 0.2335 0.2894 0.3135 -0.0055 -0.0502 0.0206  178 PHE B CZ  
3273 N N   . TRP B 144 ? 0.1517 0.2227 0.2672 -0.0123 -0.0410 -0.0088 179 TRP B N   
3274 C CA  . TRP B 144 ? 0.1768 0.2396 0.2793 -0.0141 -0.0380 -0.0129 179 TRP B CA  
3275 C C   . TRP B 144 ? 0.1727 0.2359 0.2706 -0.0184 -0.0418 -0.0203 179 TRP B C   
3276 O O   . TRP B 144 ? 0.1749 0.2346 0.2607 -0.0180 -0.0413 -0.0249 179 TRP B O   
3277 C CB  . TRP B 144 ? 0.1472 0.2002 0.2514 -0.0141 -0.0308 -0.0135 179 TRP B CB  
3278 C CG  . TRP B 144 ? 0.1832 0.2330 0.2859 -0.0108 -0.0270 -0.0073 179 TRP B CG  
3279 C CD1 . TRP B 144 ? 0.1977 0.2454 0.3086 -0.0097 -0.0236 -0.0047 179 TRP B CD1 
3280 C CD2 . TRP B 144 ? 0.2110 0.2594 0.3026 -0.0094 -0.0264 -0.0035 179 TRP B CD2 
3281 N NE1 . TRP B 144 ? 0.1661 0.2079 0.2707 -0.0076 -0.0217 0.0002  179 TRP B NE1 
3282 C CE2 . TRP B 144 ? 0.1926 0.2352 0.2857 -0.0081 -0.0236 0.0018  179 TRP B CE2 
3283 C CE3 . TRP B 144 ? 0.2140 0.2665 0.2940 -0.0099 -0.0275 -0.0047 179 TRP B CE3 
3284 C CZ2 . TRP B 144 ? 0.1515 0.1910 0.2346 -0.0087 -0.0230 0.0074  179 TRP B CZ2 
3285 C CZ3 . TRP B 144 ? 0.2118 0.2650 0.2828 -0.0104 -0.0259 0.0011  179 TRP B CZ3 
3286 C CH2 . TRP B 144 ? 0.2167 0.2627 0.2894 -0.0104 -0.0242 0.0075  179 TRP B CH2 
3287 N N   . LEU B 145 ? 0.1962 0.3221 0.3447 -0.0318 -0.0594 0.0085  180 LEU B N   
3288 C CA  . LEU B 145 ? 0.1890 0.3173 0.3241 -0.0467 -0.0600 0.0036  180 LEU B CA  
3289 C C   . LEU B 145 ? 0.2049 0.3434 0.3245 -0.0566 -0.0698 0.0091  180 LEU B C   
3290 O O   . LEU B 145 ? 0.2079 0.3463 0.3099 -0.0700 -0.0727 0.0026  180 LEU B O   
3291 C CB  . LEU B 145 ? 0.1009 0.2330 0.2398 -0.0490 -0.0569 -0.0028 180 LEU B CB  
3292 C CG  . LEU B 145 ? 0.1456 0.2693 0.2933 -0.0378 -0.0487 -0.0057 180 LEU B CG  
3293 C CD1 . LEU B 145 ? 0.1329 0.2655 0.2858 -0.0427 -0.0454 -0.0072 180 LEU B CD1 
3294 C CD2 . LEU B 145 ? 0.1532 0.2538 0.2908 -0.0344 -0.0414 -0.0113 180 LEU B CD2 
3295 N N   . SER B 146 ? 0.1924 0.3366 0.3155 -0.0509 -0.0764 0.0212  181 SER B N   
3296 C CA  . SER B 146 ? 0.1862 0.3411 0.2920 -0.0569 -0.0881 0.0299  181 SER B CA  
3297 C C   . SER B 146 ? 0.2309 0.3705 0.3013 -0.0637 -0.0796 0.0289  181 SER B C   
3298 O O   . SER B 146 ? 0.2333 0.3633 0.3026 -0.0591 -0.0700 0.0358  181 SER B O   
3299 C CB  . SER B 146 ? 0.2264 0.3876 0.3482 -0.0447 -0.0984 0.0461  181 SER B CB  
3300 O OG  . SER B 146 ? 0.2507 0.4149 0.3487 -0.0481 -0.1078 0.0587  181 SER B OG  
3301 N N   . GLN B 147 ? 0.2707 0.4092 0.3118 -0.0753 -0.0829 0.0195  182 GLN B N   
3302 C CA  . GLN B 147 ? 0.2719 0.3973 0.2719 -0.0789 -0.0751 0.0172  182 GLN B CA  
3303 C C   . GLN B 147 ? 0.2880 0.4210 0.2766 -0.0754 -0.0787 0.0369  182 GLN B C   
3304 O O   . GLN B 147 ? 0.2795 0.4051 0.2491 -0.0736 -0.0641 0.0416  182 GLN B O   
3305 C CB  . GLN B 147 ? 0.3437 0.4632 0.3090 -0.0925 -0.0834 0.0024  182 GLN B CB  
3306 C CG  . GLN B 147 ? 0.3735 0.4744 0.2896 -0.0926 -0.0723 -0.0055 182 GLN B CG  
3307 C CD  . GLN B 147 ? 0.4421 0.5250 0.3590 -0.0815 -0.0487 -0.0134 182 GLN B CD  
3308 O OE1 . GLN B 147 ? 0.5488 0.6206 0.4873 -0.0786 -0.0437 -0.0219 182 GLN B OE1 
3309 N NE2 . GLN B 147 ? 0.4604 0.5438 0.3532 -0.0745 -0.0338 -0.0093 182 GLN B NE2 
3310 N N   . THR B 148 ? 0.2562 0.4052 0.2548 -0.0738 -0.0975 0.0502  183 THR B N   
3311 C CA  . THR B 148 ? 0.3026 0.4514 0.2845 -0.0699 -0.1016 0.0721  183 THR B CA  
3312 C C   . THR B 148 ? 0.2697 0.4047 0.2736 -0.0636 -0.0885 0.0850  183 THR B C   
3313 O O   . THR B 148 ? 0.2950 0.4226 0.2784 -0.0664 -0.0791 0.0996  183 THR B O   
3314 C CB  . THR B 148 ? 0.3325 0.5001 0.3206 -0.0652 -0.1264 0.0849  183 THR B CB  
3315 O OG1 . THR B 148 ? 0.4066 0.5777 0.4392 -0.0526 -0.1314 0.0906  183 THR B OG1 
3316 C CG2 . THR B 148 ? 0.3038 0.4922 0.2815 -0.0755 -0.1416 0.0702  183 THR B CG2 
3317 N N   . ASN B 149 ? 0.2577 0.3898 0.3016 -0.0572 -0.0874 0.0796  184 ASN B N   
3318 C CA  . ASN B 149 ? 0.2497 0.3671 0.3141 -0.0545 -0.0785 0.0890  184 ASN B CA  
3319 C C   . ASN B 149 ? 0.2677 0.3843 0.3231 -0.0615 -0.0573 0.0838  184 ASN B C   
3320 O O   . ASN B 149 ? 0.2470 0.3593 0.3027 -0.0666 -0.0483 0.0986  184 ASN B O   
3321 C CB  . ASN B 149 ? 0.2035 0.3172 0.3060 -0.0452 -0.0825 0.0800  184 ASN B CB  
3322 C CG  . ASN B 149 ? 0.3084 0.4237 0.4244 -0.0331 -0.1005 0.0880  184 ASN B CG  
3323 O OD1 . ASN B 149 ? 0.3130 0.4262 0.4140 -0.0306 -0.1112 0.1051  184 ASN B OD1 
3324 N ND2 . ASN B 149 ? 0.2536 0.3735 0.3962 -0.0229 -0.1033 0.0765  184 ASN B ND2 
3325 N N   . LEU B 150 ? 0.2146 0.3359 0.2621 -0.0616 -0.0490 0.0638  185 LEU B N   
3326 C CA  . LEU B 150 ? 0.2576 0.3816 0.2962 -0.0624 -0.0285 0.0570  185 LEU B CA  
3327 C C   . LEU B 150 ? 0.3536 0.4828 0.3554 -0.0676 -0.0188 0.0686  185 LEU B C   
3328 O O   . LEU B 150 ? 0.3010 0.4394 0.3082 -0.0701 -0.0026 0.0788  185 LEU B O   
3329 C CB  . LEU B 150 ? 0.2227 0.3412 0.2510 -0.0586 -0.0237 0.0339  185 LEU B CB  
3330 C CG  . LEU B 150 ? 0.3187 0.4383 0.3257 -0.0541 -0.0031 0.0247  185 LEU B CG  
3331 C CD1 . LEU B 150 ? 0.3307 0.4664 0.3698 -0.0501 0.0111  0.0322  185 LEU B CD1 
3332 C CD2 . LEU B 150 ? 0.3206 0.4223 0.3105 -0.0485 0.0000  0.0019  185 LEU B CD2 
3333 N N   . ASP B 151 ? 0.3081 0.4352 0.2715 -0.0702 -0.0285 0.0676  186 ASP B N   
3334 C CA  . ASP B 151 ? 0.3683 0.4999 0.2881 -0.0735 -0.0178 0.0775  186 ASP B CA  
3335 C C   . ASP B 151 ? 0.4037 0.5371 0.3262 -0.0785 -0.0183 0.1080  186 ASP B C   
3336 O O   . ASP B 151 ? 0.4804 0.6207 0.3732 -0.0824 -0.0029 0.1210  186 ASP B O   
3337 C CB  . ASP B 151 ? 0.3731 0.5006 0.2449 -0.0758 -0.0304 0.0672  186 ASP B CB  
3338 C CG  . ASP B 151 ? 0.4788 0.5952 0.3404 -0.0742 -0.0279 0.0374  186 ASP B CG  
3339 O OD1 . ASP B 151 ? 0.5483 0.6616 0.4146 -0.0671 -0.0070 0.0267  186 ASP B OD1 
3340 O OD2 . ASP B 151 ? 0.5812 0.6920 0.4305 -0.0804 -0.0466 0.0256  186 ASP B OD2 
3341 N N   . LYS B 152 ? 0.3351 0.4596 0.2904 -0.0780 -0.0338 0.1200  187 LYS B N   
3342 C CA  . LYS B 152 ? 0.4479 0.5626 0.4043 -0.0831 -0.0354 0.1496  187 LYS B CA  
3343 C C   . LYS B 152 ? 0.3906 0.5025 0.3871 -0.0901 -0.0224 0.1563  187 LYS B C   
3344 O O   . LYS B 152 ? 0.3716 0.4717 0.3693 -0.0994 -0.0203 0.1817  187 LYS B O   
3345 C CB  . LYS B 152 ? 0.4971 0.5984 0.4587 -0.0756 -0.0622 0.1597  187 LYS B CB  
3346 C CG  . LYS B 152 ? 0.5274 0.6368 0.4421 -0.0733 -0.0755 0.1642  187 LYS B CG  
3347 C CD  . LYS B 152 ? 0.5710 0.6904 0.4993 -0.0643 -0.0999 0.1515  187 LYS B CD  
3348 C CE  . LYS B 152 ? 0.5638 0.6936 0.4531 -0.0616 -0.1207 0.1621  187 LYS B CE  
3349 N NZ  . LYS B 152 ? 0.6226 0.7439 0.5204 -0.0491 -0.1408 0.1875  187 LYS B NZ  
3350 N N   . ALA B 153 ? 0.3979 0.5205 0.4248 -0.0873 -0.0140 0.1350  188 ALA B N   
3351 C CA  . ALA B 153 ? 0.4036 0.5284 0.4720 -0.0945 -0.0064 0.1385  188 ALA B CA  
3352 C C   . ALA B 153 ? 0.4326 0.5744 0.4949 -0.1088 0.0150  0.1583  188 ALA B C   
3353 O O   . ALA B 153 ? 0.4314 0.5953 0.4658 -0.1064 0.0330  0.1548  188 ALA B O   
3354 C CB  . ALA B 153 ? 0.3142 0.4526 0.4096 -0.0863 -0.0014 0.1125  188 ALA B CB  
3355 N N   . PRO B 154 ? 0.4631 0.5937 0.5478 -0.1243 0.0141  0.1798  189 PRO B N   
3356 C CA  . PRO B 154 ? 0.4410 0.5902 0.5209 -0.1424 0.0356  0.2040  189 PRO B CA  
3357 C C   . PRO B 154 ? 0.5178 0.7061 0.6398 -0.1514 0.0547  0.1978  189 PRO B C   
3358 O O   . PRO B 154 ? 0.6322 0.8169 0.7689 -0.1656 0.0599  0.2091  189 PRO B O   
3359 C CB  . PRO B 154 ? 0.5248 0.6336 0.6070 -0.1567 0.0213  0.2316  189 PRO B CB  
3360 C CG  . PRO B 154 ? 0.6325 0.7169 0.7524 -0.1501 -0.0004 0.2131  189 PRO B CG  
3361 C CD  . PRO B 154 ? 0.4418 0.5387 0.5550 -0.1267 -0.0067 0.1829  189 PRO B CD  
3362 N N   . ASP B 155 ? 0.3969 0.6124 0.5324 -0.1361 0.0615  0.1711  190 ASP B N   
3363 C CA  . ASP B 155 ? 0.3913 0.6484 0.5596 -0.1357 0.0798  0.1615  190 ASP B CA  
3364 C C   . ASP B 155 ? 0.2617 0.5368 0.4390 -0.1141 0.0810  0.1340  190 ASP B C   
3365 O O   . ASP B 155 ? 0.2448 0.4882 0.4123 -0.1023 0.0620  0.1180  190 ASP B O   
3366 C CB  . ASP B 155 ? 0.3244 0.5721 0.5344 -0.1493 0.0695  0.1617  190 ASP B CB  
3367 C CG  . ASP B 155 ? 0.3899 0.6107 0.6211 -0.1431 0.0445  0.1451  190 ASP B CG  
3368 O OD1 . ASP B 155 ? 0.4519 0.6312 0.6729 -0.1471 0.0260  0.1534  190 ASP B OD1 
3369 O OD2 . ASP B 155 ? 0.3402 0.5803 0.5963 -0.1325 0.0433  0.1240  190 ASP B OD2 
3370 N N   . ASP B 156 ? 0.2602 0.5754 0.4529 -0.1045 0.1007  0.1240  191 ASP B N   
3371 C CA  . ASP B 156 ? 0.2358 0.5641 0.4346 -0.0805 0.1028  0.0990  191 ASP B CA  
3372 C C   . ASP B 156 ? 0.2150 0.5290 0.4502 -0.0775 0.0800  0.0857  191 ASP B C   
3373 O O   . ASP B 156 ? 0.1763 0.4707 0.3988 -0.0589 0.0717  0.0660  191 ASP B O   
3374 C CB  . ASP B 156 ? 0.2935 0.6638 0.5007 -0.0665 0.1274  0.0915  191 ASP B CB  
3375 C CG  . ASP B 156 ? 0.3131 0.6924 0.4688 -0.0549 0.1510  0.0915  191 ASP B CG  
3376 O OD1 . ASP B 156 ? 0.4249 0.7700 0.5336 -0.0582 0.1437  0.0941  191 ASP B OD1 
3377 O OD2 . ASP B 156 ? 0.3346 0.7417 0.4901 -0.0404 0.1720  0.0844  191 ASP B OD2 
3378 N N   . GLU B 157 ? 0.2424 0.5474 0.5067 -0.0922 0.0672  0.0892  192 GLU B N   
3379 C CA  . GLU B 157 ? 0.2398 0.5248 0.5236 -0.0867 0.0451  0.0728  192 GLU B CA  
3380 C C   . GLU B 157 ? 0.2025 0.4457 0.4678 -0.0848 0.0266  0.0716  192 GLU B C   
3381 O O   . GLU B 157 ? 0.2353 0.4663 0.4990 -0.0695 0.0164  0.0550  192 GLU B O   
3382 C CB  . GLU B 157 ? 0.3063 0.5916 0.6170 -0.1037 0.0362  0.0747  192 GLU B CB  
3383 C CG  . GLU B 157 ? 0.3779 0.6386 0.6964 -0.0998 0.0126  0.0587  192 GLU B CG  
3384 C CD  . GLU B 157 ? 0.4745 0.7183 0.8070 -0.1213 0.0004  0.0647  192 GLU B CD  
3385 O OE1 . GLU B 157 ? 0.4487 0.7228 0.8062 -0.1352 0.0074  0.0678  192 GLU B OE1 
3386 O OE2 . GLU B 157 ? 0.5296 0.7300 0.8500 -0.1240 -0.0160 0.0659  192 GLU B OE2 
3387 N N   . SER B 158 ? 0.2418 0.4631 0.4916 -0.0986 0.0225  0.0897  193 SER B N   
3388 C CA  . SER B 158 ? 0.2205 0.4045 0.4516 -0.0928 0.0049  0.0870  193 SER B CA  
3389 C C   . SER B 158 ? 0.1752 0.3561 0.3733 -0.0749 0.0092  0.0721  193 SER B C   
3390 O O   . SER B 158 ? 0.2025 0.3656 0.3967 -0.0637 -0.0028 0.0578  193 SER B O   
3391 C CB  . SER B 158 ? 0.2896 0.4482 0.5020 -0.1059 -0.0004 0.1093  193 SER B CB  
3392 O OG  . SER B 158 ? 0.3989 0.5482 0.6343 -0.1231 -0.0047 0.1213  193 SER B OG  
3393 N N   . LYS B 159 ? 0.2043 0.4010 0.3759 -0.0734 0.0268  0.0754  194 LYS B N   
3394 C CA  . LYS B 159 ? 0.1835 0.3710 0.3195 -0.0592 0.0300  0.0593  194 LYS B CA  
3395 C C   . LYS B 159 ? 0.1713 0.3598 0.3220 -0.0441 0.0295  0.0392  194 LYS B C   
3396 O O   . LYS B 159 ? 0.1845 0.3511 0.3156 -0.0359 0.0226  0.0257  194 LYS B O   
3397 C CB  . LYS B 159 ? 0.2168 0.4210 0.3202 -0.0571 0.0510  0.0618  194 LYS B CB  
3398 C CG  . LYS B 159 ? 0.2973 0.4991 0.3733 -0.0702 0.0530  0.0829  194 LYS B CG  
3399 C CD  . LYS B 159 ? 0.4556 0.6650 0.4826 -0.0634 0.0703  0.0782  194 LYS B CD  
3400 C CE  . LYS B 159 ? 0.3894 0.5924 0.3795 -0.0751 0.0686  0.1000  194 LYS B CE  
3401 N NZ  . LYS B 159 ? 0.4628 0.6383 0.4150 -0.0725 0.0482  0.0918  194 LYS B NZ  
3402 N N   . GLY B 160 ? 0.1479 0.3637 0.3327 -0.0410 0.0368  0.0383  195 GLY B N   
3403 C CA  . GLY B 160 ? 0.1646 0.3824 0.3618 -0.0236 0.0354  0.0216  195 GLY B CA  
3404 C C   . GLY B 160 ? 0.2130 0.4064 0.4194 -0.0224 0.0154  0.0151  195 GLY B C   
3405 O O   . GLY B 160 ? 0.1409 0.3195 0.3370 -0.0085 0.0128  0.0022  195 GLY B O   
3406 N N   . PHE B 161 ? 0.1775 0.3636 0.4004 -0.0358 0.0021  0.0242  196 PHE B N   
3407 C CA  . PHE B 161 ? 0.1047 0.2676 0.3309 -0.0318 -0.0151 0.0170  196 PHE B CA  
3408 C C   . PHE B 161 ? 0.1345 0.2751 0.3295 -0.0272 -0.0174 0.0122  196 PHE B C   
3409 O O   . PHE B 161 ? 0.1033 0.2322 0.2928 -0.0179 -0.0218 0.0018  196 PHE B O   
3410 C CB  . PHE B 161 ? 0.1040 0.2495 0.3340 -0.0425 -0.0263 0.0248  196 PHE B CB  
3411 C CG  . PHE B 161 ? 0.1048 0.2544 0.3494 -0.0452 -0.0303 0.0210  196 PHE B CG  
3412 C CD1 . PHE B 161 ? 0.2459 0.4281 0.5067 -0.0475 -0.0206 0.0209  196 PHE B CD1 
3413 C CD2 . PHE B 161 ? 0.2191 0.3435 0.4644 -0.0461 -0.0443 0.0181  196 PHE B CD2 
