data_8KEL
# 
_entry.id   8KEL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8KEL         pdb_00008kel 10.2210/pdb8kel/pdb 
WWPDB D_1300040012 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8KEL 
_pdbx_database_status.recvd_initial_deposition_date   2023-08-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yanli@hust.edu.cn 
_pdbx_contact_author.name_first         Yan 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1963-839X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, Y.H.' 1 0000-0002-5983-0151 
'Ma, B.'    2 ?                   
'Kang, Y.'  3 ?                   
'Liu, B.'   4 ?                   
'Li, Y.'    5 0000-0003-1963-839X 
# 
_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                     'Structure of EXOD at 2.4 Angstroms resolution' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Liu, Y.H.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           Exodeoxyribonuclease 
_entity.formula_weight             25995.654 
_entity.pdbx_number_of_molecules   4 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PHE n 
1 3   ASP n 
1 4   PHE n 
1 5   ILE n 
1 6   ILE n 
1 7   ASP n 
1 8   PHE n 
1 9   GLU n 
1 10  THR n 
1 11  MET n 
1 12  GLY n 
1 13  SER n 
1 14  GLY n 
1 15  GLU n 
1 16  LYS n 
1 17  ALA n 
1 18  ALA n 
1 19  VAL n 
1 20  ILE n 
1 21  ASP n 
1 22  LEU n 
1 23  ALA n 
1 24  VAL n 
1 25  ILE n 
1 26  ALA n 
1 27  PHE n 
1 28  ASP n 
1 29  PRO n 
1 30  ASN n 
1 31  PRO n 
1 32  GLU n 
1 33  VAL n 
1 34  VAL n 
1 35  GLU n 
1 36  THR n 
1 37  PHE n 
1 38  ASP n 
1 39  GLU n 
1 40  LEU n 
1 41  VAL n 
1 42  SER n 
1 43  ARG n 
1 44  GLY n 
1 45  ILE n 
1 46  LYS n 
1 47  ILE n 
1 48  LYS n 
1 49  PHE n 
1 50  ASP n 
1 51  LEU n 
1 52  LYS n 
1 53  SER n 
1 54  GLN n 
1 55  LYS n 
1 56  GLY n 
1 57  HIS n 
1 58  ARG n 
1 59  LEU n 
1 60  PHE n 
1 61  THR n 
1 62  LYS n 
1 63  SER n 
1 64  THR n 
1 65  ILE n 
1 66  GLU n 
1 67  TRP n 
1 68  TRP n 
1 69  LYS n 
1 70  ASN n 
1 71  GLN n 
1 72  SER n 
1 73  PRO n 
1 74  GLU n 
1 75  ALA n 
1 76  ARG n 
1 77  LYS n 
1 78  ASN n 
1 79  ILE n 
1 80  ALA n 
1 81  PRO n 
1 82  SER n 
1 83  ASP n 
1 84  GLU n 
1 85  ASP n 
1 86  VAL n 
1 87  SER n 
1 88  THR n 
1 89  ILE n 
1 90  ASP n 
1 91  GLY n 
1 92  ILE n 
1 93  ALA n 
1 94  LYS n 
1 95  PHE n 
1 96  ASN n 
1 97  ASP n 
1 98  TYR n 
1 99  ILE n 
1 100 ASN n 
1 101 ALA n 
1 102 HIS n 
1 103 ASN n 
1 104 ILE n 
1 105 ASP n 
1 106 PRO n 
1 107 TRP n 
1 108 LYS n 
1 109 SER n 
1 110 GLN n 
1 111 GLY n 
1 112 TRP n 
1 113 CYS n 
1 114 ARG n 
1 115 GLY n 
1 116 MET n 
1 117 SER n 
1 118 PHE n 
1 119 ASP n 
1 120 PHE n 
1 121 PRO n 
1 122 ILE n 
1 123 LEU n 
1 124 VAL n 
1 125 ASP n 
1 126 LEU n 
1 127 ILE n 
1 128 ARG n 
1 129 ASP n 
1 130 ILE n 
1 131 GLN n 
1 132 ARG n 
1 133 LEU n 
1 134 ASN n 
1 135 GLY n 
1 136 VAL n 
1 137 SER n 
1 138 GLU n 
1 139 ASN n 
1 140 GLU n 
1 141 LEU n 
1 142 ASP n 
1 143 THR n 
1 144 PHE n 
1 145 LYS n 
1 146 LEU n 
1 147 GLU n 
1 148 PRO n 
1 149 CYS n 
1 150 LYS n 
1 151 PHE n 
1 152 TRP n 
1 153 ASN n 
1 154 GLN n 
1 155 ARG n 
1 156 ASP n 
1 157 ILE n 
1 158 ARG n 
1 159 THR n 
1 160 ARG n 
1 161 ILE n 
1 162 GLU n 
1 163 ALA n 
1 164 LEU n 
1 165 LEU n 
1 166 LEU n 
1 167 VAL n 
1 168 ARG n 
1 169 ASP n 
1 170 MET n 
1 171 THR n 
1 172 THR n 
1 173 CYS n 
1 174 PRO n 
1 175 LEU n 
1 176 PRO n 
1 177 LYS n 
1 178 GLY n 
1 179 THR n 
1 180 LEU n 
1 181 ASP n 
1 182 GLY n 
1 183 PHE n 
1 184 VAL n 
1 185 ALA n 
1 186 HIS n 
1 187 ASP n 
1 188 SER n 
1 189 ILE n 
1 190 HIS n 
1 191 ASP n 
1 192 CYS n 
1 193 ALA n 
1 194 LYS n 
1 195 ASP n 
1 196 ILE n 
1 197 LEU n 
1 198 MET n 
1 199 MET n 
1 200 LYS n 
1 201 TYR n 
1 202 ALA n 
1 203 LEU n 
1 204 ARG n 
1 205 TYR n 
1 206 ALA n 
1 207 MET n 
1 208 GLY n 
1 209 LEU n 
1 210 GLU n 
1 211 ASP n 
1 212 ALA n 
1 213 PRO n 
1 214 SER n 
1 215 GLU n 
1 216 GLU n 
1 217 GLU n 
1 218 CYS n 
1 219 ASP n 
1 220 PRO n 
1 221 LEU n 
1 222 SER n 
1 223 LEU n 
1 224 PRO n 
1 225 THR n 
1 226 LYS n 
1 227 ARG 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                   227 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 dexA 
_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      'Escherichia coli 0.1197' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1005443 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   PHE 2   2   2   PHE PHE A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TRP 67  67  67  TRP TRP A . n 
A 1 68  TRP 68  68  68  TRP TRP A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 HIS 102 102 102 HIS HIS A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 TRP 112 112 112 TRP TRP A . n 
A 1 113 CYS 113 113 113 CYS CYS A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 MET 116 116 116 MET MET A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 ASP 119 119 119 ASP ASP A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 CYS 149 149 149 CYS CYS A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 TRP 152 152 152 TRP TRP A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 CYS 173 173 173 CYS CYS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 HIS 190 190 190 HIS HIS A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 MET 198 198 198 MET MET A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 CYS 218 218 218 CYS CYS A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 SER 222 222 ?   ?   ?   A . n 
A 1 223 LEU 223 223 ?   ?   ?   A . n 
A 1 224 PRO 224 224 ?   ?   ?   A . n 
A 1 225 THR 225 225 ?   ?   ?   A . n 
A 1 226 LYS 226 226 ?   ?   ?   A . n 
A 1 227 ARG 227 227 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   PHE 2   2   2   PHE PHE B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   PHE 4   4   4   PHE PHE B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   ASP 7   7   7   ASP ASP B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   GLU 9   9   9   GLU GLU B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  MET 11  11  11  MET MET B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  PRO 31  31  31  PRO PRO B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  ARG 43  43  43  ARG ARG B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  GLN 54  54  54  GLN GLN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  HIS 57  57  57  HIS HIS B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  PHE 60  60  60  PHE PHE B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  LYS 62  62  62  LYS LYS B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TRP 67  67  67  TRP TRP B . n 
B 1 68  TRP 68  68  68  TRP TRP B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  GLN 71  71  71  GLN GLN B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  ASN 78  78  78  ASN ASN B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  PRO 81  81  81  PRO PRO B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  SER 87  87  87  SER SER B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 ASN 100 100 100 ASN ASN B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 HIS 102 102 102 HIS HIS B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 TRP 107 107 107 TRP TRP B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 SER 109 109 109 SER SER B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 TRP 112 112 112 TRP TRP B . n 
B 1 113 CYS 113 113 113 CYS CYS B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 MET 116 116 116 MET MET B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 ASP 119 119 119 ASP ASP B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 ARG 128 128 128 ARG ARG B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 VAL 136 136 136 VAL VAL B . n 
B 1 137 SER 137 137 137 SER SER B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 THR 143 143 143 THR THR B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 PRO 148 148 148 PRO PRO B . n 
B 1 149 CYS 149 149 149 CYS CYS B . n 
B 1 150 LYS 150 150 150 LYS LYS B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 TRP 152 152 152 TRP TRP B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 THR 159 159 159 THR THR B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 ILE 161 161 161 ILE ILE B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 ARG 168 168 168 ARG ARG B . n 
B 1 169 ASP 169 169 169 ASP ASP B . n 
B 1 170 MET 170 170 170 MET MET B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 THR 172 172 172 THR THR B . n 
B 1 173 CYS 173 173 173 CYS CYS B . n 
B 1 174 PRO 174 174 174 PRO PRO B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 PRO 176 176 176 PRO PRO B . n 
B 1 177 LYS 177 177 177 LYS LYS B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 HIS 186 186 186 HIS HIS B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 HIS 190 190 190 HIS HIS B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 CYS 192 192 192 CYS CYS B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 MET 198 198 198 MET MET B . n 
B 1 199 MET 199 199 199 MET MET B . n 
B 1 200 LYS 200 200 200 LYS LYS B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 ALA 202 202 202 ALA ALA B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 TYR 205 205 205 TYR TYR B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 MET 207 207 207 MET MET B . n 
B 1 208 GLY 208 208 208 GLY GLY B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 PRO 213 213 213 PRO PRO B . n 
B 1 214 SER 214 214 214 SER SER B . n 
B 1 215 GLU 215 215 215 GLU GLU B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 CYS 218 218 218 CYS CYS B . n 
B 1 219 ASP 219 219 219 ASP ASP B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 PRO 224 224 224 PRO PRO B . n 
B 1 225 THR 225 225 ?   ?   ?   B . n 
B 1 226 LYS 226 226 ?   ?   ?   B . n 
B 1 227 ARG 227 227 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   PHE 2   2   2   PHE PHE C . n 
C 1 3   ASP 3   3   3   ASP ASP C . n 
C 1 4   PHE 4   4   4   PHE PHE C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   ILE 6   6   6   ILE ILE C . n 
C 1 7   ASP 7   7   7   ASP ASP C . n 
C 1 8   PHE 8   8   8   PHE PHE C . n 
C 1 9   GLU 9   9   9   GLU GLU C . n 
C 1 10  THR 10  10  10  THR THR C . n 
C 1 11  MET 11  11  11  MET MET C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  SER 13  13  13  SER SER C . n 
C 1 14  GLY 14  14  14  GLY GLY C . n 
C 1 15  GLU 15  15  15  GLU GLU C . n 
C 1 16  LYS 16  16  16  LYS LYS C . n 
C 1 17  ALA 17  17  17  ALA ALA C . n 
C 1 18  ALA 18  18  18  ALA ALA C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  ILE 20  20  20  ILE ILE C . n 
C 1 21  ASP 21  21  21  ASP ASP C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  VAL 24  24  24  VAL VAL C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  ALA 26  26  26  ALA ALA C . n 
C 1 27  PHE 27  27  27  PHE PHE C . n 
C 1 28  ASP 28  28  28  ASP ASP C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ASN 30  30  30  ASN ASN C . n 
C 1 31  PRO 31  31  31  PRO PRO C . n 
C 1 32  GLU 32  32  ?   ?   ?   C . n 
C 1 33  VAL 33  33  ?   ?   ?   C . n 
C 1 34  VAL 34  34  ?   ?   ?   C . n 
C 1 35  GLU 35  35  ?   ?   ?   C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  ASP 38  38  38  ASP ASP C . n 
C 1 39  GLU 39  39  39  GLU GLU C . n 
C 1 40  LEU 40  40  40  LEU LEU C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  ARG 43  43  43  ARG ARG C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  ILE 45  45  45  ILE ILE C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  ILE 47  47  47  ILE ILE C . n 
C 1 48  LYS 48  48  48  LYS LYS C . n 
C 1 49  PHE 49  49  49  PHE PHE C . n 
C 1 50  ASP 50  50  50  ASP ASP C . n 
C 1 51  LEU 51  51  51  LEU LEU C . n 
C 1 52  LYS 52  52  52  LYS LYS C . n 
C 1 53  SER 53  53  53  SER SER C . n 
C 1 54  GLN 54  54  54  GLN GLN C . n 
C 1 55  LYS 55  55  55  LYS LYS C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  HIS 57  57  57  HIS HIS C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  LEU 59  59  59  LEU LEU C . n 
C 1 60  PHE 60  60  60  PHE PHE C . n 
C 1 61  THR 61  61  61  THR THR C . n 
C 1 62  LYS 62  62  62  LYS LYS C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  THR 64  64  64  THR THR C . n 
C 1 65  ILE 65  65  65  ILE ILE C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  TRP 67  67  67  TRP TRP C . n 
C 1 68  TRP 68  68  68  TRP TRP C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  ASN 70  70  70  ASN ASN C . n 
C 1 71  GLN 71  71  71  GLN GLN C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  GLU 74  74  74  GLU GLU C . n 
C 1 75  ALA 75  75  75  ALA ALA C . n 
C 1 76  ARG 76  76  76  ARG ARG C . n 
C 1 77  LYS 77  77  77  LYS LYS C . n 
C 1 78  ASN 78  78  78  ASN ASN C . n 
C 1 79  ILE 79  79  79  ILE ILE C . n 
C 1 80  ALA 80  80  80  ALA ALA C . n 
C 1 81  PRO 81  81  81  PRO PRO C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  GLU 84  84  84  GLU GLU C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  SER 87  87  87  SER SER C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ILE 89  89  89  ILE ILE C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  GLY 91  91  91  GLY GLY C . n 
C 1 92  ILE 92  92  92  ILE ILE C . n 
C 1 93  ALA 93  93  93  ALA ALA C . n 
C 1 94  LYS 94  94  94  LYS LYS C . n 
C 1 95  PHE 95  95  95  PHE PHE C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  TYR 98  98  98  TYR TYR C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 ASN 100 100 100 ASN ASN C . n 
C 1 101 ALA 101 101 101 ALA ALA C . n 
C 1 102 HIS 102 102 102 HIS HIS C . n 
C 1 103 ASN 103 103 103 ASN ASN C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 ASP 105 105 105 ASP ASP C . n 
C 1 106 PRO 106 106 106 PRO PRO C . n 
C 1 107 TRP 107 107 107 TRP TRP C . n 
C 1 108 LYS 108 108 108 LYS LYS C . n 
C 1 109 SER 109 109 109 SER SER C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 GLY 111 111 111 GLY GLY C . n 
C 1 112 TRP 112 112 112 TRP TRP C . n 
C 1 113 CYS 113 113 113 CYS CYS C . n 
C 1 114 ARG 114 114 114 ARG ARG C . n 
C 1 115 GLY 115 115 115 GLY GLY C . n 
C 1 116 MET 116 116 116 MET MET C . n 
C 1 117 SER 117 117 117 SER SER C . n 
C 1 118 PHE 118 118 118 PHE PHE C . n 
C 1 119 ASP 119 119 119 ASP ASP C . n 
C 1 120 PHE 120 120 120 PHE PHE C . n 
C 1 121 PRO 121 121 121 PRO PRO C . n 
C 1 122 ILE 122 122 122 ILE ILE C . n 
C 1 123 LEU 123 123 123 LEU LEU C . n 
C 1 124 VAL 124 124 124 VAL VAL C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 ILE 127 127 127 ILE ILE C . n 
C 1 128 ARG 128 128 128 ARG ARG C . n 
C 1 129 ASP 129 129 129 ASP ASP C . n 
C 1 130 ILE 130 130 130 ILE ILE C . n 
C 1 131 GLN 131 131 131 GLN GLN C . n 
C 1 132 ARG 132 132 132 ARG ARG C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 GLY 135 135 135 GLY GLY C . n 
C 1 136 VAL 136 136 136 VAL VAL C . n 
C 1 137 SER 137 137 137 SER SER C . n 
C 1 138 GLU 138 138 138 GLU GLU C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 GLU 140 140 140 GLU GLU C . n 
C 1 141 LEU 141 141 141 LEU LEU C . n 
C 1 142 ASP 142 142 142 ASP ASP C . n 
C 1 143 THR 143 143 143 THR THR C . n 
C 1 144 PHE 144 144 144 PHE PHE C . n 
C 1 145 LYS 145 145 145 LYS LYS C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 PRO 148 148 148 PRO PRO C . n 
C 1 149 CYS 149 149 149 CYS CYS C . n 
C 1 150 LYS 150 150 150 LYS LYS C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 TRP 152 152 152 TRP TRP C . n 
C 1 153 ASN 153 153 153 ASN ASN C . n 
C 1 154 GLN 154 154 154 GLN GLN C . n 
C 1 155 ARG 155 155 155 ARG ARG C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 ILE 157 157 157 ILE ILE C . n 
C 1 158 ARG 158 158 158 ARG ARG C . n 
C 1 159 THR 159 159 159 THR THR C . n 
C 1 160 ARG 160 160 160 ARG ARG C . n 
C 1 161 ILE 161 161 161 ILE ILE C . n 
C 1 162 GLU 162 162 162 GLU GLU C . n 
C 1 163 ALA 163 163 163 ALA ALA C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 LEU 165 165 165 LEU LEU C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 VAL 167 167 167 VAL VAL C . n 
C 1 168 ARG 168 168 168 ARG ARG C . n 
C 1 169 ASP 169 169 169 ASP ASP C . n 
C 1 170 MET 170 170 170 MET MET C . n 
C 1 171 THR 171 171 171 THR THR C . n 
C 1 172 THR 172 172 172 THR THR C . n 
C 1 173 CYS 173 173 173 CYS CYS C . n 
C 1 174 PRO 174 174 ?   ?   ?   C . n 
C 1 175 LEU 175 175 ?   ?   ?   C . n 
C 1 176 PRO 176 176 ?   ?   ?   C . n 
C 1 177 LYS 177 177 ?   ?   ?   C . n 
C 1 178 GLY 178 178 ?   ?   ?   C . n 
C 1 179 THR 179 179 179 THR THR C . n 
C 1 180 LEU 180 180 180 LEU LEU C . n 
C 1 181 ASP 181 181 181 ASP ASP C . n 
C 1 182 GLY 182 182 182 GLY GLY C . n 
C 1 183 PHE 183 183 183 PHE PHE C . n 
C 1 184 VAL 184 184 184 VAL VAL C . n 
C 1 185 ALA 185 185 185 ALA ALA C . n 
C 1 186 HIS 186 186 186 HIS HIS C . n 
C 1 187 ASP 187 187 187 ASP ASP C . n 
C 1 188 SER 188 188 188 SER SER C . n 
C 1 189 ILE 189 189 189 ILE ILE C . n 
C 1 190 HIS 190 190 190 HIS HIS C . n 
C 1 191 ASP 191 191 191 ASP ASP C . n 
C 1 192 CYS 192 192 192 CYS CYS C . n 
C 1 193 ALA 193 193 193 ALA ALA C . n 
C 1 194 LYS 194 194 194 LYS LYS C . n 
C 1 195 ASP 195 195 195 ASP ASP C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 MET 198 198 198 MET MET C . n 
C 1 199 MET 199 199 199 MET MET C . n 
C 1 200 LYS 200 200 200 LYS LYS C . n 
C 1 201 TYR 201 201 201 TYR TYR C . n 
C 1 202 ALA 202 202 202 ALA ALA C . n 
C 1 203 LEU 203 203 203 LEU LEU C . n 
C 1 204 ARG 204 204 204 ARG ARG C . n 
C 1 205 TYR 205 205 205 TYR TYR C . n 
C 1 206 ALA 206 206 206 ALA ALA C . n 
C 1 207 MET 207 207 ?   ?   ?   C . n 
C 1 208 GLY 208 208 ?   ?   ?   C . n 
C 1 209 LEU 209 209 ?   ?   ?   C . n 
C 1 210 GLU 210 210 ?   ?   ?   C . n 
C 1 211 ASP 211 211 ?   ?   ?   C . n 
C 1 212 ALA 212 212 ?   ?   ?   C . n 
C 1 213 PRO 213 213 ?   ?   ?   C . n 
C 1 214 SER 214 214 ?   ?   ?   C . n 
C 1 215 GLU 215 215 ?   ?   ?   C . n 
C 1 216 GLU 216 216 ?   ?   ?   C . n 
C 1 217 GLU 217 217 ?   ?   ?   C . n 
C 1 218 CYS 218 218 ?   ?   ?   C . n 
C 1 219 ASP 219 219 ?   ?   ?   C . n 
C 1 220 PRO 220 220 ?   ?   ?   C . n 
C 1 221 LEU 221 221 ?   ?   ?   C . n 
C 1 222 SER 222 222 ?   ?   ?   C . n 
C 1 223 LEU 223 223 ?   ?   ?   C . n 
C 1 224 PRO 224 224 ?   ?   ?   C . n 
C 1 225 THR 225 225 ?   ?   ?   C . n 
C 1 226 LYS 226 226 ?   ?   ?   C . n 
C 1 227 ARG 227 227 ?   ?   ?   C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   PHE 2   2   2   PHE PHE D . n 
D 1 3   ASP 3   3   3   ASP ASP D . n 
D 1 4   PHE 4   4   4   PHE PHE D . n 
D 1 5   ILE 5   5   5   ILE ILE D . n 
D 1 6   ILE 6   6   6   ILE ILE D . n 
D 1 7   ASP 7   7   7   ASP ASP D . n 
D 1 8   PHE 8   8   8   PHE PHE D . n 
D 1 9   GLU 9   9   9   GLU GLU D . n 
D 1 10  THR 10  10  10  THR THR D . n 
D 1 11  MET 11  11  11  MET MET D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  SER 13  13  13  SER SER D . n 
D 1 14  GLY 14  14  14  GLY GLY D . n 
D 1 15  GLU 15  15  15  GLU GLU D . n 
D 1 16  LYS 16  16  16  LYS LYS D . n 
D 1 17  ALA 17  17  17  ALA ALA D . n 
D 1 18  ALA 18  18  18  ALA ALA D . n 
D 1 19  VAL 19  19  19  VAL VAL D . n 
D 1 20  ILE 20  20  20  ILE ILE D . n 
D 1 21  ASP 21  21  21  ASP ASP D . n 
D 1 22  LEU 22  22  22  LEU LEU D . n 
D 1 23  ALA 23  23  23  ALA ALA D . n 
D 1 24  VAL 24  24  24  VAL VAL D . n 
D 1 25  ILE 25  25  25  ILE ILE D . n 
D 1 26  ALA 26  26  26  ALA ALA D . n 
D 1 27  PHE 27  27  27  PHE PHE D . n 
D 1 28  ASP 28  28  28  ASP ASP D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ASN 30  30  30  ASN ASN D . n 
D 1 31  PRO 31  31  31  PRO PRO D . n 
D 1 32  GLU 32  32  32  GLU GLU D . n 
D 1 33  VAL 33  33  ?   ?   ?   D . n 
D 1 34  VAL 34  34  ?   ?   ?   D . n 
D 1 35  GLU 35  35  ?   ?   ?   D . n 
D 1 36  THR 36  36  36  THR THR D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  ASP 38  38  38  ASP ASP D . n 
D 1 39  GLU 39  39  39  GLU GLU D . n 
D 1 40  LEU 40  40  40  LEU LEU D . n 
D 1 41  VAL 41  41  41  VAL VAL D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  ARG 43  43  43  ARG ARG D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  ILE 45  45  45  ILE ILE D . n 
D 1 46  LYS 46  46  46  LYS LYS D . n 
D 1 47  ILE 47  47  47  ILE ILE D . n 
D 1 48  LYS 48  48  48  LYS LYS D . n 
D 1 49  PHE 49  49  49  PHE PHE D . n 
D 1 50  ASP 50  50  50  ASP ASP D . n 
D 1 51  LEU 51  51  51  LEU LEU D . n 
D 1 52  LYS 52  52  52  LYS LYS D . n 
D 1 53  SER 53  53  53  SER SER D . n 
D 1 54  GLN 54  54  54  GLN GLN D . n 
D 1 55  LYS 55  55  55  LYS LYS D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  HIS 57  57  57  HIS HIS D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  LEU 59  59  59  LEU LEU D . n 
D 1 60  PHE 60  60  60  PHE PHE D . n 
D 1 61  THR 61  61  61  THR THR D . n 
D 1 62  LYS 62  62  62  LYS LYS D . n 
D 1 63  SER 63  63  63  SER SER D . n 
D 1 64  THR 64  64  64  THR THR D . n 
D 1 65  ILE 65  65  65  ILE ILE D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  TRP 67  67  67  TRP TRP D . n 
D 1 68  TRP 68  68  68  TRP TRP D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  ASN 70  70  70  ASN ASN D . n 
D 1 71  GLN 71  71  71  GLN GLN D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  GLU 74  74  74  GLU GLU D . n 
D 1 75  ALA 75  75  75  ALA ALA D . n 
D 1 76  ARG 76  76  76  ARG ARG D . n 
D 1 77  LYS 77  77  77  LYS LYS D . n 
D 1 78  ASN 78  78  78  ASN ASN D . n 
D 1 79  ILE 79  79  79  ILE ILE D . n 
D 1 80  ALA 80  80  80  ALA ALA D . n 
D 1 81  PRO 81  81  81  PRO PRO D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  GLU 84  84  84  GLU GLU D . n 
D 1 85  ASP 85  85  85  ASP ASP D . n 
D 1 86  VAL 86  86  86  VAL VAL D . n 
D 1 87  SER 87  87  87  SER SER D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ILE 89  89  89  ILE ILE D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  GLY 91  91  91  GLY GLY D . n 
D 1 92  ILE 92  92  92  ILE ILE D . n 
D 1 93  ALA 93  93  93  ALA ALA D . n 
D 1 94  LYS 94  94  94  LYS LYS D . n 
D 1 95  PHE 95  95  95  PHE PHE D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  ASP 97  97  97  ASP ASP D . n 
D 1 98  TYR 98  98  98  TYR TYR D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 ASN 100 100 100 ASN ASN D . n 
D 1 101 ALA 101 101 101 ALA ALA D . n 
D 1 102 HIS 102 102 102 HIS HIS D . n 
D 1 103 ASN 103 103 103 ASN ASN D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 ASP 105 105 105 ASP ASP D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 TRP 107 107 107 TRP TRP D . n 
D 1 108 LYS 108 108 108 LYS LYS D . n 
D 1 109 SER 109 109 109 SER SER D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 GLY 111 111 111 GLY GLY D . n 
D 1 112 TRP 112 112 112 TRP TRP D . n 
D 1 113 CYS 113 113 113 CYS CYS D . n 
D 1 114 ARG 114 114 114 ARG ARG D . n 
D 1 115 GLY 115 115 115 GLY GLY D . n 
D 1 116 MET 116 116 116 MET MET D . n 
D 1 117 SER 117 117 117 SER SER D . n 
D 1 118 PHE 118 118 118 PHE PHE D . n 
D 1 119 ASP 119 119 119 ASP ASP D . n 
D 1 120 PHE 120 120 120 PHE PHE D . n 
D 1 121 PRO 121 121 121 PRO PRO D . n 
D 1 122 ILE 122 122 122 ILE ILE D . n 
D 1 123 LEU 123 123 123 LEU LEU D . n 
D 1 124 VAL 124 124 124 VAL VAL D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 ILE 127 127 127 ILE ILE D . n 
D 1 128 ARG 128 128 128 ARG ARG D . n 
D 1 129 ASP 129 129 129 ASP ASP D . n 
D 1 130 ILE 130 130 130 ILE ILE D . n 
D 1 131 GLN 131 131 131 GLN GLN D . n 
D 1 132 ARG 132 132 132 ARG ARG D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 GLY 135 135 135 GLY GLY D . n 
D 1 136 VAL 136 136 136 VAL VAL D . n 
D 1 137 SER 137 137 137 SER SER D . n 
D 1 138 GLU 138 138 138 GLU GLU D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 GLU 140 140 140 GLU GLU D . n 
D 1 141 LEU 141 141 141 LEU LEU D . n 
D 1 142 ASP 142 142 142 ASP ASP D . n 
D 1 143 THR 143 143 143 THR THR D . n 
D 1 144 PHE 144 144 144 PHE PHE D . n 
D 1 145 LYS 145 145 145 LYS LYS D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 PRO 148 148 148 PRO PRO D . n 
D 1 149 CYS 149 149 149 CYS CYS D . n 
D 1 150 LYS 150 150 150 LYS LYS D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 TRP 152 152 152 TRP TRP D . n 
D 1 153 ASN 153 153 153 ASN ASN D . n 
D 1 154 GLN 154 154 154 GLN GLN D . n 
D 1 155 ARG 155 155 155 ARG ARG D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 ILE 157 157 157 ILE ILE D . n 
D 1 158 ARG 158 158 158 ARG ARG D . n 
D 1 159 THR 159 159 159 THR THR D . n 
D 1 160 ARG 160 160 160 ARG ARG D . n 
D 1 161 ILE 161 161 161 ILE ILE D . n 
D 1 162 GLU 162 162 162 GLU GLU D . n 
D 1 163 ALA 163 163 163 ALA ALA D . n 
D 1 164 LEU 164 164 164 LEU LEU D . n 
D 1 165 LEU 165 165 165 LEU LEU D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 VAL 167 167 167 VAL VAL D . n 
D 1 168 ARG 168 168 168 ARG ARG D . n 
D 1 169 ASP 169 169 169 ASP ASP D . n 
D 1 170 MET 170 170 170 MET MET D . n 
D 1 171 THR 171 171 171 THR THR D . n 
D 1 172 THR 172 172 172 THR THR D . n 
D 1 173 CYS 173 173 173 CYS CYS D . n 
D 1 174 PRO 174 174 174 PRO PRO D . n 
D 1 175 LEU 175 175 175 LEU LEU D . n 
D 1 176 PRO 176 176 176 PRO PRO D . n 
D 1 177 LYS 177 177 ?   ?   ?   D . n 
D 1 178 GLY 178 178 ?   ?   ?   D . n 
D 1 179 THR 179 179 ?   ?   ?   D . n 
D 1 180 LEU 180 180 ?   ?   ?   D . n 
D 1 181 ASP 181 181 ?   ?   ?   D . n 
D 1 182 GLY 182 182 ?   ?   ?   D . n 
D 1 183 PHE 183 183 ?   ?   ?   D . n 
D 1 184 VAL 184 184 184 VAL VAL D . n 
D 1 185 ALA 185 185 185 ALA ALA D . n 
D 1 186 HIS 186 186 186 HIS HIS D . n 
D 1 187 ASP 187 187 187 ASP ASP D . n 
D 1 188 SER 188 188 188 SER SER D . n 
D 1 189 ILE 189 189 189 ILE ILE D . n 
D 1 190 HIS 190 190 190 HIS HIS D . n 
D 1 191 ASP 191 191 191 ASP ASP D . n 
D 1 192 CYS 192 192 192 CYS CYS D . n 
D 1 193 ALA 193 193 193 ALA ALA D . n 
D 1 194 LYS 194 194 194 LYS LYS D . n 
D 1 195 ASP 195 195 195 ASP ASP D . n 
D 1 196 ILE 196 196 196 ILE ILE D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 MET 198 198 198 MET MET D . n 
D 1 199 MET 199 199 199 MET MET D . n 
D 1 200 LYS 200 200 200 LYS LYS D . n 
D 1 201 TYR 201 201 201 TYR TYR D . n 
D 1 202 ALA 202 202 202 ALA ALA D . n 
D 1 203 LEU 203 203 203 LEU LEU D . n 
D 1 204 ARG 204 204 204 ARG ARG D . n 
D 1 205 TYR 205 205 205 TYR TYR D . n 
D 1 206 ALA 206 206 206 ALA ALA D . n 
D 1 207 MET 207 207 207 MET MET D . n 
D 1 208 GLY 208 208 208 GLY GLY D . n 
D 1 209 LEU 209 209 209 LEU LEU D . n 
D 1 210 GLU 210 210 210 GLU GLU D . n 
D 1 211 ASP 211 211 211 ASP ASP D . n 
D 1 212 ALA 212 212 212 ALA ALA D . n 
D 1 213 PRO 213 213 213 PRO PRO D . n 
D 1 214 SER 214 214 214 SER SER D . n 
D 1 215 GLU 215 215 215 GLU GLU D . n 
D 1 216 GLU 216 216 ?   ?   ?   D . n 
D 1 217 GLU 217 217 ?   ?   ?   D . n 
D 1 218 CYS 218 218 ?   ?   ?   D . n 
D 1 219 ASP 219 219 219 ASP ASP D . n 
D 1 220 PRO 220 220 220 PRO PRO D . n 
D 1 221 LEU 221 221 221 LEU LEU D . n 
D 1 222 SER 222 222 222 SER SER D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 PRO 224 224 224 PRO PRO D . n 
D 1 225 THR 225 225 ?   ?   ?   D . n 
D 1 226 LYS 226 226 ?   ?   ?   D . n 
D 1 227 ARG 227 227 ?   ?   ?   D . n 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ILE 20  ? CG1 ? A ILE 20  CG1 
2   1 Y 1 A ILE 20  ? CG2 ? A ILE 20  CG2 
3   1 Y 1 A ILE 20  ? CD1 ? A ILE 20  CD1 
4   1 Y 1 A LYS 46  ? CG  ? A LYS 46  CG  
5   1 Y 1 A LYS 46  ? CD  ? A LYS 46  CD  
6   1 Y 1 A LYS 46  ? CE  ? A LYS 46  CE  
7   1 Y 1 A LYS 46  ? NZ  ? A LYS 46  NZ  
8   1 Y 1 A LYS 48  ? CG  ? A LYS 48  CG  
9   1 Y 1 A LYS 48  ? CD  ? A LYS 48  CD  
10  1 Y 1 A LYS 48  ? CE  ? A LYS 48  CE  
11  1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
12  1 Y 1 A LYS 52  ? CG  ? A LYS 52  CG  
13  1 Y 1 A LYS 52  ? CD  ? A LYS 52  CD  
14  1 Y 1 A LYS 52  ? CE  ? A LYS 52  CE  
15  1 Y 1 A LYS 52  ? NZ  ? A LYS 52  NZ  
16  1 Y 1 A LYS 55  ? CG  ? A LYS 55  CG  
17  1 Y 1 A LYS 55  ? CD  ? A LYS 55  CD  
18  1 Y 1 A LYS 55  ? CE  ? A LYS 55  CE  
19  1 Y 1 A LYS 55  ? NZ  ? A LYS 55  NZ  
20  1 Y 1 A GLU 74  ? CG  ? A GLU 74  CG  
21  1 Y 1 A GLU 74  ? CD  ? A GLU 74  CD  
22  1 Y 1 A GLU 74  ? OE1 ? A GLU 74  OE1 
23  1 Y 1 A GLU 74  ? OE2 ? A GLU 74  OE2 
24  1 Y 1 A LYS 77  ? CG  ? A LYS 77  CG  
25  1 Y 1 A LYS 77  ? CD  ? A LYS 77  CD  
26  1 Y 1 A LYS 77  ? CE  ? A LYS 77  CE  
27  1 Y 1 A LYS 77  ? NZ  ? A LYS 77  NZ  
28  1 Y 1 A GLU 84  ? CG  ? A GLU 84  CG  
29  1 Y 1 A GLU 84  ? CD  ? A GLU 84  CD  
30  1 Y 1 A GLU 84  ? OE1 ? A GLU 84  OE1 
31  1 Y 1 A GLU 84  ? OE2 ? A GLU 84  OE2 
32  1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
33  1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
34  1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
35  1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
36  1 Y 1 A LYS 177 ? CG  ? A LYS 177 CG  
37  1 Y 1 A LYS 177 ? CD  ? A LYS 177 CD  
38  1 Y 1 A LYS 177 ? CE  ? A LYS 177 CE  
39  1 Y 1 A LYS 177 ? NZ  ? A LYS 177 NZ  
40  1 Y 1 A HIS 186 ? CG  ? A HIS 186 CG  
41  1 Y 1 A HIS 186 ? ND1 ? A HIS 186 ND1 
42  1 Y 1 A HIS 186 ? CD2 ? A HIS 186 CD2 
43  1 Y 1 A HIS 186 ? CE1 ? A HIS 186 CE1 
44  1 Y 1 A HIS 186 ? NE2 ? A HIS 186 NE2 
45  1 Y 1 A ASP 211 ? CG  ? A ASP 211 CG  
46  1 Y 1 A ASP 211 ? OD1 ? A ASP 211 OD1 
47  1 Y 1 A ASP 211 ? OD2 ? A ASP 211 OD2 
48  1 Y 1 A SER 214 ? OG  ? A SER 214 OG  
49  1 Y 1 A ASP 219 ? CG  ? A ASP 219 CG  
50  1 Y 1 A ASP 219 ? OD1 ? A ASP 219 OD1 
51  1 Y 1 A ASP 219 ? OD2 ? A ASP 219 OD2 
52  1 Y 1 A LEU 221 ? CG  ? A LEU 221 CG  
53  1 Y 1 A LEU 221 ? CD1 ? A LEU 221 CD1 
54  1 Y 1 A LEU 221 ? CD2 ? A LEU 221 CD2 
55  1 Y 1 B VAL 34  ? CG1 ? B VAL 34  CG1 
56  1 Y 1 B VAL 34  ? CG2 ? B VAL 34  CG2 
57  1 Y 1 B GLU 35  ? CG  ? B GLU 35  CG  
58  1 Y 1 B GLU 35  ? CD  ? B GLU 35  CD  
59  1 Y 1 B GLU 35  ? OE1 ? B GLU 35  OE1 
60  1 Y 1 B GLU 35  ? OE2 ? B GLU 35  OE2 
61  1 Y 1 B ASP 38  ? CG  ? B ASP 38  CG  
62  1 Y 1 B ASP 38  ? OD1 ? B ASP 38  OD1 
63  1 Y 1 B ASP 38  ? OD2 ? B ASP 38  OD2 
64  1 Y 1 B LYS 46  ? CG  ? B LYS 46  CG  
65  1 Y 1 B LYS 46  ? CD  ? B LYS 46  CD  
66  1 Y 1 B LYS 46  ? CE  ? B LYS 46  CE  
67  1 Y 1 B LYS 46  ? NZ  ? B LYS 46  NZ  
68  1 Y 1 B GLU 66  ? CG  ? B GLU 66  CG  
69  1 Y 1 B GLU 66  ? CD  ? B GLU 66  CD  
70  1 Y 1 B GLU 66  ? OE1 ? B GLU 66  OE1 
71  1 Y 1 B GLU 66  ? OE2 ? B GLU 66  OE2 
72  1 Y 1 B GLU 74  ? CG  ? B GLU 74  CG  
73  1 Y 1 B GLU 74  ? CD  ? B GLU 74  CD  
74  1 Y 1 B GLU 74  ? OE1 ? B GLU 74  OE1 
75  1 Y 1 B GLU 74  ? OE2 ? B GLU 74  OE2 
76  1 Y 1 B ARG 76  ? CG  ? B ARG 76  CG  
77  1 Y 1 B ARG 76  ? CD  ? B ARG 76  CD  
78  1 Y 1 B ARG 76  ? NE  ? B ARG 76  NE  
79  1 Y 1 B ARG 76  ? CZ  ? B ARG 76  CZ  
80  1 Y 1 B ARG 76  ? NH1 ? B ARG 76  NH1 
81  1 Y 1 B ARG 76  ? NH2 ? B ARG 76  NH2 
82  1 Y 1 B LYS 77  ? CG  ? B LYS 77  CG  
83  1 Y 1 B LYS 77  ? CD  ? B LYS 77  CD  
84  1 Y 1 B LYS 77  ? CE  ? B LYS 77  CE  
85  1 Y 1 B LYS 77  ? NZ  ? B LYS 77  NZ  
86  1 Y 1 B ASN 78  ? CG  ? B ASN 78  CG  
87  1 Y 1 B ASN 78  ? OD1 ? B ASN 78  OD1 
88  1 Y 1 B ASN 78  ? ND2 ? B ASN 78  ND2 
89  1 Y 1 B ILE 79  ? CG1 ? B ILE 79  CG1 
90  1 Y 1 B ILE 79  ? CG2 ? B ILE 79  CG2 
91  1 Y 1 B ILE 79  ? CD1 ? B ILE 79  CD1 
92  1 Y 1 B ASN 103 ? CG  ? B ASN 103 CG  
93  1 Y 1 B ASN 103 ? OD1 ? B ASN 103 OD1 
94  1 Y 1 B ASN 103 ? ND2 ? B ASN 103 ND2 
95  1 Y 1 B ASP 169 ? CG  ? B ASP 169 CG  
96  1 Y 1 B ASP 169 ? OD1 ? B ASP 169 OD1 
97  1 Y 1 B ASP 169 ? OD2 ? B ASP 169 OD2 
98  1 Y 1 B LYS 177 ? CG  ? B LYS 177 CG  
99  1 Y 1 B LYS 177 ? CD  ? B LYS 177 CD  
100 1 Y 1 B LYS 177 ? CE  ? B LYS 177 CE  
101 1 Y 1 B LYS 177 ? NZ  ? B LYS 177 NZ  
102 1 Y 1 B LEU 180 ? CG  ? B LEU 180 CG  
103 1 Y 1 B LEU 180 ? CD1 ? B LEU 180 CD1 
104 1 Y 1 B LEU 180 ? CD2 ? B LEU 180 CD2 
105 1 Y 1 B ASP 181 ? CG  ? B ASP 181 CG  
106 1 Y 1 B ASP 181 ? OD1 ? B ASP 181 OD1 
107 1 Y 1 B ASP 181 ? OD2 ? B ASP 181 OD2 
108 1 Y 1 B VAL 184 ? CG1 ? B VAL 184 CG1 
109 1 Y 1 B VAL 184 ? CG2 ? B VAL 184 CG2 
110 1 Y 1 B LYS 194 ? CG  ? B LYS 194 CG  
111 1 Y 1 B LYS 194 ? CD  ? B LYS 194 CD  
112 1 Y 1 B LYS 194 ? CE  ? B LYS 194 CE  
113 1 Y 1 B LYS 194 ? NZ  ? B LYS 194 NZ  
114 1 Y 1 B LYS 200 ? CG  ? B LYS 200 CG  
115 1 Y 1 B LYS 200 ? CD  ? B LYS 200 CD  
116 1 Y 1 B LYS 200 ? CE  ? B LYS 200 CE  
117 1 Y 1 B LYS 200 ? NZ  ? B LYS 200 NZ  
118 1 Y 1 B ARG 204 ? CG  ? B ARG 204 CG  
119 1 Y 1 B ARG 204 ? CD  ? B ARG 204 CD  
120 1 Y 1 B ARG 204 ? NE  ? B ARG 204 NE  
121 1 Y 1 B ARG 204 ? CZ  ? B ARG 204 CZ  
122 1 Y 1 B ARG 204 ? NH1 ? B ARG 204 NH1 
123 1 Y 1 B ARG 204 ? NH2 ? B ARG 204 NH2 
124 1 Y 1 B GLU 210 ? CG  ? B GLU 210 CG  
125 1 Y 1 B GLU 210 ? CD  ? B GLU 210 CD  
126 1 Y 1 B GLU 210 ? OE1 ? B GLU 210 OE1 
127 1 Y 1 B GLU 210 ? OE2 ? B GLU 210 OE2 
128 1 Y 1 B ASP 211 ? CG  ? B ASP 211 CG  
129 1 Y 1 B ASP 211 ? OD1 ? B ASP 211 OD1 
130 1 Y 1 B ASP 211 ? OD2 ? B ASP 211 OD2 
131 1 Y 1 B GLU 215 ? CG  ? B GLU 215 CG  
132 1 Y 1 B GLU 215 ? CD  ? B GLU 215 CD  
133 1 Y 1 B GLU 215 ? OE1 ? B GLU 215 OE1 
134 1 Y 1 B GLU 215 ? OE2 ? B GLU 215 OE2 
135 1 Y 1 B GLU 216 ? CG  ? B GLU 216 CG  
136 1 Y 1 B GLU 216 ? CD  ? B GLU 216 CD  
137 1 Y 1 B GLU 216 ? OE1 ? B GLU 216 OE1 
138 1 Y 1 B GLU 216 ? OE2 ? B GLU 216 OE2 
139 1 Y 1 B GLU 217 ? CG  ? B GLU 217 CG  
140 1 Y 1 B GLU 217 ? CD  ? B GLU 217 CD  
141 1 Y 1 B GLU 217 ? OE1 ? B GLU 217 OE1 
142 1 Y 1 B GLU 217 ? OE2 ? B GLU 217 OE2 
143 1 Y 1 B ASP 219 ? CG  ? B ASP 219 CG  
144 1 Y 1 B ASP 219 ? OD1 ? B ASP 219 OD1 
145 1 Y 1 B ASP 219 ? OD2 ? B ASP 219 OD2 
146 1 Y 1 B LEU 221 ? CG  ? B LEU 221 CG  
147 1 Y 1 B LEU 221 ? CD1 ? B LEU 221 CD1 
148 1 Y 1 B LEU 221 ? CD2 ? B LEU 221 CD2 
149 1 Y 1 B LEU 223 ? CG  ? B LEU 223 CG  
150 1 Y 1 B LEU 223 ? CD1 ? B LEU 223 CD1 
151 1 Y 1 B LEU 223 ? CD2 ? B LEU 223 CD2 
152 1 Y 1 B PRO 224 ? CG  ? B PRO 224 CG  
153 1 Y 1 B PRO 224 ? CD  ? B PRO 224 CD  
154 1 Y 1 C ILE 20  ? CG1 ? C ILE 20  CG1 
155 1 Y 1 C ILE 20  ? CG2 ? C ILE 20  CG2 
156 1 Y 1 C ILE 20  ? CD1 ? C ILE 20  CD1 
157 1 Y 1 C LYS 46  ? CG  ? C LYS 46  CG  
158 1 Y 1 C LYS 46  ? CD  ? C LYS 46  CD  
159 1 Y 1 C LYS 46  ? CE  ? C LYS 46  CE  
160 1 Y 1 C LYS 46  ? NZ  ? C LYS 46  NZ  
161 1 Y 1 C LYS 48  ? CG  ? C LYS 48  CG  
162 1 Y 1 C LYS 48  ? CD  ? C LYS 48  CD  
163 1 Y 1 C LYS 48  ? CE  ? C LYS 48  CE  
164 1 Y 1 C LYS 48  ? NZ  ? C LYS 48  NZ  
165 1 Y 1 C LYS 52  ? CG  ? C LYS 52  CG  
166 1 Y 1 C LYS 52  ? CD  ? C LYS 52  CD  
167 1 Y 1 C LYS 52  ? CE  ? C LYS 52  CE  
168 1 Y 1 C LYS 52  ? NZ  ? C LYS 52  NZ  
169 1 Y 1 C GLU 74  ? CG  ? C GLU 74  CG  
170 1 Y 1 C GLU 74  ? CD  ? C GLU 74  CD  
171 1 Y 1 C GLU 74  ? OE1 ? C GLU 74  OE1 
172 1 Y 1 C GLU 74  ? OE2 ? C GLU 74  OE2 
173 1 Y 1 C LYS 77  ? CG  ? C LYS 77  CG  
174 1 Y 1 C LYS 77  ? CD  ? C LYS 77  CD  
175 1 Y 1 C LYS 77  ? CE  ? C LYS 77  CE  
176 1 Y 1 C LYS 77  ? NZ  ? C LYS 77  NZ  
177 1 Y 1 C GLU 84  ? CG  ? C GLU 84  CG  
178 1 Y 1 C GLU 84  ? CD  ? C GLU 84  CD  
179 1 Y 1 C GLU 84  ? OE1 ? C GLU 84  OE1 
180 1 Y 1 C GLU 84  ? OE2 ? C GLU 84  OE2 
181 1 Y 1 C LYS 108 ? CG  ? C LYS 108 CG  
182 1 Y 1 C LYS 108 ? CD  ? C LYS 108 CD  
183 1 Y 1 C LYS 108 ? CE  ? C LYS 108 CE  
184 1 Y 1 C LYS 108 ? NZ  ? C LYS 108 NZ  
185 1 Y 1 C HIS 186 ? CG  ? C HIS 186 CG  
186 1 Y 1 C HIS 186 ? ND1 ? C HIS 186 ND1 
187 1 Y 1 C HIS 186 ? CD2 ? C HIS 186 CD2 
188 1 Y 1 C HIS 186 ? CE1 ? C HIS 186 CE1 
189 1 Y 1 C HIS 186 ? NE2 ? C HIS 186 NE2 
190 1 Y 1 C TYR 201 ? CG  ? C TYR 201 CG  
191 1 Y 1 C TYR 201 ? CD1 ? C TYR 201 CD1 
192 1 Y 1 C TYR 201 ? CD2 ? C TYR 201 CD2 
193 1 Y 1 C TYR 201 ? CE1 ? C TYR 201 CE1 
194 1 Y 1 C TYR 201 ? CE2 ? C TYR 201 CE2 
195 1 Y 1 C TYR 201 ? CZ  ? C TYR 201 CZ  
196 1 Y 1 C TYR 201 ? OH  ? C TYR 201 OH  
197 1 Y 1 C ARG 204 ? CG  ? C ARG 204 CG  
198 1 Y 1 C ARG 204 ? CD  ? C ARG 204 CD  
199 1 Y 1 C ARG 204 ? NE  ? C ARG 204 NE  
200 1 Y 1 C ARG 204 ? CZ  ? C ARG 204 CZ  
201 1 Y 1 C ARG 204 ? NH1 ? C ARG 204 NH1 
202 1 Y 1 C ARG 204 ? NH2 ? C ARG 204 NH2 
203 1 Y 1 C TYR 205 ? CG  ? C TYR 205 CG  
204 1 Y 1 C TYR 205 ? CD1 ? C TYR 205 CD1 
205 1 Y 1 C TYR 205 ? CD2 ? C TYR 205 CD2 
206 1 Y 1 C TYR 205 ? CE1 ? C TYR 205 CE1 
207 1 Y 1 C TYR 205 ? CE2 ? C TYR 205 CE2 
208 1 Y 1 C TYR 205 ? CZ  ? C TYR 205 CZ  
209 1 Y 1 C TYR 205 ? OH  ? C TYR 205 OH  
210 1 Y 1 D ASP 38  ? CG  ? D ASP 38  CG  
211 1 Y 1 D ASP 38  ? OD1 ? D ASP 38  OD1 
212 1 Y 1 D ASP 38  ? OD2 ? D ASP 38  OD2 
213 1 Y 1 D LYS 46  ? CG  ? D LYS 46  CG  
214 1 Y 1 D LYS 46  ? CD  ? D LYS 46  CD  
215 1 Y 1 D LYS 46  ? CE  ? D LYS 46  CE  
216 1 Y 1 D LYS 46  ? NZ  ? D LYS 46  NZ  
217 1 Y 1 D GLU 66  ? CG  ? D GLU 66  CG  
218 1 Y 1 D GLU 66  ? CD  ? D GLU 66  CD  
219 1 Y 1 D GLU 66  ? OE1 ? D GLU 66  OE1 
220 1 Y 1 D GLU 66  ? OE2 ? D GLU 66  OE2 
221 1 Y 1 D GLU 74  ? CG  ? D GLU 74  CG  
222 1 Y 1 D GLU 74  ? CD  ? D GLU 74  CD  
223 1 Y 1 D GLU 74  ? OE1 ? D GLU 74  OE1 
224 1 Y 1 D GLU 74  ? OE2 ? D GLU 74  OE2 
225 1 Y 1 D ARG 76  ? CG  ? D ARG 76  CG  
226 1 Y 1 D ARG 76  ? CD  ? D ARG 76  CD  
227 1 Y 1 D ARG 76  ? NE  ? D ARG 76  NE  
228 1 Y 1 D ARG 76  ? CZ  ? D ARG 76  CZ  
229 1 Y 1 D ARG 76  ? NH1 ? D ARG 76  NH1 
230 1 Y 1 D ARG 76  ? NH2 ? D ARG 76  NH2 
231 1 Y 1 D LYS 77  ? CG  ? D LYS 77  CG  
232 1 Y 1 D LYS 77  ? CD  ? D LYS 77  CD  
233 1 Y 1 D LYS 77  ? CE  ? D LYS 77  CE  
234 1 Y 1 D LYS 77  ? NZ  ? D LYS 77  NZ  
235 1 Y 1 D ASN 78  ? CG  ? D ASN 78  CG  
236 1 Y 1 D ASN 78  ? OD1 ? D ASN 78  OD1 
237 1 Y 1 D ASN 78  ? ND2 ? D ASN 78  ND2 
238 1 Y 1 D ILE 79  ? CG1 ? D ILE 79  CG1 
239 1 Y 1 D ILE 79  ? CG2 ? D ILE 79  CG2 
240 1 Y 1 D ILE 79  ? CD1 ? D ILE 79  CD1 
241 1 Y 1 D ASN 103 ? CG  ? D ASN 103 CG  
242 1 Y 1 D ASN 103 ? OD1 ? D ASN 103 OD1 
243 1 Y 1 D ASN 103 ? ND2 ? D ASN 103 ND2 
244 1 Y 1 D LEU 164 ? CG  ? D LEU 164 CG  
245 1 Y 1 D LEU 164 ? CD1 ? D LEU 164 CD1 
246 1 Y 1 D LEU 164 ? CD2 ? D LEU 164 CD2 
247 1 Y 1 D ASP 169 ? CG  ? D ASP 169 CG  
248 1 Y 1 D ASP 169 ? OD1 ? D ASP 169 OD1 
249 1 Y 1 D ASP 169 ? OD2 ? D ASP 169 OD2 
250 1 Y 1 D LEU 175 ? CG  ? D LEU 175 CG  
251 1 Y 1 D LEU 175 ? CD1 ? D LEU 175 CD1 
252 1 Y 1 D LEU 175 ? CD2 ? D LEU 175 CD2 
253 1 Y 1 D VAL 184 ? CG1 ? D VAL 184 CG1 
254 1 Y 1 D VAL 184 ? CG2 ? D VAL 184 CG2 
255 1 Y 1 D LYS 194 ? CG  ? D LYS 194 CG  
256 1 Y 1 D LYS 194 ? CD  ? D LYS 194 CD  
257 1 Y 1 D LYS 194 ? CE  ? D LYS 194 CE  
258 1 Y 1 D LYS 194 ? NZ  ? D LYS 194 NZ  
259 1 Y 1 D MET 199 ? CG  ? D MET 199 CG  
260 1 Y 1 D MET 199 ? SD  ? D MET 199 SD  
261 1 Y 1 D MET 199 ? CE  ? D MET 199 CE  
262 1 Y 1 D LYS 200 ? CG  ? D LYS 200 CG  
263 1 Y 1 D LYS 200 ? CD  ? D LYS 200 CD  
264 1 Y 1 D LYS 200 ? CE  ? D LYS 200 CE  
265 1 Y 1 D LYS 200 ? NZ  ? D LYS 200 NZ  
266 1 Y 1 D TYR 201 ? CG  ? D TYR 201 CG  
267 1 Y 1 D TYR 201 ? CD1 ? D TYR 201 CD1 
268 1 Y 1 D TYR 201 ? CD2 ? D TYR 201 CD2 
269 1 Y 1 D TYR 201 ? CE1 ? D TYR 201 CE1 
270 1 Y 1 D TYR 201 ? CE2 ? D TYR 201 CE2 
271 1 Y 1 D TYR 201 ? CZ  ? D TYR 201 CZ  
272 1 Y 1 D TYR 201 ? OH  ? D TYR 201 OH  
273 1 Y 1 D LEU 203 ? CG  ? D LEU 203 CG  
274 1 Y 1 D LEU 203 ? CD1 ? D LEU 203 CD1 
275 1 Y 1 D LEU 203 ? CD2 ? D LEU 203 CD2 
276 1 Y 1 D ARG 204 ? CG  ? D ARG 204 CG  
277 1 Y 1 D ARG 204 ? CD  ? D ARG 204 CD  
278 1 Y 1 D ARG 204 ? NE  ? D ARG 204 NE  
279 1 Y 1 D ARG 204 ? CZ  ? D ARG 204 CZ  
280 1 Y 1 D ARG 204 ? NH1 ? D ARG 204 NH1 
281 1 Y 1 D ARG 204 ? NH2 ? D ARG 204 NH2 
282 1 Y 1 D TYR 205 ? CG  ? D TYR 205 CG  
283 1 Y 1 D TYR 205 ? CD1 ? D TYR 205 CD1 
284 1 Y 1 D TYR 205 ? CD2 ? D TYR 205 CD2 
285 1 Y 1 D TYR 205 ? CE1 ? D TYR 205 CE1 
286 1 Y 1 D TYR 205 ? CE2 ? D TYR 205 CE2 
287 1 Y 1 D TYR 205 ? CZ  ? D TYR 205 CZ  
288 1 Y 1 D TYR 205 ? OH  ? D TYR 205 OH  
289 1 Y 1 D MET 207 ? CG  ? D MET 207 CG  
290 1 Y 1 D MET 207 ? SD  ? D MET 207 SD  
291 1 Y 1 D MET 207 ? CE  ? D MET 207 CE  
292 1 Y 1 D LEU 209 ? CG  ? D LEU 209 CG  
293 1 Y 1 D LEU 209 ? CD1 ? D LEU 209 CD1 
294 1 Y 1 D LEU 209 ? CD2 ? D LEU 209 CD2 
295 1 Y 1 D GLU 210 ? CG  ? D GLU 210 CG  
296 1 Y 1 D GLU 210 ? CD  ? D GLU 210 CD  
297 1 Y 1 D GLU 210 ? OE1 ? D GLU 210 OE1 
298 1 Y 1 D GLU 210 ? OE2 ? D GLU 210 OE2 
299 1 Y 1 D ASP 211 ? CG  ? D ASP 211 CG  
300 1 Y 1 D ASP 211 ? OD1 ? D ASP 211 OD1 
301 1 Y 1 D ASP 211 ? OD2 ? D ASP 211 OD2 
302 1 Y 1 D GLU 215 ? CG  ? D GLU 215 CG  
303 1 Y 1 D GLU 215 ? CD  ? D GLU 215 CD  
304 1 Y 1 D GLU 215 ? OE1 ? D GLU 215 OE1 
305 1 Y 1 D GLU 215 ? OE2 ? D GLU 215 OE2 
306 1 Y 1 D ASP 219 ? CG  ? D ASP 219 CG  
307 1 Y 1 D ASP 219 ? OD1 ? D ASP 219 OD1 
308 1 Y 1 D ASP 219 ? OD2 ? D ASP 219 OD2 
309 1 Y 1 D LEU 221 ? CG  ? D LEU 221 CG  
310 1 Y 1 D LEU 221 ? CD1 ? D LEU 221 CD1 
311 1 Y 1 D LEU 221 ? CD2 ? D LEU 221 CD2 
312 1 Y 1 D LEU 223 ? CG  ? D LEU 223 CG  
313 1 Y 1 D LEU 223 ? CD1 ? D LEU 223 CD1 
314 1 Y 1 D LEU 223 ? CD2 ? D LEU 223 CD2 
315 1 Y 1 D PRO 224 ? CG  ? D PRO 224 CG  
316 1 Y 1 D PRO 224 ? CD  ? D PRO 224 CD  
# 
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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.360 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8KEL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.548 
_cell.length_a_esd                 ? 
_cell.length_b                     76.285 
_cell.length_b_esd                 ? 
_cell.length_c                     108.009 
_cell.length_c_esd                 ? 
_cell.volume                       695432.903 
_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                         8KEL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8KEL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.22 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.02M Calcium chloride dihydrate, 0.1M Sodium acetate trihydrate pH 4.6, 30% v/v (+/-)-2-Methyl-2,4-pentanediol' 
_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         2022-07-30 
_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   0.9791 
_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        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          70.54 
_reflns.entry_id                                       8KEL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.88 
_reflns.d_resolution_low                               35.94 
_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                                     30240 
_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                           95.96 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.25 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.88 
_reflns_shell.d_res_low                                     2.98 
_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                             3066 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.704 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               83.85 
_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                                 8KEL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.88 
_refine.ls_d_res_low                             35.94 
_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                     30056 
_refine.ls_number_reflns_R_free                  1434 
_refine.ls_number_reflns_R_work                  28622 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.03 
_refine.ls_percent_reflns_R_free                 4.77 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2250 
_refine.ls_R_factor_R_free                       0.2762 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2225 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.2548 
_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                            0.4335 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.88 
_refine_hist.d_res_low                        35.94 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6550 
_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        6550 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0089 ? 6694 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0820 ? 9089 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0584 ? 1017 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0098 ? 1186 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.2162 ? 891  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.88 2.98  . . 153 2913 99.16 . . . . 0.2936 . . . . . . . . . . . 0.3737 
'X-RAY DIFFRACTION' 2.98 3.10  . . 155 2942 99.65 . . . . 0.2660 . . . . . . . . . . . 0.3533 
'X-RAY DIFFRACTION' 3.10 3.24  . . 175 2929 99.65 . . . . 0.2510 . . . . . . . . . . . 0.3832 
'X-RAY DIFFRACTION' 3.24 3.42  . . 140 2959 99.61 . . . . 0.2346 . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 3.42 3.63  . . 115 2929 97.72 . . . . 0.2287 . . . . . . . . . . . 0.2675 
'X-RAY DIFFRACTION' 3.63 3.91  . . 99  2166 72.55 . . . . 0.2327 . . . . . . . . . . . 0.2888 
'X-RAY DIFFRACTION' 3.91 4.30  . . 155 2921 98.84 . . . . 0.2093 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 4.30 4.92  . . 136 2931 97.43 . . . . 0.1967 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 4.92 6.20  . . 142 2956 98.73 . . . . 0.2498 . . . . . . . . . . . 0.2951 
'X-RAY DIFFRACTION' 6.20 35.94 . . 164 2976 97.00 . . . . 0.1964 . . . . . . . . . . . 0.2240 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
_struct_ncs_oper.details 
1 given 0.951793382292 -0.278576918468 -0.128391035209  -0.278492320202 -0.960250938354 0.0189779603472  -0.128574433748 
0.0176928202207 -0.991542020844 9.74156165566 19.3261864035 106.647569463 ? 
2 given 0.981567799158 -0.176777388239 -0.0726251379569 0.173818952974  0.983736805375  -0.0452644378976 0.0794457503153 
0.031806489248  0.996331631536  44.6700384362 19.9665920243 54.1579481284 ? 
# 
_struct.entry_id                     8KEL 
_struct.title                        'Structure of DexA reveal the novel Mechanism of DNA catalysis' 
_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        8KEL 
_struct_keywords.text            'chlorinase, SAM, ClDA, FDA, ANTIBIOTIC, OXIDOREDUCTASE, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EXOD_BPT4 
_struct_ref.pdbx_db_accession          P04536 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFDFIIDFETMGSGEKAAVIDLAVIAFDPNPEVVETFDELVSRGIKIKFDLKSQKGHRLFTKSTIEWWKNQSPEARKNIA
PSDEDVSTIDGIAKFNDYINAHNIDPWKSQGWCRGMSFDFPILVDLIRDIQRLNGVSENELDTFKLEPCKFWNQRDIRTR
IEALLLVRDMTTCPLPKGTLDGFVAHDSIHDCAKDILMMKYALRYAMGLEDAPSEEECDPLSLPTKR
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8KEL A 1 ? 227 ? P04536 1 ? 227 ? 1 227 
2 1 8KEL B 1 ? 227 ? P04536 1 ? 227 ? 1 227 
3 1 8KEL C 1 ? 227 ? P04536 1 ? 227 ? 1 227 
4 1 8KEL D 1 ? 227 ? P04536 1 ? 227 ? 1 227 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B 
2 1 C,D 
# 
_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 THR A 36  ? GLY A 44  ? THR A 36  GLY A 44  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 50  ? LYS A 55  ? ASP A 50  LYS A 55  1 ? 6  
HELX_P HELX_P3  AA3 THR A 61  ? ASN A 70  ? THR A 61  ASN A 70  1 ? 10 
HELX_P HELX_P4  AA4 GLU A 74  ? ALA A 80  ? GLU A 74  ALA A 80  5 ? 7  
HELX_P HELX_P5  AA5 SER A 87  ? ALA A 101 ? SER A 87  ALA A 101 1 ? 15 
HELX_P HELX_P6  AA6 GLY A 115 ? ASN A 134 ? GLY A 115 ASN A 134 1 ? 20 
HELX_P HELX_P7  AA7 SER A 137 ? LEU A 141 ? SER A 137 LEU A 141 5 ? 5  
HELX_P HELX_P8  AA8 LYS A 150 ? TRP A 152 ? LYS A 150 TRP A 152 5 ? 3  
HELX_P HELX_P9  AA9 ILE A 157 ? LEU A 166 ? ILE A 157 LEU A 166 1 ? 10 
HELX_P HELX_P10 AB1 ASP A 187 ? GLY A 208 ? ASP A 187 GLY A 208 1 ? 22 
HELX_P HELX_P11 AB2 THR B 36  ? GLY B 44  ? THR B 36  GLY B 44  1 ? 9  
HELX_P HELX_P12 AB3 LEU B 51  ? LYS B 55  ? LEU B 51  LYS B 55  5 ? 5  
HELX_P HELX_P13 AB4 THR B 61  ? ASN B 70  ? THR B 61  ASN B 70  1 ? 10 
HELX_P HELX_P14 AB5 GLU B 74  ? ASN B 78  ? GLU B 74  ASN B 78  5 ? 5  
HELX_P HELX_P15 AB6 SER B 87  ? HIS B 102 ? SER B 87  HIS B 102 1 ? 16 
HELX_P HELX_P16 AB7 PHE B 118 ? ASN B 134 ? PHE B 118 ASN B 134 1 ? 17 
HELX_P HELX_P17 AB8 THR B 143 ? GLU B 147 ? THR B 143 GLU B 147 5 ? 5  
HELX_P HELX_P18 AB9 LYS B 150 ? GLN B 154 ? LYS B 150 GLN B 154 5 ? 5  
HELX_P HELX_P19 AC1 ASP B 156 ? LEU B 166 ? ASP B 156 LEU B 166 1 ? 11 
HELX_P HELX_P20 AC2 ASP B 187 ? GLY B 208 ? ASP B 187 GLY B 208 1 ? 22 
HELX_P HELX_P21 AC3 PHE C 37  ? SER C 42  ? PHE C 37  SER C 42  1 ? 6  
HELX_P HELX_P22 AC4 LEU C 51  ? LYS C 55  ? LEU C 51  LYS C 55  5 ? 5  
HELX_P HELX_P23 AC5 THR C 61  ? LYS C 69  ? THR C 61  LYS C 69  1 ? 9  
HELX_P HELX_P24 AC6 SER C 72  ? ALA C 80  ? SER C 72  ALA C 80  1 ? 9  
HELX_P HELX_P25 AC7 SER C 87  ? ALA C 101 ? SER C 87  ALA C 101 1 ? 15 
HELX_P HELX_P26 AC8 PHE C 118 ? ASN C 134 ? PHE C 118 ASN C 134 1 ? 17 
HELX_P HELX_P27 AC9 SER C 137 ? LEU C 141 ? SER C 137 LEU C 141 5 ? 5  
HELX_P HELX_P28 AD1 ILE C 157 ? LEU C 165 ? ILE C 157 LEU C 165 1 ? 9  
HELX_P HELX_P29 AD2 ASP C 187 ? ALA C 206 ? ASP C 187 ALA C 206 1 ? 20 
HELX_P HELX_P30 AD3 PHE D 37  ? GLY D 44  ? PHE D 37  GLY D 44  1 ? 8  
HELX_P HELX_P31 AD4 THR D 61  ? ASN D 70  ? THR D 61  ASN D 70  1 ? 10 
HELX_P HELX_P32 AD5 SER D 72  ? ASN D 78  ? SER D 72  ASN D 78  1 ? 7  
HELX_P HELX_P33 AD6 SER D 87  ? ALA D 101 ? SER D 87  ALA D 101 1 ? 15 
HELX_P HELX_P34 AD7 PHE D 118 ? LEU D 133 ? PHE D 118 LEU D 133 1 ? 16 
HELX_P HELX_P35 AD8 THR D 143 ? GLU D 147 ? THR D 143 GLU D 147 5 ? 5  
HELX_P HELX_P36 AD9 ASP D 156 ? LEU D 165 ? ASP D 156 LEU D 165 1 ? 10 
HELX_P HELX_P37 AE1 ASP D 187 ? GLY D 208 ? ASP D 187 GLY D 208 1 ? 22 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 85  ? VAL A 86  ? ASP A 85  VAL A 86  
AA1 2 ILE A 45  ? PHE A 49  ? ILE A 45  PHE A 49  
AA1 3 VAL A 19  ? PHE A 27  ? VAL A 19  PHE A 27  
AA1 4 ASP A 3   ? THR A 10  ? ASP A 3   THR A 10  
AA1 5 GLY A 111 ? CYS A 113 ? GLY A 111 CYS A 113 
AA1 6 GLN A 154 ? ASP A 156 ? GLN A 154 ASP A 156 
AA2 1 ILE B 45  ? LYS B 48  ? ILE B 45  LYS B 48  
AA2 2 VAL B 19  ? PHE B 27  ? VAL B 19  PHE B 27  
AA2 3 ASP B 3   ? THR B 10  ? ASP B 3   THR B 10  
AA2 4 GLY B 111 ? TRP B 112 ? GLY B 111 TRP B 112 
AA3 1 ILE C 45  ? LYS C 48  ? ILE C 45  LYS C 48  
AA3 2 VAL C 19  ? PHE C 27  ? VAL C 19  PHE C 27  
AA3 3 ASP C 3   ? THR C 10  ? ASP C 3   THR C 10  
AA3 4 GLY C 111 ? CYS C 113 ? GLY C 111 CYS C 113 
AA3 5 ARG C 155 ? ASP C 156 ? ARG C 155 ASP C 156 
AA4 1 PHE D 8   ? THR D 10  ? PHE D 8   THR D 10  
AA4 2 VAL D 19  ? PHE D 27  ? VAL D 19  PHE D 27  
AA4 3 ILE D 45  ? LYS D 48  ? ILE D 45  LYS D 48  
AA5 1 PHE D 8   ? THR D 10  ? PHE D 8   THR D 10  
AA5 2 VAL D 19  ? PHE D 27  ? VAL D 19  PHE D 27  
AA5 3 ASP D 3   ? ILE D 5   ? ASP D 3   ILE D 5   
AA5 4 GLY D 111 ? TRP D 112 ? GLY D 111 TRP D 112 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 86  ? O VAL A 86  N LYS A 48  ? N LYS A 48  
AA1 2 3 O ILE A 47  ? O ILE A 47  N LEU A 22  ? N LEU A 22  
AA1 3 4 O ILE A 20  ? O ILE A 20  N GLU A 9   ? N GLU A 9   
AA1 4 5 N ILE A 6   ? N ILE A 6   O TRP A 112 ? O TRP A 112 
AA1 5 6 N GLY A 111 ? N GLY A 111 O ARG A 155 ? O ARG A 155 
AA2 1 2 O ILE B 47  ? O ILE B 47  N LEU B 22  ? N LEU B 22  
AA2 2 3 O ILE B 20  ? O ILE B 20  N GLU B 9   ? N GLU B 9   
AA2 3 4 N PHE B 4   ? N PHE B 4   O TRP B 112 ? O TRP B 112 
AA3 1 2 O ILE C 47  ? O ILE C 47  N LEU C 22  ? N LEU C 22  
AA3 2 3 O ILE C 20  ? O ILE C 20  N GLU C 9   ? N GLU C 9   
AA3 3 4 N ILE C 6   ? N ILE C 6   O TRP C 112 ? O TRP C 112 
AA3 4 5 N GLY C 111 ? N GLY C 111 O ARG C 155 ? O ARG C 155 
AA4 1 2 N GLU D 9   ? N GLU D 9   O ILE D 20  ? O ILE D 20  
AA4 2 3 N LEU D 22  ? N LEU D 22  O ILE D 47  ? O ILE D 47  
AA5 1 2 N GLU D 9   ? N GLU D 9   O ILE D 20  ? O ILE D 20  
AA5 2 3 O PHE D 27  ? O PHE D 27  N ASP D 3   ? N ASP D 3   
AA5 3 4 N PHE D 4   ? N PHE D 4   O TRP D 112 ? O TRP D 112 
# 
_pdbx_entry_details.entry_id                   8KEL 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 C GLN 154 ? ? OG  D SER 117 ? ? 2.08 
2 1 NE2 A GLN 131 ? ? O   A ASP 142 ? ? 2.15 
3 1 O   A GLN 71  ? ? NH2 A ARG 76  ? ? 2.16 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A PHE 27  ? ? CG A PHE 27  ? ? CD2 A PHE 27  ? ? 115.81 120.80 -4.99 0.70 N 
2 1 CB A PHE 27  ? ? CG A PHE 27  ? ? CD1 A PHE 27  ? ? 125.89 120.80 5.09  0.70 N 
3 1 C  D LEU 223 ? ? N  D PRO 224 ? ? CA  D PRO 224 ? ? 128.64 119.30 9.34  1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 186 ? ? -90.32  46.01  
2  1 ASN B 70  ? ? -93.06  30.08  
3  1 CYS B 113 ? ? -179.01 142.15 
4  1 HIS B 186 ? ? -101.47 40.02  
5  1 HIS C 57  ? ? -130.06 -36.24 
6  1 PHE C 118 ? ? -100.71 -62.55 
7  1 ASP C 169 ? ? 35.57   40.96  
8  1 HIS C 186 ? ? -105.00 40.36  
9  1 ASN D 70  ? ? -99.74  36.37  
10 1 TRP D 107 ? ? -93.38  -62.48 
11 1 CYS D 113 ? ? -175.89 141.29 
12 1 ASP D 169 ? ? 70.85   -6.13  
13 1 PRO D 220 ? ? -57.40  17.16  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         20.1862326079 
_pdbx_refine_tls.origin_y         -1.2054905967 
_pdbx_refine_tls.origin_z         27.4364867559 
_pdbx_refine_tls.T[1][1]          0.436484056932 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00673395690591 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0334192892096 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.424626455137 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0812569866822 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.583848421435 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.0399000338 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.407801180355 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -1.42475055925 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.73111742144 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.804994313991 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.73027672255 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0143200064421 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1441208628 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.142534477372 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.149855031297 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0390703105085 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0765506234968 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.00960094792165 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.132486436774 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0497581455539 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    211 
_pdbx_refine_tls_group.end_auth_asym_id    D 
_pdbx_refine_tls_group.end_auth_seq_id     224 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 222 ? A SER 222 
2  1 Y 1 A LEU 223 ? A LEU 223 
3  1 Y 1 A PRO 224 ? A PRO 224 
4  1 Y 1 A THR 225 ? A THR 225 
5  1 Y 1 A LYS 226 ? A LYS 226 
6  1 Y 1 A ARG 227 ? A ARG 227 
7  1 Y 1 B THR 225 ? B THR 225 
8  1 Y 1 B LYS 226 ? B LYS 226 
9  1 Y 1 B ARG 227 ? B ARG 227 
10 1 Y 1 C GLU 32  ? C GLU 32  
11 1 Y 1 C VAL 33  ? C VAL 33  
12 1 Y 1 C VAL 34  ? C VAL 34  
13 1 Y 1 C GLU 35  ? C GLU 35  
14 1 Y 1 C PRO 174 ? C PRO 174 
15 1 Y 1 C LEU 175 ? C LEU 175 
16 1 Y 1 C PRO 176 ? C PRO 176 
17 1 Y 1 C LYS 177 ? C LYS 177 
18 1 Y 1 C GLY 178 ? C GLY 178 
19 1 Y 1 C MET 207 ? C MET 207 
20 1 Y 1 C GLY 208 ? C GLY 208 
21 1 Y 1 C LEU 209 ? C LEU 209 
22 1 Y 1 C GLU 210 ? C GLU 210 
23 1 Y 1 C ASP 211 ? C ASP 211 
24 1 Y 1 C ALA 212 ? C ALA 212 
25 1 Y 1 C PRO 213 ? C PRO 213 
26 1 Y 1 C SER 214 ? C SER 214 
27 1 Y 1 C GLU 215 ? C GLU 215 
28 1 Y 1 C GLU 216 ? C GLU 216 
29 1 Y 1 C GLU 217 ? C GLU 217 
30 1 Y 1 C CYS 218 ? C CYS 218 
31 1 Y 1 C ASP 219 ? C ASP 219 
32 1 Y 1 C PRO 220 ? C PRO 220 
33 1 Y 1 C LEU 221 ? C LEU 221 
34 1 Y 1 C SER 222 ? C SER 222 
35 1 Y 1 C LEU 223 ? C LEU 223 
36 1 Y 1 C PRO 224 ? C PRO 224 
37 1 Y 1 C THR 225 ? C THR 225 
38 1 Y 1 C LYS 226 ? C LYS 226 
39 1 Y 1 C ARG 227 ? C ARG 227 
40 1 Y 1 D VAL 33  ? D VAL 33  
41 1 Y 1 D VAL 34  ? D VAL 34  
42 1 Y 1 D GLU 35  ? D GLU 35  
43 1 Y 1 D LYS 177 ? D LYS 177 
44 1 Y 1 D GLY 178 ? D GLY 178 
45 1 Y 1 D THR 179 ? D THR 179 
46 1 Y 1 D LEU 180 ? D LEU 180 
47 1 Y 1 D ASP 181 ? D ASP 181 
48 1 Y 1 D GLY 182 ? D GLY 182 
49 1 Y 1 D PHE 183 ? D PHE 183 
50 1 Y 1 D GLU 216 ? D GLU 216 
51 1 Y 1 D GLU 217 ? D GLU 217 
52 1 Y 1 D CYS 218 ? D CYS 218 
53 1 Y 1 D THR 225 ? D THR 225 
54 1 Y 1 D LYS 226 ? D LYS 226 
55 1 Y 1 D ARG 227 ? D ARG 227 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82172299 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             other 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   AF-A0A2M9X318-F1-model-v4 
_pdbx_initial_refinement_model.details          'We used the structure that predicted by AlphaFold as the searching model' 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8KEL 
_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]   0.011828 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000694 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013109 
_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]   0.009274 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . MET A 1 1   ? 22.18546  -15.93883 51.91144  1.000 66.45004  ? 1   MET A N   1 
ATOM 2    C CA  . MET A 1 1   ? 21.46344  -14.85325 52.59905  1.000 74.81114  ? 1   MET A CA  1 
ATOM 3    C C   . MET A 1 1   ? 21.56001  -13.50490 51.86974  1.000 68.73460  ? 1   MET A C   1 
ATOM 4    O O   . MET A 1 1   ? 22.58082  -12.83154 51.93269  1.000 68.50170  ? 1   MET A O   1 
ATOM 5    C CB  . MET A 1 1   ? 21.97883  -14.71075 54.03377  1.000 71.16134  ? 1   MET A CB  1 
ATOM 6    C CG  . MET A 1 1   ? 21.28369  -13.64615 54.88165  1.000 69.76690  ? 1   MET A CG  1 
ATOM 7    S SD  . MET A 1 1   ? 22.07003  -11.99462 54.96965  1.000 86.86672  ? 1   MET A SD  1 
ATOM 8    C CE  . MET A 1 1   ? 20.98929  -11.16109 56.08298  1.000 65.04057  ? 1   MET A CE  1 
ATOM 9    N N   . PHE A 1 2   ? 20.47459  -13.10074 51.21999  1.000 65.90270  ? 2   PHE A N   1 
ATOM 10   C CA  . PHE A 1 2   ? 20.50412  -12.03380 50.22717  1.000 67.39989  ? 2   PHE A CA  1 
ATOM 11   C C   . PHE A 1 2   ? 20.03403  -10.68387 50.76892  1.000 65.67290  ? 2   PHE A C   1 
ATOM 12   O O   . PHE A 1 2   ? 19.44723  -10.57911 51.84697  1.000 66.19984  ? 2   PHE A O   1 
ATOM 13   C CB  . PHE A 1 2   ? 19.63316  -12.38830 49.01565  1.000 68.49980  ? 2   PHE A CB  1 
ATOM 14   C CG  . PHE A 1 2   ? 20.26830  -13.33786 48.06123  1.000 71.53731  ? 2   PHE A CG  1 
ATOM 15   C CD1 . PHE A 1 2   ? 21.51067  -13.88332 48.32239  1.000 74.02036  ? 2   PHE A CD1 1 
ATOM 16   C CD2 . PHE A 1 2   ? 19.67883  -13.58171 46.83163  1.000 71.50974  ? 2   PHE A CD2 1 
ATOM 17   C CE1 . PHE A 1 2   ? 22.11781  -14.73434 47.40782  1.000 75.30425  ? 2   PHE A CE1 1 
ATOM 18   C CE2 . PHE A 1 2   ? 20.28427  -14.41664 45.90289  1.000 72.98546  ? 2   PHE A CE2 1 