3414 C CE1 . PHE B 161 ? 0.2477 0.4394 0.5246 -0.0532 -0.0268 0.0179  196 PHE B CE1 
3415 C CE2 . PHE B 161 ? 0.2354 0.3639 0.4952 -0.0518 -0.0504 0.0144  196 PHE B CE2 
3416 C CZ  . PHE B 161 ? 0.2516 0.4151 0.5271 -0.0570 -0.0423 0.0148  196 PHE B CZ  
3417 N N   . PHE B 162 ? 0.1060 0.2428 0.2798 -0.0350 -0.0147 0.0206  197 PHE B N   
3418 C CA  . PHE B 162 ? 0.1117 0.2341 0.2589 -0.0340 -0.0190 0.0155  197 PHE B CA  
3419 C C   . PHE B 162 ? 0.1483 0.2631 0.2753 -0.0263 -0.0100 0.0013  197 PHE B C   
3420 O O   . PHE B 162 ? 0.1620 0.2624 0.2803 -0.0249 -0.0154 -0.0065 197 PHE B O   
3421 C CB  . PHE B 162 ? 0.1344 0.2569 0.2588 -0.0432 -0.0200 0.0266  197 PHE B CB  
3422 C CG  . PHE B 162 ? 0.1360 0.2547 0.2725 -0.0480 -0.0323 0.0413  197 PHE B CG  
3423 C CD1 . PHE B 162 ? 0.1972 0.3094 0.3374 -0.0441 -0.0467 0.0406  197 PHE B CD1 
3424 C CD2 . PHE B 162 ? 0.1532 0.2746 0.2984 -0.0558 -0.0288 0.0566  197 PHE B CD2 
3425 C CE1 . PHE B 162 ? 0.1729 0.2771 0.3228 -0.0433 -0.0584 0.0538  197 PHE B CE1 
3426 C CE2 . PHE B 162 ? 0.2374 0.3446 0.3900 -0.0593 -0.0410 0.0710  197 PHE B CE2 
3427 C CZ  . PHE B 162 ? 0.1562 0.2528 0.3099 -0.0506 -0.0562 0.0687  197 PHE B CZ  
3428 N N   . LYS B 163 ? 0.1830 0.3061 0.3010 -0.0213 0.0045  -0.0014 198 LYS B N   
3429 C CA  . LYS B 163 ? 0.1539 0.2611 0.2481 -0.0103 0.0131  -0.0157 198 LYS B CA  
3430 C C   . LYS B 163 ? 0.1694 0.2672 0.2781 0.0009  0.0094  -0.0227 198 LYS B C   
3431 O O   . LYS B 163 ? 0.1555 0.2261 0.2428 0.0041  0.0085  -0.0314 198 LYS B O   
3432 C CB  . LYS B 163 ? 0.2030 0.3252 0.2879 -0.0008 0.0313  -0.0178 198 LYS B CB  
3433 C CG  . LYS B 163 ? 0.3053 0.4332 0.3623 -0.0099 0.0382  -0.0120 198 LYS B CG  
3434 C CD  . LYS B 163 ? 0.2750 0.4164 0.3157 0.0041  0.0598  -0.0179 198 LYS B CD  
3435 C CE  . LYS B 163 ? 0.4381 0.6036 0.4659 -0.0050 0.0711  -0.0044 198 LYS B CE  
3436 N NZ  . LYS B 163 ? 0.5281 0.7046 0.5275 0.0112  0.0947  -0.0134 198 LYS B NZ  
3437 N N   . GLY B 164 ? 0.1196 0.2383 0.2617 0.0061  0.0069  -0.0186 199 GLY B N   
3438 C CA  . GLY B 164 ? 0.1205 0.2327 0.2732 0.0179  0.0011  -0.0240 199 GLY B CA  
3439 C C   . GLY B 164 ? 0.1509 0.2425 0.2955 0.0127  -0.0091 -0.0249 199 GLY B C   
3440 O O   . GLY B 164 ? 0.2486 0.3200 0.3790 0.0204  -0.0088 -0.0299 199 GLY B O   
3441 N N   . ALA B 165 ? 0.1489 0.2456 0.3018 0.0005  -0.0174 -0.0187 200 ALA B N   
3442 C CA  . ALA B 165 ? 0.1744 0.2610 0.3231 -0.0027 -0.0247 -0.0192 200 ALA B CA  
3443 C C   . ALA B 165 ? 0.1523 0.2212 0.2743 -0.0098 -0.0209 -0.0227 200 ALA B C   
3444 O O   . ALA B 165 ? 0.1352 0.1924 0.2504 -0.0102 -0.0213 -0.0247 200 ALA B O   
3445 C CB  . ALA B 165 ? 0.1193 0.2161 0.2822 -0.0098 -0.0340 -0.0119 200 ALA B CB  
3446 N N   . MET B 166 ? 0.1721 0.2385 0.2772 -0.0176 -0.0177 -0.0232 201 MET B N   
3447 C CA  . MET B 166 ? 0.1890 0.2353 0.2663 -0.0278 -0.0171 -0.0291 201 MET B CA  
3448 C C   . MET B 166 ? 0.2279 0.2429 0.2849 -0.0195 -0.0091 -0.0377 201 MET B C   
3449 O O   . MET B 166 ? 0.1999 0.1939 0.2448 -0.0276 -0.0108 -0.0396 201 MET B O   
3450 C CB  . MET B 166 ? 0.2359 0.2850 0.2935 -0.0351 -0.0162 -0.0296 201 MET B CB  
3451 C CG  . MET B 166 ? 0.2300 0.3028 0.3007 -0.0440 -0.0269 -0.0186 201 MET B CG  
3452 S SD  . MET B 166 ? 0.3067 0.3832 0.3470 -0.0507 -0.0255 -0.0161 201 MET B SD  
3453 C CE  . MET B 166 ? 0.2373 0.3377 0.2987 -0.0562 -0.0414 0.0008  201 MET B CE  
3454 N N   . ALA B 167 ? 0.1877 0.2008 0.2432 -0.0026 -0.0004 -0.0411 202 ALA B N   
3455 C CA  . ALA B 167 ? 0.2733 0.2538 0.3081 0.0113  0.0066  -0.0485 202 ALA B CA  
3456 C C   . ALA B 167 ? 0.2733 0.2446 0.3160 0.0160  0.0026  -0.0439 202 ALA B C   
3457 O O   . ALA B 167 ? 0.2618 0.1943 0.2795 0.0181  0.0052  -0.0463 202 ALA B O   
3458 C CB  . ALA B 167 ? 0.2561 0.2495 0.2964 0.0330  0.0165  -0.0516 202 ALA B CB  
3459 N N   . SER B 168 ? 0.2087 0.2108 0.2814 0.0171  -0.0039 -0.0370 203 SER B N   
3460 C CA  . SER B 168 ? 0.2220 0.2193 0.2983 0.0245  -0.0071 -0.0332 203 SER B CA  
3461 C C   . SER B 168 ? 0.1958 0.1874 0.2669 0.0081  -0.0091 -0.0286 203 SER B C   
3462 O O   . SER B 168 ? 0.2702 0.2425 0.3275 0.0106  -0.0066 -0.0249 203 SER B O   
3463 C CB  . SER B 168 ? 0.2445 0.2737 0.3501 0.0344  -0.0140 -0.0313 203 SER B CB  
3464 O OG  . SER B 168 ? 0.1414 0.1848 0.2585 0.0473  -0.0118 -0.0340 203 SER B OG  
3465 N N   . LEU B 169 ? 0.1860 0.1976 0.2689 -0.0077 -0.0133 -0.0271 204 LEU B N   
3466 C CA  . LEU B 169 ? 0.2691 0.2887 0.3557 -0.0218 -0.0147 -0.0221 204 LEU B CA  
3467 C C   . LEU B 169 ? 0.1905 0.1956 0.2613 -0.0442 -0.0146 -0.0232 204 LEU B C   
3468 O O   . LEU B 169 ? 0.2135 0.2194 0.2843 -0.0578 -0.0128 -0.0181 204 LEU B O   
3469 C CB  . LEU B 169 ? 0.2518 0.3083 0.3658 -0.0223 -0.0216 -0.0188 204 LEU B CB  
3470 C CG  . LEU B 169 ? 0.3820 0.4525 0.5086 -0.0088 -0.0220 -0.0169 204 LEU B CG  
3471 C CD1 . LEU B 169 ? 0.3190 0.4183 0.4668 -0.0110 -0.0277 -0.0144 204 LEU B CD1 
3472 C CD2 . LEU B 169 ? 0.2287 0.2894 0.3412 -0.0124 -0.0140 -0.0125 204 LEU B CD2 
3473 N N   . ASN B 170 ? 0.2014 0.1997 0.2610 -0.0505 -0.0172 -0.0293 205 ASN B N   
3474 C CA  . ASN B 170 ? 0.2251 0.2120 0.2691 -0.0742 -0.0214 -0.0327 205 ASN B CA  
3475 C C   . ASN B 170 ? 0.2539 0.1953 0.2714 -0.0846 -0.0162 -0.0348 205 ASN B C   
3476 O O   . ASN B 170 ? 0.2744 0.2146 0.2900 -0.1106 -0.0207 -0.0336 205 ASN B O   
3477 C CB  . ASN B 170 ? 0.2745 0.2570 0.3015 -0.0753 -0.0247 -0.0407 205 ASN B CB  
3478 C CG  . ASN B 170 ? 0.2416 0.2662 0.2901 -0.0780 -0.0337 -0.0348 205 ASN B CG  
3479 O OD1 . ASN B 170 ? 0.3075 0.3639 0.3845 -0.0798 -0.0390 -0.0263 205 ASN B OD1 
3480 N ND2 . ASN B 170 ? 0.2675 0.2913 0.2989 -0.0775 -0.0354 -0.0385 205 ASN B ND2 
3481 N N   . PRO B 171 ? 0.3068 0.2107 0.3048 -0.0670 -0.0082 -0.0364 206 PRO B N   
3482 C CA  . PRO B 171 ? 0.3554 0.2102 0.3270 -0.0767 -0.0036 -0.0341 206 PRO B CA  
3483 C C   . PRO B 171 ? 0.4067 0.2803 0.3946 -0.0917 -0.0014 -0.0203 206 PRO B C   
3484 O O   . PRO B 171 ? 0.3652 0.2115 0.3388 -0.1165 0.0000  -0.0162 206 PRO B O   
3485 C CB  . PRO B 171 ? 0.3598 0.1834 0.3144 -0.0456 0.0033  -0.0353 206 PRO B CB  
3486 C CG  . PRO B 171 ? 0.3729 0.2165 0.3345 -0.0282 0.0029  -0.0447 206 PRO B CG  
3487 C CD  . PRO B 171 ? 0.2650 0.1667 0.2618 -0.0383 -0.0036 -0.0404 206 PRO B CD  
3488 N N   . TYR B 172 ? 0.3103 0.2293 0.3267 -0.0778 -0.0002 -0.0131 207 TYR B N   
3489 C CA  . TYR B 172 ? 0.2840 0.2287 0.3155 -0.0883 0.0046  -0.0008 207 TYR B CA  
3490 C C   . TYR B 172 ? 0.3073 0.2952 0.3653 -0.1136 -0.0008 0.0006  207 TYR B C   
3491 O O   . TYR B 172 ? 0.3005 0.2956 0.3632 -0.1378 0.0034  0.0093  207 TYR B O   
3492 C CB  . TYR B 172 ? 0.2310 0.2054 0.2780 -0.0617 0.0068  0.0026  207 TYR B CB  
3493 C CG  . TYR B 172 ? 0.2488 0.1883 0.2716 -0.0383 0.0102  0.0037  207 TYR B CG  
3494 C CD1 . TYR B 172 ? 0.2901 0.2176 0.3092 -0.0186 0.0054  -0.0054 207 TYR B CD1 
3495 C CD2 . TYR B 172 ? 0.2756 0.2001 0.2805 -0.0345 0.0181  0.0154  207 TYR B CD2 
3496 C CE1 . TYR B 172 ? 0.3165 0.2206 0.3185 0.0055  0.0062  -0.0040 207 TYR B CE1 
3497 C CE2 . TYR B 172 ? 0.3451 0.2398 0.3263 -0.0100 0.0182  0.0176  207 TYR B CE2 
3498 C CZ  . TYR B 172 ? 0.3412 0.2275 0.3232 0.0105  0.0111  0.0072  207 TYR B CZ  
3499 O OH  . TYR B 172 ? 0.4056 0.2708 0.3694 0.0369  0.0089  0.0096  207 TYR B OH  
3500 N N   . VAL B 173 ? 0.2541 0.2724 0.3301 -0.1094 -0.0106 -0.0063 208 VAL B N   
3501 C CA  . VAL B 173 ? 0.2378 0.2992 0.3383 -0.1304 -0.0193 -0.0048 208 VAL B CA  
3502 C C   . VAL B 173 ? 0.3066 0.3419 0.3900 -0.1618 -0.0229 -0.0074 208 VAL B C   
3503 O O   . VAL B 173 ? 0.2678 0.3283 0.3685 -0.1749 -0.0222 -0.0008 208 VAL B O   
3504 C CB  . VAL B 173 ? 0.2270 0.3109 0.3378 -0.1194 -0.0307 -0.0107 208 VAL B CB  
3505 C CG1 . VAL B 173 ? 0.2385 0.3583 0.3678 -0.1266 -0.0397 -0.0090 208 VAL B CG1 
3506 C CG2 . VAL B 173 ? 0.1949 0.2964 0.3217 -0.0901 -0.0284 -0.0085 208 VAL B CG2 
3507 N N   . LYS B 174 ? 0.3025 0.2824 0.3490 -0.1654 -0.0255 -0.0185 209 LYS B N   
3508 C CA  . LYS B 174 ? 0.3805 0.3286 0.4063 -0.1848 -0.0300 -0.0237 209 LYS B CA  
3509 C C   . LYS B 174 ? 0.3839 0.3024 0.4010 -0.2000 -0.0206 -0.0141 209 LYS B C   
3510 O O   . LYS B 174 ? 0.4245 0.3336 0.4384 -0.2206 -0.0248 -0.0147 209 LYS B O   
3511 C CB  . LYS B 174 ? 0.4682 0.3609 0.4519 -0.1797 -0.0335 -0.0399 209 LYS B CB  
3512 C CG  . LYS B 174 ? 0.5242 0.4421 0.5079 -0.1737 -0.0438 -0.0492 209 LYS B CG  
3513 C CD  . LYS B 174 ? 0.5980 0.4607 0.5360 -0.1636 -0.0418 -0.0657 209 LYS B CD  
3514 C CE  . LYS B 174 ? 0.7438 0.6322 0.6766 -0.1575 -0.0490 -0.0730 209 LYS B CE  
3515 N NZ  . LYS B 174 ? 0.8894 0.7469 0.7936 -0.1302 -0.0380 -0.0826 209 LYS B NZ  
3516 N N   . ALA B 175 ? 0.3756 0.2993 0.4317 -0.1399 -0.0652 -0.0522 210 ALA B N   
3517 C CA  . ALA B 175 ? 0.4259 0.3375 0.4824 -0.1475 -0.0638 -0.0463 210 ALA B CA  
3518 C C   . ALA B 175 ? 0.3562 0.2926 0.4257 -0.1555 -0.0587 -0.0379 210 ALA B C   
3519 O O   . ALA B 175 ? 0.3990 0.3279 0.4679 -0.1628 -0.0567 -0.0316 210 ALA B O   
3520 C CB  . ALA B 175 ? 0.3937 0.2822 0.4422 -0.1412 -0.0618 -0.0418 210 ALA B CB  
3521 N N   . GLY B 176 ? 0.3095 0.2749 0.3902 -0.1538 -0.0568 -0.0377 211 GLY B N   
3522 C CA  . GLY B 176 ? 0.3158 0.3064 0.4105 -0.1589 -0.0513 -0.0311 211 GLY B CA  
3523 C C   . GLY B 176 ? 0.3539 0.3463 0.4488 -0.1560 -0.0433 -0.0231 211 GLY B C   
3524 O O   . GLY B 176 ? 0.2766 0.2820 0.3785 -0.1623 -0.0380 -0.0175 211 GLY B O   
3525 N N   . LYS B 177 ? 0.2889 0.2693 0.3761 -0.1470 -0.0422 -0.0228 212 LYS B N   
3526 C CA  . LYS B 177 ? 0.2949 0.2739 0.3801 -0.1445 -0.0358 -0.0157 212 LYS B CA  
3527 C C   . LYS B 177 ? 0.2528 0.2514 0.3460 -0.1359 -0.0314 -0.0152 212 LYS B C   
3528 O O   . LYS B 177 ? 0.2816 0.2785 0.3725 -0.1327 -0.0268 -0.0107 212 LYS B O   
3529 C CB  . LYS B 177 ? 0.2873 0.2346 0.3577 -0.1411 -0.0386 -0.0142 212 LYS B CB  
3530 C CG  . LYS B 177 ? 0.3431 0.2685 0.4046 -0.1500 -0.0421 -0.0116 212 LYS B CG  
3531 C CD  . LYS B 177 ? 0.4365 0.3297 0.4859 -0.1435 -0.0484 -0.0147 212 LYS B CD  
3532 C CE  . LYS B 177 ? 0.5029 0.3726 0.5426 -0.1506 -0.0513 -0.0085 212 LYS B CE  
3533 N NZ  . LYS B 177 ? 0.4559 0.3329 0.4934 -0.1539 -0.0459 0.0021  212 LYS B NZ  
3534 N N   . PHE B 178 ? 0.2214 0.2381 0.3236 -0.1323 -0.0334 -0.0195 213 PHE B N   
3535 C CA  . PHE B 178 ? 0.1986 0.2344 0.3097 -0.1242 -0.0296 -0.0186 213 PHE B CA  
3536 C C   . PHE B 178 ? 0.1890 0.2538 0.3164 -0.1253 -0.0258 -0.0174 213 PHE B C   
3537 O O   . PHE B 178 ? 0.2060 0.2833 0.3411 -0.1285 -0.0299 -0.0201 213 PHE B O   
3538 C CB  . PHE B 178 ? 0.1926 0.2286 0.3015 -0.1146 -0.0336 -0.0230 213 PHE B CB  
3539 C CG  . PHE B 178 ? 0.1727 0.2255 0.2901 -0.1026 -0.0292 -0.0212 213 PHE B CG  
3540 C CD1 . PHE B 178 ? 0.1971 0.2441 0.3129 -0.0956 -0.0236 -0.0180 213 PHE B CD1 
3541 C CD2 . PHE B 178 ? 0.1651 0.2383 0.2922 -0.0990 -0.0319 -0.0223 213 PHE B CD2 
3542 C CE1 . PHE B 178 ? 0.2318 0.2918 0.3556 -0.0853 -0.0202 -0.0166 213 PHE B CE1 
3543 C CE2 . PHE B 178 ? 0.1509 0.2359 0.2856 -0.0880 -0.0290 -0.0200 213 PHE B CE2 
3544 C CZ  . PHE B 178 ? 0.1422 0.2200 0.2755 -0.0815 -0.0228 -0.0174 213 PHE B CZ  
3545 N N   . LYS B 179 ? 0.1894 0.2649 0.3223 -0.1222 -0.0186 -0.0142 214 LYS B N   
3546 C CA  . LYS B 179 ? 0.2255 0.3281 0.3744 -0.1221 -0.0142 -0.0138 214 LYS B CA  
3547 C C   . LYS B 179 ? 0.2257 0.3437 0.3844 -0.1111 -0.0109 -0.0148 214 LYS B C   
3548 O O   . LYS B 179 ? 0.1511 0.2688 0.3079 -0.1083 -0.0044 -0.0134 214 LYS B O   
3549 C CB  . LYS B 179 ? 0.2485 0.3514 0.3945 -0.1302 -0.0076 -0.0101 214 LYS B CB  
3550 C CG  . LYS B 179 ? 0.1817 0.3137 0.3444 -0.1312 -0.0026 -0.0109 214 LYS B CG  
3551 C CD  . LYS B 179 ? 0.3619 0.4955 0.5195 -0.1413 0.0046  -0.0073 214 LYS B CD  
3552 C CE  . LYS B 179 ? 0.3660 0.5309 0.5415 -0.1423 0.0104  -0.0094 214 LYS B CE  
3553 N NZ  . LYS B 179 ? 0.4302 0.5989 0.5993 -0.1533 0.0186  -0.0061 214 LYS B NZ  
3554 N N   . PRO B 180 ? 0.1719 0.3033 0.3410 -0.1045 -0.0155 -0.0174 215 PRO B N   
3555 C CA  . PRO B 180 ? 0.1285 0.2704 0.3071 -0.0927 -0.0131 -0.0186 215 PRO B CA  
3556 C C   . PRO B 180 ? 0.1334 0.2968 0.3262 -0.0896 -0.0076 -0.0190 215 PRO B C   
3557 O O   . PRO B 180 ? 0.1331 0.3079 0.3315 -0.0964 -0.0060 -0.0186 215 PRO B O   
3558 C CB  . PRO B 180 ? 0.1628 0.3075 0.3438 -0.0856 -0.0215 -0.0191 215 PRO B CB  
3559 C CG  . PRO B 180 ? 0.2596 0.4136 0.4445 -0.0962 -0.0269 -0.0209 215 PRO B CG  
3560 C CD  . PRO B 180 ? 0.1598 0.2947 0.3309 -0.1069 -0.0242 -0.0196 215 PRO B CD  
3561 N N   . PHE B 181 ? 0.1267 0.2945 0.3262 -0.0790 -0.0043 -0.0207 216 PHE B N   
3562 C CA  . PHE B 181 ? 0.1429 0.3310 0.3573 -0.0727 0.0004  -0.0234 216 PHE B CA  
3563 C C   . PHE B 181 ? 0.1058 0.2987 0.3324 -0.0590 -0.0048 -0.0248 216 PHE B C   
3564 O O   . PHE B 181 ? 0.1580 0.3367 0.3783 -0.0553 -0.0107 -0.0222 216 PHE B O   
3565 C CB  . PHE B 181 ? 0.1131 0.2977 0.3214 -0.0736 0.0099  -0.0250 216 PHE B CB  
3566 C CG  . PHE B 181 ? 0.1068 0.2725 0.3068 -0.0683 0.0103  -0.0250 216 PHE B CG  
3567 C CD1 . PHE B 181 ? 0.1171 0.2816 0.3244 -0.0547 0.0089  -0.0267 216 PHE B CD1 
3568 C CD2 . PHE B 181 ? 0.1202 0.2638 0.3007 -0.0748 0.0104  -0.0211 216 PHE B CD2 
3569 C CE1 . PHE B 181 ? 0.1281 0.2710 0.3230 -0.0494 0.0083  -0.0244 216 PHE B CE1 
3570 C CE2 . PHE B 181 ? 0.1141 0.2380 0.2835 -0.0682 0.0096  -0.0192 216 PHE B CE2 
3571 C CZ  . PHE B 181 ? 0.1503 0.2744 0.3269 -0.0561 0.0089  -0.0209 216 PHE B CZ  
3572 N N   . SER B 182 ? 0.1028 0.3131 0.3452 -0.0506 -0.0029 -0.0281 217 SER B N   
3573 C CA  . SER B 182 ? 0.1490 0.3605 0.4032 -0.0365 -0.0089 -0.0286 217 SER B CA  
3574 C C   . SER B 182 ? 0.2154 0.4292 0.4773 -0.0271 -0.0026 -0.0337 217 SER B C   
3575 O O   . SER B 182 ? 0.1632 0.3944 0.4343 -0.0262 0.0030  -0.0385 217 SER B O   
3576 C CB  . SER B 182 ? 0.2125 0.4421 0.4809 -0.0329 -0.0171 -0.0279 217 SER B CB  
3577 O OG  . SER B 182 ? 0.2791 0.5071 0.5580 -0.0187 -0.0238 -0.0271 217 SER B OG  
3578 N N   . GLY B 183 ? 0.1070 0.3035 0.3657 -0.0201 -0.0035 -0.0329 218 GLY B N   
3579 C CA  . GLY B 183 ? 0.1106 0.3082 0.3772 -0.0109 0.0013  -0.0391 218 GLY B CA  
3580 C C   . GLY B 183 ? 0.1872 0.3899 0.4468 -0.0180 0.0127  -0.0448 218 GLY B C   
3581 O O   . GLY B 183 ? 0.1677 0.3679 0.4140 -0.0305 0.0164  -0.0421 218 GLY B O   
3582 N N   . ASN B 184 ? 0.1642 0.3739 0.4325 -0.0100 0.0179  -0.0530 219 ASN B N   
3583 C CA  . ASN B 184 ? 0.1204 0.3370 0.3820 -0.0159 0.0291  -0.0597 219 ASN B CA  
3584 C C   . ASN B 184 ? 0.2302 0.4632 0.4872 -0.0284 0.0346  -0.0581 219 ASN B C   
3585 O O   . ASN B 184 ? 0.1273 0.3789 0.3973 -0.0264 0.0340  -0.0594 219 ASN B O   
3586 C CB  . ASN B 184 ? 0.1370 0.3624 0.4112 -0.0038 0.0330  -0.0706 219 ASN B CB  
3587 C CG  . ASN B 184 ? 0.1693 0.3749 0.4475 0.0081  0.0274  -0.0724 219 ASN B CG  
3588 O OD1 . ASN B 184 ? 0.1953 0.3790 0.4617 0.0061  0.0218  -0.0643 219 ASN B OD1 
3589 N ND2 . ASN B 184 ? 0.2709 0.4798 0.5602 0.0200  0.0286  -0.0819 219 ASN B ND2 
3590 N N   . THR B 185 ? 0.1235 0.3493 0.3628 -0.0417 0.0394  -0.0548 220 THR B N   
3591 C CA  . THR B 185 ? 0.1701 0.4055 0.4030 -0.0552 0.0426  -0.0505 220 THR B CA  
3592 C C   . THR B 185 ? 0.1744 0.4050 0.3884 -0.0672 0.0511  -0.0501 220 THR B C   
3593 O O   . THR B 185 ? 0.1897 0.4014 0.3901 -0.0695 0.0501  -0.0479 220 THR B O   
3594 C CB  . THR B 185 ? 0.1299 0.3533 0.3570 -0.0618 0.0338  -0.0415 220 THR B CB  
3595 O OG1 . THR B 185 ? 0.1707 0.3971 0.4119 -0.0517 0.0250  -0.0410 220 THR B OG1 
3596 C CG2 . THR B 185 ? 0.1853 0.4171 0.4083 -0.0757 0.0361  -0.0374 220 THR B CG2 
3597 N N   . ASP B 186 ? 0.1689 0.4160 0.3813 -0.0758 0.0588  -0.0512 221 ASP B N   
3598 C CA  . ASP B 186 ? 0.2122 0.4527 0.4028 -0.0896 0.0655  -0.0481 221 ASP B CA  
3599 C C   . ASP B 186 ? 0.2682 0.4892 0.4450 -0.1013 0.0588  -0.0368 221 ASP B C   
3600 O O   . ASP B 186 ? 0.2399 0.4655 0.4238 -0.1052 0.0549  -0.0330 221 ASP B O   
3601 C CB  . ASP B 186 ? 0.2232 0.4865 0.4146 -0.0962 0.0760  -0.0520 221 ASP B CB  
3602 C CG  . ASP B 186 ? 0.1740 0.4554 0.3761 -0.0849 0.0837  -0.0648 221 ASP B CG  
3603 O OD1 . ASP B 186 ? 0.2156 0.4890 0.4225 -0.0730 0.0809  -0.0704 221 ASP B OD1 
3604 O OD2 . ASP B 186 ? 0.2010 0.5049 0.4084 -0.0878 0.0922  -0.0698 221 ASP B OD2 
3605 N N   . LEU B 187 ? 0.1866 0.3849 0.3447 -0.1061 0.0566  -0.0321 222 LEU B N   
3606 C CA  . LEU B 187 ? 0.2187 0.3948 0.3604 -0.1171 0.0506  -0.0221 222 LEU B CA  
3607 C C   . LEU B 187 ? 0.2381 0.4121 0.3601 -0.1314 0.0569  -0.0174 222 LEU B C   
3608 O O   . LEU B 187 ? 0.3394 0.5351 0.4647 -0.1348 0.0659  -0.0213 222 LEU B O   
3609 C CB  . LEU B 187 ? 0.2340 0.3853 0.3682 -0.1127 0.0429  -0.0194 222 LEU B CB  
3610 C CG  . LEU B 187 ? 0.1425 0.2970 0.2950 -0.0988 0.0374  -0.0236 222 LEU B CG  
3611 C CD1 . LEU B 187 ? 0.1465 0.2734 0.2885 -0.0905 0.0294  -0.0199 222 LEU B CD1 
3612 C CD2 . LEU B 187 ? 0.1746 0.3384 0.3392 -0.0988 0.0326  -0.0221 222 LEU B CD2 
3613 N N   . VAL B 188 ? 0.3142 0.4618 0.4161 -0.1399 0.0514  -0.0085 223 VAL B N   
3614 C CA  . VAL B 188 ? 0.2794 0.4184 0.3578 -0.1531 0.0551  -0.0020 223 VAL B CA  
3615 C C   . VAL B 188 ? 0.2960 0.4551 0.3711 -0.1531 0.0663  -0.0089 223 VAL B C   
3616 O O   . VAL B 188 ? 0.3010 0.4653 0.3834 -0.1430 0.0679  -0.0167 223 VAL B O   
3617 C CB  . VAL B 188 ? 0.4125 0.5179 0.4710 -0.1558 0.0461  0.0063  223 VAL B CB  
3618 C CG1 . VAL B 188 ? 0.4955 0.5939 0.5293 -0.1654 0.0498  0.0111  223 VAL B CG1 
3619 C CG2 . VAL B 188 ? 0.3042 0.3885 0.3579 -0.1610 0.0373  0.0141  223 VAL B CG2 
3620 N N   . PRO B 189 ? 0.3644 0.5362 0.4292 -0.1639 0.0746  -0.0074 224 PRO B N   
3621 C CA  . PRO B 189 ? 0.2612 0.4504 0.3181 -0.1647 0.0856  -0.0146 224 PRO B CA  
3622 C C   . PRO B 189 ? 0.2608 0.4339 0.3010 -0.1632 0.0836  -0.0145 224 PRO B C   
3623 O O   . PRO B 189 ? 0.3470 0.4937 0.3640 -0.1715 0.0766  -0.0034 224 PRO B O   
3624 C CB  . PRO B 189 ? 0.3787 0.5715 0.4172 -0.1807 0.0912  -0.0077 224 PRO B CB  
3625 C CG  . PRO B 189 ? 0.2896 0.4852 0.3440 -0.1835 0.0873  -0.0038 224 PRO B CG  
3626 C CD  . PRO B 189 ? 0.3095 0.4814 0.3703 -0.1761 0.0746  -0.0001 224 PRO B CD  
3627 N N   . GLY B 190 ? 0.2990 0.4825 0.3498 -0.1488 0.0867  -0.0266 225 GLY B N   
3628 C CA  . GLY B 190 ? 0.2495 0.4106 0.2854 -0.1391 0.0798  -0.0276 225 GLY B CA  
3629 C C   . GLY B 190 ? 0.2264 0.3725 0.2783 -0.1226 0.0693  -0.0297 225 GLY B C   
3630 O O   . GLY B 190 ? 0.2525 0.3849 0.2976 -0.1133 0.0645  -0.0329 225 GLY B O   
3631 N N   . ILE B 191 ? 0.2251 0.3732 0.2969 -0.1193 0.0653  -0.0279 226 ILE B N   
3632 C CA  . ILE B 191 ? 0.1901 0.3244 0.2751 -0.1051 0.0558  -0.0288 226 ILE B CA  
3633 C C   . ILE B 191 ? 0.2403 0.3953 0.3532 -0.0977 0.0579  -0.0352 226 ILE B C   
3634 O O   . ILE B 191 ? 0.1903 0.3602 0.3120 -0.1059 0.0608  -0.0334 226 ILE B O   
3635 C CB  . ILE B 191 ? 0.1904 0.2985 0.2662 -0.1084 0.0452  -0.0178 226 ILE B CB  
3636 C CG1 . ILE B 191 ? 0.2606 0.3485 0.3093 -0.1169 0.0419  -0.0100 226 ILE B CG1 
3637 C CG2 . ILE B 191 ? 0.2168 0.3125 0.3039 -0.0943 0.0371  -0.0192 226 ILE B CG2 
3638 C CD1 . ILE B 191 ? 0.2725 0.3345 0.3126 -0.1206 0.0314  0.0004  226 ILE B CD1 
3639 N N   . LYS B 192 ? 0.2034 0.3588 0.3302 -0.0827 0.0554  -0.0421 227 LYS B N   
3640 C CA  . LYS B 192 ? 0.1915 0.3627 0.3441 -0.0738 0.0545  -0.0468 227 LYS B CA  
3641 C C   . LYS B 192 ? 0.1664 0.3190 0.3243 -0.0635 0.0443  -0.0433 227 LYS B C   
3642 O O   . LYS B 192 ? 0.1821 0.3156 0.3306 -0.0585 0.0402  -0.0422 227 LYS B O   
3643 C CB  . LYS B 192 ? 0.1914 0.3840 0.3607 -0.0639 0.0613  -0.0595 227 LYS B CB  
3644 C CG  . LYS B 192 ? 0.2537 0.4720 0.4222 -0.0710 0.0742  -0.0671 227 LYS B CG  
3645 C CD  . LYS B 192 ? 0.3496 0.5563 0.4893 -0.0816 0.0779  -0.0640 227 LYS B CD  
3646 C CE  . LYS B 192 ? 0.4384 0.6347 0.5713 -0.0711 0.0775  -0.0723 227 LYS B CE  
3647 N NZ  . LYS B 192 ? 0.2756 0.4545 0.3786 -0.0794 0.0769  -0.0679 227 LYS B NZ  
3648 N N   . ALA B 193 ? 0.1593 0.3197 0.3332 -0.0604 0.0403  -0.0419 228 ALA B N   
3649 C CA  . ALA B 193 ? 0.1462 0.2943 0.3271 -0.0500 0.0319  -0.0395 228 ALA B CA  
3650 C C   . ALA B 193 ? 0.1111 0.2675 0.3088 -0.0369 0.0322  -0.0470 228 ALA B C   
3651 O O   . ALA B 193 ? 0.1248 0.3037 0.3389 -0.0341 0.0364  -0.0537 228 ALA B O   
3652 C CB  . ALA B 193 ? 0.1089 0.2607 0.2968 -0.0528 0.0265  -0.0346 228 ALA B CB  
3653 N N   . LEU B 194 ? 0.1627 0.3009 0.3578 -0.0288 0.0273  -0.0459 229 LEU B N   
3654 C CA  . LEU B 194 ? 0.1583 0.2972 0.3678 -0.0162 0.0254  -0.0518 229 LEU B CA  
3655 C C   . LEU B 194 ? 0.1476 0.2719 0.3604 -0.0104 0.0164  -0.0445 229 LEU B C   
3656 O O   . LEU B 194 ? 0.1041 0.2103 0.3045 -0.0127 0.0134  -0.0387 229 LEU B O   
3657 C CB  . LEU B 194 ? 0.1669 0.2964 0.3683 -0.0137 0.0286  -0.0583 229 LEU B CB  
3658 C CG  . LEU B 194 ? 0.1426 0.2686 0.3575 -0.0011 0.0263  -0.0657 229 LEU B CG  
3659 C CD1 . LEU B 194 ? 0.1758 0.3242 0.4064 0.0049  0.0326  -0.0776 229 LEU B CD1 
3660 C CD2 . LEU B 194 ? 0.2030 0.3088 0.4056 -0.0003 0.0250  -0.0682 229 LEU B CD2 
3661 N N   . ALA B 195 ? 0.1896 0.3232 0.4193 -0.0028 0.0120  -0.0447 230 ALA B N   
3662 C CA  . ALA B 195 ? 0.1010 0.2232 0.3325 0.0015  0.0033  -0.0365 230 ALA B CA  
3663 C C   . ALA B 195 ? 0.1216 0.2231 0.3495 0.0069  0.0003  -0.0350 230 ALA B C   
3664 O O   . ALA B 195 ? 0.1970 0.2967 0.4337 0.0143  0.0008  -0.0419 230 ALA B O   
3665 C CB  . ALA B 195 ? 0.1554 0.2922 0.4055 0.0089  -0.0019 -0.0370 230 ALA B CB  
3666 N N   . SER B 196 ? 0.1425 0.2288 0.3581 0.0027  -0.0025 -0.0269 231 SER B N   
3667 C CA  . SER B 196 ? 0.1131 0.1808 0.3262 0.0057  -0.0056 -0.0240 231 SER B CA  
3668 C C   . SER B 196 ? 0.1315 0.1908 0.3395 0.0043  -0.0109 -0.0133 231 SER B C   
3669 O O   . SER B 196 ? 0.1651 0.2137 0.3632 -0.0001 -0.0104 -0.0087 231 SER B O   
3670 C CB  . SER B 196 ? 0.1220 0.1816 0.3242 0.0008  -0.0014 -0.0273 231 SER B CB  
3671 O OG  . SER B 196 ? 0.2011 0.2603 0.3908 -0.0072 0.0004  -0.0231 231 SER B OG  
3672 N N   . HIS B 197 ? 0.1456 0.2120 0.3599 0.0076  -0.0158 -0.0095 232 HIS B N   
3673 C CA  . HIS B 197 ? 0.1572 0.2184 0.3636 0.0053  -0.0204 0.0004  232 HIS B CA  
3674 C C   . HIS B 197 ? 0.1707 0.2147 0.3754 0.0072  -0.0239 0.0072  232 HIS B C   
3675 O O   . HIS B 197 ? 0.2035 0.2395 0.4176 0.0129  -0.0262 0.0050  232 HIS B O   
3676 C CB  . HIS B 197 ? 0.1468 0.2199 0.3606 0.0089  -0.0266 0.0028  232 HIS B CB  
3677 C CG  . HIS B 197 ? 0.1090 0.2010 0.3286 0.0066  -0.0238 -0.0040 232 HIS B CG  
3678 N ND1 . HIS B 197 ? 0.1189 0.2145 0.3306 -0.0011 -0.0167 -0.0083 232 HIS B ND1 
3679 C CD2 . HIS B 197 ? 0.1100 0.2191 0.3429 0.0102  -0.0276 -0.0063 232 HIS B CD2 
3680 C CE1 . HIS B 197 ? 0.1379 0.2512 0.3572 -0.0033 -0.0156 -0.0128 232 HIS B CE1 
3681 N NE2 . HIS B 197 ? 0.1077 0.2310 0.3410 0.0035  -0.0219 -0.0122 232 HIS B NE2 
3682 N N   . GLY B 198 ? 0.1303 0.1689 0.3230 0.0019  -0.0241 0.0152  233 GLY B N   
3683 C CA  . GLY B 198 ? 0.2367 0.2615 0.4258 0.0009  -0.0269 0.0240  233 GLY B CA  
3684 C C   . GLY B 198 ? 0.1753 0.1969 0.3529 -0.0067 -0.0217 0.0272  233 GLY B C   
3685 O O   . GLY B 198 ? 0.2162 0.2356 0.3852 -0.0100 -0.0228 0.0357  233 GLY B O   
3686 N N   . HIS B 199 ? 0.1209 0.1443 0.2976 -0.0094 -0.0161 0.0205  234 HIS B N   
3687 C CA  . HIS B 199 ? 0.2085 0.2329 0.3763 -0.0151 -0.0116 0.0221  234 HIS B CA  
3688 C C   . HIS B 199 ? 0.1686 0.2010 0.3262 -0.0169 -0.0112 0.0239  234 HIS B C   
3689 O O   . HIS B 199 ? 0.1482 0.1809 0.2975 -0.0203 -0.0092 0.0287  234 HIS B O   
3690 C CB  . HIS B 199 ? 0.1100 0.1352 0.2787 -0.0164 -0.0078 0.0145  234 HIS B CB  
3691 C CG  . HIS B 199 ? 0.1328 0.1596 0.2958 -0.0202 -0.0041 0.0148  234 HIS B CG  
3692 N ND1 . HIS B 199 ? 0.1811 0.2058 0.3453 -0.0231 -0.0023 0.0193  234 HIS B ND1 
3693 C CD2 . HIS B 199 ? 0.1003 0.1308 0.2579 -0.0213 -0.0019 0.0105  234 HIS B CD2 
3694 C CE1 . HIS B 199 ? 0.1780 0.2074 0.3391 -0.0248 0.0012  0.0168  234 HIS B CE1 
3695 N NE2 . HIS B 199 ? 0.1009 0.1321 0.2575 -0.0232 0.0009  0.0115  234 HIS B NE2 
3696 N N   . THR B 200 ? 0.1390 0.1785 0.2973 -0.0153 -0.0129 0.0197  235 THR B N   