ATOM 19   C CZ  . PHE A 1 2   ? 21.50455  -14.99521 46.19573  1.000 75.86325  ? 2   PHE A CZ  1 
ATOM 20   N N   . ASP A 1 3   ? 20.28231  -9.63683  49.96935  1.000 59.13878  ? 3   ASP A N   1 
ATOM 21   C CA  . ASP A 1 3   ? 19.58789  -8.36367  50.08653  1.000 55.10260  ? 3   ASP A CA  1 
ATOM 22   C C   . ASP A 1 3   ? 18.59328  -8.26874  48.95418  1.000 55.05947  ? 3   ASP A C   1 
ATOM 23   O O   . ASP A 1 3   ? 18.48522  -9.18470  48.13801  1.000 58.59828  ? 3   ASP A O   1 
ATOM 24   C CB  . ASP A 1 3   ? 20.54073  -7.17470  50.05471  1.000 56.03108  ? 3   ASP A CB  1 
ATOM 25   C CG  . ASP A 1 3   ? 21.37246  -7.05510  51.31739  1.000 62.74997  ? 3   ASP A CG  1 
ATOM 26   O OD1 . ASP A 1 3   ? 20.99960  -7.65787  52.36198  1.000 61.58060  ? 3   ASP A OD1 1 
ATOM 27   O OD2 . ASP A 1 3   ? 22.37462  -6.30079  51.28469  1.000 64.22900  ? 3   ASP A OD2 1 
ATOM 28   N N   . PHE A 1 4   ? 17.86581  -7.15432  48.89704  1.000 51.30249  ? 4   PHE A N   1 
ATOM 29   C CA  . PHE A 1 4   ? 16.96889  -6.93247  47.77007  1.000 51.11135  ? 4   PHE A CA  1 
ATOM 30   C C   . PHE A 1 4   ? 16.91566  -5.45039  47.42017  1.000 47.54870  ? 4   PHE A C   1 
ATOM 31   O O   . PHE A 1 4   ? 17.43000  -4.59881  48.13662  1.000 46.91033  ? 4   PHE A O   1 
ATOM 32   C CB  . PHE A 1 4   ? 15.56876  -7.47654  48.04694  1.000 49.59015  ? 4   PHE A CB  1 
ATOM 33   C CG  . PHE A 1 4   ? 14.83629  -6.73447  49.11367  1.000 52.49546  ? 4   PHE A CG  1 
ATOM 34   C CD1 . PHE A 1 4   ? 14.96605  -7.10558  50.44639  1.000 55.28866  ? 4   PHE A CD1 1 
ATOM 35   C CD2 . PHE A 1 4   ? 14.01638  -5.66728  48.79046  1.000 48.71330  ? 4   PHE A CD2 1 
ATOM 36   C CE1 . PHE A 1 4   ? 14.30330  -6.42782  51.42942  1.000 48.96646  ? 4   PHE A CE1 1 
ATOM 37   C CE2 . PHE A 1 4   ? 13.34977  -4.99592  49.74658  1.000 48.79555  ? 4   PHE A CE2 1 
ATOM 38   C CZ  . PHE A 1 4   ? 13.49339  -5.37923  51.08307  1.000 54.63121  ? 4   PHE A CZ  1 
ATOM 39   N N   . ILE A 1 5   ? 16.30646  -5.17070  46.27208  1.000 46.96857  ? 5   ILE A N   1 
ATOM 40   C CA  . ILE A 1 5   ? 16.14105  -3.83436  45.72832  1.000 46.08535  ? 5   ILE A CA  1 
ATOM 41   C C   . ILE A 1 5   ? 14.72143  -3.73471  45.17723  1.000 49.05507  ? 5   ILE A C   1 
ATOM 42   O O   . ILE A 1 5   ? 14.12995  -4.73096  44.75967  1.000 46.24084  ? 5   ILE A O   1 
ATOM 43   C CB  . ILE A 1 5   ? 17.18835  -3.52841  44.63474  1.000 49.02634  ? 5   ILE A CB  1 
ATOM 44   C CG1 . ILE A 1 5   ? 17.10993  -2.06932  44.19891  1.000 49.12822  ? 5   ILE A CG1 1 
ATOM 45   C CG2 . ILE A 1 5   ? 16.95282  -4.39919  43.42759  1.000 48.14880  ? 5   ILE A CG2 1 
ATOM 46   C CD1 . ILE A 1 5   ? 18.28852  -1.63810  43.42728  1.000 52.03491  ? 5   ILE A CD1 1 
ATOM 47   N N   . ILE A 1 6   ? 14.15540  -2.52370  45.20874  1.000 53.27245  ? 6   ILE A N   1 
ATOM 48   C CA  . ILE A 1 6   ? 12.78404  -2.27658  44.77515  1.000 49.33601  ? 6   ILE A CA  1 
ATOM 49   C C   . ILE A 1 6   ? 12.76664  -0.99537  43.95117  1.000 45.17001  ? 6   ILE A C   1 
ATOM 50   O O   . ILE A 1 6   ? 13.62916  -0.12783  44.10129  1.000 43.80622  ? 6   ILE A O   1 
ATOM 51   C CB  . ILE A 1 6   ? 11.77523  -2.18112  45.96207  1.000 44.20844  ? 6   ILE A CB  1 
ATOM 52   C CG1 . ILE A 1 6   ? 12.12464  -1.01427  46.87550  1.000 47.82269  ? 6   ILE A CG1 1 
ATOM 53   C CG2 . ILE A 1 6   ? 11.77428  -3.44069  46.77218  1.000 42.48399  ? 6   ILE A CG2 1 
ATOM 54   C CD1 . ILE A 1 6   ? 11.01724  -0.62616  47.79839  1.000 49.53691  ? 6   ILE A CD1 1 
ATOM 55   N N   . ASP A 1 7   ? 11.76958  -0.89048  43.07261  1.000 47.67023  ? 7   ASP A N   1 
ATOM 56   C CA  . ASP A 1 7   ? 11.57141  0.29628   42.25350  1.000 50.02511  ? 7   ASP A CA  1 
ATOM 57   C C   . ASP A 1 7   ? 10.10726  0.43868   41.84963  1.000 50.41996  ? 7   ASP A C   1 
ATOM 58   O O   . ASP A 1 7   ? 9.51500   -0.48819  41.29863  1.000 50.48579  ? 7   ASP A O   1 
ATOM 59   C CB  . ASP A 1 7   ? 12.43716  0.24707   41.00550  1.000 50.53004  ? 7   ASP A CB  1 
ATOM 60   C CG  . ASP A 1 7   ? 12.45377  1.55778   40.27341  1.000 60.13651  ? 7   ASP A CG  1 
ATOM 61   O OD1 . ASP A 1 7   ? 11.97806  2.58504   40.83986  1.000 61.44952  ? 7   ASP A OD1 1 
ATOM 62   O OD2 . ASP A 1 7   ? 12.87601  1.54122   39.09077  1.000 67.11117  ? 7   ASP A OD2 1 
ATOM 63   N N   . PHE A 1 8   ? 9.52987   1.59954   42.12462  1.000 47.56296  ? 8   PHE A N   1 
ATOM 64   C CA  . PHE A 1 8   ? 8.15135   1.90607   41.79211  1.000 47.63612  ? 8   PHE A CA  1 
ATOM 65   C C   . PHE A 1 8   ? 8.12256   2.90112   40.65015  1.000 52.48005  ? 8   PHE A C   1 
ATOM 66   O O   . PHE A 1 8   ? 8.97592   3.78590   40.55920  1.000 55.05850  ? 8   PHE A O   1 
ATOM 67   C CB  . PHE A 1 8   ? 7.39043   2.53419   42.96606  1.000 50.42716  ? 8   PHE A CB  1 
ATOM 68   C CG  . PHE A 1 8   ? 6.88035   1.56772   43.97894  1.000 46.35068  ? 8   PHE A CG  1 
ATOM 69   C CD1 . PHE A 1 8   ? 5.64001   0.95463   43.79614  1.000 46.67224  ? 8   PHE A CD1 1 
ATOM 70   C CD2 . PHE A 1 8   ? 7.61597   1.28384   45.12373  1.000 45.34394  ? 8   PHE A CD2 1 
ATOM 71   C CE1 . PHE A 1 8   ? 5.14407   0.05021   44.72462  1.000 44.51106  ? 8   PHE A CE1 1 
ATOM 72   C CE2 . PHE A 1 8   ? 7.13483   0.38238   46.05635  1.000 48.04548  ? 8   PHE A CE2 1 
ATOM 73   C CZ  . PHE A 1 8   ? 5.88872   -0.22682  45.86932  1.000 45.13149  ? 8   PHE A CZ  1 
ATOM 74   N N   . GLU A 1 9   ? 7.12305   2.75096   39.79382  1.000 52.20679  ? 9   GLU A N   1 
ATOM 75   C CA  . GLU A 1 9   ? 6.74269   3.76689   38.84078  1.000 51.46678  ? 9   GLU A CA  1 
ATOM 76   C C   . GLU A 1 9   ? 5.32698   4.16022   39.21318  1.000 52.44559  ? 9   GLU A C   1 
ATOM 77   O O   . GLU A 1 9   ? 4.51011   3.28925   39.54761  1.000 48.49434  ? 9   GLU A O   1 
ATOM 78   C CB  . GLU A 1 9   ? 6.84769   3.25840   37.40115  1.000 57.39959  ? 9   GLU A CB  1 
ATOM 79   C CG  . GLU A 1 9   ? 8.28556   2.84656   36.98314  1.000 62.74195  ? 9   GLU A CG  1 
ATOM 80   C CD  . GLU A 1 9   ? 8.42437   2.57196   35.46354  1.000 75.05277  ? 9   GLU A CD  1 
ATOM 81   O OE1 . GLU A 1 9   ? 7.41589   2.67332   34.72217  1.000 74.87967  ? 9   GLU A OE1 1 
ATOM 82   O OE2 . GLU A 1 9   ? 9.54561   2.24634   35.00149  1.000 74.89183  ? 9   GLU A OE2 1 
ATOM 83   N N   . THR A 1 10  ? 5.06123   5.47833   39.22869  1.000 54.58858  ? 10  THR A N   1 
ATOM 84   C CA  . THR A 1 10  ? 3.91177   6.02310   39.94634  1.000 51.69644  ? 10  THR A CA  1 
ATOM 85   C C   . THR A 1 10  ? 3.29153   7.18213   39.18761  1.000 52.06872  ? 10  THR A C   1 
ATOM 86   O O   . THR A 1 10  ? 3.97439   7.87799   38.44379  1.000 62.47934  ? 10  THR A O   1 
ATOM 87   C CB  . THR A 1 10  ? 4.29982   6.52688   41.34885  1.000 54.46234  ? 10  THR A CB  1 
ATOM 88   O OG1 . THR A 1 10  ? 5.21276   7.61007   41.21737  1.000 56.31984  ? 10  THR A OG1 1 
ATOM 89   C CG2 . THR A 1 10  ? 4.97307   5.43907   42.19220  1.000 52.87061  ? 10  THR A CG2 1 
ATOM 90   N N   . MET A 1 11  ? 1.99565   7.40293   39.41482  1.000 51.56013  ? 11  MET A N   1 
ATOM 91   C CA  . MET A 1 11  ? 1.25799   8.57714   38.95301  1.000 53.07958  ? 11  MET A CA  1 
ATOM 92   C C   . MET A 1 11  ? 1.11780   9.68205   40.00189  1.000 58.12069  ? 11  MET A C   1 
ATOM 93   O O   . MET A 1 11  ? 0.29201   10.58830  39.82198  1.000 56.40885  ? 11  MET A O   1 
ATOM 94   C CB  . MET A 1 11  ? -0.14137  8.17809   38.50577  1.000 55.91188  ? 11  MET A CB  1 
ATOM 95   C CG  . MET A 1 11  ? -0.16028  7.46603   37.22288  1.000 62.56942  ? 11  MET A CG  1 
ATOM 96   S SD  . MET A 1 11  ? 0.43656   8.54341   35.90614  1.000 71.73489  ? 11  MET A SD  1 
ATOM 97   C CE  . MET A 1 11  ? 0.55969   7.31533   34.62036  1.000 71.73533  ? 11  MET A CE  1 
ATOM 98   N N   . GLY A 1 12  ? 1.85056   9.60153   41.10772  1.000 56.30683  ? 12  GLY A N   1 
ATOM 99   C CA  . GLY A 1 12  ? 1.78097   10.60313  42.14813  1.000 55.21875  ? 12  GLY A CA  1 
ATOM 100  C C   . GLY A 1 12  ? 3.06914   10.49949  42.91729  1.000 61.47754  ? 12  GLY A C   1 
ATOM 101  O O   . GLY A 1 12  ? 3.92154   9.67035   42.59920  1.000 64.60767  ? 12  GLY A O   1 
ATOM 102  N N   . SER A 1 13  ? 3.21336   11.34670  43.95180  1.000 71.37671  ? 13  SER A N   1 
ATOM 103  C CA  . SER A 1 13  ? 4.48350   11.38022  44.67588  1.000 74.15848  ? 13  SER A CA  1 
ATOM 104  C C   . SER A 1 13  ? 4.35704   11.42561  46.20593  1.000 75.24800  ? 13  SER A C   1 
ATOM 105  O O   . SER A 1 13  ? 5.36177   11.67432  46.88585  1.000 78.70858  ? 13  SER A O   1 
ATOM 106  C CB  . SER A 1 13  ? 5.37020   12.55405  44.17813  1.000 71.05498  ? 13  SER A CB  1 
ATOM 107  O OG  . SER A 1 13  ? 4.74012   13.82667  44.26397  1.000 71.17254  ? 13  SER A OG  1 
ATOM 108  N N   . GLY A 1 14  ? 3.18092   11.16026  46.78208  1.000 61.21477  ? 14  GLY A N   1 
ATOM 109  C CA  . GLY A 1 14  ? 3.07691   10.87167  48.19764  1.000 61.54977  ? 14  GLY A CA  1 
ATOM 110  C C   . GLY A 1 14  ? 2.91484   9.37575   48.45460  1.000 60.78986  ? 14  GLY A C   1 
ATOM 111  O O   . GLY A 1 14  ? 2.83844   8.56418   47.53986  1.000 62.98448  ? 14  GLY A O   1 
ATOM 112  N N   . GLU A 1 15  ? 2.80996   9.01130   49.73226  1.000 58.92036  ? 15  GLU A N   1 
ATOM 113  C CA  . GLU A 1 15  ? 2.72304   7.57955   50.02875  1.000 55.11026  ? 15  GLU A CA  1 
ATOM 114  C C   . GLU A 1 15  ? 1.43505   6.95927   49.48832  1.000 54.04240  ? 15  GLU A C   1 
ATOM 115  O O   . GLU A 1 15  ? 1.31255   5.72984   49.49566  1.000 56.84835  ? 15  GLU A O   1 
ATOM 116  C CB  . GLU A 1 15  ? 2.85513   7.31941   51.54537  1.000 55.76373  ? 15  GLU A CB  1 
ATOM 117  C CG  . GLU A 1 15  ? 1.58957   7.59861   52.39461  1.000 57.76781  ? 15  GLU A CG  1 
ATOM 118  C CD  . GLU A 1 15  ? 1.83681   7.67978   53.92393  1.000 60.07429  ? 15  GLU A CD  1 
ATOM 119  O OE1 . GLU A 1 15  ? 3.01238   7.64642   54.39450  1.000 58.79508  ? 15  GLU A OE1 1 
ATOM 120  O OE2 . GLU A 1 15  ? 0.82599   7.79234   54.65843  1.000 60.47591  ? 15  GLU A OE2 1 
ATOM 121  N N   . LYS A 1 16  ? 0.48779   7.77589   49.02405  1.000 48.64570  ? 16  LYS A N   1 
ATOM 122  C CA  . LYS A 1 16  ? -0.72977  7.34979   48.35185  1.000 46.71613  ? 16  LYS A CA  1 
ATOM 123  C C   . LYS A 1 16  ? -0.61021  7.43538   46.82815  1.000 51.38269  ? 16  LYS A C   1 
ATOM 124  O O   . LYS A 1 16  ? -1.62304  7.36303   46.11085  1.000 47.12867  ? 16  LYS A O   1 
ATOM 125  C CB  . LYS A 1 16  ? -1.89934  8.20167   48.84566  1.000 48.36367  ? 16  LYS A CB  1 
ATOM 126  C CG  . LYS A 1 16  ? -2.17919  8.02243   50.30442  1.000 52.06850  ? 16  LYS A CG  1 
ATOM 127  C CD  . LYS A 1 16  ? -2.60095  6.60346   50.48787  1.000 56.18972  ? 16  LYS A CD  1 
ATOM 128  C CE  . LYS A 1 16  ? -2.87115  6.23010   51.88759  1.000 53.66127  ? 16  LYS A CE  1 
ATOM 129  N NZ  . LYS A 1 16  ? -3.02762  4.76198   51.84927  1.000 52.92417  ? 16  LYS A NZ  1 
ATOM 130  N N   . ALA A 1 17  ? 0.60484   7.64934   46.33117  1.000 51.02390  ? 17  ALA A N   1 
ATOM 131  C CA  . ALA A 1 17  ? 0.88089   7.55032   44.91321  1.000 52.80479  ? 17  ALA A CA  1 
ATOM 132  C C   . ALA A 1 17  ? 0.17663   6.34098   44.31074  1.000 52.11025  ? 17  ALA A C   1 
ATOM 133  O O   . ALA A 1 17  ? 0.30826   5.21603   44.81025  1.000 47.24253  ? 17  ALA A O   1 
ATOM 134  C CB  . ALA A 1 17  ? 2.39041   7.43883   44.69774  1.000 53.11436  ? 17  ALA A CB  1 
ATOM 135  N N   . ALA A 1 18  ? -0.59538  6.58801   43.25058  1.000 51.06055  ? 18  ALA A N   1 
ATOM 136  C CA  . ALA A 1 18  ? -1.02755  5.50510   42.38479  1.000 48.80729  ? 18  ALA A CA  1 
ATOM 137  C C   . ALA A 1 18  ? 0.20944   4.84502   41.78994  1.000 48.50447  ? 18  ALA A C   1 
ATOM 138  O O   . ALA A 1 18  ? 1.19487   5.52281   41.48737  1.000 48.00815  ? 18  ALA A O   1 
ATOM 139  C CB  . ALA A 1 18  ? -1.96250  6.03631   41.30296  1.000 49.20435  ? 18  ALA A CB  1 
ATOM 140  N N   . VAL A 1 19  ? 0.19996   3.50896   41.70157  1.000 46.31179  ? 19  VAL A N   1 
ATOM 141  C CA  . VAL A 1 19  ? 1.40790   2.74123   41.38373  1.000 47.66066  ? 19  VAL A CA  1 
ATOM 142  C C   . VAL A 1 19  ? 1.22539   2.04106   40.04398  1.000 47.91593  ? 19  VAL A C   1 
ATOM 143  O O   . VAL A 1 19  ? 0.23400   1.32910   39.83227  1.000 44.57630  ? 19  VAL A O   1 
ATOM 144  C CB  . VAL A 1 19  ? 1.78108   1.74199   42.49671  1.000 44.88281  ? 19  VAL A CB  1 
ATOM 145  C CG1 . VAL A 1 19  ? 2.26342   2.48436   43.70471  1.000 45.88562  ? 19  VAL A CG1 1 
ATOM 146  C CG2 . VAL A 1 19  ? 0.59839   0.89584   42.88512  1.000 44.39658  ? 19  VAL A CG2 1 
ATOM 147  N N   . ILE A 1 20  ? 2.17356   2.27293   39.13360  1.000 48.97962  ? 20  ILE A N   1 
ATOM 148  C CA  . ILE A 1 20  ? 2.10137   1.71411   37.78250  1.000 50.92532  ? 20  ILE A CA  1 
ATOM 149  C C   . ILE A 1 20  ? 2.70298   0.31168   37.74150  1.000 48.89464  ? 20  ILE A C   1 
ATOM 150  O O   . ILE A 1 20  ? 2.06069   -0.62573  37.25162  1.000 47.02720  ? 20  ILE A O   1 
ATOM 151  C CB  . ILE A 1 20  ? 2.76527   2.67042   36.75363  1.000 43.28626  ? 20  ILE A CB  1 
ATOM 152  N N   . ASP A 1 21  ? 3.90381   0.14007   38.30519  1.000 45.31047  ? 21  ASP A N   1 
ATOM 153  C CA  . ASP A 1 21  ? 4.52557   -1.17364  38.37889  1.000 46.46027  ? 21  ASP A CA  1 
ATOM 154  C C   . ASP A 1 21  ? 5.53457   -1.18071  39.52130  1.000 48.49528  ? 21  ASP A C   1 
ATOM 155  O O   . ASP A 1 21  ? 6.03568   -0.13495  39.94141  1.000 47.76665  ? 21  ASP A O   1 
ATOM 156  C CB  . ASP A 1 21  ? 5.16164   -1.55636  37.02377  1.000 49.82051  ? 21  ASP A CB  1 
ATOM 157  C CG  . ASP A 1 21  ? 6.54759   -0.87821  36.74042  1.000 59.32936  ? 21  ASP A CG  1 
ATOM 158  O OD1 . ASP A 1 21  ? 7.37413   -0.61079  37.65772  1.000 57.59660  ? 21  ASP A OD1 1 
ATOM 159  O OD2 . ASP A 1 21  ? 6.76960   -0.51447  35.55439  1.000 62.22531  ? 21  ASP A OD2 1 
ATOM 160  N N   . LEU A 1 22  ? 5.83551   -2.38111  40.01358  1.000 49.74612  ? 22  LEU A N   1 
ATOM 161  C CA  . LEU A 1 22  ? 6.80759   -2.57721  41.08380  1.000 48.94100  ? 22  LEU A CA  1 
ATOM 162  C C   . LEU A 1 22  ? 7.81987   -3.62756  40.64528  1.000 48.17816  ? 22  LEU A C   1 
ATOM 163  O O   . LEU A 1 22  ? 7.43856   -4.69991  40.17337  1.000 46.24077  ? 22  LEU A O   1 
ATOM 164  C CB  . LEU A 1 22  ? 6.12128   -2.99436  42.41092  1.000 45.39013  ? 22  LEU A CB  1 
ATOM 165  C CG  . LEU A 1 22  ? 7.06024   -3.35635  43.57494  1.000 44.03242  ? 22  LEU A CG  1 
ATOM 166  C CD1 . LEU A 1 22  ? 8.02472   -2.24183  43.97513  1.000 40.48219  ? 22  LEU A CD1 1 
ATOM 167  C CD2 . LEU A 1 22  ? 6.27862   -3.85516  44.77696  1.000 44.47920  ? 22  LEU A CD2 1 
ATOM 168  N N   . ALA A 1 23  ? 9.10121   -3.32286  40.82203  1.000 47.64966  ? 23  ALA A N   1 
ATOM 169  C CA  . ALA A 1 23  ? 10.18903  -4.18436  40.40432  1.000 45.48274  ? 23  ALA A CA  1 
ATOM 170  C C   . ALA A 1 23  ? 11.07694  -4.49413  41.59633  1.000 46.00322  ? 23  ALA A C   1 
ATOM 171  O O   . ALA A 1 23  ? 11.52876  -3.57963  42.28899  1.000 45.35706  ? 23  ALA A O   1 
ATOM 172  C CB  . ALA A 1 23  ? 11.01217  -3.51360  39.30168  1.000 51.18382  ? 23  ALA A CB  1 
ATOM 173  N N   . VAL A 1 24  ? 11.36569  -5.77456  41.80152  1.000 43.38321  ? 24  VAL A N   1 
ATOM 174  C CA  . VAL A 1 24  ? 12.17181  -6.21089  42.92953  1.000 48.90349  ? 24  VAL A CA  1 
ATOM 175  C C   . VAL A 1 24  ? 13.17615  -7.25055  42.43527  1.000 48.17094  ? 24  VAL A C   1 
ATOM 176  O O   . VAL A 1 24  ? 12.80606  -8.15631  41.68923  1.000 48.49472  ? 24  VAL A O   1 
ATOM 177  C CB  . VAL A 1 24  ? 11.27416  -6.74699  44.08169  1.000 44.86342  ? 24  VAL A CB  1 
ATOM 178  C CG1 . VAL A 1 24  ? 10.40630  -7.88294  43.62284  1.000 44.12533  ? 24  VAL A CG1 1 
ATOM 179  C CG2 . VAL A 1 24  ? 12.10156  -7.15705  45.29744  1.000 39.58488  ? 24  VAL A CG2 1 
ATOM 180  N N   . ILE A 1 25  ? 14.44659  -7.10991  42.83615  1.000 46.67866  ? 25  ILE A N   1 
ATOM 181  C CA  . ILE A 1 25  ? 15.48410  -8.10559  42.59072  1.000 49.01788  ? 25  ILE A CA  1 
ATOM 182  C C   . ILE A 1 25  ? 16.20918  -8.40702  43.90059  1.000 50.81709  ? 25  ILE A C   1 
ATOM 183  O O   . ILE A 1 25  ? 16.65529  -7.49257  44.59736  1.000 51.54185  ? 25  ILE A O   1 
ATOM 184  C CB  . ILE A 1 25  ? 16.50748  -7.65067  41.52190  1.000 54.43223  ? 25  ILE A CB  1 
ATOM 185  C CG1 . ILE A 1 25  ? 15.83767  -7.30014  40.17643  1.000 50.55956  ? 25  ILE A CG1 1 
ATOM 186  C CG2 . ILE A 1 25  ? 17.55285  -8.74677  41.30732  1.000 52.26540  ? 25  ILE A CG2 1 
ATOM 187  C CD1 . ILE A 1 25  ? 16.75690  -6.58465  39.19310  1.000 49.55967  ? 25  ILE A CD1 1 
ATOM 188  N N   . ALA A 1 26  ? 16.33578  -9.68775  44.22508  1.000 55.58489  ? 26  ALA A N   1 
ATOM 189  C CA  . ALA A 1 26  ? 17.18212  -10.15349 45.31184  1.000 54.87575  ? 26  ALA A CA  1 
ATOM 190  C C   . ALA A 1 26  ? 18.58553  -10.38091 44.77215  1.000 60.28759  ? 26  ALA A C   1 
ATOM 191  O O   . ALA A 1 26  ? 18.76420  -10.70059 43.59738  1.000 63.08228  ? 26  ALA A O   1 
ATOM 192  C CB  . ALA A 1 26  ? 16.62073  -11.43949 45.90664  1.000 54.25573  ? 26  ALA A CB  1 
ATOM 193  N N   . PHE A 1 27  ? 19.59046  -10.21310 45.62392  1.000 60.78757  ? 27  PHE A N   1 
ATOM 194  C CA  . PHE A 1 27  ? 20.90115  -9.93355  45.06560  1.000 62.72042  ? 27  PHE A CA  1 
ATOM 195  C C   . PHE A 1 27  ? 21.90988  -10.34742 46.12463  1.000 69.09767  ? 27  PHE A C   1 
ATOM 196  O O   . PHE A 1 27  ? 21.59120  -10.34117 47.31526  1.000 68.84147  ? 27  PHE A O   1 
ATOM 197  C CB  . PHE A 1 27  ? 20.80746  -8.45046  44.62445  1.000 60.37162  ? 27  PHE A CB  1 
ATOM 198  C CG  . PHE A 1 27  ? 21.48531  -7.39888  45.49263  1.000 60.68100  ? 27  PHE A CG  1 
ATOM 199  C CD1 . PHE A 1 27  ? 22.28487  -7.64607  46.57259  1.000 62.36855  ? 27  PHE A CD1 1 
ATOM 200  C CD2 . PHE A 1 27  ? 20.95606  -6.13031  45.42060  1.000 56.84134  ? 27  PHE A CD2 1 
ATOM 201  C CE1 . PHE A 1 27  ? 22.80015  -6.62523  47.32085  1.000 61.07386  ? 27  PHE A CE1 1 
ATOM 202  C CE2 . PHE A 1 27  ? 21.41791  -5.11640  46.22040  1.000 52.22125  ? 27  PHE A CE2 1 
ATOM 203  C CZ  . PHE A 1 27  ? 22.33045  -5.36247  47.15840  1.000 51.28299  ? 27  PHE A CZ  1 
ATOM 204  N N   . ASP A 1 28  ? 23.11476  -10.72712 45.71028  1.000 73.73628  ? 28  ASP A N   1 
ATOM 205  C CA  . ASP A 1 28  ? 24.10854  -11.15177 46.68943  1.000 75.41502  ? 28  ASP A CA  1 
ATOM 206  C C   . ASP A 1 28  ? 24.99031  -9.96848  47.06397  1.000 76.07518  ? 28  ASP A C   1 
ATOM 207  O O   . ASP A 1 28  ? 25.69698  -9.44802  46.19744  1.000 77.97190  ? 28  ASP A O   1 
ATOM 208  C CB  . ASP A 1 28  ? 24.95576  -12.29256 46.15087  1.000 79.19279  ? 28  ASP A CB  1 
ATOM 209  C CG  . ASP A 1 28  ? 25.87848  -12.90580 47.21959  1.000 83.69562  ? 28  ASP A CG  1 
ATOM 210  O OD1 . ASP A 1 28  ? 25.86962  -12.45115 48.39067  1.000 80.94648  ? 28  ASP A OD1 1 
ATOM 211  O OD2 . ASP A 1 28  ? 26.63492  -13.84312 46.88188  1.000 87.11288  ? 28  ASP A OD2 1 
ATOM 212  N N   . PRO A 1 29  ? 24.99365  -9.52380  48.32140  1.000 77.00118  ? 29  PRO A N   1 
ATOM 213  C CA  . PRO A 1 29  ? 25.77211  -8.33313  48.68568  1.000 75.75313  ? 29  PRO A CA  1 
ATOM 214  C C   . PRO A 1 29  ? 27.25223  -8.59662  48.88860  1.000 78.51874  ? 29  PRO A C   1 
ATOM 215  O O   . PRO A 1 29  ? 27.98173  -7.66144  49.23047  1.000 81.78171  ? 29  PRO A O   1 
ATOM 216  C CB  . PRO A 1 29  ? 25.11542  -7.88888  50.00694  1.000 72.96211  ? 29  PRO A CB  1 
ATOM 217  C CG  . PRO A 1 29  ? 24.62178  -9.15160  50.61387  1.000 68.84687  ? 29  PRO A CG  1 
ATOM 218  C CD  . PRO A 1 29  ? 24.17779  -10.01584 49.45322  1.000 71.17008  ? 29  PRO A CD  1 
ATOM 219  N N   . ASN A 1 30  ? 27.70961  -9.82605  48.72552  1.000 80.79512  ? 30  ASN A N   1 
ATOM 220  C CA  . ASN A 1 30  ? 29.13560  -10.13198 48.85655  1.000 86.13544  ? 30  ASN A CA  1 
ATOM 221  C C   . ASN A 1 30  ? 29.95403  -9.47936  47.73768  1.000 90.76030  ? 30  ASN A C   1 
ATOM 222  O O   . ASN A 1 30  ? 29.73762  -9.78306  46.54885  1.000 84.47295  ? 30  ASN A O   1 
ATOM 223  C CB  . ASN A 1 30  ? 29.32506  -11.64333 48.84505  1.000 87.95768  ? 30  ASN A CB  1 
ATOM 224  C CG  . ASN A 1 30  ? 30.74605  -12.05969 49.12947  1.000 88.60121  ? 30  ASN A CG  1 
ATOM 225  O OD1 . ASN A 1 30  ? 31.62304  -11.22530 49.35607  1.000 88.78705  ? 30  ASN A OD1 1 
ATOM 226  N ND2 . ASN A 1 30  ? 30.98421  -13.36434 49.10932  1.000 82.41749  ? 30  ASN A ND2 1 
ATOM 227  N N   . PRO A 1 31  ? 30.91335  -8.60771  48.06619  1.000 89.39108  ? 31  PRO A N   1 
ATOM 228  C CA  . PRO A 1 31  ? 31.68251  -7.92578  47.01583  1.000 88.60650  ? 31  PRO A CA  1 
ATOM 229  C C   . PRO A 1 31  ? 32.57934  -8.84741  46.19999  1.000 93.60042  ? 31  PRO A C   1 
ATOM 230  O O   . PRO A 1 31  ? 33.04984  -8.42944  45.13275  1.000 90.71317  ? 31  PRO A O   1 
ATOM 231  C CB  . PRO A 1 31  ? 32.49929  -6.88628  47.79876  1.000 89.13485  ? 31  PRO A CB  1 
ATOM 232  C CG  . PRO A 1 31  ? 32.58704  -7.42552  49.17520  1.000 92.33402  ? 31  PRO A CG  1 
ATOM 233  C CD  . PRO A 1 31  ? 31.28998  -8.14904  49.41494  1.000 90.95568  ? 31  PRO A CD  1 
ATOM 234  N N   . GLU A 1 32  ? 32.84834  -10.07185 46.65741  1.000 103.80587 ? 32  GLU A N   1 
ATOM 235  C CA  . GLU A 1 32  ? 33.53641  -11.02550 45.79567  1.000 104.23822 ? 32  GLU A CA  1 
ATOM 236  C C   . GLU A 1 32  ? 32.61102  -11.73022 44.81761  1.000 103.15626 ? 32  GLU A C   1 
ATOM 237  O O   . GLU A 1 32  ? 33.10277  -12.44095 43.93944  1.000 104.02048 ? 32  GLU A O   1 
ATOM 238  C CB  . GLU A 1 32  ? 34.28325  -12.08559 46.60416  1.000 103.15866 ? 32  GLU A CB  1 
ATOM 239  C CG  . GLU A 1 32  ? 35.60559  -11.62954 47.18344  1.000 107.77334 ? 32  GLU A CG  1 
ATOM 240  C CD  . GLU A 1 32  ? 35.48172  -11.03585 48.56818  1.000 117.74389 ? 32  GLU A CD  1 
ATOM 241  O OE1 . GLU A 1 32  ? 34.36472  -11.04745 49.13439  1.000 115.23444 ? 32  GLU A OE1 1 
ATOM 242  O OE2 . GLU A 1 32  ? 36.51217  -10.56658 49.10106  1.000 122.83800 ? 32  GLU A OE2 1 
ATOM 243  N N   . VAL A 1 33  ? 31.30349  -11.54991 44.92603  1.000 91.64436  ? 33  VAL A N   1 
ATOM 244  C CA  . VAL A 1 33  ? 30.34653  -12.18958 44.02962  1.000 90.63246  ? 33  VAL A CA  1 
ATOM 245  C C   . VAL A 1 33  ? 29.88664  -11.13153 43.02428  1.000 85.36114  ? 33  VAL A C   1 
ATOM 246  O O   . VAL A 1 33  ? 29.08603  -10.25339 43.35437  1.000 87.85877  ? 33  VAL A O   1 
ATOM 247  C CB  . VAL A 1 33  ? 29.17508  -12.78668 44.81646  1.000 85.16834  ? 33  VAL A CB  1 
ATOM 248  C CG1 . VAL A 1 33  ? 28.17473  -13.46131 43.88453  1.000 82.88663  ? 33  VAL A CG1 1 
ATOM 249  C CG2 . VAL A 1 33  ? 29.69047  -13.73608 45.87425  1.000 80.64670  ? 33  VAL A CG2 1 
ATOM 250  N N   . VAL A 1 34  ? 30.37881  -11.19058 41.79142  1.000 79.98263  ? 34  VAL A N   1 
ATOM 251  C CA  . VAL A 1 34  ? 29.99787  -10.21708 40.76873  1.000 81.09966  ? 34  VAL A CA  1 
ATOM 252  C C   . VAL A 1 34  ? 29.09140  -10.90641 39.75344  1.000 79.21506  ? 34  VAL A C   1 
ATOM 253  O O   . VAL A 1 34  ? 29.48697  -11.86736 39.08192  1.000 76.48990  ? 34  VAL A O   1 
ATOM 254  C CB  . VAL A 1 34  ? 31.21938  -9.55536  40.10783  1.000 79.54859  ? 34  VAL A CB  1 
ATOM 255  C CG1 . VAL A 1 34  ? 32.10763  -10.57763 39.37819  1.000 83.30840  ? 34  VAL A CG1 1 
ATOM 256  C CG2 . VAL A 1 34  ? 30.76281  -8.45387  39.17657  1.000 77.15741  ? 34  VAL A CG2 1 
ATOM 257  N N   . GLU A 1 35  ? 27.86991  -10.41259 39.65271  1.000 78.65804  ? 35  GLU A N   1 
ATOM 258  C CA  . GLU A 1 35  ? 26.78101  -11.11047 38.99903  1.000 74.78132  ? 35  GLU A CA  1 
ATOM 259  C C   . GLU A 1 35  ? 26.43476  -10.36685 37.72651  1.000 70.64585  ? 35  GLU A C   1 
ATOM 260  O O   . GLU A 1 35  ? 26.60763  -9.15296  37.63426  1.000 70.57299  ? 35  GLU A O   1 
ATOM 261  C CB  . GLU A 1 35  ? 25.56658  -11.20384 39.92929  1.000 75.93901  ? 35  GLU A CB  1 
ATOM 262  C CG  . GLU A 1 35  ? 25.77299  -12.16014 41.11606  1.000 78.41523  ? 35  GLU A CG  1 
ATOM 263  C CD  . GLU A 1 35  ? 24.64771  -12.10212 42.14376  1.000 81.99786  ? 35  GLU A CD  1 
ATOM 264  O OE1 . GLU A 1 35  ? 23.85995  -11.13362 42.11609  1.000 81.04025  ? 35  GLU A OE1 1 
ATOM 265  O OE2 . GLU A 1 35  ? 24.53386  -13.03993 42.96603  1.000 83.58107  ? 35  GLU A OE2 1 
ATOM 266  N N   . THR A 1 36  ? 25.99611  -11.09674 36.72310  1.000 72.00478  ? 36  THR A N   1 
ATOM 267  C CA  . THR A 1 36  ? 25.91795  -10.39204 35.46732  1.000 69.61339  ? 36  THR A CA  1 
ATOM 268  C C   . THR A 1 36  ? 24.58138  -9.69101  35.36896  1.000 66.80079  ? 36  THR A C   1 
ATOM 269  O O   . THR A 1 36  ? 23.62162  -10.03354 36.05101  1.000 65.56774  ? 36  THR A O   1 
ATOM 270  C CB  . THR A 1 36  ? 26.11889  -11.32985 34.28247  1.000 67.39233  ? 36  THR A CB  1 
ATOM 271  O OG1 . THR A 1 36  ? 24.96908  -12.15685 34.13242  1.000 68.63074  ? 36  THR A OG1 1 
ATOM 272  C CG2 . THR A 1 36  ? 27.34061  -12.19959 34.51566  1.000 59.31139  ? 36  THR A CG2 1 
ATOM 273  N N   . PHE A 1 37  ? 24.54985  -8.66451  34.52897  1.000 67.47580  ? 37  PHE A N   1 
ATOM 274  C CA  . PHE A 1 37  ? 23.30023  -8.00015  34.21656  1.000 63.08549  ? 37  PHE A CA  1 
ATOM 275  C C   . PHE A 1 37  ? 22.24149  -9.00525  33.76567  1.000 69.41943  ? 37  PHE A C   1 
ATOM 276  O O   . PHE A 1 37  ? 21.12821  -9.01911  34.30150  1.000 68.63724  ? 37  PHE A O   1 
ATOM 277  C CB  . PHE A 1 37  ? 23.56651  -6.93905  33.16150  1.000 58.88201  ? 37  PHE A CB  1 
ATOM 278  C CG  . PHE A 1 37  ? 22.36459  -6.18076  32.74474  1.000 60.87777  ? 37  PHE A CG  1 
ATOM 279  C CD1 . PHE A 1 37  ? 21.88723  -5.13764  33.51279  1.000 60.87869  ? 37  PHE A CD1 1 
ATOM 280  C CD2 . PHE A 1 37  ? 21.70559  -6.50593  31.58031  1.000 62.96256  ? 37  PHE A CD2 1 
ATOM 281  C CE1 . PHE A 1 37  ? 20.77074  -4.42725  33.12024  1.000 61.10587  ? 37  PHE A CE1 1 
ATOM 282  C CE2 . PHE A 1 37  ? 20.59108  -5.79677  31.17990  1.000 67.73095  ? 37  PHE A CE2 1 
ATOM 283  C CZ  . PHE A 1 37  ? 20.11352  -4.75443  31.96087  1.000 62.55031  ? 37  PHE A CZ  1 
ATOM 284  N N   . ASP A 1 38  ? 22.58178  -9.88402  32.80877  1.000 83.27766  ? 38  ASP A N   1 
ATOM 285  C CA  . ASP A 1 38  ? 21.60905  -10.86285 32.30960  1.000 84.33031  ? 38  ASP A CA  1 
ATOM 286  C C   . ASP A 1 38  ? 21.10651  -11.75069 33.43219  1.000 84.74215  ? 38  ASP A C   1 
ATOM 287  O O   . ASP A 1 38  ? 19.93367  -12.14721 33.45990  1.000 85.23558  ? 38  ASP A O   1 
ATOM 288  C CB  . ASP A 1 38  ? 22.23226  -11.73740 31.22356  1.000 86.87896  ? 38  ASP A CB  1 
ATOM 289  C CG  . ASP A 1 38  ? 22.52564  -10.97537 29.93949  1.000 96.46950  ? 38  ASP A CG  1 
ATOM 290  O OD1 . ASP A 1 38  ? 21.78563  -10.01557 29.62453  1.000 96.45253  ? 38  ASP A OD1 1 
ATOM 291  O OD2 . ASP A 1 38  ? 23.50157  -11.34809 29.24038  1.000 100.66537 ? 38  ASP A OD2 1 
ATOM 292  N N   . GLU A 1 39  ? 22.00026  -12.07232 34.36083  1.000 74.33551  ? 39  GLU A N   1 
ATOM 293  C CA  . GLU A 1 39  ? 21.69562  -12.93839 35.49141  1.000 70.36184  ? 39  GLU A CA  1 
ATOM 294  C C   . GLU A 1 39  ? 20.73381  -12.26697 36.47065  1.000 69.06719  ? 39  GLU A C   1 
ATOM 295  O O   . GLU A 1 39  ? 19.77115  -12.89406 36.92374  1.000 69.60756  ? 39  GLU A O   1 
ATOM 296  C CB  . GLU A 1 39  ? 23.02280  -13.30489 36.14782  1.000 70.09843  ? 39  GLU A CB  1 
ATOM 297  C CG  . GLU A 1 39  ? 23.06337  -14.37112 37.17069  1.000 74.47740  ? 39  GLU A CG  1 
ATOM 298  C CD  . GLU A 1 39  ? 24.50652  -14.64288 37.57269  1.000 79.30000  ? 39  GLU A CD  1 
ATOM 299  O OE1 . GLU A 1 39  ? 25.39823  -13.99831 36.97111  1.000 76.31288  ? 39  GLU A OE1 1 
ATOM 300  O OE2 . GLU A 1 39  ? 24.75400  -15.47129 38.49115  1.000 87.49879  ? 39  GLU A OE2 1 
ATOM 301  N N   . LEU A 1 40  ? 20.97068  -10.99064 36.80755  1.000 66.25393  ? 40  LEU A N   1 
ATOM 302  C CA  . LEU A 1 40  ? 20.06577  -10.26253 37.69753  1.000 58.49822  ? 40  LEU A CA  1 
ATOM 303  C C   . LEU A 1 40  ? 18.70311  -10.07651 37.06051  1.000 59.18787  ? 40  LEU A C   1 
ATOM 304  O O   . LEU A 1 40  ? 17.67767  -10.31254 37.70304  1.000 58.72922  ? 40  LEU A O   1 
ATOM 305  C CB  . LEU A 1 40  ? 20.64319  -8.90140  38.04499  1.000 56.49807  ? 40  LEU A CB  1 
ATOM 306  C CG  . LEU A 1 40  ? 21.97117  -8.94388  38.77560  1.000 60.88215  ? 40  LEU A CG  1 
ATOM 307  C CD1 . LEU A 1 40  ? 22.54993  -7.54423  38.82549  1.000 56.40665  ? 40  LEU A CD1 1 
ATOM 308  C CD2 . LEU A 1 40  ? 21.80933  -9.56336  40.16568  1.000 59.78054  ? 40  LEU A CD2 1 
ATOM 309  N N   . VAL A 1 41  ? 18.67552  -9.65388  35.79305  1.000 59.28360  ? 41  VAL A N   1 
ATOM 310  C CA  . VAL A 1 41  ? 17.41402  -9.35322  35.12330  1.000 57.00655  ? 41  VAL A CA  1 
ATOM 311  C C   . VAL A 1 41  ? 16.48858  -10.56518 35.13711  1.000 60.92648  ? 41  VAL A C   1 
ATOM 312  O O   . VAL A 1 41  ? 15.29303  -10.44988 35.43260  1.000 62.30599  ? 41  VAL A O   1 
ATOM 313  C CB  . VAL A 1 41  ? 17.67277  -8.85849  33.69285  1.000 59.13821  ? 41  VAL A CB  1 
ATOM 314  C CG1 . VAL A 1 41  ? 16.37319  -8.77319  32.91471  1.000 55.76137  ? 41  VAL A CG1 1 
ATOM 315  C CG2 . VAL A 1 41  ? 18.34529  -7.51313  33.74127  1.000 61.06730  ? 41  VAL A CG2 1 
ATOM 316  N N   . SER A 1 42  ? 17.01125  -11.74967 34.82994  1.000 59.99984  ? 42  SER A N   1 
ATOM 317  C CA  . SER A 1 42  ? 16.11151  -12.89802 34.87748  1.000 58.79335  ? 42  SER A CA  1 
ATOM 318  C C   . SER A 1 42  ? 15.73835  -13.29198 36.31634  1.000 56.53042  ? 42  SER A C   1 
ATOM 319  O O   . SER A 1 42  ? 14.69119  -13.92114 36.53287  1.000 51.14913  ? 42  SER A O   1 
ATOM 320  C CB  . SER A 1 42  ? 16.71564  -14.06365 34.08520  1.000 56.30117  ? 42  SER A CB  1 
ATOM 321  O OG  . SER A 1 42  ? 17.94893  -14.48574 34.62237  1.000 64.57948  ? 42  SER A OG  1 
ATOM 322  N N   . ARG A 1 43  ? 16.52859  -12.89090 37.31017  1.000 53.19942  ? 43  ARG A N   1 
ATOM 323  C CA  . ARG A 1 43  ? 16.15369  -13.16663 38.68743  1.000 50.87962  ? 43  ARG A CA  1 
ATOM 324  C C   . ARG A 1 43  ? 15.04497  -12.23207 39.20131  1.000 57.18598  ? 43  ARG A C   1 
ATOM 325  O O   . ARG A 1 43  ? 14.34483  -12.58509 40.15516  1.000 56.35285  ? 43  ARG A O   1 
ATOM 326  C CB  . ARG A 1 43  ? 17.39257  -13.06582 39.58943  1.000 53.03111  ? 43  ARG A CB  1 
ATOM 327  C CG  . ARG A 1 43  ? 17.20421  -13.78240 40.89400  1.000 52.41435  ? 43  ARG A CG  1 
ATOM 328  C CD  . ARG A 1 43  ? 18.32651  -13.64412 41.90350  1.000 57.47290  ? 43  ARG A CD  1 
ATOM 329  N NE  . ARG A 1 43  ? 19.62616  -14.13105 41.46835  1.000 63.47499  ? 43  ARG A NE  1 
ATOM 330  C CZ  . ARG A 1 43  ? 20.76264  -13.45862 41.60889  1.000 68.83331  ? 43  ARG A CZ  1 
ATOM 331  N NH1 . ARG A 1 43  ? 20.80949  -12.31891 42.27916  1.000 67.90090  ? 43  ARG A NH1 1 
ATOM 332  N NH2 . ARG A 1 43  ? 21.88896  -13.96469 41.10161  1.000 69.79624  ? 43  ARG A NH2 1 
ATOM 333  N N   . GLY A 1 44  ? 14.84082  -11.04861 38.58583  1.000 53.61161  ? 44  GLY A N   1 
ATOM 334  C CA  . GLY A 1 44  ? 13.82948  -10.14762 39.08268  1.000 51.78838  ? 44  GLY A CA  1 
ATOM 335  C C   . GLY A 1 44  ? 12.40682  -10.47298 38.64108  1.000 53.94578  ? 44  GLY A C   1 
ATOM 336  O O   . GLY A 1 44  ? 12.16472  -11.30193 37.76699  1.000 55.57277  ? 44  GLY A O   1 
ATOM 337  N N   . ILE A 1 45  ? 11.43737  -9.79073  39.27641  1.000 52.74400  ? 45  ILE A N   1 
ATOM 338  C CA  . ILE A 1 45  ? 10.06099  -9.73787  38.78857  1.000 50.69826  ? 45  ILE A CA  1 
ATOM 339  C C   . ILE A 1 45  ? 9.57540   -8.28860  38.75173  1.000 49.28352  ? 45  ILE A C   1 
ATOM 340  O O   . ILE A 1 45  ? 10.04189  -7.42519  39.50571  1.000 45.58755  ? 45  ILE A O   1 
ATOM 341  C CB  . ILE A 1 45  ? 9.09879   -10.59491 39.63727  1.000 52.37581  ? 45  ILE A CB  1 
ATOM 342  C CG1 . ILE A 1 45  ? 8.95555   -10.00478 41.05179  1.000 53.14060  ? 45  ILE A CG1 1 
ATOM 343  C CG2 . ILE A 1 45  ? 9.57665   -12.01823 39.67422  1.000 50.95266  ? 45  ILE A CG2 1 
ATOM 344  C CD1 . ILE A 1 45  ? 7.85908   -10.63612 41.91746  1.000 49.11300  ? 45  ILE A CD1 1 
ATOM 345  N N   . LYS A 1 46  ? 8.65549   -8.02083  37.82550  1.000 48.43291  ? 46  LYS A N   1 
ATOM 346  C CA  . LYS A 1 46  ? 7.91873   -6.77220  37.77160  1.000 44.95915  ? 46  LYS A CA  1 
ATOM 347  C C   . LYS A 1 46  ? 6.45247   -7.11321  37.94976  1.000 50.49766  ? 46  LYS A C   1 
ATOM 348  O O   . LYS A 1 46  ? 5.91560   -7.94665  37.21830  1.000 49.87958  ? 46  LYS A O   1 
ATOM 349  C CB  . LYS A 1 46  ? 8.13611   -6.02429  36.46650  1.000 39.88153  ? 46  LYS A CB  1 
ATOM 350  N N   . ILE A 1 47  ? 5.83066   -6.49475  38.95134  1.000 52.55411  ? 47  ILE A N   1 
ATOM 351  C CA  . ILE A 1 47  ? 4.40382   -6.58844  39.23970  1.000 50.01026  ? 47  ILE A CA  1 
ATOM 352  C C   . ILE A 1 47  ? 3.77176   -5.36972  38.58211  1.000 49.98935  ? 47  ILE A C   1 
ATOM 353  O O   . ILE A 1 47  ? 4.27276   -4.25174  38.74976  1.000 51.14182  ? 47  ILE A O   1 
ATOM 354  C CB  . ILE A 1 47  ? 4.16629   -6.60623  40.77050  1.000 48.62641  ? 47  ILE A CB  1 
ATOM 355  C CG1 . ILE A 1 47  ? 4.89965   -7.79970  41.41675  1.000 48.60831  ? 47  ILE A CG1 1 
ATOM 356  C CG2 . ILE A 1 47  ? 2.66899   -6.64840  41.11711  1.000 48.58169  ? 47  ILE A CG2 1 
ATOM 357  C CD1 . ILE A 1 47  ? 5.26082   -7.66168  42.88555  1.000 47.46756  ? 47  ILE A CD1 1 
ATOM 358  N N   . LYS A 1 48  ? 2.72954   -5.56500  37.78201  1.000 50.26492  ? 48  LYS A N   1 
ATOM 359  C CA  . LYS A 1 48  ? 2.09437   -4.43462  37.11175  1.000 51.58055  ? 48  LYS A CA  1 
ATOM 360  C C   . LYS A 1 48  ? 0.67153   -4.27912  37.63331  1.000 55.18323  ? 48  LYS A C   1 
ATOM 361  O O   . LYS A 1 48  ? -0.11893  -5.23058  37.58548  1.000 56.53586  ? 48  LYS A O   1 
ATOM 362  C CB  . LYS A 1 48  ? 2.11814   -4.59301  35.58433  1.000 44.02653  ? 48  LYS A CB  1 
ATOM 363  N N   . PHE A 1 49  ? 0.34821   -3.07806  38.13169  1.000 54.73973  ? 49  PHE A N   1 
ATOM 364  C CA  . PHE A 1 49  ? -0.92029  -2.81566  38.80975  1.000 53.26870  ? 49  PHE A CA  1 
ATOM 365  C C   . PHE A 1 49  ? -1.95339  -2.20141  37.85698  1.000 54.86411  ? 49  PHE A C   1 
ATOM 366  O O   . PHE A 1 49  ? -1.62219  -1.44993  36.93395  1.000 54.01901  ? 49  PHE A O   1 
ATOM 367  C CB  . PHE A 1 49  ? -0.72970  -1.87083  40.00227  1.000 47.32273  ? 49  PHE A CB  1 
ATOM 368  C CG  . PHE A 1 49  ? 0.31350   -2.30401  40.97336  1.000 43.02841  ? 49  PHE A CG  1 
ATOM 369  C CD1 . PHE A 1 49  ? 0.05353   -3.26957  41.90558  1.000 43.53463  ? 49  PHE A CD1 1 
ATOM 370  C CD2 . PHE A 1 49  ? 1.55539   -1.70760  40.97025  1.000 45.55488  ? 49  PHE A CD2 1 
ATOM 371  C CE1 . PHE A 1 49  ? 1.01944   -3.66129  42.79520  1.000 42.62210  ? 49  PHE A CE1 1 
ATOM 372  C CE2 . PHE A 1 49  ? 2.52692   -2.08237  41.87093  1.000 46.17246  ? 49  PHE A CE2 1 
ATOM 373  C CZ  . PHE A 1 49  ? 2.25507   -3.07071  42.78094  1.000 44.50602  ? 49  PHE A CZ  1 
ATOM 374  N N   . ASP A 1 50  ? -3.22131  -2.50272  38.12117  1.000 55.89653  ? 50  ASP A N   1 
ATOM 375  C CA  . ASP A 1 50  ? -4.34636  -1.88631  37.41879  1.000 54.21876  ? 50  ASP A CA  1 
ATOM 376  C C   . ASP A 1 50  ? -4.56177  -0.45612  37.92928  1.000 57.45611  ? 50  ASP A C   1 
ATOM 377  O O   . ASP A 1 50  ? -4.95324  -0.25587  39.08807  1.000 58.60489  ? 50  ASP A O   1 
ATOM 378  C CB  . ASP A 1 50  ? -5.57786  -2.77354  37.60746  1.000 54.61100  ? 50  ASP A CB  1 
ATOM 379  C CG  . ASP A 1 50  ? -6.85460  -2.16946  37.05199  1.000 56.71595  ? 50  ASP A CG  1 
ATOM 380  O OD1 . ASP A 1 50  ? -6.83537  -0.99435  36.66326  1.000 61.69201  ? 50  ASP A OD1 1 
ATOM 381  O OD2 . ASP A 1 50  ? -7.90577  -2.86308  37.00332  1.000 60.07437  ? 50  ASP A OD2 1 
ATOM 382  N N   . LEU A 1 51  ? -4.31814  0.54254   37.05711  1.000 56.11113  ? 51  LEU A N   1 
ATOM 383  C CA  . LEU A 1 51  ? -4.54040  1.94560   37.42599  1.000 55.70490  ? 51  LEU A CA  1 
ATOM 384  C C   . LEU A 1 51  ? -6.01797  2.23850   37.69656  1.000 57.47386  ? 51  LEU A C   1 
ATOM 385  O O   . LEU A 1 51  ? -6.35855  2.81550   38.74206  1.000 56.85398  ? 51  LEU A O   1 
ATOM 386  C CB  . LEU A 1 51  ? -3.99706  2.89454   36.35534  1.000 49.25622  ? 51  LEU A CB  1 
ATOM 387  C CG  . LEU A 1 51  ? -2.47082  2.97027   36.29717  1.000 47.58965  ? 51  LEU A CG  1 
ATOM 388  C CD1 . LEU A 1 51  ? -1.94879  3.92574   35.16983  1.000 47.87221  ? 51  LEU A CD1 1 
ATOM 389  C CD2 . LEU A 1 51  ? -1.87962  3.32504   37.66086  1.000 50.49611  ? 51  LEU A CD2 1 
ATOM 390  N N   . LYS A 1 52  ? -6.91404  1.84244   36.77640  1.000 52.89750  ? 52  LYS A N   1 
ATOM 391  C CA  . LYS A 1 52  ? -8.33184  2.16756   36.94599  1.000 57.03419  ? 52  LYS A CA  1 
ATOM 392  C C   . LYS A 1 52  ? -8.84162  1.76551   38.34124  1.000 64.24138  ? 52  LYS A C   1 
ATOM 393  O O   . LYS A 1 52  ? -9.59773  2.51324   38.98694  1.000 62.45684  ? 52  LYS A O   1 
ATOM 394  C CB  . LYS A 1 52  ? -9.16764  1.50639   35.84566  1.000 56.32999  ? 52  LYS A CB  1 
ATOM 395  N N   . SER A 1 53  ? -8.40024  0.60793   38.84391  1.000 60.95912  ? 53  SER A N   1 
ATOM 396  C CA  . SER A 1 53  ? -8.93458  0.09411   40.09742  1.000 57.96079  ? 53  SER A CA  1 
ATOM 397  C C   . SER A 1 53  ? -8.49626  0.92569   41.30131  1.000 57.89398  ? 53  SER A C   1 
ATOM 398  O O   . SER A 1 53  ? -9.19615  0.92576   42.31539  1.000 57.29234  ? 53  SER A O   1 
ATOM 399  C CB  . SER A 1 53  ? -8.52505  -1.37192  40.24959  1.000 57.14301  ? 53  SER A CB  1 
ATOM 400  O OG  . SER A 1 53  ? -7.11384  -1.49845  40.34588  1.000 56.30026  ? 53  SER A OG  1 
ATOM 401  N N   . GLN A 1 54  ? -7.37191  1.64961   41.19995  1.000 57.62685  ? 54  GLN A N   1 
ATOM 402  C CA  . GLN A 1 54  ? -6.87104  2.51876   42.26070  1.000 53.57294  ? 54  GLN A CA  1 
ATOM 403  C C   . GLN A 1 54  ? -7.55455  3.88797   42.27830  1.000 59.77848  ? 54  GLN A C   1 
ATOM 404  O O   . GLN A 1 54  ? -7.34606  4.65326   43.21753  1.000 61.08745  ? 54  GLN A O   1 
ATOM 405  C CB  . GLN A 1 54  ? -5.36241  2.72854   42.09898  1.000 48.00757  ? 54  GLN A CB  1 
ATOM 406  C CG  . GLN A 1 54  ? -4.59101  1.46907   41.83857  1.000 51.88835  ? 54  GLN A CG  1 
ATOM 407  C CD  . GLN A 1 54  ? -3.09760  1.66534   41.58176  1.000 52.38997  ? 54  GLN A CD  1 
ATOM 408  O OE1 . GLN A 1 54  ? -2.51596  2.68364   41.91968  1.000 51.43764  ? 54  GLN A OE1 1 
ATOM 409  N NE2 . GLN A 1 54  ? -2.50507  0.72058   40.86089  1.000 51.07126  ? 54  GLN A NE2 1 
ATOM 410  N N   . LYS A 1 55  ? -8.34727  4.23097   41.26638  1.000 64.46786  ? 55  LYS A N   1 
ATOM 411  C CA  . LYS A 1 55  ? -8.91752  5.56969   41.19387  1.000 65.46600  ? 55  LYS A CA  1 
ATOM 412  C C   . LYS A 1 55  ? -9.85217  5.79462   42.36439  1.000 64.44566  ? 55  LYS A C   1 
ATOM 413  O O   . LYS A 1 55  ? -10.76990 5.00501   42.59684  1.000 65.96666  ? 55  LYS A O   1 
ATOM 414  C CB  . LYS A 1 55  ? -9.66852  5.77032   39.87197  1.000 72.41630  ? 55  LYS A CB  1 
ATOM 415  N N   . GLY A 1 56  ? -9.63525  6.88742   43.08539  1.000 74.72369  ? 56  GLY A N   1 
ATOM 416  C CA  . GLY A 1 56  ? -10.40656 7.14533   44.28210  1.000 74.76087  ? 56  GLY A CA  1 
ATOM 417  C C   . GLY A 1 56  ? -9.87665  6.44569   45.50555  1.000 75.79386  ? 56  GLY A C   1 
ATOM 418  O O   . GLY A 1 56  ? -10.46328 6.58657   46.57726  1.000 78.55481  ? 56  GLY A O   1 
ATOM 419  N N   . HIS A 1 57  ? -8.79414  5.68373   45.36665  1.000 64.98137  ? 57  HIS A N   1 
ATOM 420  C CA  . HIS A 1 57  ? -8.07432  5.03612   46.44884  1.000 57.50743  ? 57  HIS A CA  1 
ATOM 421  C C   . HIS A 1 57  ? -6.65026  5.54813   46.56087  1.000 57.43013  ? 57  HIS A C   1 
ATOM 422  O O   . HIS A 1 57  ? -6.19934  5.90566   47.64989  1.000 61.71907  ? 57  HIS A O   1 
ATOM 423  C CB  . HIS A 1 57  ? -8.05794  3.51893   46.21433  1.000 59.01574  ? 57  HIS A CB  1 
ATOM 424  C CG  . HIS A 1 57  ? -9.40971  2.88294   46.26605  1.000 65.65975  ? 57  HIS A CG  1 
ATOM 425  N ND1 . HIS A 1 57  ? -10.25625 2.84744   45.17915  1.000 67.61716  ? 57  HIS A ND1 1 
ATOM 426  C CD2 . HIS A 1 57  ? -10.05895 2.24416   47.27030  1.000 71.31407  ? 57  HIS A CD2 1 
ATOM 427  C CE1 . HIS A 1 57  ? -11.37184 2.22100   45.51240  1.000 71.11788  ? 57  HIS A CE1 1 
ATOM 428  N NE2 . HIS A 1 57  ? -11.27836 1.84574   46.77623  1.000 72.42273  ? 57  HIS A NE2 1 
ATOM 429  N N   . ARG A 1 58  ? -5.91802  5.56367   45.46335  1.000 57.49296  ? 58  ARG A N   1 
ATOM 430  C CA  . ARG A 1 58  ? -4.57386  6.10608   45.40070  1.000 54.15214  ? 58  ARG A CA  1 
ATOM 431  C C   . ARG A 1 58  ? -4.63693  7.48812   44.74528  1.000 54.07494  ? 58  ARG A C   1 
ATOM 432  O O   . ARG A 1 58  ? -5.68805  7.92811   44.27120  1.000 53.00723  ? 58  ARG A O   1 
ATOM 433  C CB  . ARG A 1 58  ? -3.66802  5.18672   44.58603  1.000 53.85290  ? 58  ARG A CB  1 
ATOM 434  C CG  . ARG A 1 58  ? -3.75851  3.69757   44.88178  1.000 53.09100  ? 58  ARG A CG  1 
ATOM 435  C CD  . ARG A 1 58  ? -3.08640  3.27777   46.09758  1.000 47.44628  ? 58  ARG A CD  1 
ATOM 436  N NE  . ARG A 1 58  ? -1.66380  3.50532   45.97050  1.000 42.74768  ? 58  ARG A NE  1 
ATOM 437  C CZ  . ARG A 1 58  ? -0.86277  3.57645   47.01908  1.000 48.26840  ? 58  ARG A CZ  1 
ATOM 438  N NH1 . ARG A 1 58  ? -1.30352  3.31914   48.24129  1.000 43.15455  ? 58  ARG A NH1 1 
ATOM 439  N NH2 . ARG A 1 58  ? 0.40197   3.93660   46.84227  1.000 51.71381  ? 58  ARG A NH2 1 
ATOM 440  N N   . LEU A 1 59  ? -3.48293  8.15056   44.67606  1.000 51.43629  ? 59  LEU A N   1 
ATOM 441  C CA  . LEU A 1 59  ? -3.40611  9.55918   44.31394  1.000 53.46800  ? 59  LEU A CA  1 
ATOM 442  C C   . LEU A 1 59  ? -2.78451  9.75878   42.92959  1.000 52.27749  ? 59  LEU A C   1 
ATOM 443  O O   . LEU A 1 59  ? -1.62612  9.39188   42.70703  1.000 51.55424  ? 59  LEU A O   1 
ATOM 444  C CB  . LEU A 1 59  ? -2.60608  10.30172  45.38156  1.000 54.51236  ? 59  LEU A CB  1 
ATOM 445  C CG  . LEU A 1 59  ? -2.47957  11.80066  45.15089  1.000 61.12930  ? 59  LEU A CG  1 
ATOM 446  C CD1 . LEU A 1 59  ? -3.86992  12.45070  45.07980  1.000 54.18599  ? 59  LEU A CD1 1 
ATOM 447  C CD2 . LEU A 1 59  ? -1.60913  12.39315  46.24452  1.000 60.01375  ? 59  LEU A CD2 1 
ATOM 448  N N   . PHE A 1 60  ? -3.52809  10.38979  42.01132  1.000 53.01642  ? 60  PHE A N   1 
ATOM 449  C CA  . PHE A 1 60  ? -2.96167  10.73791  40.71016  1.000 54.71094  ? 60  PHE A CA  1 
ATOM 450  C C   . PHE A 1 60  ? -2.64623  12.23621  40.69384  1.000 55.83609  ? 60  PHE A C   1 
ATOM 451  O O   . PHE A 1 60  ? -3.55075  13.06935  40.57031  1.000 55.94764  ? 60  PHE A O   1 
ATOM 452  C CB  . PHE A 1 60  ? -3.85608  10.37724  39.51933  1.000 57.79504  ? 60  PHE A CB  1 
ATOM 453  C CG  . PHE A 1 60  ? -4.29347  8.92983   39.45380  1.000 56.76163  ? 60  PHE A CG  1 
ATOM 454  C CD1 . PHE A 1 60  ? -4.75728  8.25019   40.55957  1.000 58.49625  ? 60  PHE A CD1 1 
ATOM 455  C CD2 . PHE A 1 60  ? -4.00334  8.19109   38.32357  1.000 57.49326  ? 60  PHE A CD2 1 
ATOM 456  C CE1 . PHE A 1 60  ? -5.12266  6.91982   40.48434  1.000 56.64458  ? 60  PHE A CE1 1 
ATOM 457  C CE2 . PHE A 1 60  ? -4.31924  6.84153   38.25504  1.000 58.31717  ? 60  PHE A CE2 1 
ATOM 458  C CZ  . PHE A 1 60  ? -4.88364  6.21081   39.34467  1.000 59.02798  ? 60  PHE A CZ  1 
ATOM 459  N N   . THR A 1 61  ? -1.35911  12.56400  40.77827  1.000 56.95901  ? 61  THR A N   1 
ATOM 460  C CA  . THR A 1 61  ? -0.87144  13.93103  40.89007  1.000 58.32851  ? 61  THR A CA  1 
ATOM 461  C C   . THR A 1 61  ? -0.73363  14.54550  39.51025  1.000 63.14471  ? 61  THR A C   1 
ATOM 462  O O   . THR A 1 61  ? -0.18810  13.91624  38.60778  1.000 67.74530  ? 61  THR A O   1 
ATOM 463  C CB  . THR A 1 61  ? 0.49310   13.93094  41.56445  1.000 61.66362  ? 61  THR A CB  1 
ATOM 464  O OG1 . THR A 1 61  ? 0.39771   13.19653  42.78490  1.000 60.48162  ? 61  THR A OG1 1 
ATOM 465  C CG2 . THR A 1 61  ? 0.96681   15.33979  41.84651  1.000 62.09175  ? 61  THR A CG2 1 
ATOM 466  N N   . LYS A 1 62  ? -1.18781  15.79233  39.36069  1.000 63.02980  ? 62  LYS A N   1 
ATOM 467  C CA  . LYS A 1 62  ? -1.17644  16.43910  38.05081  1.000 65.46257  ? 62  LYS A CA  1 
ATOM 468  C C   . LYS A 1 62  ? 0.23686   16.67210  37.51006  1.000 68.69169  ? 62  LYS A C   1 
ATOM 469  O O   . LYS A 1 62  ? 0.45827   16.54619  36.30315  1.000 71.47064  ? 62  LYS A O   1 
ATOM 470  C CB  . LYS A 1 62  ? -1.94193  17.75223  38.10857  1.000 68.41907  ? 62  LYS A CB  1 
ATOM 471  C CG  . LYS A 1 62  ? -3.36320  17.65805  37.57330  1.000 72.56587  ? 62  LYS A CG  1 
ATOM 472  C CD  . LYS A 1 62  ? -4.18014  16.63669  38.34217  1.000 72.83096  ? 62  LYS A CD  1 
ATOM 473  C CE  . LYS A 1 62  ? -5.59325  16.49813  37.77277  1.000 77.07039  ? 62  LYS A CE  1 
ATOM 474  N NZ  . LYS A 1 62  ? -6.39245  17.75182  37.93512  1.000 80.85096  ? 62  LYS A NZ  1 
ATOM 475  N N   . SER A 1 63  ? 1.19954   17.04676  38.35579  1.000 64.09875  ? 63  SER A N   1 
ATOM 476  C CA  . SER A 1 63  ? 2.54864   17.25295  37.83509  1.000 66.74383  ? 63  SER A CA  1 
ATOM 477  C C   . SER A 1 63  ? 3.12352   15.95790  37.27714  1.000 72.72942  ? 63  SER A C   1 
ATOM 478  O O   . SER A 1 63  ? 3.77066   15.96096  36.22283  1.000 80.05773  ? 63  SER A O   1 
ATOM 479  C CB  . SER A 1 63  ? 3.47764   17.82832  38.90739  1.000 69.54372  ? 63  SER A CB  1 
ATOM 480  O OG  . SER A 1 63  ? 3.83233   16.88619  39.90105  1.000 69.25267  ? 63  SER A OG  1 
ATOM 481  N N   . THR A 1 64  ? 2.89834   14.83851  37.97076  1.000 73.30210  ? 64  THR A N   1 
ATOM 482  C CA  . THR A 1 64  ? 3.37958   13.54497  37.49284  1.000 69.68575  ? 64  THR A CA  1 
ATOM 483  C C   . THR A 1 64  ? 2.63452   13.10288  36.23729  1.000 69.71810  ? 64  THR A C   1 
ATOM 484  O O   . THR A 1 64  ? 3.22065   12.47435  35.35204  1.000 70.19027  ? 64  THR A O   1 
ATOM 485  C CB  . THR A 1 64  ? 3.23843   12.50281  38.59712  1.000 68.84121  ? 64  THR A CB  1 
ATOM 486  O OG1 . THR A 1 64  ? 3.93741   12.95458  39.76032  1.000 71.62401  ? 64  THR A OG1 1 
ATOM 487  C CG2 . THR A 1 64  ? 3.83663   11.17614  38.16266  1.000 68.38135  ? 64  THR A CG2 1 
ATOM 488  N N   . ILE A 1 65  ? 1.34255   13.40518  36.14420  1.000 65.02032  ? 65  ILE A N   1 
ATOM 489  C CA  . ILE A 1 65  ? 0.61539   13.08960  34.92314  1.000 71.13682  ? 65  ILE A CA  1 
ATOM 490  C C   . ILE A 1 65  ? 1.13548   13.91922  33.75142  1.000 78.55184  ? 65  ILE A C   1 
ATOM 491  O O   . ILE A 1 65  ? 1.27191   13.41455  32.63247  1.000 78.58825  ? 65  ILE A O   1 
ATOM 492  C CB  . ILE A 1 65  ? -0.89634  13.26550  35.14283  1.000 69.62820  ? 65  ILE A CB  1 
ATOM 493  C CG1 . ILE A 1 65  ? -1.38922  12.17596  36.09636  1.000 67.81118  ? 65  ILE A CG1 1 
ATOM 494  C CG2 . ILE A 1 65  ? -1.65379  13.22270  33.82867  1.000 63.59983  ? 65  ILE A CG2 1 
ATOM 495  C CD1 . ILE A 1 65  ? -2.82670  12.32932  36.51218  1.000 63.99876  ? 65  ILE A CD1 1 
ATOM 496  N N   . GLU A 1 66  ? 1.44300   15.19856  33.98291  1.000 82.67801  ? 66  GLU A N   1 
ATOM 497  C CA  . GLU A 1 66  ? 2.07345   15.99817  32.93515  1.000 83.99682  ? 66  GLU A CA  1 
ATOM 498  C C   . GLU A 1 66  ? 3.42166   15.40915  32.54008  1.000 82.57340  ? 66  GLU A C   1 
ATOM 499  O O   . GLU A 1 66  ? 3.72728   15.28081  31.35321  1.000 84.09420  ? 66  GLU A O   1 
ATOM 500  C CB  . GLU A 1 66  ? 2.21271   17.46226  33.38968  1.000 86.99684  ? 66  GLU A CB  1 
ATOM 501  C CG  . GLU A 1 66  ? 0.89902   18.28273  33.28225  1.000 95.22102  ? 66  GLU A CG  1 
ATOM 502  C CD  . GLU A 1 66  ? 0.96966   19.70421  33.89020  1.000 104.02124 ? 66  GLU A CD  1 
ATOM 503  O OE1 . GLU A 1 66  ? 1.95481   20.01899  34.59924  1.000 100.70421 ? 66  GLU A OE1 1 
ATOM 504  O OE2 . GLU A 1 66  ? 0.03190   20.51058  33.64759  1.000 101.55392 ? 66  GLU A OE2 1 
ATOM 505  N N   . TRP A 1 67  ? 4.21692   15.00295  33.52263  1.000 75.81072  ? 67  TRP A N   1 
ATOM 506  C CA  . TRP A 1 67  ? 5.55358   14.48504  33.25715  1.000 75.38976  ? 67  TRP A CA  1 
ATOM 507  C C   . TRP A 1 67  ? 5.52765   13.26414  32.32956  1.000 79.38165  ? 67  TRP A C   1 
ATOM 508  O O   . TRP A 1 67  ? 6.40693   13.10944  31.47525  1.000 79.96997  ? 67  TRP A O   1 
ATOM 509  C CB  . TRP A 1 67  ? 6.19716   14.13221  34.58974  1.000 73.80011  ? 67  TRP A CB  1 
ATOM 510  C CG  . TRP A 1 67  ? 7.56314   13.58937  34.51099  1.000 72.93997  ? 67  TRP A CG  1 
ATOM 511  C CD1 . TRP A 1 67  ? 8.72158   14.28573  34.50767  1.000 68.05670  ? 67  TRP A CD1 1 
ATOM 512  C CD2 . TRP A 1 67  ? 7.91575   12.21300  34.34176  1.000 74.31562  ? 67  TRP A CD2 1 
ATOM 513  N NE1 . TRP A 1 67  ? 9.78945   13.42798  34.41466  1.000 67.89706  ? 67  TRP A NE1 1 
ATOM 514  C CE2 . TRP A 1 67  ? 9.31976   12.14783  34.29167  1.000 73.44313  ? 67  TRP A CE2 1 
ATOM 515  C CE3 . TRP A 1 67  ? 7.17908   11.02732  34.25157  1.000 73.91938  ? 67  TRP A CE3 1 
ATOM 516  C CZ2 . TRP A 1 67  ? 10.00903  10.94153  34.15384  1.000 72.74951  ? 67  TRP A CZ2 1 
ATOM 517  C CZ3 . TRP A 1 67  ? 7.86265   9.83197   34.11551  1.000 77.32273  ? 67  TRP A CZ3 1 
ATOM 518  C CH2 . TRP A 1 67  ? 9.26462   9.79889   34.06760  1.000 74.84353  ? 67  TRP A CH2 1 
ATOM 519  N N   . TRP A 1 68  ? 4.55951   12.35505  32.51557  1.000 79.33846  ? 68  TRP A N   1 
ATOM 520  C CA  . TRP A 1 68  ? 4.42634   11.21236  31.61309  1.000 78.25241  ? 68  TRP A CA  1 
ATOM 521  C C   . TRP A 1 68  ? 3.97442   11.62586  30.22451  1.000 80.19059  ? 68  TRP A C   1 
ATOM 522  O O   . TRP A 1 68  ? 4.12092   10.84417  29.28037  1.000 85.55214  ? 68  TRP A O   1 
ATOM 523  C CB  . TRP A 1 68  ? 3.43493   10.16430  32.14771  1.000 76.73544  ? 68  TRP A CB  1 
ATOM 524  C CG  . TRP A 1 68  ? 3.96648   9.28049   33.23610  1.000 76.26864  ? 68  TRP A CG  1 
ATOM 525  C CD1 . TRP A 1 68  ? 3.70739   9.36493   34.58393  1.000 74.63852  ? 68  TRP A CD1 1 
ATOM 526  C CD2 . TRP A 1 68  ? 4.85650   8.17405   33.07133  1.000 78.58281  ? 68  TRP A CD2 1 
ATOM 527  N NE1 . TRP A 1 68  ? 4.38414   8.37612   35.26199  1.000 70.38401  ? 68  TRP A NE1 1 
ATOM 528  C CE2 . TRP A 1 68  ? 5.09980   7.63430   34.35848  1.000 74.85953  ? 68  TRP A CE2 1 
ATOM 529  C CE3 . TRP A 1 68  ? 5.47016   7.58137   31.96053  1.000 77.92688  ? 68  TRP A CE3 1 
ATOM 530  C CZ2 . TRP A 1 68  ? 5.92688   6.53697   34.55909  1.000 72.54883  ? 68  TRP A CZ2 1 
ATOM 531  C CZ3 . TRP A 1 68  ? 6.29386   6.49817   32.16250  1.000 78.22883  ? 68  TRP A CZ3 1 
ATOM 532  C CH2 . TRP A 1 68  ? 6.51471   5.98310   33.45561  1.000 77.78497  ? 68  TRP A CH2 1 
ATOM 533  N N   . LYS A 1 69  ? 3.39705   12.81295  30.08302  1.000 78.33965  ? 69  LYS A N   1 
ATOM 534  C CA  . LYS A 1 69  ? 2.98532   13.26630  28.76326  1.000 83.06045  ? 69  LYS A CA  1 
ATOM 535  C C   . LYS A 1 69  ? 4.18738   13.69153  27.92164  1.000 86.50317  ? 69  LYS A C   1 
ATOM 536  O O   . LYS A 1 69  ? 4.14525   13.58876  26.68962  1.000 85.25032  ? 69  LYS A O   1 
ATOM 537  C CB  . LYS A 1 69  ? 1.97076   14.40671  28.90658  1.000 82.62676  ? 69  LYS A CB  1 
ATOM 538  C CG  . LYS A 1 69  ? 0.66958   13.96793  29.55533  1.000 78.86135  ? 69  LYS A CG  1 
ATOM 539  C CD  . LYS A 1 69  ? -0.35835  15.07692  29.63203  1.000 78.23383  ? 69  LYS A CD  1 
ATOM 540  C CE  . LYS A 1 69  ? -1.63308  14.58050  30.32791  1.000 76.21899  ? 69  LYS A CE  1 
ATOM 541  N NZ  . LYS A 1 69  ? -2.72534  15.60464  30.37278  1.000 80.37527  ? 69  LYS A NZ  1 
ATOM 542  N N   . ASN A 1 70  ? 5.26420   14.15268  28.57190  1.000 83.79403  ? 70  ASN A N   1 
ATOM 543  C CA  . ASN A 1 70  ? 6.49449   14.59203  27.92729  1.000 82.97126  ? 70  ASN A CA  1 
ATOM 544  C C   . ASN A 1 70  ? 7.46765   13.45521  27.66414  1.000 88.10869  ? 70  ASN A C   1 
ATOM 545  O O   . ASN A 1 70  ? 8.53664   13.69612  27.09289  1.000 91.53231  ? 70  ASN A O   1 
ATOM 546  C CB  . ASN A 1 70  ? 7.21235   15.62900  28.79162  1.000 79.53542  ? 70  ASN A CB  1 
ATOM 547  C CG  . ASN A 1 70  ? 6.37607   16.86198  29.03540  1.000 89.37891  ? 70  ASN A CG  1 
ATOM 548  O OD1 . ASN A 1 70  ? 5.65283   17.33258  28.15172  1.000 91.70761  ? 70  ASN A OD1 1 
ATOM 549  N ND2 . ASN A 1 70  ? 6.47113   17.40283  30.24937  1.000 92.74038  ? 70  ASN A ND2 1 
ATOM 550  N N   . GLN A 1 71  ? 7.15318   12.24645  28.10768  1.000 87.34215  ? 71  GLN A N   1 
ATOM 551  C CA  . GLN A 1 71  ? 8.01361   11.09018  27.92566  1.000 89.36534  ? 71  GLN A CA  1 
ATOM 552  C C   . GLN A 1 71  ? 7.70835   10.40732  26.59574  1.000 92.52304  ? 71  GLN A C   1 
ATOM 553  O O   . GLN A 1 71  ? 6.59819   10.49798  26.07242  1.000 91.75264  ? 71  GLN A O   1 
ATOM 554  C CB  . GLN A 1 71  ? 7.83034   10.12905  29.09478  1.000 86.61536  ? 71  GLN A CB  1 
ATOM 555  C CG  . GLN A 1 71  ? 8.27268   10.77040  30.35718  1.000 83.76587  ? 71  GLN A CG  1 
ATOM 556  C CD  . GLN A 1 71  ? 9.75255   11.04482  30.33704  1.000 86.25548  ? 71  GLN A CD  1 
ATOM 557  O OE1 . GLN A 1 71  ? 10.54962  10.16890  29.99803  1.000 88.64060  ? 71  GLN A OE1 1 
ATOM 558  N NE2 . GLN A 1 71  ? 10.13120  12.28177  30.63973  1.000 87.31663  ? 71  GLN A NE2 1 
ATOM 559  N N   . SER A 1 72  ? 8.71157   9.71122   26.05278  1.000 91.96809  ? 72  SER A N   1 
ATOM 560  C CA  . SER A 1 72  ? 8.59810   9.16034   24.70630  1.000 95.06973  ? 72  SER A CA  1 
ATOM 561  C C   . SER A 1 72  ? 7.50337   8.10172   24.64948  1.000 94.95173  ? 72  SER A C   1 
ATOM 562  O O   . SER A 1 72  ? 7.13795   7.52268   25.66948  1.000 97.45822  ? 72  SER A O   1 
ATOM 563  C CB  . SER A 1 72  ? 9.91766   8.53652   24.26981  1.000 94.17203  ? 72  SER A CB  1 
ATOM 564  O OG  . SER A 1 72  ? 10.17805  7.36040   25.01183  1.000 93.87677  ? 72  SER A OG  1 
ATOM 565  N N   . PRO A 1 73  ? 6.95622   7.82911   23.46677  1.000 97.54238  ? 73  PRO A N   1 
ATOM 566  C CA  . PRO A 1 73  ? 5.98053   6.73177   23.36558  1.000 96.02139  ? 73  PRO A CA  1 
ATOM 567  C C   . PRO A 1 73  ? 6.55062   5.36899   23.72592  1.000 94.70529  ? 73  PRO A C   1 
ATOM 568  O O   . PRO A 1 73  ? 5.76859   4.44467   23.96539  1.000 93.68253  ? 73  PRO A O   1 
ATOM 569  C CB  . PRO A 1 73  ? 5.52492   6.79222   21.90122  1.000 100.33696 ? 73  PRO A CB  1 
ATOM 570  C CG  . PRO A 1 73  ? 5.74903   8.22522   21.50761  1.000 102.40208 ? 73  PRO A CG  1 
ATOM 571  C CD  . PRO A 1 73  ? 7.00310   8.64312   22.24067  1.000 99.32760  ? 73  PRO A CD  1 
ATOM 572  N N   . GLU A 1 74  ? 7.87333   5.19294   23.75996  1.000 91.11073  ? 74  GLU A N   1 
ATOM 573  C CA  . GLU A 1 74  ? 8.41361   3.93352   24.27293  1.000 95.03380  ? 74  GLU A CA  1 
ATOM 574  C C   . GLU A 1 74  ? 8.32270   3.87934   25.80097  1.000 94.70507  ? 74  GLU A C   1 
ATOM 575  O O   . GLU A 1 74  ? 7.84126   2.89126   26.37038  1.000 91.83172  ? 74  GLU A O   1 
ATOM 576  C CB  . GLU A 1 74  ? 9.85667   3.73415   23.79486  1.000 92.07550  ? 74  GLU A CB  1 
ATOM 577  N N   . ALA A 1 75  ? 8.76841   4.94200   26.48281  1.000 94.41843  ? 75  ALA A N   1 
ATOM 578  C CA  . ALA A 1 75  ? 8.63353   5.01327   27.93683  1.000 89.10805  ? 75  ALA A CA  1 
ATOM 579  C C   . ALA A 1 75  ? 7.16698   5.00180   28.35468  1.000 87.84753  ? 75  ALA A C   1 
ATOM 580  O O   . ALA A 1 75  ? 6.77186   4.28057   29.27623  1.000 86.76888  ? 75  ALA A O   1 
ATOM 581  C CB  . ALA A 1 75  ? 9.33411   6.26583   28.46303  1.000 85.07087  ? 75  ALA A CB  1 
ATOM 582  N N   . ARG A 1 76  ? 6.34299   5.78855   27.66777  1.000 88.65883  ? 76  ARG A N   1 
ATOM 583  C CA  . ARG A 1 76  ? 4.91161   5.85422   27.93408  1.000 86.14122  ? 76  ARG A CA  1 
ATOM 584  C C   . ARG A 1 76  ? 4.21698   4.52196   27.68971  1.000 82.41755  ? 76  ARG A C   1 
ATOM 585  O O   . ARG A 1 76  ? 3.08237   4.32476   28.13716  1.000 80.92110  ? 76  ARG A O   1 
ATOM 586  C CB  . ARG A 1 76  ? 4.30709   6.94585   27.05098  1.000 87.76199  ? 76  ARG A CB  1 
ATOM 587  C CG  . ARG A 1 76  ? 2.85791   7.24675   27.25149  1.000 87.24124  ? 76  ARG A CG  1 
ATOM 588  C CD  . ARG A 1 76  ? 2.40951   8.26164   26.21839  1.000 91.76314  ? 76  ARG A CD  1 
ATOM 589  N NE  . ARG A 1 76  ? 3.14068   9.51467   26.35054  1.000 94.93527  ? 76  ARG A NE  1 
ATOM 590  C CZ  . ARG A 1 76  ? 3.95864   10.01688  25.43228  1.000 98.77031  ? 76  ARG A CZ  1 
ATOM 591  N NH1 . ARG A 1 76  ? 4.17567   9.40130   24.27692  1.000 98.45100  ? 76  ARG A NH1 1 
ATOM 592  N NH2 . ARG A 1 76  ? 4.58275   11.16668  25.68124  1.000 95.60175  ? 76  ARG A NH2 1 
ATOM 593  N N   . LYS A 1 77  ? 4.85817   3.60854   26.96922  1.000 83.53734  ? 77  LYS A N   1 
ATOM 594  C CA  . LYS A 1 77  ? 4.24294   2.31033   26.73576  1.000 85.13191  ? 77  LYS A CA  1 
ATOM 595  C C   . LYS A 1 77  ? 4.13739   1.50478   28.01262  1.000 81.96982  ? 77  LYS A C   1 
ATOM 596  O O   . LYS A 1 77  ? 3.36922   0.53977   28.05184  1.000 80.48369  ? 77  LYS A O   1 
ATOM 597  C CB  . LYS A 1 77  ? 5.03041   1.52137   25.69042  1.000 91.11603  ? 77  LYS A CB  1 
ATOM 598  N N   . ASN A 1 78  ? 4.89431   1.88650   29.05083  1.000 82.94819  ? 78  ASN A N   1 
ATOM 599  C CA  . ASN A 1 78  ? 4.80849   1.21575   30.34769  1.000 79.96764  ? 78  ASN A CA  1 
ATOM 600  C C   . ASN A 1 78  ? 3.40273   1.31606   30.94536  1.000 78.36879  ? 78  ASN A C   1 
ATOM 601  O O   . ASN A 1 78  ? 2.91277   0.36966   31.57332  1.000 77.32039  ? 78  ASN A O   1 
ATOM 602  C CB  . ASN A 1 78  ? 5.82428   1.81206   31.33652  1.000 78.16927  ? 78  ASN A CB  1 
ATOM 603  C CG  . ASN A 1 78  ? 7.28254   1.51201   30.97325  1.000 78.50171  ? 78  ASN A CG  1 
ATOM 604  O OD1 . ASN A 1 78  ? 7.58880   0.48032   30.38963  1.000 78.92184  ? 78  ASN A OD1 1 
ATOM 605  N ND2 . ASN A 1 78  ? 8.19190   2.37819   31.41181  1.000 78.47364  ? 78  ASN A ND2 1 
ATOM 606  N N   . ILE A 1 79  ? 2.73649   2.45468   30.77147  1.000 76.33699  ? 79  ILE A N   1 
ATOM 607  C CA  . ILE A 1 79  ? 1.55059   2.74929   31.55834  1.000 72.74409  ? 79  ILE A CA  1 
ATOM 608  C C   . ILE A 1 79  ? 0.26558   2.33898   30.84137  1.000 70.62180  ? 79  ILE A C   1 
ATOM 609  O O   . ILE A 1 79  ? -0.82967  2.68454   31.29243  1.000 68.66958  ? 79  ILE A O   1 
ATOM 610  C CB  . ILE A 1 79  ? 1.52830   4.23399   31.96830  1.000 72.54311  ? 79  ILE A CB  1 
ATOM 611  C CG1 . ILE A 1 79  ? 1.30604   5.14209   30.77738  1.000 75.95116  ? 79  ILE A CG1 1 
ATOM 612  C CG2 . ILE A 1 79  ? 2.86253   4.64198   32.57543  1.000 74.29442  ? 79  ILE A CG2 1 
ATOM 613  C CD1 . ILE A 1 79  ? 1.14154   6.57988   31.17060  1.000 74.63903  ? 79  ILE A CD1 1 
ATOM 614  N N   . ALA A 1 80  ? 0.36654   1.59105   29.76165  1.000 70.63888  ? 80  ALA A N   1 
ATOM 615  C CA  . ALA A 1 80  ? -0.87002  1.20420   29.10004  1.000 68.13040  ? 80  ALA A CA  1 
ATOM 616  C C   . ALA A 1 80  ? -1.48113  -0.04727  29.74400  1.000 62.30055  ? 80  ALA A C   1 
ATOM 617  O O   . ALA A 1 80  ? -0.76030  -0.94037  30.20190  1.000 60.84207  ? 80  ALA A O   1 
ATOM 618  C CB  . ALA A 1 80  ? -0.61509  0.95890   27.61787  1.000 68.10328  ? 80  ALA A CB  1 
ATOM 619  N N   . PRO A 1 81  ? -2.80788  -0.13938  29.76672  1.000 56.99460  ? 81  PRO A N   1 
ATOM 620  C CA  . PRO A 1 81  ? -3.46222  -1.30822  30.36492  1.000 55.70469  ? 81  PRO A CA  1 