3697 C CA  . THR B 200 ? 0.1667 0.2132 0.3167 -0.0169 -0.0147 0.0205  235 THR B CA  
3698 C C   . THR B 200 ? 0.1213 0.1747 0.2797 -0.0131 -0.0202 0.0198  235 THR B C   
3699 O O   . THR B 200 ? 0.1809 0.2350 0.3510 -0.0094 -0.0203 0.0160  235 THR B O   
3700 C CB  . THR B 200 ? 0.1540 0.2036 0.2978 -0.0204 -0.0112 0.0141  235 THR B CB  
3701 O OG1 . THR B 200 ? 0.1395 0.1911 0.2905 -0.0201 -0.0101 0.0083  235 THR B OG1 
3702 C CG2 . THR B 200 ? 0.1315 0.1760 0.2695 -0.0225 -0.0061 0.0134  235 THR B CG2 
3703 N N   . PRO B 201 ? 0.1640 0.2242 0.3173 -0.0139 -0.0248 0.0221  236 PRO B N   
3704 C CA  . PRO B 201 ? 0.1457 0.2152 0.3103 -0.0096 -0.0312 0.0216  236 PRO B CA  
3705 C C   . PRO B 201 ? 0.1749 0.2541 0.3507 -0.0095 -0.0282 0.0128  236 PRO B C   
3706 O O   . PRO B 201 ? 0.1325 0.2201 0.3229 -0.0043 -0.0313 0.0106  236 PRO B O   
3707 C CB  . PRO B 201 ? 0.2363 0.3119 0.3903 -0.0124 -0.0366 0.0247  236 PRO B CB  
3708 C CG  . PRO B 201 ? 0.1749 0.2410 0.3126 -0.0156 -0.0341 0.0307  236 PRO B CG  
3709 C CD  . PRO B 201 ? 0.1566 0.2168 0.2942 -0.0178 -0.0254 0.0258  236 PRO B CD  
3710 N N   . GLY B 202 ? 0.1234 0.2024 0.2929 -0.0153 -0.0225 0.0079  237 GLY B N   
3711 C CA  . GLY B 202 ? 0.1162 0.2041 0.2933 -0.0176 -0.0191 0.0010  237 GLY B CA  
3712 C C   . GLY B 202 ? 0.1608 0.2416 0.3363 -0.0189 -0.0126 -0.0027 237 GLY B C   
3713 O O   . GLY B 202 ? 0.1070 0.1929 0.2826 -0.0235 -0.0089 -0.0073 237 GLY B O   
3714 N N   . HIS B 203 ? 0.1473 0.2166 0.3209 -0.0159 -0.0116 -0.0003 238 HIS B N   
3715 C CA  . HIS B 203 ? 0.1071 0.1691 0.2778 -0.0174 -0.0070 -0.0035 238 HIS B CA  
3716 C C   . HIS B 203 ? 0.1378 0.2074 0.3158 -0.0168 -0.0040 -0.0099 238 HIS B C   
3717 O O   . HIS B 203 ? 0.1220 0.1982 0.3117 -0.0113 -0.0052 -0.0123 238 HIS B O   
3718 C CB  . HIS B 203 ? 0.0972 0.1481 0.2686 -0.0144 -0.0075 -0.0004 238 HIS B CB  
3719 C CG  . HIS B 203 ? 0.0952 0.1395 0.2637 -0.0163 -0.0044 -0.0037 238 HIS B CG  
3720 N ND1 . HIS B 203 ? 0.0962 0.1407 0.2693 -0.0146 -0.0029 -0.0093 238 HIS B ND1 
3721 C CD2 . HIS B 203 ? 0.0941 0.1318 0.2558 -0.0192 -0.0031 -0.0026 238 HIS B CD2 
3722 C CE1 . HIS B 203 ? 0.1064 0.1443 0.2739 -0.0172 -0.0015 -0.0109 238 HIS B CE1 
3723 N NE2 . HIS B 203 ? 0.1019 0.1360 0.2637 -0.0197 -0.0020 -0.0067 238 HIS B NE2 
3724 N N   . THR B 204 ? 0.1166 0.1849 0.2870 -0.0224 -0.0002 -0.0128 239 THR B N   
3725 C CA  . THR B 204 ? 0.1070 0.1849 0.2806 -0.0244 0.0040  -0.0186 239 THR B CA  
3726 C C   . THR B 204 ? 0.0976 0.1676 0.2628 -0.0265 0.0070  -0.0212 239 THR B C   
3727 O O   . THR B 204 ? 0.1256 0.1846 0.2802 -0.0301 0.0059  -0.0182 239 THR B O   
3728 C CB  . THR B 204 ? 0.1487 0.2371 0.3203 -0.0317 0.0052  -0.0188 239 THR B CB  
3729 O OG1 . THR B 204 ? 0.0936 0.1914 0.2743 -0.0293 0.0012  -0.0172 239 THR B OG1 
3730 C CG2 . THR B 204 ? 0.0983 0.2007 0.2743 -0.0348 0.0111  -0.0246 239 THR B CG2 
3731 N N   . THR B 205 ? 0.1309 0.2066 0.3010 -0.0238 0.0102  -0.0275 240 THR B N   
3732 C CA  . THR B 205 ? 0.1649 0.2356 0.3252 -0.0267 0.0130  -0.0311 240 THR B CA  
3733 C C   . THR B 205 ? 0.1500 0.2313 0.3032 -0.0346 0.0183  -0.0331 240 THR B C   
3734 O O   . THR B 205 ? 0.1737 0.2711 0.3357 -0.0354 0.0216  -0.0357 240 THR B O   
3735 C CB  . THR B 205 ? 0.1410 0.2109 0.3087 -0.0196 0.0137  -0.0382 240 THR B CB  
3736 O OG1 . THR B 205 ? 0.1802 0.2374 0.3526 -0.0147 0.0083  -0.0346 240 THR B OG1 
3737 C CG2 . THR B 205 ? 0.1209 0.1877 0.2766 -0.0229 0.0167  -0.0438 240 THR B CG2 
3738 N N   . TYR B 206 ? 0.1674 0.2403 0.3048 -0.0412 0.0187  -0.0312 241 TYR B N   
3739 C CA  . TYR B 206 ? 0.1629 0.2437 0.2905 -0.0509 0.0237  -0.0311 241 TYR B CA  
3740 C C   . TYR B 206 ? 0.1775 0.2601 0.2952 -0.0523 0.0278  -0.0368 241 TYR B C   
3741 O O   . TYR B 206 ? 0.1651 0.2340 0.2730 -0.0512 0.0240  -0.0362 241 TYR B O   
3742 C CB  . TYR B 206 ? 0.1460 0.2143 0.2607 -0.0588 0.0198  -0.0229 241 TYR B CB  
3743 C CG  . TYR B 206 ? 0.1268 0.1966 0.2501 -0.0585 0.0170  -0.0197 241 TYR B CG  
3744 C CD1 . TYR B 206 ? 0.2026 0.2878 0.3326 -0.0641 0.0203  -0.0204 241 TYR B CD1 
3745 C CD2 . TYR B 206 ? 0.1603 0.2189 0.2863 -0.0527 0.0114  -0.0168 241 TYR B CD2 
3746 C CE1 . TYR B 206 ? 0.1202 0.2069 0.2572 -0.0640 0.0165  -0.0182 241 TYR B CE1 
3747 C CE2 . TYR B 206 ? 0.1133 0.1739 0.2450 -0.0525 0.0089  -0.0148 241 TYR B CE2 
3748 C CZ  . TYR B 206 ? 0.1146 0.1885 0.2512 -0.0579 0.0108  -0.0156 241 TYR B CZ  
3749 O OH  . TYR B 206 ? 0.1365 0.2116 0.2773 -0.0580 0.0071  -0.0141 241 TYR B OH  
3750 N N   . VAL B 207 ? 0.2182 0.3190 0.3390 -0.0544 0.0357  -0.0433 242 VAL B N   
3751 C CA  . VAL B 207 ? 0.2102 0.3148 0.3222 -0.0543 0.0406  -0.0513 242 VAL B CA  
3752 C C   . VAL B 207 ? 0.2290 0.3393 0.3224 -0.0674 0.0462  -0.0483 242 VAL B C   
3753 O O   . VAL B 207 ? 0.1862 0.3136 0.2844 -0.0739 0.0526  -0.0481 242 VAL B O   
3754 C CB  . VAL B 207 ? 0.1997 0.3216 0.3294 -0.0453 0.0464  -0.0633 242 VAL B CB  
3755 C CG1 . VAL B 207 ? 0.2093 0.3342 0.3275 -0.0450 0.0518  -0.0737 242 VAL B CG1 
3756 C CG2 . VAL B 207 ? 0.2003 0.3145 0.3477 -0.0333 0.0398  -0.0641 242 VAL B CG2 
3757 N N   . VAL B 208 ? 0.2142 0.3106 0.2864 -0.0718 0.0433  -0.0458 243 VAL B N   
3758 C CA  . VAL B 208 ? 0.2422 0.3380 0.2914 -0.0852 0.0463  -0.0402 243 VAL B CA  
3759 C C   . VAL B 208 ? 0.2234 0.3312 0.2612 -0.0867 0.0543  -0.0501 243 VAL B C   
3760 O O   . VAL B 208 ? 0.2561 0.3570 0.2915 -0.0792 0.0513  -0.0573 243 VAL B O   
3761 C CB  . VAL B 208 ? 0.2663 0.3369 0.2985 -0.0885 0.0354  -0.0296 243 VAL B CB  
3762 C CG1 . VAL B 208 ? 0.2366 0.3031 0.2444 -0.1027 0.0367  -0.0215 243 VAL B CG1 
3763 C CG2 . VAL B 208 ? 0.2214 0.2803 0.2668 -0.0841 0.0278  -0.0229 243 VAL B CG2 
3764 N N   . GLU B 209 ? 0.2371 0.3627 0.2667 -0.0972 0.0645  -0.0509 244 GLU B N   
3765 C CA  . GLU B 209 ? 0.2548 0.3962 0.2741 -0.0986 0.0744  -0.0623 244 GLU B CA  
3766 C C   . GLU B 209 ? 0.2912 0.4382 0.2844 -0.1161 0.0809  -0.0552 244 GLU B C   
3767 O O   . GLU B 209 ? 0.2796 0.4368 0.2765 -0.1263 0.0856  -0.0482 244 GLU B O   
3768 C CB  . GLU B 209 ? 0.3137 0.4818 0.3592 -0.0900 0.0844  -0.0761 244 GLU B CB  
3769 C CG  . GLU B 209 ? 0.3128 0.4738 0.3789 -0.0726 0.0785  -0.0852 244 GLU B CG  
3770 C CD  . GLU B 209 ? 0.3594 0.5450 0.4490 -0.0625 0.0875  -0.1006 244 GLU B CD  
3771 O OE1 . GLU B 209 ? 0.4443 0.6423 0.5581 -0.0584 0.0880  -0.0996 244 GLU B OE1 
3772 O OE2 . GLU B 209 ? 0.3585 0.5518 0.4422 -0.0587 0.0939  -0.1142 244 GLU B OE2 
3773 N N   . SER B 210 ? 0.3021 0.4425 0.2682 -0.1204 0.0809  -0.0568 245 SER B N   
3774 C CA  . SER B 210 ? 0.3311 0.4766 0.2681 -0.1380 0.0873  -0.0497 245 SER B CA  
3775 C C   . SER B 210 ? 0.3612 0.5138 0.2759 -0.1386 0.0932  -0.0607 245 SER B C   
3776 O O   . SER B 210 ? 0.3588 0.4933 0.2632 -0.1318 0.0833  -0.0633 245 SER B O   
3777 C CB  . SER B 210 ? 0.3586 0.4759 0.2749 -0.1476 0.0747  -0.0307 245 SER B CB  
3778 O OG  . SER B 210 ? 0.4412 0.5605 0.3258 -0.1652 0.0798  -0.0226 245 SER B OG  
3779 N N   . GLN B 211 ? 0.3725 0.5524 0.2795 -0.1477 0.1093  -0.0675 246 GLN B N   
3780 C CA  . GLN B 211 ? 0.4007 0.5912 0.2827 -0.1506 0.1176  -0.0791 246 GLN B CA  
3781 C C   . GLN B 211 ? 0.3918 0.5802 0.2865 -0.1323 0.1149  -0.0977 246 GLN B C   
3782 O O   . GLN B 211 ? 0.4293 0.6091 0.3001 -0.1319 0.1118  -0.1041 246 GLN B O   
3783 C CB  . GLN B 211 ? 0.4321 0.6020 0.2716 -0.1646 0.1100  -0.0652 246 GLN B CB  
3784 C CG  . GLN B 211 ? 0.4578 0.6255 0.2809 -0.1842 0.1117  -0.0457 246 GLN B CG  
3785 C CD  . GLN B 211 ? 0.6454 0.8470 0.4616 -0.1981 0.1322  -0.0502 246 GLN B CD  
3786 O OE1 . GLN B 211 ? 0.6137 0.8341 0.4209 -0.1960 0.1426  -0.0651 246 GLN B OE1 
3787 N NE2 . GLN B 211 ? 0.6172 0.8230 0.4427 -0.2091 0.1343  -0.0376 246 GLN B NE2 
3788 N N   . GLY B 212 ? 0.3630 0.5578 0.2948 -0.1175 0.1148  -0.1060 247 GLY B N   
3789 C CA  . GLY B 212 ? 0.3826 0.5729 0.3294 -0.1003 0.1114  -0.1226 247 GLY B CA  
3790 C C   . GLY B 212 ? 0.4211 0.5794 0.3683 -0.0930 0.0934  -0.1165 247 GLY B C   
3791 O O   . GLY B 212 ? 0.4174 0.5685 0.3730 -0.0810 0.0894  -0.1294 247 GLY B O   
3792 N N   . GLN B 213 ? 0.3610 0.5004 0.3005 -0.0999 0.0827  -0.0978 248 GLN B N   
3793 C CA  . GLN B 213 ? 0.3256 0.4382 0.2686 -0.0933 0.0663  -0.0915 248 GLN B CA  
3794 C C   . GLN B 213 ? 0.3081 0.4173 0.2811 -0.0865 0.0623  -0.0844 248 GLN B C   
3795 O O   . GLN B 213 ? 0.3223 0.4372 0.2985 -0.0937 0.0653  -0.0742 248 GLN B O   
3796 C CB  . GLN B 213 ? 0.4118 0.5055 0.3256 -0.1042 0.0561  -0.0765 248 GLN B CB  
3797 C CG  . GLN B 213 ? 0.4637 0.5613 0.3429 -0.1134 0.0598  -0.0809 248 GLN B CG  
3798 C CD  . GLN B 213 ? 0.5641 0.6558 0.4399 -0.1048 0.0550  -0.0957 248 GLN B CD  
3799 O OE1 . GLN B 213 ? 0.7111 0.7827 0.5833 -0.1018 0.0403  -0.0914 248 GLN B OE1 
3800 N NE2 . GLN B 213 ? 0.6772 0.7869 0.5558 -0.1003 0.0671  -0.1143 248 GLN B NE2 
3801 N N   . LYS B 214 ? 0.2848 0.3849 0.2787 -0.0737 0.0556  -0.0900 249 LYS B N   
3802 C CA  . LYS B 214 ? 0.2550 0.3532 0.2772 -0.0659 0.0523  -0.0854 249 LYS B CA  
3803 C C   . LYS B 214 ? 0.2969 0.3722 0.3220 -0.0628 0.0385  -0.0760 249 LYS B C   
3804 O O   . LYS B 214 ? 0.3221 0.3848 0.3392 -0.0606 0.0313  -0.0793 249 LYS B O   
3805 C CB  . LYS B 214 ? 0.2662 0.3744 0.3129 -0.0532 0.0566  -0.0995 249 LYS B CB  
3806 C CG  . LYS B 214 ? 0.3408 0.4545 0.4142 -0.0472 0.0563  -0.0950 249 LYS B CG  
3807 C CD  . LYS B 214 ? 0.3297 0.4466 0.4268 -0.0331 0.0565  -0.1072 249 LYS B CD  
3808 C CE  . LYS B 214 ? 0.4240 0.5631 0.5251 -0.0298 0.0683  -0.1228 249 LYS B CE  
3809 N NZ  . LYS B 214 ? 0.4409 0.6026 0.5614 -0.0291 0.0750  -0.1217 249 LYS B NZ  
3810 N N   . LEU B 215 ? 0.2437 0.3155 0.2816 -0.0625 0.0353  -0.0656 250 LEU B N   
3811 C CA  . LEU B 215 ? 0.2421 0.2962 0.2866 -0.0590 0.0242  -0.0570 250 LEU B CA  
3812 C C   . LEU B 215 ? 0.2338 0.2919 0.3020 -0.0528 0.0248  -0.0547 250 LEU B C   
3813 O O   . LEU B 215 ? 0.2337 0.3001 0.3051 -0.0570 0.0288  -0.0498 250 LEU B O   
3814 C CB  . LEU B 215 ? 0.2535 0.2959 0.2805 -0.0676 0.0180  -0.0444 250 LEU B CB  
3815 C CG  . LEU B 215 ? 0.2032 0.2313 0.2400 -0.0635 0.0082  -0.0360 250 LEU B CG  
3816 C CD1 . LEU B 215 ? 0.2088 0.2288 0.2521 -0.0566 0.0011  -0.0408 250 LEU B CD1 
3817 C CD2 . LEU B 215 ? 0.2577 0.2738 0.2794 -0.0705 0.0019  -0.0244 250 LEU B CD2 
3818 N N   . ALA B 216 ? 0.2378 0.2898 0.3221 -0.0439 0.0205  -0.0576 251 ALA B N   
3819 C CA  . ALA B 216 ? 0.2229 0.2775 0.3271 -0.0382 0.0201  -0.0544 251 ALA B CA  
3820 C C   . ALA B 216 ? 0.1789 0.2202 0.2844 -0.0385 0.0123  -0.0444 251 ALA B C   
3821 O O   . ALA B 216 ? 0.1839 0.2147 0.2906 -0.0359 0.0065  -0.0443 251 ALA B O   
3822 C CB  . ALA B 216 ? 0.2041 0.2603 0.3251 -0.0285 0.0205  -0.0630 251 ALA B CB  
3823 N N   . LEU B 217 ? 0.1441 0.1869 0.2499 -0.0418 0.0125  -0.0369 252 LEU B N   
3824 C CA  . LEU B 217 ? 0.1694 0.2017 0.2772 -0.0412 0.0064  -0.0291 252 LEU B CA  
3825 C C   . LEU B 217 ? 0.1328 0.1676 0.2575 -0.0348 0.0061  -0.0286 252 LEU B C   
3826 O O   . LEU B 217 ? 0.1602 0.2034 0.2911 -0.0346 0.0088  -0.0277 252 LEU B O   
3827 C CB  . LEU B 217 ? 0.2137 0.2434 0.3120 -0.0479 0.0058  -0.0223 252 LEU B CB  
3828 C CG  . LEU B 217 ? 0.1748 0.2009 0.2541 -0.0561 0.0058  -0.0202 252 LEU B CG  
3829 C CD1 . LEU B 217 ? 0.2325 0.2533 0.3051 -0.0626 0.0044  -0.0129 252 LEU B CD1 
3830 C CD2 . LEU B 217 ? 0.2509 0.2655 0.3213 -0.0550 -0.0010 -0.0196 252 LEU B CD2 
3831 N N   . LEU B 218 ? 0.1493 0.2669 0.2310 -0.0357 -0.0072 0.0079  253 LEU B N   
3832 C CA  . LEU B 218 ? 0.1504 0.2542 0.2350 -0.0309 -0.0024 0.0047  253 LEU B CA  
3833 C C   . LEU B 218 ? 0.1507 0.2328 0.2333 -0.0387 -0.0031 0.0077  253 LEU B C   
3834 O O   . LEU B 218 ? 0.1636 0.2363 0.2472 -0.0368 0.0002  0.0076  253 LEU B O   
3835 C CB  . LEU B 218 ? 0.1557 0.2488 0.2461 -0.0217 0.0016  -0.0086 253 LEU B CB  
3836 C CG  . LEU B 218 ? 0.1574 0.2677 0.2483 -0.0128 0.0027  -0.0165 253 LEU B CG  
3837 C CD1 . LEU B 218 ? 0.1638 0.2566 0.2602 -0.0053 0.0051  -0.0299 253 LEU B CD1 
3838 C CD2 . LEU B 218 ? 0.1725 0.3074 0.2634 -0.0058 0.0051  -0.0119 253 LEU B CD2 
3839 N N   . GLY B 219 ? 0.1564 0.2312 0.2359 -0.0472 -0.0076 0.0107  254 GLY B N   
3840 C CA  . GLY B 219 ? 0.1545 0.2093 0.2310 -0.0533 -0.0075 0.0108  254 GLY B CA  
3841 C C   . GLY B 219 ? 0.1924 0.2307 0.2738 -0.0489 -0.0015 0.0013  254 GLY B C   
3842 O O   . GLY B 219 ? 0.1694 0.2034 0.2573 -0.0454 -0.0006 -0.0063 254 GLY B O   
3843 N N   . ASP B 220 ? 0.1582 0.1889 0.2369 -0.0500 0.0020  0.0028  255 ASP B N   
3844 C CA  . ASP B 220 ? 0.1601 0.1769 0.2433 -0.0480 0.0072  -0.0036 255 ASP B CA  
3845 C C   . ASP B 220 ? 0.1609 0.1805 0.2494 -0.0413 0.0097  -0.0034 255 ASP B C   
3846 O O   . ASP B 220 ? 0.1651 0.1753 0.2553 -0.0421 0.0128  -0.0031 255 ASP B O   
3847 C CB  . ASP B 220 ? 0.1665 0.1723 0.2425 -0.0551 0.0093  -0.0023 255 ASP B CB  
3848 C CG  . ASP B 220 ? 0.1687 0.1649 0.2448 -0.0584 0.0087  -0.0082 255 ASP B CG  
3849 O OD1 . ASP B 220 ? 0.1643 0.1635 0.2463 -0.0560 0.0053  -0.0105 255 ASP B OD1 
3850 O OD2 . ASP B 220 ? 0.1763 0.1631 0.2466 -0.0629 0.0113  -0.0105 255 ASP B OD2 
3851 N N   . LEU B 221 ? 0.1843 0.2170 0.2758 -0.0344 0.0082  -0.0035 256 LEU B N   
3852 C CA  . LEU B 221 ? 0.2658 0.2977 0.3645 -0.0260 0.0100  -0.0060 256 LEU B CA  
3853 C C   . LEU B 221 ? 0.2941 0.3109 0.4003 -0.0237 0.0115  -0.0152 256 LEU B C   
3854 O O   . LEU B 221 ? 0.3671 0.3760 0.4797 -0.0191 0.0122  -0.0163 256 LEU B O   
3855 C CB  . LEU B 221 ? 0.2296 0.2795 0.3305 -0.0172 0.0090  -0.0073 256 LEU B CB  
3856 C CG  . LEU B 221 ? 0.3170 0.3830 0.4165 -0.0157 0.0083  0.0032  256 LEU B CG  
3857 C CD1 . LEU B 221 ? 0.2816 0.3704 0.3841 -0.0060 0.0087  0.0013  256 LEU B CD1 
3858 C CD2 . LEU B 221 ? 0.2161 0.2711 0.3209 -0.0135 0.0094  0.0073  256 LEU B CD2 
3859 N N   . ILE B 222 ? 0.2267 0.2394 0.3335 -0.0269 0.0110  -0.0210 257 ILE B N   
3860 C CA  . ILE B 222 ? 0.2345 0.2342 0.3492 -0.0272 0.0120  -0.0281 257 ILE B CA  
3861 C C   . ILE B 222 ? 0.3017 0.2966 0.4161 -0.0343 0.0133  -0.0282 257 ILE B C   
3862 O O   . ILE B 222 ? 0.3044 0.3053 0.4145 -0.0367 0.0113  -0.0268 257 ILE B O   
3863 C CB  . ILE B 222 ? 0.2709 0.2732 0.3899 -0.0211 0.0093  -0.0375 257 ILE B CB  
3864 C CG1 . ILE B 222 ? 0.2479 0.2355 0.3761 -0.0224 0.0092  -0.0435 257 ILE B CG1 
3865 C CG2 . ILE B 222 ? 0.3564 0.3711 0.4713 -0.0226 0.0065  -0.0389 257 ILE B CG2 
3866 C CD1 . ILE B 222 ? 0.3367 0.3239 0.4680 -0.0174 0.0055  -0.0541 257 ILE B CD1 
3867 N N   . LEU B 223 ? 0.2427 0.2275 0.3624 -0.0376 0.0165  -0.0290 258 LEU B N   
3868 C CA  . LEU B 223 ? 0.2413 0.2232 0.3621 -0.0429 0.0194  -0.0299 258 LEU B CA  
3869 C C   . LEU B 223 ? 0.2806 0.2592 0.4133 -0.0432 0.0196  -0.0358 258 LEU B C   
3870 O O   . LEU B 223 ? 0.2225 0.2025 0.3591 -0.0447 0.0203  -0.0383 258 LEU B O   
3871 C CB  . LEU B 223 ? 0.2385 0.2168 0.3541 -0.0481 0.0243  -0.0246 258 LEU B CB  
3872 C CG  . LEU B 223 ? 0.2996 0.2817 0.4025 -0.0499 0.0233  -0.0178 258 LEU B CG  
3873 C CD1 . LEU B 223 ? 0.2693 0.2492 0.3660 -0.0557 0.0272  -0.0116 258 LEU B CD1 
3874 C CD2 . LEU B 223 ? 0.2300 0.2148 0.3261 -0.0517 0.0209  -0.0189 258 LEU B CD2 
3875 N N   . VAL B 224 ? 0.1841 0.1582 0.3241 -0.0417 0.0183  -0.0380 259 VAL B N   
3876 C CA  . VAL B 224 ? 0.1686 0.1398 0.3208 -0.0436 0.0176  -0.0423 259 VAL B CA  
3877 C C   . VAL B 224 ? 0.2848 0.2534 0.4399 -0.0395 0.0117  -0.0481 259 VAL B C   
3878 O O   . VAL B 224 ? 0.1996 0.1597 0.3570 -0.0382 0.0102  -0.0483 259 VAL B O   
3879 C CB  . VAL B 224 ? 0.2392 0.2058 0.3977 -0.0491 0.0219  -0.0382 259 VAL B CB  
3880 C CG1 . VAL B 224 ? 0.2176 0.1843 0.3905 -0.0524 0.0210  -0.0411 259 VAL B CG1 
3881 C CG2 . VAL B 224 ? 0.1841 0.1552 0.3360 -0.0524 0.0283  -0.0344 259 VAL B CG2 
3882 N N   . ALA B 225 ? 0.1940 0.1694 0.3488 -0.0376 0.0077  -0.0529 260 ALA B N   
3883 C CA  . ALA B 225 ? 0.1755 0.1508 0.3296 -0.0336 0.0021  -0.0602 260 ALA B CA  
3884 C C   . ALA B 225 ? 0.2872 0.2511 0.4513 -0.0359 -0.0007 -0.0646 260 ALA B C   
3885 O O   . ALA B 225 ? 0.2332 0.1895 0.3957 -0.0319 -0.0042 -0.0705 260 ALA B O   
3886 C CB  . ALA B 225 ? 0.2606 0.2475 0.4132 -0.0337 -0.0021 -0.0628 260 ALA B CB  
3887 N N   . ALA B 226 ? 0.2428 0.2056 0.4178 -0.0424 0.0003  -0.0620 261 ALA B N   
3888 C CA  . ALA B 226 ? 0.3016 0.2550 0.4872 -0.0467 -0.0038 -0.0647 261 ALA B CA  
3889 C C   . ALA B 226 ? 0.2939 0.2334 0.4813 -0.0475 -0.0033 -0.0613 261 ALA B C   
3890 O O   . ALA B 226 ? 0.3686 0.2970 0.5644 -0.0513 -0.0085 -0.0633 261 ALA B O   
3891 C CB  . ALA B 226 ? 0.2931 0.2534 0.4921 -0.0535 -0.0022 -0.0611 261 ALA B CB  
3892 N N   . VAL B 227 ? 0.2939 0.2333 0.4741 -0.0447 0.0015  -0.0554 262 VAL B N   
3893 C CA  . VAL B 227 ? 0.2871 0.2142 0.4695 -0.0454 0.0010  -0.0500 262 VAL B CA  
3894 C C   . VAL B 227 ? 0.3314 0.2545 0.5057 -0.0357 -0.0009 -0.0530 262 VAL B C   
3895 O O   . VAL B 227 ? 0.2837 0.1927 0.4624 -0.0321 -0.0060 -0.0563 262 VAL B O   
3896 C CB  . VAL B 227 ? 0.2884 0.2204 0.4707 -0.0518 0.0078  -0.0383 262 VAL B CB  
3897 C CG1 . VAL B 227 ? 0.3392 0.2598 0.5245 -0.0540 0.0060  -0.0301 262 VAL B CG1 
3898 C CG2 . VAL B 227 ? 0.2169 0.1553 0.4092 -0.0601 0.0104  -0.0362 262 VAL B CG2 
3899 N N   . GLN B 228 ? 0.2404 0.1763 0.4043 -0.0311 0.0028  -0.0522 263 GLN B N   
3900 C CA  . GLN B 228 ? 0.2814 0.2195 0.4389 -0.0230 0.0031  -0.0509 263 GLN B CA  
3901 C C   . GLN B 228 ? 0.2685 0.2107 0.4220 -0.0134 -0.0001 -0.0621 263 GLN B C   
3902 O O   . GLN B 228 ? 0.2197 0.1643 0.3708 -0.0049 0.0000  -0.0624 263 GLN B O   
3903 C CB  . GLN B 228 ? 0.2226 0.1740 0.3711 -0.0252 0.0082  -0.0425 263 GLN B CB  
3904 C CG  . GLN B 228 ? 0.2047 0.1532 0.3546 -0.0340 0.0122  -0.0324 263 GLN B CG  
3905 C CD  . GLN B 228 ? 0.2381 0.1973 0.3772 -0.0366 0.0164  -0.0260 263 GLN B CD  
3906 O OE1 . GLN B 228 ? 0.2346 0.2021 0.3687 -0.0365 0.0171  -0.0293 263 GLN B OE1 
3907 N NE2 . GLN B 228 ? 0.2335 0.1918 0.3692 -0.0404 0.0183  -0.0165 263 GLN B NE2 
3908 N N   . PHE B 229 ? 0.2150 0.1601 0.3679 -0.0143 -0.0030 -0.0712 264 PHE B N   
3909 C CA  . PHE B 229 ? 0.2585 0.2058 0.4070 -0.0056 -0.0064 -0.0837 264 PHE B CA  
3910 C C   . PHE B 229 ? 0.3202 0.2463 0.4762 -0.0021 -0.0116 -0.0915 264 PHE B C   
3911 O O   . PHE B 229 ? 0.3378 0.2605 0.4926 0.0085  -0.0125 -0.0983 264 PHE B O   
3912 C CB  . PHE B 229 ? 0.2215 0.1798 0.3657 -0.0089 -0.0089 -0.0902 264 PHE B CB  
3913 C CG  . PHE B 229 ? 0.2698 0.2497 0.4050 -0.0087 -0.0059 -0.0850 264 PHE B CG  
3914 C CD1 . PHE B 229 ? 0.2459 0.2391 0.3734 -0.0008 -0.0035 -0.0850 264 PHE B CD1 
3915 C CD2 . PHE B 229 ? 0.2072 0.1943 0.3435 -0.0165 -0.0060 -0.0790 264 PHE B CD2 
3916 C CE1 . PHE B 229 ? 0.2921 0.3057 0.4119 -0.0024 -0.0018 -0.0779 264 PHE B CE1 
3917 C CE2 . PHE B 229 ? 0.2328 0.2371 0.3616 -0.0173 -0.0049 -0.0729 264 PHE B CE2 
3918 C CZ  . PHE B 229 ? 0.2613 0.2790 0.3815 -0.0111 -0.0031 -0.0718 264 PHE B CZ  
3919 N N   . ASP B 230 ? 0.2531 0.1648 0.4182 -0.0108 -0.0152 -0.0903 265 ASP B N   
3920 C CA  . ASP B 230 ? 0.3993 0.2874 0.5730 -0.0098 -0.0218 -0.0956 265 ASP B CA  
3921 C C   . ASP B 230 ? 0.4004 0.2778 0.5798 -0.0061 -0.0210 -0.0864 265 ASP B C   
3922 O O   . ASP B 230 ? 0.3427 0.2039 0.5265 0.0021  -0.0258 -0.0930 265 ASP B O   
3923 C CB  . ASP B 230 ? 0.3532 0.2319 0.5365 -0.0224 -0.0261 -0.0928 265 ASP B CB  
3924 C CG  . ASP B 230 ? 0.3908 0.2757 0.5706 -0.0251 -0.0302 -0.1036 265 ASP B CG  
3925 O OD1 . ASP B 230 ? 0.6399 0.5220 0.8124 -0.0175 -0.0342 -0.1180 265 ASP B OD1 
3926 O OD2 . ASP B 230 ? 0.6088 0.5034 0.7921 -0.0342 -0.0293 -0.0970 265 ASP B OD2 
3927 N N   . ASP B 231 ? 0.3223 0.2082 0.5019 -0.0118 -0.0154 -0.0713 266 ASP B N   
3928 C CA  . ASP B 231 ? 0.3863 0.2647 0.5710 -0.0105 -0.0153 -0.0599 266 ASP B CA  
3929 C C   . ASP B 231 ? 0.3153 0.2129 0.4913 -0.0083 -0.0084 -0.0510 266 ASP B C   
3930 O O   . ASP B 231 ? 0.2611 0.1653 0.4350 -0.0174 -0.0042 -0.0392 266 ASP B O   
3931 C CB  . ASP B 231 ? 0.3894 0.2564 0.5837 -0.0233 -0.0173 -0.0480 266 ASP B CB  
3932 C CG  . ASP B 231 ? 0.3909 0.2466 0.5921 -0.0225 -0.0201 -0.0360 266 ASP B CG  
3933 O OD1 . ASP B 231 ? 0.3739 0.2333 0.5726 -0.0119 -0.0192 -0.0356 266 ASP B OD1 
3934 O OD2 . ASP B 231 ? 0.3563 0.2014 0.5665 -0.0329 -0.0234 -0.0256 266 ASP B OD2 
3935 N N   . PRO B 232 ? 0.2918 0.1991 0.4628 0.0034  -0.0072 -0.0562 267 PRO B N   
3936 C CA  . PRO B 232 ? 0.2404 0.1669 0.4037 0.0044  -0.0020 -0.0468 267 PRO B CA  
3937 C C   . PRO B 232 ? 0.2925 0.2148 0.4598 0.0008  -0.0019 -0.0314 267 PRO B C   
3938 O O   . PRO B 232 ? 0.3193 0.2567 0.4797 -0.0005 0.0015  -0.0225 267 PRO B O   
3939 C CB  . PRO B 232 ? 0.3144 0.2522 0.4750 0.0184  -0.0017 -0.0558 267 PRO B CB  
3940 C CG  . PRO B 232 ? 0.4021 0.3319 0.5630 0.0224  -0.0050 -0.0725 267 PRO B CG  
3941 C CD  . PRO B 232 ? 0.2755 0.1797 0.4465 0.0158  -0.0104 -0.0719 267 PRO B CD  
3942 N N   . SER B 233 ? 0.3088 0.2117 0.4869 -0.0019 -0.0067 -0.0269 268 SER B N   
3943 C CA  . SER B 233 ? 0.3162 0.2167 0.4978 -0.0070 -0.0076 -0.0101 268 SER B CA  
3944 C C   . SER B 233 ? 0.2860 0.1922 0.4616 -0.0223 -0.0034 0.0003  268 SER B C   
3945 O O   . SER B 233 ? 0.2868 0.1975 0.4600 -0.0279 -0.0026 0.0143  268 SER B O   
3946 C CB  . SER B 233 ? 0.3049 0.1822 0.5016 -0.0045 -0.0156 -0.0068 268 SER B CB  
3947 O OG  . SER B 233 ? 0.4075 0.2699 0.6099 -0.0143 -0.0188 -0.0082 268 SER B OG  
3948 N N   . VAL B 234 ? 0.2524 0.1597 0.4258 -0.0290 -0.0007 -0.0060 269 VAL B N   
3949 C CA  . VAL B 234 ? 0.2391 0.1536 0.4080 -0.0419 0.0043  0.0024  269 VAL B CA  
3950 C C   . VAL B 234 ? 0.2251 0.1569 0.3798 -0.0427 0.0102  0.0045  269 VAL B C   
3951 O O   . VAL B 234 ? 0.2329 0.1726 0.3819 -0.0372 0.0117  -0.0042 269 VAL B O   
3952 C CB  . VAL B 234 ? 0.2487 0.1613 0.4222 -0.0477 0.0054  -0.0048 269 VAL B CB  
3953 C CG1 . VAL B 234 ? 0.2307 0.1541 0.4003 -0.0592 0.0121  0.0027  269 VAL B CG1 
3954 C CG2 . VAL B 234 ? 0.2533 0.1469 0.4410 -0.0483 -0.0023 -0.0068 269 VAL B CG2 
3955 N N   . THR B 235 ? 0.2265 0.1641 0.3747 -0.0508 0.0129  0.0165  270 THR B N   
3956 C CA  . THR B 235 ? 0.2218 0.1733 0.3555 -0.0534 0.0174  0.0185  270 THR B CA  
3957 C C   . THR B 235 ? 0.2966 0.2538 0.4238 -0.0638 0.0239  0.0190  270 THR B C   
3958 O O   . THR B 235 ? 0.2434 0.1972 0.3785 -0.0683 0.0255  0.0175  270 THR B O   
3959 C CB  . THR B 235 ? 0.3140 0.2698 0.4434 -0.0531 0.0147  0.0306  270 THR B CB  
3960 O OG1 . THR B 235 ? 0.2836 0.2361 0.4149 -0.0622 0.0140  0.0430  270 THR B OG1 
3961 C CG2 . THR B 235 ? 0.2259 0.1779 0.3647 -0.0407 0.0092  0.0290  270 THR B CG2 
3962 N N   . THR B 236 ? 0.2995 0.2661 0.4124 -0.0674 0.0274  0.0203  271 THR B N   
3963 C CA  . THR B 236 ? 0.2833 0.2561 0.3885 -0.0754 0.0343  0.0183  271 THR B CA  
3964 C C   . THR B 236 ? 0.2959 0.2757 0.3859 -0.0833 0.0360  0.0274  271 THR B C   
3965 O O   . THR B 236 ? 0.2592 0.2406 0.3437 -0.0824 0.0315  0.0347  271 THR B O   
3966 C CB  . THR B 236 ? 0.3066 0.2817 0.4083 -0.0718 0.0368  0.0062  271 THR B CB  
3967 O OG1 . THR B 236 ? 0.2952 0.2737 0.3845 -0.0707 0.0346  0.0068  271 THR B OG1 
3968 C CG2 . THR B 236 ? 0.2826 0.2528 0.3970 -0.0642 0.0335  -0.0017 271 THR B CG2 
3969 N N   . ASP B 237 ? 0.2427 0.2289 0.3258 -0.0912 0.0429  0.0265  272 ASP B N   
3970 C CA  . ASP B 237 ? 0.3137 0.3079 0.3787 -0.0995 0.0451  0.0322  272 ASP B CA  
3971 C C   . ASP B 237 ? 0.3362 0.3308 0.3870 -0.0978 0.0444  0.0250  272 ASP B C   
3972 O O   . ASP B 237 ? 0.3953 0.3951 0.4290 -0.1051 0.0452  0.0282  272 ASP B O   
3973 C CB  . ASP B 237 ? 0.3884 0.3918 0.4489 -0.1079 0.0536  0.0316  272 ASP B CB  
3974 C CG  . ASP B 237 ? 0.4253 0.4300 0.4904 -0.1037 0.0604  0.0167  272 ASP B CG  
3975 O OD1 . ASP B 237 ? 0.4120 0.4097 0.4800 -0.0957 0.0579  0.0073  272 ASP B OD1 
3976 O OD2 . ASP B 237 ? 0.5840 0.5986 0.6506 -0.1085 0.0681  0.0154  272 ASP B OD2 
3977 N N   . LEU B 238 ? 0.2693 0.2586 0.3259 -0.0897 0.0421  0.0161  273 LEU B N   
3978 C CA  . LEU B 238 ? 0.3405 0.3292 0.3854 -0.0892 0.0391  0.0122  273 LEU B CA  
3979 C C   . LEU B 238 ? 0.3715 0.3621 0.4174 -0.0860 0.0314  0.0205  273 LEU B C   