ATOM 621  C C   . PRO A 1 81  ? -3.01321  -2.61419  29.73227  1.000 64.28134  ? 81  PRO A C   1 
ATOM 622  O O   . PRO A 1 81  ? -2.81087  -2.70865  28.51788  1.000 73.93641  ? 81  PRO A O   1 
ATOM 623  C CB  . PRO A 1 81  ? -4.95044  -1.04900  30.10277  1.000 54.69720  ? 81  PRO A CB  1 
ATOM 624  C CG  . PRO A 1 81  ? -5.06114  0.42248   30.03092  1.000 56.53474  ? 81  PRO A CG  1 
ATOM 625  C CD  . PRO A 1 81  ? -3.77692  0.89514   29.37915  1.000 62.15186  ? 81  PRO A CD  1 
ATOM 626  N N   . SER A 1 82  ? -2.90042  -3.63403  30.57412  1.000 60.54990  ? 82  SER A N   1 
ATOM 627  C CA  . SER A 1 82  ? -2.32473  -4.92270  30.23368  1.000 62.00289  ? 82  SER A CA  1 
ATOM 628  C C   . SER A 1 82  ? -3.21284  -6.03775  30.75697  1.000 74.09360  ? 82  SER A C   1 
ATOM 629  O O   . SER A 1 82  ? -4.00771  -5.84093  31.67931  1.000 80.93086  ? 82  SER A O   1 
ATOM 630  C CB  . SER A 1 82  ? -0.93225  -5.06301  30.82836  1.000 64.72942  ? 82  SER A CB  1 
ATOM 631  O OG  . SER A 1 82  ? -0.47649  -6.38538  30.73936  1.000 67.78140  ? 82  SER A OG  1 
ATOM 632  N N   . ASP A 1 83  ? -3.07067  -7.22710  30.16302  1.000 83.82167  ? 83  ASP A N   1 
ATOM 633  C CA  . ASP A 1 83  ? -3.74343  -8.40817  30.69558  1.000 84.14398  ? 83  ASP A CA  1 
ATOM 634  C C   . ASP A 1 83  ? -2.98990  -9.04235  31.86339  1.000 82.56233  ? 83  ASP A C   1 
ATOM 635  O O   . ASP A 1 83  ? -3.49951  -9.98311  32.47981  1.000 83.13871  ? 83  ASP A O   1 
ATOM 636  C CB  . ASP A 1 83  ? -3.97087  -9.42623  29.58015  1.000 89.19029  ? 83  ASP A CB  1 
ATOM 637  C CG  . ASP A 1 83  ? -5.12108  -9.04071  28.68543  1.000 98.22270  ? 83  ASP A CG  1 
ATOM 638  O OD1 . ASP A 1 83  ? -6.00327  -8.29217  29.16277  1.000 96.91688  ? 83  ASP A OD1 1 
ATOM 639  O OD2 . ASP A 1 83  ? -5.16506  -9.50707  27.52469  1.000 111.89169 ? 83  ASP A OD2 1 
ATOM 640  N N   . GLU A 1 84  ? -1.80429  -8.53012  32.18303  1.000 76.33834  ? 84  GLU A N   1 
ATOM 641  C CA  . GLU A 1 84  ? -0.98532  -8.96365  33.30213  1.000 72.60149  ? 84  GLU A CA  1 
ATOM 642  C C   . GLU A 1 84  ? -1.14936  -8.06478  34.52982  1.000 65.10509  ? 84  GLU A C   1 
ATOM 643  O O   . GLU A 1 84  ? -0.27511  -8.05810  35.40815  1.000 61.14978  ? 84  GLU A O   1 
ATOM 644  C CB  . GLU A 1 84  ? 0.48461   -9.01528  32.86483  1.000 70.72537  ? 84  GLU A CB  1 
ATOM 645  N N   . ASP A 1 85  ? -2.24935  -7.31519  34.60942  1.000 66.34742  ? 85  ASP A N   1 
ATOM 646  C CA  . ASP A 1 85  ? -2.44973  -6.34854  35.69225  1.000 65.73252  ? 85  ASP A CA  1 
ATOM 647  C C   . ASP A 1 85  ? -3.07001  -6.95981  36.95785  1.000 62.39598  ? 85  ASP A C   1 
ATOM 648  O O   . ASP A 1 85  ? -3.97861  -7.79456  36.89779  1.000 65.52683  ? 85  ASP A O   1 
ATOM 649  C CB  . ASP A 1 85  ? -3.34957  -5.19991  35.23154  1.000 68.10393  ? 85  ASP A CB  1 
ATOM 650  C CG  . ASP A 1 85  ? -2.67547  -4.25246  34.26219  1.000 67.16719  ? 85  ASP A CG  1 
ATOM 651  O OD1 . ASP A 1 85  ? -1.42523  -4.21195  34.19796  1.000 66.54730  ? 85  ASP A OD1 1 
ATOM 652  O OD2 . ASP A 1 85  ? -3.42565  -3.47934  33.63002  1.000 67.83818  ? 85  ASP A OD2 1 
ATOM 653  N N   . VAL A 1 86  ? -2.62048  -6.48377  38.11090  1.000 56.35989  ? 86  VAL A N   1 
ATOM 654  C CA  . VAL A 1 86  ? -3.09459  -6.99019  39.39202  1.000 59.82900  ? 86  VAL A CA  1 
ATOM 655  C C   . VAL A 1 86  ? -3.56894  -5.83872  40.26677  1.000 53.82772  ? 86  VAL A C   1 
ATOM 656  O O   . VAL A 1 86  ? -3.02413  -4.73224  40.21337  1.000 54.71561  ? 86  VAL A O   1 
ATOM 657  C CB  . VAL A 1 86  ? -1.99064  -7.78957  40.10647  1.000 60.69742  ? 86  VAL A CB  1 
ATOM 658  C CG1 . VAL A 1 86  ? -1.76316  -9.13303  39.40775  1.000 52.79357  ? 86  VAL A CG1 1 
ATOM 659  C CG2 . VAL A 1 86  ? -0.70416  -6.93896  40.14816  1.000 53.16055  ? 86  VAL A CG2 1 
ATOM 660  N N   . SER A 1 87  ? -4.59529  -6.10253  41.07370  1.000 52.30847  ? 87  SER A N   1 
ATOM 661  C CA  . SER A 1 87  ? -5.01725  -5.13663  42.07591  1.000 48.92125  ? 87  SER A CA  1 
ATOM 662  C C   . SER A 1 87  ? -3.89649  -4.95692  43.07842  1.000 48.38599  ? 87  SER A C   1 
ATOM 663  O O   . SER A 1 87  ? -2.93180  -5.71837  43.09367  1.000 52.81463  ? 87  SER A O   1 
ATOM 664  C CB  . SER A 1 87  ? -6.27784  -5.58874  42.77745  1.000 50.34311  ? 87  SER A CB  1 
ATOM 665  O OG  . SER A 1 87  ? -5.98102  -6.69811  43.57062  1.000 55.52837  ? 87  SER A OG  1 
ATOM 666  N N   . THR A 1 88  ? -3.97302  -3.88208  43.85974  1.000 46.63114  ? 88  THR A N   1 
ATOM 667  C CA  . THR A 1 88  ? -2.82107  -3.54371  44.69386  1.000 46.72539  ? 88  THR A CA  1 
ATOM 668  C C   . THR A 1 88  ? -2.64057  -4.54671  45.83074  1.000 49.36487  ? 88  THR A C   1 
ATOM 669  O O   . THR A 1 88  ? -1.50131  -4.81001  46.23543  1.000 46.91192  ? 88  THR A O   1 
ATOM 670  C CB  . THR A 1 88  ? -2.91356  -2.09649  45.24346  1.000 54.63884  ? 88  THR A CB  1 
ATOM 671  O OG1 . THR A 1 88  ? -4.09425  -1.89295  46.06431  1.000 51.78614  ? 88  THR A OG1 1 
ATOM 672  C CG2 . THR A 1 88  ? -2.85357  -1.07105  44.10124  1.000 48.17681  ? 88  THR A CG2 1 
ATOM 673  N N   . ILE A 1 89  ? -3.73967  -5.11614  46.35386  1.000 50.61642  ? 89  ILE A N   1 
ATOM 674  C CA  . ILE A 1 89  ? -3.62103  -6.22282  47.30296  1.000 49.72596  ? 89  ILE A CA  1 
ATOM 675  C C   . ILE A 1 89  ? -2.92111  -7.39948  46.65582  1.000 52.58689  ? 89  ILE A C   1 
ATOM 676  O O   . ILE A 1 89  ? -1.90775  -7.89295  47.16595  1.000 53.23649  ? 89  ILE A O   1 
ATOM 677  C CB  . ILE A 1 89  ? -4.99643  -6.62309  47.88063  1.000 48.02573  ? 89  ILE A CB  1 
ATOM 678  C CG1 . ILE A 1 89  ? -5.27286  -5.83108  49.15885  1.000 50.87752  ? 89  ILE A CG1 1 
ATOM 679  C CG2 . ILE A 1 89  ? -5.06384  -8.10259  48.16945  1.000 50.57937  ? 89  ILE A CG2 1 
ATOM 680  C CD1 . ILE A 1 89  ? -4.22022  -6.08968  50.24488  1.000 46.57951  ? 89  ILE A CD1 1 
ATOM 681  N N   . ASP A 1 90  ? -3.42881  -7.83614  45.50116  1.000 60.66662  ? 90  ASP A N   1 
ATOM 682  C CA  . ASP A 1 90  ? -2.82867  -8.94951  44.78958  1.000 61.19779  ? 90  ASP A CA  1 
ATOM 683  C C   . ASP A 1 90  ? -1.33948  -8.71135  44.57467  1.000 60.93904  ? 90  ASP A C   1 
ATOM 684  O O   . ASP A 1 90  ? -0.51832  -9.60148  44.81183  1.000 61.66644  ? 90  ASP A O   1 
ATOM 685  C CB  . ASP A 1 90  ? -3.57969  -9.13451  43.47414  1.000 63.37599  ? 90  ASP A CB  1 
ATOM 686  C CG  . ASP A 1 90  ? -3.12729  -10.36253 42.67038  1.000 71.94693  ? 90  ASP A CG  1 
ATOM 687  O OD1 . ASP A 1 90  ? -2.16904  -11.08664 43.06807  1.000 72.21548  ? 90  ASP A OD1 1 
ATOM 688  O OD2 . ASP A 1 90  ? -3.76164  -10.59286 41.60939  1.000 73.55027  ? 90  ASP A OD2 1 
ATOM 689  N N   . GLY A 1 91  ? -0.96649  -7.49720  44.18165  1.000 52.40724  ? 91  GLY A N   1 
ATOM 690  C CA  . GLY A 1 91  ? 0.43294   -7.20786  43.96221  1.000 47.58692  ? 91  GLY A CA  1 
ATOM 691  C C   . GLY A 1 91  ? 1.28025   -7.40634  45.19992  1.000 49.82306  ? 91  GLY A C   1 
ATOM 692  O O   . GLY A 1 91  ? 2.39909   -7.91190  45.11517  1.000 49.58164  ? 91  GLY A O   1 
ATOM 693  N N   . ILE A 1 92  ? 0.78386   -6.97896  46.36721  1.000 50.63781  ? 92  ILE A N   1 
ATOM 694  C CA  . ILE A 1 92  ? 1.64297   -7.06510  47.54833  1.000 49.86762  ? 92  ILE A CA  1 
ATOM 695  C C   . ILE A 1 92  ? 1.80205   -8.52434  47.97266  1.000 51.49799  ? 92  ILE A C   1 
ATOM 696  O O   . ILE A 1 92  ? 2.87646   -8.93388  48.42853  1.000 52.16719  ? 92  ILE A O   1 
ATOM 697  C CB  . ILE A 1 92  ? 1.13397   -6.16467  48.69735  1.000 47.38643  ? 92  ILE A CB  1 
ATOM 698  C CG1 . ILE A 1 92  ? 2.27443   -5.85162  49.65742  1.000 45.43020  ? 92  ILE A CG1 1 
ATOM 699  C CG2 . ILE A 1 92  ? 0.04505   -6.84203  49.52813  1.000 47.74735  ? 92  ILE A CG2 1 
ATOM 700  C CD1 . ILE A 1 92  ? 3.36199   -5.02045  49.04883  1.000 43.66196  ? 92  ILE A CD1 1 
ATOM 701  N N   . ALA A 1 93  ? 0.76011   -9.33922  47.80349  1.000 50.22087  ? 93  ALA A N   1 
ATOM 702  C CA  . ALA A 1 93  ? 0.91900   -10.77056 48.01326  1.000 51.38394  ? 93  ALA A CA  1 
ATOM 703  C C   . ALA A 1 93  ? 2.01125   -11.33766 47.10564  1.000 53.31266  ? 93  ALA A C   1 
ATOM 704  O O   . ALA A 1 93  ? 2.88756   -12.07448 47.56791  1.000 51.87168  ? 93  ALA A O   1 
ATOM 705  C CB  . ALA A 1 93  ? -0.42093  -11.47867 47.79153  1.000 50.65365  ? 93  ALA A CB  1 
ATOM 706  N N   . LYS A 1 94  ? 1.99971   -10.96455 45.81740  1.000 55.24884  ? 94  LYS A N   1 
ATOM 707  C CA  . LYS A 1 94  ? 3.06904   -11.34911 44.89453  1.000 50.72205  ? 94  LYS A CA  1 
ATOM 708  C C   . LYS A 1 94  ? 4.41793   -10.78132 45.32350  1.000 48.50401  ? 94  LYS A C   1 
ATOM 709  O O   . LYS A 1 94  ? 5.45177   -11.43564 45.16885  1.000 48.02685  ? 94  LYS A O   1 
ATOM 710  C CB  . LYS A 1 94  ? 2.72788   -10.88393 43.48397  1.000 52.29338  ? 94  LYS A CB  1 
ATOM 711  C CG  . LYS A 1 94  ? 1.57444   -11.59930 42.86077  1.000 56.90450  ? 94  LYS A CG  1 
ATOM 712  C CD  . LYS A 1 94  ? 1.37803   -11.13474 41.44458  1.000 60.01043  ? 94  LYS A CD  1 
ATOM 713  C CE  . LYS A 1 94  ? 0.31916   -11.96742 40.73218  1.000 70.63996  ? 94  LYS A CE  1 
ATOM 714  N NZ  . LYS A 1 94  ? 0.77465   -13.37454 40.42855  1.000 71.12576  ? 94  LYS A NZ  1 
ATOM 715  N N   . PHE A 1 95  ? 4.44031   -9.55403  45.83568  1.000 49.76423  ? 95  PHE A N   1 
ATOM 716  C CA  . PHE A 1 95  ? 5.67340   -9.05812  46.43150  1.000 50.71676  ? 95  PHE A CA  1 
ATOM 717  C C   . PHE A 1 95  ? 6.14482   -9.98245  47.55071  1.000 52.19982  ? 95  PHE A C   1 
ATOM 718  O O   . PHE A 1 95  ? 7.31773   -10.36198 47.61099  1.000 49.85574  ? 95  PHE A O   1 
ATOM 719  C CB  . PHE A 1 95  ? 5.48043   -7.63748  46.96408  1.000 45.67855  ? 95  PHE A CB  1 
ATOM 720  C CG  . PHE A 1 95  ? 6.70931   -7.08552  47.63261  1.000 45.39704  ? 95  PHE A CG  1 
ATOM 721  C CD1 . PHE A 1 95  ? 7.74752   -6.54951  46.86987  1.000 40.50313  ? 95  PHE A CD1 1 
ATOM 722  C CD2 . PHE A 1 95  ? 6.84367   -7.14123  49.03827  1.000 43.98732  ? 95  PHE A CD2 1 
ATOM 723  C CE1 . PHE A 1 95  ? 8.89945   -6.05363  47.48860  1.000 42.56155  ? 95  PHE A CE1 1 
ATOM 724  C CE2 . PHE A 1 95  ? 7.98788   -6.65329  49.67585  1.000 41.44374  ? 95  PHE A CE2 1 
ATOM 725  C CZ  . PHE A 1 95  ? 9.02639   -6.11697  48.90722  1.000 43.22432  ? 95  PHE A CZ  1 
ATOM 726  N N   . ASN A 1 96  ? 5.23813   -10.34828 48.46150  1.000 56.21398  ? 96  ASN A N   1 
ATOM 727  C CA  . ASN A 1 96  ? 5.66707   -11.11157 49.62473  1.000 55.98511  ? 96  ASN A CA  1 
ATOM 728  C C   . ASN A 1 96  ? 6.07289   -12.53356 49.24166  1.000 58.25128  ? 96  ASN A C   1 
ATOM 729  O O   . ASN A 1 96  ? 7.00551   -13.09499 49.82761  1.000 58.37168  ? 96  ASN A O   1 
ATOM 730  C CB  . ASN A 1 96  ? 4.58448   -11.10732 50.69685  1.000 56.56246  ? 96  ASN A CB  1 
ATOM 731  C CG  . ASN A 1 96  ? 4.45984   -9.76969  51.39764  1.000 59.12844  ? 96  ASN A CG  1 
ATOM 732  O OD1 . ASN A 1 96  ? 5.40031   -8.96731  51.42055  1.000 60.25732  ? 96  ASN A OD1 1 
ATOM 733  N ND2 . ASN A 1 96  ? 3.33670   -9.57321  52.08385  1.000 60.55349  ? 96  ASN A ND2 1 
ATOM 734  N N   . ASP A 1 97  ? 5.40037   -13.12360 48.24991  1.000 61.58511  ? 97  ASP A N   1 
ATOM 735  C CA  . ASP A 1 97  ? 5.85792   -14.39516 47.70795  1.000 61.72400  ? 97  ASP A CA  1 
ATOM 736  C C   . ASP A 1 97  ? 7.33046   -14.33768 47.31659  1.000 61.88097  ? 97  ASP A C   1 
ATOM 737  O O   . ASP A 1 97  ? 8.11149   -15.21564 47.70818  1.000 64.31604  ? 97  ASP A O   1 
ATOM 738  C CB  . ASP A 1 97  ? 5.01731   -14.80207 46.50521  1.000 63.58973  ? 97  ASP A CB  1 
ATOM 739  C CG  . ASP A 1 97  ? 3.62499   -15.20140 46.88291  1.000 65.72123  ? 97  ASP A CG  1 
ATOM 740  O OD1 . ASP A 1 97  ? 3.42999   -15.59446 48.05543  1.000 71.26697  ? 97  ASP A OD1 1 
ATOM 741  O OD2 . ASP A 1 97  ? 2.73303   -15.16153 46.00052  1.000 67.88087  ? 97  ASP A OD2 1 
ATOM 742  N N   . TYR A 1 98  ? 7.74006   -13.30169 46.55313  1.000 54.80199  ? 98  TYR A N   1 
ATOM 743  C CA  . TYR A 1 98  ? 9.11195   -13.28685 46.05751  1.000 49.70534  ? 98  TYR A CA  1 
ATOM 744  C C   . TYR A 1 98  ? 10.10942  -13.07423 47.17896  1.000 53.93697  ? 98  TYR A C   1 
ATOM 745  O O   . TYR A 1 98  ? 11.12859  -13.76911 47.23078  1.000 55.92690  ? 98  TYR A O   1 
ATOM 746  C CB  . TYR A 1 98  ? 9.24204   -12.31938 44.86968  1.000 52.23554  ? 98  TYR A CB  1 
ATOM 747  C CG  . TYR A 1 98  ? 10.63718  -11.87171 44.35930  1.000 58.04286  ? 98  TYR A CG  1 
ATOM 748  C CD1 . TYR A 1 98  ? 11.80701  -12.02024 45.09211  1.000 60.77352  ? 98  TYR A CD1 1 
ATOM 749  C CD2 . TYR A 1 98  ? 10.81516  -11.71543 42.99362  1.000 54.54125  ? 98  TYR A CD2 1 
ATOM 750  C CE1 . TYR A 1 98  ? 13.05662  -11.70362 44.56977  1.000 56.20356  ? 98  TYR A CE1 1 
ATOM 751  C CE2 . TYR A 1 98  ? 12.05130  -11.43875 42.44748  1.000 56.86955  ? 98  TYR A CE2 1 
ATOM 752  C CZ  . TYR A 1 98  ? 13.17419  -11.44989 43.24335  1.000 56.64799  ? 98  TYR A CZ  1 
ATOM 753  O OH  . TYR A 1 98  ? 14.41712  -11.18495 42.71482  1.000 57.18241  ? 98  TYR A OH  1 
ATOM 754  N N   . ILE A 1 99  ? 9.81478   -12.19989 48.13168  1.000 54.65731  ? 99  ILE A N   1 
ATOM 755  C CA  . ILE A 1 99  ? 10.74350  -12.04099 49.23888  1.000 52.81620  ? 99  ILE A CA  1 
ATOM 756  C C   . ILE A 1 99  ? 10.89022  -13.36229 50.00073  1.000 59.42483  ? 99  ILE A C   1 
ATOM 757  O O   . ILE A 1 99  ? 12.00008  -13.75445 50.38813  1.000 59.64258  ? 99  ILE A O   1 
ATOM 758  C CB  . ILE A 1 99  ? 10.28648  -10.88000 50.13850  1.000 54.85609  ? 99  ILE A CB  1 
ATOM 759  C CG1 . ILE A 1 99  ? 10.28390  -9.55759  49.37085  1.000 51.59761  ? 99  ILE A CG1 1 
ATOM 760  C CG2 . ILE A 1 99  ? 11.22449  -10.72167 51.31900  1.000 57.88003  ? 99  ILE A CG2 1 
ATOM 761  C CD1 . ILE A 1 99  ? 11.68907  -9.02380  49.03608  1.000 48.83139  ? 99  ILE A CD1 1 
ATOM 762  N N   . ASN A 1 100 ? 9.78315   -14.09377 50.18878  1.000 59.85350  ? 100 ASN A N   1 
ATOM 763  C CA  . ASN A 1 100 ? 9.81964   -15.34819 50.93479  1.000 57.56843  ? 100 ASN A CA  1 
ATOM 764  C C   . ASN A 1 100 ? 10.55920  -16.46038 50.20460  1.000 58.02600  ? 100 ASN A C   1 
ATOM 765  O O   . ASN A 1 100 ? 10.91005  -17.47078 50.81572  1.000 59.99266  ? 100 ASN A O   1 
ATOM 766  C CB  . ASN A 1 100 ? 8.39981   -15.85240 51.24145  1.000 59.82179  ? 100 ASN A CB  1 
ATOM 767  C CG  . ASN A 1 100 ? 7.67723   -15.02330 52.28254  1.000 60.12029  ? 100 ASN A CG  1 
ATOM 768  O OD1 . ASN A 1 100 ? 8.28987   -14.48390 53.20252  1.000 61.64598  ? 100 ASN A OD1 1 
ATOM 769  N ND2 . ASN A 1 100 ? 6.35032   -14.97972 52.18058  1.000 61.08342  ? 100 ASN A ND2 1 
ATOM 770  N N   . ALA A 1 101 ? 10.79563  -16.32839 48.91970  1.000 60.08059  ? 101 ALA A N   1 
ATOM 771  C CA  . ALA A 1 101 ? 11.41593  -17.41756 48.19246  1.000 61.83739  ? 101 ALA A CA  1 
ATOM 772  C C   . ALA A 1 101 ? 12.83296  -17.08017 47.73696  1.000 64.52985  ? 101 ALA A C   1 
ATOM 773  O O   . ALA A 1 101 ? 13.37172  -17.77037 46.86581  1.000 69.65054  ? 101 ALA A O   1 
ATOM 774  C CB  . ALA A 1 101 ? 10.53713  -17.79730 47.00074  1.000 61.53471  ? 101 ALA A CB  1 
ATOM 775  N N   . HIS A 1 102 ? 13.46354  -16.04493 48.29734  1.000 58.96409  ? 102 HIS A N   1 
ATOM 776  C CA  . HIS A 1 102 ? 14.74367  -15.59379 47.75356  1.000 59.35209  ? 102 HIS A CA  1 
ATOM 777  C C   . HIS A 1 102 ? 15.74559  -15.21789 48.82763  1.000 58.87395  ? 102 HIS A C   1 
ATOM 778  O O   . HIS A 1 102 ? 16.55559  -14.30753 48.63054  1.000 59.28659  ? 102 HIS A O   1 
ATOM 779  C CB  . HIS A 1 102 ? 14.55789  -14.42272 46.80871  1.000 55.61121  ? 102 HIS A CB  1 
ATOM 780  C CG  . HIS A 1 102 ? 14.05058  -14.80677 45.46233  1.000 58.17910  ? 102 HIS A CG  1 
ATOM 781  N ND1 . HIS A 1 102 ? 12.72130  -15.07176 45.21613  1.000 58.97869  ? 102 HIS A ND1 1 
ATOM 782  C CD2 . HIS A 1 102 ? 14.68260  -14.89808 44.26993  1.000 58.83023  ? 102 HIS A CD2 1 
ATOM 783  C CE1 . HIS A 1 102 ? 12.56046  -15.33275 43.93148  1.000 60.80678  ? 102 HIS A CE1 1 
ATOM 784  N NE2 . HIS A 1 102 ? 13.73516  -15.23365 43.33491  1.000 63.10983  ? 102 HIS A NE2 1 
ATOM 785  N N   . ASN A 1 103 ? 15.74630  -15.92805 49.95233  1.000 55.23931  ? 103 ASN A N   1 
ATOM 786  C CA  . ASN A 1 103 ? 16.84541  -15.82852 50.91450  1.000 59.10040  ? 103 ASN A CA  1 
ATOM 787  C C   . ASN A 1 103 ? 16.96074  -14.44803 51.53203  1.000 60.06280  ? 103 ASN A C   1 
ATOM 788  O O   . ASN A 1 103 ? 18.06004  -13.91316 51.70596  1.000 61.14203  ? 103 ASN A O   1 
ATOM 789  C CB  . ASN A 1 103 ? 18.17274  -16.23619 50.28372  1.000 66.68040  ? 103 ASN A CB  1 
ATOM 790  C CG  . ASN A 1 103 ? 18.38573  -17.70449 50.33945  1.000 67.97454  ? 103 ASN A CG  1 
ATOM 791  O OD1 . ASN A 1 103 ? 18.26794  -18.40840 49.34287  1.000 67.07609  ? 103 ASN A OD1 1 
ATOM 792  N ND2 . ASN A 1 103 ? 18.72080  -18.18954 51.53176  1.000 75.78193  ? 103 ASN A ND2 1 
ATOM 793  N N   . ILE A 1 104 ? 15.82162  -13.88858 51.89936  1.000 60.20812  ? 104 ILE A N   1 
ATOM 794  C CA  . ILE A 1 104 ? 15.76369  -12.63908 52.63143  1.000 58.27495  ? 104 ILE A CA  1 
ATOM 795  C C   . ILE A 1 104 ? 15.54391  -12.95113 54.11027  1.000 60.48706  ? 104 ILE A C   1 
ATOM 796  O O   . ILE A 1 104 ? 14.63435  -13.70702 54.46976  1.000 61.44270  ? 104 ILE A O   1 
ATOM 797  C CB  . ILE A 1 104 ? 14.66504  -11.73709 52.05909  1.000 56.16577  ? 104 ILE A CB  1 
ATOM 798  C CG1 . ILE A 1 104 ? 14.92613  -11.52807 50.55993  1.000 61.41564  ? 104 ILE A CG1 1 
ATOM 799  C CG2 . ILE A 1 104 ? 14.61237  -10.42311 52.80689  1.000 56.93082  ? 104 ILE A CG2 1 
ATOM 800  C CD1 . ILE A 1 104 ? 16.30856  -10.93486 50.21776  1.000 57.87836  ? 104 ILE A CD1 1 
ATOM 801  N N   . ASP A 1 105 ? 16.40441  -12.40061 54.96036  1.000 61.36891  ? 105 ASP A N   1 
ATOM 802  C CA  . ASP A 1 105 ? 16.29050  -12.53577 56.40651  1.000 63.11291  ? 105 ASP A CA  1 
ATOM 803  C C   . ASP A 1 105 ? 15.52732  -11.34539 56.98792  1.000 65.13125  ? 105 ASP A C   1 
ATOM 804  O O   . ASP A 1 105 ? 15.96760  -10.19798 56.81102  1.000 63.58258  ? 105 ASP A O   1 
ATOM 805  C CB  . ASP A 1 105 ? 17.68964  -12.64454 57.00888  1.000 65.57353  ? 105 ASP A CB  1 
ATOM 806  C CG  . ASP A 1 105 ? 17.70963  -12.69325 58.53517  1.000 67.77829  ? 105 ASP A CG  1 
ATOM 807  O OD1 . ASP A 1 105 ? 16.66411  -12.54235 59.21143  1.000 67.98983  ? 105 ASP A OD1 1 
ATOM 808  O OD2 . ASP A 1 105 ? 18.82759  -12.85875 59.05736  1.000 71.24594  ? 105 ASP A OD2 1 
ATOM 809  N N   . PRO A 1 106 ? 14.41293  -11.56418 57.70832  1.000 65.42223  ? 106 PRO A N   1 
ATOM 810  C CA  . PRO A 1 106 ? 13.62505  -10.42045 58.20957  1.000 63.38862  ? 106 PRO A CA  1 
ATOM 811  C C   . PRO A 1 106 ? 14.40331  -9.47422  59.10240  1.000 63.64790  ? 106 PRO A C   1 
ATOM 812  O O   . PRO A 1 106 ? 14.03249  -8.29819  59.18117  1.000 62.22649  ? 106 PRO A O   1 
ATOM 813  C CB  . PRO A 1 106 ? 12.47652  -11.09085 58.98046  1.000 62.16582  ? 106 PRO A CB  1 
ATOM 814  C CG  . PRO A 1 106 ? 12.36254  -12.44484 58.39561  1.000 63.95481  ? 106 PRO A CG  1 
ATOM 815  C CD  . PRO A 1 106 ? 13.76981  -12.85140 58.02930  1.000 63.75496  ? 106 PRO A CD  1 
ATOM 816  N N   . TRP A 1 107 ? 15.45986  -9.93425  59.78224  1.000 63.34630  ? 107 TRP A N   1 
ATOM 817  C CA  . TRP A 1 107 ? 16.16609  -9.06733  60.72288  1.000 64.71339  ? 107 TRP A CA  1 
ATOM 818  C C   . TRP A 1 107 ? 17.50344  -8.54606  60.21564  1.000 63.39834  ? 107 TRP A C   1 
ATOM 819  O O   . TRP A 1 107 ? 17.90922  -7.45037  60.61685  1.000 60.45187  ? 107 TRP A O   1 
ATOM 820  C CB  . TRP A 1 107 ? 16.38542  -9.78486  62.06451  1.000 68.07890  ? 107 TRP A CB  1 
ATOM 821  C CG  . TRP A 1 107 ? 15.10834  -9.95636  62.85253  1.000 65.67221  ? 107 TRP A CG  1 
ATOM 822  C CD1 . TRP A 1 107 ? 14.26353  -11.01899 62.80636  1.000 67.10883  ? 107 TRP A CD1 1 
ATOM 823  C CD2 . TRP A 1 107 ? 14.54684  -9.04325  63.79510  1.000 66.13740  ? 107 TRP A CD2 1 
ATOM 824  N NE1 . TRP A 1 107 ? 13.20195  -10.82662 63.64357  1.000 64.36513  ? 107 TRP A NE1 1 
ATOM 825  C CE2 . TRP A 1 107 ? 13.34787  -9.62037  64.26925  1.000 66.33566  ? 107 TRP A CE2 1 
ATOM 826  C CE3 . TRP A 1 107 ? 14.93352  -7.78812  64.28409  1.000 68.78123  ? 107 TRP A CE3 1 
ATOM 827  C CZ2 . TRP A 1 107 ? 12.52650  -8.98878  65.21140  1.000 66.86669  ? 107 TRP A CZ2 1 
ATOM 828  C CZ3 . TRP A 1 107 ? 14.10785  -7.15298  65.22874  1.000 66.72559  ? 107 TRP A CZ3 1 
ATOM 829  C CH2 . TRP A 1 107 ? 12.92350  -7.76112  65.67861  1.000 67.69086  ? 107 TRP A CH2 1 
ATOM 830  N N   . LYS A 1 108 ? 18.19775  -9.26231  59.33118  1.000 62.79241  ? 108 LYS A N   1 
ATOM 831  C CA  . LYS A 1 108 ? 19.54542  -8.84568  58.95820  1.000 61.82796  ? 108 LYS A CA  1 
ATOM 832  C C   . LYS A 1 108 ? 19.69948  -8.39783  57.49469  1.000 61.76402  ? 108 LYS A C   1 
ATOM 833  O O   . LYS A 1 108 ? 20.72886  -7.80110  57.14422  1.000 59.58686  ? 108 LYS A O   1 
ATOM 834  C CB  . LYS A 1 108 ? 20.53211  -9.98038  59.29025  1.000 58.61227  ? 108 LYS A CB  1 
ATOM 835  N N   . SER A 1 109 ? 18.71359  -8.63532  56.63764  1.000 59.16463  ? 109 SER A N   1 
ATOM 836  C CA  . SER A 1 109 ? 18.83898  -8.25794  55.23741  1.000 59.75674  ? 109 SER A CA  1 
ATOM 837  C C   . SER A 1 109 ? 18.65359  -6.75309  55.06677  1.000 58.68411  ? 109 SER A C   1 
ATOM 838  O O   . SER A 1 109 ? 18.16491  -6.06173  55.95874  1.000 59.33943  ? 109 SER A O   1 
ATOM 839  C CB  . SER A 1 109 ? 17.80752  -9.00030  54.39341  1.000 59.37584  ? 109 SER A CB  1 
ATOM 840  O OG  . SER A 1 109 ? 17.97740  -10.39092 54.54196  1.000 60.29009  ? 109 SER A OG  1 
ATOM 841  N N   . GLN A 1 110 ? 19.03611  -6.24205  53.89727  1.000 56.83002  ? 110 GLN A N   1 
ATOM 842  C CA  . GLN A 1 110 ? 18.92201  -4.82140  53.62525  1.000 52.47275  ? 110 GLN A CA  1 
ATOM 843  C C   . GLN A 1 110 ? 18.04038  -4.60876  52.40640  1.000 53.25087  ? 110 GLN A C   1 
ATOM 844  O O   . GLN A 1 110 ? 18.04036  -5.43294  51.49142  1.000 56.16394  ? 110 GLN A O   1 
ATOM 845  C CB  . GLN A 1 110 ? 20.30607  -4.18652  53.47759  1.000 53.64771  ? 110 GLN A CB  1 
ATOM 846  C CG  . GLN A 1 110 ? 20.97909  -3.94595  54.84176  1.000 55.07661  ? 110 GLN A CG  1 
ATOM 847  C CD  . GLN A 1 110 ? 22.41738  -3.41958  54.78471  1.000 60.61023  ? 110 GLN A CD  1 
ATOM 848  O OE1 . GLN A 1 110 ? 23.05566  -3.36853  53.72725  1.000 63.41294  ? 110 GLN A OE1 1 
ATOM 849  N NE2 . GLN A 1 110 ? 22.92496  -3.00766  55.94055  1.000 60.73005  ? 110 GLN A NE2 1 
ATOM 850  N N   . GLY A 1 111 ? 17.22357  -3.55618  52.45678  1.000 48.18293  ? 111 GLY A N   1 
ATOM 851  C CA  . GLY A 1 111 ? 16.35599  -3.15828  51.36000  1.000 45.78743  ? 111 GLY A CA  1 
ATOM 852  C C   . GLY A 1 111 ? 16.83976  -1.82069  50.81937  1.000 54.39854  ? 111 GLY A C   1 
ATOM 853  O O   . GLY A 1 111 ? 17.17171  -0.91743  51.60169  1.000 54.17864  ? 111 GLY A O   1 
ATOM 854  N N   . TRP A 1 112 ? 16.87033  -1.69850  49.46994  1.000 50.97830  ? 112 TRP A N   1 
ATOM 855  C CA  . TRP A 1 112 ? 17.55067  -0.63239  48.73723  1.000 45.87610  ? 112 TRP A CA  1 
ATOM 856  C C   . TRP A 1 112 ? 16.57797  0.03331   47.77151  1.000 50.09489  ? 112 TRP A C   1 
ATOM 857  O O   . TRP A 1 112 ? 15.63906  -0.61602  47.30265  1.000 48.75176  ? 112 TRP A O   1 
ATOM 858  C CB  . TRP A 1 112 ? 18.72277  -1.19568  47.94129  1.000 47.19406  ? 112 TRP A CB  1 
ATOM 859  C CG  . TRP A 1 112 ? 19.77864  -1.74694  48.76753  1.000 45.88849  ? 112 TRP A CG  1 
ATOM 860  C CD1 . TRP A 1 112 ? 19.89666  -3.03446  49.19891  1.000 48.83843  ? 112 TRP A CD1 1 
ATOM 861  C CD2 . TRP A 1 112 ? 20.92247  -1.05495  49.24567  1.000 48.21269  ? 112 TRP A CD2 1 
ATOM 862  N NE1 . TRP A 1 112 ? 21.03729  -3.18146  49.95690  1.000 50.52274  ? 112 TRP A NE1 1 
ATOM 863  C CE2 . TRP A 1 112 ? 21.67838  -1.97206  50.00842  1.000 51.53570  ? 112 TRP A CE2 1 
ATOM 864  C CE3 . TRP A 1 112 ? 21.37541  0.26223   49.12900  1.000 49.49216  ? 112 TRP A CE3 1 
ATOM 865  C CZ2 . TRP A 1 112 ? 22.85496  -1.61040  50.64929  1.000 52.30531  ? 112 TRP A CZ2 1 
ATOM 866  C CZ3 . TRP A 1 112 ? 22.55140  0.61873   49.77202  1.000 49.22580  ? 112 TRP A CZ3 1 
ATOM 867  C CH2 . TRP A 1 112 ? 23.27462  -0.31128  50.51588  1.000 50.09139  ? 112 TRP A CH2 1 
ATOM 868  N N   . CYS A 1 113 ? 16.80056  1.32983   47.47786  1.000 52.19639  ? 113 CYS A N   1 
ATOM 869  C CA  . CYS A 1 113 ? 16.12646  2.01455   46.36463  1.000 55.11328  ? 113 CYS A CA  1 
ATOM 870  C C   . CYS A 1 113 ? 16.80130  3.35650   46.06269  1.000 54.99622  ? 113 CYS A C   1 
ATOM 871  O O   . CYS A 1 113 ? 17.76208  3.75823   46.72351  1.000 56.41681  ? 113 CYS A O   1 
ATOM 872  C CB  . CYS A 1 113 ? 14.64169  2.21471   46.63941  1.000 56.39285  ? 113 CYS A CB  1 
ATOM 873  S SG  . CYS A 1 113 ? 14.30585  3.19479   48.07907  1.000 63.11636  ? 113 CYS A SG  1 
ATOM 874  N N   . ARG A 1 114 ? 16.31548  4.03006   45.01904  1.000 50.92697  ? 114 ARG A N   1 
ATOM 875  C CA  . ARG A 1 114 ? 16.76700  5.38151   44.68973  1.000 60.71924  ? 114 ARG A CA  1 
ATOM 876  C C   . ARG A 1 114 ? 15.73522  6.37280   45.19418  1.000 61.62011  ? 114 ARG A C   1 
ATOM 877  O O   . ARG A 1 114 ? 14.60157  6.40811   44.69788  1.000 62.75776  ? 114 ARG A O   1 
ATOM 878  C CB  . ARG A 1 114 ? 17.00476  5.61112   43.18558  1.000 58.75855  ? 114 ARG A CB  1 
ATOM 879  C CG  . ARG A 1 114 ? 18.34004  5.16066   42.70524  1.000 56.93205  ? 114 ARG A CG  1 
ATOM 880  C CD  . ARG A 1 114 ? 18.62581  5.58144   41.28183  1.000 60.94355  ? 114 ARG A CD  1 
ATOM 881  N NE  . ARG A 1 114 ? 19.88841  5.00022   40.82779  1.000 58.35335  ? 114 ARG A NE  1 
ATOM 882  C CZ  . ARG A 1 114 ? 21.08031  5.55699   41.00489  1.000 62.34958  ? 114 ARG A CZ  1 
ATOM 883  N NH1 . ARG A 1 114 ? 21.20895  6.77330   41.51551  1.000 61.09956  ? 114 ARG A NH1 1 
ATOM 884  N NH2 . ARG A 1 114 ? 22.17361  4.87307   40.66750  1.000 62.65433  ? 114 ARG A NH2 1 
ATOM 885  N N   . GLY A 1 115 ? 16.13813  7.20972   46.13391  1.000 60.17224  ? 115 GLY A N   1 
ATOM 886  C CA  . GLY A 1 115 ? 15.11581  7.96720   46.81488  1.000 67.02668  ? 115 GLY A CA  1 
ATOM 887  C C   . GLY A 1 115 ? 14.39934  7.06735   47.79547  1.000 58.60813  ? 115 GLY A C   1 
ATOM 888  O O   . GLY A 1 115 ? 13.23484  6.70146   47.61293  1.000 56.81830  ? 115 GLY A O   1 
ATOM 889  N N   . MET A 1 116 ? 15.14169  6.67258   48.82018  1.000 60.95817  ? 116 MET A N   1 
ATOM 890  C CA  . MET A 1 116 ? 14.57086  5.94313   49.94144  1.000 62.35811  ? 116 MET A CA  1 
ATOM 891  C C   . MET A 1 116 ? 13.25338  6.54534   50.44289  1.000 60.23269  ? 116 MET A C   1 
ATOM 892  O O   . MET A 1 116 ? 12.35001  5.80332   50.83257  1.000 60.22125  ? 116 MET A O   1 
ATOM 893  C CB  . MET A 1 116 ? 15.62785  5.88189   51.03554  1.000 60.14686  ? 116 MET A CB  1 
ATOM 894  C CG  . MET A 1 116 ? 15.27916  5.13969   52.25921  1.000 58.94729  ? 116 MET A CG  1 
ATOM 895  S SD  . MET A 1 116 ? 16.80485  5.09307   53.23182  1.000 64.17420  ? 116 MET A SD  1 
ATOM 896  C CE  . MET A 1 116 ? 16.12593  4.53900   54.79139  1.000 62.45685  ? 116 MET A CE  1 
ATOM 897  N N   . SER A 1 117 ? 13.09517  7.86906   50.39078  1.000 58.95434  ? 117 SER A N   1 
ATOM 898  C CA  . SER A 1 117 ? 11.86466  8.51176   50.85854  1.000 56.60078  ? 117 SER A CA  1 
ATOM 899  C C   . SER A 1 117 ? 10.72478  8.48337   49.84386  1.000 59.14411  ? 117 SER A C   1 
ATOM 900  O O   . SER A 1 117 ? 9.66527   9.06456   50.11438  1.000 58.82495  ? 117 SER A O   1 
ATOM 901  C CB  . SER A 1 117 ? 12.15467  9.95713   51.27997  1.000 54.83780  ? 117 SER A CB  1 
ATOM 902  O OG  . SER A 1 117 ? 12.72250  10.72751  50.23269  1.000 57.01850  ? 117 SER A OG  1 
ATOM 903  N N   . PHE A 1 118 ? 10.91023  7.83437   48.69721  1.000 64.44830  ? 118 PHE A N   1 
ATOM 904  C CA  . PHE A 1 118 ? 9.87441   7.67361   47.68723  1.000 64.15473  ? 118 PHE A CA  1 
ATOM 905  C C   . PHE A 1 118 ? 9.39334   6.23651   47.58284  1.000 63.82510  ? 118 PHE A C   1 
ATOM 906  O O   . PHE A 1 118 ? 8.18995   5.97033   47.61262  1.000 62.68149  ? 118 PHE A O   1 
ATOM 907  C CB  . PHE A 1 118 ? 10.40300  8.14758   46.32068  1.000 66.89367  ? 118 PHE A CB  1 
ATOM 908  C CG  . PHE A 1 118 ? 9.45326   7.89984   45.15898  1.000 70.63257  ? 118 PHE A CG  1 
ATOM 909  C CD1 . PHE A 1 118 ? 8.26346   8.62239   45.03304  1.000 70.11277  ? 118 PHE A CD1 1 
ATOM 910  C CD2 . PHE A 1 118 ? 9.78115   6.97084   44.16010  1.000 70.17407  ? 118 PHE A CD2 1 
ATOM 911  C CE1 . PHE A 1 118 ? 7.39289   8.40232   43.95300  1.000 69.01337  ? 118 PHE A CE1 1 
ATOM 912  C CE2 . PHE A 1 118 ? 8.92040   6.74495   43.06942  1.000 67.86993  ? 118 PHE A CE2 1 
ATOM 913  C CZ  . PHE A 1 118 ? 7.72331   7.46694   42.97096  1.000 68.22368  ? 118 PHE A CZ  1 
ATOM 914  N N   . ASP A 1 119 ? 10.32253  5.29849   47.46977  1.000 61.67010  ? 119 ASP A N   1 
ATOM 915  C CA  . ASP A 1 119 ? 9.97249   3.90883   47.25107  1.000 58.53445  ? 119 ASP A CA  1 
ATOM 916  C C   . ASP A 1 119 ? 9.45425   3.24615   48.51795  1.000 56.99616  ? 119 ASP A C   1 
ATOM 917  O O   . ASP A 1 119 ? 8.37129   2.65748   48.50468  1.000 57.90312  ? 119 ASP A O   1 
ATOM 918  C CB  . ASP A 1 119 ? 11.18680  3.17488   46.69973  1.000 60.38090  ? 119 ASP A CB  1 
ATOM 919  C CG  . ASP A 1 119 ? 11.35857  3.37947   45.22268  1.000 62.45565  ? 119 ASP A CG  1 
ATOM 920  O OD1 . ASP A 1 119 ? 10.33747  3.29996   44.50835  1.000 63.31193  ? 119 ASP A OD1 1 
ATOM 921  O OD2 . ASP A 1 119 ? 12.49069  3.68347   44.78487  1.000 64.39793  ? 119 ASP A OD2 1 
ATOM 922  N N   . PHE A 1 120 ? 10.20010  3.32889   49.62255  1.000 53.01877  ? 120 PHE A N   1 
ATOM 923  C CA  . PHE A 1 120 ? 9.74897   2.65333   50.84074  1.000 52.29291  ? 120 PHE A CA  1 
ATOM 924  C C   . PHE A 1 120 ? 8.44084   3.19528   51.41470  1.000 51.55398  ? 120 PHE A C   1 
ATOM 925  O O   . PHE A 1 120 ? 7.51951   2.39188   51.64716  1.000 51.12226  ? 120 PHE A O   1 
ATOM 926  C CB  . PHE A 1 120 ? 10.87249  2.64264   51.87419  1.000 49.87545  ? 120 PHE A CB  1 
ATOM 927  C CG  . PHE A 1 120 ? 11.90276  1.61330   51.59039  1.000 53.39252  ? 120 PHE A CG  1 
ATOM 928  C CD1 . PHE A 1 120 ? 11.59727  0.26225   51.75321  1.000 49.76358  ? 120 PHE A CD1 1 
ATOM 929  C CD2 . PHE A 1 120 ? 13.17469  1.97004   51.15735  1.000 55.28094  ? 120 PHE A CD2 1 
ATOM 930  C CE1 . PHE A 1 120 ? 12.53804  -0.71243  51.47559  1.000 51.19539  ? 120 PHE A CE1 1 
ATOM 931  C CE2 . PHE A 1 120 ? 14.13635  0.98502   50.87801  1.000 52.59502  ? 120 PHE A CE2 1 
ATOM 932  C CZ  . PHE A 1 120 ? 13.81315  -0.35012  51.03615  1.000 51.92687  ? 120 PHE A CZ  1 
ATOM 933  N N   . PRO A 1 121 ? 8.26518   4.49341   51.64997  1.000 50.52721  ? 121 PRO A N   1 
ATOM 934  C CA  . PRO A 1 121 ? 6.94141   4.95961   52.08360  1.000 45.72304  ? 121 PRO A CA  1 
ATOM 935  C C   . PRO A 1 121 ? 5.77384   4.43141   51.26508  1.000 50.36420  ? 121 PRO A C   1 
ATOM 936  O O   . PRO A 1 121 ? 4.72185   4.16767   51.85913  1.000 51.06301  ? 121 PRO A O   1 
ATOM 937  C CB  . PRO A 1 121 ? 7.07319   6.47635   51.97281  1.000 47.05323  ? 121 PRO A CB  1 
ATOM 938  C CG  . PRO A 1 121 ? 8.52600   6.71526   52.29563  1.000 49.44310  ? 121 PRO A CG  1 
ATOM 939  C CD  . PRO A 1 121 ? 9.26622   5.57840   51.68790  1.000 52.78388  ? 121 PRO A CD  1 
ATOM 940  N N   . ILE A 1 122 ? 5.89622   4.29023   49.93608  1.000 50.60524  ? 122 ILE A N   1 
ATOM 941  C CA  . ILE A 1 122 ? 4.79415   3.71267   49.16442  1.000 48.90962  ? 122 ILE A CA  1 
ATOM 942  C C   . ILE A 1 122 ? 4.62372   2.24048   49.52053  1.000 45.23089  ? 122 ILE A C   1 
ATOM 943  O O   . ILE A 1 122 ? 3.50202   1.73828   49.65298  1.000 41.11093  ? 122 ILE A O   1 
ATOM 944  C CB  . ILE A 1 122 ? 5.01259   3.91550   47.64752  1.000 49.16263  ? 122 ILE A CB  1 
ATOM 945  C CG1 . ILE A 1 122 ? 4.86461   5.39047   47.26778  1.000 54.34697  ? 122 ILE A CG1 1 
ATOM 946  C CG2 . ILE A 1 122 ? 4.03803   3.07132   46.82232  1.000 46.70615  ? 122 ILE A CG2 1 
ATOM 947  C CD1 . ILE A 1 122 ? 5.43683   5.80342   45.87629  1.000 53.08641  ? 122 ILE A CD1 1 
ATOM 948  N N   . LEU A 1 123 ? 5.73463   1.52756   49.67699  1.000 46.61327  ? 123 LEU A N   1 
ATOM 949  C CA  . LEU A 1 123 ? 5.65933   0.08753   49.87245  1.000 45.99388  ? 123 LEU A CA  1 
ATOM 950  C C   . LEU A 1 123 ? 4.99353   -0.23637  51.20142  1.000 45.23121  ? 123 LEU A C   1 
ATOM 951  O O   . LEU A 1 123 ? 4.07579   -1.06266  51.25157  1.000 42.14761  ? 123 LEU A O   1 
ATOM 952  C CB  . LEU A 1 123 ? 7.05583   -0.53383  49.80276  1.000 46.06433  ? 123 LEU A CB  1 
ATOM 953  C CG  . LEU A 1 123 ? 7.10495   -2.07122  49.84176  1.000 47.11073  ? 123 LEU A CG  1 
ATOM 954  C CD1 . LEU A 1 123 ? 6.64121   -2.68851  48.49343  1.000 45.40589  ? 123 LEU A CD1 1 
ATOM 955  C CD2 . LEU A 1 123 ? 8.46174   -2.57572  50.28939  1.000 42.29711  ? 123 LEU A CD2 1 
ATOM 956  N N   . VAL A 1 124 ? 5.41140   0.45874   52.27605  1.000 47.28267  ? 124 VAL A N   1 
ATOM 957  C CA  . VAL A 1 124 ? 4.81919   0.29353   53.60693  1.000 45.66114  ? 124 VAL A CA  1 
ATOM 958  C C   . VAL A 1 124 ? 3.31961   0.59618   53.59617  1.000 43.61686  ? 124 VAL A C   1 
ATOM 959  O O   . VAL A 1 124 ? 2.52757   -0.17627  54.12519  1.000 48.59568  ? 124 VAL A O   1 
ATOM 960  C CB  . VAL A 1 124 ? 5.56480   1.16559   54.62872  1.000 45.89418  ? 124 VAL A CB  1 
ATOM 961  C CG1 . VAL A 1 124 ? 4.92986   1.03341   55.98164  1.000 49.90021  ? 124 VAL A CG1 1 
ATOM 962  C CG2 . VAL A 1 124 ? 7.01992   0.77187   54.69154  1.000 42.40178  ? 124 VAL A CG2 1 
ATOM 963  N N   . ASP A 1 125 ? 2.89783   1.67498   52.94290  1.000 39.13747  ? 125 ASP A N   1 
ATOM 964  C CA  . ASP A 1 125 ? 1.46864   1.93937   52.80611  1.000 41.43103  ? 125 ASP A CA  1 
ATOM 965  C C   . ASP A 1 125 ? 0.71641   0.78831   52.13515  1.000 46.50447  ? 125 ASP A C   1 
ATOM 966  O O   . ASP A 1 125 ? -0.40312  0.45015   52.53967  1.000 49.63269  ? 125 ASP A O   1 
ATOM 967  C CB  . ASP A 1 125 ? 1.23661   3.23095   52.02894  1.000 44.94374  ? 125 ASP A CB  1 
ATOM 968  C CG  . ASP A 1 125 ? -0.17835  3.78259   52.23542  1.000 51.09777  ? 125 ASP A CG  1 
ATOM 969  O OD1 . ASP A 1 125 ? -0.49350  4.27999   53.35274  1.000 56.51602  ? 125 ASP A OD1 1 
ATOM 970  O OD2 . ASP A 1 125 ? -0.98522  3.72550   51.30374  1.000 49.71818  ? 125 ASP A OD2 1 
ATOM 971  N N   . LEU A 1 126 ? 1.28809   0.19015   51.08844  1.000 48.72247  ? 126 LEU A N   1 
ATOM 972  C CA  . LEU A 1 126 ? 0.64801   -0.97940  50.47617  1.000 49.64695  ? 126 LEU A CA  1 
ATOM 973  C C   . LEU A 1 126 ? 0.61830   -2.18196  51.42764  1.000 47.74792  ? 126 LEU A C   1 
ATOM 974  O O   . LEU A 1 126 ? -0.31668  -2.99075  51.37342  1.000 45.58480  ? 126 LEU A O   1 
ATOM 975  C CB  . LEU A 1 126 ? 1.35014   -1.33822  49.16009  1.000 46.59177  ? 126 LEU A CB  1 
ATOM 976  C CG  . LEU A 1 126 ? 1.22977   -0.36095  47.98310  1.000 44.07356  ? 126 LEU A CG  1 
ATOM 977  C CD1 . LEU A 1 126 ? 2.17737   -0.84839  46.94356  1.000 40.02943  ? 126 LEU A CD1 1 
ATOM 978  C CD2 . LEU A 1 126 ? -0.18974  -0.23829  47.43197  1.000 41.35235  ? 126 LEU A CD2 1 
ATOM 979  N N   . ILE A 1 127 ? 1.62691   -2.30968  52.29592  1.000 43.55123  ? 127 ILE A N   1 
ATOM 980  C CA  . ILE A 1 127 ? 1.57956   -3.28051  53.38371  1.000 46.72842  ? 127 ILE A CA  1 
ATOM 981  C C   . ILE A 1 127 ? 0.45180   -2.95121  54.35753  1.000 54.70366  ? 127 ILE A C   1 
ATOM 982  O O   . ILE A 1 127 ? -0.26780  -3.84575  54.81165  1.000 57.44629  ? 127 ILE A O   1 
ATOM 983  C CB  . ILE A 1 127 ? 2.92539   -3.32962  54.12829  1.000 50.60518  ? 127 ILE A CB  1 
ATOM 984  C CG1 . ILE A 1 127 ? 4.08673   -3.63338  53.17839  1.000 48.29010  ? 127 ILE A CG1 1 
ATOM 985  C CG2 . ILE A 1 127 ? 2.85770   -4.31008  55.31323  1.000 49.24549  ? 127 ILE A CG2 1 
ATOM 986  C CD1 . ILE A 1 127 ? 3.97856   -4.90242  52.49011  1.000 45.53729  ? 127 ILE A CD1 1 
ATOM 987  N N   . ARG A 1 128 ? 0.30472   -1.67119  54.73427  1.000 60.59866  ? 128 ARG A N   1 
ATOM 988  C CA  . ARG A 1 128 ? -0.71756  -1.30032  55.71412  1.000 60.81119  ? 128 ARG A CA  1 
ATOM 989  C C   . ARG A 1 128 ? -2.11730  -1.60395  55.18552  1.000 61.88053  ? 128 ARG A C   1 
ATOM 990  O O   . ARG A 1 128 ? -3.03798  -1.87571  55.97411  1.000 62.71307  ? 128 ARG A O   1 
ATOM 991  C CB  . ARG A 1 128 ? -0.60834  0.18568   56.08637  1.000 58.30732  ? 128 ARG A CB  1 
ATOM 992  C CG  . ARG A 1 128 ? 0.72366   0.63228   56.63214  1.000 56.85694  ? 128 ARG A CG  1 
ATOM 993  C CD  . ARG A 1 128 ? 0.63458   2.10647   56.93359  1.000 61.82374  ? 128 ARG A CD  1 
ATOM 994  N NE  . ARG A 1 128 ? 1.92835   2.77873   57.06356  1.000 66.57246  ? 128 ARG A NE  1 
ATOM 995  C CZ  . ARG A 1 128 ? 2.69532   2.76791   58.14930  1.000 71.73760  ? 128 ARG A CZ  1 
ATOM 996  N NH1 . ARG A 1 128 ? 2.38201   2.03749   59.22189  1.000 75.36526  ? 128 ARG A NH1 1 
ATOM 997  N NH2 . ARG A 1 128 ? 3.81509   3.49267   58.15597  1.000 66.93940  ? 128 ARG A NH2 1 
ATOM 998  N N   . ASP A 1 129 ? -2.30188  -1.54745  53.85759  1.000 60.43159  ? 129 ASP A N   1 
ATOM 999  C CA  . ASP A 1 129 ? -3.58303  -1.93325  53.28015  1.000 61.35825  ? 129 ASP A CA  1 
ATOM 1000 C C   . ASP A 1 129 ? -3.87535  -3.41743  53.46272  1.000 63.13244  ? 129 ASP A C   1 
ATOM 1001 O O   . ASP A 1 129 ? -5.04410  -3.81337  53.42665  1.000 64.32579  ? 129 ASP A O   1 
ATOM 1002 C CB  . ASP A 1 129 ? -3.65675  -1.57338  51.79637  1.000 61.00383  ? 129 ASP A CB  1 
ATOM 1003 C CG  . ASP A 1 129 ? -3.88117  -0.07990  51.54323  1.000 64.28930  ? 129 ASP A CG  1 
ATOM 1004 O OD1 . ASP A 1 129 ? -4.53037  0.60411   52.38740  1.000 59.72641  ? 129 ASP A OD1 1 
ATOM 1005 O OD2 . ASP A 1 129 ? -3.42122  0.39348   50.45362  1.000 65.28510  ? 129 ASP A OD2 1 
ATOM 1006 N N   . ILE A 1 130 ? -2.86438  -4.25920  53.67181  1.000 55.59774  ? 130 ILE A N   1 
ATOM 1007 C CA  . ILE A 1 130 ? -3.17578  -5.57317  54.22843  1.000 57.52115  ? 130 ILE A CA  1 
ATOM 1008 C C   . ILE A 1 130 ? -3.88133  -5.40784  55.57961  1.000 59.47233  ? 130 ILE A C   1 
ATOM 1009 O O   . ILE A 1 130 ? -4.94725  -5.98609  55.81953  1.000 58.94029  ? 130 ILE A O   1 
ATOM 1010 C CB  . ILE A 1 130 ? -1.91334  -6.44264  54.36844  1.000 51.77476  ? 130 ILE A CB  1 
ATOM 1011 C CG1 . ILE A 1 130 ? -1.19785  -6.62022  53.04581  1.000 53.33698  ? 130 ILE A CG1 1 
ATOM 1012 C CG2 . ILE A 1 130 ? -2.29770  -7.79960  54.88525  1.000 52.41069  ? 130 ILE A CG2 1 
ATOM 1013 C CD1 . ILE A 1 130 ? 0.20403   -7.18809  53.21928  1.000 50.98805  ? 130 ILE A CD1 1 
ATOM 1014 N N   . GLN A 1 131 ? -3.31812  -4.59488  56.47746  1.000 55.54185  ? 131 GLN A N   1 
ATOM 1015 C CA  . GLN A 1 131 ? -3.98093  -4.47180  57.76219  1.000 56.66433  ? 131 GLN A CA  1 
ATOM 1016 C C   . GLN A 1 131 ? -5.32043  -3.75011  57.64889  1.000 58.67431  ? 131 GLN A C   1 
ATOM 1017 O O   . GLN A 1 131 ? -6.25510  -4.07122  58.39710  1.000 56.13660  ? 131 GLN A O   1 
ATOM 1018 C CB  . GLN A 1 131 ? -3.09062  -3.77325  58.78260  1.000 59.39359  ? 131 GLN A CB  1 
ATOM 1019 C CG  . GLN A 1 131 ? -1.87577  -4.56797  59.18212  1.000 63.25582  ? 131 GLN A CG  1 
ATOM 1020 C CD  . GLN A 1 131 ? -1.41784  -4.22249  60.58727  1.000 62.70857  ? 131 GLN A CD  1 
ATOM 1021 O OE1 . GLN A 1 131 ? -2.04004  -3.41489  61.26895  1.000 64.72048  ? 131 GLN A OE1 1 
ATOM 1022 N NE2 . GLN A 1 131 ? -0.34980  -4.85568  61.03534  1.000 63.86841  ? 131 GLN A NE2 1 
ATOM 1023 N N   . ARG A 1 132 ? -5.44129  -2.77287  56.73677  1.000 57.35369  ? 132 ARG A N   1 
ATOM 1024 C CA  . ARG A 1 132 ? -6.71856  -2.08869  56.61853  1.000 53.19120  ? 132 ARG A CA  1 
ATOM 1025 C C   . ARG A 1 132 ? -7.79048  -3.03695  56.11680  1.000 50.81099  ? 132 ARG A C   1 
ATOM 1026 O O   . ARG A 1 132 ? -8.96697  -2.85608  56.41302  1.000 55.07654  ? 132 ARG A O   1 
ATOM 1027 C CB  . ARG A 1 132 ? -6.59764  -0.87419  55.70402  1.000 51.66862  ? 132 ARG A CB  1 
ATOM 1028 C CG  . ARG A 1 132 ? -5.54602  0.12702   56.14268  1.000 53.24185  ? 132 ARG A CG  1 
ATOM 1029 C CD  . ARG A 1 132 ? -5.58079  1.40423   55.28594  1.000 53.85041  ? 132 ARG A CD  1 
ATOM 1030 N NE  . ARG A 1 132 ? -4.53925  2.37008   55.64120  1.000 53.79198  ? 132 ARG A NE  1 
ATOM 1031 C CZ  . ARG A 1 132 ? -3.39999  2.54222   54.98059  1.000 56.81540  ? 132 ARG A CZ  1 
ATOM 1032 N NH1 . ARG A 1 132 ? -3.18059  1.96414   53.80465  1.000 56.79608  ? 132 ARG A NH1 1 
ATOM 1033 N NH2 . ARG A 1 132 ? -2.46085  3.32330   55.50100  1.000 55.88790  ? 132 ARG A NH2 1 
ATOM 1034 N N   . LEU A 1 133 ? -7.39810  -4.06873  55.39951  1.000 56.19465  ? 133 LEU A N   1 
ATOM 1035 C CA  . LEU A 1 133 ? -8.33159  -5.06796  54.89570  1.000 57.24354  ? 133 LEU A CA  1 
ATOM 1036 C C   . LEU A 1 133 ? -8.82478  -5.98852  56.00735  1.000 54.83915  ? 133 LEU A C   1 
ATOM 1037 O O   . LEU A 1 133 ? -9.99110  -6.39306  56.01262  1.000 54.17986  ? 133 LEU A O   1 
ATOM 1038 C CB  . LEU A 1 133 ? -7.63351  -5.85660  53.77738  1.000 52.76544  ? 133 LEU A CB  1 
ATOM 1039 C CG  . LEU A 1 133 ? -8.39670  -6.95248  53.06589  1.000 54.34228  ? 133 LEU A CG  1 
ATOM 1040 C CD1 . LEU A 1 133 ? -9.64807  -6.34655  52.51195  1.000 55.20152  ? 133 LEU A CD1 1 
ATOM 1041 C CD2 . LEU A 1 133 ? -7.51841  -7.53213  51.95081  1.000 55.44955  ? 133 LEU A CD2 1 
ATOM 1042 N N   . ASN A 1 134 ? -7.95655  -6.30719  56.95503  1.000 52.88544  ? 134 ASN A N   1 
ATOM 1043 C CA  . ASN A 1 134 ? -8.26367  -7.11761  58.11511  1.000 52.04506  ? 134 ASN A CA  1 
ATOM 1044 C C   . ASN A 1 134 ? -9.10463  -6.38888  59.15653  1.000 56.41678  ? 134 ASN A C   1 
ATOM 1045 O O   . ASN A 1 134 ? -9.28555  -6.91307  60.25901  1.000 60.74809  ? 134 ASN A O   1 
ATOM 1046 C CB  . ASN A 1 134 ? -6.94896  -7.60439  58.71785  1.000 54.85879  ? 134 ASN A CB  1 
ATOM 1047 C CG  . ASN A 1 134 ? -6.49411  -8.91906  58.13041  1.000 53.98813  ? 134 ASN A CG  1 
ATOM 1048 O OD1 . ASN A 1 134 ? -7.14706  -9.93310  58.30474  1.000 56.57559  ? 134 ASN A OD1 1 
ATOM 1049 N ND2 . ASN A 1 134 ? -5.44580  -8.88550  57.34329  1.000 56.74080  ? 134 ASN A ND2 1 
ATOM 1050 N N   . GLY A 1 135 ? -9.62566  -5.20792  58.83579  1.000 57.37354  ? 135 GLY A N   1 
ATOM 1051 C CA  . GLY A 1 135 ? -10.46547 -4.46307  59.73921  1.000 52.85249  ? 135 GLY A CA  1 
ATOM 1052 C C   . GLY A 1 135 ? -9.73549  -3.61893  60.74590  1.000 53.28373  ? 135 GLY A C   1 
ATOM 1053 O O   . GLY A 1 135 ? -10.37173 -3.13615  61.68282  1.000 54.31764  ? 135 GLY A O   1 
ATOM 1054 N N   . VAL A 1 136 ? -8.43292  -3.41726  60.58428  1.000 53.18524  ? 136 VAL A N   1 
ATOM 1055 C CA  . VAL A 1 136 ? -7.64943  -2.62326  61.52530  1.000 54.67572  ? 136 VAL A CA  1 
ATOM 1056 C C   . VAL A 1 136 ? -7.86906  -1.13930  61.24183  1.000 62.22073  ? 136 VAL A C   1 
ATOM 1057 O O   . VAL A 1 136 ? -8.03558  -0.73782  60.08203  1.000 64.97558  ? 136 VAL A O   1 
ATOM 1058 C CB  . VAL A 1 136 ? -6.16399  -2.99718  61.41431  1.000 54.63090  ? 136 VAL A CB  1 
ATOM 1059 C CG1 . VAL A 1 136 ? -5.35535  -2.26947  62.44165  1.000 56.26037  ? 136 VAL A CG1 1 
ATOM 1060 C CG2 . VAL A 1 136 ? -5.98796  -4.48395  61.53761  1.000 57.63329  ? 136 VAL A CG2 1 
ATOM 1061 N N   . SER A 1 137 ? -7.87668  -0.30935  62.28988  1.000 60.14793  ? 137 SER A N   1 
ATOM 1062 C CA  . SER A 1 137 ? -8.03489  1.12992   62.12043  1.000 60.33119  ? 137 SER A CA  1 
ATOM 1063 C C   . SER A 1 137 ? -6.67107  1.83888   62.08047  1.000 62.16401  ? 137 SER A C   1 
ATOM 1064 O O   . SER A 1 137 ? -5.63342  1.27977   62.45064  1.000 60.20051  ? 137 SER A O   1 
ATOM 1065 C CB  . SER A 1 137 ? -8.91592  1.70698   63.22991  1.000 66.53652  ? 137 SER A CB  1 
ATOM 1066 O OG  . SER A 1 137 ? -8.28127  1.64185   64.50026  1.000 70.25373  ? 137 SER A OG  1 
ATOM 1067 N N   . GLU A 1 138 ? -6.69131  3.10389   61.63389  1.000 64.37988  ? 138 GLU A N   1 
ATOM 1068 C CA  . GLU A 1 138 ? -5.45657  3.78180   61.22790  1.000 65.16588  ? 138 GLU A CA  1 
ATOM 1069 C C   . GLU A 1 138 ? -4.48282  3.95898   62.38030  1.000 64.67895  ? 138 GLU A C   1 
ATOM 1070 O O   . GLU A 1 138 ? -3.26076  3.81197   62.20002  1.000 63.26445  ? 138 GLU A O   1 
ATOM 1071 C CB  . GLU A 1 138 ? -5.76762  5.14302   60.61345  1.000 66.34671  ? 138 GLU A CB  1 
ATOM 1072 C CG  . GLU A 1 138 ? -6.45727  5.03709   59.29469  1.000 69.97746  ? 138 GLU A CG  1 
ATOM 1073 C CD  . GLU A 1 138 ? -5.59808  4.34149   58.24491  1.000 69.89311  ? 138 GLU A CD  1 
ATOM 1074 O OE1 . GLU A 1 138 ? -4.36595  4.60830   58.16603  1.000 69.19871  ? 138 GLU A OE1 1 
ATOM 1075 O OE2 . GLU A 1 138 ? -6.16806  3.47799   57.53738  1.000 69.54679  ? 138 GLU A OE2 1 
ATOM 1076 N N   . ASN A 1 139 ? -4.99935  4.34524   63.55234  1.000 64.15451  ? 139 ASN A N   1 
ATOM 1077 C CA  . ASN A 1 139 ? -4.18438  4.54918   64.74106  1.000 63.33658  ? 139 ASN A CA  1 
ATOM 1078 C C   . ASN A 1 139 ? -3.68462  3.24063   65.31858  1.000 59.18127  ? 139 ASN A C   1 
ATOM 1079 O O   . ASN A 1 139 ? -2.81823  3.25205   66.19630  1.000 57.62108  ? 139 ASN A O   1 
ATOM 1080 C CB  . ASN A 1 139 ? -4.99019  5.33144   65.76417  1.000 68.37712  ? 139 ASN A CB  1 
ATOM 1081 C CG  . ASN A 1 139 ? -6.29237  4.65417   66.10963  1.000 72.41549  ? 139 ASN A CG  1 
ATOM 1082 O OD1 . ASN A 1 139 ? -6.54991  3.50502   65.70900  1.000 71.94518  ? 139 ASN A OD1 1 
ATOM 1083 N ND2 . ASN A 1 139 ? -7.13908  5.36828   66.84093  1.000 71.16977  ? 139 ASN A ND2 1 
ATOM 1084 N N   . GLU A 1 140 ? -4.18970  2.12827   64.81135  1.000 59.57066  ? 140 GLU A N   1 
ATOM 1085 C CA  . GLU A 1 140 ? -3.72453  0.80940   65.17698  1.000 64.23795  ? 140 GLU A CA  1 
ATOM 1086 C C   . GLU A 1 140 ? -2.95787  0.08801   64.07147  1.000 63.81988  ? 140 GLU A C   1 
ATOM 1087 O O   . GLU A 1 140 ? -2.55539  -1.05895  64.27887  1.000 63.55345  ? 140 GLU A O   1 
ATOM 1088 C CB  . GLU A 1 140 ? -4.91845  -0.03297  65.60018  1.000 64.15989  ? 140 GLU A CB  1 
ATOM 1089 C CG  . GLU A 1 140 ? -5.55601  0.47559   66.84984  1.000 70.35175  ? 140 GLU A CG  1 
ATOM 1090 C CD  . GLU A 1 140 ? -6.85104  -0.23775  67.15581  1.000 81.61602  ? 140 GLU A CD  1 
ATOM 1091 O OE1 . GLU A 1 140 ? -7.35456  -0.96954  66.25744  1.000 81.04347  ? 140 GLU A OE1 1 
ATOM 1092 O OE2 . GLU A 1 140 ? -7.35197  -0.07874  68.29757  1.000 81.80012  ? 140 GLU A OE2 1 
ATOM 1093 N N   . LEU A 1 141 ? -2.74847  0.69436   62.90534  1.000 61.80003  ? 141 LEU A N   1 
ATOM 1094 C CA  . LEU A 1 141 ? -1.94337  0.01132   61.89731  1.000 65.46960  ? 141 LEU A CA  1 
ATOM 1095 C C   . LEU A 1 141 ? -0.55910  -0.24392  62.46102  1.000 65.19787  ? 141 LEU A C   1 
ATOM 1096 O O   . LEU A 1 141 ? 0.01961   0.61211   63.12979  1.000 68.36424  ? 141 LEU A O   1 
ATOM 1097 C CB  . LEU A 1 141 ? -1.84159  0.82170   60.60144  1.000 63.42393  ? 141 LEU A CB  1 
ATOM 1098 C CG  . LEU A 1 141 ? -3.18222  1.01874   59.90585  1.000 58.41683  ? 141 LEU A CG  1 
ATOM 1099 C CD1 . LEU A 1 141 ? -3.00887  1.95475   58.79077  1.000 56.30624  ? 141 LEU A CD1 1 
ATOM 1100 C CD2 . LEU A 1 141 ? -3.74278  -0.29374  59.43487  1.000 57.50212  ? 141 LEU A CD2 1 
ATOM 1101 N N   . ASP A 1 142 ? -0.05404  -1.45006  62.23592  1.000 65.08911  ? 142 ASP A N   1 
ATOM 1102 C CA  . ASP A 1 142 ? 1.26804   -1.81406  62.73398  1.000 67.59619  ? 142 ASP A CA  1 
ATOM 1103 C C   . ASP A 1 142 ? 1.82699   -2.93756  61.87535  1.000 65.22804  ? 142 ASP A C   1 
ATOM 1104 O O   . ASP A 1 142 ? 1.40676   -4.08928  62.01614  1.000 63.55276  ? 142 ASP A O   1 
ATOM 1105 C CB  . ASP A 1 142 ? 1.21000   -2.22336  64.19265  1.000 68.42349  ? 142 ASP A CB  1 
ATOM 1106 C CG  . ASP A 1 142 ? 2.51904   -2.83214  64.66542  1.000 72.56625  ? 142 ASP A CG  1 
ATOM 1107 O OD1 . ASP A 1 142 ? 3.53865   -2.10490  64.75554  1.000 77.12606  ? 142 ASP A OD1 1 
ATOM 1108 O OD2 . ASP A 1 142 ? 2.53174   -4.05146  64.93370  1.000 70.81746  ? 142 ASP A OD2 1 
ATOM 1109 N N   . THR A 1 143 ? 2.80207   -2.60612  61.03142  1.000 60.67436  ? 143 THR A N   1 
ATOM 1110 C CA  . THR A 1 143 ? 3.29148   -3.50956  60.00046  1.000 61.31172  ? 143 THR A CA  1 
ATOM 1111 C C   . THR A 1 143 ? 4.71806   -3.97440  60.25910  1.000 59.97363  ? 143 THR A C   1 
ATOM 1112 O O   . THR A 1 143 ? 5.39116   -4.39647  59.32470  1.000 58.71243  ? 143 THR A O   1 
ATOM 1113 C CB  . THR A 1 143 ? 3.20179   -2.84974  58.61436  1.000 59.80635  ? 143 THR A CB  1 
ATOM 1114 O OG1 . THR A 1 143 ? 3.96819   -1.63539  58.58180  1.000 58.09290  ? 143 THR A OG1 1 
ATOM 1115 C CG2 . THR A 1 143 ? 1.76341   -2.53961  58.24187  1.000 58.99158  ? 143 THR A CG2 1 
ATOM 1116 N N   . PHE A 1 144 ? 5.18453   -3.92651  61.50711  1.000 60.70334  ? 144 PHE A N   1 
ATOM 1117 C CA  . PHE A 1 144 ? 6.58950   -4.20317  61.78865  1.000 56.97795  ? 144 PHE A CA  1 
ATOM 1118 C C   . PHE A 1 144 ? 7.00185   -5.58666  61.30655  1.000 64.68181  ? 144 PHE A C   1 
ATOM 1119 O O   . PHE A 1 144 ? 8.03701   -5.74891  60.64277  1.000 65.28323  ? 144 PHE A O   1 
ATOM 1120 C CB  . PHE A 1 144 ? 6.83058   -4.09282  63.27884  1.000 61.00998  ? 144 PHE A CB  1 
ATOM 1121 C CG  . PHE A 1 144 ? 8.23564   -4.35481  63.68077  1.000 60.32221  ? 144 PHE A CG  1 
ATOM 1122 C CD1 . PHE A 1 144 ? 9.18795   -3.35285  63.59086  1.000 55.74613  ? 144 PHE A CD1 1 
ATOM 1123 C CD2 . PHE A 1 144 ? 8.60695   -5.61023  64.16399  1.000 62.45800  ? 144 PHE A CD2 1 
ATOM 1124 C CE1 . PHE A 1 144 ? 10.48910  -3.59433  63.97449  1.000 58.16784  ? 144 PHE A CE1 1 
ATOM 1125 C CE2 . PHE A 1 144 ? 9.90575   -5.86900  64.54478  1.000 60.78651  ? 144 PHE A CE2 1 
ATOM 1126 C CZ  . PHE A 1 144 ? 10.85106  -4.86441  64.45837  1.000 60.25341  ? 144 PHE A CZ  1 
ATOM 1127 N N   . LYS A 1 145 ? 6.20904   -6.60285  61.64103  1.000 69.71909  ? 145 LYS A N   1 
ATOM 1128 C CA  . LYS A 1 145 ? 6.54636   -7.98165  61.31734  1.000 69.52379  ? 145 LYS A CA  1 
ATOM 1129 C C   . LYS A 1 145 ? 6.20410   -8.33852  59.88474  1.000 70.10966  ? 145 LYS A C   1 
ATOM 1130 O O   . LYS A 1 145 ? 6.52064   -9.45148  59.45399  1.000 71.19047  ? 145 LYS A O   1 
ATOM 1131 C CB  . LYS A 1 145 ? 5.81001   -8.94722  62.24875  1.000 71.21138  ? 145 LYS A CB  1 
ATOM 1132 C CG  . LYS A 1 145 ? 5.96816   -8.68253  63.76216  1.000 76.10904  ? 145 LYS A CG  1 
ATOM 1133 C CD  . LYS A 1 145 ? 7.35516   -8.99393  64.31326  1.000 78.83475  ? 145 LYS A CD  1 
ATOM 1134 C CE  . LYS A 1 145 ? 7.32648   -8.90107  65.84946  1.000 80.11091  ? 145 LYS A CE  1 
ATOM 1135 N NZ  . LYS A 1 145 ? 8.62734   -9.23396  66.51878  1.000 76.86385  ? 145 LYS A NZ  1 
ATOM 1136 N N   . LEU A 1 146 ? 5.54474   -7.43760  59.14788  1.000 64.32683  ? 146 LEU A N   1 
ATOM 1137 C CA  . LEU A 1 146 ? 5.17431   -7.66154  57.75231  1.000 56.78442  ? 146 LEU A CA  1 
ATOM 1138 C C   . LEU A 1 146 ? 6.17006   -7.08988  56.75860  1.000 55.28948  ? 146 LEU A C   1 
ATOM 1139 O O   . LEU A 1 146 ? 6.21403   -7.55312  55.62145  1.000 61.39972  ? 146 LEU A O   1 
ATOM 1140 C CB  . LEU A 1 146 ? 3.81026   -7.04346  57.45583  1.000 57.01068  ? 146 LEU A CB  1 
ATOM 1141 C CG  . LEU A 1 146 ? 2.61681   -7.61304  58.20357  1.000 57.04285  ? 146 LEU A CG  1 
ATOM 1142 C CD1 . LEU A 1 146 ? 1.36439   -6.79807  57.90703  1.000 53.87770  ? 146 LEU A CD1 1 
ATOM 1143 C CD2 . LEU A 1 146 ? 2.43651   -9.06276  57.83075  1.000 55.82054  ? 146 LEU A CD2 1 
ATOM 1144 N N   . GLU A 1 147 ? 6.96213   -6.11022  57.14807  1.000 56.98808  ? 147 GLU A N   1 
ATOM 1145 C CA  . GLU A 1 147 ? 7.80245   -5.41711  56.19567  1.000 52.77347  ? 147 GLU A CA  1 
ATOM 1146 C C   . GLU A 1 147 ? 8.96303   -6.30885  55.76075  1.000 56.44523  ? 147 GLU A C   1 
ATOM 1147 O O   . GLU A 1 147 ? 9.46903   -7.10043  56.56708  1.000 55.92414  ? 147 GLU A O   1 
ATOM 1148 C CB  . GLU A 1 147 ? 8.29059   -4.12658  56.82332  1.000 53.20094  ? 147 GLU A CB  1 
ATOM 1149 C CG  . GLU A 1 147 ? 7.11078   -3.22562  57.08496  1.000 55.37198  ? 147 GLU A CG  1 
ATOM 1150 C CD  . GLU A 1 147 ? 7.41738   -1.90795  57.78161  1.000 56.97480  ? 147 GLU A CD  1 
ATOM 1151 O OE1 . GLU A 1 147 ? 8.59771   -1.59279  58.09596  1.000 55.57951  ? 147 GLU A OE1 1 
ATOM 1152 O OE2 . GLU A 1 147 ? 6.42114   -1.20278  58.05526  1.000 56.15538  ? 147 GLU A OE2 1 
ATOM 1153 N N   . PRO A 1 148 ? 9.38588   -6.23097  54.48540  1.000 59.84249  ? 148 PRO A N   1 
ATOM 1154 C CA  . PRO A 1 148 ? 10.44884  -7.13735  53.99983  1.000 59.26535  ? 148 PRO A CA  1 
ATOM 1155 C C   . PRO A 1 148 ? 11.77928  -6.92778  54.69029  1.000 59.56215  ? 148 PRO A C   1 
ATOM 1156 O O   . PRO A 1 148 ? 12.63260  -7.82052  54.65752  1.000 60.23269  ? 148 PRO A O   1 
ATOM 1157 C CB  . PRO A 1 148 ? 10.54138  -6.80779  52.50869  1.000 56.61872  ? 148 PRO A CB  1 
ATOM 1158 C CG  . PRO A 1 148 ? 10.09470  -5.38967  52.41924  1.000 56.15967  ? 148 PRO A CG  1 
ATOM 1159 C CD  . PRO A 1 148 ? 9.01118   -5.24185  53.45913  1.000 58.12407  ? 148 PRO A CD  1 
ATOM 1160 N N   . CYS A 1 149 ? 11.97874  -5.78314  55.32783  1.000 53.60388  ? 149 CYS A N   1 
ATOM 1161 C CA  . CYS A 1 149 ? 13.15412  -5.57340  56.14301  1.000 53.87130  ? 149 CYS A CA  1 
ATOM 1162 C C   . CYS A 1 149 ? 12.81004  -4.55014  57.21709  1.000 56.05355  ? 149 CYS A C   1 
ATOM 1163 O O   . CYS A 1 149 ? 11.96439  -3.67530  57.01111  1.000 53.27743  ? 149 CYS A O   1 
ATOM 1164 C CB  . CYS A 1 149 ? 14.32563  -5.09024  55.29397  1.000 53.60035  ? 149 CYS A CB  1 
ATOM 1165 S SG  . CYS A 1 149 ? 14.04291  -3.42321  54.58924  1.000 54.48828  ? 149 CYS A SG  1 
ATOM 1166 N N   . LYS A 1 150 ? 13.49522  -4.64547  58.35430  1.000 56.30229  ? 150 LYS A N   1 
ATOM 1167 C CA  . LYS A 1 150 ? 13.28922  -3.66799  59.40936  1.000 56.07722  ? 150 LYS A CA  1 
ATOM 1168 C C   . LYS A 1 150 ? 13.69292  -2.27843  58.92455  1.000 53.98386  ? 150 LYS A C   1 
ATOM 1169 O O   . LYS A 1 150 ? 14.65799  -2.11883  58.18174  1.000 52.35738  ? 150 LYS A O   1 
ATOM 1170 C CB  . LYS A 1 150 ? 14.07327  -4.07570  60.65631  1.000 55.41975  ? 150 LYS A CB  1 
ATOM 1171 C CG  . LYS A 1 150 ? 13.67104  -5.44968  61.11594  1.000 56.52257  ? 150 LYS A CG  1 
ATOM 1172 C CD  . LYS A 1 150 ? 12.17240  -5.45193  61.26148  1.000 58.01510  ? 150 LYS A CD  1 
ATOM 1173 C CE  . LYS A 1 150 ? 11.68636  -6.77216  61.69815  1.000 61.53110  ? 150 LYS A CE  1 
ATOM 1174 N NZ  . LYS A 1 150 ? 11.91820  -7.70544  60.59193  1.000 67.60960  ? 150 LYS A NZ  1 
ATOM 1175 N N   . PHE A 1 151 ? 12.94974  -1.26324  59.36275  1.000 56.80390  ? 151 PHE A N   1 
ATOM 1176 C CA  . PHE A 1 151 ? 13.13133  0.07978   58.82283  1.000 55.14409  ? 151 PHE A CA  1 
ATOM 1177 C C   . PHE A 1 151 ? 14.55367  0.60568   58.99094  1.000 55.02783  ? 151 PHE A C   1 
ATOM 1178 O O   . PHE A 1 151 ? 14.96795  1.48513   58.22906  1.000 56.88669  ? 151 PHE A O   1 
ATOM 1179 C CB  . PHE A 1 151 ? 12.12525  1.04713   59.46007  1.000 54.78561  ? 151 PHE A CB  1 
ATOM 1180 C CG  . PHE A 1 151 ? 12.21743  1.12237   60.94543  1.000 55.89199  ? 151 PHE A CG  1 
ATOM 1181 C CD1 . PHE A 1 151 ? 11.37937  0.35410   61.73707  1.000 59.87582  ? 151 PHE A CD1 1 
ATOM 1182 C CD2 . PHE A 1 151 ? 13.15088  1.94166   61.56210  1.000 58.45939  ? 151 PHE A CD2 1 
ATOM 1183 C CE1 . PHE A 1 151 ? 11.45713  0.40346   63.13675  1.000 61.91067  ? 151 PHE A CE1 1 
ATOM 1184 C CE2 . PHE A 1 151 ? 13.24053  1.99412   62.96572  1.000 64.80756  ? 151 PHE A CE2 1 
ATOM 1185 C CZ  . PHE A 1 151 ? 12.38791  1.21905   63.75451  1.000 60.61618  ? 151 PHE A CZ  1 
ATOM 1186 N N   . TRP A 1 152 ? 15.30980  0.10934   59.96229  1.000 55.95862  ? 152 TRP A N   1 
ATOM 1187 C CA  . TRP A 1 152 ? 16.67102  0.59985   60.12873  1.000 56.29678  ? 152 TRP A CA  1 
ATOM 1188 C C   . TRP A 1 152 ? 17.65142  -0.09575  59.21300  1.000 51.02858  ? 152 TRP A C   1 
ATOM 1189 O O   . TRP A 1 152 ? 18.80210  0.33789   59.13220  1.000 50.38014  ? 152 TRP A O   1 
ATOM 1190 C CB  . TRP A 1 152 ? 17.13105  0.43720   61.58833  1.000 57.55249  ? 152 TRP A CB  1 
ATOM 1191 C CG  . TRP A 1 152 ? 17.10344  -0.97788  62.10271  1.000 52.24209  ? 152 TRP A CG  1 
ATOM 1192 C CD1 . TRP A 1 152 ? 18.09770  -1.90131  62.01367  1.000 52.33445  ? 152 TRP A CD1 1 
ATOM 1193 C CD2 . TRP A 1 152 ? 16.02669  -1.61490  62.78682  1.000 55.95401  ? 152 TRP A CD2 1 
ATOM 1194 N NE1 . TRP A 1 152 ? 17.70956  -3.07902  62.58335  1.000 53.50824  ? 152 TRP A NE1 1 
ATOM 1195 C CE2 . TRP A 1 152 ? 16.44056  -2.93082  63.07735  1.000 58.14877  ? 152 TRP A CE2 1 
ATOM 1196 C CE3 . TRP A 1 152 ? 14.74816  -1.19895  63.19339  1.000 59.31695  ? 152 TRP A CE3 1 
ATOM 1197 C CZ2 . TRP A 1 152 ? 15.62168  -3.84276  63.75626  1.000 60.20564  ? 152 TRP A CZ2 1 
ATOM 1198 C CZ3 . TRP A 1 152 ? 13.92939  -2.10540  63.86235  1.000 59.38250  ? 152 TRP A CZ3 1 
ATOM 1199 C CH2 . TRP A 1 152 ? 14.37689  -3.41373  64.14337  1.000 60.70939  ? 152 TRP A CH2 1 
ATOM 1200 N N   . ASN A 1 153 ? 17.23503  -1.19012  58.57878  1.000 57.11734  ? 153 ASN A N   1 
ATOM 1201 C CA  . ASN A 1 153 ? 18.01824  -1.90319  57.57313  1.000 59.43824  ? 153 ASN A CA  1 
ATOM 1202 C C   . ASN A 1 153 ? 17.72143  -1.45187  56.14370  1.000 58.58536  ? 153 ASN A C   1 
ATOM 1203 O O   . ASN A 1 153 ? 18.10939  -2.14319  55.20036  1.000 59.36335  ? 153 ASN A O   1 
ATOM 1204 C CB  . ASN A 1 153 ? 17.77828  -3.40622  57.65830  1.000 58.98264  ? 153 ASN A CB  1 
ATOM 1205 C CG  . ASN A 1 153 ? 18.46769  -4.02352  58.81867  1.000 58.69013  ? 153 ASN A CG  1 
ATOM 1206 O OD1 . ASN A 1 153 ? 19.47393  -3.49361  59.29279  1.000 56.52787  ? 153 ASN A OD1 1 
ATOM 1207 N ND2 . ASN A 1 153 ? 18.00666  -5.21411  59.22141  1.000 60.53688  ? 153 ASN A ND2 1 
ATOM 1208 N N   . GLN A 1 154 ? 16.98797  -0.35534  55.98123  1.000 53.82744  ? 154 GLN A N   1 
ATOM 1209 C CA  . GLN A 1 154 ? 16.77968  0.31695   54.72274  1.000 50.87688  ? 154 GLN A CA  1 
ATOM 1210 C C   . GLN A 1 154 ? 18.03579  1.09190   54.34769  1.000 55.09876  ? 154 GLN A C   1 
ATOM 1211 O O   . GLN A 1 154 ? 18.85477  1.43661   55.20655  1.000 51.13486  ? 154 GLN A O   1 
ATOM 1212 C CB  . GLN A 1 154 ? 15.59157  1.25761   54.82214  1.000 50.59938  ? 154 GLN A CB  1 
ATOM 1213 C CG  . GLN A 1 154 ? 14.25864  0.61249   55.05089  1.000 47.91405  ? 154 GLN A CG  1 
ATOM 1214 C CD  . GLN A 1 154 ? 13.14382  1.63142   55.01959  1.000 51.81554  ? 154 GLN A CD  1 
ATOM 1215 O OE1 . GLN A 1 154 ? 13.38702  2.82660   54.88391  1.000 55.65334  ? 154 GLN A OE1 1 
ATOM 1216 N NE2 . GLN A 1 154 ? 11.91560  1.16860   55.11459  1.000 51.25287  ? 154 GLN A NE2 1 
ATOM 1217 N N   . ARG A 1 155 ? 18.19517  1.34439   53.04062  1.000 56.50258  ? 155 ARG A N   1 
ATOM 1218 C CA  . ARG A 1 155 ? 19.42683  1.91823   52.50782  1.000 51.21690  ? 155 ARG A CA  1 
ATOM 1219 C C   . ARG A 1 155 ? 19.15441  2.72090   51.25240  1.000 49.60357  ? 155 ARG A C   1 
ATOM 1220 O O   . ARG A 1 155 ? 18.38944  2.28493   50.39534  1.000 52.10896  ? 155 ARG A O   1 
ATOM 1221 C CB  . ARG A 1 155 ? 20.43280  0.83775   52.18285  1.000 51.98725  ? 155 ARG A CB  1 