3980 O O   . LEU B 238 ? 0.3480 0.3402 0.3850 -0.0870 0.0276  0.0200  273 LEU B O   
3981 C CB  . LEU B 238 ? 0.2765 0.2606 0.3268 -0.0835 0.0402  -0.0003 273 LEU B CB  
3982 C CG  . LEU B 238 ? 0.4274 0.4114 0.4731 -0.0863 0.0478  -0.0099 273 LEU B CG  
3983 C CD1 . LEU B 238 ? 0.5237 0.5018 0.5742 -0.0806 0.0470  -0.0212 273 LEU B CD1 
3984 C CD2 . LEU B 238 ? 0.3903 0.3779 0.4158 -0.0951 0.0507  -0.0084 273 LEU B CD2 
3985 N N   . ASP B 239 ? 0.2490 0.2399 0.3068 -0.0819 0.0286  0.0279  274 ASP B N   
3986 C CA  . ASP B 239 ? 0.2833 0.2788 0.3441 -0.0772 0.0222  0.0356  274 ASP B CA  
3987 C C   . ASP B 239 ? 0.2840 0.2860 0.3348 -0.0848 0.0193  0.0487  274 ASP B C   
3988 O O   . ASP B 239 ? 0.3571 0.3586 0.4076 -0.0903 0.0205  0.0561  274 ASP B O   
3989 C CB  . ASP B 239 ? 0.2135 0.2050 0.2921 -0.0677 0.0201  0.0361  274 ASP B CB  
3990 C CG  . ASP B 239 ? 0.2854 0.2719 0.3729 -0.0606 0.0215  0.0233  274 ASP B CG  
3991 O OD1 . ASP B 239 ? 0.2445 0.2357 0.3290 -0.0573 0.0203  0.0181  274 ASP B OD1 
3992 O OD2 . ASP B 239 ? 0.3726 0.3512 0.4706 -0.0589 0.0229  0.0197  274 ASP B OD2 
3993 N N   . SER B 240 ? 0.2657 0.2755 0.3089 -0.0862 0.0147  0.0532  275 SER B N   
3994 C CA  . SER B 240 ? 0.2986 0.3166 0.3326 -0.0940 0.0104  0.0668  275 SER B CA  
3995 C C   . SER B 240 ? 0.3166 0.3376 0.3650 -0.0890 0.0067  0.0793  275 SER B C   
3996 O O   . SER B 240 ? 0.3487 0.3729 0.3929 -0.0964 0.0046  0.0914  275 SER B O   
3997 C CB  . SER B 240 ? 0.2751 0.3017 0.3004 -0.0967 0.0050  0.0697  275 SER B CB  
3998 O OG  . SER B 240 ? 0.4589 0.4794 0.4724 -0.1010 0.0068  0.0582  275 SER B OG  
3999 N N   . ASP B 241 ? 0.3124 0.3329 0.3777 -0.0763 0.0052  0.0768  276 ASP B N   
4000 C CA  . ASP B 241 ? 0.2351 0.2556 0.3171 -0.0686 0.0012  0.0862  276 ASP B CA  
4001 C C   . ASP B 241 ? 0.2280 0.2366 0.3251 -0.0576 0.0034  0.0751  276 ASP B C   
4002 O O   . ASP B 241 ? 0.2294 0.2413 0.3338 -0.0469 0.0033  0.0672  276 ASP B O   
4003 C CB  . ASP B 241 ? 0.2962 0.3320 0.3835 -0.0628 -0.0041 0.0950  276 ASP B CB  
4004 C CG  . ASP B 241 ? 0.2703 0.3061 0.3764 -0.0536 -0.0088 0.1051  276 ASP B CG  
4005 O OD1 . ASP B 241 ? 0.3454 0.3663 0.4626 -0.0492 -0.0085 0.1027  276 ASP B OD1 
4006 O OD2 . ASP B 241 ? 0.3108 0.3615 0.4222 -0.0503 -0.0135 0.1159  276 ASP B OD2 
4007 N N   . SER B 242 ? 0.2552 0.2637 0.3925 -0.0087 -0.0800 0.0901  277 SER B N   
4008 C CA  . SER B 242 ? 0.2678 0.2657 0.4121 -0.0123 -0.0766 0.0903  277 SER B CA  
4009 C C   . SER B 242 ? 0.2476 0.2290 0.4156 -0.0074 -0.0808 0.0834  277 SER B C   
4010 O O   . SER B 242 ? 0.2627 0.2380 0.4366 -0.0066 -0.0744 0.0717  277 SER B O   
4011 C CB  . SER B 242 ? 0.3454 0.3434 0.4825 -0.0204 -0.0813 0.1091  277 SER B CB  
4012 O OG  . SER B 242 ? 0.4954 0.5103 0.6119 -0.0247 -0.0735 0.1121  277 SER B OG  
4013 N N   . LYS B 243 ? 0.3496 0.3239 0.5312 -0.0032 -0.0920 0.0901  278 LYS B N   
4014 C CA  . LYS B 243 ? 0.3137 0.2716 0.5184 0.0032  -0.0961 0.0825  278 LYS B CA  
4015 C C   . LYS B 243 ? 0.2841 0.2494 0.4981 0.0110  -0.0880 0.0631  278 LYS B C   
4016 O O   . LYS B 243 ? 0.2516 0.2086 0.4766 0.0148  -0.0839 0.0507  278 LYS B O   
4017 C CB  . LYS B 243 ? 0.4387 0.3861 0.6584 0.0071  -0.1111 0.0945  278 LYS B CB  
4018 C CG  . LYS B 243 ? 0.6462 0.5869 0.8909 0.0193  -0.1138 0.0812  278 LYS B CG  
4019 C CD  . LYS B 243 ? 0.6780 0.6018 0.9422 0.0248  -0.1298 0.0912  278 LYS B CD  
4020 C CE  . LYS B 243 ? 0.5993 0.5330 0.8834 0.0372  -0.1328 0.0828  278 LYS B CE  
4021 N NZ  . LYS B 243 ? 0.6111 0.5434 0.9122 0.0474  -0.1247 0.0611  278 LYS B NZ  
4022 N N   . ALA B 244 ? 0.2410 0.2229 0.4492 0.0124  -0.0856 0.0604  279 ALA B N   
4023 C CA  . ALA B 244 ? 0.3229 0.3153 0.5385 0.0171  -0.0776 0.0444  279 ALA B CA  
4024 C C   . ALA B 244 ? 0.2677 0.2611 0.4726 0.0129  -0.0656 0.0342  279 ALA B C   
4025 O O   . ALA B 244 ? 0.2318 0.2269 0.4465 0.0165  -0.0591 0.0210  279 ALA B O   
4026 C CB  . ALA B 244 ? 0.2294 0.2377 0.4387 0.0167  -0.0791 0.0454  279 ALA B CB  
4027 N N   . VAL B 245 ? 0.2486 0.2436 0.4330 0.0056  -0.0621 0.0401  280 VAL B N   
4028 C CA  . VAL B 245 ? 0.2543 0.2511 0.4294 0.0019  -0.0518 0.0312  280 VAL B CA  
4029 C C   . VAL B 245 ? 0.2210 0.2043 0.4047 0.0016  -0.0507 0.0269  280 VAL B C   
4030 O O   . VAL B 245 ? 0.2121 0.1963 0.3973 0.0020  -0.0434 0.0147  280 VAL B O   
4031 C CB  . VAL B 245 ? 0.2494 0.2528 0.4026 -0.0041 -0.0486 0.0376  280 VAL B CB  
4032 C CG1 . VAL B 245 ? 0.2723 0.2697 0.4204 -0.0094 -0.0502 0.0483  280 VAL B CG1 
4033 C CG2 . VAL B 245 ? 0.2477 0.2568 0.3927 -0.0058 -0.0393 0.0270  280 VAL B CG2 
4034 N N   . ALA B 246 ? 0.2218 0.1916 0.4114 0.0006  -0.0590 0.0367  281 ALA B N   
4035 C CA  . ALA B 246 ? 0.2633 0.2168 0.4611 0.0001  -0.0600 0.0317  281 ALA B CA  
4036 C C   . ALA B 246 ? 0.3153 0.2648 0.5306 0.0099  -0.0590 0.0161  281 ALA B C   
4037 O O   . ALA B 246 ? 0.2713 0.2171 0.4871 0.0104  -0.0531 0.0032  281 ALA B O   
4038 C CB  . ALA B 246 ? 0.2819 0.2201 0.4833 -0.0041 -0.0712 0.0470  281 ALA B CB  
4039 N N   . VAL B 247 ? 0.2491 0.2026 0.4783 0.0179  -0.0643 0.0167  282 VAL B N   
4040 C CA  . VAL B 247 ? 0.3093 0.2655 0.5568 0.0287  -0.0620 0.0015  282 VAL B CA  
4041 C C   . VAL B 247 ? 0.2903 0.2643 0.5314 0.0276  -0.0488 -0.0118 282 VAL B C   
4042 O O   . VAL B 247 ? 0.2728 0.2456 0.5179 0.0310  -0.0428 -0.0260 282 VAL B O   
4043 C CB  . VAL B 247 ? 0.2448 0.2075 0.5091 0.0369  -0.0700 0.0063  282 VAL B CB  
4044 C CG1 . VAL B 247 ? 0.2933 0.2687 0.5762 0.0478  -0.0647 -0.0098 282 VAL B CG1 
4045 C CG2 . VAL B 247 ? 0.3927 0.3346 0.6671 0.0395  -0.0845 0.0179  282 VAL B CG2 
4046 N N   . GLU B 248 ? 0.2078 0.1979 0.4376 0.0225  -0.0449 -0.0073 283 GLU B N   
4047 C CA  . GLU B 248 ? 0.2578 0.2642 0.4826 0.0205  -0.0342 -0.0177 283 GLU B CA  
4048 C C   . GLU B 248 ? 0.2646 0.2658 0.4749 0.0141  -0.0269 -0.0231 283 GLU B C   
4049 O O   . GLU B 248 ? 0.2015 0.2111 0.4120 0.0143  -0.0187 -0.0348 283 GLU B O   
4050 C CB  . GLU B 248 ? 0.2291 0.2492 0.4447 0.0159  -0.0343 -0.0111 283 GLU B CB  
4051 C CG  . GLU B 248 ? 0.2073 0.2372 0.4384 0.0214  -0.0407 -0.0081 283 GLU B CG  
4052 C CD  . GLU B 248 ? 0.3648 0.4071 0.6168 0.0289  -0.0364 -0.0196 283 GLU B CD  
4053 O OE1 . GLU B 248 ? 0.3584 0.4113 0.6070 0.0260  -0.0266 -0.0288 283 GLU B OE1 
4054 O OE2 . GLU B 248 ? 0.3396 0.3814 0.6114 0.0379  -0.0428 -0.0194 283 GLU B OE2 
4055 N N   . ARG B 249 ? 0.2508 0.2400 0.4489 0.0080  -0.0299 -0.0145 284 ARG B N   
4056 C CA  . ARG B 249 ? 0.2267 0.2114 0.4131 0.0018  -0.0245 -0.0188 284 ARG B CA  
4057 C C   . ARG B 249 ? 0.2876 0.2616 0.4831 0.0059  -0.0240 -0.0310 284 ARG B C   
4058 O O   . ARG B 249 ? 0.2036 0.1832 0.3942 0.0047  -0.0165 -0.0422 284 ARG B O   
4059 C CB  . ARG B 249 ? 0.2471 0.2243 0.4219 -0.0055 -0.0282 -0.0061 284 ARG B CB  
4060 C CG  . ARG B 249 ? 0.2166 0.1887 0.3822 -0.0122 -0.0245 -0.0098 284 ARG B CG  
4061 C CD  . ARG B 249 ? 0.2652 0.2352 0.4220 -0.0195 -0.0278 0.0039  284 ARG B CD  
4062 N NE  . ARG B 249 ? 0.3289 0.3125 0.4762 -0.0197 -0.0259 0.0115  284 ARG B NE  
4063 C CZ  . ARG B 249 ? 0.3478 0.3343 0.4907 -0.0218 -0.0300 0.0248  284 ARG B CZ  
4064 N NH1 . ARG B 249 ? 0.2845 0.2612 0.4332 -0.0248 -0.0371 0.0348  284 ARG B NH1 
4065 N NH2 . ARG B 249 ? 0.2092 0.2084 0.3407 -0.0210 -0.0273 0.0283  284 ARG B NH2 
4066 N N   . LYS B 250 ? 0.2514 0.2091 0.4594 0.0109  -0.0329 -0.0290 285 LYS B N   
4067 C CA  . LYS B 250 ? 0.2575 0.2013 0.4742 0.0164  -0.0342 -0.0423 285 LYS B CA  
4068 C C   . LYS B 250 ? 0.3413 0.3005 0.5670 0.0255  -0.0260 -0.0588 285 LYS B C   
4069 O O   . LYS B 250 ? 0.2749 0.2329 0.4981 0.0273  -0.0207 -0.0735 285 LYS B O   
4070 C CB  . LYS B 250 ? 0.4436 0.3657 0.6743 0.0212  -0.0471 -0.0363 285 LYS B CB  
4071 C CG  . LYS B 250 ? 0.4825 0.3924 0.7049 0.0106  -0.0552 -0.0179 285 LYS B CG  
4072 C CD  . LYS B 250 ? 0.5654 0.4497 0.8008 0.0130  -0.0696 -0.0112 285 LYS B CD  
4073 C CE  . LYS B 250 ? 0.4570 0.3347 0.6835 0.0002  -0.0766 0.0097  285 LYS B CE  
4074 N NZ  . LYS B 250 ? 0.4560 0.3294 0.6909 0.0017  -0.0875 0.0264  285 LYS B NZ  
4075 N N   . LYS B 251 ? 0.2987 0.2749 0.5342 0.0305  -0.0248 -0.0562 286 LYS B N   
4076 C CA  . LYS B 251 ? 0.3152 0.3122 0.5606 0.0378  -0.0163 -0.0695 286 LYS B CA  
4077 C C   . LYS B 251 ? 0.2579 0.2693 0.4873 0.0299  -0.0050 -0.0759 286 LYS B C   
4078 O O   . LYS B 251 ? 0.2535 0.2724 0.4840 0.0337  0.0023  -0.0907 286 LYS B O   
4079 C CB  . LYS B 251 ? 0.2153 0.2294 0.4732 0.0414  -0.0184 -0.0622 286 LYS B CB  
4080 C CG  . LYS B 251 ? 0.3689 0.4074 0.6435 0.0498  -0.0114 -0.0735 286 LYS B CG  
4081 C CD  . LYS B 251 ? 0.3071 0.3621 0.5927 0.0502  -0.0155 -0.0634 286 LYS B CD  
4082 C CE  . LYS B 251 ? 0.3716 0.4123 0.6728 0.0587  -0.0284 -0.0561 286 LYS B CE  
4083 N NZ  . LYS B 251 ? 0.3586 0.4143 0.6716 0.0599  -0.0345 -0.0462 286 LYS B NZ  
4084 N N   . ALA B 252 ? 0.2599 0.2755 0.4738 0.0192  -0.0038 -0.0650 287 ALA B N   
4085 C CA  . ALA B 252 ? 0.2608 0.2897 0.4604 0.0114  0.0053  -0.0688 287 ALA B CA  
4086 C C   . ALA B 252 ? 0.2695 0.2868 0.4574 0.0079  0.0076  -0.0766 287 ALA B C   
4087 O O   . ALA B 252 ? 0.2285 0.2570 0.4100 0.0060  0.0155  -0.0865 287 ALA B O   
4088 C CB  . ALA B 252 ? 0.2658 0.2983 0.4525 0.0024  0.0042  -0.0560 287 ALA B CB  
4089 N N   . PHE B 253 ? 0.2339 0.2299 0.4186 0.0060  0.0001  -0.0715 288 PHE B N   
4090 C CA  . PHE B 253 ? 0.2761 0.2599 0.4505 0.0017  0.0003  -0.0786 288 PHE B CA  
4091 C C   . PHE B 253 ? 0.3136 0.2941 0.4956 0.0106  0.0024  -0.0970 288 PHE B C   
4092 O O   . PHE B 253 ? 0.3014 0.2857 0.4725 0.0079  0.0080  -0.1081 288 PHE B O   
4093 C CB  . PHE B 253 ? 0.2666 0.2296 0.4389 -0.0031 -0.0093 -0.0678 288 PHE B CB  
4094 C CG  . PHE B 253 ? 0.2741 0.2429 0.4350 -0.0122 -0.0094 -0.0526 288 PHE B CG  
4095 C CD1 . PHE B 253 ? 0.2267 0.2134 0.3802 -0.0145 -0.0029 -0.0504 288 PHE B CD1 
4096 C CD2 . PHE B 253 ? 0.2712 0.2282 0.4292 -0.0182 -0.0163 -0.0408 288 PHE B CD2 
4097 C CE1 . PHE B 253 ? 0.2884 0.2791 0.4318 -0.0205 -0.0034 -0.0387 288 PHE B CE1 
4098 C CE2 . PHE B 253 ? 0.2643 0.2300 0.4126 -0.0245 -0.0154 -0.0284 288 PHE B CE2 
4099 C CZ  . PHE B 253 ? 0.2547 0.2364 0.3954 -0.0247 -0.0089 -0.0285 288 PHE B CZ  
4100 N N   . ALA B 254 ? 0.2637 0.2373 0.4638 0.0220  -0.0024 -0.1009 289 ALA B N   
4101 C CA  . ALA B 254 ? 0.2883 0.2587 0.4963 0.0329  -0.0005 -0.1205 289 ALA B CA  
4102 C C   . ALA B 254 ? 0.2640 0.2648 0.4717 0.0364  0.0127  -0.1320 289 ALA B C   
4103 O O   . ALA B 254 ? 0.2962 0.3009 0.4965 0.0387  0.0187  -0.1482 289 ALA B O   
4104 C CB  . ALA B 254 ? 0.3031 0.2588 0.5329 0.0458  -0.0099 -0.1217 289 ALA B CB  
4105 N N   . ASP B 255 ? 0.2604 0.2838 0.4743 0.0353  0.0170  -0.1232 290 ASP B N   
4106 C CA  . ASP B 255 ? 0.3315 0.3863 0.5464 0.0365  0.0292  -0.1315 290 ASP B CA  
4107 C C   . ASP B 255 ? 0.2542 0.3171 0.4461 0.0242  0.0364  -0.1326 290 ASP B C   
4108 O O   . ASP B 255 ? 0.2738 0.3544 0.4610 0.0258  0.0457  -0.1457 290 ASP B O   
4109 C CB  . ASP B 255 ? 0.2535 0.3291 0.4805 0.0358  0.0301  -0.1201 290 ASP B CB  
4110 C CG  . ASP B 255 ? 0.2285 0.3391 0.4628 0.0380  0.0416  -0.1279 290 ASP B CG  
4111 O OD1 . ASP B 255 ? 0.2918 0.4137 0.5448 0.0514  0.0441  -0.1391 290 ASP B OD1 
4112 O OD2 . ASP B 255 ? 0.3212 0.4490 0.5434 0.0264  0.0478  -0.1222 290 ASP B OD2 
4113 N N   . ALA B 256 ? 0.2660 0.3171 0.4432 0.0122  0.0319  -0.1191 291 ALA B N   
4114 C CA  . ALA B 256 ? 0.2776 0.3357 0.4342 0.0007  0.0371  -0.1184 291 ALA B CA  
4115 C C   . ALA B 256 ? 0.3715 0.4166 0.5166 0.0008  0.0369  -0.1317 291 ALA B C   
4116 O O   . ALA B 256 ? 0.2629 0.3212 0.3938 -0.0044 0.0439  -0.1387 291 ALA B O   
4117 C CB  . ALA B 256 ? 0.2791 0.3290 0.4256 -0.0099 0.0319  -0.1011 291 ALA B CB  
4118 N N   . ALA B 257 ? 0.2800 0.2991 0.4304 0.0059  0.0281  -0.1351 292 ALA B N   
4119 C CA  . ALA B 257 ? 0.3195 0.3239 0.4600 0.0064  0.0262  -0.1495 292 ALA B CA  
4120 C C   . ALA B 257 ? 0.4049 0.4224 0.5495 0.0180  0.0340  -0.1708 292 ALA B C   
4121 O O   . ALA B 257 ? 0.3671 0.3885 0.4960 0.0158  0.0384  -0.1840 292 ALA B O   