ATOM 1222 C CG  . ARG A 1 155 ? 21.00559  0.14986   53.34699  1.000 54.76244  ? 155 ARG A CG  1 
ATOM 1223 C CD  . ARG A 1 155 ? 21.76387  1.15260   54.14557  1.000 54.55144  ? 155 ARG A CD  1 
ATOM 1224 N NE  . ARG A 1 155 ? 22.45794  0.51452   55.24281  1.000 57.04515  ? 155 ARG A NE  1 
ATOM 1225 C CZ  . ARG A 1 155 ? 21.86503  0.21202   56.38130  1.000 58.29215  ? 155 ARG A CZ  1 
ATOM 1226 N NH1 . ARG A 1 155 ? 20.56904  0.40159   56.54442  1.000 54.42418  ? 155 ARG A NH1 1 
ATOM 1227 N NH2 . ARG A 1 155 ? 22.58546  -0.31188  57.36895  1.000 61.87770  ? 155 ARG A NH2 1 
ATOM 1228 N N   . ASP A 1 156 ? 19.80171  3.87889   51.13932  1.000 53.27213  ? 156 ASP A N   1 
ATOM 1229 C CA  . ASP A 1 156 ? 19.60691  4.79055   50.01252  1.000 54.12764  ? 156 ASP A CA  1 
ATOM 1230 C C   . ASP A 1 156 ? 20.71986  4.58856   48.99642  1.000 54.50601  ? 156 ASP A C   1 
ATOM 1231 O O   . ASP A 1 156 ? 21.90187  4.61016   49.35601  1.000 53.78219  ? 156 ASP A O   1 
ATOM 1232 C CB  . ASP A 1 156 ? 19.58675  6.24972   50.46423  1.000 53.98832  ? 156 ASP A CB  1 
ATOM 1233 C CG  . ASP A 1 156 ? 19.25592  7.20984   49.33039  1.000 56.55111  ? 156 ASP A CG  1 
ATOM 1234 O OD1 . ASP A 1 156 ? 18.10878  7.15031   48.82733  1.000 57.67408  ? 156 ASP A OD1 1 
ATOM 1235 O OD2 . ASP A 1 156 ? 20.11784  8.05348   48.98039  1.000 54.31395  ? 156 ASP A OD2 1 
ATOM 1236 N N   . ILE A 1 157 ? 20.34242  4.39298   47.73129  1.000 50.91429  ? 157 ILE A N   1 
ATOM 1237 C CA  . ILE A 1 157 ? 21.35393  4.08598   46.72902  1.000 57.47405  ? 157 ILE A CA  1 
ATOM 1238 C C   . ILE A 1 157 ? 22.22944  5.30527   46.44906  1.000 56.43373  ? 157 ILE A C   1 
ATOM 1239 O O   . ILE A 1 157 ? 23.45776  5.18081   46.38542  1.000 58.20201  ? 157 ILE A O   1 
ATOM 1240 C CB  . ILE A 1 157 ? 20.70877  3.50602   45.45127  1.000 60.18758  ? 157 ILE A CB  1 
ATOM 1241 C CG1 . ILE A 1 157 ? 20.22056  2.06534   45.71285  1.000 52.57211  ? 157 ILE A CG1 1 
ATOM 1242 C CG2 . ILE A 1 157 ? 21.68452  3.56951   44.26646  1.000 56.33431  ? 157 ILE A CG2 1 
ATOM 1243 C CD1 . ILE A 1 157 ? 19.29972  1.52409   44.64468  1.000 50.84172  ? 157 ILE A CD1 1 
ATOM 1244 N N   . ARG A 1 158 ? 21.62992  6.50266   46.33109  1.000 54.54153  ? 158 ARG A N   1 
ATOM 1245 C CA  . ARG A 1 158 ? 22.41942  7.70398   46.04266  1.000 57.66664  ? 158 ARG A CA  1 
ATOM 1246 C C   . ARG A 1 158 ? 23.42323  7.98548   47.15612  1.000 56.24508  ? 158 ARG A C   1 
ATOM 1247 O O   . ARG A 1 158 ? 24.55089  8.41623   46.89577  1.000 58.53467  ? 158 ARG A O   1 
ATOM 1248 C CB  . ARG A 1 158 ? 21.51933  8.92712   45.84336  1.000 55.20574  ? 158 ARG A CB  1 
ATOM 1249 C CG  . ARG A 1 158 ? 20.47621  8.79368   44.76824  1.000 52.91622  ? 158 ARG A CG  1 
ATOM 1250 C CD  . ARG A 1 158 ? 19.72706  10.09535  44.57103  1.000 52.79597  ? 158 ARG A CD  1 
ATOM 1251 N NE  . ARG A 1 158 ? 18.62092  9.96665   43.62540  1.000 56.70106  ? 158 ARG A NE  1 
ATOM 1252 C CZ  . ARG A 1 158 ? 17.33293  9.87726   43.94343  1.000 59.91866  ? 158 ARG A CZ  1 
ATOM 1253 N NH1 . ARG A 1 158 ? 16.90939  10.03643  45.18871  1.000 65.20382  ? 158 ARG A NH1 1 
ATOM 1254 N NH2 . ARG A 1 158 ? 16.44117  9.65161   42.98209  1.000 60.60315  ? 158 ARG A NH2 1 
ATOM 1255 N N   . THR A 1 159 ? 23.02872  7.76831   48.40492  1.000 57.53242  ? 159 THR A N   1 
ATOM 1256 C CA  . THR A 1 159 ? 23.96807  7.94878   49.51081  1.000 59.76756  ? 159 THR A CA  1 
ATOM 1257 C C   . THR A 1 159 ? 25.10222  6.93073   49.42007  1.000 58.08408  ? 159 THR A C   1 
ATOM 1258 O O   . THR A 1 159 ? 26.27441  7.27414   49.60992  1.000 58.91110  ? 159 THR A O   1 
ATOM 1259 C CB  . THR A 1 159 ? 23.22046  7.83770   50.85233  1.000 55.69150  ? 159 THR A CB  1 
ATOM 1260 O OG1 . THR A 1 159 ? 22.05171  8.65512   50.80727  1.000 54.45992  ? 159 THR A OG1 1 
ATOM 1261 C CG2 . THR A 1 159 ? 24.07346  8.34094   51.99263  1.000 55.52661  ? 159 THR A CG2 1 
ATOM 1262 N N   . ARG A 1 160 ? 24.75761  5.68094   49.09148  1.000 59.31266  ? 160 ARG A N   1 
ATOM 1263 C CA  . ARG A 1 160 ? 25.71512  4.58034   49.00938  1.000 57.76338  ? 160 ARG A CA  1 
ATOM 1264 C C   . ARG A 1 160 ? 26.80716  4.87484   47.99839  1.000 60.39433  ? 160 ARG A C   1 
ATOM 1265 O O   . ARG A 1 160 ? 27.99261  4.95723   48.34268  1.000 61.47748  ? 160 ARG A O   1 
ATOM 1266 C CB  . ARG A 1 160 ? 24.96619  3.30565   48.62224  1.000 54.62697  ? 160 ARG A CB  1 
ATOM 1267 C CG  . ARG A 1 160 ? 25.78232  2.06000   48.51987  1.000 49.76419  ? 160 ARG A CG  1 
ATOM 1268 C CD  . ARG A 1 160 ? 26.38750  1.72731   49.81868  1.000 48.15708  ? 160 ARG A CD  1 
ATOM 1269 N NE  . ARG A 1 160 ? 26.95225  0.39501   49.78912  1.000 51.16952  ? 160 ARG A NE  1 
ATOM 1270 C CZ  . ARG A 1 160 ? 27.73061  -0.09942  50.73521  1.000 56.63575  ? 160 ARG A CZ  1 
ATOM 1271 N NH1 . ARG A 1 160 ? 28.06504  0.62072   51.79342  1.000 63.72251  ? 160 ARG A NH1 1 
ATOM 1272 N NH2 . ARG A 1 160 ? 28.18287  -1.34791  50.61958  1.000 55.99044  ? 160 ARG A NH2 1 
ATOM 1273 N N   . ILE A 1 161 ? 26.40997  5.04588   46.73616  1.000 60.80077  ? 161 ILE A N   1 
ATOM 1274 C CA  . ILE A 1 161 ? 27.36677  5.27748   45.65830  1.000 62.39880  ? 161 ILE A CA  1 
ATOM 1275 C C   . ILE A 1 161 ? 28.18083  6.53341   45.92205  1.000 65.13044  ? 161 ILE A C   1 
ATOM 1276 O O   . ILE A 1 161 ? 29.41144  6.52956   45.78393  1.000 66.02625  ? 161 ILE A O   1 
ATOM 1277 C CB  . ILE A 1 161 ? 26.63749  5.35770   44.31448  1.000 58.35886  ? 161 ILE A CB  1 
ATOM 1278 C CG1 . ILE A 1 161 ? 26.06661  3.98664   43.97855  1.000 57.78801  ? 161 ILE A CG1 1 
ATOM 1279 C CG2 . ILE A 1 161 ? 27.58272  5.84596   43.27463  1.000 65.23275  ? 161 ILE A CG2 1 
ATOM 1280 C CD1 . ILE A 1 161 ? 25.08210  4.01966   42.85804  1.000 61.85011  ? 161 ILE A CD1 1 
ATOM 1281 N N   . GLU A 1 162 ? 27.50566  7.62356   46.32314  1.000 63.41401  ? 162 GLU A N   1 
ATOM 1282 C CA  . GLU A 1 162 ? 28.20840  8.86695   46.61750  1.000 60.43298  ? 162 GLU A CA  1 
ATOM 1283 C C   . GLU A 1 162 ? 29.19623  8.69224   47.75575  1.000 62.04884  ? 162 GLU A C   1 
ATOM 1284 O O   . GLU A 1 162 ? 30.23774  9.35114   47.76670  1.000 64.26193  ? 162 GLU A O   1 
ATOM 1285 C CB  . GLU A 1 162 ? 27.22188  9.98798   46.94387  1.000 60.35014  ? 162 GLU A CB  1 
ATOM 1286 C CG  . GLU A 1 162 ? 27.89256  11.33449  47.27292  1.000 62.86472  ? 162 GLU A CG  1 
ATOM 1287 C CD  . GLU A 1 162 ? 26.90924  12.48183  47.63251  1.000 67.94715  ? 162 GLU A CD  1 
ATOM 1288 O OE1 . GLU A 1 162 ? 25.67457  12.28066  47.71728  1.000 64.93535  ? 162 GLU A OE1 1 
ATOM 1289 O OE2 . GLU A 1 162 ? 27.38899  13.62063  47.82120  1.000 71.20425  ? 162 GLU A OE2 1 
ATOM 1290 N N   . ALA A 1 163 ? 28.89983  7.82536   48.72313  1.000 63.98007  ? 163 ALA A N   1 
ATOM 1291 C CA  . ALA A 1 163 ? 29.83041  7.63484   49.83074  1.000 65.76005  ? 163 ALA A CA  1 
ATOM 1292 C C   . ALA A 1 163 ? 30.86907  6.56062   49.55185  1.000 68.70458  ? 163 ALA A C   1 
ATOM 1293 O O   . ALA A 1 163 ? 31.91662  6.54029   50.21366  1.000 69.96663  ? 163 ALA A O   1 
ATOM 1294 C CB  . ALA A 1 163 ? 29.08384  7.28945   51.12024  1.000 65.28672  ? 163 ALA A CB  1 
ATOM 1295 N N   . LEU A 1 164 ? 30.60041  5.66008   48.60453  1.000 69.11931  ? 164 LEU A N   1 
ATOM 1296 C CA  . LEU A 1 164 ? 31.62530  4.70624   48.20920  1.000 68.26621  ? 164 LEU A CA  1 
ATOM 1297 C C   . LEU A 1 164 ? 32.67090  5.35239   47.31613  1.000 70.12340  ? 164 LEU A C   1 
ATOM 1298 O O   . LEU A 1 164 ? 33.86353  5.05942   47.45456  1.000 72.53471  ? 164 LEU A O   1 
ATOM 1299 C CB  . LEU A 1 164 ? 30.99473  3.50010   47.51854  1.000 68.24180  ? 164 LEU A CB  1 
ATOM 1300 C CG  . LEU A 1 164 ? 30.29745  2.55529   48.50099  1.000 68.45420  ? 164 LEU A CG  1 
ATOM 1301 C CD1 . LEU A 1 164 ? 29.51263  1.47748   47.77342  1.000 68.44619  ? 164 LEU A CD1 1 
ATOM 1302 C CD2 . LEU A 1 164 ? 31.30484  1.93665   49.47074  1.000 66.34903  ? 164 LEU A CD2 1 
ATOM 1303 N N   . LEU A 1 165 ? 32.25265  6.24257   46.41140  1.000 68.71293  ? 165 LEU A N   1 
ATOM 1304 C CA  . LEU A 1 165 ? 33.18645  6.89438   45.49952  1.000 65.88427  ? 165 LEU A CA  1 
ATOM 1305 C C   . LEU A 1 165 ? 33.81629  8.14883   46.09371  1.000 65.20521  ? 165 LEU A C   1 
ATOM 1306 O O   . LEU A 1 165 ? 34.75084  8.68263   45.50695  1.000 69.90670  ? 165 LEU A O   1 
ATOM 1307 C CB  . LEU A 1 165 ? 32.49248  7.24176   44.17034  1.000 62.81945  ? 165 LEU A CB  1 
ATOM 1308 C CG  . LEU A 1 165 ? 31.92856  6.06631   43.33632  1.000 67.28057  ? 165 LEU A CG  1 
ATOM 1309 C CD1 . LEU A 1 165 ? 31.14374  6.52071   42.10881  1.000 68.60555  ? 165 LEU A CD1 1 
ATOM 1310 C CD2 . LEU A 1 165 ? 32.98215  5.05624   42.92063  1.000 66.16949  ? 165 LEU A CD2 1 
ATOM 1311 N N   . LEU A 1 166 ? 33.35503  8.61772   47.24570  1.000 64.74613  ? 166 LEU A N   1 
ATOM 1312 C CA  . LEU A 1 166 ? 33.87031  9.84390   47.86872  1.000 65.04723  ? 166 LEU A CA  1 
ATOM 1313 C C   . LEU A 1 166 ? 33.86361  11.03259  46.90270  1.000 63.68504  ? 166 LEU A C   1 
ATOM 1314 O O   . LEU A 1 166 ? 34.82717  11.79640  46.82992  1.000 65.70412  ? 166 LEU A O   1 
ATOM 1315 C CB  . LEU A 1 166 ? 35.27894  9.64946   48.43497  1.000 65.16443  ? 166 LEU A CB  1 
ATOM 1316 C CG  . LEU A 1 166 ? 35.54254  8.84155   49.71314  1.000 73.17154  ? 166 LEU A CG  1 
ATOM 1317 C CD1 . LEU A 1 166 ? 34.60131  9.23980   50.86235  1.000 71.84403  ? 166 LEU A CD1 1 
ATOM 1318 C CD2 . LEU A 1 166 ? 35.53890  7.32871   49.46423  1.000 76.46395  ? 166 LEU A CD2 1 
ATOM 1319 N N   . VAL A 1 167 ? 32.77103  11.20742  46.15786  1.000 61.86136  ? 167 VAL A N   1 
ATOM 1320 C CA  . VAL A 1 167 ? 32.61515  12.36116  45.27198  1.000 63.65460  ? 167 VAL A CA  1 
ATOM 1321 C C   . VAL A 1 167 ? 31.21174  12.94135  45.39883  1.000 61.97682  ? 167 VAL A C   1 
ATOM 1322 O O   . VAL A 1 167 ? 30.22157  12.23743  45.18538  1.000 65.34126  ? 167 VAL A O   1 
ATOM 1323 C CB  . VAL A 1 167 ? 32.91546  11.99111  43.80803  1.000 64.70337  ? 167 VAL A CB  1 
ATOM 1324 C CG1 . VAL A 1 167 ? 32.40008  13.06746  42.88336  1.000 62.20495  ? 167 VAL A CG1 1 
ATOM 1325 C CG2 . VAL A 1 167 ? 34.41108  11.85486  43.62913  1.000 61.18860  ? 167 VAL A CG2 1 
ATOM 1326 N N   . ARG A 1 168 ? 31.12461  14.23370  45.68873  1.000 59.05244  ? 168 ARG A N   1 
ATOM 1327 C CA  . ARG A 1 168 ? 29.82719  14.84163  45.95403  1.000 66.91767  ? 168 ARG A CA  1 
ATOM 1328 C C   . ARG A 1 168 ? 28.90143  14.70981  44.74945  1.000 69.19338  ? 168 ARG A C   1 
ATOM 1329 O O   . ARG A 1 168 ? 29.31394  14.88934  43.60460  1.000 69.64224  ? 168 ARG A O   1 
ATOM 1330 C CB  . ARG A 1 168 ? 29.97903  16.32500  46.32576  1.000 70.00289  ? 168 ARG A CB  1 
ATOM 1331 C CG  . ARG A 1 168 ? 28.65871  16.97778  46.76147  1.000 71.37222  ? 168 ARG A CG  1 
ATOM 1332 C CD  . ARG A 1 168 ? 28.78955  18.46003  47.11647  1.000 70.69362  ? 168 ARG A CD  1 
ATOM 1333 N NE  . ARG A 1 168 ? 27.50229  19.00926  47.54432  1.000 75.05901  ? 168 ARG A NE  1 
ATOM 1334 C CZ  . ARG A 1 168 ? 27.07313  19.02818  48.80341  1.000 75.76918  ? 168 ARG A CZ  1 
ATOM 1335 N NH1 . ARG A 1 168 ? 27.82745  18.58231  49.79809  1.000 72.66331  ? 168 ARG A NH1 1 
ATOM 1336 N NH2 . ARG A 1 168 ? 25.86075  19.51425  49.07312  1.000 72.04517  ? 168 ARG A NH2 1 
ATOM 1337 N N   . ASP A 1 169 ? 27.63532  14.40646  45.02627  1.000 78.45288  ? 169 ASP A N   1 
ATOM 1338 C CA  . ASP A 1 169 ? 26.56870  14.28231  44.03424  1.000 78.28773  ? 169 ASP A CA  1 
ATOM 1339 C C   . ASP A 1 169 ? 26.88560  13.28776  42.93260  1.000 77.17841  ? 169 ASP A C   1 
ATOM 1340 O O   . ASP A 1 169 ? 26.26226  13.33238  41.86945  1.000 78.11362  ? 169 ASP A O   1 
ATOM 1341 C CB  . ASP A 1 169 ? 26.17930  15.64931  43.45246  1.000 78.86548  ? 169 ASP A CB  1 
ATOM 1342 C CG  . ASP A 1 169 ? 25.03543  16.32327  44.25357  1.000 86.63311  ? 169 ASP A CG  1 
ATOM 1343 O OD1 . ASP A 1 169 ? 24.04855  15.61568  44.58610  1.000 88.13955  ? 169 ASP A OD1 1 
ATOM 1344 O OD2 . ASP A 1 169 ? 25.13132  17.52911  44.60659  1.000 89.95414  ? 169 ASP A OD2 1 
ATOM 1345 N N   . MET A 1 170 ? 27.80628  12.35133  43.16857  1.000 67.25561  ? 170 MET A N   1 
ATOM 1346 C CA  . MET A 1 170 ? 28.09169  11.30989  42.18973  1.000 66.95410  ? 170 MET A CA  1 
ATOM 1347 C C   . MET A 1 170 ? 27.36053  10.03955  42.61175  1.000 71.29527  ? 170 MET A C   1 
ATOM 1348 O O   . MET A 1 170 ? 27.79970  9.30597   43.50224  1.000 68.33760  ? 170 MET A O   1 
ATOM 1349 C CB  . MET A 1 170 ? 29.58196  11.06073  42.01477  1.000 68.37320  ? 170 MET A CB  1 
ATOM 1350 C CG  . MET A 1 170 ? 29.81099  10.11459  40.83012  1.000 73.95290  ? 170 MET A CG  1 
ATOM 1351 S SD  . MET A 1 170 ? 31.49415  9.89518   40.26033  1.000 74.69442  ? 170 MET A SD  1 
ATOM 1352 C CE  . MET A 1 170 ? 31.24090  8.61199   39.03248  1.000 76.79970  ? 170 MET A CE  1 
ATOM 1353 N N   . THR A 1 171 ? 26.25921  9.76662   41.92771  1.000 72.01765  ? 171 THR A N   1 
ATOM 1354 C CA  . THR A 1 171 ? 25.35113  8.71522   42.31245  1.000 71.47320  ? 171 THR A CA  1 
ATOM 1355 C C   . THR A 1 171 ? 25.21305  7.63239   41.24847  1.000 72.29493  ? 171 THR A C   1 
ATOM 1356 O O   . THR A 1 171 ? 24.40940  6.70751   41.43953  1.000 72.30053  ? 171 THR A O   1 
ATOM 1357 C CB  . THR A 1 171 ? 23.97830  9.32093   42.62616  1.000 72.61941  ? 171 THR A CB  1 
ATOM 1358 O OG1 . THR A 1 171 ? 23.37970  9.76837   41.40510  1.000 78.33201  ? 171 THR A OG1 1 
ATOM 1359 C CG2 . THR A 1 171 ? 24.13980  10.52799  43.53865  1.000 68.57842  ? 171 THR A CG2 1 
ATOM 1360 N N   . THR A 1 172 ? 25.94949  7.72055   40.12841  1.000 72.02506  ? 172 THR A N   1 
ATOM 1361 C CA  . THR A 1 172 ? 26.12682  6.58801   39.22214  1.000 67.79905  ? 172 THR A CA  1 
ATOM 1362 C C   . THR A 1 172 ? 27.60311  6.23146   39.11922  1.000 69.40307  ? 172 THR A C   1 
ATOM 1363 O O   . THR A 1 172 ? 28.48209  7.09688   39.17126  1.000 72.08631  ? 172 THR A O   1 
ATOM 1364 C CB  . THR A 1 172 ? 25.57998  6.83635   37.81472  1.000 64.39400  ? 172 THR A CB  1 
ATOM 1365 O OG1 . THR A 1 172 ? 26.35929  7.83189   37.15173  1.000 67.75551  ? 172 THR A OG1 1 
ATOM 1366 C CG2 . THR A 1 172 ? 24.13319  7.26373   37.87019  1.000 64.09148  ? 172 THR A CG2 1 
ATOM 1367 N N   . CYS A 1 173 ? 27.86217  4.95447   38.97562  1.000 71.13414  ? 173 CYS A N   1 
ATOM 1368 C CA  . CYS A 1 173 ? 29.21983  4.44000   39.00369  1.000 72.64552  ? 173 CYS A CA  1 
ATOM 1369 C C   . CYS A 1 173 ? 29.60843  3.85834   37.65470  1.000 73.19718  ? 173 CYS A C   1 
ATOM 1370 O O   . CYS A 1 173 ? 28.80827  3.15234   37.03265  1.000 73.98765  ? 173 CYS A O   1 
ATOM 1371 C CB  . CYS A 1 173 ? 29.37268  3.35716   40.07889  1.000 72.52901  ? 173 CYS A CB  1 
ATOM 1372 S SG  . CYS A 1 173 ? 31.00094  2.62022   40.14186  1.000 75.05805  ? 173 CYS A SG  1 
ATOM 1373 N N   . PRO A 1 174 ? 30.82891  4.14544   37.19715  1.000 79.39954  ? 174 PRO A N   1 
ATOM 1374 C CA  . PRO A 1 174 ? 31.29812  3.63310   35.89853  1.000 77.79446  ? 174 PRO A CA  1 
ATOM 1375 C C   . PRO A 1 174 ? 31.54794  2.12823   35.91010  1.000 75.90120  ? 174 PRO A C   1 
ATOM 1376 O O   . PRO A 1 174 ? 32.14665  1.58358   36.84153  1.000 72.39635  ? 174 PRO A O   1 
ATOM 1377 C CB  . PRO A 1 174 ? 32.60639  4.39924   35.67824  1.000 81.71869  ? 174 PRO A CB  1 
ATOM 1378 C CG  . PRO A 1 174 ? 32.49888  5.61443   36.55090  1.000 83.08468  ? 174 PRO A CG  1 
ATOM 1379 C CD  . PRO A 1 174 ? 31.73433  5.16203   37.75650  1.000 79.45484  ? 174 PRO A CD  1 
ATOM 1380 N N   . LEU A 1 175 ? 31.13266  1.46342   34.82640  1.000 79.91466  ? 175 LEU A N   1 
ATOM 1381 C CA  . LEU A 1 175 ? 31.18057  0.00730   34.76853  1.000 80.15067  ? 175 LEU A CA  1 
ATOM 1382 C C   . LEU A 1 175 ? 32.12919  -0.48493  33.67629  1.000 78.81828  ? 175 LEU A C   1 
ATOM 1383 O O   . LEU A 1 175 ? 32.20540  0.10948   32.59647  1.000 72.50582  ? 175 LEU A O   1 
ATOM 1384 C CB  . LEU A 1 175 ? 29.77467  -0.58129  34.52548  1.000 73.19075  ? 175 LEU A CB  1 
ATOM 1385 C CG  . LEU A 1 175 ? 28.78787  -0.27530  35.65567  1.000 71.11359  ? 175 LEU A CG  1 
ATOM 1386 C CD1 . LEU A 1 175 ? 27.37567  -0.69845  35.30364  1.000 65.64134  ? 175 LEU A CD1 1 
ATOM 1387 C CD2 . LEU A 1 175 ? 29.24944  -0.93073  36.92638  1.000 65.49332  ? 175 LEU A CD2 1 
ATOM 1388 N N   . PRO A 1 176 ? 32.84005  -1.58524  33.92432  1.000 77.73019  ? 176 PRO A N   1 
ATOM 1389 C CA  . PRO A 1 176 ? 33.66417  -2.17815  32.87161  1.000 73.01736  ? 176 PRO A CA  1 
ATOM 1390 C C   . PRO A 1 176 ? 32.81565  -2.52193  31.65520  1.000 75.61249  ? 176 PRO A C   1 
ATOM 1391 O O   . PRO A 1 176 ? 31.63191  -2.85386  31.77138  1.000 71.49742  ? 176 PRO A O   1 
ATOM 1392 C CB  . PRO A 1 176 ? 34.24211  -3.42940  33.53905  1.000 71.06197  ? 176 PRO A CB  1 
ATOM 1393 C CG  . PRO A 1 176 ? 34.19075  -3.13336  35.00474  1.000 76.48894  ? 176 PRO A CG  1 
ATOM 1394 C CD  . PRO A 1 176 ? 32.94708  -2.32601  35.19549  1.000 74.88641  ? 176 PRO A CD  1 
ATOM 1395 N N   . LYS A 1 177 ? 33.44389  -2.41804  30.47544  1.000 78.81616  ? 177 LYS A N   1 
ATOM 1396 C CA  . LYS A 1 177 ? 32.72217  -2.37332  29.20643  1.000 73.39021  ? 177 LYS A CA  1 
ATOM 1397 C C   . LYS A 1 177 ? 32.04725  -3.70272  28.88521  1.000 67.64692  ? 177 LYS A C   1 
ATOM 1398 O O   . LYS A 1 177 ? 32.61489  -4.77521  29.08754  1.000 69.90349  ? 177 LYS A O   1 
ATOM 1399 C CB  . LYS A 1 177 ? 33.67763  -1.97600  28.08353  1.000 76.27602  ? 177 LYS A CB  1 
ATOM 1400 N N   . GLY A 1 178 ? 30.82799  -3.62445  28.36981  1.000 66.95798  ? 178 GLY A N   1 
ATOM 1401 C CA  . GLY A 1 178 ? 30.01709  -4.79019  28.13159  1.000 66.06545  ? 178 GLY A CA  1 
ATOM 1402 C C   . GLY A 1 178 ? 29.11626  -5.19542  29.28459  1.000 73.86570  ? 178 GLY A C   1 
ATOM 1403 O O   . GLY A 1 178 ? 28.25798  -6.06941  29.09550  1.000 75.31307  ? 178 GLY A O   1 
ATOM 1404 N N   . THR A 1 179 ? 29.27806  -4.59920  30.47339  1.000 72.25154  ? 179 THR A N   1 
ATOM 1405 C CA  . THR A 1 179 ? 28.46004  -4.98662  31.62021  1.000 69.18575  ? 179 THR A CA  1 
ATOM 1406 C C   . THR A 1 179 ? 26.97928  -4.86412  31.29263  1.000 68.95280  ? 179 THR A C   1 
ATOM 1407 O O   . THR A 1 179 ? 26.22032  -5.83634  31.36207  1.000 66.93185  ? 179 THR A O   1 
ATOM 1408 C CB  . THR A 1 179 ? 28.80328  -4.11273  32.83184  1.000 68.29500  ? 179 THR A CB  1 
ATOM 1409 O OG1 . THR A 1 179 ? 30.15511  -4.34413  33.23385  1.000 71.38615  ? 179 THR A OG1 1 
ATOM 1410 C CG2 . THR A 1 179 ? 27.88155  -4.39850  33.98579  1.000 59.25459  ? 179 THR A CG2 1 
ATOM 1411 N N   . LEU A 1 180 ? 26.57235  -3.68256  30.85489  1.000 67.71028  ? 180 LEU A N   1 
ATOM 1412 C CA  . LEU A 1 180 ? 25.17278  -3.37476  30.66064  1.000 67.03456  ? 180 LEU A CA  1 
ATOM 1413 C C   . LEU A 1 180 ? 24.67077  -3.77693  29.28767  1.000 71.05798  ? 180 LEU A C   1 
ATOM 1414 O O   . LEU A 1 180 ? 23.59772  -3.32342  28.88209  1.000 71.11225  ? 180 LEU A O   1 
ATOM 1415 C CB  . LEU A 1 180 ? 24.94132  -1.88666  30.91084  1.000 70.15161  ? 180 LEU A CB  1 
ATOM 1416 C CG  . LEU A 1 180 ? 25.23602  -1.48329  32.36038  1.000 67.31688  ? 180 LEU A CG  1 
ATOM 1417 C CD1 . LEU A 1 180 ? 25.23498  0.01844   32.53714  1.000 65.66468  ? 180 LEU A CD1 1 
ATOM 1418 C CD2 . LEU A 1 180 ? 24.22142  -2.13056  33.29083  1.000 62.95336  ? 180 LEU A CD2 1 
ATOM 1419 N N   . ASP A 1 181 ? 25.41276  -4.61896  28.56709  1.000 73.50480  ? 181 ASP A N   1 
ATOM 1420 C CA  . ASP A 1 181 ? 24.92554  -5.14655  27.29865  1.000 69.43888  ? 181 ASP A CA  1 
ATOM 1421 C C   . ASP A 1 181 ? 23.58440  -5.82659  27.49576  1.000 68.48037  ? 181 ASP A C   1 
ATOM 1422 O O   . ASP A 1 181 ? 23.48432  -6.84664  28.19086  1.000 65.95790  ? 181 ASP A O   1 
ATOM 1423 C CB  . ASP A 1 181 ? 25.90303  -6.15396  26.70206  1.000 74.88929  ? 181 ASP A CB  1 
ATOM 1424 C CG  . ASP A 1 181 ? 25.50619  -6.57710  25.26937  1.000 78.44983  ? 181 ASP A CG  1 
ATOM 1425 O OD1 . ASP A 1 181 ? 24.70739  -5.83880  24.64372  1.000 78.01759  ? 181 ASP A OD1 1 
ATOM 1426 O OD2 . ASP A 1 181 ? 25.90008  -7.69085  24.81832  1.000 77.01858  ? 181 ASP A OD2 1 
ATOM 1427 N N   . GLY A 1 182 ? 22.57741  -5.29875  26.81686  1.000 73.06529  ? 182 GLY A N   1 
ATOM 1428 C CA  . GLY A 1 182 ? 21.21017  -5.73440  26.96350  1.000 74.45943  ? 182 GLY A CA  1 
ATOM 1429 C C   . GLY A 1 182 ? 20.33280  -4.70372  27.62238  1.000 73.96298  ? 182 GLY A C   1 
ATOM 1430 O O   . GLY A 1 182 ? 19.11543  -4.90941  27.69876  1.000 76.60163  ? 182 GLY A O   1 
ATOM 1431 N N   . PHE A 1 183 ? 20.90524  -3.59342  28.08086  1.000 66.54894  ? 183 PHE A N   1 
ATOM 1432 C CA  . PHE A 1 183 ? 20.13855  -2.60541  28.81811  1.000 66.12397  ? 183 PHE A CA  1 
ATOM 1433 C C   . PHE A 1 183 ? 19.05617  -1.99164  27.93853  1.000 69.48163  ? 183 PHE A C   1 
ATOM 1434 O O   . PHE A 1 183 ? 19.25462  -1.77862  26.74306  1.000 77.23285  ? 183 PHE A O   1 
ATOM 1435 C CB  . PHE A 1 183 ? 21.06677  -1.51360  29.34233  1.000 69.08400  ? 183 PHE A CB  1 
ATOM 1436 C CG  . PHE A 1 183 ? 20.41551  -0.60980  30.33489  1.000 70.25898  ? 183 PHE A CG  1 
ATOM 1437 C CD1 . PHE A 1 183 ? 20.29862  -1.00021  31.65733  1.000 66.10696  ? 183 PHE A CD1 1 
ATOM 1438 C CD2 . PHE A 1 183 ? 19.87311  0.59949   29.94037  1.000 70.77368  ? 183 PHE A CD2 1 
ATOM 1439 C CE1 . PHE A 1 183 ? 19.67165  -0.18953  32.56419  1.000 69.33349  ? 183 PHE A CE1 1 
ATOM 1440 C CE2 . PHE A 1 183 ? 19.24946  1.41231   30.84189  1.000 72.66986  ? 183 PHE A CE2 1 
ATOM 1441 C CZ  . PHE A 1 183 ? 19.14585  1.02244   32.15512  1.000 72.53564  ? 183 PHE A CZ  1 
ATOM 1442 N N   . VAL A 1 184 ? 17.89998  -1.71503  28.53476  1.000 71.72264  ? 184 VAL A N   1 
ATOM 1443 C CA  . VAL A 1 184 ? 16.76377  -1.10149  27.85214  1.000 76.44524  ? 184 VAL A CA  1 
ATOM 1444 C C   . VAL A 1 184 ? 16.21333  0.02715   28.71675  1.000 84.60025  ? 184 VAL A C   1 
ATOM 1445 O O   . VAL A 1 184 ? 16.15184  -0.08355  29.94854  1.000 76.80238  ? 184 VAL A O   1 
ATOM 1446 C CB  . VAL A 1 184 ? 15.67603  -2.13946  27.51162  1.000 73.05354  ? 184 VAL A CB  1 
ATOM 1447 C CG1 . VAL A 1 184 ? 14.39664  -1.47706  27.09975  1.000 72.94710  ? 184 VAL A CG1 1 
ATOM 1448 C CG2 . VAL A 1 184 ? 16.16153  -2.99157  26.36495  1.000 78.08815  ? 184 VAL A CG2 1 
ATOM 1449 N N   . ALA A 1 185 ? 15.83370  1.12567   28.05942  1.000 109.08860 ? 185 ALA A N   1 
ATOM 1450 C CA  . ALA A 1 185 ? 15.65085  2.40848   28.72305  1.000 109.08736 ? 185 ALA A CA  1 
ATOM 1451 C C   . ALA A 1 185 ? 14.54090  2.41192   29.76957  1.000 109.47128 ? 185 ALA A C   1 
ATOM 1452 O O   . ALA A 1 185 ? 14.80579  2.53917   30.97139  1.000 107.89607 ? 185 ALA A O   1 
ATOM 1453 C CB  . ALA A 1 185 ? 15.37290  3.48393   27.67420  1.000 109.68008 ? 185 ALA A CB  1 
ATOM 1454 N N   . HIS A 1 186 ? 13.29712  2.25922   29.33565  1.000 94.17644  ? 186 HIS A N   1 
ATOM 1455 C CA  . HIS A 1 186 ? 12.19705  2.48264   30.26223  1.000 87.81816  ? 186 HIS A CA  1 
ATOM 1456 C C   . HIS A 1 186 ? 11.80951  1.19610   30.98492  1.000 79.55150  ? 186 HIS A C   1 
ATOM 1457 O O   . HIS A 1 186 ? 10.63510  0.88344   31.18111  1.000 76.41846  ? 186 HIS A O   1 
ATOM 1458 C CB  . HIS A 1 186 ? 11.02111  3.07263   29.49548  1.000 87.86678  ? 186 HIS A CB  1 
ATOM 1459 N N   . ASP A 1 187 ? 12.80535  0.47334   31.47232  1.000 72.08661  ? 187 ASP A N   1 
ATOM 1460 C CA  . ASP A 1 187 ? 12.57077  -0.84748  32.02781  1.000 68.79012  ? 187 ASP A CA  1 
ATOM 1461 C C   . ASP A 1 187 ? 12.89930  -0.83123  33.51075  1.000 69.04924  ? 187 ASP A C   1 
ATOM 1462 O O   . ASP A 1 187 ? 14.03690  -0.53125  33.89750  1.000 64.90445  ? 187 ASP A O   1 
ATOM 1463 C CB  . ASP A 1 187 ? 13.40324  -1.92032  31.33720  1.000 67.88358  ? 187 ASP A CB  1 
ATOM 1464 C CG  . ASP A 1 187 ? 12.86038  -3.30649  31.59379  1.000 67.40774  ? 187 ASP A CG  1 
ATOM 1465 O OD1 . ASP A 1 187 ? 11.69882  -3.42581  32.03434  1.000 71.79867  ? 187 ASP A OD1 1 
ATOM 1466 O OD2 . ASP A 1 187 ? 13.61002  -4.28246  31.44510  1.000 68.78002  ? 187 ASP A OD2 1 
ATOM 1467 N N   . SER A 1 188 ? 11.90876  -1.19741  34.32820  1.000 66.67747  ? 188 SER A N   1 
ATOM 1468 C CA  . SER A 1 188 ? 12.07403  -1.18014  35.77153  1.000 59.49000  ? 188 SER A CA  1 
ATOM 1469 C C   . SER A 1 188 ? 13.08328  -2.22405  36.21726  1.000 60.45381  ? 188 SER A C   1 
ATOM 1470 O O   . SER A 1 188 ? 13.94663  -1.94113  37.05991  1.000 59.39563  ? 188 SER A O   1 
ATOM 1471 C CB  . SER A 1 188 ? 10.72392  -1.42696  36.41217  1.000 60.89552  ? 188 SER A CB  1 
ATOM 1472 O OG  . SER A 1 188 ? 9.78119   -0.59641  35.76256  1.000 68.07982  ? 188 SER A OG  1 
ATOM 1473 N N   . ILE A 1 189 ? 13.00537  -3.43535  35.65417  1.000 57.97777  ? 189 ILE A N   1 
ATOM 1474 C CA  . ILE A 1 189 ? 13.91269  -4.47157  36.12022  1.000 55.43054  ? 189 ILE A CA  1 
ATOM 1475 C C   . ILE A 1 189 ? 15.32845  -4.18224  35.66821  1.000 55.75240  ? 189 ILE A C   1 
ATOM 1476 O O   . ILE A 1 189 ? 16.27905  -4.46008  36.40005  1.000 56.47159  ? 189 ILE A O   1 
ATOM 1477 C CB  . ILE A 1 189 ? 13.43460  -5.86788  35.68942  1.000 57.17123  ? 189 ILE A CB  1 
ATOM 1478 C CG1 . ILE A 1 189 ? 12.10623  -6.18602  36.36502  1.000 51.86030  ? 189 ILE A CG1 1 
ATOM 1479 C CG2 . ILE A 1 189 ? 14.45115  -6.94380  36.07002  1.000 54.02563  ? 189 ILE A CG2 1 
ATOM 1480 C CD1 . ILE A 1 189 ? 11.49649  -7.47585  35.91367  1.000 48.06655  ? 189 ILE A CD1 1 
ATOM 1481 N N   . HIS A 1 190 ? 15.50663  -3.59427  34.48287  1.000 61.07315  ? 190 HIS A N   1 
ATOM 1482 C CA  . HIS A 1 190 ? 16.86055  -3.28629  34.03399  1.000 58.55981  ? 190 HIS A CA  1 
ATOM 1483 C C   . HIS A 1 190 ? 17.48973  -2.18617  34.87242  1.000 59.38225  ? 190 HIS A C   1 
ATOM 1484 O O   . HIS A 1 190 ? 18.65047  -2.31776  35.28491  1.000 54.44159  ? 190 HIS A O   1 
ATOM 1485 C CB  . HIS A 1 190 ? 16.86716  -2.92180  32.55667  1.000 62.04831  ? 190 HIS A CB  1 
ATOM 1486 C CG  . HIS A 1 190 ? 16.53668  -4.07672  31.65759  1.000 66.28012  ? 190 HIS A CG  1 
ATOM 1487 N ND1 . HIS A 1 190 ? 16.52488  -3.97995  30.28162  1.000 66.73628  ? 190 HIS A ND1 1 
ATOM 1488 C CD2 . HIS A 1 190 ? 16.16143  -5.34603  31.94647  1.000 62.69826  ? 190 HIS A CD2 1 
ATOM 1489 C CE1 . HIS A 1 190 ? 16.16823  -5.13856  29.76344  1.000 63.55910  ? 190 HIS A CE1 1 
ATOM 1490 N NE2 . HIS A 1 190 ? 15.93103  -5.98132  30.75325  1.000 64.52933  ? 190 HIS A NE2 1 
ATOM 1491 N N   . ASP A 1 191 ? 16.72369  -1.11538  35.16500  1.000 63.95770  ? 191 ASP A N   1 
ATOM 1492 C CA  . ASP A 1 191 ? 17.15336  -0.07282  36.10803  1.000 58.49702  ? 191 ASP A CA  1 
ATOM 1493 C C   . ASP A 1 191 ? 17.60931  -0.67052  37.42813  1.000 57.09641  ? 191 ASP A C   1 
ATOM 1494 O O   . ASP A 1 191 ? 18.64502  -0.27583  37.96975  1.000 58.26243  ? 191 ASP A O   1 
ATOM 1495 C CB  . ASP A 1 191 ? 16.02654  0.93820   36.36559  1.000 63.48200  ? 191 ASP A CB  1 
ATOM 1496 C CG  . ASP A 1 191 ? 15.81722  1.93826   35.20155  1.000 75.05381  ? 191 ASP A CG  1 
ATOM 1497 O OD1 . ASP A 1 191 ? 16.79181  2.25042   34.47342  1.000 74.68410  ? 191 ASP A OD1 1 
ATOM 1498 O OD2 . ASP A 1 191 ? 14.67283  2.44185   35.03352  1.000 74.44115  ? 191 ASP A OD2 1 
ATOM 1499 N N   . CYS A 1 192 ? 16.85017  -1.63414  37.96226  1.000 52.52540  ? 192 CYS A N   1 
ATOM 1500 C CA  . CYS A 1 192 ? 17.25869  -2.26603  39.21597  1.000 53.76824  ? 192 CYS A CA  1 
ATOM 1501 C C   . CYS A 1 192 ? 18.56448  -3.04369  39.06934  1.000 55.98328  ? 192 CYS A C   1 
ATOM 1502 O O   . CYS A 1 192 ? 19.43946  -2.95853  39.93897  1.000 56.97112  ? 192 CYS A O   1 
ATOM 1503 C CB  . CYS A 1 192 ? 16.15443  -3.17407  39.75331  1.000 54.83358  ? 192 CYS A CB  1 
ATOM 1504 S SG  . CYS A 1 192 ? 14.73072  -2.30708  40.50145  1.000 54.93535  ? 192 CYS A SG  1 
ATOM 1505 N N   . ALA A 1 193 ? 18.72072  -3.80983  37.98082  1.000 60.74599  ? 193 ALA A N   1 
ATOM 1506 C CA  . ALA A 1 193 ? 19.97023  -4.54145  37.76688  1.000 57.10553  ? 193 ALA A CA  1 
ATOM 1507 C C   . ALA A 1 193 ? 21.14605  -3.58910  37.61053  1.000 56.40227  ? 193 ALA A C   1 
ATOM 1508 O O   . ALA A 1 193 ? 22.22576  -3.84289  38.15118  1.000 57.21133  ? 193 ALA A O   1 
ATOM 1509 C CB  . ALA A 1 193 ? 19.86307  -5.45808  36.54923  1.000 56.30990  ? 193 ALA A CB  1 
ATOM 1510 N N   . LYS A 1 194 ? 20.95838  -2.47830  36.88463  1.000 57.11585  ? 194 LYS A N   1 
ATOM 1511 C CA  . LYS A 1 194 ? 22.02794  -1.48388  36.78009  1.000 56.44789  ? 194 LYS A CA  1 
ATOM 1512 C C   . LYS A 1 194 ? 22.39921  -0.92991  38.15188  1.000 57.65441  ? 194 LYS A C   1 
ATOM 1513 O O   . LYS A 1 194 ? 23.58605  -0.79354  38.48144  1.000 56.55075  ? 194 LYS A O   1 
ATOM 1514 C CB  . LYS A 1 194 ? 21.62480  -0.34203  35.85629  1.000 55.89241  ? 194 LYS A CB  1 
ATOM 1515 C CG  . LYS A 1 194 ? 22.68618  0.73518   35.81956  1.000 59.70771  ? 194 LYS A CG  1 
ATOM 1516 C CD  . LYS A 1 194 ? 22.27214  1.98545   35.03575  1.000 68.92874  ? 194 LYS A CD  1 
ATOM 1517 C CE  . LYS A 1 194 ? 21.29652  2.86539   35.84780  1.000 73.83230  ? 194 LYS A CE  1 
ATOM 1518 N NZ  . LYS A 1 194 ? 21.08041  4.22528   35.22059  1.000 85.73601  ? 194 LYS A NZ  1 
ATOM 1519 N N   . ASP A 1 195 ? 21.39169  -0.60059  38.96819  1.000 55.62564  ? 195 ASP A N   1 
ATOM 1520 C CA  . ASP A 1 195 ? 21.68134  -0.08779  40.30180  1.000 56.27260  ? 195 ASP A CA  1 
ATOM 1521 C C   . ASP A 1 195 ? 22.41696  -1.12676  41.15156  1.000 57.97131  ? 195 ASP A C   1 
ATOM 1522 O O   . ASP A 1 195 ? 23.37104  -0.77954  41.86809  1.000 57.97908  ? 195 ASP A O   1 
ATOM 1523 C CB  . ASP A 1 195 ? 20.39388  0.38980   40.99004  1.000 60.32207  ? 195 ASP A CB  1 
ATOM 1524 C CG  . ASP A 1 195 ? 19.96575  1.82346   40.56395  1.000 62.88206  ? 195 ASP A CG  1 
ATOM 1525 O OD1 . ASP A 1 195 ? 20.85973  2.65650   40.27648  1.000 61.69887  ? 195 ASP A OD1 1 
ATOM 1526 O OD2 . ASP A 1 195 ? 18.73412  2.11926   40.53518  1.000 62.92963  ? 195 ASP A OD2 1 
ATOM 1527 N N   . ILE A 1 196 ? 22.00500  -2.40618  41.07500  1.000 55.26270  ? 196 ILE A N   1 
ATOM 1528 C CA  . ILE A 1 196 ? 22.70757  -3.45909  41.81455  1.000 56.90163  ? 196 ILE A CA  1 
ATOM 1529 C C   . ILE A 1 196 ? 24.14507  -3.55156  41.33683  1.000 58.84534  ? 196 ILE A C   1 
ATOM 1530 O O   . ILE A 1 196 ? 25.06761  -3.75521  42.13616  1.000 61.89652  ? 196 ILE A O   1 
ATOM 1531 C CB  . ILE A 1 196 ? 22.00051  -4.82051  41.67094  1.000 55.11938  ? 196 ILE A CB  1 
ATOM 1532 C CG1 . ILE A 1 196 ? 20.58536  -4.77592  42.20260  1.000 53.77134  ? 196 ILE A CG1 1 
ATOM 1533 C CG2 . ILE A 1 196 ? 22.73903  -5.89030  42.43673  1.000 51.00167  ? 196 ILE A CG2 1 
ATOM 1534 C CD1 . ILE A 1 196 ? 19.79582  -5.96280  41.75662  1.000 53.29007  ? 196 ILE A CD1 1 
ATOM 1535 N N   . LEU A 1 197 ? 24.35651  -3.37948  40.02470  1.000 56.30862  ? 197 LEU A N   1 
ATOM 1536 C CA  . LEU A 1 197 ? 25.69433  -3.47528  39.44290  1.000 57.94350  ? 197 LEU A CA  1 
ATOM 1537 C C   . LEU A 1 197 ? 26.57219  -2.29731  39.83827  1.000 57.27499  ? 197 LEU A C   1 
ATOM 1538 O O   . LEU A 1 197 ? 27.72705  -2.49376  40.23591  1.000 56.33139  ? 197 LEU A O   1 
ATOM 1539 C CB  . LEU A 1 197 ? 25.58888  -3.60146  37.91804  1.000 57.89216  ? 197 LEU A CB  1 
ATOM 1540 C CG  . LEU A 1 197 ? 25.17360  -5.00070  37.44184  1.000 53.91205  ? 197 LEU A CG  1 
ATOM 1541 C CD1 . LEU A 1 197 ? 24.63472  -4.99549  36.04627  1.000 58.45486  ? 197 LEU A CD1 1 
ATOM 1542 C CD2 . LEU A 1 197 ? 26.37560  -5.89376  37.50882  1.000 51.55770  ? 197 LEU A CD2 1 
ATOM 1543 N N   . MET A 1 198 ? 26.04070  -1.07149  39.76203  1.000 53.94082  ? 198 MET A N   1 
ATOM 1544 C CA  . MET A 1 198 ? 26.84484  0.09492   40.10387  1.000 55.83883  ? 198 MET A CA  1 
ATOM 1545 C C   . MET A 1 198 ? 27.17995  0.17310   41.58718  1.000 61.15744  ? 198 MET A C   1 
ATOM 1546 O O   . MET A 1 198 ? 28.20229  0.77186   41.94405  1.000 60.85697  ? 198 MET A O   1 
ATOM 1547 C CB  . MET A 1 198 ? 26.14235  1.36746   39.68213  1.000 59.59682  ? 198 MET A CB  1 
ATOM 1548 C CG  . MET A 1 198 ? 26.01680  1.51134   38.20284  1.000 62.93037  ? 198 MET A CG  1 
ATOM 1549 S SD  . MET A 1 198 ? 25.48912  3.15843   37.73379  1.000 63.51211  ? 198 MET A SD  1 
ATOM 1550 C CE  . MET A 1 198 ? 23.77659  3.17020   38.22708  1.000 65.20843  ? 198 MET A CE  1 
ATOM 1551 N N   . MET A 1 199 ? 26.32700  -0.38092  42.47014  1.000 62.27072  ? 199 MET A N   1 
ATOM 1552 C CA  . MET A 1 199 ? 26.65617  -0.39750  43.89789  1.000 60.02086  ? 199 MET A CA  1 
ATOM 1553 C C   . MET A 1 199 ? 27.72272  -1.42314  44.21409  1.000 61.94855  ? 199 MET A C   1 
ATOM 1554 O O   . MET A 1 199 ? 28.63097  -1.15343  45.00340  1.000 64.03142  ? 199 MET A O   1 
ATOM 1555 C CB  . MET A 1 199 ? 25.43875  -0.69630  44.75517  1.000 58.76564  ? 199 MET A CB  1 
ATOM 1556 C CG  . MET A 1 199 ? 24.41933  0.39450   44.82755  1.000 63.46128  ? 199 MET A CG  1 
ATOM 1557 S SD  . MET A 1 199 ? 23.20428  -0.01841  46.09878  1.000 62.97761  ? 199 MET A SD  1 
ATOM 1558 C CE  . MET A 1 199 ? 22.35772  -1.41865  45.34897  1.000 58.74359  ? 199 MET A CE  1 
ATOM 1559 N N   . LYS A 1 200 ? 27.59772  -2.61993  43.64794  1.000 60.03777  ? 200 LYS A N   1 
ATOM 1560 C CA  . LYS A 1 200 ? 28.59041  -3.66478  43.87506  1.000 63.86023  ? 200 LYS A CA  1 
ATOM 1561 C C   . LYS A 1 200 ? 29.97109  -3.25172  43.34239  1.000 67.80429  ? 200 LYS A C   1 
ATOM 1562 O O   . LYS A 1 200 ? 30.98270  -3.42098  44.03594  1.000 67.81153  ? 200 LYS A O   1 
ATOM 1563 C CB  . LYS A 1 200 ? 28.09236  -4.96907  43.23639  1.000 66.43639  ? 200 LYS A CB  1 
ATOM 1564 C CG  . LYS A 1 200 ? 28.96775  -6.19739  43.42329  1.000 73.99607  ? 200 LYS A CG  1 
ATOM 1565 C CD  . LYS A 1 200 ? 28.97722  -6.68103  44.84652  1.000 77.72478  ? 200 LYS A CD  1 
ATOM 1566 C CE  . LYS A 1 200 ? 27.63269  -7.25869  45.17564  1.000 80.28828  ? 200 LYS A CE  1 
ATOM 1567 N NZ  . LYS A 1 200 ? 27.38407  -8.51565  44.40532  1.000 80.23735  ? 200 LYS A NZ  1 
ATOM 1568 N N   . TYR A 1 201 ? 30.04169  -2.68390  42.12569  1.000 65.18267  ? 201 TYR A N   1 
ATOM 1569 C CA  . TYR A 1 201 ? 31.34137  -2.22041  41.63443  1.000 70.33671  ? 201 TYR A CA  1 
ATOM 1570 C C   . TYR A 1 201 ? 31.87975  -1.04351  42.44515  1.000 70.59044  ? 201 TYR A C   1 
ATOM 1571 O O   . TYR A 1 201 ? 33.06614  -1.02569  42.79389  1.000 71.49499  ? 201 TYR A O   1 
ATOM 1572 C CB  . TYR A 1 201 ? 31.30183  -1.87630  40.13339  1.000 73.24232  ? 201 TYR A CB  1 
ATOM 1573 C CG  . TYR A 1 201 ? 31.54245  -3.09057  39.22791  1.000 73.43838  ? 201 TYR A CG  1 
ATOM 1574 C CD1 . TYR A 1 201 ? 32.81191  -3.66140  39.12226  1.000 73.78133  ? 201 TYR A CD1 1 
ATOM 1575 C CD2 . TYR A 1 201 ? 30.51172  -3.65191  38.48117  1.000 67.65183  ? 201 TYR A CD2 1 
ATOM 1576 C CE1 . TYR A 1 201 ? 33.02949  -4.77435  38.32208  1.000 77.91728  ? 201 TYR A CE1 1 
ATOM 1577 C CE2 . TYR A 1 201 ? 30.72246  -4.75171  37.68449  1.000 70.38257  ? 201 TYR A CE2 1 
ATOM 1578 C CZ  . TYR A 1 201 ? 31.97918  -5.30995  37.59901  1.000 76.54025  ? 201 TYR A CZ  1 
ATOM 1579 O OH  . TYR A 1 201 ? 32.17040  -6.40351  36.78454  1.000 75.69950  ? 201 TYR A OH  1 
ATOM 1580 N N   . ALA A 1 202 ? 31.03795  -0.05625  42.76126  1.000 70.29939  ? 202 ALA A N   1 
ATOM 1581 C CA  . ALA A 1 202 ? 31.49101  1.03890   43.61693  1.000 70.66704  ? 202 ALA A CA  1 
ATOM 1582 C C   . ALA A 1 202 ? 32.12315  0.51335   44.90366  1.000 69.47277  ? 202 ALA A C   1 
ATOM 1583 O O   . ALA A 1 202 ? 33.15713  1.01965   45.35119  1.000 67.86183  ? 202 ALA A O   1 
ATOM 1584 C CB  . ALA A 1 202 ? 30.32172  1.96610   43.93460  1.000 68.50358  ? 202 ALA A CB  1 
ATOM 1585 N N   . LEU A 1 203 ? 31.51078  -0.51121  45.50654  1.000 69.58736  ? 203 LEU A N   1 
ATOM 1586 C CA  . LEU A 1 203 ? 32.09800  -1.17194  46.66943  1.000 69.37161  ? 203 LEU A CA  1 
ATOM 1587 C C   . LEU A 1 203 ? 33.40275  -1.86265  46.30591  1.000 72.26929  ? 203 LEU A C   1 
ATOM 1588 O O   . LEU A 1 203 ? 34.38894  -1.77925  47.04751  1.000 74.91952  ? 203 LEU A O   1 
ATOM 1589 C CB  . LEU A 1 203 ? 31.10002  -2.17543  47.25695  1.000 69.37812  ? 203 LEU A CB  1 
ATOM 1590 C CG  . LEU A 1 203 ? 31.41079  -3.05009  48.48166  1.000 70.80696  ? 203 LEU A CG  1 
ATOM 1591 C CD1 . LEU A 1 203 ? 31.61878  -2.23432  49.74671  1.000 65.67908  ? 203 LEU A CD1 1 
ATOM 1592 C CD2 . LEU A 1 203 ? 30.27856  -4.04793  48.65104  1.000 73.36896  ? 203 LEU A CD2 1 
ATOM 1593 N N   . ARG A 1 204 ? 33.42929  -2.55898  45.17102  1.000 73.29819  ? 204 ARG A N   1 
ATOM 1594 C CA  . ARG A 1 204 ? 34.68509  -3.13789  44.71295  1.000 74.04570  ? 204 ARG A CA  1 
ATOM 1595 C C   . ARG A 1 204 ? 35.72555  -2.04786  44.50621  1.000 72.73810  ? 204 ARG A C   1 
ATOM 1596 O O   . ARG A 1 204 ? 36.87839  -2.18803  44.92764  1.000 73.94502  ? 204 ARG A O   1 
ATOM 1597 C CB  . ARG A 1 204 ? 34.44846  -3.94169  43.43020  1.000 77.19267  ? 204 ARG A CB  1 
ATOM 1598 C CG  . ARG A 1 204 ? 33.64331  -5.23999  43.64393  1.000 78.21341  ? 204 ARG A CG  1 
ATOM 1599 C CD  . ARG A 1 204 ? 33.33079  -5.97376  42.32891  1.000 80.54680  ? 204 ARG A CD  1 
ATOM 1600 N NE  . ARG A 1 204 ? 34.54063  -6.27831  41.56940  1.000 87.53211  ? 204 ARG A NE  1 
ATOM 1601 C CZ  . ARG A 1 204 ? 35.34638  -7.30911  41.79437  1.000 86.51076  ? 204 ARG A CZ  1 
ATOM 1602 N NH1 . ARG A 1 204 ? 35.13974  -8.14671  42.79592  1.000 88.63449  ? 204 ARG A NH1 1 
ATOM 1603 N NH2 . ARG A 1 204 ? 36.39454  -7.49537  41.00076  1.000 88.11328  ? 204 ARG A NH2 1 
ATOM 1604 N N   . TYR A 1 205 ? 35.31680  -0.93292  43.89936  1.000 74.59324  ? 205 TYR A N   1 
ATOM 1605 C CA  . TYR A 1 205 ? 36.23597  0.17492   43.67802  1.000 74.38303  ? 205 TYR A CA  1 
ATOM 1606 C C   . TYR A 1 205 ? 36.71663  0.74963   44.99604  1.000 70.65230  ? 205 TYR A C   1 
ATOM 1607 O O   . TYR A 1 205 ? 37.90828  1.01401   45.16872  1.000 70.83789  ? 205 TYR A O   1 
ATOM 1608 C CB  . TYR A 1 205 ? 35.56055  1.26318   42.83992  1.000 75.38595  ? 205 TYR A CB  1 
ATOM 1609 C CG  . TYR A 1 205 ? 35.22008  0.87074   41.40405  1.000 81.73553  ? 205 TYR A CG  1 
ATOM 1610 C CD1 . TYR A 1 205 ? 35.73136  -0.29132  40.81840  1.000 84.16112  ? 205 TYR A CD1 1 
ATOM 1611 C CD2 . TYR A 1 205 ? 34.38622  1.67740   40.62547  1.000 85.06857  ? 205 TYR A CD2 1 
ATOM 1612 C CE1 . TYR A 1 205 ? 35.40652  -0.63748  39.50230  1.000 84.56036  ? 205 TYR A CE1 1 
ATOM 1613 C CE2 . TYR A 1 205 ? 34.06881  1.33867   39.30540  1.000 82.80006  ? 205 TYR A CE2 1 
ATOM 1614 C CZ  . TYR A 1 205 ? 34.57916  0.18573   38.75847  1.000 81.72013  ? 205 TYR A CZ  1 
ATOM 1615 O OH  . TYR A 1 205 ? 34.25198  -0.12869  37.46707  1.000 83.94122  ? 205 TYR A OH  1 
ATOM 1616 N N   . ALA A 1 206 ? 35.80074  0.93294   45.94603  1.000 74.09782  ? 206 ALA A N   1 
ATOM 1617 C CA  . ALA A 1 206 ? 36.15333  1.53407   47.23012  1.000 71.81709  ? 206 ALA A CA  1 
ATOM 1618 C C   . ALA A 1 206 ? 37.00629  0.60508   48.07950  1.000 72.21728  ? 206 ALA A C   1 
ATOM 1619 O O   . ALA A 1 206 ? 37.87100  1.07381   48.82514  1.000 74.48583  ? 206 ALA A O   1 
ATOM 1620 C CB  . ALA A 1 206 ? 34.88873  1.92682   47.98917  1.000 70.53905  ? 206 ALA A CB  1 
ATOM 1621 N N   . MET A 1 207 ? 36.76644  -0.70270  47.99941  1.000 74.20298  ? 207 MET A N   1 
ATOM 1622 C CA  . MET A 1 207 ? 37.60644  -1.68504  48.66727  1.000 74.04657  ? 207 MET A CA  1 
ATOM 1623 C C   . MET A 1 207 ? 38.93506  -1.94346  47.95454  1.000 76.44468  ? 207 MET A C   1 
ATOM 1624 O O   . MET A 1 207 ? 39.83647  -2.53898  48.55470  1.000 78.38996  ? 207 MET A O   1 
ATOM 1625 C CB  . MET A 1 207 ? 36.83570  -2.99861  48.82365  1.000 79.87856  ? 207 MET A CB  1 
ATOM 1626 C CG  . MET A 1 207 ? 35.83208  -3.03120  49.98258  1.000 85.57364  ? 207 MET A CG  1 
ATOM 1627 S SD  . MET A 1 207 ? 34.94394  -4.60870  50.14297  1.000 94.71363  ? 207 MET A SD  1 
ATOM 1628 C CE  . MET A 1 207 ? 33.99647  -4.33296  51.65399  1.000 89.51986  ? 207 MET A CE  1 
ATOM 1629 N N   . GLY A 1 208 ? 39.09891  -1.50201  46.71243  1.000 78.31935  ? 208 GLY A N   1 
ATOM 1630 C CA  . GLY A 1 208 ? 40.31731  -1.82089  46.00003  1.000 77.04073  ? 208 GLY A CA  1 
ATOM 1631 C C   . GLY A 1 208 ? 40.44862  -3.28342  45.64718  1.000 83.35361  ? 208 GLY A C   1 
ATOM 1632 O O   . GLY A 1 208 ? 41.56340  -3.81302  45.63030  1.000 85.40137  ? 208 GLY A O   1 
ATOM 1633 N N   . LEU A 1 209 ? 39.33067  -3.96861  45.41414  1.000 82.52409  ? 209 LEU A N   1 
ATOM 1634 C CA  . LEU A 1 209 ? 39.36135  -5.26971  44.76100  1.000 85.09837  ? 209 LEU A CA  1 
ATOM 1635 C C   . LEU A 1 209 ? 39.51473  -5.15761  43.25460  1.000 92.31627  ? 209 LEU A C   1 
ATOM 1636 O O   . LEU A 1 209 ? 39.77986  -6.16858  42.59253  1.000 93.37357  ? 209 LEU A O   1 
ATOM 1637 C CB  . LEU A 1 209 ? 38.08004  -6.04443  45.02712  1.000 84.41161  ? 209 LEU A CB  1 
ATOM 1638 C CG  . LEU A 1 209 ? 37.85251  -6.90892  46.24133  1.000 88.10864  ? 209 LEU A CG  1 
ATOM 1639 C CD1 . LEU A 1 209 ? 37.71973  -6.06220  47.48495  1.000 88.74555  ? 209 LEU A CD1 1 
ATOM 1640 C CD2 . LEU A 1 209 ? 36.57196  -7.67243  45.96873  1.000 93.85378  ? 209 LEU A CD2 1 
ATOM 1641 N N   . GLU A 1 210 ? 39.30922  -3.96737  42.70336  1.000 91.98160  ? 210 GLU A N   1 
ATOM 1642 C CA  . GLU A 1 210 ? 39.31795  -3.76050  41.26857  1.000 94.78999  ? 210 GLU A CA  1 
ATOM 1643 C C   . GLU A 1 210 ? 39.48802  -2.26792  41.03281  1.000 97.45547  ? 210 GLU A C   1 
ATOM 1644 O O   . GLU A 1 210 ? 39.03574  -1.44446  41.83585  1.000 94.73895  ? 210 GLU A O   1 
ATOM 1645 C CB  . GLU A 1 210 ? 38.03163  -4.29459  40.63074  1.000 94.28874  ? 210 GLU A CB  1 
ATOM 1646 C CG  . GLU A 1 210 ? 38.02334  -4.29164  39.12171  1.000 98.77524  ? 210 GLU A CG  1 
ATOM 1647 C CD  . GLU A 1 210 ? 36.75975  -4.92084  38.55470  1.000 99.62015  ? 210 GLU A CD  1 
ATOM 1648 O OE1 . GLU A 1 210 ? 35.89518  -5.34311  39.36174  1.000 94.04362  ? 210 GLU A OE1 1 
ATOM 1649 O OE2 . GLU A 1 210 ? 36.63061  -4.98647  37.30590  1.000 98.71089  ? 210 GLU A OE2 1 
ATOM 1650 N N   . ASP A 1 211 ? 40.17550  -1.92791  39.94841  1.000 101.60554 ? 211 ASP A N   1 
ATOM 1651 C CA  . ASP A 1 211 ? 40.42691  -0.53650  39.61464  1.000 101.21708 ? 211 ASP A CA  1 
ATOM 1652 C C   . ASP A 1 211 ? 39.34484  -0.05078  38.65822  1.000 105.04173 ? 211 ASP A C   1 
ATOM 1653 O O   . ASP A 1 211 ? 38.98491  -0.75250  37.70516  1.000 103.12976 ? 211 ASP A O   1 
ATOM 1654 C CB  . ASP A 1 211 ? 41.81541  -0.37242  38.99836  1.000 104.05091 ? 211 ASP A CB  1 
ATOM 1655 N N   . ALA A 1 212 ? 38.80636  1.13237   38.93826  1.000 108.87833 ? 212 ALA A N   1 
ATOM 1656 C CA  . ALA A 1 212 ? 37.79974  1.71904   38.06600  1.000 111.01407 ? 212 ALA A CA  1 
ATOM 1657 C C   . ALA A 1 212 ? 38.43116  2.17245   36.74972  1.000 111.63562 ? 212 ALA A C   1 
ATOM 1658 O O   . ALA A 1 212 ? 39.51485  2.77462   36.74883  1.000 109.04054 ? 212 ALA A O   1 
ATOM 1659 C CB  . ALA A 1 212 ? 37.12047  2.90421   38.74906  1.000 110.79061 ? 212 ALA A CB  1 
ATOM 1660 N N   . PRO A 1 213 ? 37.78115  1.90774   35.62036  1.000 108.79438 ? 213 PRO A N   1 
ATOM 1661 C CA  . PRO A 1 213 ? 38.30601  2.36444   34.33011  1.000 109.31916 ? 213 PRO A CA  1 
ATOM 1662 C C   . PRO A 1 213 ? 38.02157  3.84563   34.10140  1.000 109.05350 ? 213 PRO A C   1 
ATOM 1663 O O   . PRO A 1 213 ? 37.26497  4.48729   34.83167  1.000 107.16893 ? 213 PRO A O   1 
ATOM 1664 C CB  . PRO A 1 213 ? 37.54841  1.49396   33.32023  1.000 108.17949 ? 213 PRO A CB  1 
ATOM 1665 C CG  . PRO A 1 213 ? 36.25087  1.17181   34.00760  1.000 100.94936 ? 213 PRO A CG  1 
ATOM 1666 C CD  . PRO A 1 213 ? 36.57370  1.07006   35.47374  1.000 100.76447 ? 213 PRO A CD  1 
ATOM 1667 N N   . SER A 1 214 ? 38.69708  4.39495   33.08969  1.000 111.35483 ? 214 SER A N   1 
ATOM 1668 C CA  . SER A 1 214 ? 38.23416  5.58829   32.39306  1.000 106.88402 ? 214 SER A CA  1 
ATOM 1669 C C   . SER A 1 214 ? 37.52025  5.23543   31.09481  1.000 112.21911 ? 214 SER A C   1 
ATOM 1670 O O   . SER A 1 214 ? 36.89505  6.11279   30.48482  1.000 110.63493 ? 214 SER A O   1 
ATOM 1671 C CB  . SER A 1 214 ? 39.40436  6.53045   32.10113  1.000 97.49680  ? 214 SER A CB  1 
ATOM 1672 N N   . GLU A 1 215 ? 37.58678  3.95851   30.69310  1.000 112.89996 ? 215 GLU A N   1 
ATOM 1673 C CA  . GLU A 1 215 ? 37.07818  3.39939   29.43582  1.000 110.69286 ? 215 GLU A CA  1 
ATOM 1674 C C   . GLU A 1 215 ? 36.00393  2.35352   29.77743  1.000 107.44762 ? 215 GLU A C   1 
ATOM 1675 O O   . GLU A 1 215 ? 36.27068  1.15702   29.93046  1.000 104.36636 ? 215 GLU A O   1 
ATOM 1676 C CB  . GLU A 1 215 ? 38.25232  2.82562   28.62355  1.000 112.94060 ? 215 GLU A CB  1 
ATOM 1677 C CG  . GLU A 1 215 ? 38.97289  1.61277   29.25116  1.000 116.09165 ? 215 GLU A CG  1 
ATOM 1678 C CD  . GLU A 1 215 ? 39.93700  1.98161   30.37097  1.000 115.80398 ? 215 GLU A CD  1 
ATOM 1679 O OE1 . GLU A 1 215 ? 39.88338  3.12399   30.86331  1.000 116.87883 ? 215 GLU A OE1 1 
ATOM 1680 O OE2 . GLU A 1 215 ? 40.73567  1.11584   30.78242  1.000 116.62478 ? 215 GLU A OE2 1 
ATOM 1681 N N   . GLU A 1 216 ? 34.77251  2.81963   29.89430  1.000 102.45346 ? 216 GLU A N   1 
ATOM 1682 C CA  . GLU A 1 216 ? 33.71629  2.04286   30.51162  1.000 99.43197  ? 216 GLU A CA  1 
ATOM 1683 C C   . GLU A 1 216 ? 32.70275  1.60613   29.47647  1.000 97.20985  ? 216 GLU A C   1 
ATOM 1684 O O   . GLU A 1 216 ? 32.71476  2.05489   28.32995  1.000 97.39221  ? 216 GLU A O   1 
ATOM 1685 C CB  . GLU A 1 216 ? 32.99197  2.86411   31.58023  1.000 99.83063  ? 216 GLU A CB  1 
ATOM 1686 C CG  . GLU A 1 216 ? 33.85485  3.32240   32.69057  1.000 100.85099 ? 216 GLU A CG  1 
ATOM 1687 C CD  . GLU A 1 216 ? 34.55113  4.59843   32.33106  1.000 106.91552 ? 216 GLU A CD  1 
ATOM 1688 O OE1 . GLU A 1 216 ? 34.31846  5.10255   31.20791  1.000 107.60574 ? 216 GLU A OE1 1 
ATOM 1689 O OE2 . GLU A 1 216 ? 35.31700  5.10665   33.16928  1.000 113.61672 ? 216 GLU A OE2 1 
ATOM 1690 N N   . GLU A 1 217 ? 31.80345  0.73186   29.91521  1.000 82.66363  ? 217 GLU A N   1 
ATOM 1691 C CA  . GLU A 1 217 ? 30.49575  0.69035   29.30070  1.000 82.18902  ? 217 GLU A CA  1 
ATOM 1692 C C   . GLU A 1 217 ? 30.01641  2.11780   29.11145  1.000 87.54011  ? 217 GLU A C   1 
ATOM 1693 O O   . GLU A 1 217 ? 30.03152  2.92149   30.04700  1.000 85.30495  ? 217 GLU A O   1 
ATOM 1694 C CB  . GLU A 1 217 ? 29.50546  -0.06671  30.17671  1.000 78.49948  ? 217 GLU A CB  1 
ATOM 1695 C CG  . GLU A 1 217 ? 28.10809  0.03362   29.61236  1.000 75.43982  ? 217 GLU A CG  1 
ATOM 1696 C CD  . GLU A 1 217 ? 27.82865  -0.98308  28.56456  1.000 82.26093  ? 217 GLU A CD  1 
ATOM 1697 O OE1 . GLU A 1 217 ? 28.18666  -2.15571  28.82503  1.000 83.44359  ? 217 GLU A OE1 1 
ATOM 1698 O OE2 . GLU A 1 217 ? 27.31197  -0.61550  27.47395  1.000 85.53266  ? 217 GLU A OE2 1 
ATOM 1699 N N   . CYS A 1 218 ? 29.61503  2.44458   27.89012  1.000 91.39884  ? 218 CYS A N   1 
ATOM 1700 C CA  . CYS A 1 218 ? 29.20300  3.81570   27.63789  1.000 91.20001  ? 218 CYS A CA  1 
ATOM 1701 C C   . CYS A 1 218 ? 27.96327  4.22542   28.43800  1.000 85.31067  ? 218 CYS A C   1 
ATOM 1702 O O   . CYS A 1 218 ? 27.69067  5.42383   28.54219  1.000 86.58725  ? 218 CYS A O   1 
ATOM 1703 C CB  . CYS A 1 218 ? 29.00455  3.98614   26.13290  1.000 94.72887  ? 218 CYS A CB  1 
ATOM 1704 S SG  . CYS A 1 218 ? 27.86530  2.80839   25.36002  1.000 130.49799 ? 218 CYS A SG  1 
ATOM 1705 N N   . ASP A 1 219 ? 27.24065  3.26922   29.04018  1.000 85.36340  ? 219 ASP A N   1 
ATOM 1706 C CA  . ASP A 1 219 ? 25.95987  3.47120   29.72210  1.000 83.49380  ? 219 ASP A CA  1 
ATOM 1707 C C   . ASP A 1 219 ? 26.05385  4.06750   31.13440  1.000 78.67176  ? 219 ASP A C   1 
ATOM 1708 O O   . ASP A 1 219 ? 25.21153  4.90260   31.47638  1.000 80.18532  ? 219 ASP A O   1 
ATOM 1709 C CB  . ASP A 1 219 ? 25.18289  2.15463   29.74733  1.000 79.87813  ? 219 ASP A CB  1 
ATOM 1710 N N   . PRO A 1 220 ? 27.01536  3.65691   32.00585  1.000 78.19928  ? 220 PRO A N   1 
ATOM 1711 C CA  . PRO A 1 220 ? 27.22667  4.37036   33.27713  1.000 76.67446  ? 220 PRO A CA  1 
ATOM 1712 C C   . PRO A 1 220 ? 27.18851  5.88732   33.18559  1.000 80.19558  ? 220 PRO A C   1 
ATOM 1713 O O   . PRO A 1 220 ? 26.40256  6.51907   33.89989  1.000 85.14901  ? 220 PRO A O   1 
ATOM 1714 C CB  . PRO A 1 220 ? 28.61558  3.88916   33.69724  1.000 78.90274  ? 220 PRO A CB  1 
ATOM 1715 C CG  . PRO A 1 220 ? 28.66290  2.51450   33.20176  1.000 75.01830  ? 220 PRO A CG  1 
ATOM 1716 C CD  . PRO A 1 220 ? 27.88622  2.47550   31.92900  1.000 79.24341  ? 220 PRO A CD  1 
ATOM 1717 N N   . LEU A 1 221 ? 28.03626  6.47678   32.34285  1.000 79.57530  ? 221 LEU A N   1 
ATOM 1718 C CA  . LEU A 1 221 ? 27.94875  7.89335   31.99271  1.000 74.11860  ? 221 LEU A CA  1 
ATOM 1719 C C   . LEU A 1 221 ? 28.09457  8.81716   33.20616  1.000 78.45495  ? 221 LEU A C   1 
ATOM 1720 O O   . LEU A 1 221 ? 27.13612  9.46068   33.64596  1.000 81.14867  ? 221 LEU A O   1 
ATOM 1721 C CB  . LEU A 1 221 ? 26.62636  8.16432   31.27523  1.000 73.42146  ? 221 LEU A CB  1 
ATOM 1722 N N   . MET B 1 1   ? 28.17969  27.65678  51.16276  1.000 83.63065  ? 1   MET B N   1 
ATOM 1723 C CA  . MET B 1 1   ? 27.08714  26.67995  51.12969  1.000 85.19147  ? 1   MET B CA  1 
ATOM 1724 C C   . MET B 1 1   ? 27.13477  25.63182  52.24386  1.000 87.01673  ? 1   MET B C   1 
ATOM 1725 O O   . MET B 1 1   ? 28.16220  24.96914  52.43638  1.000 85.35635  ? 1   MET B O   1 
ATOM 1726 C CB  . MET B 1 1   ? 27.06881  25.90437  49.81847  1.000 84.24167  ? 1   MET B CB  1 
ATOM 1727 C CG  . MET B 1 1   ? 25.89328  24.93521  49.78022  1.000 84.27407  ? 1   MET B CG  1 
ATOM 1728 S SD  . MET B 1 1   ? 25.98812  23.57202  48.60895  1.000 92.01458  ? 1   MET B SD  1 
ATOM 1729 C CE  . MET B 1 1   ? 27.15399  22.50478  49.46021  1.000 85.45438  ? 1   MET B CE  1 
ATOM 1730 N N   . PHE B 1 2   ? 25.99814  25.43037  52.91558  1.000 83.75434  ? 2   PHE B N   1 
ATOM 1731 C CA  . PHE B 1 2   ? 25.86058  24.43521  53.96890  1.000 80.41377  ? 2   PHE B CA  1 
ATOM 1732 C C   . PHE B 1 2   ? 24.88689  23.32754  53.58885  1.000 78.07323  ? 2   PHE B C   1 
ATOM 1733 O O   . PHE B 1 2   ? 23.93631  23.53650  52.83195  1.000 79.41377  ? 2   PHE B O   1 
ATOM 1734 C CB  . PHE B 1 2   ? 25.36570  25.05502  55.28009  1.000 78.96358  ? 2   PHE B CB  1 
ATOM 1735 C CG  . PHE B 1 2   ? 26.40731  25.80762  56.02467  1.000 78.21728  ? 2   PHE B CG  1 
ATOM 1736 C CD1 . PHE B 1 2   ? 27.69222  25.89165  55.54529  1.000 80.62157  ? 2   PHE B CD1 1 
ATOM 1737 C CD2 . PHE B 1 2   ? 26.12725  26.33658  57.26472  1.000 79.07757  ? 2   PHE B CD2 1 
ATOM 1738 C CE1 . PHE B 1 2   ? 28.66035  26.56423  56.24883  1.000 83.94262  ? 2   PHE B CE1 1 
ATOM 1739 C CE2 . PHE B 1 2   ? 27.10004  27.00310  57.98666  1.000 80.69667  ? 2   PHE B CE2 1 
ATOM 1740 C CZ  . PHE B 1 2   ? 28.36584  27.11796  57.47547  1.000 83.84167  ? 2   PHE B CZ  1 
ATOM 1741 N N   . ASP B 1 3   ? 25.13902  22.14323  54.13222  1.000 79.71913  ? 3   ASP B N   1 
ATOM 1742 C CA  . ASP B 1 3   ? 24.12962  21.10640  54.26490  1.000 78.37307  ? 3   ASP B CA  1 
ATOM 1743 C C   . ASP B 1 3   ? 23.42046  21.24160  55.61899  1.000 78.37971  ? 3   ASP B C   1 
ATOM 1744 O O   . ASP B 1 3   ? 23.87443  21.94610  56.52749  1.000 78.05644  ? 3   ASP B O   1 
ATOM 1745 C CB  . ASP B 1 3   ? 24.75523  19.72118  54.13051  1.000 77.93919  ? 3   ASP B CB  1 
ATOM 1746 C CG  . ASP B 1 3   ? 25.14028  19.38647  52.70884  1.000 78.72897  ? 3   ASP B CG  1 
ATOM 1747 O OD1 . ASP B 1 3   ? 24.48463  19.90102  51.77740  1.000 80.27185  ? 3   ASP B OD1 1 
ATOM 1748 O OD2 . ASP B 1 3   ? 26.08216  18.58197  52.51457  1.000 78.25058  ? 3   ASP B OD2 1 
ATOM 1749 N N   . PHE B 1 4   ? 22.29374  20.54347  55.75120  1.000 70.38118  ? 4   PHE B N   1 
ATOM 1750 C CA  . PHE B 1 4   ? 21.53326  20.58818  56.98268  1.000 64.29566  ? 4   PHE B CA  1 
ATOM 1751 C C   . PHE B 1 4   ? 21.07809  19.19362  57.35388  1.000 62.53228  ? 4   PHE B C   1 
ATOM 1752 O O   . PHE B 1 4   ? 21.07807  18.27083  56.54316  1.000 65.10661  ? 4   PHE B O   1 
ATOM 1753 C CB  . PHE B 1 4   ? 20.31887  21.51048  56.89206  1.000 64.34608  ? 4   PHE B CB  1 
ATOM 1754 C CG  . PHE B 1 4   ? 19.23336  21.01557  55.98869  1.000 63.38847  ? 4   PHE B CG  1 
ATOM 1755 C CD1 . PHE B 1 4   ? 19.25412  21.29893  54.63834  1.000 64.11203  ? 4   PHE B CD1 1 
ATOM 1756 C CD2 . PHE B 1 4   ? 18.15468  20.32741  56.49870  1.000 62.64297  ? 4   PHE B CD2 1 
ATOM 1757 C CE1 . PHE B 1 4   ? 18.23879  20.87371  53.81159  1.000 60.40982  ? 4   PHE B CE1 1 
ATOM 1758 C CE2 . PHE B 1 4   ? 17.13782  19.90302  55.66804  1.000 61.32788  ? 4   PHE B CE2 1 
ATOM 1759 C CZ  . PHE B 1 4   ? 17.18970  20.17984  54.32069  1.000 59.24766  ? 4   PHE B CZ  1 
ATOM 1760 N N   . ILE B 1 5   ? 20.68717  19.06212  58.60259  1.000 61.93966  ? 5   ILE B N   1 
ATOM 1761 C CA  . ILE B 1 5   ? 20.20180  17.81288  59.14951  1.000 62.33632  ? 5   ILE B CA  1 
ATOM 1762 C C   . ILE B 1 5   ? 18.89825  18.11361  59.86725  1.000 59.82585  ? 5   ILE B C   1 
ATOM 1763 O O   . ILE B 1 5   ? 18.73319  19.19533  60.43718  1.000 58.33186  ? 5   ILE B O   1 
ATOM 1764 C CB  . ILE B 1 5   ? 21.24517  17.19459  60.09664  1.000 63.49267  ? 5   ILE B CB  1 
ATOM 1765 C CG1 . ILE B 1 5   ? 20.81321  15.80913  60.55883  1.000 59.08724  ? 5   ILE B CG1 1 
ATOM 1766 C CG2 . ILE B 1 5   ? 21.52097  18.12751  61.25848  1.000 63.90334  ? 5   ILE B CG2 1 
ATOM 1767 C CD1 . ILE B 1 5   ? 21.90789  15.10715  61.28471  1.000 64.49439  ? 5   ILE B CD1 1 
ATOM 1768 N N   . ILE B 1 6   ? 17.95662  17.18707  59.80070  1.000 56.72647  ? 6   ILE B N   1 
ATOM 1769 C CA  . ILE B 1 6   ? 16.68790  17.34889  60.49031  1.000 58.26588  ? 6   ILE B CA  1 
ATOM 1770 C C   . ILE B 1 6   ? 16.43620  16.09684  61.31297  1.000 59.56238  ? 6   ILE B C   1 
ATOM 1771 O O   . ILE B 1 6   ? 16.94490  15.01639  60.99665  1.000 62.61852  ? 6   ILE B O   1 
ATOM 1772 C CB  . ILE B 1 6   ? 15.50968  17.60409  59.52200  1.000 58.32362  ? 6   ILE B CB  1 
ATOM 1773 C CG1 . ILE B 1 6   ? 15.33835  16.41964  58.56348  1.000 58.22740  ? 6   ILE B CG1 1 
ATOM 1774 C CG2 . ILE B 1 6   ? 15.71367  18.89392  58.77151  1.000 57.26470  ? 6   ILE B CG2 1 
ATOM 1775 C CD1 . ILE B 1 6   ? 14.03385  16.43344  57.79287  1.000 54.72695  ? 6   ILE B CD1 1 
ATOM 1776 N N   . ASP B 1 7   ? 15.66005  16.25435  62.38809  1.000 59.18388  ? 7   ASP B N   1 
ATOM 1777 C CA  . ASP B 1 7   ? 15.18497  15.14607  63.20518  1.000 58.36900  ? 7   ASP B CA  1 
ATOM 1778 C C   . ASP B 1 7   ? 13.78518  15.47975  63.68595  1.000 57.75539  ? 7   ASP B C   1 
ATOM 1779 O O   . ASP B 1 7   ? 13.56115  16.57071  64.19858  1.000 60.62554  ? 7   ASP B O   1 
ATOM 1780 C CB  . ASP B 1 7   ? 16.09804  14.89778  64.41296  1.000 60.38862  ? 7   ASP B CB  1 
ATOM 1781 C CG  . ASP B 1 7   ? 15.83787  13.54013  65.08160  1.000 66.68848  ? 7   ASP B CG  1 
ATOM 1782 O OD1 . ASP B 1 7   ? 15.00474  12.75686  64.55173  1.000 66.11862  ? 7   ASP B OD1 1 
ATOM 1783 O OD2 . ASP B 1 7   ? 16.45169  13.26081  66.14478  1.000 75.36473  ? 7   ASP B OD2 1 
ATOM 1784 N N   . PHE B 1 8   ? 12.85091  14.56209  63.52432  1.000 57.89774  ? 8   PHE B N   1 
ATOM 1785 C CA  . PHE B 1 8   ? 11.55686  14.65952  64.17649  1.000 55.57922  ? 8   PHE B CA  1 
ATOM 1786 C C   . PHE B 1 8   ? 11.47866  13.70931  65.36432  1.000 59.76524  ? 8   PHE B C   1 
ATOM 1787 O O   . PHE B 1 8   ? 12.14077  12.66995  65.39835  1.000 63.28030  ? 8   PHE B O   1 
ATOM 1788 C CB  . PHE B 1 8   ? 10.42098  14.30246  63.22989  1.000 55.77927  ? 8   PHE B CB  1 
ATOM 1789 C CG  . PHE B 1 8   ? 9.97236   15.40215  62.34827  1.000 53.56630  ? 8   PHE B CG  1 
ATOM 1790 C CD1 . PHE B 1 8   ? 9.04491   16.31056  62.79782  1.000 52.65312  ? 8   PHE B CD1 1 
ATOM 1791 C CD2 . PHE B 1 8   ? 10.41049  15.48352  61.03615  1.000 58.04516  ? 8   PHE B CD2 1 
ATOM 1792 C CE1 . PHE B 1 8   ? 8.58003   17.30585  61.98424  1.000 51.82411  ? 8   PHE B CE1 1 
ATOM 1793 C CE2 . PHE B 1 8   ? 9.95215   16.49078  60.19649  1.000 55.53308  ? 8   PHE B CE2 1 
ATOM 1794 C CZ  . PHE B 1 8   ? 9.02962   17.39831  60.67978  1.000 55.05627  ? 8   PHE B CZ  1 
ATOM 1795 N N   . GLU B 1 9   ? 10.64418  14.07143  66.33306  1.000 59.75056  ? 9   GLU B N   1 
ATOM 1796 C CA  . GLU B 1 9   ? 10.12004  13.13894  67.31743  1.000 61.63893  ? 9   GLU B CA  1 
ATOM 1797 C C   . GLU B 1 9   ? 8.61653   13.09949  67.11769  1.000 60.08301  ? 9   GLU B C   1 
ATOM 1798 O O   . GLU B 1 9   ? 7.97033   14.15080  67.07368  1.000 56.39912  ? 9   GLU B O   1 
ATOM 1799 C CB  . GLU B 1 9   ? 10.48066  13.55137  68.74954  1.000 63.55960  ? 9   GLU B CB  1 
ATOM 1800 C CG  . GLU B 1 9   ? 11.96706  13.46150  69.05259  1.000 69.27589  ? 9   GLU B CG  1 
ATOM 1801 C CD  . GLU B 1 9   ? 12.31531  13.86427  70.47956  1.000 79.62748  ? 9   GLU B CD  1 
ATOM 1802 O OE1 . GLU B 1 9   ? 11.41781  14.35978  71.18826  1.000 83.92712  ? 9   GLU B OE1 1 
ATOM 1803 O OE2 . GLU B 1 9   ? 13.48540  13.67856  70.90316  1.000 85.11891  ? 9   GLU B OE2 1 
ATOM 1804 N N   . THR B 1 10  ? 8.06572   11.89924  66.95547  1.000 59.47752  ? 10  THR B N   1 
ATOM 1805 C CA  . THR B 1 10  ? 6.70898   11.77580  66.45058  1.000 59.66853  ? 10  THR B CA  1 
ATOM 1806 C C   . THR B 1 10  ? 5.87538   10.91604  67.38050  1.000 58.66968  ? 10  THR B C   1 
ATOM 1807 O O   . THR B 1 10  ? 6.39057   10.15473  68.19572  1.000 64.03383  ? 10  THR B O   1 
ATOM 1808 C CB  . THR B 1 10  ? 6.67338   11.18794  65.02338  1.000 59.39280  ? 10  THR B CB  1 
ATOM 1809 O OG1 . THR B 1 10  ? 7.14127   9.83841   65.04431  1.000 56.91522  ? 10  THR B OG1 1 
ATOM 1810 C CG2 . THR B 1 10  ? 7.56282   12.01260  64.10125  1.000 56.53816  ? 10  THR B CG2 1 
ATOM 1811 N N   . MET B 1 11  ? 4.56568   11.08179  67.24968  1.000 58.05346  ? 11  MET B N   1 
ATOM 1812 C CA  . MET B 1 11  ? 3.56218   10.33268  67.98514  1.000 59.25938  ? 11  MET B CA  1 
ATOM 1813 C C   . MET B 1 11  ? 2.82792   9.36652   67.05014  1.000 59.42378  ? 11  MET B C   1 
ATOM 1814 O O   . MET B 1 11  ? 1.70573   8.93486   67.31870  1.000 59.93415  ? 11  MET B O   1 
ATOM 1815 C CB  . MET B 1 11  ? 2.61547   11.32609  68.67617  1.000 59.72651  ? 11  MET B CB  1 
ATOM 1816 C CG  . MET B 1 11  ? 1.70519   10.73410  69.73818  1.000 63.10492  ? 11  MET B CG  1 
ATOM 1817 S SD  . MET B 1 11  ? 2.64014   10.07150  71.12993  1.000 77.58375  ? 11  MET B SD  1 
ATOM 1818 C CE  . MET B 1 11  ? 3.06325   11.59903  71.99083  1.000 63.72628  ? 11  MET B CE  1 
ATOM 1819 N N   . GLY B 1 12  ? 3.44698   9.04834   65.92957  1.000 60.86673  ? 12  GLY B N   1 
ATOM 1820 C CA  . GLY B 1 12  ? 2.85442   8.21885   64.91516  1.000 57.10310  ? 12  GLY B CA  1 
ATOM 1821 C C   . GLY B 1 12  ? 3.96403   7.80817   63.98243  1.000 60.61408  ? 12  GLY B C   1 
ATOM 1822 O O   . GLY B 1 12  ? 5.13583   8.12573   64.21116  1.000 57.92003  ? 12  GLY B O   1 