4122 C CB  . ALA B 257 ? 0.3079 0.2798 0.4543 0.0076  0.0131  -0.1464 292 ALA B CB  
4123 N N   . LYS B 258 ? 0.3084 0.3351 0.4738 0.0310  0.0359  -0.1749 293 LYS B N   
4124 C CA  . LYS B 258 ? 0.4203 0.4631 0.5920 0.0442  0.0442  -0.1961 293 LYS B CA  
4125 C C   . LYS B 258 ? 0.3999 0.4793 0.5598 0.0381  0.0584  -0.1988 293 LYS B C   
4126 O O   . LYS B 258 ? 0.3410 0.4300 0.4885 0.0405  0.0654  -0.2160 293 LYS B O   
4127 C CB  . LYS B 258 ? 0.3500 0.3980 0.5494 0.0598  0.0427  -0.1982 293 LYS B CB  
4128 C CG  . LYS B 258 ? 0.4690 0.5375 0.6768 0.0754  0.0522  -0.2213 293 LYS B CG  
4129 C CD  . LYS B 258 ? 0.4283 0.4919 0.6648 0.0945  0.0472  -0.2280 293 LYS B CD  
4130 C CE  . LYS B 258 ? 0.4332 0.5334 0.6753 0.1045  0.0588  -0.2376 293 LYS B CE  
4131 N NZ  . LYS B 258 ? 0.5578 0.6648 0.8263 0.1181  0.0548  -0.2336 293 LYS B NZ  
4132 N N   . GLY B 259 ? 0.3347 0.4344 0.4972 0.0294  0.0620  -0.1817 294 GLY B N   
4133 C CA  . GLY B 259 ? 0.2916 0.4259 0.4445 0.0215  0.0740  -0.1807 294 GLY B CA  
4134 C C   . GLY B 259 ? 0.3605 0.4925 0.4866 0.0059  0.0747  -0.1754 294 GLY B C   
4135 O O   . GLY B 259 ? 0.3689 0.5277 0.4833 -0.0005 0.0843  -0.1777 294 GLY B O   
4136 N N   . GLY B 260 ? 0.3490 0.4516 0.4657 -0.0008 0.0645  -0.1675 295 GLY B N   
4137 C CA  . GLY B 260 ? 0.2832 0.3826 0.3763 -0.0146 0.0635  -0.1626 295 GLY B CA  
4138 C C   . GLY B 260 ? 0.3508 0.4682 0.4370 -0.0273 0.0665  -0.1454 295 GLY B C   
4139 O O   . GLY B 260 ? 0.3084 0.4372 0.3760 -0.0373 0.0701  -0.1444 295 GLY B O   
4140 N N   . TYR B 261 ? 0.2817 0.3998 0.3816 -0.0274 0.0636  -0.1317 296 TYR B N   
4141 C CA  . TYR B 261 ? 0.2764 0.4081 0.3717 -0.0386 0.0645  -0.1158 296 TYR B CA  
4142 C C   . TYR B 261 ? 0.2575 0.3668 0.3487 -0.0442 0.0546  -0.1012 296 TYR B C   
4143 O O   . TYR B 261 ? 0.2415 0.3290 0.3372 -0.0392 0.0478  -0.1013 296 TYR B O   
4144 C CB  . TYR B 261 ? 0.2524 0.4060 0.3656 -0.0351 0.0691  -0.1125 296 TYR B CB  
4145 C CG  . TYR B 261 ? 0.2059 0.3483 0.3399 -0.0244 0.0636  -0.1113 296 TYR B CG  
4146 C CD1 . TYR B 261 ? 0.2399 0.3655 0.3761 -0.0273 0.0547  -0.0973 296 TYR B CD1 
4147 C CD2 . TYR B 261 ? 0.2143 0.3650 0.3658 -0.0110 0.0672  -0.1238 296 TYR B CD2 
4148 C CE1 . TYR B 261 ? 0.2064 0.3234 0.3593 -0.0188 0.0492  -0.0949 296 TYR B CE1 
4149 C CE2 . TYR B 261 ? 0.2086 0.3493 0.3794 -0.0017 0.0609  -0.1211 296 TYR B CE2 
4150 C CZ  . TYR B 261 ? 0.2050 0.3290 0.3755 -0.0065 0.0518  -0.1059 296 TYR B CZ  
4151 O OH  . TYR B 261 ? 0.1902 0.3049 0.3772 0.0014  0.0447  -0.1016 296 TYR B OH  
4152 N N   . LEU B 262 ? 0.2427 0.3582 0.3249 -0.0547 0.0535  -0.0884 297 LEU B N   
4153 C CA  . LEU B 262 ? 0.1902 0.2880 0.2678 -0.0590 0.0449  -0.0756 297 LEU B CA  
4154 C C   . LEU B 262 ? 0.1780 0.2676 0.2702 -0.0527 0.0402  -0.0693 297 LEU B C   
4155 O O   . LEU B 262 ? 0.1833 0.2851 0.2874 -0.0500 0.0425  -0.0689 297 LEU B O   
4156 C CB  . LEU B 262 ? 0.2755 0.3815 0.3413 -0.0704 0.0440  -0.0644 297 LEU B CB  
4157 C CG  . LEU B 262 ? 0.2971 0.4098 0.3455 -0.0781 0.0468  -0.0681 297 LEU B CG  
4158 C CD1 . LEU B 262 ? 0.2612 0.3858 0.2998 -0.0899 0.0463  -0.0563 297 LEU B CD1 
4159 C CD2 . LEU B 262 ? 0.2034 0.2967 0.2442 -0.0779 0.0405  -0.0688 297 LEU B CD2 
4160 N N   . ILE B 263 ? 0.1967 0.2677 0.2880 -0.0510 0.0333  -0.0638 298 ILE B N   
4161 C CA  . ILE B 263 ? 0.1625 0.2265 0.2621 -0.0472 0.0281  -0.0554 298 ILE B CA  
4162 C C   . ILE B 263 ? 0.2207 0.2773 0.3097 -0.0524 0.0230  -0.0449 298 ILE B C   
4163 O O   . ILE B 263 ? 0.1995 0.2539 0.2774 -0.0577 0.0224  -0.0436 298 ILE B O   
4164 C CB  . ILE B 263 ? 0.1637 0.2151 0.2738 -0.0389 0.0246  -0.0577 298 ILE B CB  
4165 C CG1 . ILE B 263 ? 0.2069 0.2440 0.3098 -0.0408 0.0207  -0.0563 298 ILE B CG1 
4166 C CG2 . ILE B 263 ? 0.1731 0.2297 0.2942 -0.0320 0.0287  -0.0698 298 ILE B CG2 
4167 C CD1 . ILE B 263 ? 0.2754 0.2990 0.3882 -0.0348 0.0158  -0.0558 298 ILE B CD1 
4168 N N   . ALA B 264 ? 0.1921 0.2453 0.2846 -0.0501 0.0187  -0.0379 299 ALA B N   
4169 C CA  . ALA B 264 ? 0.2464 0.2912 0.3307 -0.0512 0.0135  -0.0298 299 ALA B CA  
4170 C C   . ALA B 264 ? 0.2509 0.2893 0.3409 -0.0444 0.0094  -0.0263 299 ALA B C   
4171 O O   . ALA B 264 ? 0.1605 0.2017 0.2603 -0.0407 0.0094  -0.0280 299 ALA B O   
4172 C CB  . ALA B 264 ? 0.1515 0.1995 0.2287 -0.0574 0.0113  -0.0247 299 ALA B CB  
4173 N N   . ALA B 265 ? 0.1843 0.2163 0.2684 -0.0427 0.0061  -0.0211 300 ALA B N   
4174 C CA  . ALA B 265 ? 0.1465 0.1750 0.2324 -0.0368 0.0024  -0.0172 300 ALA B CA  
4175 C C   . ALA B 265 ? 0.1498 0.1757 0.2262 -0.0352 -0.0007 -0.0126 300 ALA B C   
4176 O O   . ALA B 265 ? 0.1650 0.1913 0.2364 -0.0375 -0.0002 -0.0112 300 ALA B O   
4177 C CB  . ALA B 265 ? 0.2173 0.2431 0.3096 -0.0335 0.0024  -0.0162 300 ALA B CB  
4178 N N   . SER B 266 ? 0.1589 0.1828 0.2334 -0.0303 -0.0043 -0.0108 301 SER B N   
4179 C CA  . SER B 266 ? 0.1859 0.2066 0.2510 -0.0267 -0.0080 -0.0092 301 SER B CA  
4180 C C   . SER B 266 ? 0.2056 0.2302 0.2673 -0.0237 -0.0064 -0.0060 301 SER B C   
4181 O O   . SER B 266 ? 0.1836 0.2074 0.2393 -0.0210 -0.0083 -0.0055 301 SER B O   
4182 C CB  . SER B 266 ? 0.2050 0.2231 0.2675 -0.0214 -0.0124 -0.0095 301 SER B CB  
4183 O OG  . SER B 266 ? 0.2179 0.2357 0.2871 -0.0247 -0.0139 -0.0112 301 SER B OG  
4184 N N   . HIS B 267 ? 0.1785 0.2077 0.2453 -0.0240 -0.0037 -0.0032 302 HIS B N   
4185 C CA  . HIS B 267 ? 0.1404 0.1769 0.2056 -0.0220 -0.0024 0.0016  302 HIS B CA  
4186 C C   . HIS B 267 ? 0.1383 0.1770 0.2088 -0.0285 -0.0004 0.0035  302 HIS B C   
4187 O O   . HIS B 267 ? 0.1387 0.1848 0.2115 -0.0290 0.0003  0.0092  302 HIS B O   
4188 C CB  . HIS B 267 ? 0.1654 0.2074 0.2301 -0.0174 -0.0025 0.0061  302 HIS B CB  
4189 C CG  . HIS B 267 ? 0.1479 0.1879 0.2048 -0.0108 -0.0053 0.0033  302 HIS B CG  
4190 N ND1 . HIS B 267 ? 0.1529 0.1922 0.2014 -0.0050 -0.0071 -0.0002 302 HIS B ND1 
4191 C CD2 . HIS B 267 ? 0.1512 0.1882 0.2072 -0.0090 -0.0080 0.0028  302 HIS B CD2 
4192 C CE1 . HIS B 267 ? 0.1600 0.1950 0.2017 -0.0001 -0.0108 -0.0036 302 HIS B CE1 
4193 N NE2 . HIS B 267 ? 0.1698 0.2042 0.2157 -0.0030 -0.0114 -0.0015 302 HIS B NE2 
4194 N N   . LEU B 268 ? 0.1406 0.1741 0.2129 -0.0340 0.0003  -0.0011 303 LEU B N   
4195 C CA  . LEU B 268 ? 0.1461 0.1808 0.2198 -0.0402 0.0010  -0.0009 303 LEU B CA  
4196 C C   . LEU B 268 ? 0.1464 0.1853 0.2145 -0.0405 -0.0003 0.0009  303 LEU B C   
4197 O O   . LEU B 268 ? 0.1605 0.1973 0.2237 -0.0371 -0.0020 0.0000  303 LEU B O   
4198 C CB  . LEU B 268 ? 0.1526 0.1820 0.2283 -0.0450 0.0025  -0.0079 303 LEU B CB  
4199 C CG  . LEU B 268 ? 0.1669 0.1915 0.2505 -0.0429 0.0031  -0.0110 303 LEU B CG  
4200 C CD1 . LEU B 268 ? 0.2283 0.2510 0.3131 -0.0460 0.0056  -0.0199 303 LEU B CD1 
4201 C CD2 . LEU B 268 ? 0.1529 0.1747 0.2421 -0.0439 0.0008  -0.0060 303 LEU B CD2 
4202 N N   . SER B 269 ? 0.1497 0.1939 0.2194 -0.0446 -0.0010 0.0043  304 SER B N   
4203 C CA  . SER B 269 ? 0.1536 0.2037 0.2202 -0.0441 -0.0032 0.0074  304 SER B CA  
4204 C C   . SER B 269 ? 0.1583 0.2020 0.2181 -0.0463 -0.0050 0.0040  304 SER B C   
4205 O O   . SER B 269 ? 0.1966 0.2366 0.2539 -0.0532 -0.0039 0.0001  304 SER B O   
4206 C CB  . SER B 269 ? 0.1763 0.2328 0.2463 -0.0510 -0.0046 0.0110  304 SER B CB  
4207 O OG  . SER B 269 ? 0.1876 0.2515 0.2564 -0.0498 -0.0076 0.0148  304 SER B OG  
4208 N N   . PHE B 270 ? 0.1505 0.1929 0.2071 -0.0403 -0.0080 0.0056  305 PHE B N   
4209 C CA  . PHE B 270 ? 0.1513 0.1856 0.2018 -0.0430 -0.0112 0.0044  305 PHE B CA  
4210 C C   . PHE B 270 ? 0.1551 0.1912 0.2020 -0.0528 -0.0121 0.0055  305 PHE B C   
4211 O O   . PHE B 270 ? 0.1751 0.2175 0.2232 -0.0545 -0.0137 0.0087  305 PHE B O   
4212 C CB  . PHE B 270 ? 0.1922 0.2228 0.2406 -0.0348 -0.0168 0.0065  305 PHE B CB  
4213 C CG  . PHE B 270 ? 0.1978 0.2179 0.2405 -0.0388 -0.0225 0.0077  305 PHE B CG  
4214 C CD1 . PHE B 270 ? 0.1692 0.1799 0.2096 -0.0393 -0.0240 0.0052  305 PHE B CD1 
4215 C CD2 . PHE B 270 ? 0.2144 0.2345 0.2546 -0.0431 -0.0273 0.0125  305 PHE B CD2 
4216 C CE1 . PHE B 270 ? 0.2478 0.2492 0.2838 -0.0452 -0.0301 0.0081  305 PHE B CE1 
4217 C CE2 . PHE B 270 ? 0.2674 0.2774 0.3020 -0.0484 -0.0336 0.0157  305 PHE B CE2 
4218 C CZ  . PHE B 270 ? 0.2344 0.2348 0.2671 -0.0499 -0.0350 0.0138  305 PHE B CZ  
4219 N N   . PRO B 271 ? 0.2015 0.2343 0.2435 -0.0599 -0.0112 0.0032  306 PRO B N   
4220 C CA  . PRO B 271 ? 0.1597 0.1877 0.2011 -0.0603 -0.0104 0.0009  306 PRO B CA  
4221 C C   . PRO B 271 ? 0.1846 0.2145 0.2320 -0.0588 -0.0045 -0.0050 306 PRO B C   
4222 O O   . PRO B 271 ? 0.1632 0.1917 0.2127 -0.0586 -0.0039 -0.0067 306 PRO B O   
4223 C CB  . PRO B 271 ? 0.2153 0.2454 0.2497 -0.0707 -0.0112 0.0027  306 PRO B CB  
4224 C CG  . PRO B 271 ? 0.2301 0.2671 0.2617 -0.0757 -0.0084 0.0006  306 PRO B CG  
4225 C CD  . PRO B 271 ? 0.1652 0.2020 0.2010 -0.0695 -0.0116 0.0038  306 PRO B CD  
4226 N N   . GLY B 272 ? 0.1504 0.1833 0.2018 -0.0581 -0.0014 -0.0074 307 GLY B N   
4227 C CA  . GLY B 272 ? 0.2023 0.2346 0.2608 -0.0551 0.0022  -0.0119 307 GLY B CA  
4228 C C   . GLY B 272 ? 0.1649 0.1998 0.2249 -0.0589 0.0065  -0.0186 307 GLY B C   
4229 O O   . GLY B 272 ? 0.1475 0.1822 0.2148 -0.0552 0.0083  -0.0217 307 GLY B O   
4230 N N   . ILE B 273 ? 0.1991 0.2383 0.2526 -0.0659 0.0080  -0.0210 308 ILE B N   
4231 C CA  . ILE B 273 ? 0.1799 0.2263 0.2331 -0.0694 0.0133  -0.0280 308 ILE B CA  
4232 C C   . ILE B 273 ? 0.1859 0.2328 0.2359 -0.0718 0.0156  -0.0356 308 ILE B C   
4233 O O   . ILE B 273 ? 0.1951 0.2409 0.2372 -0.0765 0.0128  -0.0335 308 ILE B O   
4234 C CB  . ILE B 273 ? 0.2206 0.2743 0.2661 -0.0768 0.0132  -0.0241 308 ILE B CB  
4235 C CG1 . ILE B 273 ? 0.1788 0.2282 0.2266 -0.0755 0.0085  -0.0166 308 ILE B CG1 
4236 C CG2 . ILE B 273 ? 0.2222 0.2891 0.2671 -0.0807 0.0204  -0.0315 308 ILE B CG2 
4237 C CD1 . ILE B 273 ? 0.2832 0.3360 0.3234 -0.0842 0.0057  -0.0101 308 ILE B CD1 
4238 N N   . GLY B 274 ? 0.1622 0.2303 0.2248 -0.0508 0.0463  0.0023  309 GLY B N   
4239 C CA  . GLY B 274 ? 0.2020 0.2773 0.2764 -0.0431 0.0444  -0.0103 309 GLY B CA  
4240 C C   . GLY B 274 ? 0.1904 0.2750 0.2697 -0.0318 0.0425  -0.0181 309 GLY B C   
4241 O O   . GLY B 274 ? 0.1886 0.2821 0.2670 -0.0309 0.0425  -0.0120 309 GLY B O   
4242 N N   . HIS B 275 ? 0.2543 0.3353 0.3384 -0.0222 0.0388  -0.0319 310 HIS B N   
4243 C CA  . HIS B 275 ? 0.2137 0.2982 0.3004 -0.0064 0.0367  -0.0423 310 HIS B CA  
4244 C C   . HIS B 275 ? 0.2860 0.3361 0.3822 -0.0035 0.0319  -0.0425 310 HIS B C   
4245 O O   . HIS B 275 ? 0.2812 0.3093 0.3836 -0.0136 0.0315  -0.0348 310 HIS B O   
4246 C CB  . HIS B 275 ? 0.2372 0.3293 0.3146 0.0053  0.0336  -0.0595 310 HIS B CB  
4247 C CG  . HIS B 275 ? 0.2098 0.3398 0.2760 0.0062  0.0405  -0.0578 310 HIS B CG  
4248 N ND1 . HIS B 275 ? 0.2758 0.4410 0.3432 0.0173  0.0485  -0.0552 310 HIS B ND1 
4249 C CD2 . HIS B 275 ? 0.2265 0.3672 0.2825 -0.0033 0.0411  -0.0548 310 HIS B CD2 
4250 C CE1 . HIS B 275 ? 0.3243 0.5213 0.3826 0.0138  0.0550  -0.0497 310 HIS B CE1 
4251 N NE2 . HIS B 275 ? 0.3410 0.5213 0.3899 0.0013  0.0499  -0.0500 310 HIS B NE2 
4252 N N   . ILE B 276 ? 0.2914 0.3378 0.3903 0.0115  0.0289  -0.0497 311 ILE B N   
4253 C CA  . ILE B 276 ? 0.2666 0.2777 0.3740 0.0143  0.0228  -0.0484 311 ILE B CA  
4254 C C   . ILE B 276 ? 0.3081 0.3062 0.4139 0.0330  0.0145  -0.0665 311 ILE B C   
4255 O O   . ILE B 276 ? 0.2748 0.2971 0.3743 0.0496  0.0178  -0.0753 311 ILE B O   
4256 C CB  . ILE B 276 ? 0.3846 0.3942 0.4932 0.0136  0.0257  -0.0336 311 ILE B CB  
4257 C CG1 . ILE B 276 ? 0.3478 0.3224 0.4632 0.0190  0.0196  -0.0308 311 ILE B CG1 
4258 C CG2 . ILE B 276 ? 0.3343 0.3766 0.4429 0.0250  0.0269  -0.0348 311 ILE B CG2 
4259 C CD1 . ILE B 276 ? 0.3546 0.3182 0.4647 0.0132  0.0228  -0.0125 311 ILE B CD1 
4260 N N   . ARG B 277 ? 0.3018 0.2610 0.4135 0.0310  0.0035  -0.0710 312 ARG B N   
4261 C CA  . ARG B 277 ? 0.4129 0.3449 0.5182 0.0482  -0.0091 -0.0903 312 ARG B CA  
4262 C C   . ARG B 277 ? 0.3512 0.2442 0.4694 0.0479  -0.0177 -0.0825 312 ARG B C   
4263 O O   . ARG B 277 ? 0.3417 0.2205 0.4747 0.0295  -0.0177 -0.0653 312 ARG B O   
4264 C CB  . ARG B 277 ? 0.4401 0.3548 0.5380 0.0424  -0.0213 -0.1042 312 ARG B CB  
4265 C CG  . ARG B 277 ? 0.5782 0.4471 0.6669 0.0544  -0.0410 -0.1236 312 ARG B CG  
4266 C CD  . ARG B 277 ? 0.5975 0.4407 0.6928 0.0354  -0.0586 -0.1255 312 ARG B CD  
4267 N NE  . ARG B 277 ? 0.6585 0.5350 0.7472 0.0260  -0.0521 -0.1243 312 ARG B NE  
4268 C CZ  . ARG B 277 ? 0.7600 0.6318 0.8634 0.0054  -0.0621 -0.1172 312 ARG B CZ  
4269 N NH1 . ARG B 277 ? 0.7246 0.5611 0.8514 -0.0090 -0.0806 -0.1113 312 ARG B NH1 
4270 N NH2 . ARG B 277 ? 0.7335 0.6376 0.8307 -0.0013 -0.0547 -0.1139 312 ARG B NH2 
4271 N N   . ALA B 278 ? 0.3819 0.2586 0.4949 0.0694  -0.0238 -0.0928 313 ALA B N   
4272 C CA  . ALA B 278 ? 0.4083 0.2421 0.5321 0.0691  -0.0345 -0.0848 313 ALA B CA  
4273 C C   . ALA B 278 ? 0.4646 0.2536 0.5940 0.0571  -0.0528 -0.0905 313 ALA B C   
4274 O O   . ALA B 278 ? 0.5233 0.2948 0.6371 0.0673  -0.0653 -0.1136 313 ALA B O   
4275 C CB  . ALA B 278 ? 0.4831 0.3077 0.6000 0.0978  -0.0385 -0.0951 313 ALA B CB  
4276 N N   . GLU B 279 ? 0.4354 0.2061 0.5863 0.0353  -0.0549 -0.0684 314 GLU B N   
4277 C CA  . GLU B 279 ? 0.6010 0.3360 0.7680 0.0177  -0.0733 -0.0668 314 GLU B CA  
4278 C C   . GLU B 279 ? 0.4868 0.1862 0.6722 0.0106  -0.0796 -0.0462 314 GLU B C   
4279 O O   . GLU B 279 ? 0.4616 0.1775 0.6544 0.0049  -0.0630 -0.0224 314 GLU B O   
4280 C CB  . GLU B 279 ? 0.6828 0.4435 0.8691 -0.0069 -0.0655 -0.0505 314 GLU B CB  
4281 C CG  . GLU B 279 ? 0.8113 0.5503 1.0165 -0.0261 -0.0877 -0.0531 314 GLU B CG  
4282 C CD  . GLU B 279 ? 0.8370 0.5836 1.0115 -0.0121 -0.0949 -0.0834 314 GLU B CD  
4283 O OE1 . GLU B 279 ? 0.7502 0.5322 0.9094 -0.0007 -0.0750 -0.0849 314 GLU B OE1 
4284 O OE2 . GLU B 279 ? 0.9160 0.6525 1.0851 -0.0181 -0.1129 -0.0973 314 GLU B OE2 
4285 N N   . GLY B 280 ? 0.6967 0.3573 0.8784 0.0102  -0.1002 -0.0521 315 GLY B N   
4286 C CA  . GLY B 280 ? 0.6692 0.3077 0.8607 0.0012  -0.1038 -0.0295 315 GLY B CA  
4287 C C   . GLY B 280 ? 0.6490 0.2898 0.8369 0.0125  -0.0903 -0.0148 315 GLY B C   
4288 O O   . GLY B 280 ? 0.5689 0.2044 0.7404 0.0375  -0.0913 -0.0305 315 GLY B O   
4289 N N   . LYS B 281 ? 0.6591 0.3112 0.8604 -0.0040 -0.0772 0.0159  316 LYS B N   
4290 C CA  . LYS B 281 ? 0.6382 0.2909 0.8312 0.0041  -0.0654 0.0336  316 LYS B CA  
4291 C C   . LYS B 281 ? 0.5144 0.1968 0.7008 0.0147  -0.0497 0.0316  316 LYS B C   
4292 O O   . LYS B 281 ? 0.5408 0.2228 0.7163 0.0265  -0.0449 0.0407  316 LYS B O   
4293 C CB  . LYS B 281 ? 0.7598 0.4172 0.9623 -0.0156 -0.0545 0.0662  316 LYS B CB  
4294 C CG  . LYS B 281 ? 0.7630 0.4588 0.9766 -0.0303 -0.0362 0.0782  316 LYS B CG  
4295 C CD  . LYS B 281 ? 0.6810 0.3887 0.9026 -0.0449 -0.0221 0.1091  316 LYS B CD  
4296 C CE  . LYS B 281 ? 0.6244 0.3299 0.8207 -0.0359 -0.0074 0.1260  316 LYS B CE  
4297 N NZ  . LYS B 281 ? 0.6367 0.3573 0.8349 -0.0465 0.0098  0.1542  316 LYS B NZ  
4298 N N   . GLY B 282 ? 0.5123 0.2257 0.7008 0.0092  -0.0414 0.0218  317 GLY B N   
4299 C CA  . GLY B 282 ? 0.5219 0.2779 0.6929 0.0138  -0.0234 0.0219  317 GLY B CA  
4300 C C   . GLY B 282 ? 0.3943 0.1806 0.5592 0.0175  -0.0222 -0.0011 317 GLY B C   
4301 O O   . GLY B 282 ? 0.4205 0.2029 0.5793 0.0324  -0.0328 -0.0243 317 GLY B O   
4302 N N   . TYR B 283 ? 0.3609 0.1766 0.5246 0.0056  -0.0082 0.0059  318 TYR B N   
4303 C CA  . TYR B 283 ? 0.3366 0.1836 0.4921 0.0078  -0.0053 -0.0115 318 TYR B CA  
4304 C C   . TYR B 283 ? 0.3339 0.1904 0.5020 -0.0097 -0.0011 -0.0056 318 TYR B C   
4305 O O   . TYR B 283 ? 0.3536 0.2026 0.5365 -0.0226 0.0054  0.0154  318 TYR B O   
4306 C CB  . TYR B 283 ? 0.3126 0.1915 0.4506 0.0145  0.0059  -0.0096 318 TYR B CB  
4307 C CG  . TYR B 283 ? 0.3410 0.2188 0.4733 0.0332  -0.0002 -0.0152 318 TYR B CG  
4308 C CD1 . TYR B 283 ? 0.3444 0.2032 0.4742 0.0363  -0.0018 0.0001  318 TYR B CD1 
4309 C CD2 . TYR B 283 ? 0.3312 0.2281 0.4608 0.0498  -0.0038 -0.0346 318 TYR B CD2 
4310 C CE1 . TYR B 283 ? 0.3660 0.2257 0.4942 0.0547  -0.0092 -0.0038 318 TYR B CE1 
4311 C CE2 . TYR B 283 ? 0.3997 0.3013 0.5293 0.0696  -0.0079 -0.0382 318 TYR B CE2 
4312 C CZ  . TYR B 283 ? 0.3597 0.2424 0.4906 0.0717  -0.0119 -0.0231 318 TYR B CZ  
4313 O OH  . TYR B 283 ? 0.3830 0.2736 0.5173 0.0927  -0.0173 -0.0258 318 TYR B OH  
4314 N N   . ARG B 284 ? 0.3100 0.1843 0.4728 -0.0085 -0.0048 -0.0230 319 ARG B N   
4315 C CA  . ARG B 284 ? 0.3170 0.2070 0.4891 -0.0225 -0.0017 -0.0192 319 ARG B CA  
4316 C C   . ARG B 284 ? 0.2960 0.2210 0.4495 -0.0196 0.0102  -0.0231 319 ARG B C   
4317 O O   . ARG B 284 ? 0.2839 0.2231 0.4213 -0.0075 0.0090  -0.0376 319 ARG B O   
4318 C CB  . ARG B 284 ? 0.3637 0.2390 0.5440 -0.0262 -0.0211 -0.0347 319 ARG B CB  
4319 C CG  . ARG B 284 ? 0.3948 0.2915 0.5838 -0.0389 -0.0198 -0.0313 319 ARG B CG  
4320 C CD  . ARG B 284 ? 0.5117 0.4054 0.7352 -0.0561 -0.0167 -0.0061 319 ARG B CD  
4321 N NE  . ARG B 284 ? 0.5438 0.4440 0.7665 -0.0547 0.0046  0.0147  319 ARG B NE  
4322 C CZ  . ARG B 284 ? 0.4378 0.3600 0.6551 -0.0556 0.0236  0.0277  319 ARG B CZ  
4323 N NH1 . ARG B 284 ? 0.5436 0.4873 0.7621 -0.0594 0.0256  0.0253  319 ARG B NH1 
4324 N NH2 . ARG B 284 ? 0.3447 0.2629 0.5511 -0.0513 0.0397  0.0431  319 ARG B NH2 
4325 N N   . PHE B 285 ? 0.2421 0.1806 0.3988 -0.0299 0.0219  -0.0084 320 PHE B N   
4326 C CA  . PHE B 285 ? 0.3114 0.2765 0.4513 -0.0303 0.0307  -0.0096 320 PHE B CA  
4327 C C   . PHE B 285 ? 0.2795 0.2569 0.4250 -0.0365 0.0250  -0.0168 320 PHE B C   
4328 O O   . PHE B 285 ? 0.2850 0.2550 0.4519 -0.0453 0.0206  -0.0102 320 PHE B O   
4329 C CB  . PHE B 285 ? 0.2273 0.1915 0.3600 -0.0345 0.0452  0.0091  320 PHE B CB  
4330 C CG  . PHE B 285 ? 0.2351 0.2173 0.3484 -0.0362 0.0511  0.0090  320 PHE B CG  
4331 C CD1 . PHE B 285 ? 0.2573 0.2532 0.3540 -0.0323 0.0483  0.0024  320 PHE B CD1 
4332 C CD2 . PHE B 285 ? 0.2771 0.2622 0.3914 -0.0417 0.0589  0.0184  320 PHE B CD2 
4333 C CE1 . PHE B 285 ? 0.2248 0.2342 0.3057 -0.0373 0.0509  0.0053  320 PHE B CE1 
4334 C CE2 . PHE B 285 ? 0.2209 0.2152 0.3150 -0.0436 0.0621  0.0190  320 PHE B CE2 
4335 C CZ  . PHE B 285 ? 0.2478 0.2526 0.3253 -0.0430 0.0570  0.0126  320 PHE B CZ  
4336 N N   . VAL B 286 ? 0.2075 0.2057 0.3357 -0.0320 0.0241  -0.0286 321 VAL B N   
4337 C CA  . VAL B 286 ? 0.2935 0.3031 0.4197 -0.0357 0.0173  -0.0365 321 VAL B CA  
4338 C C   . VAL B 286 ? 0.1876 0.2201 0.3011 -0.0402 0.0272  -0.0286 321 VAL B C   
4339 O O   . VAL B 286 ? 0.1837 0.2348 0.2811 -0.0359 0.0307  -0.0322 321 VAL B O   
4340 C CB  . VAL B 286 ? 0.2443 0.2556 0.3542 -0.0235 0.0075  -0.0579 321 VAL B CB  
4341 C CG1 . VAL B 286 ? 0.2380 0.2564 0.3387 -0.0265 -0.0017 -0.0665 321 VAL B CG1 
4342 C CG2 . VAL B 286 ? 0.3651 0.3455 0.4825 -0.0169 -0.0038 -0.0666 321 VAL B CG2 
4343 N N   . PRO B 287 ? 0.1780 0.2092 0.3018 -0.0489 0.0312  -0.0156 322 PRO B N   
4344 C CA  . PRO B 287 ? 0.1660 0.2108 0.2753 -0.0525 0.0384  -0.0080 322 PRO B CA  
4345 C C   . PRO B 287 ? 0.1906 0.2559 0.2852 -0.0525 0.0328  -0.0169 322 PRO B C   
4346 O O   . PRO B 287 ? 0.1850 0.2525 0.2806 -0.0508 0.0226  -0.0276 322 PRO B O   
4347 C CB  . PRO B 287 ? 0.1634 0.2025 0.2896 -0.0575 0.0418  0.0049  322 PRO B CB  
4348 C CG  . PRO B 287 ? 0.2212 0.2461 0.3716 -0.0575 0.0424  0.0106  322 PRO B CG  
4349 C CD  . PRO B 287 ? 0.2036 0.2222 0.3543 -0.0548 0.0300  -0.0051 322 PRO B CD  
4350 N N   . VAL B 288 ? 0.1609 0.2392 0.2395 -0.0550 0.0383  -0.0108 323 VAL B N   
4351 C CA  . VAL B 288 ? 0.1811 0.2831 0.2454 -0.0556 0.0360  -0.0142 323 VAL B CA  
4352 C C   . VAL B 288 ? 0.2552 0.3571 0.3203 -0.0595 0.0291  -0.0141 323 VAL B C   
4353 O O   . VAL B 288 ? 0.2070 0.2966 0.2838 -0.0642 0.0291  -0.0050 323 VAL B O   
4354 C CB  . VAL B 288 ? 0.2327 0.3468 0.2856 -0.0624 0.0410  -0.0022 323 VAL B CB  
4355 C CG1 . VAL B 288 ? 0.2233 0.3155 0.2736 -0.0696 0.0426  0.0099  323 VAL B CG1 
4356 C CG2 . VAL B 288 ? 0.3316 0.4743 0.3725 -0.0646 0.0406  -0.0006 323 VAL B CG2 
4357 N N   . ASN B 289 ? 0.2293 0.3448 0.2814 -0.0554 0.0229  -0.0242 324 ASN B N   
4358 C CA  . ASN B 289 ? 0.2281 0.3449 0.2755 -0.0591 0.0130  -0.0239 324 ASN B CA  
4359 C C   . ASN B 289 ? 0.2407 0.3663 0.2809 -0.0674 0.0175  -0.0076 324 ASN B C   
4360 O O   . ASN B 289 ? 0.2115 0.3525 0.2385 -0.0694 0.0248  -0.0014 324 ASN B O   
4361 C CB  . ASN B 289 ? 0.2271 0.3544 0.2498 -0.0502 0.0066  -0.0389 324 ASN B CB  
4362 C CG  . ASN B 289 ? 0.3307 0.4547 0.3440 -0.0530 -0.0085 -0.0411 324 ASN B CG  
4363 O OD1 . ASN B 289 ? 0.3738 0.4832 0.4091 -0.0597 -0.0198 -0.0379 324 ASN B OD1 
4364 N ND2 . ASN B 289 ? 0.3324 0.4729 0.3136 -0.0480 -0.0085 -0.0440 324 ASN B ND2 
4365 N N   . TYR B 290 ? 0.1835 0.2997 0.2349 -0.0722 0.0120  0.0010  325 TYR B N   
4366 C CA  . TYR B 290 ? 0.2119 0.3299 0.2544 -0.0782 0.0138  0.0158  325 TYR B CA  
4367 C C   . TYR B 290 ? 0.1982 0.3365 0.2153 -0.0800 0.0109  0.0165  325 TYR B C   
4368 O O   . TYR B 290 ? 0.2144 0.3604 0.2208 -0.0758 0.0022  0.0069  325 TYR B O   
4369 C CB  . TYR B 290 ? 0.2171 0.3257 0.2772 -0.0788 0.0069  0.0238  325 TYR B CB  
4370 C CG  . TYR B 290 ? 0.2429 0.3470 0.2929 -0.0822 0.0073  0.0391  325 TYR B CG  
4371 C CD1 . TYR B 290 ? 0.2863 0.3720 0.3333 -0.0818 0.0165  0.0483  325 TYR B CD1 
4372 C CD2 . TYR B 290 ? 0.2800 0.3936 0.3187 -0.0849 -0.0035 0.0438  325 TYR B CD2 
4373 C CE1 . TYR B 290 ? 0.2683 0.3417 0.3030 -0.0838 0.0143  0.0612  325 TYR B CE1 
4374 C CE2 . TYR B 290 ? 0.2505 0.3560 0.2792 -0.0878 -0.0047 0.0590  325 TYR B CE2 
4375 C CZ  . TYR B 290 ? 0.2787 0.3627 0.3065 -0.0871 0.0038  0.0672  325 TYR B CZ  
4376 O OH  . TYR B 290 ? 0.3312 0.3998 0.3464 -0.0890 0.0001  0.0812  325 TYR B OH  
4377 N N   . SER B 291 ? 0.1979 0.3434 0.2034 -0.0866 0.0173  0.0289  326 SER B N   
4378 C CA  . SER B 291 ? 0.2374 0.4070 0.2214 -0.0900 0.0182  0.0357  326 SER B CA  
4379 C C   . SER B 291 ? 0.2747 0.4362 0.2530 -0.1015 0.0160  0.0556  326 SER B C   
4380 O O   . SER B 291 ? 0.3212 0.4634 0.3063 -0.1069 0.0177  0.0626  326 SER B O   
4381 C CB  . SER B 291 ? 0.2108 0.4053 0.1915 -0.0878 0.0287  0.0341  326 SER B CB  
4382 O OG  . SER B 291 ? 0.2665 0.4900 0.2279 -0.0886 0.0324  0.0424  326 SER B OG  
4383 N N   . VAL B 292 ? 0.2976 0.4685 0.2599 -0.1046 0.0106  0.0645  327 VAL B N   
4384 C CA  . VAL B 292 ? 0.2600 0.4199 0.2152 -0.1161 0.0066  0.0851  327 VAL B CA  
4385 C C   . VAL B 292 ? 0.4303 0.6131 0.3783 -0.1266 0.0130  0.0988  327 VAL B C   
4386 O O   . VAL B 292 ? 0.4151 0.6305 0.3553 -0.1217 0.0197  0.0965  327 VAL B O   
4387 C CB  . VAL B 292 ? 0.3230 0.4809 0.2655 -0.1155 -0.0041 0.0924  327 VAL B CB  
4388 C CG1 . VAL B 292 ? 0.3928 0.5351 0.3263 -0.1275 -0.0092 0.1155  327 VAL B CG1 
4389 C CG2 . VAL B 292 ? 0.3089 0.4490 0.2681 -0.1062 -0.0125 0.0823  327 VAL B CG2 
4390 N N   . VAL B 293 ? 0.3778 0.5347 0.3322 -0.1321 0.0070  0.1064  328 VAL B N   
4391 C CA  . VAL B 293 ? 0.4580 0.6258 0.4169 -0.1376 0.0056  0.1149  328 VAL B CA  
4392 C C   . VAL B 293 ? 0.4678 0.6271 0.4180 -0.1468 -0.0036 0.1321  328 VAL B C   
4393 O O   . VAL B 293 ? 0.5214 0.6442 0.4659 -0.1501 -0.0127 0.1363  328 VAL B O   
4394 C CB  . VAL B 293 ? 0.4634 0.6076 0.4317 -0.1401 0.0019  0.1116  328 VAL B CB  
4395 C CG1 . VAL B 293 ? 0.5040 0.6583 0.4780 -0.1503 -0.0046 0.1252  328 VAL B CG1 
4396 C CG2 . VAL B 293 ? 0.3285 0.4829 0.3066 -0.1310 0.0109  0.0966  328 VAL B CG2 
4397 N N   . ASN B 294 ? 0.5042 0.6958 0.4526 -0.1493 -0.0003 0.1425  329 ASN B N   
4398 C CA  . ASN B 294 ? 0.5711 0.7563 0.5126 -0.1590 -0.0088 0.1606  329 ASN B CA  
4399 C C   . ASN B 294 ? 0.5167 0.7129 0.4716 -0.1704 -0.0127 0.1748  329 ASN B C   
4400 O O   . ASN B 294 ? 0.6329 0.8677 0.5979 -0.1683 -0.0033 0.1784  329 ASN B O   
4401 C CB  . ASN B 294 ? 0.5096 0.7208 0.4348 -0.1542 -0.0032 0.1659  329 ASN B CB  
4402 C CG  . ASN B 294 ? 0.5913 0.7924 0.5013 -0.1458 -0.0045 0.1551  329 ASN B CG  
4403 O OD1 . ASN B 294 ? 0.5290 0.7532 0.4288 -0.1358 0.0036  0.1435  329 ASN B OD1 
4404 N ND2 . ASN B 294 ? 0.5669 0.7327 0.4743 -0.1491 -0.0159 0.1595  329 ASN B ND2 
# 