ATOM 1823 N N   . SER B 1 13  ? 3.57932   7.10680   62.91223  1.000 61.25982  ? 13  SER B N   1 
ATOM 1824 C CA  . SER B 1 13  ? 4.56969   6.44026   62.07723  1.000 59.47441  ? 13  SER B CA  1 
ATOM 1825 C C   . SER B 1 13  ? 4.46792   6.81399   60.60095  1.000 62.57053  ? 13  SER B C   1 
ATOM 1826 O O   . SER B 1 13  ? 5.49331   6.89246   59.92188  1.000 67.77867  ? 13  SER B O   1 
ATOM 1827 C CB  . SER B 1 13  ? 4.46752   4.91863   62.28518  1.000 61.44956  ? 13  SER B CB  1 
ATOM 1828 O OG  . SER B 1 13  ? 3.16737   4.41504   61.99428  1.000 60.86630  ? 13  SER B OG  1 
ATOM 1829 N N   . GLY B 1 14  ? 3.26953   7.06078   60.08184  1.000 61.93525  ? 14  GLY B N   1 
ATOM 1830 C CA  . GLY B 1 14  ? 3.16225   7.33296   58.65505  1.000 61.05913  ? 14  GLY B CA  1 
ATOM 1831 C C   . GLY B 1 14  ? 3.74504   8.67042   58.23930  1.000 60.84948  ? 14  GLY B C   1 
ATOM 1832 O O   . GLY B 1 14  ? 4.55288   9.24391   58.97224  1.000 59.61247  ? 14  GLY B O   1 
ATOM 1833 N N   . GLU B 1 15  ? 3.37327   9.19056   57.06573  1.000 68.71540  ? 15  GLU B N   1 
ATOM 1834 C CA  . GLU B 1 15  ? 3.72727   10.58374  56.78215  1.000 66.45862  ? 15  GLU B CA  1 
ATOM 1835 C C   . GLU B 1 15  ? 2.78166   11.55900  57.47170  1.000 64.45765  ? 15  GLU B C   1 
ATOM 1836 O O   . GLU B 1 15  ? 3.12644   12.73806  57.60808  1.000 65.39056  ? 15  GLU B O   1 
ATOM 1837 C CB  . GLU B 1 15  ? 3.73460   10.88403  55.27564  1.000 63.94089  ? 15  GLU B CB  1 
ATOM 1838 C CG  . GLU B 1 15  ? 2.34973   11.00083  54.67408  1.000 63.83629  ? 15  GLU B CG  1 
ATOM 1839 C CD  . GLU B 1 15  ? 2.38346   11.11744  53.17559  1.000 65.37154  ? 15  GLU B CD  1 
ATOM 1840 O OE1 . GLU B 1 15  ? 3.49363   11.06568  52.60989  1.000 65.24272  ? 15  GLU B OE1 1 
ATOM 1841 O OE2 . GLU B 1 15  ? 1.30771   11.25146  52.55345  1.000 67.58775  ? 15  GLU B OE2 1 
ATOM 1842 N N   . LYS B 1 16  ? 1.60224   11.09840  57.90266  1.000 56.59237  ? 16  LYS B N   1 
ATOM 1843 C CA  . LYS B 1 16  ? 0.66043   11.92495  58.64123  1.000 57.99463  ? 16  LYS B CA  1 
ATOM 1844 C C   . LYS B 1 16  ? 0.90120   11.87047  60.14884  1.000 57.03265  ? 16  LYS B C   1 
ATOM 1845 O O   . LYS B 1 16  ? 0.01758   12.26893  60.92190  1.000 54.78333  ? 16  LYS B O   1 
ATOM 1846 C CB  . LYS B 1 16  ? -0.79131  11.52818  58.32773  1.000 58.09653  ? 16  LYS B CB  1 
ATOM 1847 C CG  . LYS B 1 16  ? -1.17174  11.59691  56.86446  1.000 54.05033  ? 16  LYS B CG  1 
ATOM 1848 C CD  . LYS B 1 16  ? -0.85759  12.94620  56.24308  1.000 57.58849  ? 16  LYS B CD  1 
ATOM 1849 C CE  . LYS B 1 16  ? -1.83292  14.02628  56.64871  1.000 60.33656  ? 16  LYS B CE  1 
ATOM 1850 N NZ  . LYS B 1 16  ? -1.47570  15.30391  55.97033  1.000 58.83261  ? 16  LYS B NZ  1 
ATOM 1851 N N   . ALA B 1 17  ? 2.07970   11.40037  60.57279  1.000 55.40407  ? 17  ALA B N   1 
ATOM 1852 C CA  . ALA B 1 17  ? 2.42278   11.35371  61.98923  1.000 54.24485  ? 17  ALA B CA  1 
ATOM 1853 C C   . ALA B 1 17  ? 2.23847   12.70528  62.66730  1.000 54.87154  ? 17  ALA B C   1 
ATOM 1854 O O   . ALA B 1 17  ? 2.76273   13.73351  62.21711  1.000 51.86422  ? 17  ALA B O   1 
ATOM 1855 C CB  . ALA B 1 17  ? 3.86766   10.89108  62.16687  1.000 54.93341  ? 17  ALA B CB  1 
ATOM 1856 N N   . ALA B 1 18  ? 1.49665   12.68977  63.76847  1.000 55.87333  ? 18  ALA B N   1 
ATOM 1857 C CA  . ALA B 1 18  ? 1.52600   13.81603  64.68626  1.000 54.67399  ? 18  ALA B CA  1 
ATOM 1858 C C   . ALA B 1 18  ? 2.95204   14.02389  65.19973  1.000 55.94445  ? 18  ALA B C   1 
ATOM 1859 O O   . ALA B 1 18  ? 3.66869   13.06386  65.50120  1.000 55.07271  ? 18  ALA B O   1 
ATOM 1860 C CB  . ALA B 1 18  ? 0.54541   13.58031  65.83361  1.000 54.37358  ? 18  ALA B CB  1 
ATOM 1861 N N   . VAL B 1 19  ? 3.37571   15.28869  65.27527  1.000 56.23126  ? 19  VAL B N   1 
ATOM 1862 C CA  . VAL B 1 19  ? 4.77518   15.63793  65.50717  1.000 57.17053  ? 19  VAL B CA  1 
ATOM 1863 C C   . VAL B 1 19  ? 4.91907   16.34612  66.85265  1.000 58.98240  ? 19  VAL B C   1 
ATOM 1864 O O   . VAL B 1 19  ? 4.21540   17.32883  67.13298  1.000 59.49307  ? 19  VAL B O   1 
ATOM 1865 C CB  . VAL B 1 19  ? 5.34628   16.48786  64.35222  1.000 52.27264  ? 19  VAL B CB  1 
ATOM 1866 C CG1 . VAL B 1 19  ? 5.49774   15.62069  63.14311  1.000 53.91370  ? 19  VAL B CG1 1 
ATOM 1867 C CG2 . VAL B 1 19  ? 4.39758   17.60189  64.01109  1.000 52.71326  ? 19  VAL B CG2 1 
ATOM 1868 N N   . ILE B 1 20  ? 5.83629   15.83351  67.67734  1.000 58.75857  ? 20  ILE B N   1 
ATOM 1869 C CA  . ILE B 1 20  ? 6.16757   16.45528  68.95612  1.000 57.98272  ? 20  ILE B CA  1 
ATOM 1870 C C   . ILE B 1 20  ? 7.04464   17.67888  68.74172  1.000 59.84854  ? 20  ILE B C   1 
ATOM 1871 O O   . ILE B 1 20  ? 6.64528   18.80917  69.03342  1.000 65.33823  ? 20  ILE B O   1 
ATOM 1872 C CB  . ILE B 1 20  ? 6.86024   15.42976  69.87255  1.000 60.87164  ? 20  ILE B CB  1 
ATOM 1873 C CG1 . ILE B 1 20  ? 5.93402   14.24617  70.14624  1.000 59.67926  ? 20  ILE B CG1 1 
ATOM 1874 C CG2 . ILE B 1 20  ? 7.31789   16.07384  71.16318  1.000 65.13567  ? 20  ILE B CG2 1 
ATOM 1875 C CD1 . ILE B 1 20  ? 6.67482   13.02945  70.62089  1.000 65.44035  ? 20  ILE B CD1 1 
ATOM 1876 N N   . ASP B 1 21  ? 8.24843   17.47646  68.21463  1.000 61.21261  ? 21  ASP B N   1 
ATOM 1877 C CA  . ASP B 1 21  ? 9.15771   18.56846  67.91090  1.000 57.72226  ? 21  ASP B CA  1 
ATOM 1878 C C   . ASP B 1 21  ? 9.93798   18.25751  66.63612  1.000 59.17024  ? 21  ASP B C   1 
ATOM 1879 O O   . ASP B 1 21  ? 9.80839   17.18525  66.03964  1.000 55.01826  ? 21  ASP B O   1 
ATOM 1880 C CB  . ASP B 1 21  ? 10.16210  18.83979  69.03793  1.000 58.51284  ? 21  ASP B CB  1 
ATOM 1881 C CG  . ASP B 1 21  ? 11.13885  17.67082  69.26443  1.000 69.18994  ? 21  ASP B CG  1 
ATOM 1882 O OD1 . ASP B 1 21  ? 10.79762  16.52833  68.90794  1.000 69.92412  ? 21  ASP B OD1 1 
ATOM 1883 O OD2 . ASP B 1 21  ? 12.29900  17.90568  69.69919  1.000 74.33786  ? 21  ASP B OD2 1 
ATOM 1884 N N   . LEU B 1 22  ? 10.80317  19.20863  66.27458  1.000 60.78935  ? 22  LEU B N   1 
ATOM 1885 C CA  . LEU B 1 22  ? 11.66242  19.18520  65.10510  1.000 54.57977  ? 22  LEU B CA  1 
ATOM 1886 C C   . LEU B 1 22  ? 12.95736  19.90374  65.43804  1.000 57.04072  ? 22  LEU B C   1 
ATOM 1887 O O   . LEU B 1 22  ? 12.92640  21.05684  65.86945  1.000 60.06757  ? 22  LEU B O   1 
ATOM 1888 C CB  . LEU B 1 22  ? 10.96590  19.85376  63.91494  1.000 55.25645  ? 22  LEU B CB  1 
ATOM 1889 C CG  . LEU B 1 22  ? 11.76204  20.17412  62.64382  1.000 52.86431  ? 22  LEU B CG  1 
ATOM 1890 C CD1 . LEU B 1 22  ? 12.49343  18.98231  62.06796  1.000 53.00801  ? 22  LEU B CD1 1 
ATOM 1891 C CD2 . LEU B 1 22  ? 10.80018  20.73620  61.63695  1.000 51.89647  ? 22  LEU B CD2 1 
ATOM 1892 N N   . ALA B 1 23  ? 14.08585  19.23754  65.22117  1.000 55.90146  ? 23  ALA B N   1 
ATOM 1893 C CA  . ALA B 1 23  ? 15.39881  19.85366  65.33164  1.000 59.45891  ? 23  ALA B CA  1 
ATOM 1894 C C   . ALA B 1 23  ? 16.04175  19.95824  63.94935  1.000 60.02166  ? 23  ALA B C   1 
ATOM 1895 O O   . ALA B 1 23  ? 15.94389  19.03467  63.13870  1.000 57.78935  ? 23  ALA B O   1 
ATOM 1896 C CB  . ALA B 1 23  ? 16.29367  19.04921  66.27705  1.000 62.16484  ? 23  ALA B CB  1 
ATOM 1897 N N   . VAL B 1 24  ? 16.68475  21.09038  63.67284  1.000 58.02637  ? 24  VAL B N   1 
ATOM 1898 C CA  . VAL B 1 24  ? 17.41590  21.29263  62.42903  1.000 57.86427  ? 24  VAL B CA  1 
ATOM 1899 C C   . VAL B 1 24  ? 18.70990  22.03074  62.74305  1.000 60.93241  ? 24  VAL B C   1 
ATOM 1900 O O   . VAL B 1 24  ? 18.73678  22.90464  63.61028  1.000 69.90997  ? 24  VAL B O   1 
ATOM 1901 C CB  . VAL B 1 24  ? 16.55916  22.04057  61.37969  1.000 60.68679  ? 24  VAL B CB  1 
ATOM 1902 C CG1 . VAL B 1 24  ? 16.11205  23.38962  61.88712  1.000 61.94407  ? 24  VAL B CG1 1 
ATOM 1903 C CG2 . VAL B 1 24  ? 17.31894  22.18922  60.04812  1.000 63.28799  ? 24  VAL B CG2 1 
ATOM 1904 N N   . ILE B 1 25  ? 19.79779  21.63445  62.08774  1.000 61.11968  ? 25  ILE B N   1 
ATOM 1905 C CA  . ILE B 1 25  ? 21.09296  22.30221  62.19824  1.000 64.10747  ? 25  ILE B CA  1 
ATOM 1906 C C   . ILE B 1 25  ? 21.72072  22.35756  60.80821  1.000 65.07768  ? 25  ILE B C   1 
ATOM 1907 O O   . ILE B 1 25  ? 21.65478  21.38659  60.04950  1.000 62.57877  ? 25  ILE B O   1 
ATOM 1908 C CB  . ILE B 1 25  ? 22.06300  21.57443  63.15695  1.000 67.84686  ? 25  ILE B CB  1 
ATOM 1909 C CG1 . ILE B 1 25  ? 21.45445  21.37533  64.54564  1.000 67.13290  ? 25  ILE B CG1 1 
ATOM 1910 C CG2 . ILE B 1 25  ? 23.41292  22.33461  63.24037  1.000 67.14509  ? 25  ILE B CG2 1 
ATOM 1911 C CD1 . ILE B 1 25  ? 22.22801  20.38705  65.41375  1.000 68.30225  ? 25  ILE B CD1 1 
ATOM 1912 N N   . ALA B 1 26  ? 22.36251  23.47515  60.49443  1.000 65.34800  ? 26  ALA B N   1 
ATOM 1913 C CA  . ALA B 1 26  ? 23.03308  23.68227  59.22336  1.000 65.59976  ? 26  ALA B CA  1 
ATOM 1914 C C   . ALA B 1 26  ? 24.53795  23.60044  59.43881  1.000 68.14453  ? 26  ALA B C   1 
ATOM 1915 O O   . ALA B 1 26  ? 25.15106  24.52914  59.95920  1.000 75.07145  ? 26  ALA B O   1 
ATOM 1916 C CB  . ALA B 1 26  ? 22.63598  25.02659  58.63145  1.000 69.70989  ? 26  ALA B CB  1 
ATOM 1917 N N   . PHE B 1 27  ? 25.14186  22.52553  58.98482  1.000 69.47663  ? 27  PHE B N   1 
ATOM 1918 C CA  . PHE B 1 27  ? 26.54912  22.27049  59.21336  1.000 69.61271  ? 27  PHE B CA  1 
ATOM 1919 C C   . PHE B 1 27  ? 27.33550  22.45301  57.92091  1.000 77.43874  ? 27  PHE B C   1 
ATOM 1920 O O   . PHE B 1 27  ? 26.77442  22.46899  56.82056  1.000 76.42058  ? 27  PHE B O   1 
ATOM 1921 C CB  . PHE B 1 27  ? 26.73017  20.85494  59.76149  1.000 71.19212  ? 27  PHE B CB  1 
ATOM 1922 C CG  . PHE B 1 27  ? 26.23318  19.76716  58.83164  1.000 68.09770  ? 27  PHE B CG  1 
ATOM 1923 C CD1 . PHE B 1 27  ? 24.89432  19.44931  58.77543  1.000 67.08648  ? 27  PHE B CD1 1 
ATOM 1924 C CD2 . PHE B 1 27  ? 27.11302  19.04373  58.05187  1.000 69.30059  ? 27  PHE B CD2 1 
ATOM 1925 C CE1 . PHE B 1 27  ? 24.43420  18.45181  57.94553  1.000 68.84760  ? 27  PHE B CE1 1 
ATOM 1926 C CE2 . PHE B 1 27  ? 26.66036  18.04306  57.22568  1.000 68.75379  ? 27  PHE B CE2 1 
ATOM 1927 C CZ  . PHE B 1 27  ? 25.31903  17.74041  57.17614  1.000 67.40542  ? 27  PHE B CZ  1 
ATOM 1928 N N   . ASP B 1 28  ? 28.65547  22.58416  58.07152  1.000 77.58515  ? 28  ASP B N   1 
ATOM 1929 C CA  . ASP B 1 28  ? 29.55841  22.83792  56.95851  1.000 75.86181  ? 28  ASP B CA  1 
ATOM 1930 C C   . ASP B 1 28  ? 30.12782  21.51915  56.45647  1.000 76.64023  ? 28  ASP B C   1 
ATOM 1931 O O   . ASP B 1 28  ? 30.93422  20.89591  57.16303  1.000 76.38323  ? 28  ASP B O   1 
ATOM 1932 C CB  . ASP B 1 28  ? 30.67521  23.77996  57.41343  1.000 81.33855  ? 28  ASP B CB  1 
ATOM 1933 C CG  . ASP B 1 28  ? 31.63461  24.18905  56.29253  1.000 87.71088  ? 28  ASP B CG  1 
ATOM 1934 O OD1 . ASP B 1 28  ? 31.55415  23.63287  55.16081  1.000 89.94363  ? 28  ASP B OD1 1 
ATOM 1935 O OD2 . ASP B 1 28  ? 32.47192  25.09681  56.55768  1.000 82.33310  ? 28  ASP B OD2 1 
ATOM 1936 N N   . PRO B 1 29  ? 29.78089  21.07324  55.24296  1.000 81.96507  ? 29  PRO B N   1 
ATOM 1937 C CA  . PRO B 1 29  ? 30.13458  19.70584  54.82200  1.000 79.48394  ? 29  PRO B CA  1 
ATOM 1938 C C   . PRO B 1 29  ? 31.60006  19.48982  54.47645  1.000 83.57031  ? 29  PRO B C   1 
ATOM 1939 O O   . PRO B 1 29  ? 31.96432  18.35303  54.16991  1.000 85.58103  ? 29  PRO B O   1 
ATOM 1940 C CB  . PRO B 1 29  ? 29.24907  19.48590  53.59739  1.000 72.39453  ? 29  PRO B CB  1 
ATOM 1941 C CG  . PRO B 1 29  ? 28.99304  20.83890  53.08148  1.000 76.22944  ? 29  PRO B CG  1 
ATOM 1942 C CD  . PRO B 1 29  ? 28.93890  21.75743  54.24576  1.000 77.78842  ? 29  PRO B CD  1 
ATOM 1943 N N   . ASN B 1 30  ? 32.44746  20.51339  54.54010  1.000 85.89316  ? 30  ASN B N   1 
ATOM 1944 C CA  . ASN B 1 30  ? 33.86366  20.39688  54.19272  1.000 91.46218  ? 30  ASN B CA  1 
ATOM 1945 C C   . ASN B 1 30  ? 34.56726  19.38736  55.09192  1.000 93.75318  ? 30  ASN B C   1 
ATOM 1946 O O   . ASN B 1 30  ? 34.55043  19.54686  56.32209  1.000 94.84480  ? 30  ASN B O   1 
ATOM 1947 C CB  . ASN B 1 30  ? 34.52979  21.77175  54.32081  1.000 97.46924  ? 30  ASN B CB  1 
ATOM 1948 C CG  . ASN B 1 30  ? 35.98854  21.78217  53.87194  1.000 100.68061 ? 30  ASN B CG  1 
ATOM 1949 O OD1 . ASN B 1 30  ? 36.56198  20.75352  53.50661  1.000 99.94001  ? 30  ASN B OD1 1 
ATOM 1950 N ND2 . ASN B 1 30  ? 36.59232  22.96425  53.90170  1.000 102.40322 ? 30  ASN B ND2 1 
ATOM 1951 N N   . PRO B 1 31  ? 35.20611  18.35510  54.53549  1.000 97.46011  ? 31  PRO B N   1 
ATOM 1952 C CA  . PRO B 1 31  ? 35.90291  17.38064  55.38988  1.000 99.74619  ? 31  PRO B CA  1 
ATOM 1953 C C   . PRO B 1 31  ? 37.12324  17.94574  56.09574  1.000 104.33780 ? 31  PRO B C   1 
ATOM 1954 O O   . PRO B 1 31  ? 37.63357  17.29901  57.02023  1.000 102.68063 ? 31  PRO B O   1 
ATOM 1955 C CB  . PRO B 1 31  ? 36.27247  16.25259  54.41324  1.000 94.51801  ? 31  PRO B CB  1 
ATOM 1956 C CG  . PRO B 1 31  ? 36.22732  16.86898  53.06577  1.000 94.65465  ? 31  PRO B CG  1 
ATOM 1957 C CD  . PRO B 1 31  ? 35.17803  17.93912  53.12256  1.000 95.72058  ? 31  PRO B CD  1 
ATOM 1958 N N   . GLU B 1 32  ? 37.60689  19.12408  55.70088  1.000 116.99435 ? 32  GLU B N   1 
ATOM 1959 C CA  . GLU B 1 32  ? 38.69094  19.74645  56.45032  1.000 117.82745 ? 32  GLU B CA  1 
ATOM 1960 C C   . GLU B 1 32  ? 38.16469  20.47262  57.68585  1.000 118.64877 ? 32  GLU B C   1 
ATOM 1961 O O   . GLU B 1 32  ? 38.83802  20.50656  58.72018  1.000 120.00748 ? 32  GLU B O   1 
ATOM 1962 C CB  . GLU B 1 32  ? 39.47320  20.70618  55.55254  1.000 118.29528 ? 32  GLU B CB  1 
ATOM 1963 C CG  . GLU B 1 32  ? 40.13621  20.03982  54.35685  1.000 123.08417 ? 32  GLU B CG  1 
ATOM 1964 C CD  . GLU B 1 32  ? 41.01667  20.99257  53.56685  1.000 134.06388 ? 32  GLU B CD  1 
ATOM 1965 O OE1 . GLU B 1 32  ? 41.09315  22.17697  53.95167  1.000 136.50611 ? 32  GLU B OE1 1 
ATOM 1966 O OE2 . GLU B 1 32  ? 41.62078  20.56425  52.55500  1.000 138.73784 ? 32  GLU B OE2 1 
ATOM 1967 N N   . VAL B 1 33  ? 36.97100  21.05444  57.59629  1.000 104.07278 ? 33  VAL B N   1 
ATOM 1968 C CA  . VAL B 1 33  ? 36.38069  21.79876  58.70556  1.000 100.42766 ? 33  VAL B CA  1 
ATOM 1969 C C   . VAL B 1 33  ? 35.77236  20.81239  59.68691  1.000 99.27371  ? 33  VAL B C   1 
ATOM 1970 O O   . VAL B 1 33  ? 35.02073  19.91993  59.28344  1.000 103.69948 ? 33  VAL B O   1 
ATOM 1971 C CB  . VAL B 1 33  ? 35.31262  22.77441  58.19152  1.000 94.58139  ? 33  VAL B CB  1 
ATOM 1972 C CG1 . VAL B 1 33  ? 34.66014  23.51310  59.34206  1.000 92.02038  ? 33  VAL B CG1 1 
ATOM 1973 C CG2 . VAL B 1 33  ? 35.90680  23.72652  57.18262  1.000 99.53387  ? 33  VAL B CG2 1 
ATOM 1974 N N   . VAL B 1 34  ? 36.07279  20.97412  60.97591  1.000 95.42444  ? 34  VAL B N   1 
ATOM 1975 C CA  . VAL B 1 34  ? 35.53279  20.10643  62.02570  1.000 91.92044  ? 34  VAL B CA  1 
ATOM 1976 C C   . VAL B 1 34  ? 34.96652  21.01363  63.11211  1.000 93.38963  ? 34  VAL B C   1 
ATOM 1977 O O   . VAL B 1 34  ? 35.68653  21.43575  64.02139  1.000 96.94573  ? 34  VAL B O   1 
ATOM 1978 C CB  . VAL B 1 34  ? 36.58345  19.14997  62.59717  1.000 87.24866  ? 34  VAL B CB  1 
ATOM 1979 N N   . GLU B 1 35  ? 33.66798  21.31716  63.03280  1.000 91.19792  ? 35  GLU B N   1 
ATOM 1980 C CA  . GLU B 1 35  ? 33.02258  22.14805  64.04155  1.000 90.13361  ? 35  GLU B CA  1 
ATOM 1981 C C   . GLU B 1 35  ? 32.74789  21.31688  65.28794  1.000 96.07856  ? 35  GLU B C   1 
ATOM 1982 O O   . GLU B 1 35  ? 32.43710  20.12374  65.18839  1.000 94.23159  ? 35  GLU B O   1 
ATOM 1983 C CB  . GLU B 1 35  ? 31.72139  22.74395  63.50386  1.000 87.00174  ? 35  GLU B CB  1 
ATOM 1984 N N   . THR B 1 36  ? 32.85722  21.95718  66.46132  1.000 97.43129  ? 36  THR B N   1 
ATOM 1985 C CA  . THR B 1 36  ? 32.70435  21.31837  67.76712  1.000 96.21733  ? 36  THR B CA  1 
ATOM 1986 C C   . THR B 1 36  ? 31.22733  21.11061  68.11797  1.000 93.82053  ? 36  THR B C   1 
ATOM 1987 O O   . THR B 1 36  ? 30.32844  21.77156  67.59001  1.000 93.51898  ? 36  THR B O   1 
ATOM 1988 C CB  . THR B 1 36  ? 33.38736  22.16190  68.86006  1.000 99.40368  ? 36  THR B CB  1 
ATOM 1989 O OG1 . THR B 1 36  ? 34.76816  22.36556  68.52753  1.000 103.42278 ? 36  THR B OG1 1 
ATOM 1990 C CG2 . THR B 1 36  ? 33.29194  21.51992  70.26192  1.000 95.34982  ? 36  THR B CG2 1 
ATOM 1991 N N   . PHE B 1 37  ? 30.99656  20.16534  69.03251  1.000 93.30052  ? 37  PHE B N   1 
ATOM 1992 C CA  . PHE B 1 37  ? 29.66684  19.90436  69.57379  1.000 91.76618  ? 37  PHE B CA  1 
ATOM 1993 C C   . PHE B 1 37  ? 28.99432  21.15539  70.14906  1.000 92.52422  ? 37  PHE B C   1 
ATOM 1994 O O   . PHE B 1 37  ? 27.77121  21.31239  70.03920  1.000 89.16902  ? 37  PHE B O   1 
ATOM 1995 C CB  . PHE B 1 37  ? 29.78233  18.80767  70.63369  1.000 87.09292  ? 37  PHE B CB  1 
ATOM 1996 C CG  . PHE B 1 37  ? 28.49404  18.46814  71.29874  1.000 84.94526  ? 37  PHE B CG  1 
ATOM 1997 C CD1 . PHE B 1 37  ? 27.45267  17.92123  70.57909  1.000 85.57015  ? 37  PHE B CD1 1 
ATOM 1998 C CD2 . PHE B 1 37  ? 28.34032  18.63278  72.65488  1.000 88.72222  ? 37  PHE B CD2 1 
ATOM 1999 C CE1 . PHE B 1 37  ? 26.25814  17.58694  71.19886  1.000 88.44578  ? 37  PHE B CE1 1 
ATOM 2000 C CE2 . PHE B 1 37  ? 27.14790  18.29787  73.28186  1.000 90.47553  ? 37  PHE B CE2 1 
ATOM 2001 C CZ  . PHE B 1 37  ? 26.10708  17.77297  72.55367  1.000 88.76019  ? 37  PHE B CZ  1 
ATOM 2002 N N   . ASP B 1 38  ? 29.76376  22.05415  70.77263  1.000 93.19761  ? 38  ASP B N   1 
ATOM 2003 C CA  . ASP B 1 38  ? 29.13535  23.18270  71.45950  1.000 96.01323  ? 38  ASP B CA  1 
ATOM 2004 C C   . ASP B 1 38  ? 28.46209  24.13428  70.47246  1.000 96.73168  ? 38  ASP B C   1 
ATOM 2005 O O   . ASP B 1 38  ? 27.30455  24.52369  70.66590  1.000 95.75069  ? 38  ASP B O   1 
ATOM 2006 C CB  . ASP B 1 38  ? 30.15105  23.92582  72.34063  1.000 97.96643  ? 38  ASP B CB  1 
ATOM 2007 N N   . GLU B 1 39  ? 29.15832  24.52164  69.40530  1.000 110.29259 ? 39  GLU B N   1 
ATOM 2008 C CA  . GLU B 1 39  ? 28.55718  25.47453  68.47796  1.000 110.13584 ? 39  GLU B CA  1 
ATOM 2009 C C   . GLU B 1 39  ? 27.67070  24.82001  67.42499  1.000 109.74764 ? 39  GLU B C   1 
ATOM 2010 O O   . GLU B 1 39  ? 26.90171  25.52743  66.76582  1.000 109.57317 ? 39  GLU B O   1 
ATOM 2011 C CB  . GLU B 1 39  ? 29.63782  26.29901  67.79515  1.000 110.66769 ? 39  GLU B CB  1 
ATOM 2012 C CG  . GLU B 1 39  ? 30.48239  25.49816  66.85465  1.000 114.87232 ? 39  GLU B CG  1 
ATOM 2013 C CD  . GLU B 1 39  ? 31.56539  24.73185  67.58172  1.000 116.33565 ? 39  GLU B CD  1 
ATOM 2014 O OE1 . GLU B 1 39  ? 31.40702  24.49545  68.80423  1.000 112.23299 ? 39  GLU B OE1 1 
ATOM 2015 O OE2 . GLU B 1 39  ? 32.58234  24.39201  66.93402  1.000 119.56489 ? 39  GLU B OE2 1 
ATOM 2016 N N   . LEU B 1 40  ? 27.76774  23.50258  67.22973  1.000 95.14197  ? 40  LEU B N   1 
ATOM 2017 C CA  . LEU B 1 40  ? 26.70805  22.79711  66.51444  1.000 87.80682  ? 40  LEU B CA  1 
ATOM 2018 C C   . LEU B 1 40  ? 25.39657  22.85342  67.28808  1.000 87.05135  ? 40  LEU B C   1 
ATOM 2019 O O   . LEU B 1 40  ? 24.33250  23.13471  66.71987  1.000 80.84810  ? 40  LEU B O   1 
ATOM 2020 C CB  . LEU B 1 40  ? 27.11961  21.35176  66.23508  1.000 84.65139  ? 40  LEU B CB  1 
ATOM 2021 C CG  . LEU B 1 40  ? 28.03762  21.24943  65.01648  1.000 84.81793  ? 40  LEU B CG  1 
ATOM 2022 C CD1 . LEU B 1 40  ? 28.61940  19.86115  64.83259  1.000 81.96223  ? 40  LEU B CD1 1 
ATOM 2023 C CD2 . LEU B 1 40  ? 27.24542  21.65419  63.79093  1.000 76.41037  ? 40  LEU B CD2 1 
ATOM 2024 N N   . VAL B 1 41  ? 25.44972  22.60521  68.59510  1.000 87.86238  ? 41  VAL B N   1 
ATOM 2025 C CA  . VAL B 1 41  ? 24.23047  22.71887  69.38050  1.000 83.55822  ? 41  VAL B CA  1 
ATOM 2026 C C   . VAL B 1 41  ? 23.75656  24.16365  69.40769  1.000 80.59635  ? 41  VAL B C   1 
ATOM 2027 O O   . VAL B 1 41  ? 22.55897  24.43864  69.27735  1.000 77.18235  ? 41  VAL B O   1 
ATOM 2028 C CB  . VAL B 1 41  ? 24.44529  22.14481  70.78874  1.000 84.91504  ? 41  VAL B CB  1 
ATOM 2029 C CG1 . VAL B 1 41  ? 23.23792  22.43081  71.67138  1.000 85.74123  ? 41  VAL B CG1 1 
ATOM 2030 C CG2 . VAL B 1 41  ? 24.67340  20.65518  70.69801  1.000 83.58786  ? 41  VAL B CG2 1 
ATOM 2031 N N   . SER B 1 42  ? 24.68352  25.11214  69.54178  1.000 81.31988  ? 42  SER B N   1 
ATOM 2032 C CA  . SER B 1 42  ? 24.25628  26.50446  69.61097  1.000 84.67678  ? 42  SER B CA  1 
ATOM 2033 C C   . SER B 1 42  ? 23.65167  26.95298  68.29435  1.000 81.43542  ? 42  SER B C   1 
ATOM 2034 O O   . SER B 1 42  ? 22.73787  27.78833  68.28160  1.000 77.64129  ? 42  SER B O   1 
ATOM 2035 C CB  . SER B 1 42  ? 25.41994  27.42425  69.97856  1.000 87.57472  ? 42  SER B CB  1 
ATOM 2036 O OG  . SER B 1 42  ? 26.28803  27.60006  68.88046  1.000 88.18068  ? 42  SER B OG  1 
ATOM 2037 N N   . ARG B 1 43  ? 24.14300  26.40521  67.18235  1.000 80.63135  ? 43  ARG B N   1 
ATOM 2038 C CA  . ARG B 1 43  ? 23.66449  26.84082  65.88068  1.000 74.71423  ? 43  ARG B CA  1 
ATOM 2039 C C   . ARG B 1 43  ? 22.28407  26.27896  65.55645  1.000 73.72480  ? 43  ARG B C   1 
ATOM 2040 O O   . ARG B 1 43  ? 21.53488  26.91434  64.81181  1.000 74.03866  ? 43  ARG B O   1 
ATOM 2041 C CB  . ARG B 1 43  ? 24.66997  26.46304  64.79878  1.000 73.50941  ? 43  ARG B CB  1 
ATOM 2042 C CG  . ARG B 1 43  ? 24.32734  27.03392  63.44536  1.000 76.62833  ? 43  ARG B CG  1 
ATOM 2043 C CD  . ARG B 1 43  ? 25.25619  26.55218  62.29416  1.000 76.92256  ? 43  ARG B CD  1 
ATOM 2044 N NE  . ARG B 1 43  ? 26.64670  26.98538  62.38042  1.000 74.42026  ? 43  ARG B NE  1 
ATOM 2045 C CZ  . ARG B 1 43  ? 27.68458  26.16403  62.46514  1.000 78.50272  ? 43  ARG B CZ  1 
ATOM 2046 N NH1 . ARG B 1 43  ? 27.53135  24.85084  62.44551  1.000 76.93564  ? 43  ARG B NH1 1 
ATOM 2047 N NH2 . ARG B 1 43  ? 28.91025  26.67348  62.56327  1.000 83.95975  ? 43  ARG B NH2 1 
ATOM 2048 N N   . GLY B 1 44  ? 21.91578  25.10680  66.10054  1.000 72.03894  ? 44  GLY B N   1 
ATOM 2049 C CA  . GLY B 1 44  ? 20.61680  24.53660  65.80714  1.000 69.94197  ? 44  GLY B CA  1 
ATOM 2050 C C   . GLY B 1 44  ? 19.49045  25.09966  66.66563  1.000 74.92184  ? 44  GLY B C   1 
ATOM 2051 O O   . GLY B 1 44  ? 19.70565  25.75354  67.68612  1.000 74.93896  ? 44  GLY B O   1 
ATOM 2052 N N   . ILE B 1 45  ? 18.25300  24.84044  66.22859  1.000 76.56437  ? 45  ILE B N   1 
ATOM 2053 C CA  . ILE B 1 45  ? 17.06073  25.25224  66.96708  1.000 77.20428  ? 45  ILE B CA  1 
ATOM 2054 C C   . ILE B 1 45  ? 16.08403  24.08244  67.01057  1.000 77.39928  ? 45  ILE B C   1 
ATOM 2055 O O   . ILE B 1 45  ? 16.04652  23.25487  66.09691  1.000 76.52288  ? 45  ILE B O   1 
ATOM 2056 C CB  . ILE B 1 45  ? 16.36398  26.49278  66.35089  1.000 77.77387  ? 45  ILE B CB  1 
ATOM 2057 C CG1 . ILE B 1 45  ? 15.71752  26.13686  65.01068  1.000 77.79497  ? 45  ILE B CG1 1 
ATOM 2058 C CG2 . ILE B 1 45  ? 17.35107  27.62899  66.15102  1.000 78.71002  ? 45  ILE B CG2 1 
ATOM 2059 C CD1 . ILE B 1 45  ? 14.78847  27.21292  64.46085  1.000 78.38513  ? 45  ILE B CD1 1 
ATOM 2060 N N   . LYS B 1 46  ? 15.29390  24.00518  68.08460  1.000 67.80230  ? 46  LYS B N   1 
ATOM 2061 C CA  . LYS B 1 46  ? 14.25352  22.98992  68.21736  1.000 64.47261  ? 46  LYS B CA  1 
ATOM 2062 C C   . LYS B 1 46  ? 12.88681  23.66225  68.17610  1.000 61.79076  ? 46  LYS B C   1 
ATOM 2063 O O   . LYS B 1 46  ? 12.63749  24.62053  68.90921  1.000 62.53339  ? 46  LYS B O   1 
ATOM 2064 C CB  . LYS B 1 46  ? 14.41133  22.17089  69.50270  1.000 58.15415  ? 46  LYS B CB  1 
ATOM 2065 N N   . ILE B 1 47  ? 12.02215  23.17895  67.29259  1.000 61.13264  ? 47  ILE B N   1 
ATOM 2066 C CA  . ILE B 1 47  ? 10.67537  23.70150  67.11756  1.000 58.41652  ? 47  ILE B CA  1 
ATOM 2067 C C   . ILE B 1 47  ? 9.74702   22.72688  67.80116  1.000 56.90443  ? 47  ILE B C   1 
ATOM 2068 O O   . ILE B 1 47  ? 9.83326   21.52677  67.55908  1.000 63.34265  ? 47  ILE B O   1 
ATOM 2069 C CB  . ILE B 1 47  ? 10.30046  23.84003  65.62830  1.000 61.95045  ? 47  ILE B CB  1 
ATOM 2070 C CG1 . ILE B 1 47  ? 11.24970  24.76267  64.87248  1.000 61.32485  ? 47  ILE B CG1 1 
ATOM 2071 C CG2 . ILE B 1 47  ? 8.88052   24.35012  65.48304  1.000 66.58475  ? 47  ILE B CG2 1 
ATOM 2072 C CD1 . ILE B 1 47  ? 12.37393  24.03192  64.24383  1.000 62.36509  ? 47  ILE B CD1 1 
ATOM 2073 N N   . LYS B 1 48  ? 8.87283   23.21542  68.65925  1.000 63.62316  ? 48  LYS B N   1 
ATOM 2074 C CA  . LYS B 1 48  ? 8.02843   22.33739  69.45279  1.000 63.90269  ? 48  LYS B CA  1 
ATOM 2075 C C   . LYS B 1 48  ? 6.57457   22.56783  69.07249  1.000 65.01515  ? 48  LYS B C   1 
ATOM 2076 O O   . LYS B 1 48  ? 6.11407   23.70984  69.01933  1.000 68.57282  ? 48  LYS B O   1 
ATOM 2077 C CB  . LYS B 1 48  ? 8.25973   22.56035  70.94869  1.000 65.62985  ? 48  LYS B CB  1 
ATOM 2078 C CG  . LYS B 1 48  ? 7.58715   21.52154  71.81089  1.000 73.39753  ? 48  LYS B CG  1 
ATOM 2079 C CD  . LYS B 1 48  ? 7.84094   21.74038  73.29089  1.000 74.59229  ? 48  LYS B CD  1 
ATOM 2080 C CE  . LYS B 1 48  ? 7.12688   20.68062  74.05868  1.000 69.46920  ? 48  LYS B CE  1 
ATOM 2081 N NZ  . LYS B 1 48  ? 5.68772   20.85519  73.78033  1.000 69.14019  ? 48  LYS B NZ  1 
ATOM 2082 N N   . PHE B 1 49  ? 5.86496   21.48528  68.79367  1.000 65.72384  ? 49  PHE B N   1 
ATOM 2083 C CA  . PHE B 1 49  ? 4.52325   21.53864  68.23225  1.000 69.43605  ? 49  PHE B CA  1 
ATOM 2084 C C   . PHE B 1 49  ? 3.49220   21.28989  69.33395  1.000 69.89284  ? 49  PHE B C   1 
ATOM 2085 O O   . PHE B 1 49  ? 3.76288   20.57138  70.30333  1.000 71.33884  ? 49  PHE B O   1 
ATOM 2086 C CB  . PHE B 1 49  ? 4.38483   20.50468  67.08642  1.000 62.38344  ? 49  PHE B CB  1 
ATOM 2087 C CG  . PHE B 1 49  ? 5.32191   20.75808  65.91496  1.000 60.63824  ? 49  PHE B CG  1 
ATOM 2088 C CD1 . PHE B 1 49  ? 5.04549   21.74408  64.98134  1.000 62.00773  ? 49  PHE B CD1 1 
ATOM 2089 C CD2 . PHE B 1 49  ? 6.48916   20.02181  65.76242  1.000 61.23777  ? 49  PHE B CD2 1 
ATOM 2090 C CE1 . PHE B 1 49  ? 5.91050   21.99389  63.91881  1.000 61.65051  ? 49  PHE B CE1 1 
ATOM 2091 C CE2 . PHE B 1 49  ? 7.35111   20.27121  64.69538  1.000 59.25377  ? 49  PHE B CE2 1 
ATOM 2092 C CZ  . PHE B 1 49  ? 7.05205   21.26143  63.77467  1.000 56.85559  ? 49  PHE B CZ  1 
ATOM 2093 N N   . ASP B 1 50  ? 2.30972   21.89537  69.18865  1.000 75.91798  ? 50  ASP B N   1 
ATOM 2094 C CA  . ASP B 1 50  ? 1.21398   21.65804  70.12872  1.000 77.93767  ? 50  ASP B CA  1 
ATOM 2095 C C   . ASP B 1 50  ? 0.43361   20.39543  69.76172  1.000 76.32545  ? 50  ASP B C   1 
ATOM 2096 O O   . ASP B 1 50  ? -0.23279  20.35931  68.72245  1.000 76.19831  ? 50  ASP B O   1 
ATOM 2097 C CB  . ASP B 1 50  ? 0.26820   22.85695  70.18269  1.000 76.22172  ? 50  ASP B CB  1 
ATOM 2098 C CG  . ASP B 1 50  ? -1.01955  22.53216  70.92623  1.000 82.01333  ? 50  ASP B CG  1 
ATOM 2099 O OD1 . ASP B 1 50  ? -0.98233  22.30681  72.15698  1.000 85.51747  ? 50  ASP B OD1 1 
ATOM 2100 O OD2 . ASP B 1 50  ? -2.07804  22.47686  70.27407  1.000 83.12729  ? 50  ASP B OD2 1 
ATOM 2101 N N   . LEU B 1 51  ? 0.47364   19.37659  70.63623  1.000 72.37574  ? 51  LEU B N   1 
ATOM 2102 C CA  . LEU B 1 51  ? -0.18718  18.10986  70.31726  1.000 68.95846  ? 51  LEU B CA  1 
ATOM 2103 C C   . LEU B 1 51  ? -1.70186  18.24926  70.21821  1.000 73.19780  ? 51  LEU B C   1 
ATOM 2104 O O   . LEU B 1 51  ? -2.31353  17.68548  69.30340  1.000 72.22544  ? 51  LEU B O   1 
ATOM 2105 C CB  . LEU B 1 51  ? 0.15313   17.01500  71.33363  1.000 60.96083  ? 51  LEU B CB  1 
ATOM 2106 C CG  . LEU B 1 51  ? 1.56581   16.43549  71.25075  1.000 60.67285  ? 51  LEU B CG  1 
ATOM 2107 C CD1 . LEU B 1 51  ? 1.75976   15.23023  72.17021  1.000 54.83662  ? 51  LEU B CD1 1 
ATOM 2108 C CD2 . LEU B 1 51  ? 1.91686   16.08927  69.81311  1.000 63.25969  ? 51  LEU B CD2 1 
ATOM 2109 N N   . LYS B 1 52  ? -2.33562  18.96681  71.14768  1.000 71.56420  ? 52  LYS B N   1 
ATOM 2110 C CA  . LYS B 1 52  ? -3.77933  18.82122  71.25783  1.000 71.76864  ? 52  LYS B CA  1 
ATOM 2111 C C   . LYS B 1 52  ? -4.48401  19.23811  69.97331  1.000 72.59962  ? 52  LYS B C   1 
ATOM 2112 O O   . LYS B 1 52  ? -5.52228  18.66644  69.62962  1.000 74.11641  ? 52  LYS B O   1 
ATOM 2113 C CB  . LYS B 1 52  ? -4.31061  19.61383  72.45007  1.000 76.16125  ? 52  LYS B CB  1 
ATOM 2114 C CG  . LYS B 1 52  ? -5.77949  19.35433  72.74706  1.000 75.58993  ? 52  LYS B CG  1 
ATOM 2115 C CD  . LYS B 1 52  ? -6.26476  20.16796  73.94601  1.000 83.87766  ? 52  LYS B CD  1 
ATOM 2116 C CE  . LYS B 1 52  ? -7.73291  19.86247  74.31818  1.000 83.26132  ? 52  LYS B CE  1 
ATOM 2117 N NZ  . LYS B 1 52  ? -8.22625  20.71881  75.42912  1.000 66.35556  ? 52  LYS B NZ  1 
ATOM 2118 N N   . SER B 1 53  ? -3.92558  20.19574  69.23007  1.000 71.58660  ? 53  SER B N   1 
ATOM 2119 C CA  . SER B 1 53  ? -4.60629  20.73874  68.05351  1.000 71.62161  ? 53  SER B CA  1 
ATOM 2120 C C   . SER B 1 53  ? -4.34651  19.95715  66.77045  1.000 71.54758  ? 53  SER B C   1 
ATOM 2121 O O   . SER B 1 53  ? -5.05423  20.17192  65.77846  1.000 69.44400  ? 53  SER B O   1 
ATOM 2122 C CB  . SER B 1 53  ? -4.19716  22.18922  67.82527  1.000 71.51239  ? 53  SER B CB  1 
ATOM 2123 O OG  . SER B 1 53  ? -2.82881  22.23765  67.49532  1.000 73.43284  ? 53  SER B OG  1 
ATOM 2124 N N   . GLN B 1 54  ? -3.35226  19.07160  66.75952  1.000 70.22991  ? 54  GLN B N   1 
ATOM 2125 C CA  . GLN B 1 54  ? -3.20246  18.12019  65.66914  1.000 68.48743  ? 54  GLN B CA  1 
ATOM 2126 C C   . GLN B 1 54  ? -4.23246  16.99985  65.74219  1.000 69.66457  ? 54  GLN B C   1 
ATOM 2127 O O   . GLN B 1 54  ? -4.24065  16.14396  64.85484  1.000 72.28743  ? 54  GLN B O   1 
ATOM 2128 C CB  . GLN B 1 54  ? -1.78621  17.53444  65.66675  1.000 58.53986  ? 54  GLN B CB  1 
ATOM 2129 C CG  . GLN B 1 54  ? -0.70784  18.58679  65.56106  1.000 55.33230  ? 54  GLN B CG  1 
ATOM 2130 C CD  . GLN B 1 54  ? 0.66780   18.01017  65.72073  1.000 54.07299  ? 54  GLN B CD  1 
ATOM 2131 O OE1 . GLN B 1 54  ? 0.83153   16.81537  65.71031  1.000 54.87150  ? 54  GLN B OE1 1 
ATOM 2132 N NE2 . GLN B 1 54  ? 1.64825   18.85457  65.98252  1.000 59.86281  ? 54  GLN B NE2 1 
ATOM 2133 N N   . LYS B 1 55  ? -5.07480  16.96051  66.77365  1.000 75.82716  ? 55  LYS B N   1 
ATOM 2134 C CA  . LYS B 1 55  ? -6.16095  15.99342  66.79006  1.000 76.54548  ? 55  LYS B CA  1 
ATOM 2135 C C   . LYS B 1 55  ? -7.01615  16.16637  65.54284  1.000 76.64112  ? 55  LYS B C   1 
ATOM 2136 O O   . LYS B 1 55  ? -7.26499  17.28910  65.09276  1.000 73.59058  ? 55  LYS B O   1 
ATOM 2137 C CB  . LYS B 1 55  ? -7.02435  16.14808  68.04393  1.000 75.60819  ? 55  LYS B CB  1 
ATOM 2138 C CG  . LYS B 1 55  ? -6.36481  15.72946  69.34772  1.000 77.54516  ? 55  LYS B CG  1 
ATOM 2139 C CD  . LYS B 1 55  ? -7.40911  15.69928  70.48346  1.000 87.99768  ? 55  LYS B CD  1 
ATOM 2140 C CE  . LYS B 1 55  ? -7.89321  17.10579  70.90986  1.000 88.35861  ? 55  LYS B CE  1 
ATOM 2141 N NZ  . LYS B 1 55  ? -8.88355  17.08926  72.04601  1.000 90.74884  ? 55  LYS B NZ  1 
ATOM 2142 N N   . GLY B 1 56  ? -7.40349  15.03650  64.94636  1.000 76.25417  ? 56  GLY B N   1 
ATOM 2143 C CA  . GLY B 1 56  ? -8.20169  15.03344  63.74020  1.000 71.93605  ? 56  GLY B CA  1 
ATOM 2144 C C   . GLY B 1 56  ? -7.50828  15.56583  62.51098  1.000 69.96640  ? 56  GLY B C   1 
ATOM 2145 O O   . GLY B 1 56  ? -8.16492  15.74958  61.48852  1.000 72.05749  ? 56  GLY B O   1 
ATOM 2146 N N   . HIS B 1 57  ? -6.21895  15.83923  62.57693  1.000 69.38490  ? 57  HIS B N   1 
ATOM 2147 C CA  . HIS B 1 57  ? -5.47702  16.31700  61.41481  1.000 69.56499  ? 57  HIS B CA  1 
ATOM 2148 C C   . HIS B 1 57  ? -4.21741  15.51907  61.14235  1.000 67.59465  ? 57  HIS B C   1 
ATOM 2149 O O   . HIS B 1 57  ? -3.88175  15.27685  59.97814  1.000 66.30580  ? 57  HIS B O   1 
ATOM 2150 C CB  . HIS B 1 57  ? -5.11685  17.78483  61.58960  1.000 73.77480  ? 57  HIS B CB  1 
ATOM 2151 C CG  . HIS B 1 57  ? -6.28198  18.70631  61.43214  1.000 77.44243  ? 57  HIS B CG  1 
ATOM 2152 N ND1 . HIS B 1 57  ? -6.83196  18.99676  60.19977  1.000 79.13957  ? 57  HIS B ND1 1 
ATOM 2153 C CD2 . HIS B 1 57  ? -7.00454  19.39851  62.34431  1.000 76.97528  ? 57  HIS B CD2 1 
ATOM 2154 C CE1 . HIS B 1 57  ? -7.84429  19.83120  60.36305  1.000 82.77402  ? 57  HIS B CE1 1 
ATOM 2155 N NE2 . HIS B 1 57  ? -7.96648  20.09474  61.65337  1.000 79.67967  ? 57  HIS B NE2 1 
ATOM 2156 N N   . ARG B 1 58  ? -3.50654  15.11757  62.18172  1.000 62.22819  ? 58  ARG B N   1 
ATOM 2157 C CA  . ARG B 1 58  ? -2.40183  14.19632  62.06713  1.000 55.63539  ? 58  ARG B CA  1 
ATOM 2158 C C   . ARG B 1 58  ? -2.74430  12.99392  62.92911  1.000 59.15610  ? 58  ARG B C   1 
ATOM 2159 O O   . ARG B 1 58  ? -3.79836  12.95252  63.56203  1.000 62.62403  ? 58  ARG B O   1 
ATOM 2160 C CB  . ARG B 1 58  ? -1.10139  14.88867  62.45313  1.000 51.99461  ? 58  ARG B CB  1 
ATOM 2161 C CG  . ARG B 1 58  ? -0.93558  16.12424  61.57759  1.000 55.49933  ? 58  ARG B CG  1 
ATOM 2162 C CD  . ARG B 1 58  ? 0.37964   16.84101  61.70810  1.000 53.32398  ? 58  ARG B CD  1 
ATOM 2163 N NE  . ARG B 1 58  ? 1.45306   15.92181  61.37289  1.000 54.75990  ? 58  ARG B NE  1 
ATOM 2164 C CZ  . ARG B 1 58  ? 1.73625   15.53553  60.14123  1.000 50.10232  ? 58  ARG B CZ  1 
ATOM 2165 N NH1 . ARG B 1 58  ? 1.03487   15.94598  59.10889  1.000 49.68158  ? 58  ARG B NH1 1 
ATOM 2166 N NH2 . ARG B 1 58  ? 2.72529   14.68908  59.94882  1.000 53.21361  ? 58  ARG B NH2 1 
ATOM 2167 N N   . LEU B 1 59  ? -1.88787  11.98389  62.91315  1.000 57.79553  ? 59  LEU B N   1 
ATOM 2168 C CA  . LEU B 1 59  ? -2.26264  10.65446  63.36548  1.000 55.66100  ? 59  LEU B CA  1 
ATOM 2169 C C   . LEU B 1 59  ? -1.42020  10.21931  64.54725  1.000 57.90977  ? 59  LEU B C   1 
ATOM 2170 O O   . LEU B 1 59  ? -0.18850  10.31740  64.50455  1.000 55.11155  ? 59  LEU B O   1 
ATOM 2171 C CB  . LEU B 1 59  ? -2.10300  9.64521   62.23635  1.000 59.95978  ? 59  LEU B CB  1 
ATOM 2172 C CG  . LEU B 1 59  ? -2.26267  8.16920   62.60218  1.000 60.28224  ? 59  LEU B CG  1 
ATOM 2173 C CD1 . LEU B 1 59  ? -3.68668  7.79892   63.04069  1.000 60.10900  ? 59  LEU B CD1 1 
ATOM 2174 C CD2 . LEU B 1 59  ? -1.80130  7.31657   61.43536  1.000 61.51108  ? 59  LEU B CD2 1 
ATOM 2175 N N   . PHE B 1 60  ? -2.08515  9.69160   65.58085  1.000 61.09385  ? 60  PHE B N   1 
ATOM 2176 C CA  . PHE B 1 60  ? -1.39707  9.14384   66.74443  1.000 59.09060  ? 60  PHE B CA  1 
ATOM 2177 C C   . PHE B 1 60  ? -1.56495  7.63291   66.70807  1.000 60.26754  ? 60  PHE B C   1 
ATOM 2178 O O   . PHE B 1 60  ? -2.68733  7.12848   66.68671  1.000 65.79338  ? 60  PHE B O   1 
ATOM 2179 C CB  . PHE B 1 60  ? -1.89827  9.69011   68.09144  1.000 61.02086  ? 60  PHE B CB  1 
ATOM 2180 C CG  . PHE B 1 60  ? -2.12912  11.18935  68.13204  1.000 58.66647  ? 60  PHE B CG  1 
ATOM 2181 C CD1 . PHE B 1 60  ? -2.90495  11.84116  67.18506  1.000 58.27668  ? 60  PHE B CD1 1 
ATOM 2182 C CD2 . PHE B 1 60  ? -1.36287  11.96550  68.97950  1.000 55.04890  ? 60  PHE B CD2 1 
ATOM 2183 C CE1 . PHE B 1 60  ? -3.06359  13.20517  67.20929  1.000 58.97017  ? 60  PHE B CE1 1 
ATOM 2184 C CE2 . PHE B 1 60  ? -1.49066  13.33173  68.98284  1.000 55.58940  ? 60  PHE B CE2 1 
ATOM 2185 C CZ  . PHE B 1 60  ? -2.34607  13.94858  68.09497  1.000 60.59984  ? 60  PHE B CZ  1 
ATOM 2186 N N   . THR B 1 61  ? -0.45844  6.91926   66.68167  1.000 62.99405  ? 61  THR B N   1 
ATOM 2187 C CA  . THR B 1 61  ? -0.45380  5.48242   66.46565  1.000 62.42395  ? 61  THR B CA  1 
ATOM 2188 C C   . THR B 1 61  ? -0.27538  4.83600   67.82731  1.000 65.17677  ? 61  THR B C   1 
ATOM 2189 O O   . THR B 1 61  ? 0.72729   5.09431   68.50416  1.000 64.92167  ? 61  THR B O   1 
ATOM 2190 C CB  . THR B 1 61  ? 0.67752   5.10056   65.49365  1.000 65.71230  ? 61  THR B CB  1 
ATOM 2191 O OG1 . THR B 1 61  ? 0.46397   5.75101   64.23688  1.000 59.78422  ? 61  THR B OG1 1 
ATOM 2192 C CG2 . THR B 1 61  ? 0.79720   3.58868   65.25052  1.000 66.37829  ? 61  THR B CG2 1 
ATOM 2193 N N   . LYS B 1 62  ? -1.26700  4.03420   68.23463  1.000 66.04803  ? 62  LYS B N   1 
ATOM 2194 C CA  . LYS B 1 62  ? -1.23981  3.20282   69.44111  1.000 67.69037  ? 62  LYS B CA  1 
ATOM 2195 C C   . LYS B 1 62  ? 0.11679   2.52172   69.63060  1.000 67.72047  ? 62  LYS B C   1 
ATOM 2196 O O   . LYS B 1 62  ? 0.63893   2.44181   70.74484  1.000 68.03143  ? 62  LYS B O   1 
ATOM 2197 C CB  . LYS B 1 62  ? -2.36740  2.15384   69.36358  1.000 67.18060  ? 62  LYS B CB  1 
ATOM 2198 C CG  . LYS B 1 62  ? -2.52111  1.24075   70.56927  1.000 65.81255  ? 62  LYS B CG  1 
ATOM 2199 C CD  . LYS B 1 62  ? -1.65647  -0.00003  70.43546  1.000 65.00418  ? 62  LYS B CD  1 
ATOM 2200 C CE  . LYS B 1 62  ? -1.66797  -0.84345  71.68052  1.000 77.22212  ? 62  LYS B CE  1 
ATOM 2201 N NZ  . LYS B 1 62  ? -0.58008  -1.85657  71.58840  1.000 82.04719  ? 62  LYS B NZ  1 
ATOM 2202 N N   . SER B 1 63  ? 0.68452   2.01648   68.53935  1.000 68.89010  ? 63  SER B N   1 
ATOM 2203 C CA  . SER B 1 63  ? 2.00703   1.41067   68.59040  1.000 67.99799  ? 63  SER B CA  1 
ATOM 2204 C C   . SER B 1 63  ? 3.02051   2.36288   69.21428  1.000 70.21148  ? 63  SER B C   1 
ATOM 2205 O O   . SER B 1 63  ? 3.85750   1.95024   70.02231  1.000 73.42924  ? 63  SER B O   1 
ATOM 2206 C CB  . SER B 1 63  ? 2.43441   1.04473   67.16908  1.000 70.80022  ? 63  SER B CB  1 
ATOM 2207 O OG  . SER B 1 63  ? 1.34710   0.44524   66.46910  1.000 75.41935  ? 63  SER B OG  1 
ATOM 2208 N N   . THR B 1 64  ? 2.95907   3.65254   68.84371  1.000 71.49482  ? 64  THR B N   1 
ATOM 2209 C CA  . THR B 1 64  ? 3.96796   4.62561   69.25388  1.000 69.10278  ? 64  THR B CA  1 
ATOM 2210 C C   . THR B 1 64  ? 3.71198   5.16334   70.65122  1.000 71.76088  ? 64  THR B C   1 
ATOM 2211 O O   . THR B 1 64  ? 4.65712   5.51056   71.36757  1.000 72.92362  ? 64  THR B O   1 
ATOM 2212 C CB  . THR B 1 64  ? 3.99365   5.80258   68.29145  1.000 63.67984  ? 64  THR B CB  1 
ATOM 2213 O OG1 . THR B 1 64  ? 4.04709   5.31452   66.95496  1.000 66.80673  ? 64  THR B OG1 1 
ATOM 2214 C CG2 . THR B 1 64  ? 5.22779   6.66042   68.56272  1.000 63.52864  ? 64  THR B CG2 1 
ATOM 2215 N N   . ILE B 1 65  ? 2.44318   5.29069   71.02803  1.000 72.73791  ? 65  ILE B N   1 
ATOM 2216 C CA  . ILE B 1 65  ? 2.10304   5.74888   72.36916  1.000 73.90759  ? 65  ILE B CA  1 
ATOM 2217 C C   . ILE B 1 65  ? 2.56676   4.73203   73.40262  1.000 74.63706  ? 65  ILE B C   1 
ATOM 2218 O O   . ILE B 1 65  ? 3.18851   5.08607   74.41023  1.000 72.96052  ? 65  ILE B O   1 
ATOM 2219 C CB  . ILE B 1 65  ? 0.59515   6.01109   72.44982  1.000 69.89279  ? 65  ILE B CB  1 
ATOM 2220 C CG1 . ILE B 1 65  ? 0.24071   7.05887   71.38659  1.000 70.38778  ? 65  ILE B CG1 1 
ATOM 2221 C CG2 . ILE B 1 65  ? 0.23288   6.45351   73.83530  1.000 64.54015  ? 65  ILE B CG2 1 
ATOM 2222 C CD1 . ILE B 1 65  ? -1.21146  7.09028   70.99815  1.000 67.58119  ? 65  ILE B CD1 1 
ATOM 2223 N N   . GLU B 1 66  ? 2.30435   3.44421   73.13893  1.000 74.07456  ? 66  GLU B N   1 
ATOM 2224 C CA  . GLU B 1 66  ? 2.85093   2.37782   73.97081  1.000 75.02288  ? 66  GLU B CA  1 
ATOM 2225 C C   . GLU B 1 66  ? 4.35874   2.53533   74.12313  1.000 77.64070  ? 66  GLU B C   1 
ATOM 2226 O O   . GLU B 1 66  ? 4.90219   2.43455   75.23018  1.000 80.77642  ? 66  GLU B O   1 
ATOM 2227 C CB  . GLU B 1 66  ? 2.50586   1.00880   73.37032  1.000 68.26217  ? 66  GLU B CB  1 
ATOM 2228 N N   . TRP B 1 67  ? 5.04568   2.82584   73.02291  1.000 77.49325  ? 67  TRP B N   1 
ATOM 2229 C CA  . TRP B 1 67  ? 6.49192   2.99620   73.08037  1.000 78.02429  ? 67  TRP B CA  1 
ATOM 2230 C C   . TRP B 1 67  ? 6.88448   4.13796   74.02095  1.000 79.74274  ? 67  TRP B C   1 
ATOM 2231 O O   . TRP B 1 67  ? 7.81918   4.00764   74.81956  1.000 80.70441  ? 67  TRP B O   1 
ATOM 2232 C CB  . TRP B 1 67  ? 7.03613   3.25074   71.67724  1.000 69.39916  ? 67  TRP B CB  1 
ATOM 2233 C CG  . TRP B 1 67  ? 8.49822   3.30705   71.64849  1.000 64.96558  ? 67  TRP B CG  1 
ATOM 2234 C CD1 . TRP B 1 67  ? 9.34308   2.25763   71.70925  1.000 65.66169  ? 67  TRP B CD1 1 
ATOM 2235 C CD2 . TRP B 1 67  ? 9.31275   4.48428   71.63441  1.000 69.33825  ? 67  TRP B CD2 1 
ATOM 2236 N NE1 . TRP B 1 67  ? 10.64252  2.69289   71.68867  1.000 70.16925  ? 67  TRP B NE1 1 
ATOM 2237 C CE2 . TRP B 1 67  ? 10.65093  4.06168   71.65088  1.000 71.19477  ? 67  TRP B CE2 1 
ATOM 2238 C CE3 . TRP B 1 67  ? 9.04085   5.85231   71.58466  1.000 72.21390  ? 67  TRP B CE3 1 
ATOM 2239 C CZ2 . TRP B 1 67  ? 11.72016  4.95778   71.62206  1.000 69.60350  ? 67  TRP B CZ2 1 
ATOM 2240 C CZ3 . TRP B 1 67  ? 10.09975  6.73780   71.57271  1.000 73.10528  ? 67  TRP B CZ3 1 
ATOM 2241 C CH2 . TRP B 1 67  ? 11.42320  6.28592   71.58713  1.000 69.63398  ? 67  TRP B CH2 1 
ATOM 2242 N N   . TRP B 1 68  ? 6.19921   5.27748   73.92460  1.000 75.54664  ? 68  TRP B N   1 
ATOM 2243 C CA  . TRP B 1 68  ? 6.59024   6.40826   74.75044  1.000 76.85026  ? 68  TRP B CA  1 
ATOM 2244 C C   . TRP B 1 68  ? 6.32677   6.15052   76.22650  1.000 84.03435  ? 68  TRP B C   1 
ATOM 2245 O O   . TRP B 1 68  ? 7.04147   6.68581   77.08327  1.000 85.54448  ? 68  TRP B O   1 
ATOM 2246 C CB  . TRP B 1 68  ? 5.86917   7.67719   74.30782  1.000 77.90266  ? 68  TRP B CB  1 
ATOM 2247 C CG  . TRP B 1 68  ? 6.51233   8.41762   73.17978  1.000 77.97448  ? 68  TRP B CG  1 
ATOM 2248 C CD1 . TRP B 1 68  ? 6.10829   8.46046   71.87555  1.000 76.82434  ? 68  TRP B CD1 1 
ATOM 2249 C CD2 . TRP B 1 68  ? 7.68004   9.23833   73.26407  1.000 79.11902  ? 68  TRP B CD2 1 
ATOM 2250 N NE1 . TRP B 1 68  ? 6.94695   9.27002   71.14639  1.000 70.75232  ? 68  TRP B NE1 1 
ATOM 2251 C CE2 . TRP B 1 68  ? 7.92514   9.75135   71.97368  1.000 75.15596  ? 68  TRP B CE2 1 
ATOM 2252 C CE3 . TRP B 1 68  ? 8.53942   9.59602   74.31027  1.000 84.56574  ? 68  TRP B CE3 1 
ATOM 2253 C CZ2 . TRP B 1 68  ? 8.99174   10.59901  71.69960  1.000 77.22690  ? 68  TRP B CZ2 1 
ATOM 2254 C CZ3 . TRP B 1 68  ? 9.59829   10.43700  74.03980  1.000 88.85670  ? 68  TRP B CZ3 1 
ATOM 2255 C CH2 . TRP B 1 68  ? 9.81809   10.92914  72.73972  1.000 84.53233  ? 68  TRP B CH2 1 
ATOM 2256 N N   . LYS B 1 69  ? 5.30510   5.35337   76.54858  1.000 84.74152  ? 69  LYS B N   1 
ATOM 2257 C CA  . LYS B 1 69  ? 5.01926   5.07722   77.94956  1.000 87.69562  ? 69  LYS B CA  1 
ATOM 2258 C C   . LYS B 1 69  ? 6.13609   4.28520   78.61988  1.000 90.52417  ? 69  LYS B C   1 
ATOM 2259 O O   . LYS B 1 69  ? 6.27621   4.35191   79.84263  1.000 97.81356  ? 69  LYS B O   1 
ATOM 2260 C CB  . LYS B 1 69  ? 3.67128   4.35547   78.08524  1.000 89.36322  ? 69  LYS B CB  1 
ATOM 2261 C CG  . LYS B 1 69  ? 2.47276   5.28459   77.86895  1.000 85.00469  ? 69  LYS B CG  1 
ATOM 2262 C CD  . LYS B 1 69  ? 1.13927   4.65711   78.25716  1.000 85.62656  ? 69  LYS B CD  1 
ATOM 2263 C CE  . LYS B 1 69  ? 0.02718   5.71148   78.20458  1.000 86.52550  ? 69  LYS B CE  1 
ATOM 2264 N NZ  . LYS B 1 69  ? -1.28318  5.25701   78.78191  1.000 85.97831  ? 69  LYS B NZ  1 
ATOM 2265 N N   . ASN B 1 70  ? 6.95066   3.57400   77.84361  1.000 90.09192  ? 70  ASN B N   1 
ATOM 2266 C CA  . ASN B 1 70  ? 8.10874   2.84282   78.33679  1.000 91.59835  ? 70  ASN B CA  1 
ATOM 2267 C C   . ASN B 1 70  ? 9.38962   3.66669   78.26386  1.000 89.06871  ? 70  ASN B C   1 
ATOM 2268 O O   . ASN B 1 70  ? 10.47710  3.11104   78.06824  1.000 88.22235  ? 70  ASN B O   1 
ATOM 2269 C CB  . ASN B 1 70  ? 8.27165   1.54707   77.54367  1.000 94.80946  ? 70  ASN B CB  1 
ATOM 2270 C CG  . ASN B 1 70  ? 7.02864   0.68283   77.59097  1.000 99.44586  ? 70  ASN B CG  1 
ATOM 2271 O OD1 . ASN B 1 70  ? 6.31369   0.64922   78.59607  1.000 105.95437 ? 70  ASN B OD1 1 
ATOM 2272 N ND2 . ASN B 1 70  ? 6.77020   -0.03200  76.50547  1.000 91.89361  ? 70  ASN B ND2 1 
ATOM 2273 N N   . GLN B 1 71  ? 9.28775   4.98191   78.38373  1.000 88.66588  ? 71  GLN B N   1 
ATOM 2274 C CA  . GLN B 1 71  ? 10.43433  5.87037   78.30046  1.000 93.24000  ? 71  GLN B CA  1 
ATOM 2275 C C   . GLN B 1 71  ? 10.56484  6.63235   79.60965  1.000 99.26245  ? 71  GLN B C   1 
ATOM 2276 O O   . GLN B 1 71  ? 9.56618   7.10465   80.16824  1.000 97.68477  ? 71  GLN B O   1 
ATOM 2277 C CB  . GLN B 1 71  ? 10.29704  6.87221   77.14114  1.000 95.53161  ? 71  GLN B CB  1 
ATOM 2278 C CG  . GLN B 1 71  ? 10.19650  6.27992   75.73032  1.000 85.26153  ? 71  GLN B CG  1 
ATOM 2279 C CD  . GLN B 1 71  ? 11.38263  5.40721   75.35785  1.000 83.96416  ? 71  GLN B CD  1 
ATOM 2280 O OE1 . GLN B 1 71  ? 11.22725  4.21674   75.08604  1.000 81.59743  ? 71  GLN B OE1 1 
ATOM 2281 N NE2 . GLN B 1 71  ? 12.58040  5.98895   75.37221  1.000 88.71179  ? 71  GLN B NE2 1 
ATOM 2282 N N   . SER B 1 72  ? 11.80285  6.75786   80.08351  1.000 105.97432 ? 72  SER B N   1 
ATOM 2283 C CA  . SER B 1 72  ? 12.12788  7.44112   81.32870  1.000 106.10360 ? 72  SER B CA  1 
ATOM 2284 C C   . SER B 1 72  ? 11.52009  8.83420   81.34219  1.000 107.91546 ? 72  SER B C   1 
ATOM 2285 O O   . SER B 1 72  ? 11.21924  9.39443   80.28034  1.000 108.75250 ? 72  SER B O   1 
ATOM 2286 C CB  . SER B 1 72  ? 13.64149  7.53531   81.50876  1.000 108.60119 ? 72  SER B CB  1 
ATOM 2287 O OG  . SER B 1 72  ? 14.21285  8.36327   80.50961  1.000 109.49283 ? 72  SER B OG  1 
ATOM 2288 N N   . PRO B 1 73  ? 11.30079  9.41614   82.51788  1.000 114.05459 ? 73  PRO B N   1 
ATOM 2289 C CA  . PRO B 1 73  ? 10.78599  10.79170  82.55409  1.000 115.33692 ? 73  PRO B CA  1 
ATOM 2290 C C   . PRO B 1 73  ? 11.68275  11.79062  81.84355  1.000 114.01185 ? 73  PRO B C   1 
ATOM 2291 O O   . PRO B 1 73  ? 11.17767  12.78622  81.31073  1.000 113.97194 ? 73  PRO B O   1 
ATOM 2292 C CB  . PRO B 1 73  ? 10.67008  11.07588  84.05824  1.000 119.31216 ? 73  PRO B CB  1 
ATOM 2293 C CG  . PRO B 1 73  ? 10.46527  9.71868   84.67502  1.000 119.48604 ? 73  PRO B CG  1 
ATOM 2294 C CD  . PRO B 1 73  ? 11.30839  8.78860   83.85179  1.000 117.04496 ? 73  PRO B CD  1 
ATOM 2295 N N   . GLU B 1 74  ? 12.99583  11.55775  81.80893  1.000 108.98525 ? 74  GLU B N   1 
ATOM 2296 C CA  . GLU B 1 74  ? 13.86383  12.42680  81.02282  1.000 106.87122 ? 74  GLU B CA  1 
ATOM 2297 C C   . GLU B 1 74  ? 13.46557  12.40073  79.55156  1.000 107.16678 ? 74  GLU B C   1 
ATOM 2298 O O   . GLU B 1 74  ? 13.42240  13.44334  78.88922  1.000 107.09948 ? 74  GLU B O   1 
ATOM 2299 C CB  . GLU B 1 74  ? 15.32267  12.00652  81.20018  1.000 105.41582 ? 74  GLU B CB  1 
ATOM 2300 N N   . ALA B 1 75  ? 13.16108  11.21441  79.02712  1.000 105.66596 ? 75  ALA B N   1 
ATOM 2301 C CA  . ALA B 1 75  ? 12.72086  11.09639  77.64300  1.000 103.60275 ? 75  ALA B CA  1 
ATOM 2302 C C   . ALA B 1 75  ? 11.34240  11.72077  77.44074  1.000 103.38890 ? 75  ALA B C   1 
ATOM 2303 O O   . ALA B 1 75  ? 11.11381  12.46096  76.47457  1.000 99.66963  ? 75  ALA B O   1 
ATOM 2304 C CB  . ALA B 1 75  ? 12.72162  9.62470   77.23550  1.000 103.66737 ? 75  ALA B CB  1 
ATOM 2305 N N   . ARG B 1 76  ? 10.40533  11.43206  78.34127  1.000 103.79488 ? 76  ARG B N   1 
ATOM 2306 C CA  . ARG B 1 76  ? 9.07331   12.00456  78.21131  1.000 99.51226  ? 76  ARG B CA  1 
ATOM 2307 C C   . ARG B 1 76  ? 9.05540   13.49970  78.48684  1.000 99.19377  ? 76  ARG B C   1 
ATOM 2308 O O   . ARG B 1 76  ? 7.97095   14.09598  78.49181  1.000 98.35054  ? 76  ARG B O   1 
ATOM 2309 C CB  . ARG B 1 76  ? 8.09570   11.27583  79.13886  1.000 94.67507  ? 76  ARG B CB  1 
ATOM 2310 N N   . LYS B 1 77  ? 10.21806  14.11266  78.73634  1.000 99.96440  ? 77  LYS B N   1 
ATOM 2311 C CA  . LYS B 1 77  ? 10.27709  15.56506  78.87113  1.000 98.12710  ? 77  LYS B CA  1 
ATOM 2312 C C   . LYS B 1 77  ? 9.87712   16.24221  77.57128  1.000 96.19194  ? 77  LYS B C   1 
ATOM 2313 O O   . LYS B 1 77  ? 9.22456   17.29290  77.58109  1.000 92.68136  ? 77  LYS B O   1 
ATOM 2314 C CB  . LYS B 1 77  ? 11.68105  16.00672  79.28511  1.000 97.61200  ? 77  LYS B CB  1 
ATOM 2315 N N   . ASN B 1 78  ? 10.25248  15.64291  76.43957  1.000 96.50923  ? 78  ASN B N   1 
ATOM 2316 C CA  . ASN B 1 78  ? 9.97884   16.25760  75.14623  1.000 94.19858  ? 78  ASN B CA  1 
ATOM 2317 C C   . ASN B 1 78  ? 8.48064   16.44172  74.92204  1.000 89.68120  ? 78  ASN B C   1 
ATOM 2318 O O   . ASN B 1 78  ? 8.03340   17.51235  74.49490  1.000 88.14017  ? 78  ASN B O   1 
ATOM 2319 C CB  . ASN B 1 78  ? 10.59561  15.40538  74.03107  1.000 89.52858  ? 78  ASN B CB  1 
ATOM 2320 N N   . ILE B 1 79  ? 7.68490   15.42184  75.23774  1.000 88.35836  ? 79  ILE B N   1 
ATOM 2321 C CA  . ILE B 1 79  ? 6.29655   15.41428  74.79598  1.000 84.23471  ? 79  ILE B CA  1 
ATOM 2322 C C   . ILE B 1 79  ? 5.38453   16.31654  75.63006  1.000 82.70751  ? 79  ILE B C   1 
ATOM 2323 O O   . ILE B 1 79  ? 4.26487   16.61640  75.19402  1.000 76.14686  ? 79  ILE B O   1 
ATOM 2324 C CB  . ILE B 1 79  ? 5.77587   13.96577  74.78262  1.000 78.40941  ? 79  ILE B CB  1 
ATOM 2325 N N   . ALA B 1 80  ? 5.82828   16.77414  76.80166  1.000 84.80436  ? 80  ALA B N   1 
ATOM 2326 C CA  . ALA B 1 80  ? 4.92547   17.45173  77.74775  1.000 83.90092  ? 80  ALA B CA  1 
ATOM 2327 C C   . ALA B 1 80  ? 4.56924   18.86390  77.28129  1.000 83.92712  ? 80  ALA B C   1 
ATOM 2328 O O   . ALA B 1 80  ? 5.46918   19.63860  76.93829  1.000 85.34261  ? 80  ALA B O   1 
ATOM 2329 C CB  . ALA B 1 80  ? 5.57004   17.50821  79.12569  1.000 82.76746  ? 80  ALA B CB  1 
ATOM 2330 N N   . PRO B 1 81  ? 3.26399   19.25009  77.28561  1.000 72.05086  ? 81  PRO B N   1 
ATOM 2331 C CA  . PRO B 1 81  ? 2.85006   20.55832  76.73863  1.000 71.30801  ? 81  PRO B CA  1 
ATOM 2332 C C   . PRO B 1 81  ? 3.62302   21.75157  77.26910  1.000 75.24604  ? 81  PRO B C   1 
ATOM 2333 O O   . PRO B 1 81  ? 4.31133   21.66142  78.28668  1.000 83.74498  ? 81  PRO B O   1 
ATOM 2334 C CB  . PRO B 1 81  ? 1.36607   20.64440  77.12722  1.000 62.16177  ? 81  PRO B CB  1 
ATOM 2335 C CG  . PRO B 1 81  ? 0.92515   19.23922  77.14511  1.000 65.76241  ? 81  PRO B CG  1 
ATOM 2336 C CD  . PRO B 1 81  ? 2.10188   18.42825  77.66439  1.000 70.54391  ? 81  PRO B CD  1 
ATOM 2337 N N   . SER B 1 82  ? 3.51269   22.88376  76.58952  1.000 74.13621  ? 82  SER B N   1 
ATOM 2338 C CA  . SER B 1 82  ? 4.42675   23.98090  76.84880  1.000 77.75093  ? 82  SER B CA  1 
ATOM 2339 C C   . SER B 1 82  ? 3.84118   25.25720  76.27506  1.000 87.17033  ? 82  SER B C   1 
ATOM 2340 O O   . SER B 1 82  ? 2.93173   25.22951  75.44487  1.000 90.16280  ? 82  SER B O   1 
ATOM 2341 C CB  . SER B 1 82  ? 5.80303   23.68808  76.25068  1.000 78.32436  ? 82  SER B CB  1 
ATOM 2342 O OG  . SER B 1 82  ? 6.65422   24.79721  76.33230  1.000 77.86965  ? 82  SER B OG  1 
ATOM 2343 N N   . ASP B 1 83  ? 4.35498   26.37991  76.75050  1.000 100.39596 ? 83  ASP B N   1 
ATOM 2344 C CA  . ASP B 1 83  ? 3.94089   27.66594  76.22202  1.000 103.35611 ? 83  ASP B CA  1 
ATOM 2345 C C   . ASP B 1 83  ? 4.78409   28.06577  75.02129  1.000 97.72296  ? 83  ASP B C   1 
ATOM 2346 O O   . ASP B 1 83  ? 4.44860   29.02534  74.32239  1.000 96.75408  ? 83  ASP B O   1 
ATOM 2347 C CB  . ASP B 1 83  ? 4.00056   28.73055  77.33654  1.000 109.00070 ? 83  ASP B CB  1 
ATOM 2348 C CG  . ASP B 1 83  ? 3.04138   28.41942  78.51556  1.000 114.15946 ? 83  ASP B CG  1 
ATOM 2349 O OD1 . ASP B 1 83  ? 2.03569   27.69781  78.31925  1.000 112.90728 ? 83  ASP B OD1 1 
ATOM 2350 O OD2 . ASP B 1 83  ? 3.28517   28.90769  79.64389  1.000 120.82591 ? 83  ASP B OD2 1 
ATOM 2351 N N   . GLU B 1 84  ? 5.84885   27.32046  74.75034  1.000 91.53114  ? 84  GLU B N   1 
ATOM 2352 C CA  . GLU B 1 84  ? 6.67554   27.52616  73.56993  1.000 88.03036  ? 84  GLU B CA  1 
ATOM 2353 C C   . GLU B 1 84  ? 6.13487   26.81274  72.33717  1.000 84.04831  ? 84  GLU B C   1 
ATOM 2354 O O   . GLU B 1 84  ? 6.62860   27.06890  71.23559  1.000 84.03402  ? 84  GLU B O   1 
ATOM 2355 C CB  . GLU B 1 84  ? 8.09821   27.05066  73.84833  1.000 87.48373  ? 84  GLU B CB  1 
ATOM 2356 C CG  . GLU B 1 84  ? 8.20412   25.54564  73.94361  1.000 88.00132  ? 84  GLU B CG  1 
ATOM 2357 C CD  . GLU B 1 84  ? 9.55288   25.08640  74.47161  1.000 94.75819  ? 84  GLU B CD  1 
ATOM 2358 O OE1 . GLU B 1 84  ? 10.36856  25.95124  74.87165  1.000 97.94213  ? 84  GLU B OE1 1 
ATOM 2359 O OE2 . GLU B 1 84  ? 9.80740   23.85994  74.46837  1.000 95.05989  ? 84  GLU B OE2 1 
ATOM 2360 N N   . ASP B 1 85  ? 5.11225   25.96903  72.48042  1.000 79.72980  ? 85  ASP B N   1 
ATOM 2361 C CA  . ASP B 1 85  ? 4.55882   25.24814  71.33917  1.000 78.67500  ? 85  ASP B CA  1 
ATOM 2362 C C   . ASP B 1 85  ? 4.17137   26.16809  70.18083  1.000 77.76783  ? 85  ASP B C   1 
ATOM 2363 O O   . ASP B 1 85  ? 4.11502   27.38626  70.33188  1.000 80.62497  ? 85  ASP B O   1 
ATOM 2364 C CB  . ASP B 1 85  ? 3.34245   24.41512  71.75286  1.000 74.02332  ? 85  ASP B CB  1 
ATOM 2365 C CG  . ASP B 1 85  ? 3.70271   23.32317  72.72389  1.000 72.83045  ? 85  ASP B CG  1 
ATOM 2366 O OD1 . ASP B 1 85  ? 4.91173   23.10219  72.91400  1.000 70.48764  ? 85  ASP B OD1 1 
ATOM 2367 O OD2 . ASP B 1 85  ? 2.79313   22.62840  73.23211  1.000 74.05833  ? 85  ASP B OD2 1 
ATOM 2368 N N   . VAL B 1 86  ? 3.96760   25.59434  68.99756  1.000 80.02385  ? 86  VAL B N   1 
ATOM 2369 C CA  . VAL B 1 86  ? 3.45053   26.30693  67.83569  1.000 79.37136  ? 86  VAL B CA  1 
ATOM 2370 C C   . VAL B 1 86  ? 2.52166   25.36300  67.07832  1.000 78.90279  ? 86  VAL B C   1 
ATOM 2371 O O   . VAL B 1 86  ? 2.51703   24.15072  67.29928  1.000 76.19498  ? 86  VAL B O   1 
ATOM 2372 C CB  . VAL B 1 86  ? 4.57190   26.80330  66.89944  1.000 76.04731  ? 86  VAL B CB  1 
ATOM 2373 C CG1 . VAL B 1 86  ? 5.50988   27.73230  67.62070  1.000 78.70709  ? 86  VAL B CG1 1 
ATOM 2374 C CG2 . VAL B 1 86  ? 5.32471   25.62746  66.34373  1.000 76.08334  ? 86  VAL B CG2 1 
ATOM 2375 N N   . SER B 1 87  ? 1.72413   25.93941  66.18034  1.000 76.33440  ? 87  SER B N   1 
ATOM 2376 C CA  . SER B 1 87  ? 0.99439   25.14801  65.20353  1.000 70.95718  ? 87  SER B CA  1 
ATOM 2377 C C   . SER B 1 87  ? 1.97475   24.57610  64.19817  1.000 69.95570  ? 87  SER B C   1 
ATOM 2378 O O   . SER B 1 87  ? 3.05523   25.12951  63.97746  1.000 70.76823  ? 87  SER B O   1 
ATOM 2379 C CB  . SER B 1 87  ? -0.03364  25.99741  64.46748  1.000 68.95893  ? 87  SER B CB  1 
ATOM 2380 O OG  . SER B 1 87  ? 0.62376   26.91767  63.62367  1.000 68.16021  ? 87  SER B OG  1 
ATOM 2381 N N   . THR B 1 88  ? 1.59685   23.45127  63.58771  1.000 68.28584  ? 88  THR B N   1 
ATOM 2382 C CA  . THR B 1 88  ? 2.43256   22.91481  62.52580  1.000 62.16643  ? 88  THR B CA  1 
ATOM 2383 C C   . THR B 1 88  ? 2.66552   23.95170  61.44067  1.000 68.32061  ? 88  THR B C   1 
ATOM 2384 O O   . THR B 1 88  ? 3.74631   23.98348  60.84276  1.000 70.34506  ? 88  THR B O   1 
ATOM 2385 C CB  . THR B 1 88  ? 1.81876   21.63852  61.95321  1.000 54.55198  ? 88  THR B CB  1 
ATOM 2386 O OG1 . THR B 1 88  ? 0.40782   21.79922  61.80416  1.000 58.24748  ? 88  THR B OG1 1 
ATOM 2387 C CG2 . THR B 1 88  ? 2.10624   20.46442  62.81361  1.000 52.88148  ? 88  THR B CG2 1 
ATOM 2388 N N   . ILE B 1 89  ? 1.68981   24.83418  61.19852  1.000 66.03258  ? 89  ILE B N   1 
ATOM 2389 C CA  . ILE B 1 89  ? 1.89169   25.90711  60.22707  1.000 65.36362  ? 89  ILE B CA  1 
ATOM 2390 C C   . ILE B 1 89  ? 2.94004   26.89366  60.73642  1.000 71.75185  ? 89  ILE B C   1 
ATOM 2391 O O   . ILE B 1 89  ? 3.82254   27.32793  59.98881  1.000 70.51133  ? 89  ILE B O   1 
ATOM 2392 C CB  . ILE B 1 89  ? 0.57289   26.63405  59.91637  1.000 65.65151  ? 89  ILE B CB  1 
ATOM 2393 C CG1 . ILE B 1 89  ? -0.55548  25.66819  59.56937  1.000 68.54245  ? 89  ILE B CG1 1 
ATOM 2394 C CG2 . ILE B 1 89  ? 0.78309   27.53617  58.76161  1.000 66.53015  ? 89  ILE B CG2 1 
ATOM 2395 C CD1 . ILE B 1 89  ? -1.46555  25.27542  60.79248  1.000 67.80513  ? 89  ILE B CD1 1 
ATOM 2396 N N   . ASP B 1 90  ? 2.84744   27.27503  62.01852  1.000 79.07160  ? 90  ASP B N   1 
ATOM 2397 C CA  . ASP B 1 90  ? 3.83518   28.17305  62.62058  1.000 79.68467  ? 90  ASP B CA  1 
ATOM 2398 C C   . ASP B 1 90  ? 5.20824   27.50872  62.72027  1.000 80.27578  ? 90  ASP B C   1 
ATOM 2399 O O   . ASP B 1 90  ? 6.24641   28.17565  62.58949  1.000 77.92083  ? 90  ASP B O   1 
ATOM 2400 C CB  . ASP B 1 90  ? 3.35153   28.61518  64.00334  1.000 79.20134  ? 90  ASP B CB  1 
ATOM 2401 C CG  . ASP B 1 90  ? 2.15403   29.56665  63.94175  1.000 80.61138  ? 90  ASP B CG  1 
ATOM 2402 O OD1 . ASP B 1 90  ? 2.09046   30.39221  62.98444  1.000 78.44700  ? 90  ASP B OD1 1 
ATOM 2403 O OD2 . ASP B 1 90  ? 1.27843   29.47937  64.85300  1.000 76.91488  ? 90  ASP B OD2 1 
ATOM 2404 N N   . GLY B 1 91  ? 5.22451   26.19410  62.97307  1.000 81.42878  ? 91  GLY B N   1 
ATOM 2405 C CA  . GLY B 1 91  ? 6.48132   25.46419  63.05036  1.000 79.30567  ? 91  GLY B CA  1 
ATOM 2406 C C   . GLY B 1 91  ? 7.21563   25.37802  61.72603  1.000 79.20768  ? 91  GLY B C   1 
ATOM 2407 O O   . GLY B 1 91  ? 8.44507   25.45463  61.68650  1.000 80.62673  ? 91  GLY B O   1 
ATOM 2408 N N   . ILE B 1 92  ? 6.47759   25.19428  60.62668  1.000 72.24940  ? 92  ILE B N   1 
ATOM 2409 C CA  . ILE B 1 92  ? 7.11724   25.12718  59.32193  1.000 73.29772  ? 92  ILE B CA  1 
ATOM 2410 C C   . ILE B 1 92  ? 7.59254   26.50289  58.87449  1.000 74.19875  ? 92  ILE B C   1 
ATOM 2411 O O   . ILE B 1 92  ? 8.53076   26.60559  58.07366  1.000 73.25237  ? 92  ILE B O   1 
ATOM 2412 C CB  . ILE B 1 92  ? 6.17141   24.49486  58.27893  1.000 73.57652  ? 92  ILE B CB  1 
ATOM 2413 C CG1 . ILE B 1 92  ? 6.95770   24.02269  57.05114  1.000 68.38638  ? 92  ILE B CG1 1 
ATOM 2414 C CG2 . ILE B 1 92  ? 5.11032   25.49534  57.83413  1.000 73.11817  ? 92  ILE B CG2 1 
ATOM 2415 C CD1 . ILE B 1 92  ? 7.90944   22.90101  57.35736  1.000 65.40498  ? 92  ILE B CD1 1 
ATOM 2416 N N   . ALA B 1 93  ? 6.97871   27.57373  59.37462  1.000 75.25769  ? 93  ALA B N   1 
ATOM 2417 C CA  . ALA B 1 93  ? 7.49313   28.90148  59.05944  1.000 76.36043  ? 93  ALA B CA  1 
ATOM 2418 C C   . ALA B 1 93  ? 8.82202   29.15428  59.75764  1.000 77.56464  ? 93  ALA B C   1 
ATOM 2419 O O   . ALA B 1 93  ? 9.75937   29.67754  59.14667  1.000 81.10570  ? 93  ALA B O   1 
ATOM 2420 C CB  . ALA B 1 93  ? 6.47002   29.96696  59.43792  1.000 75.30284  ? 93  ALA B CB  1 
ATOM 2421 N N   . LYS B 1 94  ? 8.92127   28.78583  61.03657  1.000 75.74113  ? 94  LYS B N   1 
ATOM 2422 C CA  . LYS B 1 94  ? 10.18960  28.89675  61.74995  1.000 76.11411  ? 94  LYS B CA  1 
ATOM 2423 C C   . LYS B 1 94  ? 11.27508  28.06350  61.07729  1.000 77.65341  ? 94  LYS B C   1 
ATOM 2424 O O   . LYS B 1 94  ? 12.44821  28.45760  61.05305  1.000 75.61061  ? 94  LYS B O   1 
ATOM 2425 C CB  . LYS B 1 94  ? 9.98734   28.47460  63.20903  1.000 76.79933  ? 94  LYS B CB  1 
ATOM 2426 C CG  . LYS B 1 94  ? 9.18669   29.48894  64.02730  1.000 82.63593  ? 94  LYS B CG  1 
ATOM 2427 C CD  . LYS B 1 94  ? 8.83222   28.98824  65.42912  1.000 85.86849  ? 94  LYS B CD  1 
ATOM 2428 C CE  . LYS B 1 94  ? 8.26047   30.10839  66.31291  1.000 89.33334  ? 94  LYS B CE  1 
ATOM 2429 N NZ  . LYS B 1 94  ? 6.96226   30.67877  65.83323  1.000 90.02826  ? 94  LYS B NZ  1 
ATOM 2430 N N   . PHE B 1 95  ? 10.89389  26.90377  60.52766  1.000 76.64671  ? 95  PHE B N   1 
ATOM 2431 C CA  . PHE B 1 95  ? 11.82626  26.04669  59.80637  1.000 71.38548  ? 95  PHE B CA  1 
ATOM 2432 C C   . PHE B 1 95  ? 12.33050  26.69858  58.52044  1.000 74.08046  ? 95  PHE B C   1 
ATOM 2433 O O   . PHE B 1 95  ? 13.50400  26.54389  58.16596  1.000 73.79870  ? 95  PHE B O   1 
ATOM 2434 C CB  . PHE B 1 95  ? 11.16835  24.69656  59.50318  1.000 69.42154  ? 95  PHE B CB  1 
ATOM 2435 C CG  . PHE B 1 95  ? 12.02892  23.77905  58.67431  1.000 66.30339  ? 95  PHE B CG  1 
ATOM 2436 C CD1 . PHE B 1 95  ? 13.16815  23.19881  59.21533  1.000 62.63705  ? 95  PHE B CD1 1 
ATOM 2437 C CD2 . PHE B 1 95  ? 11.70382  23.50681  57.36355  1.000 63.17039  ? 95  PHE B CD2 1 
ATOM 2438 C CE1 . PHE B 1 95  ? 13.96665  22.38530  58.48088  1.000 56.40103  ? 95  PHE B CE1 1 
ATOM 2439 C CE2 . PHE B 1 95  ? 12.49903  22.69205  56.63001  1.000 64.69971  ? 95  PHE B CE2 1 
ATOM 2440 C CZ  . PHE B 1 95  ? 13.63847  22.12396  57.19474  1.000 62.46587  ? 95  PHE B CZ  1 
ATOM 2441 N N   . ASN B 1 96  ? 11.46679  27.39090  57.77671  1.000 78.99222  ? 96  ASN B N   1 
ATOM 2442 C CA  . ASN B 1 96  ? 11.97642  28.03173  56.57068  1.000 82.27258  ? 96  ASN B CA  1 
ATOM 2443 C C   . ASN B 1 96  ? 12.78509  29.27825  56.91611  1.000 85.23144  ? 96  ASN B C   1 
ATOM 2444 O O   . ASN B 1 96  ? 13.70527  29.64515  56.16849  1.000 84.54807  ? 96  ASN B O   1 
ATOM 2445 C CB  . ASN B 1 96  ? 10.84442  28.39203  55.61131  1.000 83.90496  ? 96  ASN B CB  1 
ATOM 2446 C CG  . ASN B 1 96  ? 10.04878  27.18880  55.16358  1.000 86.43892  ? 96  ASN B CG  1 
ATOM 2447 O OD1 . ASN B 1 96  ? 10.57252  26.07511  55.05114  1.000 85.90235  ? 96  ASN B OD1 1 
ATOM 2448 N ND2 . ASN B 1 96  ? 8.77013   27.41619  54.86291  1.000 90.47113  ? 96  ASN B ND2 1 
ATOM 2449 N N   . ASP B 1 97  ? 12.44653  29.94261  58.03285  1.000 84.78030  ? 97  ASP B N   1 
ATOM 2450 C CA  . ASP B 1 97  ? 13.29109  31.01060  58.55751  1.000 84.68796  ? 97  ASP B CA  1 
ATOM 2451 C C   . ASP B 1 97  ? 14.71435  30.50586  58.78831  1.000 84.67692  ? 97  ASP B C   1 
ATOM 2452 O O   . ASP B 1 97  ? 15.69377  31.13724  58.37063  1.000 84.38690  ? 97  ASP B O   1 
ATOM 2453 C CB  . ASP B 1 97  ? 12.70225  31.56459  59.86446  1.000 85.38676  ? 97  ASP B CB  1 
ATOM 2454 C CG  . ASP B 1 97  ? 11.39542  32.34745  59.66404  1.000 87.96077  ? 97  ASP B CG  1 
ATOM 2455 O OD1 . ASP B 1 97  ? 11.17717  32.89737  58.57062  1.000 90.37874  ? 97  ASP B OD1 1 
ATOM 2456 O OD2 . ASP B 1 97  ? 10.58808  32.43812  60.62287  1.000 88.56119  ? 97  ASP B OD2 1 
ATOM 2457 N N   . TYR B 1 98  ? 14.84559  29.35601  59.44855  1.000 76.37330  ? 98  TYR B N   1 
ATOM 2458 C CA  . TYR B 1 98  ? 16.16790  28.80365  59.71245  1.000 73.84392  ? 98  TYR B CA  1 
ATOM 2459 C C   . TYR B 1 98  ? 16.89299  28.47573  58.41070  1.000 77.21579  ? 98  TYR B C   1 
ATOM 2460 O O   . TYR B 1 98  ? 18.06016  28.83651  58.23731  1.000 78.26334  ? 98  TYR B O   1 
ATOM 2461 C CB  . TYR B 1 98  ? 16.04851  27.55237  60.58915  1.000 73.40625  ? 98  TYR B CB  1 
ATOM 2462 C CG  . TYR B 1 98  ? 17.38032  27.00766  61.02886  1.000 71.74227  ? 98  TYR B CG  1 
ATOM 2463 C CD1 . TYR B 1 98  ? 18.00075  27.50191  62.16039  1.000 67.90498  ? 98  TYR B CD1 1 
ATOM 2464 C CD2 . TYR B 1 98  ? 18.04864  26.04430  60.27441  1.000 71.12092  ? 98  TYR B CD2 1 
ATOM 2465 C CE1 . TYR B 1 98  ? 19.21720  27.03514  62.56627  1.000 68.35052  ? 98  TYR B CE1 1 
ATOM 2466 C CE2 . TYR B 1 98  ? 19.28631  25.57483  60.66733  1.000 70.42444  ? 98  TYR B CE2 1 
ATOM 2467 C CZ  . TYR B 1 98  ? 19.86628  26.08099  61.82096  1.000 70.36694  ? 98  TYR B CZ  1 
ATOM 2468 O OH  . TYR B 1 98  ? 21.09681  25.63082  62.24084  1.000 70.07424  ? 98  TYR B OH  1 
ATOM 2469 N N   . ILE B 1 99  ? 16.21056  27.80037  57.47525  1.000 75.41678  ? 99  ILE B N   1 
ATOM 2470 C CA  . ILE B 1 99  ? 16.87392  27.36252  56.25032  1.000 76.13926  ? 99  ILE B CA  1 
ATOM 2471 C C   . ILE B 1 99  ? 17.40270  28.55682  55.46591  1.000 78.92399  ? 99  ILE B C   1 
ATOM 2472 O O   . ILE B 1 99  ? 18.54607  28.54343  54.99619  1.000 79.77356  ? 99  ILE B O   1 
ATOM 2473 C CB  . ILE B 1 99  ? 15.93645  26.48876  55.39137  1.000 75.51155  ? 99  ILE B CB  1 
ATOM 2474 C CG1 . ILE B 1 99  ? 15.57046  25.18941  56.11648  1.000 72.24937  ? 99  ILE B CG1 1 
ATOM 2475 C CG2 . ILE B 1 99  ? 16.59359  26.13504  54.06755  1.000 68.94733  ? 99  ILE B CG2 1 
ATOM 2476 C CD1 . ILE B 1 99  ? 16.75220  24.28339  56.39532  1.000 67.09758  ? 99  ILE B CD1 1 
ATOM 2477 N N   . ASN B 1 100 ? 16.60002  29.61515  55.32085  1.000 76.78647  ? 100 ASN B N   1 
ATOM 2478 C CA  . ASN B 1 100 ? 17.07782  30.74816  54.53325  1.000 78.70740  ? 100 ASN B CA  1 
ATOM 2479 C C   . ASN B 1 100 ? 18.17684  31.50977  55.25049  1.000 78.93286  ? 100 ASN B C   1 
ATOM 2480 O O   . ASN B 1 100 ? 19.02813  32.12045  54.59878  1.000 80.55083  ? 100 ASN B O   1 
ATOM 2481 C CB  . ASN B 1 100 ? 15.93750  31.69443  54.18013  1.000 82.93710  ? 100 ASN B CB  1 
ATOM 2482 C CG  . ASN B 1 100 ? 14.87248  31.01992  53.34256  1.000 90.06557  ? 100 ASN B CG  1 
ATOM 2483 O OD1 . ASN B 1 100 ? 13.70981  30.96183  53.74617  1.000 94.74007  ? 100 ASN B OD1 1 
ATOM 2484 N ND2 . ASN B 1 100 ? 15.26792  30.46324  52.18941  1.000 83.44869  ? 100 ASN B ND2 1 
ATOM 2485 N N   . ALA B 1 101 ? 18.18826  31.47468  56.57860  1.000 80.38279  ? 101 ALA B N   1 
ATOM 2486 C CA  . ALA B 1 101 ? 19.18317  32.21112  57.34090  1.000 76.63532  ? 101 ALA B CA  1 
ATOM 2487 C C   . ALA B 1 101 ? 20.52824  31.50352  57.43297  1.000 75.58646  ? 101 ALA B C   1 
ATOM 2488 O O   . ALA B 1 101 ? 21.48694  32.10940  57.91625  1.000 78.47475  ? 101 ALA B O   1 
ATOM 2489 C CB  . ALA B 1 101 ? 18.66136  32.48671  58.74903  1.000 75.77101  ? 101 ALA B CB  1 
ATOM 2490 N N   . HIS B 1 102 ? 20.64785  30.25803  56.98548  1.000 76.16387  ? 102 HIS B N   1 
ATOM 2491 C CA  . HIS B 1 102 ? 21.88201  29.51652  57.21777  1.000 73.53428  ? 102 HIS B CA  1 
ATOM 2492 C C   . HIS B 1 102 ? 22.46287  28.99243  55.93270  1.000 74.47533  ? 102 HIS B C   1 
ATOM 2493 O O   . HIS B 1 102 ? 22.90139  27.84625  55.84897  1.000 73.81857  ? 102 HIS B O   1 
ATOM 2494 C CB  . HIS B 1 102 ? 21.67324  28.39852  58.21327  1.000 73.45920  ? 102 HIS B CB  1 
ATOM 2495 C CG  . HIS B 1 102 ? 21.57082  28.88640  59.62128  1.000 75.40526  ? 102 HIS B CG  1 
ATOM 2496 N ND1 . HIS B 1 102 ? 20.37564  29.25021  60.20089  1.000 77.32253  ? 102 HIS B ND1 1 
ATOM 2497 C CD2 . HIS B 1 102 ? 22.52682  29.11776  60.55024  1.000 73.77410  ? 102 HIS B CD2 1 
ATOM 2498 C CE1 . HIS B 1 102 ? 20.59759  29.66138  61.43483  1.000 76.98837  ? 102 HIS B CE1 1 
ATOM 2499 N NE2 . HIS B 1 102 ? 21.89512  29.58927  61.67079  1.000 77.26891  ? 102 HIS B NE2 1 
ATOM 2500 N N   . ASN B 1 103 ? 22.50845  29.86505  54.92521  1.000 78.56206  ? 103 ASN B N   1 
ATOM 2501 C CA  . ASN B 1 103 ? 23.29795  29.65467  53.71759  1.000 79.65416  ? 103 ASN B CA  1 
ATOM 2502 C C   . ASN B 1 103 ? 23.03526  28.26721  53.12961  1.000 78.94030  ? 103 ASN B C   1 
ATOM 2503 O O   . ASN B 1 103 ? 23.94920  27.49870  52.82199  1.000 77.94097  ? 103 ASN B O   1 
ATOM 2504 C CB  . ASN B 1 103 ? 24.78700  29.88736  54.00092  1.000 78.32323  ? 103 ASN B CB  1 
ATOM 2505 N N   . ILE B 1 104 ? 21.75362  27.94050  53.00788  1.000 80.46376  ? 104 ILE B N   1 
ATOM 2506 C CA  . ILE B 1 104 ? 21.30546  26.68385  52.42100  1.000 80.37153  ? 104 ILE B CA  1 
ATOM 2507 C C   . ILE B 1 104 ? 20.92479  26.96294  50.97564  1.000 82.07779  ? 104 ILE B C   1 
ATOM 2508 O O   . ILE B 1 104 ? 20.10890  27.85297  50.70209  1.000 83.61911  ? 104 ILE B O   1 
ATOM 2509 C CB  . ILE B 1 104 ? 20.12694  26.08061  53.21098  1.000 77.02200  ? 104 ILE B CB  1 
ATOM 2510 C CG1 . ILE B 1 104 ? 20.53649  25.78531  54.65486  1.000 75.47074  ? 104 ILE B CG1 1 
ATOM 2511 C CG2 . ILE B 1 104 ? 19.64408  24.79137  52.57731  1.000 76.45277  ? 104 ILE B CG2 1 
ATOM 2512 C CD1 . ILE B 1 104 ? 21.65914  24.75706  54.77504  1.000 74.79550  ? 104 ILE B CD1 1 
ATOM 2513 N N   . ASP B 1 105 ? 21.53307  26.21531  50.05578  1.000 89.54489  ? 105 ASP B N   1 
ATOM 2514 C CA  . ASP B 1 105 ? 21.35148  26.40312  48.61774  1.000 90.49202  ? 105 ASP B CA  1 
ATOM 2515 C C   . ASP B 1 105 ? 20.18865  25.54226  48.13198  1.000 90.87421  ? 105 ASP B C   1 
ATOM 2516 O O   . ASP B 1 105 ? 20.19487  24.32542  48.36521  1.000 91.03890  ? 105 ASP B O   1 
ATOM 2517 C CB  . ASP B 1 105 ? 22.64754  26.04330  47.88539  1.000 91.07101  ? 105 ASP B CB  1 
ATOM 2518 C CG  . ASP B 1 105 ? 22.62525  26.36792  46.39572  1.000 91.65221  ? 105 ASP B CG  1 
ATOM 2519 O OD1 . ASP B 1 105 ? 21.56151  26.68710  45.83457  1.000 93.68930  ? 105 ASP B OD1 1 
ATOM 2520 O OD2 . ASP B 1 105 ? 23.71303  26.33919  45.78333  1.000 93.28187  ? 105 ASP B OD2 1 
ATOM 2521 N N   . PRO B 1 106 ? 19.17538  26.11944  47.47912  1.000 83.38784  ? 106 PRO B N   1 
ATOM 2522 C CA  . PRO B 1 106 ? 18.02165  25.30716  47.06148  1.000 79.37688  ? 106 PRO B CA  1 
ATOM 2523 C C   . PRO B 1 106 ? 18.39276  24.16329  46.14665  1.000 77.52665  ? 106 PRO B C   1 
ATOM 2524 O O   . PRO B 1 106 ? 17.71920  23.12251  46.17031  1.000 77.69869  ? 106 PRO B O   1 
ATOM 2525 C CB  . PRO B 1 106 ? 17.11875  26.32124  46.34697  1.000 82.44494  ? 106 PRO B CB  1 
ATOM 2526 C CG  . PRO B 1 106 ? 17.51689  27.65300  46.91198  1.000 83.03719  ? 106 PRO B CG  1 
ATOM 2527 C CD  . PRO B 1 106 ? 18.99060  27.54964  47.17383  1.000 82.59224  ? 106 PRO B CD  1 
ATOM 2528 N N   . TRP B 1 107 ? 19.45437  24.30989  45.35537  1.000 75.52785  ? 107 TRP B N   1 
ATOM 2529 C CA  . TRP B 1 107 ? 19.81698  23.31426  44.35473  1.000 72.46930  ? 107 TRP B CA  1 
ATOM 2530 C C   . TRP B 1 107 ? 21.00647  22.45960  44.74359  1.000 69.73155  ? 107 TRP B C   1 
ATOM 2531 O O   . TRP B 1 107 ? 20.99970  21.26384  44.48173  1.000 64.04741  ? 107 TRP B O   1 
ATOM 2532 C CB  . TRP B 1 107 ? 20.08943  24.00819  43.02249  1.000 71.43652  ? 107 TRP B CB  1 
ATOM 2533 C CG  . TRP B 1 107 ? 18.82001  24.47652  42.43694  1.000 71.34421  ? 107 TRP B CG  1 
ATOM 2534 C CD1 . TRP B 1 107 ? 18.23070  25.69986  42.61005  1.000 74.65874  ? 107 TRP B CD1 1 
ATOM 2535 C CD2 . TRP B 1 107 ? 17.94425  23.72020  41.60156  1.000 66.19329  ? 107 TRP B CD2 1 
ATOM 2536 N NE1 . TRP B 1 107 ? 17.03867  25.74715  41.92756  1.000 71.43504  ? 107 TRP B NE1 1 
ATOM 2537 C CE2 . TRP B 1 107 ? 16.83988  24.54376  41.30135  1.000 64.56570  ? 107 TRP B CE2 1 
ATOM 2538 C CE3 . TRP B 1 107 ? 17.98953  22.42306  41.07217  1.000 64.32057  ? 107 TRP B CE3 1 
ATOM 2539 C CZ2 . TRP B 1 107 ? 15.79421  24.11843  40.49449  1.000 61.64965  ? 107 TRP B CZ2 1 
ATOM 2540 C CZ3 . TRP B 1 107 ? 16.94962  21.99583  40.27796  1.000 61.12152  ? 107 TRP B CZ3 1 
ATOM 2541 C CH2 . TRP B 1 107 ? 15.86073  22.84250  39.99663  1.000 63.17324  ? 107 TRP B CH2 1 
ATOM 2542 N N   . LYS B 1 108 ? 22.02091  23.03334  45.37428  1.000 74.49968  ? 108 LYS B N   1 
ATOM 2543 C CA  . LYS B 1 108 ? 23.23258  22.27884  45.65473  1.000 75.43732  ? 108 LYS B CA  1 
ATOM 2544 C C   . LYS B 1 108 ? 23.22385  21.62116  47.02854  1.000 73.88215  ? 108 LYS B C   1 
ATOM 2545 O O   . LYS B 1 108 ? 23.81643  20.54672  47.19545  1.000 71.75573  ? 108 LYS B O   1 
ATOM 2546 C CB  . LYS B 1 108 ? 24.45416  23.19462  45.50584  1.000 79.96303  ? 108 LYS B CB  1 
ATOM 2547 C CG  . LYS B 1 108 ? 24.74585  23.60369  44.05011  1.000 82.84560  ? 108 LYS B CG  1 
ATOM 2548 C CD  . LYS B 1 108 ? 25.79938  24.73020  43.89725  1.000 88.07260  ? 108 LYS B CD  1 
ATOM 2549 C CE  . LYS B 1 108 ? 27.24088  24.26496  44.13005  1.000 92.89766  ? 108 LYS B CE  1 
ATOM 2550 N NZ  . LYS B 1 108 ? 28.26761  25.33597  43.84097  1.000 92.03971  ? 108 LYS B NZ  1 
ATOM 2551 N N   . SER B 1 109 ? 22.54428  22.22178  48.00301  1.000 77.34614  ? 109 SER B N   1 
ATOM 2552 C CA  . SER B 1 109 ? 22.57435  21.72878  49.37407  1.000 75.14753  ? 109 SER B CA  1 
ATOM 2553 C C   . SER B 1 109 ? 21.87393  20.38417  49.53453  1.000 73.88277  ? 109 SER B C   1 
ATOM 2554 O O   . SER B 1 109 ? 20.89852  20.06660  48.84317  1.000 72.92012  ? 109 SER B O   1 
ATOM 2555 C CB  . SER B 1 109 ? 21.92916  22.72828  50.31685  1.000 73.77179  ? 109 SER B CB  1 
ATOM 2556 O OG  . SER B 1 109 ? 22.73317  23.86931  50.42973  1.000 78.53905  ? 109 SER B OG  1 
ATOM 2557 N N   . GLN B 1 110 ? 22.36607  19.61619  50.50319  1.000 68.62847  ? 110 GLN B N   1 
ATOM 2558 C CA  . GLN B 1 110 ? 21.85693  18.29974  50.83129  1.000 66.36044  ? 110 GLN B CA  1 
ATOM 2559 C C   . GLN B 1 110 ? 21.22264  18.31581  52.21529  1.000 68.05857  ? 110 GLN B C   1 
ATOM 2560 O O   . GLN B 1 110 ? 21.69789  19.00872  53.12401  1.000 66.89075  ? 110 GLN B O   1 
ATOM 2561 C CB  . GLN B 1 110 ? 22.98042  17.26613  50.76183  1.000 66.51611  ? 110 GLN B CB  1 
ATOM 2562 C CG  . GLN B 1 110 ? 23.40969  16.98177  49.32612  1.000 70.00263  ? 110 GLN B CG  1 
ATOM 2563 C CD  . GLN B 1 110 ? 24.62098  16.07446  49.21241  1.000 68.29594  ? 110 GLN B CD  1 
ATOM 2564 O OE1 . GLN B 1 110 ? 25.26611  15.72489  50.21099  1.000 65.65534  ? 110 GLN B OE1 1 
ATOM 2565 N NE2 . GLN B 1 110 ? 24.93755  15.68706  47.98211  1.000 68.84714  ? 110 GLN B NE2 1 
ATOM 2566 N N   . GLY B 1 111 ? 20.13672  17.55411  52.35976  1.000 66.51289  ? 111 GLY B N   1 
ATOM 2567 C CA  . GLY B 1 111 ? 19.43797  17.42636  53.61773  1.000 61.12493  ? 111 GLY B CA  1 
ATOM 2568 C C   . GLY B 1 111 ? 19.63408  16.06811  54.24913  1.000 57.06671  ? 111 GLY B C   1 
ATOM 2569 O O   . GLY B 1 111 ? 19.05591  15.07630  53.80918  1.000 54.63358  ? 111 GLY B O   1 
ATOM 2570 N N   . TRP B 1 112 ? 20.42768  16.02303  55.30519  1.000 58.18800  ? 112 TRP B N   1 
ATOM 2571 C CA  . TRP B 1 112 ? 20.73404  14.78165  55.98884  1.000 58.68466  ? 112 TRP B CA  1 
ATOM 2572 C C   . TRP B 1 112 ? 19.68674  14.45431  57.03821  1.000 59.49762  ? 112 TRP B C   1 
ATOM 2573 O O   . TRP B 1 112 ? 18.88963  15.30140  57.45101  1.000 59.57692  ? 112 TRP B O   1 
ATOM 2574 C CB  . TRP B 1 112 ? 22.10926  14.85320  56.62614  1.000 59.01955  ? 112 TRP B CB  1 
ATOM 2575 C CG  . TRP B 1 112 ? 23.13409  14.76373  55.61493  1.000 58.21703  ? 112 TRP B CG  1 
ATOM 2576 C CD1 . TRP B 1 112 ? 23.74552  15.79368  54.97229  1.000 59.80598  ? 112 TRP B CD1 1 
ATOM 2577 C CD2 . TRP B 1 112 ? 23.68510  13.56080  55.07635  1.000 60.85340  ? 112 TRP B CD2 1 
ATOM 2578 N NE1 . TRP B 1 112 ? 24.65963  15.30220  54.06605  1.000 61.42440  ? 112 TRP B NE1 1 
ATOM 2579 C CE2 . TRP B 1 112 ? 24.63579  13.93138  54.11416  1.000 58.94022  ? 112 TRP B CE2 1 
ATOM 2580 C CE3 . TRP B 1 112 ? 23.46509  12.19840  55.31470  1.000 62.74271  ? 112 TRP B CE3 1 
ATOM 2581 C CZ2 . TRP B 1 112 ? 25.36650  12.99206  53.39736  1.000 59.05419  ? 112 TRP B CZ2 1 
ATOM 2582 C CZ3 . TRP B 1 112 ? 24.19444  11.26666  54.58757  1.000 59.05049  ? 112 TRP B CZ3 1 
ATOM 2583 C CH2 . TRP B 1 112 ? 25.12560  11.66854  53.64705  1.000 56.28447  ? 112 TRP B CH2 1 
ATOM 2584 N N   . CYS B 1 113 ? 19.69712  13.18669  57.44874  1.000 57.41378  ? 113 CYS B N   1 
ATOM 2585 C CA  . CYS B 1 113 ? 18.59974  12.57742  58.18136  1.000 55.22548  ? 113 CYS B CA  1 
ATOM 2586 C C   . CYS B 1 113 ? 18.91338  11.12786  58.53273  1.000 55.52394  ? 113 CYS B C   1 
ATOM 2587 O O   . CYS B 1 113 ? 19.53558  10.42638  57.74580  1.000 61.36568  ? 113 CYS B O   1 
ATOM 2588 C CB  . CYS B 1 113 ? 17.34588  12.68822  57.34166  1.000 55.25877  ? 113 CYS B CB  1 
ATOM 2589 S SG  . CYS B 1 113 ? 16.05426  11.67458  57.86504  1.000 62.18139  ? 113 CYS B SG  1 
ATOM 2590 N N   . ARG B 1 114 ? 18.52224  10.66871  59.69998  1.000 58.96444  ? 114 ARG B N   1 
ATOM 2591 C CA  . ARG B 1 114 ? 18.75411  9.29469   60.14359  1.000 60.22169  ? 114 ARG B CA  1 
ATOM 2592 C C   . ARG B 1 114 ? 17.40478  8.59986   60.10085  1.000 62.14779  ? 114 ARG B C   1 
ATOM 2593 O O   . ARG B 1 114 ? 16.61187  8.73638   61.03226  1.000 70.35037  ? 114 ARG B O   1 
ATOM 2594 C CB  . ARG B 1 114 ? 19.36371  9.25611   61.54935  1.000 60.63866  ? 114 ARG B CB  1 
ATOM 2595 C CG  . ARG B 1 114 ? 19.51809  7.85256   62.11566  1.000 66.42851  ? 114 ARG B CG  1 
ATOM 2596 C CD  . ARG B 1 114 ? 20.22161  7.77767   63.48824  1.000 72.47767  ? 114 ARG B CD  1 
ATOM 2597 N NE  . ARG B 1 114 ? 21.67907  7.91885   63.46988  1.000 73.49293  ? 114 ARG B NE  1 
ATOM 2598 C CZ  . ARG B 1 114 ? 22.53403  6.92378   63.24086  1.000 72.47378  ? 114 ARG B CZ  1 
ATOM 2599 N NH1 . ARG B 1 114 ? 22.11672  5.71424   62.90155  1.000 66.58601  ? 114 ARG B NH1 1 
ATOM 2600 N NH2 . ARG B 1 114 ? 23.84198  7.14771   63.36161  1.000 74.10773  ? 114 ARG B NH2 1 
ATOM 2601 N N   . GLY B 1 115 ? 17.14176  7.84796   59.03955  1.000 60.04492  ? 115 GLY B N   1 
ATOM 2602 C CA  . GLY B 1 115 ? 15.77654  7.43150   58.80823  1.000 59.50511  ? 115 GLY B CA  1 
ATOM 2603 C C   . GLY B 1 115 ? 15.12959  8.18010   57.66396  1.000 58.88505  ? 115 GLY B C   1 
ATOM 2604 O O   . GLY B 1 115 ? 14.02898  8.70963   57.81449  1.000 59.21455  ? 115 GLY B O   1 
ATOM 2605 N N   . MET B 1 116 ? 15.82659  8.25066   56.52623  1.000 60.18358  ? 116 MET B N   1 
ATOM 2606 C CA  . MET B 1 116 ? 15.42634  9.11402   55.41004  1.000 60.14891  ? 116 MET B CA  1 
ATOM 2607 C C   . MET B 1 116 ? 13.98484  8.89062   54.94446  1.000 58.40703  ? 116 MET B C   1 
ATOM 2608 O O   . MET B 1 116 ? 13.33725  9.82619   54.45834  1.000 56.81343  ? 116 MET B O   1 
ATOM 2609 C CB  . MET B 1 116 ? 16.41799  8.93137   54.25822  1.000 58.42822  ? 116 MET B CB  1 
ATOM 2610 C CG  . MET B 1 116 ? 16.11533  9.71718   53.00761  1.000 62.71354  ? 116 MET B CG  1 
ATOM 2611 S SD  . MET B 1 116 ? 17.44958  9.68165   51.74645  1.000 69.07992  ? 116 MET B SD  1 
ATOM 2612 C CE  . MET B 1 116 ? 16.50123  10.19845  50.32531  1.000 64.78776  ? 116 MET B CE  1 
ATOM 2613 N N   . SER B 1 117 ? 13.45875  7.67520   55.07872  1.000 54.19653  ? 117 SER B N   1 
ATOM 2614 C CA  . SER B 1 117 ? 12.07945  7.44510   54.65920  1.000 52.11034  ? 117 SER B CA  1 
ATOM 2615 C C   . SER B 1 117 ? 11.06277  7.74608   55.74482  1.000 56.02546  ? 117 SER B C   1 
ATOM 2616 O O   . SER B 1 117 ? 9.85901   7.57153   55.50958  1.000 52.27098  ? 117 SER B O   1 
ATOM 2617 C CB  . SER B 1 117 ? 11.89544  6.01338   54.16532  1.000 53.83293  ? 117 SER B CB  1 
ATOM 2618 O OG  . SER B 1 117 ? 12.29654  5.08245   55.13824  1.000 55.61915  ? 117 SER B OG  1 
ATOM 2619 N N   . PHE B 1 118 ? 11.51580  8.21062   56.90898  1.000 62.55573  ? 118 PHE B N   1 
ATOM 2620 C CA  . PHE B 1 118 ? 10.65989  8.64615   58.00197  1.000 60.71788  ? 118 PHE B CA  1 
ATOM 2621 C C   . PHE B 1 118 ? 10.52381  10.16565  58.07202  1.000 61.40763  ? 118 PHE B C   1 
ATOM 2622 O O   . PHE B 1 118 ? 9.40538   10.68750  58.01031  1.000 61.25298  ? 118 PHE B O   1 
ATOM 2623 C CB  . PHE B 1 118 ? 11.21746  8.09417   59.32131  1.000 63.88659  ? 118 PHE B CB  1 
ATOM 2624 C CG  . PHE B 1 118 ? 10.42403  8.49734   60.53981  1.000 67.81118  ? 118 PHE B CG  1 
ATOM 2625 C CD1 . PHE B 1 118 ? 9.18801   7.91608   60.80735  1.000 68.08860  ? 118 PHE B CD1 1 
ATOM 2626 C CD2 . PHE B 1 118 ? 10.90526  9.46836   61.40898  1.000 66.36973  ? 118 PHE B CD2 1 
ATOM 2627 C CE1 . PHE B 1 118 ? 8.44220   8.29679   61.91080  1.000 65.97675  ? 118 PHE B CE1 1 
ATOM 2628 C CE2 . PHE B 1 118 ? 10.16412  9.84528   62.50916  1.000 66.41476  ? 118 PHE B CE2 1 
ATOM 2629 C CZ  . PHE B 1 118 ? 8.93581   9.24950   62.75942  1.000 67.57297  ? 118 PHE B CZ  1 
ATOM 2630 N N   . ASP B 1 119 ? 11.64888  10.88454  58.15248  1.000 54.26033  ? 119 ASP B N   1 
ATOM 2631 C CA  . ASP B 1 119 ? 11.64608  12.31916  58.43926  1.000 52.06628  ? 119 ASP B CA  1 
ATOM 2632 C C   . ASP B 1 119 ? 11.12968  13.16129  57.26761  1.000 52.68322  ? 119 ASP B C   1 
ATOM 2633 O O   . ASP B 1 119 ? 10.11512  13.86488  57.38822  1.000 51.18927  ? 119 ASP B O   1 
ATOM 2634 C CB  . ASP B 1 119 ? 13.05565  12.73425  58.82533  1.000 50.38855  ? 119 ASP B CB  1 
ATOM 2635 C CG  . ASP B 1 119 ? 13.38162  12.40015  60.24667  1.000 58.82597  ? 119 ASP B CG  1 
ATOM 2636 O OD1 . ASP B 1 119 ? 12.52600  12.65301  61.11259  1.000 64.28948  ? 119 ASP B OD1 1 
ATOM 2637 O OD2 . ASP B 1 119 ? 14.46050  11.84144  60.52050  1.000 61.94383  ? 119 ASP B OD2 1 
ATOM 2638 N N   . PHE B 1 120 ? 11.82017  13.11857  56.13014  1.000 50.68295  ? 120 PHE B N   1 
ATOM 2639 C CA  . PHE B 1 120 ? 11.40314  13.91124  54.97450  1.000 49.82690  ? 120 PHE B CA  1 
ATOM 2640 C C   . PHE B 1 120 ? 9.95324   13.70074  54.54710  1.000 49.43466  ? 120 PHE B C   1 
ATOM 2641 O O   . PHE B 1 120 ? 9.30847   14.69210  54.16326  1.000 44.65965  ? 120 PHE B O   1 
ATOM 2642 C CB  . PHE B 1 120 ? 12.35052  13.64674  53.79094  1.000 52.33322  ? 120 PHE B CB  1 
ATOM 2643 C CG  . PHE B 1 120 ? 13.70097  14.24640  53.97618  1.000 52.02515  ? 120 PHE B CG  1 
ATOM 2644 C CD1 . PHE B 1 120 ? 13.85852  15.62429  53.90953  1.000 49.58603  ? 120 PHE B CD1 1 
ATOM 2645 C CD2 . PHE B 1 120 ? 14.80081  13.44970  54.22542  1.000 51.14038  ? 120 PHE B CD2 1 
ATOM 2646 C CE1 . PHE B 1 120 ? 15.07215  16.19244  54.11109  1.000 51.90712  ? 120 PHE B CE1 1 
ATOM 2647 C CE2 . PHE B 1 120 ? 16.02572  14.01617  54.40315  1.000 54.03762  ? 120 PHE B CE2 1 
ATOM 2648 C CZ  . PHE B 1 120 ? 16.16417  15.38976  54.34983  1.000 55.06420  ? 120 PHE B CZ  1 
ATOM 2649 N N   . PRO B 1 121 ? 9.39481   12.48073  54.54325  1.000 50.90523  ? 121 PRO B N   1 
ATOM 2650 C CA  . PRO B 1 121 ? 7.95586   12.35886  54.27215  1.000 48.69690  ? 121 PRO B CA  1 
ATOM 2651 C C   . PRO B 1 121 ? 7.07833   13.14087  55.23743  1.000 50.28369  ? 121 PRO B C   1 
ATOM 2652 O O   . PRO B 1 121 ? 6.00677   13.59564  54.81911  1.000 51.63716  ? 121 PRO B O   1 
ATOM 2653 C CB  . PRO B 1 121 ? 7.71411   10.84865  54.36372  1.000 44.40108  ? 121 PRO B CB  1 
ATOM 2654 C CG  . PRO B 1 121 ? 8.98772   10.26576  54.07302  1.000 44.29885  ? 121 PRO B CG  1 
ATOM 2655 C CD  . PRO B 1 121 ? 10.03155  11.15409  54.63242  1.000 45.75528  ? 121 PRO B CD  1 
ATOM 2656 N N   . ILE B 1 122 ? 7.48005   13.29806  56.50777  1.000 44.32453  ? 122 ILE B N   1 
ATOM 2657 C CA  . ILE B 1 122 ? 6.73292   14.17039  57.41384  1.000 50.65977  ? 122 ILE B CA  1 
ATOM 2658 C C   . ILE B 1 122 ? 6.99006   15.63945  57.08287  1.000 50.13451  ? 122 ILE B C   1 
ATOM 2659 O O   . ILE B 1 122 ? 6.06400   16.46506  57.06596  1.000 47.79168  ? 122 ILE B O   1 
ATOM 2660 C CB  . ILE B 1 122 ? 7.07192   13.84214  58.88551  1.000 56.02295  ? 122 ILE B CB  1 
ATOM 2661 C CG1 . ILE B 1 122 ? 6.40774   12.55661  59.35090  1.000 54.66768  ? 122 ILE B CG1 1 
ATOM 2662 C CG2 . ILE B 1 122 ? 6.64904   14.94241  59.82759  1.000 54.14907  ? 122 ILE B CG2 1 
ATOM 2663 C CD1 . ILE B 1 122 ? 7.02686   12.03504  60.62044  1.000 52.61024  ? 122 ILE B CD1 1 
ATOM 2664 N N   . LEU B 1 123 ? 8.25245   15.98655  56.82205  1.000 50.38351  ? 123 LEU B N   1 
ATOM 2665 C CA  . LEU B 1 123 ? 8.58877   17.34333  56.40004  1.000 47.22802  ? 123 LEU B CA  1 
ATOM 2666 C C   . LEU B 1 123 ? 7.77209   17.76574  55.19044  1.000 48.80135  ? 123 LEU B C   1 
ATOM 2667 O O   . LEU B 1 123 ? 7.19044   18.85321  55.17411  1.000 53.83869  ? 123 LEU B O   1 
ATOM 2668 C CB  . LEU B 1 123 ? 10.07247  17.45875  56.06850  1.000 45.37120  ? 123 LEU B CB  1 
ATOM 2669 C CG  . LEU B 1 123 ? 10.39328  18.91957  55.78318  1.000 50.84797  ? 123 LEU B CG  1 
ATOM 2670 C CD1 . LEU B 1 123 ? 10.12778  19.71823  57.07772  1.000 56.02934  ? 123 LEU B CD1 1 
ATOM 2671 C CD2 . LEU B 1 123 ? 11.81643  19.14944  55.26993  1.000 48.86454  ? 123 LEU B CD2 1 
ATOM 2672 N N   . VAL B 1 124 ? 7.71495   16.92838  54.15952  1.000 49.51016  ? 124 VAL B N   1 
ATOM 2673 C CA  . VAL B 1 124 ? 6.98482   17.34668  52.97640  1.000 48.85119  ? 124 VAL B CA  1 
ATOM 2674 C C   . VAL B 1 124 ? 5.49825   17.45825  53.28675  1.000 47.26709  ? 124 VAL B C   1 
ATOM 2675 O O   . VAL B 1 124 ? 4.83102   18.39348  52.84462  1.000 49.20894  ? 124 VAL B O   1 
ATOM 2676 C CB  . VAL B 1 124 ? 7.29094   16.41110  51.78924  1.000 48.33348  ? 124 VAL B CB  1 
ATOM 2677 C CG1 . VAL B 1 124 ? 6.42794   16.75030  50.58783  1.000 45.31713  ? 124 VAL B CG1 1 
ATOM 2678 C CG2 . VAL B 1 124 ? 8.74276   16.55877  51.40141  1.000 50.28514  ? 124 VAL B CG2 1 
ATOM 2679 N N   . ASP B 1 125 ? 4.95867   16.54570  54.08000  1.000 47.03453  ? 125 ASP B N   1 
ATOM 2680 C CA  . ASP B 1 125 ? 3.53283   16.62807  54.35069  1.000 49.95385  ? 125 ASP B CA  1 
ATOM 2681 C C   . ASP B 1 125 ? 3.18927   17.88822  55.14949  1.000 53.86901  ? 125 ASP B C   1 
ATOM 2682 O O   . ASP B 1 125 ? 2.11929   18.48627  54.96138  1.000 53.43745  ? 125 ASP B O   1 
ATOM 2683 C CB  . ASP B 1 125 ? 3.05841   15.37660  55.07892  1.000 54.89123  ? 125 ASP B CB  1 
ATOM 2684 C CG  . ASP B 1 125 ? 1.53660   15.26467  55.08729  1.000 60.47895  ? 125 ASP B CG  1 
ATOM 2685 O OD1 . ASP B 1 125 ? 0.96871   14.97115  54.00062  1.000 63.74870  ? 125 ASP B OD1 1 
ATOM 2686 O OD2 . ASP B 1 125 ? 0.91086   15.49789  56.14378  1.000 55.13097  ? 125 ASP B OD2 1 
ATOM 2687 N N   . LEU B 1 126 ? 4.08223   18.31157  56.04622  1.000 50.84131  ? 126 LEU B N   1 
ATOM 2688 C CA  . LEU B 1 126 ? 3.88307   19.59580  56.70708  1.000 52.63236  ? 126 LEU B CA  1 
ATOM 2689 C C   . LEU B 1 126 ? 3.96433   20.76620  55.72096  1.000 53.35347  ? 126 LEU B C   1 
ATOM 2690 O O   . LEU B 1 126 ? 3.16844   21.71261  55.79611  1.000 51.72161  ? 126 LEU B O   1 
ATOM 2691 C CB  . LEU B 1 126 ? 4.88921   19.75885  57.84514  1.000 53.53412  ? 126 LEU B CB  1 
ATOM 2692 C CG  . LEU B 1 126 ? 4.62061   18.87986  59.06584  1.000 50.71052  ? 126 LEU B CG  1 
ATOM 2693 C CD1 . LEU B 1 126 ? 5.64740   19.15068  60.12141  1.000 50.56962  ? 126 LEU B CD1 1 
ATOM 2694 C CD2 . LEU B 1 126 ? 3.22372   19.09570  59.60255  1.000 47.04496  ? 126 LEU B CD2 1 
ATOM 2695 N N   . ILE B 1 127 ? 4.90871   20.71599  54.78348  1.000 51.54542  ? 127 ILE B N   1 
ATOM 2696 C CA  . ILE B 1 127 ? 4.99924   21.75338  53.75817  1.000 52.34094  ? 127 ILE B CA  1 
ATOM 2697 C C   . ILE B 1 127 ? 3.72878   21.80992  52.89139  1.000 52.75572  ? 127 ILE B C   1 
ATOM 2698 O O   . ILE B 1 127 ? 3.18239   22.89697  52.65869  1.000 50.35328  ? 127 ILE B O   1 
ATOM 2699 C CB  . ILE B 1 127 ? 6.26376   21.54709  52.91250  1.000 52.93194  ? 127 ILE B CB  1 
ATOM 2700 C CG1 . ILE B 1 127 ? 7.50410   21.69537  53.78642  1.000 51.81557  ? 127 ILE B CG1 1 
ATOM 2701 C CG2 . ILE B 1 127 ? 6.30232   22.54200  51.79566  1.000 58.23550  ? 127 ILE B CG2 1 
ATOM 2702 C CD1 . ILE B 1 127 ? 8.76524   21.29234  53.08888  1.000 53.71361  ? 127 ILE B CD1 1 
ATOM 2703 N N   . ARG B 1 128 ? 3.21987   20.65799  52.40014  1.000 50.62928  ? 128 ARG B N   1 
ATOM 2704 C CA  . ARG B 1 128 ? 2.02326   20.77536  51.55329  1.000 51.39229  ? 128 ARG B CA  1 
ATOM 2705 C C   . ARG B 1 128 ? 0.81886   21.34091  52.28353  1.000 55.96224  ? 128 ARG B C   1 
ATOM 2706 O O   . ARG B 1 128 ? -0.09093  21.86194  51.62022  1.000 56.15450  ? 128 ARG B O   1 
ATOM 2707 C CB  . ARG B 1 128 ? 1.58493   19.48363  50.81411  1.000 52.80331  ? 128 ARG B CB  1 
ATOM 2708 C CG  . ARG B 1 128 ? 1.83423   18.11306  51.37790  1.000 53.37743  ? 128 ARG B CG  1 
ATOM 2709 C CD  . ARG B 1 128 ? 2.44547   17.22737  50.28418  1.000 53.63463  ? 128 ARG B CD  1 
ATOM 2710 N NE  . ARG B 1 128 ? 3.13474   16.03103  50.77518  1.000 61.20131  ? 128 ARG B NE  1 
ATOM 2711 C CZ  . ARG B 1 128 ? 2.58135   14.89098  51.20059  1.000 63.51769  ? 128 ARG B CZ  1 
ATOM 2712 N NH1 . ARG B 1 128 ? 1.26938   14.75893  51.37741  1.000 60.99907  ? 128 ARG B NH1 1 
ATOM 2713 N NH2 . ARG B 1 128 ? 3.37499   13.87428  51.52822  1.000 60.54129  ? 128 ARG B NH2 1 
ATOM 2714 N N   . ASP B 1 129 ? 0.80832   21.30408  53.62330  1.000 69.27516  ? 129 ASP B N   1 
ATOM 2715 C CA  . ASP B 1 129 ? -0.30047  21.87779  54.38624  1.000 69.83408  ? 129 ASP B CA  1 
ATOM 2716 C C   . ASP B 1 129 ? -0.45330  23.37530  54.20043  1.000 71.27197  ? 129 ASP B C   1 
ATOM 2717 O O   . ASP B 1 129 ? -1.56040  23.88914  54.39371  1.000 71.73292  ? 129 ASP B O   1 
ATOM 2718 C CB  . ASP B 1 129 ? -0.14743  21.58757  55.86289  1.000 70.31441  ? 129 ASP B CB  1 
ATOM 2719 C CG  . ASP B 1 129 ? -0.55846  20.19366  56.20954  1.000 72.14601  ? 129 ASP B CG  1 
ATOM 2720 O OD1 . ASP B 1 129 ? -1.36621  19.63899  55.43449  1.000 73.02038  ? 129 ASP B OD1 1 
ATOM 2721 O OD2 . ASP B 1 129 ? -0.12003  19.67719  57.27099  1.000 73.90886  ? 129 ASP B OD2 1 
ATOM 2722 N N   . ILE B 1 130 ? 0.62130   24.09436  53.85565  1.000 58.20858  ? 130 ILE B N   1 
ATOM 2723 C CA  . ILE B 1 130 ? 0.46961   25.50511  53.51188  1.000 53.56238  ? 130 ILE B CA  1 
ATOM 2724 C C   . ILE B 1 130 ? -0.40151  25.62390  52.26987  1.000 57.21478  ? 130 ILE B C   1 
ATOM 2725 O O   . ILE B 1 130 ? -1.18086  26.57604  52.11372  1.000 56.21493  ? 130 ILE B O   1 
ATOM 2726 C CB  . ILE B 1 130 ? 1.84502   26.14490  53.27936  1.000 54.01235  ? 130 ILE B CB  1 
ATOM 2727 C CG1 . ILE B 1 130 ? 2.79707   25.82141  54.41069  1.000 53.01832  ? 130 ILE B CG1 1 
ATOM 2728 C CG2 . ILE B 1 130 ? 1.71629   27.64199  53.16236  1.000 56.16240  ? 130 ILE B CG2 1 
ATOM 2729 C CD1 . ILE B 1 130 ? 4.25397   26.03500  54.00646  1.000 55.08800  ? 130 ILE B CD1 1 
ATOM 2730 N N   . GLN B 1 131 ? -0.26687  24.65035  51.35309  1.000 56.91032  ? 131 GLN B N   1 
ATOM 2731 C CA  . GLN B 1 131 ? -1.03924  24.65582  50.12285  1.000 54.47086  ? 131 GLN B CA  1 
ATOM 2732 C C   . GLN B 1 131 ? -2.42818  24.08887  50.30927  1.000 54.48431  ? 131 GLN B C   1 
ATOM 2733 O O   . GLN B 1 131 ? -3.38559  24.61487  49.72874  1.000 56.04242  ? 131 GLN B O   1 
ATOM 2734 C CB  . GLN B 1 131 ? -0.30095  23.89585  49.04199  1.000 55.42027  ? 131 GLN B CB  1 
ATOM 2735 C CG  . GLN B 1 131 ? 0.73309   24.71993  48.36564  1.000 54.43502  ? 131 GLN B CG  1 
ATOM 2736 C CD  . GLN B 1 131 ? 1.53648   23.89007  47.41058  1.000 61.63346  ? 131 GLN B CD  1 
ATOM 2737 O OE1 . GLN B 1 131 ? 1.38316   22.66810  47.35783  1.000 61.68448  ? 131 GLN B OE1 1 
ATOM 2738 N NE2 . GLN B 1 131 ? 2.41234   24.53847  46.64978  1.000 66.62055  ? 131 GLN B NE2 1 
ATOM 2739 N N   . ARG B 1 132 ? -2.56776  23.02529  51.09800  1.000 52.95409  ? 132 ARG B N   1 
ATOM 2740 C CA  . ARG B 1 132 ? -3.91413  22.57811  51.42755  1.000 53.17970  ? 132 ARG B CA  1 
ATOM 2741 C C   . ARG B 1 132 ? -4.73214  23.71655  52.02938  1.000 54.77244  ? 132 ARG B C   1 
ATOM 2742 O O   . ARG B 1 132 ? -5.89989  23.90146  51.67890  1.000 56.02823  ? 132 ARG B O   1 
ATOM 2743 C CB  . ARG B 1 132 ? -3.86204  21.40573  52.38669  1.000 51.48412  ? 132 ARG B CB  1 
ATOM 2744 C CG  . ARG B 1 132 ? -3.21568  20.20938  51.86735  1.000 50.07021  ? 132 ARG B CG  1 
ATOM 2745 C CD  . ARG B 1 132 ? -3.24979  19.14465  52.89418  1.000 48.72903  ? 132 ARG B CD  1 
ATOM 2746 N NE  . ARG B 1 132 ? -2.72196  17.89061  52.38316  1.000 55.37680  ? 132 ARG B NE  1 
ATOM 2747 C CZ  . ARG B 1 132 ? -1.55441  17.35897  52.70868  1.000 56.72732  ? 132 ARG B CZ  1 
ATOM 2748 N NH1 . ARG B 1 132 ? -0.81316  17.85818  53.68501  1.000 57.84267  ? 132 ARG B NH1 1 
ATOM 2749 N NH2 . ARG B 1 132 ? -1.14464  16.26569  52.07183  1.000 57.71505  ? 132 ARG B NH2 1 
ATOM 2750 N N   . LEU B 1 133 ? -4.11388  24.49583  52.92536  1.000 54.87498  ? 133 LEU B N   1 
ATOM 2751 C CA  . LEU B 1 133 ? -4.72918  25.66799  53.54831  1.000 56.45272  ? 133 LEU B CA  1 
ATOM 2752 C C   . LEU B 1 133 ? -5.18282  26.70763  52.52740  1.000 58.59583  ? 133 LEU B C   1 
ATOM 2753 O O   . LEU B 1 133 ? -6.18272  27.41117  52.74912  1.000 60.16183  ? 133 LEU B O   1 
ATOM 2754 C CB  . LEU B 1 133 ? -3.71630  26.27929  54.51017  1.000 56.19906  ? 133 LEU B CB  1 
ATOM 2755 C CG  . LEU B 1 133 ? -4.03187  27.53559  55.32363  1.000 57.72076  ? 133 LEU B CG  1 
ATOM 2756 C CD1 . LEU B 1 133 ? -5.18284  27.32089  56.27666  1.000 57.73239  ? 133 LEU B CD1 1 
ATOM 2757 C CD2 . LEU B 1 133 ? -2.76777  27.95126  56.07152  1.000 57.34202  ? 133 LEU B CD2 1 
ATOM 2758 N N   . ASN B 1 134 ? -4.44879  26.81288  51.40627  1.000 58.79410  ? 134 ASN B N   1 
ATOM 2759 C CA  . ASN B 1 134 ? -4.70636  27.64934  50.24782  1.000 60.76664  ? 134 ASN B CA  1 
ATOM 2760 C C   . ASN B 1 134 ? -5.85583  27.13567  49.39734  1.000 61.41959  ? 134 ASN B C   1 
ATOM 2761 O O   . ASN B 1 134 ? -6.15973  27.75757  48.38794  1.000 63.19139  ? 134 ASN B O   1 
ATOM 2762 C CB  . ASN B 1 134 ? -3.43676  27.70907  49.40022  1.000 60.44291  ? 134 ASN B CB  1 
ATOM 2763 C CG  . ASN B 1 134 ? -3.27635  29.03549  48.59518  1.000 62.78369  ? 134 ASN B CG  1 
ATOM 2764 O OD1 . ASN B 1 134 ? -4.06301  30.00508  48.69898  1.000 64.78299  ? 134 ASN B OD1 1 
ATOM 2765 N ND2 . ASN B 1 134 ? -2.21150  29.07410  47.81042  1.000 62.61633  ? 134 ASN B ND2 1 
ATOM 2766 N N   . GLY B 1 135 ? -6.48843  26.01941  49.75133  1.000 60.53117  ? 135 GLY B N   1 
ATOM 2767 C CA  . GLY B 1 135 ? -7.53753  25.42580  48.94582  1.000 60.87498  ? 135 GLY B CA  1 
ATOM 2768 C C   . GLY B 1 135 ? -7.06612  24.54758  47.80065  1.000 61.02166  ? 135 GLY B C   1 
ATOM 2769 O O   . GLY B 1 135 ? -7.90375  24.05238  47.03757  1.000 62.38602  ? 135 GLY B O   1 
ATOM 2770 N N   . VAL B 1 136 ? -5.75784  24.34492  47.64957  1.000 58.70672  ? 136 VAL B N   1 
ATOM 2771 C CA  . VAL B 1 136 ? -5.23467  23.47798  46.60370  1.000 61.62827  ? 136 VAL B CA  1 
ATOM 2772 C C   . VAL B 1 136 ? -5.65642  22.03797  46.88640  1.000 65.39455  ? 136 VAL B C   1 
ATOM 2773 O O   . VAL B 1 136 ? -5.40201  21.50302  47.97568  1.000 55.13675  ? 136 VAL B O   1 
ATOM 2774 C CB  . VAL B 1 136 ? -3.70228  23.60461  46.53521  1.000 58.52619  ? 136 VAL B CB  1 
ATOM 2775 C CG1 . VAL B 1 136 ? -3.12202  22.68883  45.48160  1.000 56.16334  ? 136 VAL B CG1 1 
ATOM 2776 C CG2 . VAL B 1 136 ? -3.29443  25.02845  46.30999  1.000 58.42315  ? 136 VAL B CG2 1 
ATOM 2777 N N   . SER B 1 137 ? -6.27698  21.39389  45.89138  1.000 69.82927  ? 137 SER B N   1 
ATOM 2778 C CA  . SER B 1 137 ? -6.70973  20.00877  46.02601  1.000 66.65430  ? 137 SER B CA  1 
ATOM 2779 C C   . SER B 1 137 ? -5.51775  19.07018  46.09408  1.000 68.14788  ? 137 SER B C   1 
ATOM 2780 O O   . SER B 1 137 ? -4.38886  19.43058  45.76332  1.000 68.63024  ? 137 SER B O   1 
ATOM 2781 C CB  . SER B 1 137 ? -7.62859  19.60079  44.88314  1.000 67.24835  ? 137 SER B CB  1 
ATOM 2782 O OG  . SER B 1 137 ? -8.90687  20.18710  45.08427  1.000 77.50140  ? 137 SER B OG  1 
ATOM 2783 N N   . GLU B 1 138 ? -5.78989  17.84682  46.56119  1.000 66.33525  ? 138 GLU B N   1 
ATOM 2784 C CA  . GLU B 1 138 ? -4.71846  16.93366  46.94490  1.000 62.75407  ? 138 GLU B CA  1 
ATOM 2785 C C   . GLU B 1 138 ? -3.96134  16.39099  45.73489  1.000 60.79553  ? 138 GLU B C   1 
ATOM 2786 O O   . GLU B 1 138 ? -2.79493  16.00656  45.88075  1.000 58.81541  ? 138 GLU B O   1 
ATOM 2787 C CB  . GLU B 1 138 ? -5.28807  15.79329  47.80258  1.000 60.97558  ? 138 GLU B CB  1 
ATOM 2788 C CG  . GLU B 1 138 ? -4.24561  14.85145  48.44570  1.000 58.53582  ? 138 GLU B CG  1 
ATOM 2789 C CD  . GLU B 1 138 ? -3.43845  15.46833  49.62834  1.000 62.68115  ? 138 GLU B CD  1 
ATOM 2790 O OE1 . GLU B 1 138 ? -3.94303  16.39644  50.31083  1.000 59.73919  ? 138 GLU B OE1 1 
ATOM 2791 O OE2 . GLU B 1 138 ? -2.29643  15.00107  49.88431  1.000 60.87172  ? 138 GLU B OE2 1 
ATOM 2792 N N   . ASN B 1 139 ? -4.59818  16.34162  44.54311  1.000 64.47360  ? 139 ASN B N   1 
ATOM 2793 C CA  . ASN B 1 139 ? -3.91841  15.95518  43.29899  1.000 64.50772  ? 139 ASN B CA  1 
ATOM 2794 C C   . ASN B 1 139 ? -3.20073  17.10119  42.60858  1.000 64.00768  ? 139 ASN B C   1 
ATOM 2795 O O   . ASN B 1 139 ? -2.45695  16.86170  41.65284  1.000 63.99605  ? 139 ASN B O   1 
ATOM 2796 C CB  . ASN B 1 139 ? -4.87945  15.35971  42.27520  1.000 63.22955  ? 139 ASN B CB  1 
ATOM 2797 C CG  . ASN B 1 139 ? -6.01636  16.25998  41.99676  1.000 69.01777  ? 139 ASN B CG  1 
ATOM 2798 O OD1 . ASN B 1 139 ? -6.22884  17.21735  42.73016  1.000 73.36113  ? 139 ASN B OD1 1 
ATOM 2799 N ND2 . ASN B 1 139 ? -6.70932  16.03410  40.88869  1.000 73.89702  ? 139 ASN B ND2 1 
ATOM 2800 N N   . GLU B 1 140 ? -3.41385  18.33125  43.04861  1.000 65.30455  ? 140 GLU B N   1 
ATOM 2801 C CA  . GLU B 1 140 ? -2.80560  19.48982  42.42536  1.000 60.84316  ? 140 GLU B CA  1 
ATOM 2802 C C   . GLU B 1 140 ? -1.76578  20.14740  43.31652  1.000 57.75692  ? 140 GLU B C   1 
ATOM 2803 O O   . GLU B 1 140 ? -1.29382  21.23373  42.99552  1.000 61.91658  ? 140 GLU B O   1 
ATOM 2804 C CB  . GLU B 1 140 ? -3.90937  20.44569  42.00214  1.000 57.26700  ? 140 GLU B CB  1 
ATOM 2805 C CG  . GLU B 1 140 ? -4.61348  19.87407  40.79683  1.000 67.32634  ? 140 GLU B CG  1 
ATOM 2806 C CD  . GLU B 1 140 ? -5.91491  20.56207  40.41274  1.000 80.04109  ? 140 GLU B CD  1 
ATOM 2807 O OE1 . GLU B 1 140 ? -6.50821  21.28174  41.25861  1.000 80.05851  ? 140 GLU B OE1 1 
ATOM 2808 O OE2 . GLU B 1 140 ? -6.32586  20.39569  39.23032  1.000 82.67059  ? 140 GLU B OE2 1 
ATOM 2809 N N   . LEU B 1 141 ? -1.36553  19.48991  44.39859  1.000 55.62157  ? 141 LEU B N   1 
ATOM 2810 C CA  . LEU B 1 141 ? -0.27461  19.98216  45.22622  1.000 58.63153  ? 141 LEU B CA  1 
ATOM 2811 C C   . LEU B 1 141 ? 1.03063   19.91341  44.44042  1.000 61.96935  ? 141 LEU B C   1 
ATOM 2812 O O   . LEU B 1 141 ? 1.25799   18.97722  43.67079  1.000 67.11476  ? 141 LEU B O   1 
ATOM 2813 C CB  . LEU B 1 141 ? -0.15775  19.15111  46.52542  1.000 59.09154  ? 141 LEU B CB  1 
ATOM 2814 C CG  . LEU B 1 141 ? -1.31121  19.02704  47.56863  1.000 59.53936  ? 141 LEU B CG  1 
ATOM 2815 C CD1 . LEU B 1 141 ? -0.98785  18.04085  48.67017  1.000 52.57060  ? 141 LEU B CD1 1 
ATOM 2816 C CD2 . LEU B 1 141 ? -1.79440  20.36532  48.18556  1.000 56.61203  ? 141 LEU B CD2 1 
ATOM 2817 N N   . ASP B 1 142 ? 1.88796   20.91534  44.61814  1.000 62.94335  ? 142 ASP B N   1 
ATOM 2818 C CA  . ASP B 1 142 ? 3.23354   20.85559  44.05478  1.000 63.45839  ? 142 ASP B CA  1 
ATOM 2819 C C   . ASP B 1 142 ? 4.20747   21.63695  44.91392  1.000 63.98611  ? 142 ASP B C   1 
ATOM 2820 O O   . ASP B 1 142 ? 4.22039   22.86531  44.86986  1.000 66.67700  ? 142 ASP B O   1 
ATOM 2821 C CB  . ASP B 1 142 ? 3.29388   21.39237  42.64373  1.000 64.06402  ? 142 ASP B CB  1 
ATOM 2822 C CG  . ASP B 1 142 ? 4.67693   21.29133  42.10622  1.000 66.95864  ? 142 ASP B CG  1 
ATOM 2823 O OD1 . ASP B 1 142 ? 5.08574   20.14571  41.84011  1.000 72.69075  ? 142 ASP B OD1 1 
ATOM 2824 O OD2 . ASP B 1 142 ? 5.38069   22.31617  42.03140  1.000 71.46267  ? 142 ASP B OD2 1 
ATOM 2825 N N   . THR B 1 143 ? 5.07632   20.93251  45.61718  1.000 62.74294  ? 143 THR B N   1 
ATOM 2826 C CA  . THR B 1 143 ? 6.00315   21.55902  46.54086  1.000 66.76021  ? 143 THR B CA  1 
ATOM 2827 C C   . THR B 1 143 ? 7.42973   21.49965  46.03324  1.000 69.54659  ? 143 THR B C   1 
ATOM 2828 O O   . THR B 1 143 ? 8.35928   21.62518  46.82930  1.000 71.10297  ? 143 THR B O   1 
ATOM 2829 C CB  . THR B 1 143 ? 5.91907   20.91019  47.93205  1.000 67.71049  ? 143 THR B CB  1 
ATOM 2830 O OG1 . THR B 1 143 ? 6.32746   19.53813  47.85634  1.000 71.65806  ? 143 THR B OG1 1 
ATOM 2831 C CG2 . THR B 1 143 ? 4.48921   20.98959  48.52960  1.000 58.46139  ? 143 THR B CG2 1 
ATOM 2832 N N   . PHE B 1 144 ? 7.63037   21.29934  44.72859  1.000 72.02166  ? 144 PHE B N   1 
ATOM 2833 C CA  . PHE B 1 144 ? 8.99214   21.10537  44.23417  1.000 73.27306  ? 144 PHE B CA  1 
ATOM 2834 C C   . PHE B 1 144 ? 9.88151   22.27493  44.60781  1.000 74.23815  ? 144 PHE B C   1 
ATOM 2835 O O   . PHE B 1 144 ? 10.99512  22.08533  45.10957  1.000 72.94581  ? 144 PHE B O   1 
ATOM 2836 C CB  . PHE B 1 144 ? 9.00843   20.93224  42.72566  1.000 73.40956  ? 144 PHE B CB  1 
ATOM 2837 C CG  . PHE B 1 144 ? 10.37256  20.66599  42.18486  1.000 71.07393  ? 144 PHE B CG  1 
ATOM 2838 C CD1 . PHE B 1 144 ? 10.92286  19.39669  42.25981  1.000 70.40819  ? 144 PHE B CD1 1 
ATOM 2839 C CD2 . PHE B 1 144 ? 11.12822  21.68759  41.63478  1.000 72.32288  ? 144 PHE B CD2 1 
ATOM 2840 C CE1 . PHE B 1 144 ? 12.20849  19.14888  41.76710  1.000 70.22689  ? 144 PHE B CE1 1 
ATOM 2841 C CE2 . PHE B 1 144 ? 12.40580  21.44863  41.13831  1.000 66.63714  ? 144 PHE B CE2 1 
ATOM 2842 C CZ  . PHE B 1 144 ? 12.94943  20.18193  41.20806  1.000 64.98254  ? 144 PHE B CZ  1 
ATOM 2843 N N   . LYS B 1 145 ? 9.39081   23.49240  44.37267  1.000 80.59374  ? 145 LYS B N   1 
ATOM 2844 C CA  . LYS B 1 145 ? 10.03416  24.76143  44.70169  1.000 81.18362  ? 145 LYS B CA  1 
ATOM 2845 C C   . LYS B 1 145 ? 9.85479   25.19676  46.16674  1.000 80.91086  ? 145 LYS B C   1 
ATOM 2846 O O   . LYS B 1 145 ? 10.12514  26.35457  46.48221  1.000 80.16260  ? 145 LYS B O   1 
ATOM 2847 C CB  . LYS B 1 145 ? 9.48731   25.86755  43.78791  1.000 83.54111  ? 145 LYS B CB  1 
ATOM 2848 C CG  . LYS B 1 145 ? 10.21172  26.01265  42.47214  1.000 86.20470  ? 145 LYS B CG  1 
ATOM 2849 C CD  . LYS B 1 145 ? 9.89541   24.87700  41.51142  1.000 91.54984  ? 145 LYS B CD  1 
ATOM 2850 C CE  . LYS B 1 145 ? 8.48618   24.95894  40.92221  1.000 94.83217  ? 145 LYS B CE  1 
ATOM 2851 N NZ  . LYS B 1 145 ? 8.24756   23.84356  39.94738  1.000 92.11195  ? 145 LYS B NZ  1 
ATOM 2852 N N   . LEU B 1 146 ? 9.38049   24.33790  47.06463  1.000 76.68094  ? 146 LEU B N   1 
ATOM 2853 C CA  . LEU B 1 146 ? 9.18194   24.72918  48.45846  1.000 73.54494  ? 146 LEU B CA  1 
ATOM 2854 C C   . LEU B 1 146 ? 9.93739   23.84857  49.43999  1.000 70.18413  ? 146 LEU B C   1 
ATOM 2855 O O   . LEU B 1 146 ? 9.68891   23.94016  50.64630  1.000 69.92882  ? 146 LEU B O   1 
ATOM 2856 C CB  . LEU B 1 146 ? 7.70551   24.68479  48.84052  1.000 68.35892  ? 146 LEU B CB  1 
ATOM 2857 C CG  . LEU B 1 146 ? 6.73028   25.46947  47.99209  1.000 71.69960  ? 146 LEU B CG  1 
ATOM 2858 C CD1 . LEU B 1 146 ? 5.37085   25.39194  48.68150  1.000 66.65087  ? 146 LEU B CD1 1 
ATOM 2859 C CD2 . LEU B 1 146 ? 7.21551   26.90203  47.75619  1.000 76.23043  ? 146 LEU B CD2 1 
ATOM 2860 N N   . GLU B 1 147 ? 10.78722  22.99754  48.97417  1.000 69.87436  ? 147 GLU B N   1 
ATOM 2861 C CA  . GLU B 1 147 ? 11.43706  22.07392  49.87592  1.000 67.43760  ? 147 GLU B CA  1 
ATOM 2862 C C   . GLU B 1 147 ? 12.86427  22.53322  50.14354  1.000 68.30366  ? 147 GLU B C   1 
ATOM 2863 O O   . GLU B 1 147 ? 13.50341  23.12886  49.26924  1.000 69.15116  ? 147 GLU B O   1 
ATOM 2864 C CB  . GLU B 1 147 ? 11.44883  20.67548  49.26916  1.000 70.01271  ? 147 GLU B CB  1 
ATOM 2865 C CG  . GLU B 1 147 ? 10.06043  20.20496  48.87887  1.000 72.21880  ? 147 GLU B CG  1 
ATOM 2866 C CD  . GLU B 1 147 ? 10.03313  18.85320  48.18174  1.000 78.05916  ? 147 GLU B CD  1 
ATOM 2867 O OE1 . GLU B 1 147 ? 11.10088  18.21001  48.02595  1.000 80.32148  ? 147 GLU B OE1 1 
ATOM 2868 O OE2 . GLU B 1 147 ? 8.93385   18.46625  47.73987  1.000 78.59745  ? 147 GLU B OE2 1 
ATOM 2869 N N   . PRO B 1 148 ? 13.38842  22.28862  51.34812  1.000 65.09909  ? 148 PRO B N   1 
ATOM 2870 C CA  . PRO B 1 148 ? 14.72384  22.79806  51.68800  1.000 63.23891  ? 148 PRO B CA  1 
ATOM 2871 C C   . PRO B 1 148 ? 15.84748  22.20346  50.85197  1.000 65.68127  ? 148 PRO B C   1 
ATOM 2872 O O   . PRO B 1 148 ? 16.96680  22.73009  50.87719  1.000 66.06059  ? 148 PRO B O   1 
ATOM 2873 C CB  . PRO B 1 148 ? 14.86795  22.42744  53.16321  1.000 62.69050  ? 148 PRO B CB  1 
ATOM 2874 C CG  . PRO B 1 148 ? 13.94867  21.30354  53.35396  1.000 64.84718  ? 148 PRO B CG  1 
ATOM 2875 C CD  . PRO B 1 148 ? 12.78507  21.54073  52.45872  1.000 64.11021  ? 148 PRO B CD  1 
ATOM 2876 N N   . CYS B 1 149 ? 15.59456  21.12071  50.13029  1.000 65.84554  ? 149 CYS B N   1 
ATOM 2877 C CA  . CYS B 1 149 ? 16.56213  20.56394  49.20188  1.000 63.69679  ? 149 CYS B CA  1 
ATOM 2878 C C   . CYS B 1 149 ? 15.78846  19.85788  48.10168  1.000 62.02942  ? 149 CYS B C   1 
ATOM 2879 O O   . CYS B 1 149 ? 14.57879  19.65010  48.20487  1.000 62.79859  ? 149 CYS B O   1 
ATOM 2880 C CB  . CYS B 1 149 ? 17.55765  19.62183  49.90466  1.000 63.56734  ? 149 CYS B CB  1 
ATOM 2881 S SG  . CYS B 1 149 ? 16.85455  18.16806  50.75627  1.000 62.08802  ? 149 CYS B SG  1 
ATOM 2882 N N   . LYS B 1 150 ? 16.48511  19.54395  47.01936  1.000 63.32162  ? 150 LYS B N   1 
ATOM 2883 C CA  . LYS B 1 150 ? 15.87520  18.80357  45.92831  1.000 59.39483  ? 150 LYS B CA  1 
ATOM 2884 C C   . LYS B 1 150 ? 15.83042  17.32218  46.28274  1.000 60.67768  ? 150 LYS B C   1 
ATOM 2885 O O   . LYS B 1 150 ? 16.76046  16.79846  46.90849  1.000 60.11679  ? 150 LYS B O   1 
ATOM 2886 C CB  . LYS B 1 150 ? 16.66387  19.04879  44.65188  1.000 59.15656  ? 150 LYS B CB  1 
ATOM 2887 C CG  . LYS B 1 150 ? 16.68258  20.50458  44.27289  1.000 58.76600  ? 150 LYS B CG  1 
ATOM 2888 C CD  . LYS B 1 150 ? 15.27400  20.95182  43.98604  1.000 60.05561  ? 150 LYS B CD  1 
ATOM 2889 C CE  . LYS B 1 150 ? 15.24654  22.40316  43.59875  1.000 64.77568  ? 150 LYS B CE  1 
ATOM 2890 N NZ  . LYS B 1 150 ? 13.86738  22.90512  43.40852  1.000 68.07006  ? 150 LYS B NZ  1 
ATOM 2891 N N   . PHE B 1 151 ? 14.74438  16.63962  45.88974  1.000 57.92905  ? 151 PHE B N   1 
ATOM 2892 C CA  . PHE B 1 151 ? 14.51443  15.31785  46.46862  1.000 55.66865  ? 151 PHE B CA  1 
ATOM 2893 C C   . PHE B 1 151 ? 15.67090  14.36915  46.23135  1.000 55.26420  ? 151 PHE B C   1 
ATOM 2894 O O   . PHE B 1 151 ? 15.86301  13.44709  47.02525  1.000 55.54275  ? 151 PHE B O   1 
ATOM 2895 C CB  . PHE B 1 151 ? 13.22924  14.67407  45.94992  1.000 56.17032  ? 151 PHE B CB  1 
ATOM 2896 C CG  . PHE B 1 151 ? 13.22276  14.38995  44.48437  1.000 55.69448  ? 151 PHE B CG  1 
ATOM 2897 C CD1 . PHE B 1 151 ? 12.62212  15.27426  43.60944  1.000 57.83128  ? 151 PHE B CD1 1 
ATOM 2898 C CD2 . PHE B 1 151 ? 13.80593  13.22357  43.97749  1.000 58.45753  ? 151 PHE B CD2 1 
ATOM 2899 C CE1 . PHE B 1 151 ? 12.60674  15.01148  42.23448  1.000 62.52631  ? 151 PHE B CE1 1 
ATOM 2900 C CE2 . PHE B 1 151 ? 13.79423  12.94982  42.61990  1.000 59.67645  ? 151 PHE B CE2 1 
ATOM 2901 C CZ  . PHE B 1 151 ? 13.19049  13.84595  41.73763  1.000 59.09767  ? 151 PHE B CZ  1 
ATOM 2902 N N   . TRP B 1 152 ? 16.44808  14.57844  45.16964  1.000 56.68829  ? 152 TRP B N   1 
ATOM 2903 C CA  . TRP B 1 152 ? 17.63360  13.77752  44.92216  1.000 53.83415  ? 152 TRP B CA  1 
ATOM 2904 C C   . TRP B 1 152 ? 18.83597  14.21996  45.74036  1.000 57.28604  ? 152 TRP B C   1 
ATOM 2905 O O   . TRP B 1 152 ? 19.87279  13.55742  45.67306  1.000 58.35625  ? 152 TRP B O   1 
ATOM 2906 C CB  . TRP B 1 152 ? 17.99286  13.83148  43.45041  1.000 56.46021  ? 152 TRP B CB  1 
ATOM 2907 C CG  . TRP B 1 152 ? 18.25458  15.22253  42.97197  1.000 56.47619  ? 152 TRP B CG  1 
ATOM 2908 C CD1 . TRP B 1 152 ? 19.42323  15.91817  43.07541  1.000 56.02718  ? 152 TRP B CD1 1 
ATOM 2909 C CD2 . TRP B 1 152 ? 17.33255  16.08594  42.30110  1.000 55.43668  ? 152 TRP B CD2 1 
ATOM 2910 N NE1 . TRP B 1 152 ? 19.27928  17.16481  42.52992  1.000 54.67047  ? 152 TRP B NE1 1 
ATOM 2911 C CE2 . TRP B 1 152 ? 18.00886  17.28970  42.03409  1.000 53.64465  ? 152 TRP B CE2 1 
ATOM 2912 C CE3 . TRP B 1 152 ? 15.99846  15.95677  41.89758  1.000 57.25349  ? 152 TRP B CE3 1 
ATOM 2913 C CZ2 . TRP B 1 152 ? 17.40042  18.35876  41.38115  1.000 53.72894  ? 152 TRP B CZ2 1 
ATOM 2914 C CZ3 . TRP B 1 152 ? 15.39554  17.02010  41.24928  1.000 55.46567  ? 152 TRP B CZ3 1 
ATOM 2915 C CH2 . TRP B 1 152 ? 16.09596  18.20662  41.00243  1.000 54.12538  ? 152 TRP B CH2 1 
ATOM 2916 N N   . ASN B 1 153 ? 18.74371  15.32520  46.48605  1.000 61.60762  ? 153 ASN B N   1 
ATOM 2917 C CA  . ASN B 1 153 ? 19.79388  15.71312  47.42123  1.000 62.46672  ? 153 ASN B CA  1 
ATOM 2918 C C   . ASN B 1 153 ? 19.48752  15.32059  48.85564  1.000 62.66867  ? 153 ASN B C   1 
ATOM 2919 O O   . ASN B 1 153 ? 20.24607  15.68937  49.75969  1.000 62.32961  ? 153 ASN B O   1 
ATOM 2920 C CB  . ASN B 1 153 ? 20.04979  17.21095  47.38182  1.000 64.05987  ? 153 ASN B CB  1 
ATOM 2921 C CG  . ASN B 1 153 ? 20.59187  17.66449  46.07496  1.000 64.55375  ? 153 ASN B CG  1 
ATOM 2922 O OD1 . ASN B 1 153 ? 19.97052  18.47601  45.39457  1.000 64.68305  ? 153 ASN B OD1 1 
ATOM 2923 N ND2 . ASN B 1 153 ? 21.75089  17.13782  45.69784  1.000 64.96579  ? 153 ASN B ND2 1 
ATOM 2924 N N   . GLN B 1 154 ? 18.38505  14.61731  49.08879  1.000 57.66699  ? 154 GLN B N   1 
ATOM 2925 C CA  . GLN B 1 154 ? 18.14795  14.02110  50.38801  1.000 56.58256  ? 154 GLN B CA  1 
ATOM 2926 C C   . GLN B 1 154 ? 19.12683  12.88415  50.61133  1.000 56.58043  ? 154 GLN B C   1 
ATOM 2927 O O   . GLN B 1 154 ? 19.56960  12.23426  49.66705  1.000 63.44228  ? 154 GLN B O   1 
ATOM 2928 C CB  . GLN B 1 154 ? 16.72423  13.52148  50.47550  1.000 54.61383  ? 154 GLN B CB  1 
ATOM 2929 C CG  . GLN B 1 154 ? 15.70954  14.61211  50.42869  1.000 53.01217  ? 154 GLN B CG  1 
ATOM 2930 C CD  . GLN B 1 154 ? 14.31963  14.05096  50.33063  1.000 53.91680  ? 154 GLN B CD  1 
ATOM 2931 O OE1 . GLN B 1 154 ? 14.11934  12.82983  50.32657  1.000 50.63182  ? 154 GLN B OE1 1 
ATOM 2932 N NE2 . GLN B 1 154 ? 13.34674  14.93572  50.19142  1.000 58.78972  ? 154 GLN B NE2 1 
ATOM 2933 N N   . ARG B 1 155 ? 19.49847  12.67314  51.86755  1.000 55.43366  ? 155 ARG B N   1 
ATOM 2934 C CA  . ARG B 1 155 ? 20.54301  11.72360  52.20999  1.000 57.51944  ? 155 ARG B CA  1 
ATOM 2935 C C   . ARG B 1 155 ? 20.22247  11.03604  53.53154  1.000 60.69565  ? 155 ARG B C   1 
ATOM 2936 O O   . ARG B 1 155 ? 19.58589  11.61438  54.41985  1.000 60.02351  ? 155 ARG B O   1 
ATOM 2937 C CB  . ARG B 1 155 ? 21.91041  12.40600  52.29333  1.000 58.31743  ? 155 ARG B CB  1 
ATOM 2938 C CG  . ARG B 1 155 ? 22.45502  12.92838  50.96864  1.000 59.60561  ? 155 ARG B CG  1 
ATOM 2939 C CD  . ARG B 1 155 ? 22.84641  11.79704  50.01712  1.000 58.55837  ? 155 ARG B CD  1 
ATOM 2940 N NE  . ARG B 1 155 ? 23.49246  12.28518  48.80023  1.000 61.27656  ? 155 ARG B NE  1 
ATOM 2941 C CZ  . ARG B 1 155 ? 22.85765  12.61117  47.67971  1.000 60.04762  ? 155 ARG B CZ  1 
ATOM 2942 N NH1 . ARG B 1 155 ? 21.53817  12.54140  47.58224  1.000 55.46845  ? 155 ARG B NH1 1 
ATOM 2943 N NH2 . ARG B 1 155 ? 23.56674  13.02649  46.63519  1.000 61.34564  ? 155 ARG B NH2 1 
ATOM 2944 N N   . ASP B 1 156 ? 20.68258  9.79136   53.64472  1.000 57.13060  ? 156 ASP B N   1 
ATOM 2945 C CA  . ASP B 1 156 ? 20.38930  8.90396   54.75919  1.000 55.71934  ? 156 ASP B CA  1 
ATOM 2946 C C   . ASP B 1 156 ? 21.65645  8.65821   55.56209  1.000 58.36077  ? 156 ASP B C   1 
ATOM 2947 O O   . ASP B 1 156 ? 22.69362  8.31579   54.98971  1.000 61.81531  ? 156 ASP B O   1 
ATOM 2948 C CB  . ASP B 1 156 ? 19.82091  7.58168   54.24546  1.000 57.32092  ? 156 ASP B CB  1 
ATOM 2949 C CG  . ASP B 1 156 ? 19.64728  6.54873   55.34757  1.000 60.63253  ? 156 ASP B CG  1 
ATOM 2950 O OD1 . ASP B 1 156 ? 18.70654  6.68074   56.17578  1.000 60.47227  ? 156 ASP B OD1 1 
ATOM 2951 O OD2 . ASP B 1 156 ? 20.47671  5.60526   55.37768  1.000 59.13141  ? 156 ASP B OD2 1 
ATOM 2952 N N   . ILE B 1 157 ? 21.57191  8.81408   56.88447  1.000 57.09076  ? 157 ILE B N   1 
ATOM 2953 C CA  . ILE B 1 157 ? 22.78450  8.79738   57.69138  1.000 59.55953  ? 157 ILE B CA  1 
ATOM 2954 C C   . ILE B 1 157 ? 23.29609  7.37897   57.90373  1.000 60.92589  ? 157 ILE B C   1 
ATOM 2955 O O   . ILE B 1 157 ? 24.50452  7.13051   57.83424  1.000 63.44711  ? 157 ILE B O   1 
ATOM 2956 C CB  . ILE B 1 157 ? 22.54850  9.54949   59.00811  1.000 62.07002  ? 157 ILE B CB  1 
ATOM 2957 C CG1 . ILE B 1 157 ? 22.38463  11.03449  58.68736  1.000 60.01201  ? 157 ILE B CG1 1 
ATOM 2958 C CG2 . ILE B 1 157 ? 23.70511  9.34348   59.95424  1.000 64.64944  ? 157 ILE B CG2 1 
ATOM 2959 C CD1 . ILE B 1 157 ? 21.89472  11.85768  59.79516  1.000 61.23330  ? 157 ILE B CD1 1 
ATOM 2960 N N   . ARG B 1 158 ? 22.40682  6.41739   58.13534  1.000 61.33815  ? 158 ARG B N   1 
ATOM 2961 C CA  . ARG B 1 158 ? 22.86721  5.03883   58.29411  1.000 63.55097  ? 158 ARG B CA  1 
ATOM 2962 C C   . ARG B 1 158 ? 23.62501  4.56192   57.05379  1.000 62.55307  ? 158 ARG B C   1 
ATOM 2963 O O   . ARG B 1 158 ? 24.72339  4.00478   57.16521  1.000 65.47002  ? 158 ARG B O   1 
ATOM 2964 C CB  . ARG B 1 158 ? 21.69394  4.10355   58.57835  1.000 61.07871  ? 158 ARG B CB  1 
ATOM 2965 C CG  . ARG B 1 158 ? 20.94801  4.35300   59.82569  1.000 57.50087  ? 158 ARG B CG  1 
ATOM 2966 C CD  . ARG B 1 158 ? 19.89114  3.30839   59.92794  1.000 59.67755  ? 158 ARG B CD  1 
ATOM 2967 N NE  . ARG B 1 158 ? 19.01194  3.52499   61.06672  1.000 66.68918  ? 158 ARG B NE  1 
ATOM 2968 C CZ  . ARG B 1 158 ? 17.85728  4.18167   61.01901  1.000 67.39958  ? 158 ARG B CZ  1 
ATOM 2969 N NH1 . ARG B 1 158 ? 17.38722  4.69001   59.88345  1.000 67.07094  ? 158 ARG B NH1 1 
ATOM 2970 N NH2 . ARG B 1 158 ? 17.14841  4.32350   62.13699  1.000 70.58704  ? 158 ARG B NH2 1 
ATOM 2971 N N   . THR B 1 159 ? 23.05410  4.77176   55.86166  1.000 59.15478  ? 159 THR B N   1 
ATOM 2972 C CA  . THR B 1 159 ? 23.75118  4.40553   54.62641  1.000 61.80941  ? 159 THR B CA  1 
ATOM 2973 C C   . THR B 1 159 ? 25.13190  5.04508   54.55453  1.000 62.58298  ? 159 THR B C   1 
ATOM 2974 O O   . THR B 1 159 ? 26.12666  4.37800   54.24499  1.000 61.51245  ? 159 THR B O   1 
ATOM 2975 C CB  . THR B 1 159 ? 22.94540  4.84113   53.40918  1.000 57.61960  ? 159 THR B CB  1 
ATOM 2976 O OG1 . THR B 1 159 ? 21.63553  4.27135   53.45719  1.000 56.19068  ? 159 THR B OG1 1 
ATOM 2977 C CG2 . THR B 1 159 ? 23.63956  4.38202   52.17229  1.000 55.60678  ? 159 THR B CG2 1 
ATOM 2978 N N   . ARG B 1 160 ? 25.19901  6.34859   54.83686  1.000 61.37626  ? 160 ARG B N   1 
ATOM 2979 C CA  . ARG B 1 160 ? 26.43714  7.10384   54.69972  1.000 62.88193  ? 160 ARG B CA  1 
ATOM 2980 C C   . ARG B 1 160 ? 27.52783  6.55666   55.60668  1.000 66.36558  ? 160 ARG B C   1 
ATOM 2981 O O   . ARG B 1 160 ? 28.65325  6.31776   55.16167  1.000 67.95144  ? 160 ARG B O   1 
ATOM 2982 C CB  . ARG B 1 160 ? 26.17185  8.57034   55.02255  1.000 63.52170  ? 160 ARG B CB  1 
ATOM 2983 C CG  . ARG B 1 160 ? 27.38401  9.47557   55.03293  1.000 61.91232  ? 160 ARG B CG  1 
ATOM 2984 C CD  . ARG B 1 160 ? 27.81499  9.82055   53.66229  1.000 62.71888  ? 160 ARG B CD  1 
ATOM 2985 N NE  . ARG B 1 160 ? 28.87519  10.82008  53.67644  1.000 67.34141  ? 160 ARG B NE  1 
ATOM 2986 C CZ  . ARG B 1 160 ? 29.45658  11.30469  52.58592  1.000 66.82192  ? 160 ARG B CZ  1 
ATOM 2987 N NH1 . ARG B 1 160 ? 29.05925  10.94814  51.37562  1.000 66.28066  ? 160 ARG B NH1 1 
ATOM 2988 N NH2 . ARG B 1 160 ? 30.45027  12.17855  52.71279  1.000 68.93949  ? 160 ARG B NH2 1 
ATOM 2989 N N   . ILE B 1 161 ? 27.22827  6.37155   56.89420  1.000 67.58722  ? 161 ILE B N   1 
ATOM 2990 C CA  . ILE B 1 161 ? 28.29528  5.95792   57.80139  1.000 71.93459  ? 161 ILE B CA  1 
ATOM 2991 C C   . ILE B 1 161 ? 28.72965  4.52328   57.51499  1.000 73.99252  ? 161 ILE B C   1 
ATOM 2992 O O   . ILE B 1 161 ? 29.92426  4.19969   57.57614  1.000 73.53736  ? 161 ILE B O   1 
ATOM 2993 C CB  . ILE B 1 161 ? 27.89326  6.15588   59.26839  1.000 68.14433  ? 161 ILE B CB  1 
ATOM 2994 C CG1 . ILE B 1 161 ? 27.84220  7.65226   59.59199  1.000 70.88606  ? 161 ILE B CG1 1 
ATOM 2995 C CG2 . ILE B 1 161 ? 28.90294  5.47106   60.15940  1.000 75.63016  ? 161 ILE B CG2 1 
ATOM 2996 C CD1 . ILE B 1 161 ? 27.29182  7.98420   60.99214  1.000 75.41079  ? 161 ILE B CD1 1 
ATOM 2997 N N   . GLU B 1 162 ? 27.77675  3.64754   57.18445  1.000 72.05614  ? 162 GLU B N   1 
ATOM 2998 C CA  . GLU B 1 162 ? 28.12235  2.28799   56.79062  1.000 69.18298  ? 162 GLU B CA  1 
ATOM 2999 C C   . GLU B 1 162 ? 29.03871  2.30673   55.56624  1.000 72.54456  ? 162 GLU B C   1 
ATOM 3000 O O   . GLU B 1 162 ? 30.09039  1.65126   55.55075  1.000 72.60059  ? 162 GLU B O   1 
ATOM 3001 C CB  . GLU B 1 162 ? 26.83957  1.50472   56.50477  1.000 67.36793  ? 162 GLU B CB  1 
ATOM 3002 C CG  . GLU B 1 162 ? 26.95466  -0.01093  56.56127  1.000 69.61372  ? 162 GLU B CG  1 
ATOM 3003 C CD  . GLU B 1 162 ? 25.68751  -0.73079  56.10077  1.000 69.71737  ? 162 GLU B CD  1 
ATOM 3004 O OE1 . GLU B 1 162 ? 24.87482  -0.13320  55.34932  1.000 65.67987  ? 162 GLU B OE1 1 
ATOM 3005 O OE2 . GLU B 1 162 ? 25.46461  -1.87623  56.56092  1.000 72.13777  ? 162 GLU B OE2 1 
ATOM 3006 N N   . ALA B 1 163 ? 28.67107  3.09341   54.54083  1.000 70.47561  ? 163 ALA B N   1 
ATOM 3007 C CA  . ALA B 1 163 ? 29.49528  3.19433   53.33741  1.000 67.64346  ? 163 ALA B CA  1 
ATOM 3008 C C   . ALA B 1 163 ? 30.85725  3.80799   53.63505  1.000 70.36875  ? 163 ALA B C   1 
ATOM 3009 O O   . ALA B 1 163 ? 31.88454  3.29388   53.18375  1.000 76.36769  ? 163 ALA B O   1 
ATOM 3010 C CB  . ALA B 1 163 ? 28.77396  4.01029   52.27139  1.000 65.37831  ? 163 ALA B CB  1 
ATOM 3011 N N   . LEU B 1 164 ? 30.88952  4.89489   54.40819  1.000 70.95759  ? 164 LEU B N   1 
ATOM 3012 C CA  . LEU B 1 164 ? 32.15994  5.51375   54.79081  1.000 74.53024  ? 164 LEU B CA  1 
ATOM 3013 C C   . LEU B 1 164 ? 33.05573  4.54770   55.56974  1.000 77.09855  ? 164 LEU B C   1 
ATOM 3014 O O   . LEU B 1 164 ? 34.28693  4.58114   55.43837  1.000 78.84558  ? 164 LEU B O   1 
ATOM 3015 C CB  . LEU B 1 164 ? 31.89586  6.77838   55.61614  1.000 74.64263  ? 164 LEU B CB  1 
ATOM 3016 C CG  . LEU B 1 164 ? 31.31265  7.95674   54.83560  1.000 72.83137  ? 164 LEU B CG  1 
ATOM 3017 C CD1 . LEU B 1 164 ? 30.88004  9.06655   55.74903  1.000 73.84248  ? 164 LEU B CD1 1 
ATOM 3018 C CD2 . LEU B 1 164 ? 32.33773  8.46414   53.85131  1.000 74.77613  ? 164 LEU B CD2 1 
ATOM 3019 N N   . LEU B 1 165 ? 32.45982  3.68944   56.39419  1.000 79.00030  ? 165 LEU B N   1 
ATOM 3020 C CA  . LEU B 1 165 ? 33.20029  2.81110   57.29273  1.000 78.58179  ? 165 LEU B CA  1 
ATOM 3021 C C   . LEU B 1 165 ? 33.27504  1.37031   56.81015  1.000 80.18492  ? 165 LEU B C   1 
ATOM 3022 O O   . LEU B 1 165 ? 33.99621  0.57286   57.42561  1.000 83.02016  ? 165 LEU B O   1 
ATOM 3023 C CB  . LEU B 1 165 ? 32.57451  2.86202   58.69447  1.000 79.02027  ? 165 LEU B CB  1 
ATOM 3024 C CG  . LEU B 1 165 ? 33.15414  3.90079   59.64854  1.000 79.79279  ? 165 LEU B CG  1 
ATOM 3025 C CD1 . LEU B 1 165 ? 33.19546  5.25034   59.00206  1.000 83.58792  ? 165 LEU B CD1 1 
ATOM 3026 C CD2 . LEU B 1 165 ? 32.24474  3.97529   60.85500  1.000 85.59412  ? 165 LEU B CD2 1 
ATOM 3027 N N   . LEU B 1 166 ? 32.54916  1.02243   55.74122  1.000 74.39897  ? 166 LEU B N   1 
ATOM 3028 C CA  . LEU B 1 166 ? 32.68784  -0.27062  55.05637  1.000 77.14288  ? 166 LEU B CA  1 
ATOM 3029 C C   . LEU B 1 166 ? 32.54840  -1.44992  56.02020  1.000 79.55590  ? 166 LEU B C   1 
ATOM 3030 O O   . LEU B 1 166 ? 33.24648  -2.46239  55.90963  1.000 81.83266  ? 166 LEU B O   1 
ATOM 3031 C CB  . LEU B 1 166 ? 34.00782  -0.34268  54.28593  1.000 73.56264  ? 166 LEU B CB  1 
ATOM 3032 C CG  . LEU B 1 166 ? 34.10421  0.60085   53.08320  1.000 72.72834  ? 166 LEU B CG  1 
ATOM 3033 C CD1 . LEU B 1 166 ? 35.46013  0.48569   52.43627  1.000 73.02850  ? 166 LEU B CD1 1 
ATOM 3034 C CD2 . LEU B 1 166 ? 33.01610  0.30555   52.07848  1.000 69.14566  ? 166 LEU B CD2 1 
ATOM 3035 N N   . VAL B 1 167 ? 31.63042  -1.31474  56.97628  1.000 80.05280  ? 167 VAL B N   1 
ATOM 3036 C CA  . VAL B 1 167 ? 31.27013  -2.38285  57.90086  1.000 78.99856  ? 167 VAL B CA  1 
ATOM 3037 C C   . VAL B 1 167 ? 29.76167  -2.53338  57.86731  1.000 77.40591  ? 167 VAL B C   1 
ATOM 3038 O O   . VAL B 1 167 ? 29.04332  -1.58634  58.19473  1.000 78.15583  ? 167 VAL B O   1 
ATOM 3039 C CB  . VAL B 1 167 ? 31.74314  -2.09754  59.33323  1.000 80.56900  ? 167 VAL B CB  1 
ATOM 3040 C CG1 . VAL B 1 167 ? 31.17201  -3.13259  60.28682  1.000 78.37068  ? 167 VAL B CG1 1 
ATOM 3041 C CG2 . VAL B 1 167 ? 33.25697  -2.08036  59.37847  1.000 78.54684  ? 167 VAL B CG2 1 
ATOM 3042 N N   . ARG B 1 168 ? 29.28552  -3.72149  57.49053  1.000 78.03173  ? 168 ARG B N   1 
ATOM 3043 C CA  . ARG B 1 168 ? 27.85298  -3.98732  57.44197  1.000 75.75955  ? 168 ARG B CA  1 
ATOM 3044 C C   . ARG B 1 168 ? 27.22424  -3.66694  58.79433  1.000 78.42192  ? 168 ARG B C   1 
ATOM 3045 O O   . ARG B 1 168 ? 27.77519  -4.00939  59.84798  1.000 77.85966  ? 168 ARG B O   1 
ATOM 3046 C CB  . ARG B 1 168 ? 27.59758  -5.45613  57.10361  1.000 74.32179  ? 168 ARG B CB  1 
ATOM 3047 C CG  . ARG B 1 168 ? 26.17628  -5.78565  56.67859  1.000 69.60811  ? 168 ARG B CG  1 
ATOM 3048 C CD  . ARG B 1 168 ? 26.04502  -5.56986  55.18732  1.000 71.93783  ? 168 ARG B CD  1 
ATOM 3049 N NE  . ARG B 1 168 ? 24.68530  -5.72817  54.68420  1.000 70.49474  ? 168 ARG B NE  1 
ATOM 3050 C CZ  . ARG B 1 168 ? 24.09021  -6.89487  54.50104  1.000 66.83081  ? 168 ARG B CZ  1 
ATOM 3051 N NH1 . ARG B 1 168 ? 24.62048  -8.01382  54.95939  1.000 69.12447  ? 168 ARG B NH1 1 
ATOM 3052 N NH2 . ARG B 1 168 ? 22.93001  -6.93608  53.85568  1.000 64.47230  ? 168 ARG B NH2 1 
ATOM 3053 N N   . ASP B 1 169 ? 26.06666  -3.00320  58.75385  1.000 77.70881  ? 169 ASP B N   1 
ATOM 3054 C CA  . ASP B 1 169 ? 25.36237  -2.54088  59.95352  1.000 78.46753  ? 169 ASP B CA  1 
ATOM 3055 C C   . ASP B 1 169 ? 26.31235  -1.83084  60.91738  1.000 80.91608  ? 169 ASP B C   1 
ATOM 3056 O O   . ASP B 1 169 ? 26.43739  -2.19113  62.08514  1.000 84.84739  ? 169 ASP B O   1 
ATOM 3057 C CB  . ASP B 1 169 ? 24.63447  -3.69472  60.64695  1.000 75.95248  ? 169 ASP B CB  1 
ATOM 3058 N N   . MET B 1 170 ? 27.01294  -0.82545  60.40348  1.000 89.22598  ? 170 MET B N   1 
ATOM 3059 C CA  . MET B 1 170 ? 27.84554  0.08510   61.19174  1.000 89.96038  ? 170 MET B CA  1 
ATOM 3060 C C   . MET B 1 170 ? 27.29115  1.48633   60.95676  1.000 88.93095  ? 170 MET B C   1 
ATOM 3061 O O   . MET B 1 170 ? 27.73077  2.18579   60.03965  1.000 86.86706  ? 170 MET B O   1 
ATOM 3062 C CB  . MET B 1 170 ? 29.31588  -0.00257  60.78848  1.000 90.64739  ? 170 MET B CB  1 
ATOM 3063 C CG  . MET B 1 170 ? 30.25120  0.97277   61.50909  1.000 96.51457  ? 170 MET B CG  1 
ATOM 3064 S SD  . MET B 1 170 ? 30.77699  0.59284   63.19307  1.000 109.19134 ? 170 MET B SD  1 
ATOM 3065 C CE  . MET B 1 170 ? 32.06580  -0.60219  62.83404  1.000 99.71802  ? 170 MET B CE  1 
ATOM 3066 N N   . THR B 1 171 ? 26.32826  1.89130   61.79117  1.000 88.96698  ? 171 THR B N   1 
ATOM 3067 C CA  . THR B 1 171 ? 25.62910  3.16162   61.63048  1.000 84.35815  ? 171 THR B CA  1 
ATOM 3068 C C   . THR B 1 171 ? 26.00419  4.20032   62.68796  1.000 86.95379  ? 171 THR B C   1 
ATOM 3069 O O   . THR B 1 171 ? 25.36035  5.25379   62.76106  1.000 86.56209  ? 171 THR B O   1 
ATOM 3070 C CB  . THR B 1 171 ? 24.11147  2.93985   61.62881  1.000 84.50655  ? 171 THR B CB  1 
ATOM 3071 O OG1 . THR B 1 171 ? 23.67072  2.47130   62.91637  1.000 88.75234  ? 171 THR B OG1 1 
ATOM 3072 C CG2 . THR B 1 171 ? 23.72736  1.93477   60.54560  1.000 77.79562  ? 171 THR B CG2 1 
ATOM 3073 N N   . THR B 1 172 ? 27.01227  3.93714   63.51778  1.000 87.01269  ? 172 THR B N   1 
ATOM 3074 C CA  . THR B 1 172 ? 27.55437  4.96209   64.39879  1.000 88.18514  ? 172 THR B CA  1 
ATOM 3075 C C   . THR B 1 172 ? 29.07566  4.95292   64.29263  1.000 91.35270  ? 172 THR B C   1 
ATOM 3076 O O   . THR B 1 172 ? 29.69583  3.89527   64.12269  1.000 90.04322  ? 172 THR B O   1 
ATOM 3077 C CB  . THR B 1 172 ? 27.09954  4.77216   65.86467  1.000 85.31163  ? 172 THR B CB  1 
ATOM 3078 O OG1 . THR B 1 172 ? 27.65229  3.56977   66.40798  1.000 91.47265  ? 172 THR B OG1 1 
ATOM 3079 C CG2 . THR B 1 172 ? 25.59191  4.68655   65.93249  1.000 81.84435  ? 172 THR B CG2 1 
ATOM 3080 N N   . CYS B 1 173 ? 29.66946  6.14319   64.36597  1.000 89.08301  ? 173 CYS B N   1 
ATOM 3081 C CA  . CYS B 1 173 ? 31.10427  6.30151   64.22193  1.000 92.91224  ? 173 CYS B CA  1 
ATOM 3082 C C   . CYS B 1 173 ? 31.74701  6.55954   65.56815  1.000 98.58316  ? 173 CYS B C   1 
ATOM 3083 O O   . CYS B 1 173 ? 31.32698  7.48559   66.27339  1.000 101.70269 ? 173 CYS B O   1 
ATOM 3084 C CB  . CYS B 1 173 ? 31.43397  7.45713   63.27503  1.000 91.07893  ? 173 CYS B CB  1 
ATOM 3085 S SG  . CYS B 1 173 ? 33.20981  7.74119   63.12368  1.000 87.19972  ? 173 CYS B SG  1 
ATOM 3086 N N   . PRO B 1 174 ? 32.75167  5.78043   65.96190  1.000 107.61319 ? 174 PRO B N   1 
ATOM 3087 C CA  . PRO B 1 174 ? 33.51893  6.13145   67.16374  1.000 107.54783 ? 174 PRO B CA  1 
ATOM 3088 C C   . PRO B 1 174 ? 34.21684  7.46756   66.96763  1.000 108.79394 ? 174 PRO B C   1 
ATOM 3089 O O   . PRO B 1 174 ? 34.72172  7.77376   65.88369  1.000 110.50227 ? 174 PRO B O   1 
ATOM 3090 C CB  . PRO B 1 174 ? 34.52781  4.98560   67.29693  1.000 108.17193 ? 174 PRO B CB  1 
ATOM 3091 C CG  . PRO B 1 174 ? 33.94189  3.86228   66.48353  1.000 110.77851 ? 174 PRO B CG  1 
ATOM 3092 C CD  . PRO B 1 174 ? 33.21320  4.52355   65.34987  1.000 104.99882 ? 174 PRO B CD  1 
ATOM 3093 N N   . LEU B 1 175 ? 34.24708  8.25732   68.02626  1.000 109.66870 ? 175 LEU B N   1 
ATOM 3094 C CA  . LEU B 1 175 ? 34.79666  9.60108   68.02543  1.000 109.11797 ? 175 LEU B CA  1 
ATOM 3095 C C   . LEU B 1 175 ? 36.05044  9.64928   68.89426  1.000 113.27934 ? 175 LEU B C   1 
ATOM 3096 O O   . LEU B 1 175 ? 36.41016  8.66109   69.53712  1.000 116.33093 ? 175 LEU B O   1 
ATOM 3097 C CB  . LEU B 1 175 ? 33.74500  10.59078  68.54432  1.000 105.66511 ? 175 LEU B CB  1 
ATOM 3098 C CG  . LEU B 1 175 ? 32.44469  10.60142  67.73567  1.000 101.14352 ? 175 LEU B CG  1 
ATOM 3099 C CD1 . LEU B 1 175 ? 31.42764  11.56312  68.32783  1.000 94.87160  ? 175 LEU B CD1 1 
ATOM 3100 C CD2 . LEU B 1 175 ? 32.70791  10.91588  66.27864  1.000 96.74945  ? 175 LEU B CD2 1 
ATOM 3101 N N   . PRO B 1 176 ? 36.77605  10.76946  68.89003  1.000 111.35889 ? 176 PRO B N   1 
ATOM 3102 C CA  . PRO B 1 176 ? 37.81082  10.97447  69.91731  1.000 113.98532 ? 176 PRO B CA  1 
ATOM 3103 C C   . PRO B 1 176 ? 37.23650  11.28104  71.30584  1.000 111.71033 ? 176 PRO B C   1 
ATOM 3104 O O   . PRO B 1 176 ? 36.11421  11.77341  71.45510  1.000 108.65164 ? 176 PRO B O   1 
ATOM 3105 C CB  . PRO B 1 176 ? 38.62904  12.14867  69.36208  1.000 110.95707 ? 176 PRO B CB  1 
ATOM 3106 C CG  . PRO B 1 176 ? 37.74216  12.80621  68.35345  1.000 108.57148 ? 176 PRO B CG  1 
ATOM 3107 C CD  . PRO B 1 176 ? 36.91225  11.71776  67.77172  1.000 106.20255 ? 176 PRO B CD  1 
ATOM 3108 N N   . LYS B 1 177 ? 38.03706  10.97213  72.33157  1.000 113.22886 ? 177 LYS B N   1 
ATOM 3109 C CA  . LYS B 1 177 ? 37.56833  11.01797  73.71460  1.000 114.14614 ? 177 LYS B CA  1 
ATOM 3110 C C   . LYS B 1 177 ? 37.22530  12.43627  74.14038  1.000 110.30679 ? 177 LYS B C   1 
ATOM 3111 O O   . LYS B 1 177 ? 37.98895  13.37414  73.90364  1.000 108.73758 ? 177 LYS B O   1 
ATOM 3112 C CB  . LYS B 1 177 ? 38.63035  10.44691  74.65959  1.000 114.00283 ? 177 LYS B CB  1 
ATOM 3113 N N   . GLY B 1 178 ? 36.07728  12.58820  74.79072  1.000 109.27838 ? 178 GLY B N   1 
ATOM 3114 C CA  . GLY B 1 178 ? 35.71271  13.85494  75.37358  1.000 110.65279 ? 178 GLY B CA  1 
ATOM 3115 C C   . GLY B 1 178 ? 35.08500  14.85029  74.42877  1.000 109.42361 ? 178 GLY B C   1 
ATOM 3116 O O   . GLY B 1 178 ? 34.66598  15.92068  74.87729  1.000 111.86515 ? 178 GLY B O   1 
ATOM 3117 N N   . THR B 1 179 ? 35.01220  14.56151  73.13380  1.000 113.99375 ? 179 THR B N   1 
ATOM 3118 C CA  . THR B 1 179 ? 34.16763  15.40472  72.30464  1.000 113.52923 ? 179 THR B CA  1 
ATOM 3119 C C   . THR B 1 179 ? 32.70401  15.20591  72.63962  1.000 113.05354 ? 179 THR B C   1 
ATOM 3120 O O   . THR B 1 179 ? 31.89255  16.10260  72.38835  1.000 112.65391 ? 179 THR B O   1 
ATOM 3121 C CB  . THR B 1 179 ? 34.38989  15.13809  70.82337  1.000 114.04552 ? 179 THR B CB  1 
ATOM 3122 O OG1 . THR B 1 179 ? 33.62210  16.08694  70.07676  1.000 113.66067 ? 179 THR B OG1 1 
ATOM 3123 C CG2 . THR B 1 179 ? 33.94231  13.73333  70.45575  1.000 113.28902 ? 179 THR B CG2 1 
ATOM 3124 N N   . LEU B 1 180 ? 32.35896  14.05935  73.22432  1.000 109.19343 ? 180 LEU B N   1 
ATOM 3125 C CA  . LEU B 1 180 ? 31.01793  13.85368  73.74096  1.000 107.18265 ? 180 LEU B CA  1 
ATOM 3126 C C   . LEU B 1 180 ? 30.71063  14.75744  74.92600  1.000 104.74450 ? 180 LEU B C   1 
ATOM 3127 O O   . LEU B 1 180 ? 29.54136  14.86229  75.30864  1.000 99.51179  ? 180 LEU B O   1 
ATOM 3128 C CB  . LEU B 1 180 ? 30.84804  12.38726  74.14280  1.000 108.22779 ? 180 LEU B CB  1 
ATOM 3129 N N   . ASP B 1 181 ? 31.72660  15.41262  75.49722  1.000 108.13609 ? 181 ASP B N   1 
ATOM 3130 C CA  . ASP B 1 181 ? 31.56345  16.15078  76.74265  1.000 101.11381 ? 181 ASP B CA  1 
ATOM 3131 C C   . ASP B 1 181 ? 30.50946  17.23713  76.58665  1.000 99.75055  ? 181 ASP B C   1 
ATOM 3132 O O   . ASP B 1 181 ? 30.54059  18.01986  75.63305  1.000 96.06021  ? 181 ASP B O   1 
ATOM 3133 C CB  . ASP B 1 181 ? 32.89783  16.76377  77.18165  1.000 96.97983  ? 181 ASP B CB  1 
ATOM 3134 N N   . GLY B 1 182 ? 29.59002  17.29174  77.55530  1.000 100.18438 ? 182 GLY B N   1 
ATOM 3135 C CA  . GLY B 1 182 ? 28.43778  18.16353  77.52634  1.000 97.66386  ? 182 GLY B CA  1 
ATOM 3136 C C   . GLY B 1 182 ? 27.16918  17.50121  77.04013  1.000 98.31053  ? 182 GLY B C   1 
ATOM 3137 O O   . GLY B 1 182 ? 26.10160  18.12495  77.09639  1.000 98.16537  ? 182 GLY B O   1 
ATOM 3138 N N   . PHE B 1 183 ? 27.25088  16.25600  76.58210  1.000 94.54734  ? 183 PHE B N   1 
ATOM 3139 C CA  . PHE B 1 183 ? 26.10445  15.60339  75.96552  1.000 93.82233  ? 183 PHE B CA  1 
ATOM 3140 C C   . PHE B 1 183 ? 25.02780  15.30912  77.00663  1.000 92.31572  ? 183 PHE B C   1 
ATOM 3141 O O   . PHE B 1 183 ? 25.32600  14.83970  78.10814  1.000 96.66843  ? 183 PHE B O   1 
ATOM 3142 C CB  . PHE B 1 183 ? 26.55450  14.31308  75.27983  1.000 93.83405  ? 183 PHE B CB  1 
ATOM 3143 C CG  . PHE B 1 183 ? 25.50557  13.69251  74.42248  1.000 92.00056  ? 183 PHE B CG  1 
ATOM 3144 C CD1 . PHE B 1 183 ? 25.23998  14.19657  73.16191  1.000 90.24428  ? 183 PHE B CD1 1 
ATOM 3145 C CD2 . PHE B 1 183 ? 24.76417  12.62310  74.88175  1.000 93.28367  ? 183 PHE B CD2 1 
ATOM 3146 C CE1 . PHE B 1 183 ? 24.26245  13.63088  72.37564  1.000 89.81670  ? 183 PHE B CE1 1 
ATOM 3147 C CE2 . PHE B 1 183 ? 23.78244  12.05242  74.09677  1.000 92.51654  ? 183 PHE B CE2 1 
ATOM 3148 C CZ  . PHE B 1 183 ? 23.52911  12.55730  72.84799  1.000 91.32525  ? 183 PHE B CZ  1 
ATOM 3149 N N   . VAL B 1 184 ? 23.77653  15.59105  76.66642  1.000 94.12190  ? 184 VAL B N   1 
ATOM 3150 C CA  . VAL B 1 184 ? 22.64978  15.23943  77.52032  1.000 96.11038  ? 184 VAL B CA  1 
ATOM 3151 C C   . VAL B 1 184 ? 21.74719  14.30617  76.72708  1.000 97.00511  ? 184 VAL B C   1 
ATOM 3152 O O   . VAL B 1 184 ? 21.73444  14.33154  75.49615  1.000 97.39908  ? 184 VAL B O   1 
ATOM 3153 C CB  . VAL B 1 184 ? 21.87742  16.47695  78.02908  1.000 91.81949  ? 184 VAL B CB  1 
ATOM 3154 N N   . ALA B 1 185 ? 20.97754  13.48752  77.44124  1.000 103.80886 ? 185 ALA B N   1 
ATOM 3155 C CA  . ALA B 1 185 ? 20.47205  12.24631  76.86122  1.000 105.20739 ? 185 ALA B CA  1 
ATOM 3156 C C   . ALA B 1 185 ? 19.37137  12.48516  75.83514  1.000 106.57936 ? 185 ALA B C   1 
ATOM 3157 O O   . ALA B 1 185 ? 19.55322  12.20684  74.64408  1.000 108.66358 ? 185 ALA B O   1 
ATOM 3158 C CB  . ALA B 1 185 ? 19.98276  11.31361  77.97012  1.000 107.37267 ? 185 ALA B CB  1 
ATOM 3159 N N   . HIS B 1 186 ? 18.21962  12.99101  76.26402  1.000 101.90392 ? 186 HIS B N   1 
ATOM 3160 C CA  . HIS B 1 186 ? 17.04245  12.93410  75.40059  1.000 103.12389 ? 186 HIS B CA  1 
ATOM 3161 C C   . HIS B 1 186 ? 16.76803  14.26824  74.71956  1.000 97.25910  ? 186 HIS B C   1 
ATOM 3162 O O   . HIS B 1 186 ? 15.62258  14.69534  74.56512  1.000 97.01547  ? 186 HIS B O   1 
ATOM 3163 C CB  . HIS B 1 186 ? 15.82859  12.44370  76.18330  1.000 107.80829 ? 186 HIS B CB  1 
ATOM 3164 C CG  . HIS B 1 186 ? 16.01845  11.08424  76.79092  1.000 108.54505 ? 186 HIS B CG  1 
ATOM 3165 N ND1 . HIS B 1 186 ? 16.27111  10.90237  78.13467  1.000 108.37555 ? 186 HIS B ND1 1 
ATOM 3166 C CD2 . HIS B 1 186 ? 16.06895  9.85128   76.22969  1.000 105.41892 ? 186 HIS B CD2 1 
ATOM 3167 C CE1 . HIS B 1 186 ? 16.41669  9.61319   78.38320  1.000 105.60872 ? 186 HIS B CE1 1 
ATOM 3168 N NE2 . HIS B 1 186 ? 16.30595  8.95388   77.24338  1.000 106.65870 ? 186 HIS B NE2 1 
ATOM 3169 N N   . ASP B 1 187 ? 17.82864  14.93230  74.28589  1.000 95.63666  ? 187 ASP B N   1 
ATOM 3170 C CA  . ASP B 1 187 ? 17.74983  16.20115  73.58013  1.000 91.49569  ? 187 ASP B CA  1 
ATOM 3171 C C   . ASP B 1 187 ? 17.83132  15.95949  72.07004  1.000 93.23276  ? 187 ASP B C   1 
ATOM 3172 O O   . ASP B 1 187 ? 18.75542  15.28884  71.58855  1.000 90.52842  ? 187 ASP B O   1 
ATOM 3173 C CB  . ASP B 1 187 ? 18.88431  17.11326  74.05214  1.000 89.42099  ? 187 ASP B CB  1 
ATOM 3174 C CG  . ASP B 1 187 ? 18.75011  18.53293  73.54907  1.000 87.65274  ? 187 ASP B CG  1 
ATOM 3175 O OD1 . ASP B 1 187 ? 17.77538  18.83352  72.82364  1.000 86.20686  ? 187 ASP B OD1 1 
ATOM 3176 O OD2 . ASP B 1 187 ? 19.63458  19.34970  73.87838  1.000 87.88517  ? 187 ASP B OD2 1 
ATOM 3177 N N   . SER B 1 188 ? 16.85925  16.50476  71.32652  1.000 90.84482  ? 188 SER B N   1 
ATOM 3178 C CA  . SER B 1 188 ? 16.86962  16.36905  69.87156  1.000 83.54828  ? 188 SER B CA  1 
ATOM 3179 C C   . SER B 1 188 ? 18.06719  17.07157  69.25039  1.000 81.12114  ? 188 SER B C   1 
ATOM 3180 O O   . SER B 1 188 ? 18.65775  16.56080  68.29770  1.000 83.60727  ? 188 SER B O   1 
ATOM 3181 C CB  . SER B 1 188 ? 15.58096  16.92578  69.27026  1.000 80.73238  ? 188 SER B CB  1 
ATOM 3182 O OG  . SER B 1 188 ? 14.46039  16.16546  69.66027  1.000 79.57628  ? 188 SER B OG  1 
ATOM 3183 N N   . ILE B 1 189 ? 18.41417  18.26391  69.74079  1.000 79.43777  ? 189 ILE B N   1 
ATOM 3184 C CA  . ILE B 1 189 ? 19.54682  18.97813  69.16486  1.000 77.86218  ? 189 ILE B CA  1 
ATOM 3185 C C   . ILE B 1 189 ? 20.85446  18.28081  69.50268  1.000 83.70099  ? 189 ILE B C   1 
ATOM 3186 O O   . ILE B 1 189 ? 21.82526  18.37540  68.74616  1.000 85.55333  ? 189 ILE B O   1 
ATOM 3187 C CB  . ILE B 1 189 ? 19.55369  20.45015  69.61362  1.000 74.91661  ? 189 ILE B CB  1 
ATOM 3188 C CG1 . ILE B 1 189 ? 18.34396  21.17066  69.05983  1.000 72.33088  ? 189 ILE B CG1 1 
ATOM 3189 C CG2 . ILE B 1 189 ? 20.79705  21.18506  69.14487  1.000 74.04266  ? 189 ILE B CG2 1 
ATOM 3190 C CD1 . ILE B 1 189 ? 18.24780  22.57513  69.53306  1.000 71.81078  ? 189 ILE B CD1 1 
ATOM 3191 N N   . HIS B 1 190 ? 20.92325  17.57969  70.63304  1.000 83.07209  ? 190 HIS B N   1 
ATOM 3192 C CA  . HIS B 1 190 ? 22.13201  16.81374  70.91544  1.000 83.96268  ? 190 HIS B CA  1 
ATOM 3193 C C   . HIS B 1 190 ? 22.25116  15.61395  69.97734  1.000 87.30149  ? 190 HIS B C   1 
ATOM 3194 O O   . HIS B 1 190 ? 23.35905  15.26777  69.55313  1.000 89.02786  ? 190 HIS B O   1 
ATOM 3195 C CB  . HIS B 1 190 ? 22.16402  16.38077  72.38164  1.000 87.89673  ? 190 HIS B CB  1 
ATOM 3196 C CG  . HIS B 1 190 ? 22.39847  17.50751  73.35095  1.000 92.27731  ? 190 HIS B CG  1 
ATOM 3197 N ND1 . HIS B 1 190 ? 22.19923  17.37598  74.71137  1.000 92.04016  ? 190 HIS B ND1 1 
ATOM 3198 C CD2 . HIS B 1 190 ? 22.82768  18.77899  73.15979  1.000 90.99368  ? 190 HIS B CD2 1 
ATOM 3199 C CE1 . HIS B 1 190 ? 22.48975  18.51696  75.31263  1.000 88.76286  ? 190 HIS B CE1 1 
ATOM 3200 N NE2 . HIS B 1 190 ? 22.87169  19.38517  74.39446  1.000 87.37756  ? 190 HIS B NE2 1 
ATOM 3201 N N   . ASP B 1 191 ? 21.12549  14.97929  69.61910  1.000 97.97171  ? 191 ASP B N   1 
ATOM 3202 C CA  . ASP B 1 191 ? 21.15436  13.90634  68.61828  1.000 96.46602  ? 191 ASP B CA  1 
ATOM 3203 C C   . ASP B 1 191 ? 21.76960  14.37662  67.30949  1.000 94.83070  ? 191 ASP B C   1 
ATOM 3204 O O   . ASP B 1 191 ? 22.67585  13.73150  66.77065  1.000 94.52392  ? 191 ASP B O   1 
ATOM 3205 C CB  . ASP B 1 191 ? 19.74697  13.38083  68.34305  1.000 98.55773  ? 191 ASP B CB  1 
ATOM 3206 C CG  . ASP B 1 191 ? 19.23493  12.49818  69.43773  1.000 106.35347 ? 191 ASP B CG  1 
ATOM 3207 O OD1 . ASP B 1 191 ? 20.07076  11.83863  70.09386  1.000 108.67699 ? 191 ASP B OD1 1 
ATOM 3208 O OD2 . ASP B 1 191 ? 17.99901  12.45615  69.63308  1.000 111.28035 ? 191 ASP B OD2 1 
ATOM 3209 N N   . CYS B 1 192 ? 21.26772  15.49244  66.77237  1.000 81.54504  ? 192 CYS B N   1 
ATOM 3210 C CA  . CYS B 1 192 ? 21.73572  15.97261  65.48037  1.000 78.88787  ? 192 CYS B CA  1 
ATOM 3211 C C   . CYS B 1 192 ? 23.21636  16.30481  65.51536  1.000 79.40947  ? 192 CYS B C   1 
ATOM 3212 O O   . CYS B 1 192 ? 23.95790  15.96374  64.58305  1.000 76.20556  ? 192 CYS B O   1 
ATOM 3213 C CB  . CYS B 1 192 ? 20.92353  17.18677  65.05099  1.000 74.05976  ? 192 CYS B CB  1 
ATOM 3214 S SG  . CYS B 1 192 ? 19.21834  16.77576  64.66052  1.000 71.20462  ? 192 CYS B SG  1 
ATOM 3215 N N   . ALA B 1 193 ? 23.66844  16.96258  66.58634  1.000 79.21518  ? 193 ALA B N   1 
ATOM 3216 C CA  . ALA B 1 193 ? 25.08112  17.30077  66.68923  1.000 76.71968  ? 193 ALA B CA  1 
ATOM 3217 C C   . ALA B 1 193 ? 25.95539  16.05606  66.82261  1.000 78.38161  ? 193 ALA B C   1 
ATOM 3218 O O   . ALA B 1 193 ? 27.08937  16.05417  66.33554  1.000 79.98432  ? 193 ALA B O   1 
ATOM 3219 C CB  . ALA B 1 193 ? 25.31151  18.26200  67.85057  1.000 77.81019  ? 193 ALA B CB  1 
ATOM 3220 N N   . LYS B 1 194 ? 25.47343  14.99193  67.47018  1.000 77.77971  ? 194 LYS B N   1 
ATOM 3221 C CA  . LYS B 1 194 ? 26.23462  13.74679  67.43799  1.000 75.24856  ? 194 LYS B CA  1 
ATOM 3222 C C   . LYS B 1 194 ? 26.34085  13.21944  66.00999  1.000 81.04148  ? 194 LYS B C   1 
ATOM 3223 O O   . LYS B 1 194 ? 27.43834  12.90975  65.52729  1.000 80.61182  ? 194 LYS B O   1 
ATOM 3224 C CB  . LYS B 1 194 ? 25.59933  12.70229  68.35376  1.000 72.73611  ? 194 LYS B CB  1 
ATOM 3225 N N   . ASP B 1 195 ? 25.20373  13.14328  65.30543  1.000 77.44687  ? 195 ASP B N   1 
ATOM 3226 C CA  . ASP B 1 195 ? 25.18290  12.54047  63.97850  1.000 74.37247  ? 195 ASP B CA  1 
ATOM 3227 C C   . ASP B 1 195 ? 26.02902  13.30646  62.97136  1.000 77.78542  ? 195 ASP B C   1 
ATOM 3228 O O   . ASP B 1 195 ? 26.65715  12.68424  62.10253  1.000 73.80451  ? 195 ASP B O   1 
ATOM 3229 C CB  . ASP B 1 195 ? 23.75101  12.41935  63.48040  1.000 72.54160  ? 195 ASP B CB  1 
ATOM 3230 C CG  . ASP B 1 195 ? 23.07981  11.15630  63.96415  1.000 73.96682  ? 195 ASP B CG  1 
ATOM 3231 O OD1 . ASP B 1 195 ? 23.80278  10.16263  64.19940  1.000 72.58150  ? 195 ASP B OD1 1 
ATOM 3232 O OD2 . ASP B 1 195 ? 21.83539  11.14001  64.06896  1.000 76.13162  ? 195 ASP B OD2 1 
ATOM 3233 N N   . ILE B 1 196 ? 26.05364  14.64360  63.05914  1.000 76.74350  ? 196 ILE B N   1 
ATOM 3234 C CA  . ILE B 1 196 ? 26.93629  15.42768  62.19578  1.000 73.76023  ? 196 ILE B CA  1 
ATOM 3235 C C   . ILE B 1 196 ? 28.39843  15.14346  62.52238  1.000 77.96151  ? 196 ILE B C   1 
ATOM 3236 O O   . ILE B 1 196 ? 29.22973  14.98458  61.61903  1.000 79.32733  ? 196 ILE B O   1 
ATOM 3237 C CB  . ILE B 1 196 ? 26.64386  16.93251  62.31471  1.000 72.41727  ? 196 ILE B CB  1 
ATOM 3238 C CG1 . ILE B 1 196 ? 25.19365  17.26013  61.97936  1.000 71.08067  ? 196 ILE B CG1 1 
ATOM 3239 C CG2 . ILE B 1 196 ? 27.52108  17.68871  61.35390  1.000 70.36596  ? 196 ILE B CG2 1 
ATOM 3240 C CD1 . ILE B 1 196 ? 24.81891  18.68311  62.35149  1.000 66.45321  ? 196 ILE B CD1 1 
ATOM 3241 N N   . LEU B 1 197 ? 28.74747  15.10511  63.81278  1.000 78.65381  ? 197 LEU B N   1 
ATOM 3242 C CA  . LEU B 1 197 ? 30.12987  14.80783  64.17943  1.000 81.87384  ? 197 LEU B CA  1 
ATOM 3243 C C   . LEU B 1 197 ? 30.52928  13.41599  63.72806  1.000 80.75788  ? 197 LEU B C   1 
ATOM 3244 O O   . LEU B 1 197 ? 31.63932  13.21264  63.22968  1.000 82.88881  ? 197 LEU B O   1 
ATOM 3245 C CB  . LEU B 1 197 ? 30.33053  14.95673  65.68405  1.000 80.19943  ? 197 LEU B CB  1 
ATOM 3246 C CG  . LEU B 1 197 ? 30.28434  16.42367  66.08155  1.000 80.17386  ? 197 LEU B CG  1 
ATOM 3247 C CD1 . LEU B 1 197 ? 30.30051  16.61529  67.59996  1.000 82.67542  ? 197 LEU B CD1 1 
ATOM 3248 C CD2 . LEU B 1 197 ? 31.44395  17.12379  65.41968  1.000 77.08934  ? 197 LEU B CD2 1 
ATOM 3249 N N   . MET B 1 198 ? 29.63587  12.44663  63.89108  1.000 78.14613  ? 198 MET B N   1 
ATOM 3250 C CA  . MET B 1 198 ? 29.94619  11.09578  63.45503  1.000 82.22294  ? 198 MET B CA  1 
ATOM 3251 C C   . MET B 1 198 ? 30.16746  11.02309  61.95306  1.000 82.65200  ? 198 MET B C   1 
ATOM 3252 O O   . MET B 1 198 ? 31.07352  10.32045  61.49981  1.000 84.59306  ? 198 MET B O   1 
ATOM 3253 C CB  . MET B 1 198 ? 28.84221  10.14689  63.87199  1.000 83.20950  ? 198 MET B CB  1 
ATOM 3254 C CG  . MET B 1 198 ? 28.91654  9.74924   65.29292  1.000 80.70585  ? 198 MET B CG  1 
ATOM 3255 S SD  . MET B 1 198 ? 27.57724  8.60311   65.55117  1.000 80.18889  ? 198 MET B SD  1 
ATOM 3256 C CE  . MET B 1 198 ? 27.97030  8.07455   67.22139  1.000 92.06878  ? 198 MET B CE  1 
ATOM 3257 N N   . MET B 1 199 ? 29.34442  11.72684  61.16239  1.000 79.14929  ? 199 MET B N   1 
ATOM 3258 C CA  . MET B 1 199 ? 29.54852  11.74958  59.71147  1.000 78.01572  ? 199 MET B CA  1 
ATOM 3259 C C   . MET B 1 199 ? 30.87899  12.38826  59.32739  1.000 83.09779  ? 199 MET B C   1 
ATOM 3260 O O   . MET B 1 199 ? 31.57095  11.89283  58.42817  1.000 83.40432  ? 199 MET B O   1 
ATOM 3261 C CB  . MET B 1 199 ? 28.40426  12.48041  59.00262  1.000 72.98145  ? 199 MET B CB  1 
ATOM 3262 C CG  . MET B 1 199 ? 27.13310  11.66463  58.81932  1.000 74.90223  ? 199 MET B CG  1 
ATOM 3263 S SD  . MET B 1 199 ? 25.81739  12.46474  57.84716  1.000 70.00578  ? 199 MET B SD  1 
ATOM 3264 C CE  . MET B 1 199 ? 25.03897  13.59519  59.02363  1.000 71.06807  ? 199 MET B CE  1 
ATOM 3265 N N   . LYS B 1 200 ? 31.24009  13.50650  59.96780  1.000 89.04513  ? 200 LYS B N   1 
ATOM 3266 C CA  . LYS B 1 200 ? 32.47842  14.19282  59.60489  1.000 89.17184  ? 200 LYS B CA  1 
ATOM 3267 C C   . LYS B 1 200 ? 33.69143  13.31237  59.87778  1.000 91.61207  ? 200 LYS B C   1 
ATOM 3268 O O   . LYS B 1 200 ? 34.52110  13.08804  58.98707  1.000 93.54882  ? 200 LYS B O   1 
ATOM 3269 C CB  . LYS B 1 200 ? 32.59273  15.52149  60.34953  1.000 85.77667  ? 200 LYS B CB  1 
ATOM 3270 N N   . TYR B 1 201 ? 33.79426  12.77478  61.09742  1.000 89.01722  ? 201 TYR B N   1 
ATOM 3271 C CA  . TYR B 1 201 ? 34.89722  11.87091  61.41277  1.000 91.39454  ? 201 TYR B CA  1 
ATOM 3272 C C   . TYR B 1 201 ? 34.91766  10.66838  60.48235  1.000 91.85039  ? 201 TYR B C   1 
ATOM 3273 O O   . TYR B 1 201 ? 35.98258  10.27755  59.99126  1.000 93.94483  ? 201 TYR B O   1 
ATOM 3274 C CB  . TYR B 1 201 ? 34.81544  11.41607  62.86734  1.000 94.92472  ? 201 TYR B CB  1 
ATOM 3275 C CG  . TYR B 1 201 ? 35.29106  12.46139  63.83744  1.000 95.14374  ? 201 TYR B CG  1 
ATOM 3276 C CD1 . TYR B 1 201 ? 36.64802  12.64929  64.05936  1.000 99.38051  ? 201 TYR B CD1 1 
ATOM 3277 C CD2 . TYR B 1 201 ? 34.39563  13.27141  64.50898  1.000 90.86983  ? 201 TYR B CD2 1 
ATOM 3278 C CE1 . TYR B 1 201 ? 37.10175  13.60833  64.93889  1.000 104.02935 ? 201 TYR B CE1 1 
ATOM 3279 C CE2 . TYR B 1 201 ? 34.83197  14.22734  65.38769  1.000 99.63011  ? 201 TYR B CE2 1 
ATOM 3280 C CZ  . TYR B 1 201 ? 36.18899  14.39416  65.60590  1.000 105.06728 ? 201 TYR B CZ  1 
ATOM 3281 O OH  . TYR B 1 201 ? 36.62721  15.35184  66.49319  1.000 107.96099 ? 201 TYR B OH  1 
ATOM 3282 N N   . ALA B 1 202 ? 33.75243  10.06901  60.22950  1.000 94.17673  ? 202 ALA B N   1 
ATOM 3283 C CA  . ALA B 1 202 ? 33.66524  9.01130   59.23270  1.000 90.29575  ? 202 ALA B CA  1 
ATOM 3284 C C   . ALA B 1 202 ? 34.28982  9.46619   57.92436  1.000 91.91488  ? 202 ALA B C   1 
ATOM 3285 O O   . ALA B 1 202 ? 35.14300  8.77625   57.35259  1.000 89.68855  ? 202 ALA B O   1 
ATOM 3286 C CB  . ALA B 1 202 ? 32.20433  8.61666   59.02353  1.000 85.56435  ? 202 ALA B CB  1 
ATOM 3287 N N   . LEU B 1 203 ? 33.90462  10.65960  57.46141  1.000 91.81535  ? 203 LEU B N   1 
ATOM 3288 C CA  . LEU B 1 203 ? 34.45494  11.17538  56.21465  1.000 93.77660  ? 203 LEU B CA  1 
ATOM 3289 C C   . LEU B 1 203 ? 35.94210  11.47146  56.34840  1.000 95.91983  ? 203 LEU B C   1 
ATOM 3290 O O   . LEU B 1 203 ? 36.71990  11.16620  55.43595  1.000 98.30124  ? 203 LEU B O   1 
ATOM 3291 C CB  . LEU B 1 203 ? 33.69577  12.42368  55.76630  1.000 92.22961  ? 203 LEU B CB  1 
ATOM 3292 C CG  . LEU B 1 203 ? 34.12032  12.88195  54.36561  1.000 92.27249  ? 203 LEU B CG  1 
ATOM 3293 C CD1 . LEU B 1 203 ? 33.83182  11.78268  53.37913  1.000 87.65056  ? 203 LEU B CD1 1 
ATOM 3294 C CD2 . LEU B 1 203 ? 33.42011  14.16506  53.94016  1.000 91.61980  ? 203 LEU B CD2 1 
ATOM 3295 N N   . ARG B 1 204 ? 36.36027  12.07056  57.47015  1.000 94.12161  ? 204 ARG B N   1 
ATOM 3296 C CA  . ARG B 1 204 ? 37.78644  12.31273  57.66941  1.000 95.48790  ? 204 ARG B CA  1 
ATOM 3297 C C   . ARG B 1 204 ? 38.55085  10.99672  57.75479  1.000 98.69758  ? 204 ARG B C   1 
ATOM 3298 O O   . ARG B 1 204 ? 39.67388  10.88842  57.24731  1.000 103.33171 ? 204 ARG B O   1 
ATOM 3299 C CB  . ARG B 1 204 ? 38.02423  13.16578  58.91516  1.000 91.68120  ? 204 ARG B CB  1 
ATOM 3300 N N   . TYR B 1 205 ? 37.95183  9.97829   58.37749  1.000 95.90650  ? 205 TYR B N   1 
ATOM 3301 C CA  . TYR B 1 205 ? 38.61279  8.67938   58.47055  1.000 97.10875  ? 205 TYR B CA  1 
ATOM 3302 C C   . TYR B 1 205 ? 38.78110  8.04854   57.09606  1.000 92.87891  ? 205 TYR B C   1 
ATOM 3303 O O   . TYR B 1 205 ? 39.86317  7.56334   56.75131  1.000 95.25724  ? 205 TYR B O   1 
ATOM 3304 C CB  . TYR B 1 205 ? 37.82529  7.74213   59.38834  1.000 98.05253  ? 205 TYR B CB  1 
ATOM 3305 C CG  . TYR B 1 205 ? 37.81964  8.14185   60.84945  1.000 98.96199  ? 205 TYR B CG  1 
ATOM 3306 C CD1 . TYR B 1 205 ? 38.76292  9.02825   61.35952  1.000 102.94757 ? 205 TYR B CD1 1 
ATOM 3307 C CD2 . TYR B 1 205 ? 36.84397  7.65467   61.71115  1.000 99.82173  ? 205 TYR B CD2 1 
ATOM 3308 C CE1 . TYR B 1 205 ? 38.74473  9.40231   62.69506  1.000 105.60615 ? 205 TYR B CE1 1 
ATOM 3309 C CE2 . TYR B 1 205 ? 36.81402  8.02503   63.05010  1.000 104.53079 ? 205 TYR B CE2 1 
ATOM 3310 C CZ  . TYR B 1 205 ? 37.76549  8.89608   63.53315  1.000 105.99918 ? 205 TYR B CZ  1 
ATOM 3311 O OH  . TYR B 1 205 ? 37.72350  9.25470   64.85577  1.000 107.62767 ? 205 TYR B OH  1 
ATOM 3312 N N   . ALA B 1 206 ? 37.72211  8.05848   56.28932  1.000 95.47504  ? 206 ALA B N   1 
ATOM 3313 C CA  . ALA B 1 206 ? 37.74983  7.32915   55.02609  1.000 95.44184  ? 206 ALA B CA  1 
ATOM 3314 C C   . ALA B 1 206 ? 38.75256  7.89917   54.02789  1.000 98.59565  ? 206 ALA B C   1 
ATOM 3315 O O   . ALA B 1 206 ? 39.12686  7.19653   53.08203  1.000 95.20237  ? 206 ALA B O   1 
ATOM 3316 C CB  . ALA B 1 206 ? 36.35389  7.30543   54.40182  1.000 87.20743  ? 206 ALA B CB  1 
ATOM 3317 N N   . MET B 1 207 ? 39.20013  9.14391   54.21370  1.000 97.49222  ? 207 MET B N   1 
ATOM 3318 C CA  . MET B 1 207 ? 40.05560  9.80347   53.23307  1.000 101.10462 ? 207 MET B CA  1 
ATOM 3319 C C   . MET B 1 207 ? 41.54295  9.77899   53.57768  1.000 107.76910 ? 207 MET B C   1 
ATOM 3320 O O   . MET B 1 207 ? 42.36663  10.09285  52.70882  1.000 108.23063 ? 207 MET B O   1 
ATOM 3321 C CB  . MET B 1 207 ? 39.61059  11.25824  53.04220  1.000 101.43470 ? 207 MET B CB  1 
ATOM 3322 C CG  . MET B 1 207 ? 38.30605  11.42052  52.28780  1.000 95.50318  ? 207 MET B CG  1 
ATOM 3323 S SD  . MET B 1 207 ? 37.85665  13.15657  52.10565  1.000 97.10846  ? 207 MET B SD  1 
ATOM 3324 C CE  . MET B 1 207 ? 36.35509  13.03715  51.12817  1.000 89.53184  ? 207 MET B CE  1 
ATOM 3325 N N   . GLY B 1 208 ? 41.90857  9.42625   54.80060  1.000 110.38547 ? 208 GLY B N   1 
ATOM 3326 C CA  . GLY B 1 208 ? 43.28984  9.38922   55.20966  1.000 111.45322 ? 208 GLY B CA  1 
ATOM 3327 C C   . GLY B 1 208 ? 43.71256  10.51692  56.11493  1.000 111.46623 ? 208 GLY B C   1 
ATOM 3328 O O   . GLY B 1 208 ? 44.91941  10.76813  56.23014  1.000 116.58245 ? 208 GLY B O   1 
ATOM 3329 N N   . LEU B 1 209 ? 42.76688  11.19235  56.77143  1.000 111.36766 ? 209 LEU B N   1 
ATOM 3330 C CA  . LEU B 1 209 ? 43.03621  12.39461  57.55106  1.000 110.75926 ? 209 LEU B CA  1 
ATOM 3331 C C   . LEU B 1 209 ? 43.31289  12.10283  59.02453  1.000 114.13825 ? 209 LEU B C   1 
ATOM 3332 O O   . LEU B 1 209 ? 44.30829  12.59164  59.56792  1.000 119.85805 ? 209 LEU B O   1 
ATOM 3333 C CB  . LEU B 1 209 ? 41.85744  13.36698  57.42927  1.000 105.57131 ? 209 LEU B CB  1 
ATOM 3334 C CG  . LEU B 1 209 ? 41.56013  13.92957  56.03434  1.000 102.64889 ? 209 LEU B CG  1 
ATOM 3335 C CD1 . LEU B 1 209 ? 40.28288  14.75655  56.03315  1.000 98.79461  ? 209 LEU B CD1 1 
ATOM 3336 C CD2 . LEU B 1 209 ? 42.72459  14.75737  55.52767  1.000 100.10543 ? 209 LEU B CD2 1 
ATOM 3337 N N   . GLU B 1 210 ? 42.47535  11.30435  59.68675  1.000 112.53854 ? 210 GLU B N   1 
ATOM 3338 C CA  . GLU B 1 210 ? 42.57090  11.10825  61.12913  1.000 116.73358 ? 210 GLU B CA  1 
ATOM 3339 C C   . GLU B 1 210 ? 42.69082  9.62011   61.45775  1.000 121.82234 ? 210 GLU B C   1 
ATOM 3340 O O   . GLU B 1 210 ? 42.51866  8.75050   60.59674  1.000 117.18026 ? 210 GLU B O   1 
ATOM 3341 C CB  . GLU B 1 210 ? 41.36418  11.72708  61.85490  1.000 113.76816 ? 210 GLU B CB  1 
ATOM 3342 N N   . ASP B 1 211 ? 43.00036  9.33850   62.72855  1.000 128.00104 ? 211 ASP B N   1 
ATOM 3343 C CA  . ASP B 1 211 ? 43.20691  7.98326   63.23148  1.000 126.27464 ? 211 ASP B CA  1 
ATOM 3344 C C   . ASP B 1 211 ? 41.96542  7.52498   63.98292  1.000 129.08864 ? 211 ASP B C   1 
ATOM 3345 O O   . ASP B 1 211 ? 41.49824  8.21585   64.89360  1.000 129.12253 ? 211 ASP B O   1 
ATOM 3346 C CB  . ASP B 1 211 ? 44.42593  7.91832   64.15706  1.000 122.23752 ? 211 ASP B CB  1 
ATOM 3347 N N   . ALA B 1 212 ? 41.42979  6.37348   63.59614  1.000 120.85496 ? 212 ALA B N   1 
ATOM 3348 C CA  . ALA B 1 212 ? 40.30145  5.81110   64.32014  1.000 115.19498 ? 212 ALA B CA  1 
ATOM 3349 C C   . ALA B 1 212 ? 40.73912  5.47117   65.73992  1.000 117.44190 ? 212 ALA B C   1 
ATOM 3350 O O   . ALA B 1 212 ? 41.79608  4.85190   65.92684  1.000 115.44599 ? 212 ALA B O   1 
ATOM 3351 C CB  . ALA B 1 212 ? 39.76559  4.56748   63.61931  1.000 115.01661 ? 212 ALA B CB  1 
ATOM 3352 N N   . PRO B 1 213 ? 39.98164  5.87510   66.75375  1.000 119.25303 ? 213 PRO B N   1 
ATOM 3353 C CA  . PRO B 1 213 ? 40.44258  5.72166   68.13733  1.000 121.85523 ? 213 PRO B CA  1 
ATOM 3354 C C   . PRO B 1 213 ? 40.46958  4.27104   68.59291  1.000 124.66983 ? 213 PRO B C   1 
ATOM 3355 O O   . PRO B 1 213 ? 39.76301  3.40312   68.07667  1.000 122.29539 ? 213 PRO B O   1 
ATOM 3356 C CB  . PRO B 1 213 ? 39.41418  6.52601   68.94244  1.000 121.19873 ? 213 PRO B CB  1 
ATOM 3357 C CG  . PRO B 1 213 ? 38.82198  7.47588   67.96590  1.000 116.81494 ? 213 PRO B CG  1 
ATOM 3358 C CD  . PRO B 1 213 ? 38.78346  6.72200   66.66525  1.000 117.43491 ? 213 PRO B CD  1 
ATOM 3359 N N   . SER B 1 214 ? 41.31704  4.02234   69.58638  1.000 137.62129 ? 214 SER B N   1 
ATOM 3360 C CA  . SER B 1 214 ? 41.23912  2.78746   70.35039  1.000 139.21801 ? 214 SER B CA  1 
ATOM 3361 C C   . SER B 1 214 ? 40.04486  2.83417   71.30604  1.000 139.64522 ? 214 SER B C   1 
ATOM 3362 O O   . SER B 1 214 ? 39.60458  3.90703   71.73124  1.000 139.63382 ? 214 SER B O   1 
ATOM 3363 C CB  . SER B 1 214 ? 42.53630  2.56703   71.12973  1.000 136.30949 ? 214 SER B CB  1 
ATOM 3364 O OG  . SER B 1 214 ? 42.71915  3.56378   72.11929  1.000 133.09944 ? 214 SER B OG  1 
ATOM 3365 N N   . GLU B 1 215 ? 39.51870  1.65086   71.64989  1.000 134.21032 ? 215 GLU B N   1 
ATOM 3366 C CA  . GLU B 1 215 ? 38.37326  1.58687   72.55694  1.000 133.57623 ? 215 GLU B CA  1 
ATOM 3367 C C   . GLU B 1 215 ? 38.67733  2.25426   73.89620  1.000 131.23355 ? 215 GLU B C   1 
ATOM 3368 O O   . GLU B 1 215 ? 37.75648  2.70713   74.58501  1.000 128.87305 ? 215 GLU B O   1 
ATOM 3369 C CB  . GLU B 1 215 ? 37.94180  0.13268   72.76390  1.000 132.35006 ? 215 GLU B CB  1 
ATOM 3370 N N   . GLU B 1 216 ? 39.95685  2.31455   74.28220  1.000 131.25150 ? 216 GLU B N   1 
ATOM 3371 C CA  . GLU B 1 216 ? 40.36893  3.14603   75.40986  1.000 128.67383 ? 216 GLU B CA  1 
ATOM 3372 C C   . GLU B 1 216 ? 40.27668  4.63377   75.07343  1.000 131.74966 ? 216 GLU B C   1 
ATOM 3373 O O   . GLU B 1 216 ? 39.95560  5.45448   75.94391  1.000 126.59424 ? 216 GLU B O   1 
ATOM 3374 C CB  . GLU B 1 216 ? 41.79445  2.78388   75.83039  1.000 123.51498 ? 216 GLU B CB  1 
ATOM 3375 N N   . GLU B 1 217 ? 40.55569  5.00015   73.81608  1.000 132.11550 ? 217 GLU B N   1 
ATOM 3376 C CA  . GLU B 1 217 ? 40.73078  6.39410   73.41770  1.000 129.49933 ? 217 GLU B CA  1 
ATOM 3377 C C   . GLU B 1 217 ? 39.45825  7.07077   72.91435  1.000 126.27852 ? 217 GLU B C   1 
ATOM 3378 O O   . GLU B 1 217 ? 39.49389  8.27317   72.63086  1.000 121.18700 ? 217 GLU B O   1 
ATOM 3379 C CB  . GLU B 1 217 ? 41.80847  6.50115   72.33157  1.000 126.96213 ? 217 GLU B CB  1 
ATOM 3380 N N   . CYS B 1 218 ? 38.34461  6.35767   72.79164  1.000 127.93850 ? 218 CYS B N   1 
ATOM 3381 C CA  . CYS B 1 218 ? 37.14796  6.94815   72.21121  1.000 126.36406 ? 218 CYS B CA  1 
ATOM 3382 C C   . CYS B 1 218 ? 36.11052  7.26963   73.28409  1.000 124.14220 ? 218 CYS B C   1 
ATOM 3383 O O   . CYS B 1 218 ? 36.00097  6.57655   74.29964  1.000 125.86239 ? 218 CYS B O   1 
ATOM 3384 C CB  . CYS B 1 218 ? 36.55305  6.03081   71.13107  1.000 128.61458 ? 218 CYS B CB  1 
ATOM 3385 S SG  . CYS B 1 218 ? 35.95938  4.40485   71.64162  1.000 138.68186 ? 218 CYS B SG  1 
ATOM 3386 N N   . ASP B 1 219 ? 35.36246  8.34797   73.05346  1.000 116.27746 ? 219 ASP B N   1 
ATOM 3387 C CA  . ASP B 1 219 ? 34.32474  8.74124   73.99348  1.000 114.76042 ? 219 ASP B CA  1 
ATOM 3388 C C   . ASP B 1 219 ? 33.27085  7.64379   74.06065  1.000 110.41075 ? 219 ASP B C   1 
ATOM 3389 O O   . ASP B 1 219 ? 32.77237  7.20291   73.01838  1.000 109.04952 ? 219 ASP B O   1 
ATOM 3390 C CB  . ASP B 1 219 ? 33.67724  10.07044  73.59358  1.000 114.34909 ? 219 ASP B CB  1 
ATOM 3391 N N   . PRO B 1 220 ? 32.92455  7.16302   75.25145  1.000 110.93007 ? 220 PRO B N   1 
ATOM 3392 C CA  . PRO B 1 220 ? 31.93560  6.07802   75.34063  1.000 107.68036 ? 220 PRO B CA  1 
ATOM 3393 C C   . PRO B 1 220 ? 30.57357  6.44229   74.77722  1.000 103.47833 ? 220 PRO B C   1 
ATOM 3394 O O   . PRO B 1 220 ? 29.80688  5.54479   74.40072  1.000 100.85433 ? 220 PRO B O   1 
ATOM 3395 C CB  . PRO B 1 220 ? 31.87699  5.79140   76.85170  1.000 107.20528 ? 220 PRO B CB  1 
ATOM 3396 C CG  . PRO B 1 220 ? 32.40034  7.03504   77.51107  1.000 102.40949 ? 220 PRO B CG  1 
ATOM 3397 C CD  . PRO B 1 220 ? 33.42616  7.58347   76.57547  1.000 107.29445 ? 220 PRO B CD  1 
ATOM 3398 N N   . LEU B 1 221 ? 30.24053  7.73252   74.71907  1.000 104.93270 ? 221 LEU B N   1 
ATOM 3399 C CA  . LEU B 1 221 ? 28.93581  8.12970   74.21300  1.000 103.03007 ? 221 LEU B CA  1 
ATOM 3400 C C   . LEU B 1 221 ? 28.78752  7.84656   72.72070  1.000 109.51847 ? 221 LEU B C   1 
ATOM 3401 O O   . LEU B 1 221 ? 27.65992  7.83743   72.21774  1.000 109.80707 ? 221 LEU B O   1 
ATOM 3402 C CB  . LEU B 1 221 ? 28.69509  9.60933   74.51317  1.000 97.94160  ? 221 LEU B CB  1 
ATOM 3403 N N   . SER B 1 222 ? 29.89481  7.58354   72.01508  1.000 112.45991 ? 222 SER B N   1 
ATOM 3404 C CA  . SER B 1 222 ? 29.91628  7.36915   70.56985  1.000 111.89956 ? 222 SER B CA  1 
ATOM 3405 C C   . SER B 1 222 ? 29.68819  5.91462   70.16917  1.000 113.82199 ? 222 SER B C   1 
ATOM 3406 O O   . SER B 1 222 ? 28.92662  5.64961   69.23051  1.000 111.29912 ? 222 SER B O   1 
ATOM 3407 C CB  . SER B 1 222 ? 31.25256  7.84326   69.98786  1.000 110.82344 ? 222 SER B CB  1 
ATOM 3408 O OG  . SER B 1 222 ? 32.32479  7.03270   70.44076  1.000 113.67074 ? 222 SER B OG  1 
ATOM 3409 N N   . LEU B 1 223 ? 30.35780  4.96821   70.83035  1.000 112.52111 ? 223 LEU B N   1 
ATOM 3410 C CA  . LEU B 1 223 ? 30.19331  3.55597   70.48597  1.000 114.05739 ? 223 LEU B CA  1 
ATOM 3411 C C   . LEU B 1 223 ? 28.79364  3.08370   70.87542  1.000 117.88615 ? 223 LEU B C   1 
ATOM 3412 O O   . LEU B 1 223 ? 28.35348  3.32723   72.00633  1.000 120.83531 ? 223 LEU B O   1 
ATOM 3413 C CB  . LEU B 1 223 ? 31.25666  2.70695   71.18214  1.000 108.70725 ? 223 LEU B CB  1 
ATOM 3414 N N   . PRO B 1 224 ? 28.05426  2.42290   69.96948  1.000 118.90174 ? 224 PRO B N   1 
ATOM 3415 C CA  . PRO B 1 224 ? 26.71028  1.89581   70.24650  1.000 118.15986 ? 224 PRO B CA  1 
ATOM 3416 C C   . PRO B 1 224 ? 26.58015  0.43481   69.83707  1.000 119.50553 ? 224 PRO B C   1 
ATOM 3417 O O   . PRO B 1 224 ? 27.60773  -0.17456  69.54014  1.000 119.68663 ? 224 PRO B O   1 
ATOM 3418 C CB  . PRO B 1 224 ? 25.79358  2.78615   69.39816  1.000 109.70410 ? 224 PRO B CB  1 
ATOM 3419 N N   . MET C 1 1   ? 14.48145  11.76443  -0.59489  1.000 120.57708 ? 1   MET C N   1 
ATOM 3420 C CA  . MET C 1 1   ? 15.42498  10.69041  -0.27300  1.000 125.87343 ? 1   MET C CA  1 
ATOM 3421 C C   . MET C 1 1   ? 15.37979  9.52662   -1.27715  1.000 128.61257 ? 1   MET C C   1 
ATOM 3422 O O   . MET C 1 1   ? 14.38455  8.80161   -1.34512  1.000 129.02889 ? 1   MET C O   1 
ATOM 3423 C CB  . MET C 1 1   ? 15.16428  10.17512  1.14831   1.000 126.46522 ? 1   MET C CB  1 
ATOM 3424 C CG  . MET C 1 1   ? 16.08746  9.03549   1.60357   1.000 133.72689 ? 1   MET C CG  1 
ATOM 3425 S SD  . MET C 1 1   ? 15.47684  7.33284   1.40239   1.000 129.48163 ? 1   MET C SD  1 
ATOM 3426 C CE  . MET C 1 1   ? 14.43841  7.14397   2.85037   1.000 122.55200 ? 1   MET C CE  1 
ATOM 3427 N N   . PHE C 1 2   ? 16.46774  9.36384   -2.04289  1.000 130.35444 ? 2   PHE C N   1 
ATOM 3428 C CA  . PHE C 1 2   ? 16.64823  8.28310   -3.01327  1.000 128.59567 ? 2   PHE C CA  1 
ATOM 3429 C C   . PHE C 1 2   ? 17.36313  7.07166   -2.39207  1.000 128.56166 ? 2   PHE C C   1 
ATOM 3430 O O   . PHE C 1 2   ? 18.18912  7.20976   -1.48420  1.000 127.64888 ? 2   PHE C O   1 
ATOM 3431 C CB  . PHE C 1 2   ? 17.47448  8.76123   -4.22438  1.000 126.40765 ? 2   PHE C CB  1 
ATOM 3432 C CG  . PHE C 1 2   ? 16.72539  9.62208   -5.22891  1.000 126.99936 ? 2   PHE C CG  1 
ATOM 3433 C CD1 . PHE C 1 2   ? 15.34204  9.67601   -5.26023  1.000 127.18804 ? 2   PHE C CD1 1 
ATOM 3434 C CD2 . PHE C 1 2   ? 17.43543  10.36027  -6.17439  1.000 127.11596 ? 2   PHE C CD2 1 
ATOM 3435 C CE1 . PHE C 1 2   ? 14.68852  10.45445  -6.20779  1.000 129.65319 ? 2   PHE C CE1 1 
ATOM 3436 C CE2 . PHE C 1 2   ? 16.78660  11.14354  -7.11504  1.000 127.07931 ? 2   PHE C CE2 1 
ATOM 3437 C CZ  . PHE C 1 2   ? 15.41389  11.19032  -7.13207  1.000 126.89983 ? 2   PHE C CZ  1 
ATOM 3438 N N   . ASP C 1 3   ? 17.04333  5.87407   -2.90645  1.000 116.13773 ? 3   ASP C N   1 
ATOM 3439 C CA  . ASP C 1 3   ? 17.87154  4.68261   -2.73647  1.000 107.72904 ? 3   ASP C CA  1 
ATOM 3440 C C   . ASP C 1 3   ? 18.85373  4.57454   -3.91494  1.000 106.46889 ? 3   ASP C C   1 
ATOM 3441 O O   . ASP C 1 3   ? 19.01188  5.51867   -4.69482  1.000 106.83329 ? 3   ASP C O   1 
ATOM 3442 C CB  . ASP C 1 3   ? 16.99771  3.43585   -2.59355  1.000 104.07392 ? 3   ASP C CB  1 
ATOM 3443 C CG  . ASP C 1 3   ? 16.35792  3.31706   -1.21762  1.000 106.88778 ? 3   ASP C CG  1 
ATOM 3444 O OD1 . ASP C 1 3   ? 16.90122  3.90024   -0.25687  1.000 104.29578 ? 3   ASP C OD1 1 
ATOM 3445 O OD2 . ASP C 1 3   ? 15.34077  2.59725   -1.08661  1.000 105.39603 ? 3   ASP C OD2 1 
ATOM 3446 N N   . PHE C 1 4   ? 19.54008  3.43479   -4.06611  1.000 99.45679  ? 4   PHE C N   1 
ATOM 3447 C CA  . PHE C 1 4   ? 20.44322  3.27970   -5.20226  1.000 95.45204  ? 4   PHE C CA  1 
ATOM 3448 C C   . PHE C 1 4   ? 20.62704  1.81394   -5.57700  1.000 93.67672  ? 4   PHE C C   1 
ATOM 3449 O O   . PHE C 1 4   ? 20.50720  0.92249   -4.73448  1.000 93.75446  ? 4   PHE C O   1 
ATOM 3450 C CB  . PHE C 1 4   ? 21.81458  3.92352   -4.94155  1.000 93.91471  ? 4   PHE C CB  1 
ATOM 3451 C CG  . PHE C 1 4   ? 22.61059  3.29621   -3.82074  1.000 92.31973  ? 4   PHE C CG  1 
ATOM 3452 C CD1 . PHE C 1 4   ? 22.59339  3.84167   -2.55100  1.000 92.71797  ? 4   PHE C CD1 1 
ATOM 3453 C CD2 . PHE C 1 4   ? 23.40998  2.18403   -4.04959  1.000 91.54099  ? 4   PHE C CD2 1 
ATOM 3454 C CE1 . PHE C 1 4   ? 23.34982  3.28922   -1.53806  1.000 88.45773  ? 4   PHE C CE1 1 
ATOM 3455 C CE2 . PHE C 1 4   ? 24.16180  1.62343   -3.03384  1.000 84.75705  ? 4   PHE C CE2 1 
ATOM 3456 C CZ  . PHE C 1 4   ? 24.13559  2.17891   -1.78632  1.000 84.91090  ? 4   PHE C CZ  1 
ATOM 3457 N N   . ILE C 1 5   ? 20.93742  1.58287   -6.86085  1.000 95.48659  ? 5   ILE C N   1 
ATOM 3458 C CA  . ILE C 1 5   ? 21.26038  0.26260   -7.40528  1.000 94.53823  ? 5   ILE C CA  1 
ATOM 3459 C C   . ILE C 1 5   ? 22.65159  0.29691   -8.03589  1.000 91.61206  ? 5   ILE C C   1 
ATOM 3460 O O   . ILE C 1 5   ? 23.06267  1.30197   -8.62698  1.000 88.30916  ? 5   ILE C O   1 
ATOM 3461 C CB  . ILE C 1 5   ? 20.22655  -0.22757  -8.44214  1.000 94.50801  ? 5   ILE C CB  1 
ATOM 3462 C CG1 . ILE C 1 5   ? 20.54010  -1.67429  -8.84608  1.000 95.78894  ? 5   ILE C CG1 1 
ATOM 3463 C CG2 . ILE C 1 5   ? 20.23576  0.66455   -9.66906  1.000 94.65573  ? 5   ILE C CG2 1 
ATOM 3464 C CD1 . ILE C 1 5   ? 19.49099  -2.33757  -9.71566  1.000 98.94209  ? 5   ILE C CD1 1 
ATOM 3465 N N   . ILE C 1 6   ? 23.38262  -0.80569  -7.88742  1.000 89.06598  ? 6   ILE C N   1 
ATOM 3466 C CA  . ILE C 1 6   ? 24.74923  -0.91473  -8.35752  1.000 82.06705  ? 6   ILE C CA  1 
ATOM 3467 C C   . ILE C 1 6   ? 24.89729  -2.23912  -9.07741  1.000 86.65450  ? 6   ILE C C   1 
ATOM 3468 O O   . ILE C 1 6   ? 24.16940  -3.20632  -8.83261  1.000 81.70736  ? 6   ILE C O   1 
ATOM 3469 C CB  . ILE C 1 6   ? 25.79521  -0.81788  -7.23074  1.000 82.91975  ? 6   ILE C CB  1 
ATOM 3470 C CG1 . ILE C 1 6   ? 25.63495  -1.98182  -6.25118  1.000 81.85014  ? 6   ILE C CG1 1 
ATOM 3471 C CG2 . ILE C 1 6   ? 25.70043  0.51892   -6.51721  1.000 85.55106  ? 6   ILE C CG2 1 
ATOM 3472 C CD1 . ILE C 1 6   ? 26.76925  -2.12231  -5.26739  1.000 73.42669  ? 6   ILE C CD1 1 
ATOM 3473 N N   . ASP C 1 7   ? 25.87786  -2.26270  -9.97416  1.000 91.69046  ? 7   ASP C N   1 
ATOM 3474 C CA  . ASP C 1 7   ? 26.05726  -3.36813  -10.89807 1.000 86.16128  ? 7   ASP C CA  1 
ATOM 3475 C C   . ASP C 1 7   ? 27.49364  -3.35294  -11.37947 1.000 83.56013  ? 7   ASP C C   1 
ATOM 3476 O O   . ASP C 1 7   ? 27.98004  -2.31595  -11.82223 1.000 84.13179  ? 7   ASP C O   1 
ATOM 3477 C CB  . ASP C 1 7   ? 25.10357  -3.24731  -12.06961 1.000 85.28961  ? 7   ASP C CB  1 
ATOM 3478 C CG  . ASP C 1 7   ? 24.98591  -4.52333  -12.82051 1.000 93.10761  ? 7   ASP C CG  1 
ATOM 3479 O OD1 . ASP C 1 7   ? 25.66929  -5.48710  -12.41924 1.000 91.99170  ? 7   ASP C OD1 1 
ATOM 3480 O OD2 . ASP C 1 7   ? 24.21409  -4.57191  -13.80130 1.000 103.68747 ? 7   ASP C OD2 1 
ATOM 3481 N N   . PHE C 1 8   ? 28.16834  -4.48623  -11.25792 1.000 80.88541  ? 8   PHE C N   1 
ATOM 3482 C CA  . PHE C 1 8   ? 29.54051  -4.64954  -11.70177 1.000 81.45105  ? 8   PHE C CA  1 
ATOM 3483 C C   . PHE C 1 8   ? 29.59388  -5.67155  -12.82103 1.000 84.33432  ? 8   PHE C C   1 
ATOM 3484 O O   . PHE C 1 8   ? 28.87763  -6.67668  -12.78809 1.000 85.91290  ? 8   PHE C O   1 
ATOM 3485 C CB  . PHE C 1 8   ? 30.46753  -5.12115  -10.57280 1.000 79.64671  ? 8   PHE C CB  1 
ATOM 3486 C CG  . PHE C 1 8   ? 30.87756  -4.04237  -9.61481  1.000 78.42926  ? 8   PHE C CG  1 
ATOM 3487 C CD1 . PHE C 1 8   ? 31.88738  -3.15180  -9.95283  1.000 79.31903  ? 8   PHE C CD1 1 
ATOM 3488 C CD2 . PHE C 1 8   ? 30.29168  -3.94017  -8.36694  1.000 75.11860  ? 8   PHE C CD2 1 
ATOM 3489 C CE1 . PHE C 1 8   ? 32.28643  -2.15406  -9.07138  1.000 78.30254  ? 8   PHE C CE1 1 
ATOM 3490 C CE2 . PHE C 1 8   ? 30.68277  -2.94377  -7.47682  1.000 73.65343  ? 8   PHE C CE2 1 
ATOM 3491 C CZ  . PHE C 1 8   ? 31.67932  -2.04892  -7.82581  1.000 73.38662  ? 8   PHE C CZ  1 
ATOM 3492 N N   . GLU C 1 9   ? 30.44118  -5.40934  -13.81039 1.000 83.04263  ? 9   GLU C N   1 
ATOM 3493 C CA  . GLU C 1 9   ? 30.92406  -6.44676  -14.70547 1.000 82.44698  ? 9   GLU C CA  1 
ATOM 3494 C C   . GLU C 1 9   ? 32.37425  -6.72487  -14.34622 1.000 77.46293  ? 9   GLU C C   1 
ATOM 3495 O O   . GLU C 1 9   ? 33.15405  -5.79114  -14.13236 1.000 76.09358  ? 9   GLU C O   1 
ATOM 3496 C CB  . GLU C 1 9   ? 30.75599  -6.04231  -16.16904 1.000 88.93954  ? 9   GLU C CB  1 
ATOM 3497 C CG  . GLU C 1 9   ? 29.27950  -5.98166  -16.54844 1.000 93.84187  ? 9   GLU C CG  1 
ATOM 3498 C CD  . GLU C 1 9   ? 29.05654  -5.75357  -18.01157 1.000 98.91080  ? 9   GLU C CD  1 
ATOM 3499 O OE1 . GLU C 1 9   ? 30.05410  -5.49260  -18.70465 1.000 103.48189 ? 9   GLU C OE1 1 
ATOM 3500 O OE2 . GLU C 1 9   ? 27.89371  -5.85124  -18.46938 1.000 102.93117 ? 9   GLU C OE2 1 
ATOM 3501 N N   . THR C 1 10  ? 32.71419  -8.00276  -14.21030 1.000 75.60745  ? 10  THR C N   1 
ATOM 3502 C CA  . THR C 1 10  ? 33.94221  -8.38406  -13.53694 1.000 73.83553  ? 10  THR C CA  1 
ATOM 3503 C C   . THR C 1 10  ? 34.71660  -9.37034  -14.38692 1.000 74.01349  ? 10  THR C C   1 
ATOM 3504 O O   . THR C 1 10  ? 34.18345  -9.98966  -15.30617 1.000 76.68968  ? 10  THR C O   1 
ATOM 3505 C CB  . THR C 1 10  ? 33.67739  -8.99986  -12.14312 1.000 77.14003  ? 10  THR C CB  1 
ATOM 3506 O OG1 . THR C 1 10  ? 32.97701  -10.24710 -12.26574 1.000 76.72318  ? 10  THR C OG1 1 
ATOM 3507 C CG2 . THR C 1 10  ? 32.83866  -8.05363  -11.30838 1.000 74.53127  ? 10  THR C CG2 1 
ATOM 3508 N N   . MET C 1 11  ? 36.00019  -9.47582  -14.06001 1.000 73.50859  ? 11  MET C N   1 
ATOM 3509 C CA  . MET C 1 11  ? 36.94278  -10.42390 -14.63687 1.000 74.25754  ? 11  MET C CA  1 
ATOM 3510 C C   . MET C 1 11  ? 37.35501  -11.52029 -13.66865 1.000 78.61905  ? 11  MET C C   1 
ATOM 3511 O O   . MET C 1 11  ? 38.30916  -12.25659 -13.96089 1.000 78.18598  ? 11  MET C O   1 
ATOM 3512 C CB  . MET C 1 11  ? 38.19676  -9.69477  -15.08961 1.000 74.11678  ? 11  MET C CB  1 
ATOM 3513 C CG  . MET C 1 11  ? 38.07172  -9.03662  -16.40367 1.000 82.94164  ? 11  MET C CG  1 
ATOM 3514 S SD  . MET C 1 11  ? 38.04995  -10.30984 -17.67380 1.000 80.34361  ? 11  MET C SD  1 
ATOM 3515 C CE  . MET C 1 11  ? 37.70251  -9.25649  -19.09185 1.000 84.16158  ? 11  MET C CE  1 
ATOM 3516 N N   . GLY C 1 12  ? 36.69016  -11.62584 -12.51646 1.000 76.98595  ? 12  GLY C N   1 
ATOM 3517 C CA  . GLY C 1 12  ? 37.13775  -12.50808 -11.46507 1.000 77.18459  ? 12  GLY C CA  1 
ATOM 3518 C C   . GLY C 1 12  ? 35.96951  -12.90986 -10.60279 1.000 80.32549  ? 12  GLY C C   1 
ATOM 3519 O O   . GLY C 1 12  ? 34.83499  -12.47837 -10.81351 1.000 81.32449  ? 12  GLY C O   1 
ATOM 3520 N N   . SER C 1 13  ? 36.26811  -13.73191 -9.60280  1.000 84.05258  ? 13  SER C N   1 
ATOM 3521 C CA  . SER C 1 13  ? 35.24606  -14.34660 -8.76633  1.000 83.84147  ? 13  SER C CA  1 
ATOM 3522 C C   . SER C 1 13  ? 34.98766  -13.58471 -7.47033  1.000 80.94071  ? 13  SER C C   1 
ATOM 3523 O O   . SER C 1 13  ? 33.84126  -13.22288 -7.20118  1.000 83.29270  ? 13  SER C O   1 
ATOM 3524 C CB  . SER C 1 13  ? 35.63928  -15.79829 -8.45382  1.000 86.83540  ? 13  SER C CB  1 
ATOM 3525 O OG  . SER C 1 13  ? 36.80758  -15.84582 -7.64491  1.000 88.09783  ? 13  SER C OG  1 
ATOM 3526 N N   . GLY C 1 14  ? 36.02399  -13.31888 -6.67021  1.000 69.73785  ? 14  GLY C N   1 
ATOM 3527 C CA  . GLY C 1 14  ? 35.84579  -12.92944 -5.28179  1.000 74.15986  ? 14  GLY C CA  1 
ATOM 3528 C C   . GLY C 1 14  ? 35.52448  -11.46231 -5.04349  1.000 73.74119  ? 14  GLY C C   1 
ATOM 3529 O O   . GLY C 1 14  ? 34.99070  -10.75651 -5.90222  1.000 76.04042  ? 14  GLY C O   1 
ATOM 3530 N N   . GLU C 1 15  ? 35.83140  -11.00832 -3.82552  1.000 70.16804  ? 15  GLU C N   1 
ATOM 3531 C CA  . GLU C 1 15  ? 35.79009  -9.58633  -3.50833  1.000 63.58773  ? 15  GLU C CA  1 
ATOM 3532 C C   . GLU C 1 15  ? 37.01960  -8.85177  -4.01382  1.000 67.81447  ? 15  GLU C C   1 
ATOM 3533 O O   . GLU C 1 15  ? 37.07746  -7.62410  -3.89324  1.000 71.29396  ? 15  GLU C O   1 
ATOM 3534 C CB  . GLU C 1 15  ? 35.72693  -9.35920  -2.00560  1.000 63.43163  ? 15  GLU C CB  1 
ATOM 3535 C CG  . GLU C 1 15  ? 37.09247  -9.54167  -1.38604  1.000 65.10057  ? 15  GLU C CG  1 
ATOM 3536 C CD  . GLU C 1 15  ? 37.10772  -9.47473  0.12707   1.000 71.50291  ? 15  GLU C CD  1 
ATOM 3537 O OE1 . GLU C 1 15  ? 36.03226  -9.43620  0.76397   1.000 71.31201  ? 15  GLU C OE1 1 
ATOM 3538 O OE2 . GLU C 1 15  ? 38.22498  -9.45083  0.67996   1.000 73.28284  ? 15  GLU C OE2 1 
ATOM 3539 N N   . LYS C 1 16  ? 38.02634  -9.56943  -4.51269  1.000 67.32482  ? 16  LYS C N   1 
ATOM 3540 C CA  . LYS C 1 16  ? 39.19949  -8.95816  -5.10995  1.000 63.49932  ? 16  LYS C CA  1 
ATOM 3541 C C   . LYS C 1 16  ? 39.13983  -9.00222  -6.61725  1.000 64.66173  ? 16  LYS C C   1 
ATOM 3542 O O   . LYS C 1 16  ? 40.16994  -8.82822  -7.27064  1.000 69.02353  ? 16  LYS C O   1 
ATOM 3543 C CB  . LYS C 1 16  ? 40.47892  -9.63759  -4.62559  1.000 61.31578  ? 16  LYS C CB  1 
ATOM 3544 C CG  . LYS C 1 16  ? 40.60334  -9.64223  -3.13683  1.000 60.97775  ? 16  LYS C CG  1 
ATOM 3545 C CD  . LYS C 1 16  ? 40.60665  -8.27340  -2.55819  1.000 57.82557  ? 16  LYS C CD  1 
ATOM 3546 C CE  . LYS C 1 16  ? 41.94719  -7.62046  -2.72609  1.000 61.17349  ? 16  LYS C CE  1 
ATOM 3547 N NZ  . LYS C 1 16  ? 41.95074  -6.30386  -2.02021  1.000 61.61699  ? 16  LYS C NZ  1 
ATOM 3548 N N   . ALA C 1 17  ? 37.95789  -9.23154  -7.17995  1.000 63.52049  ? 17  ALA C N   1 
ATOM 3549 C CA  . ALA C 1 17  ? 37.81778  -9.39508  -8.62175  1.000 68.77115  ? 17  ALA C CA  1 
ATOM 3550 C C   . ALA C 1 17  ? 38.16866  -8.12045  -9.39522  1.000 66.76802  ? 17  ALA C C   1 
ATOM 3551 O O   . ALA C 1 17  ? 37.89839  -6.99562  -8.95686  1.000 64.60940  ? 17  ALA C O   1 
ATOM 3552 C CB  . ALA C 1 17  ? 36.38994  -9.81571  -8.95534  1.000 71.46786  ? 17  ALA C CB  1 
ATOM 3553 N N   . ALA C 1 18  ? 38.76120  -8.30767  -10.57339 1.000 68.03788  ? 18  ALA C N   1 
ATOM 3554 C CA  . ALA C 1 18  ? 38.96055  -7.18573  -11.48643 1.000 68.08856  ? 18  ALA C CA  1 
ATOM 3555 C C   . ALA C 1 18  ? 37.61726  -6.69090  -12.01060 1.000 69.00501  ? 18  ALA C C   1 
ATOM 3556 O O   . ALA C 1 18  ? 36.71168  -7.47205  -12.31599 1.000 70.70861  ? 18  ALA C O   1 
ATOM 3557 C CB  . ALA C 1 18  ? 39.87244  -7.57917  -12.64691 1.000 65.92701  ? 18  ALA C CB  1 
ATOM 3558 N N   . VAL C 1 19  ? 37.47476  -5.38194  -12.09126 1.000 67.61332  ? 19  VAL C N   1 
ATOM 3559 C CA  . VAL C 1 19  ? 36.20194  -4.77559  -12.43119 1.000 69.08768  ? 19  VAL C CA  1 
ATOM 3560 C C   . VAL C 1 19  ? 36.29955  -4.20892  -13.83215 1.000 74.58629  ? 19  VAL C C   1 
ATOM 3561 O O   . VAL C 1 19  ? 37.19277  -3.40556  -14.13304 1.000 72.93833  ? 19  VAL C O   1 
ATOM 3562 C CB  . VAL C 1 19  ? 35.80916  -3.70499  -11.41469 1.000 69.22778  ? 19  VAL C CB  1 
ATOM 3563 C CG1 . VAL C 1 19  ? 35.33481  -4.37956  -10.17762 1.000 73.74141  ? 19  VAL C CG1 1 
ATOM 3564 C CG2 . VAL C 1 19  ? 37.02199  -2.88060  -11.06390 1.000 65.61638  ? 19  VAL C CG2 1 
ATOM 3565 N N   . ILE C 1 20  ? 35.39855  -4.65808  -14.69785 1.000 76.27480  ? 20  ILE C N   1 
ATOM 3566 C CA  . ILE C 1 20  ? 35.29135  -4.06531  -16.01812 1.000 76.40223  ? 20  ILE C CA  1 
ATOM 3567 C C   . ILE C 1 20  ? 34.56165  -2.72883  -15.92810 1.000 78.68816  ? 20  ILE C C   1 
ATOM 3568 O O   . ILE C 1 20  ? 35.06081  -1.69990  -16.39900 1.000 79.78430  ? 20  ILE C O   1 
ATOM 3569 C CB  . ILE C 1 20  ? 34.60939  -5.05449  -16.98413 1.000 76.06751  ? 20  ILE C CB  1 
ATOM 3570 N N   . ASP C 1 21  ? 33.40042  -2.70173  -15.27367 1.000 88.42632  ? 21  ASP C N   1 
ATOM 3571 C CA  . ASP C 1 21  ? 32.71008  -1.43573  -15.06789 1.000 88.40055  ? 21  ASP C CA  1 
ATOM 3572 C C   . ASP C 1 21  ? 31.79857  -1.51907  -13.84524 1.000 88.56487  ? 21  ASP C C   1 
ATOM 3573 O O   . ASP C 1 21  ? 31.50035  -2.60002  -13.32925 1.000 89.00046  ? 21  ASP C O   1 
ATOM 3574 C CB  . ASP C 1 21  ? 31.91465  -1.00249  -16.31991 1.000 90.19442  ? 21  ASP C CB  1 
ATOM 3575 C CG  . ASP C 1 21  ? 30.58595  -1.76634  -16.51852 1.000 95.61946  ? 21  ASP C CG  1 
ATOM 3576 O OD1 . ASP C 1 21  ? 30.21340  -2.68349  -15.74149 1.000 97.86307  ? 21  ASP C OD1 1 
ATOM 3577 O OD2 . ASP C 1 21  ? 29.87234  -1.40479  -17.47529 1.000 98.55113  ? 21  ASP C OD2 1 
ATOM 3578 N N   . LEU C 1 22  ? 31.34788  -0.34742  -13.40242 1.000 82.42739  ? 22  LEU C N   1 
ATOM 3579 C CA  . LEU C 1 22  ? 30.32169  -0.20357  -12.38554 1.000 84.91836  ? 22  LEU C CA  1 
ATOM 3580 C C   . LEU C 1 22  ? 29.19988  0.67412   -12.91698 1.000 84.00812  ? 22  LEU C C   1 
ATOM 3581 O O   . LEU C 1 22  ? 29.45382  1.74544   -13.46729 1.000 83.50312  ? 22  LEU C O   1 
ATOM 3582 C CB  . LEU C 1 22  ? 30.88956  0.40808   -11.09357 1.000 82.60590  ? 22  LEU C CB  1 
ATOM 3583 C CG  . LEU C 1 22  ? 29.83245  0.77552   -10.03951 1.000 81.37005  ? 22  LEU C CG  1 
ATOM 3584 C CD1 . LEU C 1 22  ? 29.05963  -0.42756  -9.53790  1.000 82.42173  ? 22  LEU C CD1 1 
ATOM 3585 C CD2 . LEU C 1 22  ? 30.44172  1.54565   -8.88786  1.000 76.99249  ? 22  LEU C CD2 1 
ATOM 3586 N N   . ALA C 1 23  ? 27.96068  0.23496   -12.71054 1.000 86.59068  ? 23  ALA C N   1 
ATOM 3587 C CA  . ALA C 1 23  ? 26.76842  0.96459   -13.12092 1.000 87.63637  ? 23  ALA C CA  1 
ATOM 3588 C C   . ALA C 1 23  ? 25.94524  1.31418   -11.89002 1.000 88.01151  ? 23  ALA C C   1 
ATOM 3589 O O   . ALA C 1 23  ? 25.62548  0.42560   -11.10126 1.000 87.10808  ? 23  ALA C O   1 
ATOM 3590 C CB  . ALA C 1 23  ? 25.93880  0.12182   -14.08818 1.000 93.48366  ? 23  ALA C CB  1 
ATOM 3591 N N   . VAL C 1 24  ? 25.59636  2.59905   -11.73185 1.000 89.66625  ? 24  VAL C N   1 
ATOM 3592 C CA  . VAL C 1 24  ? 24.96300  3.11622   -10.51416 1.000 87.93291  ? 24  VAL C CA  1 
ATOM 3593 C C   . VAL C 1 24  ? 23.83823  4.08660   -10.87353 1.000 92.85428  ? 24  VAL C C   1 
ATOM 3594 O O   . VAL C 1 24  ? 24.08799  5.12231   -11.50061 1.000 94.28741  ? 24  VAL C O   1 
ATOM 3595 C CB  . VAL C 1 24  ? 25.97214  3.83895   -9.60945  1.000 85.64169  ? 24  VAL C CB  1 
ATOM 3596 C CG1 . VAL C 1 24  ? 25.29089  4.29349   -8.31937  1.000 86.10145  ? 24  VAL C CG1 1 
ATOM 3597 C CG2 . VAL C 1 24  ? 27.16670  2.96967   -9.34628  1.000 84.22060  ? 24  VAL C CG2 1 
ATOM 3598 N N   . ILE C 1 25  ? 22.62055  3.80152   -10.40707 1.000 94.46616  ? 25  ILE C N   1 
ATOM 3599 C CA  . ILE C 1 25  ? 21.46601  4.67801   -10.59441 1.000 95.34189  ? 25  ILE C CA  1 
ATOM 3600 C C   . ILE C 1 25  ? 20.79423  4.94237   -9.24397  1.000 100.43130 ? 25  ILE C C   1 
ATOM 3601 O O   . ILE C 1 25  ? 20.42289  4.00040   -8.53206  1.000 97.13656  ? 25  ILE C O   1 
ATOM 3602 C CB  . ILE C 1 25  ? 20.42997  4.06646   -11.55382 1.000 97.06076  ? 25  ILE C CB  1 
ATOM 3603 C CG1 . ILE C 1 25  ? 21.04815  3.63053   -12.86892 1.000 96.79324  ? 25  ILE C CG1 1 
ATOM 3604 C CG2 . ILE C 1 25  ? 19.36293  5.06727   -11.87385 1.000 103.40270 ? 25  ILE C CG2 1 
ATOM 3605 C CD1 . ILE C 1 25  ? 20.05030  2.90358   -13.72315 1.000 97.80405  ? 25  ILE C CD1 1 
ATOM 3606 N N   . ALA C 1 26  ? 20.61190  6.21919   -8.90804  1.000 103.73248 ? 26  ALA C N   1 
ATOM 3607 C CA  . ALA C 1 26  ? 19.66684  6.59662   -7.86583  1.000 103.54260 ? 26  ALA C CA  1 
ATOM 3608 C C   . ALA C 1 26  ? 18.23984  6.48026   -8.39593  1.000 108.46125 ? 26  ALA C C   1 
ATOM 3609 O O   . ALA C 1 26  ? 17.99982  6.54558   -9.60174  1.000 106.97017 ? 26  ALA C O   1 
ATOM 3610 C CB  . ALA C 1 26  ? 19.93529  8.02112   -7.38545  1.000 102.64561 ? 26  ALA C CB  1 
ATOM 3611 N N   . PHE C 1 27  ? 17.28183  6.29113   -7.49053  1.000 112.08916 ? 27  PHE C N   1 
ATOM 3612 C CA  . PHE C 1 27  ? 15.89467  6.12325   -7.91593  1.000 114.68517 ? 27  PHE C CA  1 
ATOM 3613 C C   . PHE C 1 27  ? 14.96880  6.43720   -6.74920  1.000 112.03710 ? 27  PHE C C   1 
ATOM 3614 O O   . PHE C 1 27  ? 15.41564  6.73914   -5.64412  1.000 111.86999 ? 27  PHE C O   1 
ATOM 3615 C CB  . PHE C 1 27  ? 15.65543  4.71912   -8.47893  1.000 111.03406 ? 27  PHE C CB  1 
ATOM 3616 C CG  . PHE C 1 27  ? 15.86500  3.62508   -7.48817  1.000 105.45816 ? 27  PHE C CG  1 
ATOM 3617 C CD1 . PHE C 1 27  ? 17.12969  3.10365   -7.26834  1.000 104.93776 ? 27  PHE C CD1 1 
ATOM 3618 C CD2 . PHE C 1 27  ? 14.80254  3.09095   -6.80444  1.000 104.35208 ? 27  PHE C CD2 1 
ATOM 3619 C CE1 . PHE C 1 27  ? 17.32791  2.08516   -6.35966  1.000 101.73488 ? 27  PHE C CE1 1 
ATOM 3620 C CE2 . PHE C 1 27  ? 14.99703  2.06567   -5.89890  1.000 104.83945 ? 27  PHE C CE2 1 
ATOM 3621 C CZ  . PHE C 1 27  ? 16.25790  1.56466   -5.67544  1.000 99.60663  ? 27  PHE C CZ  1 
ATOM 3622 N N   . ASP C 1 28  ? 13.66228  6.37716   -7.02114  1.000 115.14631 ? 28  ASP C N   1 
ATOM 3623 C CA  . ASP C 1 28  ? 12.61861  6.77394   -6.07871  1.000 115.95294 ? 28  ASP C CA  1 
ATOM 3624 C C   . ASP C 1 28  ? 12.00839  5.54051   -5.43197  1.000 119.71280 ? 28  ASP C C   1 
ATOM 3625 O O   . ASP C 1 28  ? 11.43041  4.70756   -6.15102  1.000 119.62188 ? 28  ASP C O   1 
ATOM 3626 C CB  . ASP C 1 28  ? 11.53628  7.56744   -6.80339  1.000 121.04569 ? 28  ASP C CB  1 
ATOM 3627 C CG  . ASP C 1 28  ? 10.51072  8.16889   -5.86000  1.000 120.29075 ? 28  ASP C CG  1 
ATOM 3628 O OD1 . ASP C 1 28  ? 10.69691  8.03861   -4.63809  1.000 122.43480 ? 28  ASP C OD1 1 
ATOM 3629 O OD2 . ASP C 1 28  ? 9.50225   8.74634   -6.33899  1.000 119.05180 ? 28  ASP C OD2 1 
ATOM 3630 N N   . PRO C 1 29  ? 12.08475  5.37936   -4.08461  1.000 123.24424 ? 29  PRO C N   1 
ATOM 3631 C CA  . PRO C 1 29  ? 11.52613  4.17361   -3.44825  1.000 120.81098 ? 29  PRO C CA  1 
ATOM 3632 C C   . PRO C 1 29  ? 10.00003  4.13333   -3.34032  1.000 128.87558 ? 29  PRO C C   1 
ATOM 3633 O O   . PRO C 1 29  ? 9.41221   3.04749   -3.40831  1.000 127.51361 ? 29  PRO C O   1 
ATOM 3634 C CB  . PRO C 1 29  ? 12.17611  4.19423   -2.05922  1.000 116.52625 ? 29  PRO C CB  1 
ATOM 3635 C CG  . PRO C 1 29  ? 12.47523  5.62697   -1.80435  1.000 113.62609 ? 29  PRO C CG  1 
ATOM 3636 C CD  . PRO C 1 29  ? 12.84405  6.20565   -3.12532  1.000 117.43385 ? 29  PRO C CD  1 
ATOM 3637 N N   . ASN C 1 30  ? 9.35182   5.29392   -3.18153  1.000 138.61694 ? 30  ASN C N   1 
ATOM 3638 C CA  . ASN C 1 30  ? 7.89295   5.35522   -3.00095  1.000 140.77474 ? 30  ASN C CA  1 
ATOM 3639 C C   . ASN C 1 30  ? 7.17094   4.85097   -4.25289  1.000 141.47287 ? 30  ASN C C   1 
ATOM 3640 O O   . ASN C 1 30  ? 7.47155   5.31137   -5.36238  1.000 139.57667 ? 30  ASN C O   1 
ATOM 3641 C CB  . ASN C 1 30  ? 7.48834   6.80188   -2.69364  1.000 139.61472 ? 30  ASN C CB  1 
ATOM 3642 C CG  . ASN C 1 30  ? 6.04981   6.93913   -2.22615  1.000 140.26332 ? 30  ASN C CG  1 
ATOM 3643 O OD1 . ASN C 1 30  ? 5.31723   5.96233   -2.11440  1.000 140.59551 ? 30  ASN C OD1 1 
ATOM 3644 N ND2 . ASN C 1 30  ? 5.64185   8.17118   -1.94711  1.000 142.16499 ? 30  ASN C ND2 1 
ATOM 3645 N N   . PRO C 1 31  ? 6.21632   3.90432   -4.12645  1.000 136.54959 ? 31  PRO C N   1 
ATOM 3646 C CA  . PRO C 1 31  ? 5.47887   3.36126   -5.28293  1.000 132.45290 ? 31  PRO C CA  1 
ATOM 3647 C C   . PRO C 1 31  ? 4.67659   4.39538   -6.08050  1.000 130.49126 ? 31  PRO C C   1 
ATOM 3648 O O   . PRO C 1 31  ? 4.33336   4.12079   -7.23622  1.000 123.00364 ? 31  PRO C O   1 
ATOM 3649 C CB  . PRO C 1 31  ? 4.53423   2.34032   -4.64387  1.000 130.08780 ? 31  PRO C CB  1 
ATOM 3650 C CG  . PRO C 1 31  ? 5.21821   1.93611   -3.38676  1.000 130.49407 ? 31  PRO C CG  1 
ATOM 3651 C CD  . PRO C 1 31  ? 5.91951   3.15929   -2.88864  1.000 132.95876 ? 31  PRO C CD  1 
ATOM 3652 N N   . THR C 1 36  ? 9.96227   5.61424   -15.11026 1.000 140.45513 ? 36  THR C N   1 
ATOM 3653 C CA  . THR C 1 36  ? 9.97959   5.15438   -16.50315 1.000 136.88950 ? 36  THR C CA  1 
ATOM 3654 C C   . THR C 1 36  ? 11.40637  5.06501   -17.07263 1.000 133.87675 ? 36  THR C C   1 
ATOM 3655 O O   . THR C 1 36  ? 12.32160  5.75192   -16.61348 1.000 133.25503 ? 36  THR C O   1 
ATOM 3656 C CB  . THR C 1 36  ? 9.12996   6.06527   -17.40541 1.000 137.93605 ? 36  THR C CB  1 
ATOM 3657 O OG1 . THR C 1 36  ? 9.67338   7.38765   -17.39288 1.000 137.92534 ? 36  THR C OG1 1 
ATOM 3658 C CG2 . THR C 1 36  ? 7.68410   6.10702   -16.91754 1.000 140.42869 ? 36  THR C CG2 1 
ATOM 3659 N N   . PHE C 1 37  ? 11.57183  4.22440   -18.09712 1.000 125.37630 ? 37  PHE C N   1 
ATOM 3660 C CA  . PHE C 1 37  ? 12.90155  3.73961   -18.45744 1.000 122.94928 ? 37  PHE C CA  1 
ATOM 3661 C C   . PHE C 1 37  ? 13.80746  4.84830   -18.99169 1.000 123.39408 ? 37  PHE C C   1 
ATOM 3662 O O   . PHE C 1 37  ? 15.00790  4.86649   -18.68835 1.000 118.70670 ? 37  PHE C O   1 
ATOM 3663 C CB  . PHE C 1 37  ? 12.77216  2.59475   -19.45984 1.000 121.93322 ? 37  PHE C CB  1 
ATOM 3664 C CG  . PHE C 1 37  ? 14.08547  2.03893   -19.92037 1.000 119.64968 ? 37  PHE C CG  1 
ATOM 3665 C CD1 . PHE C 1 37  ? 14.92673  1.38494   -19.03100 1.000 115.87338 ? 37  PHE C CD1 1 
ATOM 3666 C CD2 . PHE C 1 37  ? 14.45666  2.12597   -21.25594 1.000 121.23283 ? 37  PHE C CD2 1 
ATOM 3667 C CE1 . PHE C 1 37  ? 16.13032  0.85081   -19.45464 1.000 115.73879 ? 37  PHE C CE1 1 
ATOM 3668 C CE2 . PHE C 1 37  ? 15.66034  1.59721   -21.69233 1.000 121.72143 ? 37  PHE C CE2 1 
ATOM 3669 C CZ  . PHE C 1 37  ? 16.50068  0.95778   -20.78805 1.000 120.33288 ? 37  PHE C CZ  1 
ATOM 3670 N N   . ASP C 1 38  ? 13.26591  5.77479   -19.79412 1.000 124.48260 ? 38  ASP C N   1 
ATOM 3671 C CA  . ASP C 1 38  ? 14.10131  6.85076   -20.32740 1.000 121.01926 ? 38  ASP C CA  1 
ATOM 3672 C C   . ASP C 1 38  ? 14.57322  7.79678   -19.22996 1.000 122.38267 ? 38  ASP C C   1 
ATOM 3673 O O   . ASP C 1 38  ? 15.63259  8.42218   -19.36712 1.000 118.55547 ? 38  ASP C O   1 
ATOM 3674 C CB  . ASP C 1 38  ? 13.35305  7.62695   -21.41232 1.000 122.69863 ? 38  ASP C CB  1 
ATOM 3675 C CG  . ASP C 1 38  ? 13.19651  6.83078   -22.70473 1.000 118.19917 ? 38  ASP C CG  1 
ATOM 3676 O OD1 . ASP C 1 38  ? 14.04948  5.95459   -22.96890 1.000 114.88357 ? 38  ASP C OD1 1 
ATOM 3677 O OD2 . ASP C 1 38  ? 12.22547  7.09265   -23.45404 1.000 108.22943 ? 38  ASP C OD2 1 
ATOM 3678 N N   . GLU C 1 39  ? 13.79942  7.91608   -18.14657 1.000 127.82296 ? 39  GLU C N   1 
ATOM 3679 C CA  . GLU C 1 39  ? 14.21478  8.70779   -16.99191 1.000 127.76470 ? 39  GLU C CA  1 
ATOM 3680 C C   . GLU C 1 39  ? 15.48421  8.14373   -16.36935 1.000 126.41571 ? 39  GLU C C   1 
ATOM 3681 O O   . GLU C 1 39  ? 16.51188  8.82559   -16.28150 1.000 126.83387 ? 39  GLU C O   1 
ATOM 3682 C CB  . GLU C 1 39  ? 13.09954  8.72857   -15.94593 1.000 129.56820 ? 39  GLU C CB  1 
ATOM 3683 C CG  . GLU C 1 39  ? 11.82715  9.41919   -16.36604 1.000 135.33178 ? 39  GLU C CG  1 
ATOM 3684 C CD  . GLU C 1 39  ? 10.72628  9.25818   -15.33215 1.000 139.43695 ? 39  GLU C CD  1 
ATOM 3685 O OE1 . GLU C 1 39  ? 10.93275  8.50500   -14.35168 1.000 139.39691 ? 39  GLU C OE1 1 
ATOM 3686 O OE2 . GLU C 1 39  ? 9.65079   9.87189   -15.50916 1.000 139.81671 ? 39  GLU C OE2 1 
ATOM 3687 N N   . LEU C 1 40  ? 15.42041  6.88600   -15.92497 1.000 121.65202 ? 40  LEU C N   1 
ATOM 3688 C CA  . LEU C 1 40  ? 16.47662  6.32247   -15.08619 1.000 120.40513 ? 40  LEU C CA  1 
ATOM 3689 C C   . LEU C 1 40  ? 17.79477  6.21630   -15.84307 1.000 115.32410 ? 40  LEU C C   1 
ATOM 3690 O O   . LEU C 1 40  ? 18.86450  6.47372   -15.27658 1.000 110.44455 ? 40  LEU C O   1 
ATOM 3691 C CB  . LEU C 1 40  ? 16.04603  4.94887   -14.56761 1.000 115.91943 ? 40  LEU C CB  1 
ATOM 3692 C CG  . LEU C 1 40  ? 14.72044  4.96431   -13.80019 1.000 119.71280 ? 40  LEU C CG  1 
ATOM 3693 C CD1 . LEU C 1 40  ? 14.29252  3.56396   -13.40361 1.000 117.22070 ? 40  LEU C CD1 1 
ATOM 3694 C CD2 . LEU C 1 40  ? 14.78389  5.87613   -12.59540 1.000 116.49345 ? 40  LEU C CD2 1 
ATOM 3695 N N   . VAL C 1 41  ? 17.73374  5.83693   -17.12338 1.000 116.31033 ? 41  VAL C N   1 
ATOM 3696 C CA  . VAL C 1 41  ? 18.94670  5.61336   -17.89890 1.000 111.12809 ? 41  VAL C CA  1 
ATOM 3697 C C   . VAL C 1 41  ? 19.71721  6.90653   -18.08485 1.000 108.87818 ? 41  VAL C C   1 
ATOM 3698 O O   . VAL C 1 41  ? 20.94982  6.89771   -18.15302 1.000 103.87969 ? 41  VAL C O   1 
ATOM 3699 C CB  . VAL C 1 41  ? 18.59498  4.96126   -19.24152 1.000 113.79861 ? 41  VAL C CB  1 
ATOM 3700 C CG1 . VAL C 1 41  ? 17.96320  3.61201   -18.99352 1.000 111.73176 ? 41  VAL C CG1 1 
ATOM 3701 C CG2 . VAL C 1 41  ? 17.66367  5.86600   -20.04112 1.000 116.98185 ? 41  VAL C CG2 1 
ATOM 3702 N N   . SER C 1 42  ? 19.02273  8.03103   -18.18029 1.000 111.99195 ? 42  SER C N   1 
ATOM 3703 C CA  . SER C 1 42  ? 19.71141  9.30915   -18.13265 1.000 112.66865 ? 42  SER C CA  1 
ATOM 3704 C C   . SER C 1 42  ? 19.94027  9.79282   -16.70244 1.000 111.98928 ? 42  SER C C   1 
ATOM 3705 O O   . SER C 1 42  ? 20.54690  10.85080  -16.51271 1.000 113.53699 ? 42  SER C O   1 
ATOM 3706 C CB  . SER C 1 42  ? 18.95100  10.35230  -18.97143 1.000 107.32192 ? 42  SER C CB  1 
ATOM 3707 O OG  . SER C 1 42  ? 17.63056  10.56007  -18.51168 1.000 111.71402 ? 42  SER C OG  1 
ATOM 3708 N N   . ARG C 1 43  ? 19.49228  9.04934   -15.68800 1.000 110.37910 ? 43  ARG C N   1 
ATOM 3709 C CA  . ARG C 1 43  ? 19.87925  9.40061   -14.32609 1.000 112.42345 ? 43  ARG C CA  1 
ATOM 3710 C C   . ARG C 1 43  ? 21.10876  8.62838   -13.84297 1.000 112.44000 ? 43  ARG C C   1 
ATOM 3711 O O   . ARG C 1 43  ? 21.87769  9.15460   -13.02754 1.000 111.67571 ? 43  ARG C O   1 
ATOM 3712 C CB  . ARG C 1 43  ? 18.72515  9.18191   -13.33261 1.000 112.55203 ? 43  ARG C CB  1 
ATOM 3713 C CG  . ARG C 1 43  ? 19.06524  9.78582   -11.96365 1.000 110.28978 ? 43  ARG C CG  1 
ATOM 3714 C CD  . ARG C 1 43  ? 18.11081  9.48587   -10.79884 1.000 117.55914 ? 43  ARG C CD  1 
ATOM 3715 N NE  . ARG C 1 43  ? 16.77753  10.07125  -10.89608 1.000 124.74592 ? 43  ARG C NE  1 
ATOM 3716 C CZ  . ARG C 1 43  ? 15.64895  9.38106   -10.80412 1.000 125.35736 ? 43  ARG C CZ  1 
ATOM 3717 N NH1 . ARG C 1 43  ? 15.65478  8.07607   -10.59875 1.000 122.04322 ? 43  ARG C NH1 1 
ATOM 3718 N NH2 . ARG C 1 43  ? 14.48563  10.02267  -10.88042 1.000 129.94643 ? 43  ARG C NH2 1 
ATOM 3719 N N   . GLY C 1 44  ? 21.33084  7.39348   -14.32721 1.000 105.72543 ? 44  GLY C N   1 
ATOM 3720 C CA  . GLY C 1 44  ? 22.47856  6.62279   -13.89349 1.000 100.69932 ? 44  GLY C CA  1 
ATOM 3721 C C   . GLY C 1 44  ? 23.76094  6.93667   -14.65760 1.000 98.09987  ? 44  GLY C C   1 
ATOM 3722 O O   . GLY C 1 44  ? 23.73543  7.50840   -15.74475 1.000 101.13396 ? 44  GLY C O   1 
ATOM 3723 N N   . ILE C 1 45  ? 24.89959  6.54647   -14.07060 1.000 94.55670  ? 45  ILE C N   1 
ATOM 3724 C CA  . ILE C 1 45  ? 26.20945  6.74155   -14.68685 1.000 92.65422  ? 45  ILE C CA  1 
ATOM 3725 C C   . ILE C 1 45  ? 26.98261  5.43038   -14.63396 1.000 90.42426  ? 45  ILE C C   1 
ATOM 3726 O O   . ILE C 1 45  ? 26.75651  4.59267   -13.75401 1.000 90.40020  ? 45  ILE C O   1 
ATOM 3727 C CB  . ILE C 1 45  ? 27.01905  7.88327   -14.01739 1.000 91.80413  ? 45  ILE C CB  1 
ATOM 3728 C CG1 . ILE C 1 45  ? 27.35085  7.58155   -12.55255 1.000 93.60265  ? 45  ILE C CG1 1 
ATOM 3729 C CG2 . ILE C 1 45  ? 26.28358  9.21245   -14.13234 1.000 94.45386  ? 45  ILE C CG2 1 
ATOM 3730 C CD1 . ILE C 1 45  ? 28.71698  6.96359   -12.33446 1.000 90.37041  ? 45  ILE C CD1 1 
ATOM 3731 N N   . LYS C 1 46  ? 27.89274  5.24886   -15.59359 1.000 85.68958  ? 46  LYS C N   1 
ATOM 3732 C CA  . LYS C 1 46  ? 28.71426  4.04744   -15.68532 1.000 84.91459  ? 46  LYS C CA  1 
ATOM 3733 C C   . LYS C 1 46  ? 30.19004  4.42116   -15.67322 1.000 81.69985  ? 46  LYS C C   1 
ATOM 3734 O O   . LYS C 1 46  ? 30.61012  5.33900   -16.38626 1.000 80.40695  ? 46  LYS C O   1 
ATOM 3735 C CB  . LYS C 1 46  ? 28.38992  3.23864   -16.94290 1.000 88.17496  ? 46  LYS C CB  1 
ATOM 3736 N N   . ILE C 1 47  ? 30.97073  3.69221   -14.87611 1.000 81.14303  ? 47  ILE C N   1 
ATOM 3737 C CA  . ILE C 1 47  ? 32.38721  3.96397   -14.66130 1.000 78.02632  ? 47  ILE C CA  1 
ATOM 3738 C C   . ILE C 1 47  ? 33.16952  2.80140   -15.24264 1.000 79.11789  ? 47  ILE C C   1 
ATOM 3739 O O   . ILE C 1 47  ? 33.02736  1.66800   -14.77623 1.000 80.18063  ? 47  ILE C O   1 
ATOM 3740 C CB  . ILE C 1 47  ? 32.71107  4.12093   -13.17126 1.000 77.45795  ? 47  ILE C CB  1 
ATOM 3741 C CG1 . ILE C 1 47  ? 31.82286  5.19285   -12.53384 1.000 82.02756  ? 47  ILE C CG1 1 
ATOM 3742 C CG2 . ILE C 1 47  ? 34.17640  4.46278   -12.99793 1.000 73.60859  ? 47  ILE C CG2 1 
ATOM 3743 C CD1 . ILE C 1 47  ? 31.76678  5.13040   -11.00553 1.000 78.70044  ? 47  ILE C CD1 1 
ATOM 3744 N N   . LYS C 1 48  ? 33.99805  3.06993   -16.24872 1.000 79.23401  ? 48  LYS C N   1 
ATOM 3745 C CA  . LYS C 1 48  ? 34.80607  2.03356   -16.87625 1.000 77.31193  ? 48  LYS C CA  1 
ATOM 3746 C C   . LYS C 1 48  ? 36.19099  2.06055   -16.25254 1.000 77.44196  ? 48  LYS C C   1 
ATOM 3747 O O   . LYS C 1 48  ? 36.78907  3.13270   -16.12380 1.000 78.03068  ? 48  LYS C O   1 
ATOM 3748 C CB  . LYS C 1 48  ? 34.89301  2.24277   -18.39113 1.000 75.00073  ? 48  LYS C CB  1 
ATOM 3749 N N   . PHE C 1 49  ? 36.69697  0.89866   -15.84815 1.000 75.87231  ? 49  PHE C N   1 
ATOM 3750 C CA  . PHE C 1 49  ? 37.97713  0.86412   -15.15862 1.000 78.37107  ? 49  PHE C CA  1 
ATOM 3751 C C   . PHE C 1 49  ? 39.05061  0.34074   -16.10583 1.000 77.62714  ? 49  PHE C C   1 
ATOM 3752 O O   . PHE C 1 49  ? 38.79039  -0.53677  -16.93046 1.000 74.89230  ? 49  PHE C O   1 
ATOM 3753 C CB  . PHE C 1 49  ? 37.99666  0.00244   -13.86955 1.000 73.66978  ? 49  PHE C CB  1 
ATOM 3754 C CG  . PHE C 1 49  ? 36.91477  0.31639   -12.85235 1.000 73.00462  ? 49  PHE C CG  1 
ATOM 3755 C CD1 . PHE C 1 49  ? 35.61628  0.60508   -13.21155 1.000 78.41735  ? 49  PHE C CD1 1 
ATOM 3756 C CD2 . PHE C 1 49  ? 37.26683  0.52760   -11.53337 1.000 78.63945  ? 49  PHE C CD2 1 
ATOM 3757 C CE1 . PHE C 1 49  ? 34.64967  0.91750   -12.25684 1.000 75.74202  ? 49  PHE C CE1 1 
ATOM 3758 C CE2 . PHE C 1 49  ? 36.30824  0.88823   -10.57967 1.000 77.79228  ? 49  PHE C CE2 1 
ATOM 3759 C CZ  . PHE C 1 49  ? 35.00058  1.08113   -10.95519 1.000 72.79630  ? 49  PHE C CZ  1 
ATOM 3760 N N   . ASP C 1 50  ? 40.25974  0.87258   -15.96378 1.000 90.86265  ? 50  ASP C N   1 
ATOM 3761 C CA  . ASP C 1 50  ? 41.44467  0.40277   -16.68300 1.000 91.92698  ? 50  ASP C CA  1 
ATOM 3762 C C   . ASP C 1 50  ? 41.82871  -0.97866  -16.16801 1.000 91.11275  ? 50  ASP C C   1 
ATOM 3763 O O   . ASP C 1 50  ? 42.39819  -1.11210  -15.08788 1.000 95.21449  ? 50  ASP C O   1 
ATOM 3764 C CB  . ASP C 1 50  ? 42.57909  1.41508   -16.51326 1.000 95.32605  ? 50  ASP C CB  1 
ATOM 3765 C CG  . ASP C 1 50  ? 43.90207  0.97433   -17.16088 1.000 100.27470 ? 50  ASP C CG  1 
ATOM 3766 O OD1 . ASP C 1 50  ? 44.04232  -0.18779  -17.60318 1.000 100.57753 ? 50  ASP C OD1 1 
ATOM 3767 O OD2 . ASP C 1 50  ? 44.82234  1.81796   -17.24754 1.000 102.82400 ? 50  ASP C OD2 1 
ATOM 3768 N N   . LEU C 1 51  ? 41.54267  -2.01590  -16.95810 1.000 81.84637  ? 51  LEU C N   1 
ATOM 3769 C CA  . LEU C 1 51  ? 41.87411  -3.38078  -16.55005 1.000 81.01135  ? 51  LEU C CA  1 
ATOM 3770 C C   . LEU C 1 51  ? 43.38068  -3.60102  -16.44548 1.000 82.73915  ? 51  LEU C C   1 
ATOM 3771 O O   . LEU C 1 51  ? 43.84625  -4.28809  -15.52805 1.000 83.01133  ? 51  LEU C O   1 
ATOM 3772 C CB  . LEU C 1 51  ? 41.25903  -4.39131  -17.51902 1.000 78.94789  ? 51  LEU C CB  1 
ATOM 3773 C CG  . LEU C 1 51  ? 39.75225  -4.63331  -17.44830 1.000 74.76695  ? 51  LEU C CG  1 
ATOM 3774 C CD1 . LEU C 1 51  ? 39.30600  -5.51083  -18.60507 1.000 79.40878  ? 51  LEU C CD1 1 
ATOM 3775 C CD2 . LEU C 1 51  ? 39.42577  -5.29311  -16.16374 1.000 67.15721  ? 51  LEU C CD2 1 
ATOM 3776 N N   . LYS C 1 52  ? 44.15790  -3.04516  -17.38089 1.000 85.97527  ? 52  LYS C N   1 
ATOM 3777 C CA  . LYS C 1 52  ? 45.60142  -3.27607  -17.38468 1.000 83.85854  ? 52  LYS C CA  1 
ATOM 3778 C C   . LYS C 1 52  ? 46.23387  -2.86114  -16.05888 1.000 85.66948  ? 52  LYS C C   1 
ATOM 3779 O O   . LYS C 1 52  ? 47.02620  -3.61210  -15.47367 1.000 83.69271  ? 52  LYS C O   1 
ATOM 3780 C CB  . LYS C 1 52  ? 46.24719  -2.52325  -18.54886 1.000 82.07053  ? 52  LYS C CB  1 
ATOM 3781 N N   . SER C 1 53  ? 45.86451  -1.67801  -15.54783 1.000 84.17073  ? 53  SER C N   1 
ATOM 3782 C CA  . SER C 1 53  ? 46.47151  -1.16689  -14.32000 1.000 82.70980  ? 53  SER C CA  1 
ATOM 3783 C C   . SER C 1 53  ? 46.13715  -2.01199  -13.09021 1.000 87.57656  ? 53  SER C C   1 
ATOM 3784 O O   . SER C 1 53  ? 46.80971  -1.87071  -12.06517 1.000 88.32935  ? 53  SER C O   1 
ATOM 3785 C CB  . SER C 1 53  ? 46.03921  0.27345   -14.07238 1.000 82.61648  ? 53  SER C CB  1 
ATOM 3786 O OG  . SER C 1 53  ? 44.69131  0.32802   -13.64255 1.000 86.20227  ? 53  SER C OG  1 
ATOM 3787 N N   . GLN C 1 54  ? 45.12301  -2.88513  -13.16854 1.000 88.18051  ? 54  GLN C N   1 
ATOM 3788 C CA  . GLN C 1 54  ? 44.73717  -3.75652  -12.06649 1.000 82.50100  ? 54  GLN C CA  1 
ATOM 3789 C C   . GLN C 1 54  ? 45.57962  -5.02160  -11.98052 1.000 93.48411  ? 54  GLN C C   1 
ATOM 3790 O O   . GLN C 1 54  ? 45.47040  -5.73802  -10.97823 1.000 92.26489  ? 54  GLN C O   1 
ATOM 3791 C CB  . GLN C 1 54  ? 43.26819  -4.16472  -12.19626 1.000 75.29684  ? 54  GLN C CB  1 
ATOM 3792 C CG  . GLN C 1 54  ? 42.33188  -2.99780  -12.42944 1.000 75.03519  ? 54  GLN C CG  1 
ATOM 3793 C CD  . GLN C 1 54  ? 40.86911  -3.37720  -12.42330 1.000 69.28533  ? 54  GLN C CD  1 
ATOM 3794 O OE1 . GLN C 1 54  ? 40.49510  -4.45294  -11.97648 1.000 69.38691  ? 54  GLN C OE1 1 
ATOM 3795 N NE2 . GLN C 1 54  ? 40.04364  -2.52746  -13.01126 1.000 69.60171  ? 54  GLN C NE2 1 
ATOM 3796 N N   . LYS C 1 55  ? 46.38204  -5.33404  -13.00925 1.000 107.95325 ? 55  LYS C N   1 
ATOM 3797 C CA  . LYS C 1 55  ? 47.19637  -6.54912  -12.98695 1.000 107.01820 ? 55  LYS C CA  1 
ATOM 3798 C C   . LYS C 1 55  ? 48.11349  -6.55545  -11.77768 1.000 109.44380 ? 55  LYS C C   1 
ATOM 3799 O O   . LYS C 1 55  ? 48.75296  -5.54934  -11.45880 1.000 111.91545 ? 55  LYS C O   1 
ATOM 3800 C CB  . LYS C 1 55  ? 48.02372  -6.69198  -14.26793 1.000 104.76785 ? 55  LYS C CB  1 
ATOM 3801 C CG  . LYS C 1 55  ? 47.26558  -7.20248  -15.47213 1.000 105.98223 ? 55  LYS C CG  1 
ATOM 3802 C CD  . LYS C 1 55  ? 46.85001  -8.66290  -15.27005 1.000 107.78911 ? 55  LYS C CD  1 
ATOM 3803 C CE  . LYS C 1 55  ? 48.02962  -9.63929  -15.33268 1.000 113.49003 ? 55  LYS C CE  1 
ATOM 3804 N NZ  . LYS C 1 55  ? 47.59247  -11.07363 -15.23209 1.000 108.41918 ? 55  LYS C NZ  1 
ATOM 3805 N N   . GLY C 1 56  ? 48.16257  -7.69227  -11.09513 1.000 102.44709 ? 56  GLY C N   1 
ATOM 3806 C CA  . GLY C 1 56  ? 48.94556  -7.74856  -9.88753  1.000 101.00934 ? 56  GLY C CA  1 
ATOM 3807 C C   . GLY C 1 56  ? 48.39671  -6.92292  -8.75137  1.000 105.16235 ? 56  GLY C C   1 
ATOM 3808 O O   . GLY C 1 56  ? 49.12372  -6.67975  -7.78551  1.000 111.97131 ? 56  GLY C O   1 
ATOM 3809 N N   . HIS C 1 57  ? 47.13765  -6.45147  -8.84749  1.000 103.40920 ? 57  HIS C N   1 
ATOM 3810 C CA  . HIS C 1 57  ? 46.44391  -5.72269  -7.78028  1.000 103.56088 ? 57  HIS C CA  1 
ATOM 3811 C C   . HIS C 1 57  ? 45.05266  -6.27420  -7.47961  1.000 97.86897  ? 57  HIS C C   1 
ATOM 3812 O O   . HIS C 1 57  ? 44.64199  -6.28002  -6.31518  1.000 94.23071  ? 57  HIS C O   1 
ATOM 3813 C CB  . HIS C 1 57  ? 46.38112  -4.22964  -8.14652  1.000 105.36782 ? 57  HIS C CB  1 
ATOM 3814 C CG  . HIS C 1 57  ? 47.72733  -3.57789  -8.19100  1.000 110.22707 ? 57  HIS C CG  1 
ATOM 3815 N ND1 . HIS C 1 57  ? 48.56248  -3.67885  -9.28290  1.000 109.71273 ? 57  HIS C ND1 1 
ATOM 3816 C CD2 . HIS C 1 57  ? 48.38942  -2.82809  -7.27850  1.000 116.25661 ? 57  HIS C CD2 1 
ATOM 3817 C CE1 . HIS C 1 57  ? 49.68340  -3.02404  -9.04053  1.000 115.67954 ? 57  HIS C CE1 1 
ATOM 3818 N NE2 . HIS C 1 57  ? 49.60200  -2.49305  -7.83378  1.000 121.71303 ? 57  HIS C NE2 1 
ATOM 3819 N N   . ARG C 1 58  ? 44.31777  -6.73265  -8.49821  1.000 86.41182  ? 58  ARG C N   1 
ATOM 3820 C CA  . ARG C 1 58  ? 43.06857  -7.47236  -8.33919  1.000 77.79203  ? 58  ARG C CA  1 
ATOM 3821 C C   . ARG C 1 58  ? 43.17413  -8.77746  -9.12757  1.000 72.97364  ? 58  ARG C C   1 
ATOM 3822 O O   . ARG C 1 58  ? 44.19311  -9.05917  -9.75493  1.000 80.41776  ? 58  ARG C O   1 
ATOM 3823 C CB  . ARG C 1 58  ? 41.86588  -6.62876  -8.77600  1.000 70.94886  ? 58  ARG C CB  1 
ATOM 3824 C CG  . ARG C 1 58  ? 41.75586  -5.35650  -7.97982  1.000 68.20012  ? 58  ARG C CG  1 
ATOM 3825 C CD  . ARG C 1 58  ? 40.51453  -4.56504  -8.29118  1.000 65.59541  ? 58  ARG C CD  1 
ATOM 3826 N NE  . ARG C 1 58  ? 39.30755  -5.23533  -7.82657  1.000 63.77993  ? 58  ARG C NE  1 
ATOM 3827 C CZ  . ARG C 1 58  ? 38.91486  -5.25903  -6.56215  1.000 62.03804  ? 58  ARG C CZ  1 
ATOM 3828 N NH1 . ARG C 1 58  ? 39.65488  -4.73982  -5.60340  1.000 61.96391  ? 58  ARG C NH1 1 
ATOM 3829 N NH2 . ARG C 1 58  ? 37.77276  -5.85750  -6.24687  1.000 62.13890  ? 58  ARG C NH2 1 
ATOM 3830 N N   . LEU C 1 59  ? 42.12342  -9.58730  -9.10442  1.000 67.72107  ? 59  LEU C N   1 
ATOM 3831 C CA  . LEU C 1 59  ? 42.20640  -10.97236 -9.54430  1.000 68.63089  ? 59  LEU C CA  1 
ATOM 3832 C C   . LEU C 1 59  ? 41.46024  -11.17453 -10.85783 1.000 72.61034  ? 59  LEU C C   1 
ATOM 3833 O O   . LEU C 1 59  ? 40.28861  -10.79476 -10.97038 1.000 70.22861  ? 59  LEU C O   1 
ATOM 3834 C CB  . LEU C 1 59  ? 41.64093  -11.89696 -8.46824  1.000 70.15176  ? 59  LEU C CB  1 
ATOM 3835 C CG  . LEU C 1 59  ? 41.72071  -13.41750 -8.59696  1.000 74.65580  ? 59  LEU C CG  1 
ATOM 3836 C CD1 . LEU C 1 59  ? 43.16089  -13.89414 -8.53288  1.000 76.37383  ? 59  LEU C CD1 1 
ATOM 3837 C CD2 . LEU C 1 59  ? 40.88655  -14.06651 -7.50328  1.000 75.50984  ? 59  LEU C CD2 1 
ATOM 3838 N N   . PHE C 1 60  ? 42.15056  -11.77974 -11.83916 1.000 73.65010  ? 60  PHE C N   1 
ATOM 3839 C CA  . PHE C 1 60  ? 41.59343  -12.23781 -13.11698 1.000 76.04372  ? 60  PHE C CA  1 
ATOM 3840 C C   . PHE C 1 60  ? 41.47675  -13.75904 -13.07390 1.000 81.46636  ? 60  PHE C C   1 
ATOM 3841 O O   . PHE C 1 60  ? 42.49356  -14.44895 -12.96681 1.000 87.02255  ? 60  PHE C O   1 
ATOM 3842 C CB  . PHE C 1 60  ? 42.50398  -11.85506 -14.28704 1.000 71.48371  ? 60  PHE C CB  1 
ATOM 3843 C CG  . PHE C 1 60  ? 42.63864  -10.38796 -14.52291 1.000 72.92988  ? 60  PHE C CG  1 
ATOM 3844 C CD1 . PHE C 1 60  ? 41.75717  -9.72195  -15.34194 1.000 75.07016  ? 60  PHE C CD1 1 
ATOM 3845 C CD2 . PHE C 1 60  ? 43.66016  -9.67107  -13.93036 1.000 77.47297  ? 60  PHE C CD2 1 
ATOM 3846 C CE1 . PHE C 1 60  ? 41.90054  -8.36125  -15.57206 1.000 76.28960  ? 60  PHE C CE1 1 
ATOM 3847 C CE2 . PHE C 1 60  ? 43.79406  -8.32585  -14.14557 1.000 78.98609  ? 60  PHE C CE2 1 
ATOM 3848 C CZ  . PHE C 1 60  ? 42.92152  -7.66871  -14.97460 1.000 75.58167  ? 60  PHE C CZ  1 
ATOM 3849 N N   . THR C 1 61  ? 40.26842  -14.29168 -13.20596 1.000 87.24172  ? 61  THR C N   1 
ATOM 3850 C CA  . THR C 1 61  ? 40.05313  -15.71987 -12.99349 1.000 90.87933  ? 61  THR C CA  1 
ATOM 3851 C C   . THR C 1 61  ? 39.88692  -16.45777 -14.31838 1.000 95.16494  ? 61  THR C C   1 
ATOM 3852 O O   . THR C 1 61  ? 39.15478  -16.00291 -15.19903 1.000 97.81913  ? 61  THR C O   1 
ATOM 3853 C CB  . THR C 1 61  ? 38.82226  -15.95570 -12.11476 1.000 91.84275  ? 61  THR C CB  1 
ATOM 3854 O OG1 . THR C 1 61  ? 38.96813  -15.23668 -10.87783 1.000 90.30916  ? 61  THR C OG1 1 
ATOM 3855 C CG2 . THR C 1 61  ? 38.63860  -17.44946 -11.83351 1.000 92.16685  ? 61  THR C CG2 1 
ATOM 3856 N N   . LYS C 1 62  ? 40.55066  -17.61867 -14.44302 1.000 94.44464  ? 62  LYS C N   1 
ATOM 3857 C CA  . LYS C 1 62  ? 40.46136  -18.41621 -15.67138 1.000 90.77815  ? 62  LYS C CA  1 
ATOM 3858 C C   . LYS C 1 62  ? 39.02407  -18.83922 -15.96721 1.000 93.89113  ? 62  LYS C C   1 
ATOM 3859 O O   . LYS C 1 62  ? 38.57149  -18.76458 -17.11520 1.000 94.84032  ? 62  LYS C O   1 
ATOM 3860 C CB  . LYS C 1 62  ? 41.36406  -19.65344 -15.57743 1.000 83.04126  ? 62  LYS C CB  1 
ATOM 3861 C CG  . LYS C 1 62  ? 42.72578  -19.51862 -16.23942 1.000 82.58089  ? 62  LYS C CG  1 
ATOM 3862 C CD  . LYS C 1 62  ? 43.61368  -18.47385 -15.59769 1.000 82.59573  ? 62  LYS C CD  1 
ATOM 3863 C CE  . LYS C 1 62  ? 44.84060  -18.21415 -16.44862 1.000 86.65023  ? 62  LYS C CE  1 
ATOM 3864 N NZ  . LYS C 1 62  ? 45.61430  -19.46469 -16.71430 1.000 94.76121  ? 62  LYS C NZ  1 
ATOM 3865 N N   . SER C 1 63  ? 38.28921  -19.28540 -14.94285 1.000 94.32127  ? 63  SER C N   1 
ATOM 3866 C CA  . SER C 1 63  ? 36.91611  -19.73908 -15.14126 1.000 95.12279  ? 63  SER C CA  1 
ATOM 3867 C C   . SER C 1 63  ? 35.98086  -18.60239 -15.53960 1.000 96.69447  ? 63  SER C C   1 
ATOM 3868 O O   . SER C 1 63  ? 34.89132  -18.86250 -16.06423 1.000 96.24593  ? 63  SER C O   1 
ATOM 3869 C CB  . SER C 1 63  ? 36.41355  -20.43393 -13.87092 1.000 99.03343  ? 63  SER C CB  1 
ATOM 3870 O OG  . SER C 1 63  ? 36.37888  -19.54265 -12.76628 1.000 103.36090 ? 63  SER C OG  1 
ATOM 3871 N N   . THR C 1 64  ? 36.37552  -17.35227 -15.29057 1.000 98.31339  ? 64  THR C N   1 
ATOM 3872 C CA  . THR C 1 64  ? 35.60293  -16.19594 -15.72356 1.000 99.14738  ? 64  THR C CA  1 
ATOM 3873 C C   . THR C 1 64  ? 36.16913  -15.51642 -16.97450 1.000 95.98140  ? 64  THR C C   1 
ATOM 3874 O O   . THR C 1 64  ? 35.41808  -14.83397 -17.67337 1.000 96.60360  ? 64  THR C O   1 
ATOM 3875 C CB  . THR C 1 64  ? 35.46852  -15.17693 -14.56572 1.000 90.31410  ? 64  THR C CB  1 
ATOM 3876 O OG1 . THR C 1 64  ? 36.75465  -14.84584 -14.04656 1.000 87.79723  ? 64  THR C OG1 1 
ATOM 3877 C CG2 . THR C 1 64  ? 34.61295  -15.72294 -13.42493 1.000 88.92337  ? 64  THR C CG2 1 
ATOM 3878 N N   . ILE C 1 65  ? 37.46143  -15.67287 -17.27673 1.000 94.00523  ? 65  ILE C N   1 
ATOM 3879 C CA  . ILE C 1 65  ? 37.98413  -15.17194 -18.54648 1.000 98.25548  ? 65  ILE C CA  1 
ATOM 3880 C C   . ILE C 1 65  ? 37.48957  -16.02942 -19.70931 1.000 109.20889 ? 65  ILE C C   1 
ATOM 3881 O O   . ILE C 1 65  ? 37.13891  -15.51198 -20.77909 1.000 107.25516 ? 65  ILE C O   1 
ATOM 3882 C CB  . ILE C 1 65  ? 39.52212  -15.11321 -18.53051 1.000 94.77874  ? 65  ILE C CB  1 
ATOM 3883 C CG1 . ILE C 1 65  ? 40.03890  -14.11646 -17.50275 1.000 87.50487  ? 65  ILE C CG1 1 
ATOM 3884 C CG2 . ILE C 1 65  ? 40.04546  -14.73819 -19.91550 1.000 92.10923  ? 65  ILE C CG2 1 
ATOM 3885 C CD1 . ILE C 1 65  ? 41.53295  -14.21704 -17.29899 1.000 79.17945  ? 65  ILE C CD1 1 
ATOM 3886 N N   . GLU C 1 66  ? 37.48552  -17.35643 -19.53597 1.000 117.58094 ? 66  GLU C N   1 
ATOM 3887 C CA  . GLU C 1 66  ? 36.98646  -18.21709 -20.59920 1.000 118.64439 ? 66  GLU C CA  1 
ATOM 3888 C C   . GLU C 1 66  ? 35.49167  -18.01740 -20.79980 1.000 120.12369 ? 66  GLU C C   1 
ATOM 3889 O O   . GLU C 1 66  ? 34.99558  -18.16769 -21.92241 1.000 121.27574 ? 66  GLU C O   1 
ATOM 3890 C CB  . GLU C 1 66  ? 37.31462  -19.68274 -20.30552 1.000 118.56001 ? 66  GLU C CB  1 
ATOM 3891 C CG  . GLU C 1 66  ? 37.08342  -20.61681 -21.50417 1.000 124.74664 ? 66  GLU C CG  1 
ATOM 3892 C CD  . GLU C 1 66  ? 37.60444  -22.03238 -21.27208 1.000 130.39566 ? 66  GLU C CD  1 
ATOM 3893 O OE1 . GLU C 1 66  ? 38.05248  -22.31819 -20.13961 1.000 137.82291 ? 66  GLU C OE1 1 
ATOM 3894 O OE2 . GLU C 1 66  ? 37.59586  -22.84932 -22.22332 1.000 121.76819 ? 66  GLU C OE2 1 
ATOM 3895 N N   . TRP C 1 67  ? 34.76717  -17.65394 -19.73562 1.000 111.28107 ? 67  TRP C N   1 
ATOM 3896 C CA  . TRP C 1 67  ? 33.35758  -17.29455 -19.87705 1.000 112.90687 ? 67  TRP C CA  1 
ATOM 3897 C C   . TRP C 1 67  ? 33.17088  -16.16727 -20.88419 1.000 112.01495 ? 67  TRP C C   1 
ATOM 3898 O O   . TRP C 1 67  ? 32.32292  -16.25540 -21.77848 1.000 115.41208 ? 67  TRP C O   1 
ATOM 3899 C CB  . TRP C 1 67  ? 32.76578  -16.85431 -18.53923 1.000 108.93931 ? 67  TRP C CB  1 
ATOM 3900 C CG  . TRP C 1 67  ? 31.29521  -16.55384 -18.64690 1.000 110.66909 ? 67  TRP C CG  1 
ATOM 3901 C CD1 . TRP C 1 67  ? 30.26485  -17.43739 -18.51134 1.000 113.30118 ? 67  TRP C CD1 1 
ATOM 3902 C CD2 . TRP C 1 67  ? 30.70142  -15.30980 -19.05066 1.000 113.84735 ? 67  TRP C CD2 1 
ATOM 3903 N NE1 . TRP C 1 67  ? 29.06424  -16.80293 -18.71968 1.000 113.66955 ? 67  TRP C NE1 1 
ATOM 3904 C CE2 . TRP C 1 67  ? 29.30545  -15.49875 -19.06473 1.000 116.45814 ? 67  TRP C CE2 1 
ATOM 3905 C CE3 . TRP C 1 67  ? 31.21438  -14.04446 -19.36903 1.000 108.49888 ? 67  TRP C CE3 1 
ATOM 3906 C CZ2 . TRP C 1 67  ? 28.41530  -14.47114 -19.38867 1.000 119.32831 ? 67  TRP C CZ2 1 
ATOM 3907 C CZ3 . TRP C 1 67  ? 30.33128  -13.02661 -19.69310 1.000 108.19116 ? 67  TRP C CZ3 1 
ATOM 3908 C CH2 . TRP C 1 67  ? 28.94716  -13.24560 -19.69903 1.000 115.41047 ? 67  TRP C CH2 1 
ATOM 3909 N N   . TRP C 1 68  ? 33.92761  -15.07289 -20.72398 1.000 108.90585 ? 68  TRP C N   1 
ATOM 3910 C CA  . TRP C 1 68  ? 33.74866  -13.92995 -21.61283 1.000 109.82617 ? 68  TRP C CA  1 
ATOM 3911 C C   . TRP C 1 68  ? 34.00007  -14.31168 -23.06063 1.000 112.61686 ? 68  TRP C C   1 
ATOM 3912 O O   . TRP C 1 68  ? 33.40447  -13.72164 -23.96633 1.000 112.99703 ? 68  TRP C O   1 
ATOM 3913 C CB  . TRP C 1 68  ? 34.66559  -12.76407 -21.22493 1.000 103.39610 ? 68  TRP C CB  1 
ATOM 3914 C CG  . TRP C 1 68  ? 34.28187  -11.97717 -19.98749 1.000 98.00926  ? 68  TRP C CG  1 
ATOM 3915 C CD1 . TRP C 1 68  ? 34.85713  -12.06124 -18.75183 1.000 95.99656  ? 68  TRP C CD1 1 
ATOM 3916 C CD2 . TRP C 1 68  ? 33.25945  -10.97357 -19.88260 1.000 94.68678  ? 68  TRP C CD2 1 
ATOM 3917 N NE1 . TRP C 1 68  ? 34.25756  -11.18244 -17.88602 1.000 91.16000  ? 68  TRP C NE1 1 
ATOM 3918 C CE2 . TRP C 1 68  ? 33.27422  -10.50080 -18.55326 1.000 91.22511  ? 68  TRP C CE2 1 
ATOM 3919 C CE3 . TRP C 1 68  ? 32.33646  -10.42864 -20.78291 1.000 95.87269  ? 68  TRP C CE3 1 
ATOM 3920 C CZ2 . TRP C 1 68  ? 32.39860  -9.51113  -18.09849 1.000 88.65295  ? 68  TRP C CZ2 1 
ATOM 3921 C CZ3 . TRP C 1 68  ? 31.46631  -9.45142  -20.33138 1.000 95.42036  ? 68  TRP C CZ3 1 
ATOM 3922 C CH2 . TRP C 1 68  ? 31.50294  -9.00198  -18.99704 1.000 90.90766  ? 68  TRP C CH2 1 
ATOM 3923 N N   . LYS C 1 69  ? 34.85896  -15.30562 -23.29556 1.000 113.13844 ? 69  LYS C N   1 
ATOM 3924 C CA  . LYS C 1 69  ? 35.22736  -15.66270 -24.65828 1.000 116.00897 ? 69  LYS C CA  1 
ATOM 3925 C C   . LYS C 1 69  ? 34.04517  -16.18983 -25.45641 1.000 117.81902 ? 69  LYS C C   1 
ATOM 3926 O O   . LYS C 1 69  ? 34.09724  -16.18880 -26.69151 1.000 117.02637 ? 69  LYS C O   1 
ATOM 3927 C CB  . LYS C 1 69  ? 36.35414  -16.69695 -24.64615 1.000 114.36920 ? 69  LYS C CB  1 
ATOM 3928 C CG  . LYS C 1 69  ? 37.62615  -16.20156 -23.97902 1.000 110.17200 ? 69  LYS C CG  1 
ATOM 3929 C CD  . LYS C 1 69  ? 38.80608  -17.06104 -24.35791 1.000 104.97080 ? 69  LYS C CD  1 
ATOM 3930 C CE  . LYS C 1 69  ? 38.70532  -18.43236 -23.76926 1.000 108.60187 ? 69  LYS C CE  1 
ATOM 3931 N NZ  . LYS C 1 69  ? 39.91268  -19.21487 -24.10776 1.000 110.92884 ? 69  LYS C NZ  1 
ATOM 3932 N N   . ASN C 1 70  ? 32.97757  -16.61828 -24.78159 1.000 117.02007 ? 70  ASN C N   1 
ATOM 3933 C CA  . ASN C 1 70  ? 31.81698  -17.18069 -25.45728 1.000 120.25851 ? 70  ASN C CA  1 
ATOM 3934 C C   . ASN C 1 70  ? 30.86128  -16.12359 -25.99110 1.000 125.81458 ? 70  ASN C C   1 
ATOM 3935 O O   . ASN C 1 70  ? 29.88331  -16.48191 -26.65803 1.000 130.67619 ? 70  ASN C O   1 
ATOM 3936 C CB  . ASN C 1 70  ? 31.03864  -18.09535 -24.50816 1.000 116.93483 ? 70  ASN C CB  1 
ATOM 3937 C CG  . ASN C 1 70  ? 31.84593  -19.28769 -24.06221 1.000 120.59106 ? 70  ASN C CG  1 
ATOM 3938 O OD1 . ASN C 1 70  ? 32.62729  -19.84195 -24.83494 1.000 124.96249 ? 70  ASN C OD1 1 
ATOM 3939 N ND2 . ASN C 1 70  ? 31.65349  -19.70378 -22.81382 1.000 118.69159 ? 70  ASN C ND2 1 
ATOM 3940 N N   . GLN C 1 71  ? 31.11509  -14.84572 -25.73344 1.000 126.83172 ? 71  GLN C N   1 
ATOM 3941 C CA  . GLN C 1 71  ? 30.05716  -13.84805 -25.75951 1.000 131.14905 ? 71  GLN C CA  1 
ATOM 3942 C C   . GLN C 1 71  ? 30.02891  -13.06207 -27.06554 1.000 136.30867 ? 71  GLN C C   1 
ATOM 3943 O O   . GLN C 1 71  ? 31.02530  -12.96274 -27.78881 1.000 132.84867 ? 71  GLN C O   1 
ATOM 3944 C CB  . GLN C 1 71  ? 30.21097  -12.89701 -24.57498 1.000 124.16069 ? 71  GLN C CB  1 
ATOM 3945 C CG  . GLN C 1 71  ? 30.31159  -13.64106 -23.27438 1.000 117.92850 ? 71  GLN C CG  1 
ATOM 3946 C CD  . GLN C 1 71  ? 29.12838  -14.55277 -23.03174 1.000 121.91421 ? 71  GLN C CD  1 
ATOM 3947 O OE1 . GLN C 1 71  ? 28.00207  -14.24598 -23.42394 1.000 127.58044 ? 71  GLN C OE1 1 
ATOM 3948 N NE2 . GLN C 1 71  ? 29.37260  -15.67320 -22.35353 1.000 120.10790 ? 71  GLN C NE2 1 
ATOM 3949 N N   . SER C 1 72  ? 28.85723  -12.48769 -27.34117 1.000 155.50067 ? 72  SER C N   1 
ATOM 3950 C CA  . SER C 1 72  ? 28.65886  -11.71431 -28.55594 1.000 154.22147 ? 72  SER C CA  1 
ATOM 3951 C C   . SER C 1 72  ? 29.67133  -10.57691 -28.61433 1.000 151.15991 ? 72  SER C C   1 
ATOM 3952 O O   . SER C 1 72  ? 30.01035  -9.99430  -27.58247 1.000 152.61254 ? 72  SER C O   1 
ATOM 3953 C CB  . SER C 1 72  ? 27.23988  -11.14275 -28.60541 1.000 153.65252 ? 72  SER C CB  1 
ATOM 3954 O OG  . SER C 1 72  ? 27.06820  -10.30621 -29.74004 1.000 155.93891 ? 72  SER C OG  1 
ATOM 3955 N N   . PRO C 1 73  ? 30.18665  -10.24478 -29.79087 1.000 132.65605 ? 73  PRO C N   1 
ATOM 3956 C CA  . PRO C 1 73  ? 31.12276  -9.11924  -29.87219 1.000 130.33381 ? 73  PRO C CA  1 
ATOM 3957 C C   . PRO C 1 73  ? 30.53300  -7.80875  -29.37740 1.000 129.15398 ? 73  PRO C C   1 
ATOM 3958 O O   . PRO C 1 73  ? 31.29530  -6.92130  -28.97411 1.000 126.78778 ? 73  PRO C O   1 
ATOM 3959 C CB  . PRO C 1 73  ? 31.47605  -9.07154  -31.36213 1.000 129.45601 ? 73  PRO C CB  1 
ATOM 3960 C CG  . PRO C 1 73  ? 31.27510  -10.48813 -31.81838 1.000 125.16003 ? 73  PRO C CG  1 
ATOM 3961 C CD  . PRO C 1 73  ? 30.09233  -10.98763 -31.05528 1.000 128.87260 ? 73  PRO C CD  1 
ATOM 3962 N N   . GLU C 1 74  ? 29.20503  -7.65659  -29.38407 1.000 129.93299 ? 74  GLU C N   1 
ATOM 3963 C CA  . GLU C 1 74  ? 28.59377  -6.52575  -28.68916 1.000 129.34748 ? 74  GLU C CA  1 
ATOM 3964 C C   . GLU C 1 74  ? 29.02124  -6.49339  -27.22700 1.000 128.64009 ? 74  GLU C C   1 
ATOM 3965 O O   . GLU C 1 74  ? 29.20718  -5.41797  -26.64668 1.000 130.77510 ? 74  GLU C O   1 
ATOM 3966 C CB  . GLU C 1 74  ? 27.06799  -6.59373  -28.79151 1.000 130.23838 ? 74  GLU C CB  1 
ATOM 3967 N N   . ALA C 1 75  ? 29.18114  -7.66908  -26.61405 1.000 131.42169 ? 75  ALA C N   1 
ATOM 3968 C CA  . ALA C 1 75  ? 29.64522  -7.73793  -25.23228 1.000 122.22438 ? 75  ALA C CA  1 
ATOM 3969 C C   . ALA C 1 75  ? 31.11467  -7.35511  -25.10129 1.000 118.62439 ? 75  ALA C C   1 
ATOM 3970 O O   . ALA C 1 75  ? 31.51999  -6.81487  -24.06991 1.000 115.69778 ? 75  ALA C O   1 
ATOM 3971 C CB  . ALA C 1 75  ? 29.41585  -9.14022  -24.67069 1.000 120.67180 ? 75  ALA C CB  1 
ATOM 3972 N N   . ARG C 1 76  ? 31.92163  -7.61270  -26.12543 1.000 119.41403 ? 76  ARG C N   1 
ATOM 3973 C CA  . ARG C 1 76  ? 33.36120  -7.40001  -26.04519 1.000 115.96381 ? 76  ARG C CA  1 
ATOM 3974 C C   . ARG C 1 76  ? 33.75222  -5.94951  -26.27899 1.000 109.84527 ? 76  ARG C C   1 
ATOM 3975 O O   . ARG C 1 76  ? 34.92065  -5.58941  -26.09222 1.000 101.88355 ? 76  ARG C O   1 
ATOM 3976 C CB  . ARG C 1 76  ? 34.04281  -8.32518  -27.05155 1.000 121.23341 ? 76  ARG C CB  1 
ATOM 3977 C CG  . ARG C 1 76  ? 35.55340  -8.46161  -26.98506 1.000 118.56301 ? 76  ARG C CG  1 
ATOM 3978 C CD  . ARG C 1 76  ? 35.90157  -9.69130  -27.79727 1.000 121.08398 ? 76  ARG C CD  1 
ATOM 3979 N NE  . ARG C 1 76  ? 35.24343  -10.85519 -27.20172 1.000 124.04279 ? 76  ARG C NE  1 
ATOM 3980 C CZ  . ARG C 1 76  ? 34.21238  -11.49859 -27.73951 1.000 125.74550 ? 76  ARG C CZ  1 
ATOM 3981 N NH1 . ARG C 1 76  ? 33.68995  -11.12441 -28.89855 1.000 127.58190 ? 76  ARG C NH1 1 
ATOM 3982 N NH2 . ARG C 1 76  ? 33.68400  -12.53418 -27.09294 1.000 121.50054 ? 76  ARG C NH2 1 
ATOM 3983 N N   . LYS C 1 77  ? 32.80313  -5.10958  -26.67551 1.000 111.89545 ? 77  LYS C N   1 
ATOM 3984 C CA  . LYS C 1 77  ? 33.06897  -3.68292  -26.72147 1.000 113.01096 ? 77  LYS C CA  1 
ATOM 3985 C C   . LYS C 1 77  ? 33.10989  -3.06475  -25.32840 1.000 107.31345 ? 77  LYS C C   1 
ATOM 3986 O O   . LYS C 1 77  ? 33.42869  -1.87557  -25.20509 1.000 101.52545 ? 77  LYS C O   1 
ATOM 3987 C CB  . LYS C 1 77  ? 32.02495  -2.98488  -27.60186 1.000 117.91192 ? 77  LYS C CB  1 
ATOM 3988 N N   . ASN C 1 78  ? 32.77908  -3.83144  -24.28242 1.000 109.43625 ? 78  ASN C N   1 
ATOM 3989 C CA  . ASN C 1 78  ? 33.01457  -3.36577  -22.91613 1.000 104.80952 ? 78  ASN C CA  1 
ATOM 3990 C C   . ASN C 1 78  ? 34.47695  -3.54013  -22.52048 1.000 97.65853  ? 78  ASN C C   1 
ATOM 3991 O O   . ASN C 1 78  ? 35.19449  -2.56175  -22.29385 1.000 95.94412  ? 78  ASN C O   1 
ATOM 3992 C CB  . ASN C 1 78  ? 32.13454  -4.11993  -21.90969 1.000 108.24483 ? 78  ASN C CB  1 
ATOM 3993 C CG  . ASN C 1 78  ? 30.65608  -3.91795  -22.14751 1.000 112.14004 ? 78  ASN C CG  1 
ATOM 3994 O OD1 . ASN C 1 78  ? 30.24036  -2.89512  -22.69706 1.000 114.13736 ? 78  ASN C OD1 1 
ATOM 3995 N ND2 . ASN C 1 78  ? 29.84132  -4.86503  -21.66538 1.000 110.15973 ? 78  ASN C ND2 1 
ATOM 3996 N N   . ILE C 1 79  ? 34.93916  -4.79136  -22.46144 1.000 98.91586  ? 79  ILE C N   1 
ATOM 3997 C CA  . ILE C 1 79  ? 36.26685  -5.09429  -21.94111 1.000 98.21643  ? 79  ILE C CA  1 
ATOM 3998 C C   . ILE C 1 79  ? 37.35826  -4.45829  -22.79722 1.000 97.46065  ? 79  ILE C C   1 
ATOM 3999 O O   . ILE C 1 79  ? 38.49598  -4.30068  -22.33821 1.000 94.65592  ? 79  ILE C O   1 
ATOM 4000 C CB  . ILE C 1 79  ? 36.45546  -6.62846  -21.84023 1.000 97.00161  ? 79  ILE C CB  1 
ATOM 4001 C CG1 . ILE C 1 79  ? 36.62429  -7.24984  -23.22209 1.000 96.04257  ? 79  ILE C CG1 1 
ATOM 4002 C CG2 . ILE C 1 79  ? 35.23979  -7.27632  -21.20063 1.000 89.98450  ? 79  ILE C CG2 1 
ATOM 4003 C CD1 . ILE C 1 79  ? 37.06132  -8.68464  -23.17480 1.000 99.12151  ? 79  ILE C CD1 1 
ATOM 4004 N N   . ALA C 1 80  ? 37.03018  -4.09035  -24.03642 1.000 99.64393  ? 80  ALA C N   1 
ATOM 4005 C CA  . ALA C 1 80  ? 37.96904  -3.42007  -24.92058 1.000 91.05668  ? 80  ALA C CA  1 
ATOM 4006 C C   . ALA C 1 80  ? 38.37863  -2.06860  -24.33550 1.000 94.17014  ? 80  ALA C C   1 
ATOM 4007 O O   . ALA C 1 80  ? 37.50414  -1.25313  -23.99130 1.000 92.55709  ? 80  ALA C O   1 
ATOM 4008 C CB  . ALA C 1 80  ? 37.33051  -3.23078  -26.29117 1.000 92.81938  ? 80  ALA C CB  1 
ATOM 4009 N N   . PRO C 1 81  ? 39.67929  -1.78447  -24.22625 1.000 92.40791  ? 81  PRO C N   1 
ATOM 4010 C CA  . PRO C 1 81  ? 40.13175  -0.55293  -23.56233 1.000 87.21496  ? 81  PRO C CA  1 
ATOM 4011 C C   . PRO C 1 81  ? 39.57169  0.70604   -24.20280 1.000 87.17569  ? 81  PRO C C   1 
ATOM 4012 O O   . PRO C 1 81  ? 39.00152  0.70563   -25.29351 1.000 94.54901  ? 81  PRO C O   1 
ATOM 4013 C CB  . PRO C 1 81  ? 41.65508  -0.61487  -23.69658 1.000 81.16303  ? 81  PRO C CB  1 
ATOM 4014 C CG  . PRO C 1 81  ? 41.94992  -2.06457  -23.79716 1.000 88.07421  ? 81  PRO C CG  1 
ATOM 4015 C CD  . PRO C 1 81  ? 40.80519  -2.67403  -24.55732 1.000 91.92860  ? 81  PRO C CD  1 
ATOM 4016 N N   . SER C 1 82  ? 39.74646  1.80493   -23.48255 1.000 84.86543  ? 82  SER C N   1 
ATOM 4017 C CA  . SER C 1 82  ? 39.16329  3.08630   -23.83619 1.000 89.38610  ? 82  SER C CA  1 
ATOM 4018 C C   . SER C 1 82  ? 40.03475  4.18556   -23.24872 1.000 96.52006  ? 82  SER C C   1 
ATOM 4019 O O   . SER C 1 82  ? 40.52481  4.05569   -22.12441 1.000 98.04612  ? 82  SER C O   1 
ATOM 4020 C CB  . SER C 1 82  ? 37.72295  3.18074   -23.31856 1.000 85.02630  ? 82  SER C CB  1 
ATOM 4021 O OG  . SER C 1 82  ? 37.20895  4.49636   -23.38566 1.000 89.43011  ? 82  SER C OG  1 
ATOM 4022 N N   . ASP C 1 83  ? 40.23974  5.26235   -24.01238 1.000 101.99417 ? 83  ASP C N   1 
ATOM 4023 C CA  . ASP C 1 83  ? 40.92483  6.41745   -23.44677 1.000 101.83079 ? 83  ASP C CA  1 
ATOM 4024 C C   . ASP C 1 83  ? 40.13989  7.00232   -22.27468 1.000 103.80303 ? 83  ASP C C   1 
ATOM 4025 O O   . ASP C 1 83  ? 40.72635  7.65474   -21.39733 1.000 103.30934 ? 83  ASP C O   1 
ATOM 4026 C CB  . ASP C 1 83  ? 41.15582  7.46950   -24.53130 1.000 107.19803 ? 83  ASP C CB  1 
ATOM 4027 C CG  . ASP C 1 83  ? 42.02223  6.94837   -25.66786 1.000 114.71371 ? 83  ASP C CG  1 
ATOM 4028 O OD1 . ASP C 1 83  ? 42.76605  5.96760   -25.44363 1.000 115.25894 ? 83  ASP C OD1 1 
ATOM 4029 O OD2 . ASP C 1 83  ? 41.97248  7.52629   -26.78049 1.000 115.78275 ? 83  ASP C OD2 1 
ATOM 4030 N N   . GLU C 1 84  ? 38.82783  6.74725   -22.23702 1.000 97.07640  ? 84  GLU C N   1 
ATOM 4031 C CA  . GLU C 1 84  ? 37.93204  7.16240   -21.16538 1.000 96.60918  ? 84  GLU C CA  1 
ATOM 4032 C C   . GLU C 1 84  ? 37.87159  6.15564   -20.01106 1.000 89.93566  ? 84  GLU C C   1 
ATOM 4033 O O   . GLU C 1 84  ? 36.81400  6.00500   -19.39099 1.000 79.40587  ? 84  GLU C O   1 
ATOM 4034 C CB  . GLU C 1 84  ? 36.53550  7.41790   -21.73664 1.000 96.73494  ? 84  GLU C CB  1 
ATOM 4035 N N   . ASP C 1 85  ? 38.95230  5.41131   -19.76606 1.000 87.40659  ? 85  ASP C N   1 
ATOM 4036 C CA  . ASP C 1 85  ? 39.10075  4.57503   -18.58067 1.000 83.76399  ? 85  ASP C CA  1 
ATOM 4037 C C   . ASP C 1 85  ? 39.59068  5.38358   -17.37755 1.000 85.40942  ? 85  ASP C C   1 
ATOM 4038 O O   . ASP C 1 85  ? 40.09508  6.50552   -17.50818 1.000 87.31563  ? 85  ASP C O   1 
ATOM 4039 C CB  . ASP C 1 85  ? 40.08906  3.43933   -18.82121 1.000 84.34005  ? 85  ASP C CB  1 
ATOM 4040 C CG  . ASP C 1 85  ? 39.58010  2.43138   -19.80483 1.000 84.10985  ? 85  ASP C CG  1 
ATOM 4041 O OD1 . ASP C 1 85  ? 38.33902  2.32826   -19.94148 1.000 83.27150  ? 85  ASP C OD1 1 
ATOM 4042 O OD2 . ASP C 1 85  ? 40.42584  1.73983   -20.41662 1.000 82.74561  ? 85  ASP C OD2 1 
ATOM 4043 N N   . VAL C 1 86  ? 39.43716  4.78539   -16.18530 1.000 85.28350  ? 86  VAL C N   1 
ATOM 4044 C CA  . VAL C 1 86  ? 39.88563  5.36797   -14.92421 1.000 76.85560  ? 86  VAL C CA  1 
ATOM 4045 C C   . VAL C 1 86  ? 40.40376  4.25961   -14.01525 1.000 78.64260  ? 86  VAL C C   1 
ATOM 4046 O O   . VAL C 1 86  ? 39.92326  3.12344   -14.05361 1.000 79.34359  ? 86  VAL C O   1 
ATOM 4047 C CB  . VAL C 1 86  ? 38.75923  6.14443   -14.22383 1.000 79.75986  ? 86  VAL C CB  1 
ATOM 4048 C CG1 . VAL C 1 86  ? 38.21732  7.24762   -15.12291 1.000 76.15697  ? 86  VAL C CG1 1 
ATOM 4049 C CG2 . VAL C 1 86  ? 37.65132  5.20232   -13.78719 1.000 77.55394  ? 86  VAL C CG2 1 
ATOM 4050 N N   . SER C 1 87  ? 41.39670  4.59420   -13.19210 1.000 80.50622  ? 87  SER C N   1 
ATOM 4051 C CA  . SER C 1 87  ? 41.92473  3.64716   -12.21909 1.000 76.96841  ? 87  SER C CA  1 
ATOM 4052 C C   . SER C 1 87  ? 40.84367  3.30189   -11.21319 1.000 76.94403  ? 87  SER C C   1 
ATOM 4053 O O   . SER C 1 87  ? 39.86476  4.03839   -11.05870 1.000 79.90381  ? 87  SER C O   1 
ATOM 4054 C CB  . SER C 1 87  ? 43.12813  4.22965   -11.48442 1.000 74.81387  ? 87  SER C CB  1 
ATOM 4055 O OG  . SER C 1 87  ? 42.72799  5.31773   -10.67586 1.000 76.23531  ? 87  SER C OG  1 
ATOM 4056 N N   . THR C 1 88  ? 41.02176  2.16782   -10.51735 1.000 77.19414  ? 88  THR C N   1 
ATOM 4057 C CA  . THR C 1 88  ? 40.00441  1.75924   -9.54849  1.000 72.36235  ? 88  THR C CA  1 
ATOM 4058 C C   . THR C 1 88  ? 39.75420  2.86023   -8.53473  1.000 73.76425  ? 88  THR C C   1 
ATOM 4059 O O   . THR C 1 88  ? 38.60123  3.14396   -8.20775  1.000 76.87361  ? 88  THR C O   1 
ATOM 4060 C CB  . THR C 1 88  ? 40.39489  0.47477   -8.83030  1.000 69.06739  ? 88  THR C CB  1 
ATOM 4061 O OG1 . THR C 1 88  ? 41.63700  0.67549   -8.15230  1.000 77.48729  ? 88  THR C OG1 1 
ATOM 4062 C CG2 . THR C 1 88  ? 40.49411  -0.68999  -9.78786  1.000 65.57329  ? 88  THR C CG2 1 
ATOM 4063 N N   . ILE C 1 89  ? 40.81669  3.53327   -8.07208  1.000 74.31933  ? 89  ILE C N   1 
ATOM 4064 C CA  . ILE C 1 89  ? 40.64962  4.64145   -7.12845  1.000 76.73263  ? 89  ILE C CA  1 
ATOM 4065 C C   . ILE C 1 89  ? 39.78732  5.74431   -7.72501  1.000 79.70208  ? 89  ILE C C   1 
ATOM 4066 O O   . ILE C 1 89  ? 38.85685  6.23895   -7.07922  1.000 79.23631  ? 89  ILE C O   1 
ATOM 4067 C CB  . ILE C 1 89  ? 42.00655  5.20423   -6.67893  1.000 75.52214  ? 89  ILE C CB  1 
ATOM 4068 C CG1 . ILE C 1 89  ? 42.79012  4.17818   -5.87514  1.000 80.79278  ? 89  ILE C CG1 1 
ATOM 4069 C CG2 . ILE C 1 89  ? 41.75294  6.36715   -5.76364  1.000 76.20347  ? 89  ILE C CG2 1 
ATOM 4070 C CD1 . ILE C 1 89  ? 42.13713  3.86775   -4.51946  1.000 78.02841  ? 89  ILE C CD1 1 
ATOM 4071 N N   . ASP C 1 90  ? 40.09790  6.17024   -8.95314  1.000 88.43352  ? 90  ASP C N   1 
ATOM 4072 C CA  . ASP C 1 90  ? 39.31335  7.23937   -9.56678  1.000 90.07957  ? 90  ASP C CA  1 
ATOM 4073 C C   . ASP C 1 90  ? 37.84968  6.84963   -9.67577  1.000 91.84418  ? 90  ASP C C   1 
ATOM 4074 O O   . ASP C 1 90  ? 36.95530  7.67222   -9.43140  1.000 92.03550  ? 90  ASP C O   1 
ATOM 4075 C CB  . ASP C 1 90  ? 39.84810  7.58498   -10.95238 1.000 90.53436  ? 90  ASP C CB  1 
ATOM 4076 C CG  . ASP C 1 90  ? 41.12249  8.37674   -10.90675 1.000 92.02952  ? 90  ASP C CG  1 
ATOM 4077 O OD1 . ASP C 1 90  ? 41.36238  9.07112   -9.89105  1.000 90.80845  ? 90  ASP C OD1 1 
ATOM 4078 O OD2 . ASP C 1 90  ? 41.86205  8.32539   -11.91206 1.000 93.70535  ? 90  ASP C OD2 1 
ATOM 4079 N N   . GLY C 1 91  ? 37.59247  5.59695   -10.05366 1.000 83.27380  ? 91  GLY C N   1 
ATOM 4080 C CA  . GLY C 1 91  ? 36.22409  5.14737   -10.22606 1.000 81.90045  ? 91  GLY C CA  1 
ATOM 4081 C C   . GLY C 1 91  ? 35.41200  5.22040   -8.95042  1.000 80.45629  ? 91  GLY C C   1 
ATOM 4082 O O   . GLY C 1 91  ? 34.21433  5.51039   -8.98789  1.000 80.62119  ? 91  GLY C O   1 
ATOM 4083 N N   . ILE C 1 92  ? 36.04409  4.94552   -7.80520  1.000 81.34804  ? 92  ILE C N   1 
ATOM 4084 C CA  . ILE C 1 92  ? 35.30170  4.97797   -6.55160  1.000 79.37435  ? 92  ILE C CA  1 
ATOM 4085 C C   . ILE C 1 92  ? 35.13015  6.41825   -6.07258  1.000 82.09883  ? 92  ILE C C   1 
ATOM 4086 O O   . ILE C 1 92  ? 34.02556  6.82628   -5.70460  1.000 82.41555  ? 92  ILE C O   1 
ATOM 4087 C CB  . ILE C 1 92  ? 35.96927  4.06239   -5.50092  1.000 77.75662  ? 92  ILE C CB  1 
ATOM 4088 C CG1 . ILE C 1 92  ? 34.99715  3.75935   -4.36103  1.000 75.45514  ? 92  ILE C CG1 1 
ATOM 4089 C CG2 . ILE C 1 92  ? 37.26828  4.63411   -4.95896  1.000 78.91437  ? 92  ILE C CG2 1 
ATOM 4090 C CD1 . ILE C 1 92  ? 33.83146  2.92074   -4.80072  1.000 70.68566  ? 92  ILE C CD1 1 
ATOM 4091 N N   . ALA C 1 93  ? 36.18949  7.23336   -6.15112  1.000 84.19922  ? 93  ALA C N   1 
ATOM 4092 C CA  . ALA C 1 93  ? 36.08107  8.65770   -5.84737  1.000 83.13681  ? 93  ALA C CA  1 
ATOM 4093 C C   . ALA C 1 93  ? 35.05602  9.36164   -6.72384  1.000 87.16121  ? 93  ALA C C   1 
ATOM 4094 O O   . ALA C 1 93  ? 34.56637  10.42943  -6.34793  1.000 90.17030  ? 93  ALA C O   1 
ATOM 4095 C CB  . ALA C 1 93  ? 37.44020  9.34169   -6.01203  1.000 83.23136  ? 93  ALA C CB  1 
ATOM 4096 N N   . LYS C 1 94  ? 34.76704  8.82129   -7.90857  1.000 86.64654  ? 94  LYS C N   1 
ATOM 4097 C CA  . LYS C 1 94  ? 33.62871  9.28713   -8.68894  1.000 86.73917  ? 94  LYS C CA  1 
ATOM 4098 C C   . LYS C 1 94  ? 32.32815  8.65306   -8.21168  1.000 87.44902  ? 94  LYS C C   1 
ATOM 4099 O O   . LYS C 1 94  ? 31.26599  9.27367   -8.30388  1.000 89.25481  ? 94  LYS C O   1 
ATOM 4100 C CB  . LYS C 1 94  ? 33.86063  8.99722   -10.17387 1.000 86.98982  ? 94  LYS C CB  1 
ATOM 4101 C CG  . LYS C 1 94  ? 35.06848  9.71632   -10.81936 1.000 93.19029  ? 94  LYS C CG  1 
ATOM 4102 C CD  . LYS C 1 94  ? 34.78257  11.20118  -11.08883 1.000 101.79397 ? 94  LYS C CD  1 
ATOM 4103 C CE  . LYS C 1 94  ? 35.30092  12.10083  -9.97164  1.000 101.38131 ? 94  LYS C CE  1 
ATOM 4104 N NZ  . LYS C 1 94  ? 34.99709  13.53583  -10.22123 1.000 108.11752 ? 94  LYS C NZ  1 
ATOM 4105 N N   . PHE C 1 95  ? 32.38813  7.42299   -7.70386  1.000 86.13630  ? 95  PHE C N   1 
ATOM 4106 C CA  . PHE C 1 95  ? 31.19119  6.80159   -7.15796  1.000 84.28996  ? 95  PHE C CA  1 
ATOM 4107 C C   . PHE C 1 95  ? 30.68094  7.57159   -5.94713  1.000 91.51817  ? 95  PHE C C   1 
ATOM 4108 O O   . PHE C 1 95  ? 29.46781  7.70931   -5.75524  1.000 94.71492  ? 95  PHE C O   1 
ATOM 4109 C CB  . PHE C 1 95  ? 31.47054  5.34367   -6.79557  1.000 81.12656  ? 95  PHE C CB  1 
ATOM 4110 C CG  . PHE C 1 95  ? 30.31630  4.66666   -6.11366  1.000 80.51961  ? 95  PHE C CG  1 
ATOM 4111 C CD1 . PHE C 1 95  ? 29.19894  4.27622   -6.82921  1.000 79.59950  ? 95  PHE C CD1 1 
ATOM 4112 C CD2 . PHE C 1 95  ? 30.33386  4.44771   -4.74800  1.000 76.39577  ? 95  PHE C CD2 1 
ATOM 4113 C CE1 . PHE C 1 95  ? 28.12307  3.67175   -6.18668  1.000 76.66672  ? 95  PHE C CE1 1 
ATOM 4114 C CE2 . PHE C 1 95  ? 29.26088  3.85437   -4.12006  1.000 73.38592  ? 95  PHE C CE2 1 
ATOM 4115 C CZ  . PHE C 1 95  ? 28.15645  3.46452   -4.84294  1.000 71.07247  ? 95  PHE C CZ  1 
ATOM 4116 N N   . ASN C 1 96  ? 31.59033  8.07430   -5.11053  1.000 90.24185  ? 96  ASN C N   1 
ATOM 4117 C CA  . ASN C 1 96  ? 31.17122  8.85614   -3.95348  1.000 90.12477  ? 96  ASN C CA  1 
ATOM 4118 C C   . ASN C 1 96  ? 30.51541  10.16200  -4.38852  1.000 100.52452 ? 96  ASN C C   1 
ATOM 4119 O O   . ASN C 1 96  ? 29.43825  10.51864  -3.89956  1.000 102.92667 ? 96  ASN C O   1 
ATOM 4120 C CB  . ASN C 1 96  ? 32.36862  9.14156   -3.05742  1.000 88.73608  ? 96  ASN C CB  1 
ATOM 4121 C CG  . ASN C 1 96  ? 33.08462  7.87815   -2.62322  1.000 89.94059  ? 96  ASN C CG  1 
ATOM 4122 O OD1 . ASN C 1 96  ? 32.47966  6.80601   -2.49171  1.000 87.49058  ? 96  ASN C OD1 1 
ATOM 4123 N ND2 . ASN C 1 96  ? 34.38229  8.00609   -2.35785  1.000 87.50957  ? 96  ASN C ND2 1 
ATOM 4124 N N   . ASP C 1 97  ? 31.14565  10.87685  -5.32940  1.000 110.10728 ? 97  ASP C N   1 
ATOM 4125 C CA  . ASP C 1 97  ? 30.57697  12.11810  -5.85030  1.000 112.45968 ? 97  ASP C CA  1 
ATOM 4126 C C   . ASP C 1 97  ? 29.15559  11.90993  -6.36041  1.000 114.98184 ? 97  ASP C C   1 
ATOM 4127 O O   . ASP C 1 97  ? 28.28350  12.77039  -6.17215  1.000 116.06080 ? 97  ASP C O   1 
ATOM 4128 C CB  . ASP C 1 97  ? 31.45345  12.67227  -6.97729  1.000 109.22344 ? 97  ASP C CB  1 
ATOM 4129 C CG  . ASP C 1 97  ? 32.85845  12.99733  -6.51645  1.000 110.35334 ? 97  ASP C CG  1 
ATOM 4130 O OD1 . ASP C 1 97  ? 33.06118  13.16082  -5.29394  1.000 113.16749 ? 97  ASP C OD1 1 
ATOM 4131 O OD2 . ASP C 1 97  ? 33.75692  13.11678  -7.37793  1.000 110.32584 ? 97  ASP C OD2 1 
ATOM 4132 N N   . TYR C 1 98  ? 28.90907  10.77594  -7.02529  1.000 105.09391 ? 98  TYR C N   1 
ATOM 4133 C CA  . TYR C 1 98  ? 27.55361  10.45034  -7.45676  1.000 105.25600 ? 98  TYR C CA  1 
ATOM 4134 C C   . TYR C 1 98  ? 26.61750  10.30711  -6.26567  1.000 104.15585 ? 98  TYR C C   1 
ATOM 4135 O O   . TYR C 1 98  ? 25.45534  10.72496  -6.32314  1.000 106.85360 ? 98  TYR C O   1 
ATOM 4136 C CB  . TYR C 1 98  ? 27.54632  9.15748   -8.26236  1.000 98.75857  ? 98  TYR C CB  1 
ATOM 4137 C CG  . TYR C 1 98  ? 26.19346  8.82672   -8.85306  1.000 100.31603 ? 98  TYR C CG  1 
ATOM 4138 C CD1 . TYR C 1 98  ? 25.82223  9.33065   -10.08605 1.000 98.49427  ? 98  TYR C CD1 1 
ATOM 4139 C CD2 . TYR C 1 98  ? 25.26517  8.05508   -8.15316  1.000 98.64404  ? 98  TYR C CD2 1 
ATOM 4140 C CE1 . TYR C 1 98  ? 24.59451  9.03748   -10.64232 1.000 99.49304  ? 98  TYR C CE1 1 
ATOM 4141 C CE2 . TYR C 1 98  ? 24.02035  7.76479   -8.69736  1.000 100.23541 ? 98  TYR C CE2 1 
ATOM 4142 C CZ  . TYR C 1 98  ? 23.69405  8.26124   -9.95208  1.000 100.95090 ? 98  TYR C CZ  1 
ATOM 4143 O OH  . TYR C 1 98  ? 22.46870  7.99272   -10.52801 1.000 102.55413 ? 98  TYR C OH  1 
ATOM 4144 N N   . ILE C 1 99  ? 27.09555  9.68560   -5.18873  1.000 103.66808 ? 99  ILE C N   1 
ATOM 4145 C CA  . ILE C 1 99  ? 26.23030  9.42588   -4.04636  1.000 103.48901 ? 99  ILE C CA  1 
ATOM 4146 C C   . ILE C 1 99  ? 25.84531  10.73140  -3.34978  1.000 105.81116 ? 99  ILE C C   1 
ATOM 4147 O O   . ILE C 1 99  ? 24.69480  10.90789  -2.93012  1.000 107.50932 ? 99  ILE C O   1 
ATOM 4148 C CB  . ILE C 1 99  ? 26.90911  8.41432   -3.10130  1.000 100.42359 ? 99  ILE C CB  1 
ATOM 4149 C CG1 . ILE C 1 99  ? 27.08408  7.05772   -3.80805  1.000 89.70717  ? 99  ILE C CG1 1 
ATOM 4150 C CG2 . ILE C 1 99  ? 26.10532  8.24082   -1.80908  1.000 98.03390  ? 99  ILE C CG2 1 
ATOM 4151 C CD1 . ILE C 1 99  ? 25.77007  6.34238   -4.14886  1.000 84.29979  ? 99  ILE C CD1 1 
ATOM 4152 N N   . ASN C 1 100 ? 26.78247  11.67841  -3.24519  1.000 104.84478 ? 100 ASN C N   1 
ATOM 4153 C CA  . ASN C 1 100 ? 26.46574  12.96103  -2.62353  1.000 106.10945 ? 100 ASN C CA  1 
ATOM 4154 C C   . ASN C 1 100 ? 25.41114  13.72022  -3.41550  1.000 110.71642 ? 100 ASN C C   1 
ATOM 4155 O O   . ASN C 1 100 ? 24.62717  14.48267  -2.84067  1.000 115.60238 ? 100 ASN C O   1 
ATOM 4156 C CB  . ASN C 1 100 ? 27.71685  13.82896  -2.51444  1.000 107.29872 ? 100 ASN C CB  1 
ATOM 4157 C CG  . ASN C 1 100 ? 28.89783  13.08297  -1.94245  1.000 111.80500 ? 100 ASN C CG  1 
ATOM 4158 O OD1 . ASN C 1 100 ? 29.93687  12.96610  -2.60376  1.000 113.22467 ? 100 ASN C OD1 1 
ATOM 4159 N ND2 . ASN C 1 100 ? 28.74531  12.54104  -0.73179  1.000 106.03497 ? 100 ASN C ND2 1 
ATOM 4160 N N   . ALA C 1 101 ? 25.37853  13.53103  -4.72791  1.000 116.19926 ? 101 ALA C N   1 
ATOM 4161 C CA  . ALA C 1 101 ? 24.60384  14.37930  -5.61985  1.000 116.48029 ? 101 ALA C CA  1 
ATOM 4162 C C   . ALA C 1 101 ? 23.19230  13.86774  -5.89311  1.000 118.48215 ? 101 ALA C C   1 
ATOM 4163 O O   . ALA C 1 101 ? 22.48489  14.47106  -6.70845  1.000 120.08498 ? 101 ALA C O   1 
ATOM 4164 C CB  . ALA C 1 101 ? 25.35245  14.55143  -6.94776  1.000 112.00997 ? 101 ALA C CB  1 
ATOM 4165 N N   . HIS C 1 102 ? 22.75070  12.78556  -5.24530  1.000 111.42990 ? 102 HIS C N   1 
ATOM 4166 C CA  . HIS C 1 102 ? 21.47543  12.20343  -5.64465  1.000 110.25687 ? 102 HIS C CA  1 
ATOM 4167 C C   . HIS C 1 102 ? 20.61197  11.80968  -4.46576  1.000 113.79394 ? 102 HIS C C   1 
ATOM 4168 O O   . HIS C 1 102 ? 19.88409  10.81633  -4.54180  1.000 115.41232 ? 102 HIS C O   1 
ATOM 4169 C CB  . HIS C 1 102 ? 21.68885  10.99784  -6.54436  1.000 109.78391 ? 102 HIS C CB  1 
ATOM 4170 C CG  . HIS C 1 102 ? 22.11855  11.35980  -7.92803  1.000 106.05626 ? 102 HIS C CG  1 
ATOM 4171 N ND1 . HIS C 1 102 ? 23.41919  11.69138  -8.23917  1.000 103.11001 ? 102 HIS C ND1 1 
ATOM 4172 C CD2 . HIS C 1 102 ? 21.42509  11.41609  -9.08813  1.000 105.71445 ? 102 HIS C CD2 1 
ATOM 4173 C CE1 . HIS C 1 102 ? 23.50587  11.95050  -9.53037  1.000 107.99047 ? 102 HIS C CE1 1 
ATOM 4174 N NE2 . HIS C 1 102 ? 22.31094  11.78605  -10.07007 1.000 110.41383 ? 102 HIS C NE2 1 
ATOM 4175 N N   . ASN C 1 103 ? 20.66898  12.58041  -3.37926  1.000 113.33698 ? 103 ASN C N   1 
ATOM 4176 C CA  . ASN C 1 103 ? 19.73808  12.45995  -2.26001  1.000 116.32982 ? 103 ASN C CA  1 
ATOM 4177 C C   . ASN C 1 103 ? 19.87213  11.13258  -1.52147  1.000 115.39170 ? 103 ASN C C   1 
ATOM 4178 O O   . ASN C 1 103 ? 18.87430  10.59420  -1.03722  1.000 119.99151 ? 103 ASN C O   1 
ATOM 4179 C CB  . ASN C 1 103 ? 18.28009  12.63920  -2.71021  1.000 121.27944 ? 103 ASN C CB  1 
ATOM 4180 C CG  . ASN C 1 103 ? 17.97234  14.04619  -3.16592  1.000 120.47570 ? 103 ASN C CG  1 
ATOM 4181 O OD1 . ASN C 1 103 ? 18.48256  15.01499  -2.60964  1.000 122.70381 ? 103 ASN C OD1 1 
ATOM 4182 N ND2 . ASN C 1 103 ? 17.10401  14.16797  -4.16385  1.000 124.99822 ? 103 ASN C ND2 1 
ATOM 4183 N N   . ILE C 1 104 ? 21.08121  10.58440  -1.41796  1.000 117.39055 ? 104 ILE C N   1 
ATOM 4184 C CA  . ILE C 1 104 ? 21.26611  9.30770   -0.73101  1.000 119.34309 ? 104 ILE C CA  1 
ATOM 4185 C C   . ILE C 1 104 ? 21.38632  9.54687   0.77300   1.000 125.95722 ? 104 ILE C C   1 
ATOM 4186 O O   . ILE C 1 104 ? 22.06238  10.48213  1.22528   1.000 121.72856 ? 104 ILE C O   1 
ATOM 4187 C CB  . ILE C 1 104 ? 22.48752  8.55948   -1.29557  1.000 107.55690 ? 104 ILE C CB  1 
ATOM 4188 C CG1 . ILE C 1 104 ? 22.34476  8.39344   -2.80731  1.000 108.09808 ? 104 ILE C CG1 1 
ATOM 4189 C CG2 . ILE C 1 104 ? 22.60849  7.18172   -0.66980  1.000 105.04059 ? 104 ILE C CG2 1 
ATOM 4190 C CD1 . ILE C 1 104 ? 21.12427  7.59321   -3.22641  1.000 108.44153 ? 104 ILE C CD1 1 
ATOM 4191 N N   . ASP C 1 105 ? 20.70421  8.70853   1.55906   1.000 150.72326 ? 105 ASP C N   1 
ATOM 4192 C CA  . ASP C 1 105 ? 20.70825  8.83317   3.01258   1.000 150.09394 ? 105 ASP C CA  1 
ATOM 4193 C C   . ASP C 1 105 ? 21.63427  7.79163   3.61546   1.000 149.72017 ? 105 ASP C C   1 
ATOM 4194 O O   . ASP C 1 105 ? 21.35256  6.58724   3.50369   1.000 149.58534 ? 105 ASP C O   1 
ATOM 4195 C CB  . ASP C 1 105 ? 19.29257  8.67697   3.56729   1.000 150.83871 ? 105 ASP C CB  1 
ATOM 4196 C CG  . ASP C 1 105 ? 19.20899  8.89098   5.07549   1.000 149.92369 ? 105 ASP C CG  1 
ATOM 4197 O OD1 . ASP C 1 105 ? 20.25253  8.98525   5.75177   1.000 149.64875 ? 105 ASP C OD1 1 
ATOM 4198 O OD2 . ASP C 1 105 ? 18.07564  9.00258   5.58445   1.000 149.49030 ? 105 ASP C OD2 1 
ATOM 4199 N N   . PRO C 1 106 ? 22.71933  8.20289   4.28063   1.000 121.41804 ? 106 PRO C N   1 
ATOM 4200 C CA  . PRO C 1 106 ? 23.64960  7.21659   4.85456   1.000 108.64838 ? 106 PRO C CA  1 
ATOM 4201 C C   . PRO C 1 106 ? 22.98205  6.19242   5.75544   1.000 103.96826 ? 106 PRO C C   1 
ATOM 4202 O O   . PRO C 1 106 ? 23.36641  5.01550   5.73727   1.000 98.27526  ? 106 PRO C O   1 
ATOM 4203 C CB  . PRO C 1 106 ? 24.64280  8.09661   5.62512   1.000 102.13897 ? 106 PRO C CB  1 
ATOM 4204 C CG  . PRO C 1 106 ? 24.61251  9.41493   4.90639   1.000 100.00588 ? 106 PRO C CG  1 
ATOM 4205 C CD  . PRO C 1 106 ? 23.19200  9.58878   4.45660   1.000 115.35966 ? 106 PRO C CD  1 
ATOM 4206 N N   . TRP C 1 107 ? 21.97828  6.59307   6.52941   1.000 104.76440 ? 107 TRP C N   1 
ATOM 4207 C CA  . TRP C 1 107 ? 21.38811  5.68201   7.49700   1.000 96.18513  ? 107 TRP C CA  1 
ATOM 4208 C C   . TRP C 1 107 ? 20.10118  5.03998   7.00909   1.000 99.29653  ? 107 TRP C C   1 
ATOM 4209 O O   . TRP C 1 107 ? 19.83248  3.89052   7.35771   1.000 93.15441  ? 107 TRP C O   1 
ATOM 4210 C CB  . TRP C 1 107 ? 21.15232  6.42279   8.81480   1.000 86.43550  ? 107 TRP C CB  1 
ATOM 4211 C CG  . TRP C 1 107 ? 22.44923  6.83764   9.47337   1.000 82.29784  ? 107 TRP C CG  1 
ATOM 4212 C CD1 . TRP C 1 107 ? 23.14248  7.99745   9.25764   1.000 82.43480  ? 107 TRP C CD1 1 
ATOM 4213 C CD2 . TRP C 1 107 ? 23.18753  6.11332   10.47650  1.000 76.19247  ? 107 TRP C CD2 1 
ATOM 4214 N NE1 . TRP C 1 107 ? 24.27742  8.03097   10.04728  1.000 78.23388  ? 107 TRP C NE1 1 
ATOM 4215 C CE2 . TRP C 1 107 ? 24.32599  6.88911   10.80291  1.000 72.37026  ? 107 TRP C CE2 1 
ATOM 4216 C CE3 . TRP C 1 107 ? 23.00345  4.88252   11.11825  1.000 74.78547  ? 107 TRP C CE3 1 
ATOM 4217 C CZ2 . TRP C 1 107 ? 25.26982  6.47601   11.73722  1.000 66.60136  ? 107 TRP C CZ2 1 
ATOM 4218 C CZ3 . TRP C 1 107 ? 23.94662  4.47246   12.04950  1.000 75.98218  ? 107 TRP C CZ3 1 
ATOM 4219 C CH2 . TRP C 1 107 ? 25.06501  5.27223   12.35155  1.000 73.20485  ? 107 TRP C CH2 1 
ATOM 4220 N N   . LYS C 1 108 ? 19.31525  5.71927   6.17929   1.000 107.24753 ? 108 LYS C N   1 
ATOM 4221 C CA  . LYS C 1 108 ? 18.02301  5.17129   5.79127   1.000 110.47210 ? 108 LYS C CA  1 
ATOM 4222 C C   . LYS C 1 108 ? 17.97124  4.63478   4.37283   1.000 111.41614 ? 108 LYS C C   1 
ATOM 4223 O O   . LYS C 1 108 ? 17.12981  3.77725   4.09100   1.000 108.18545 ? 108 LYS C O   1 
ATOM 4224 C CB  . LYS C 1 108 ? 16.91976  6.22216   5.95599   1.000 116.56667 ? 108 LYS C CB  1 
ATOM 4225 N N   . SER C 1 109 ? 18.83175  5.11551   3.47440   1.000 115.48518 ? 109 SER C N   1 
ATOM 4226 C CA  . SER C 1 109 ? 18.78656  4.66597   2.08737   1.000 112.56765 ? 109 SER C CA  1 
ATOM 4227 C C   . SER C 1 109 ? 19.24135  3.21767   1.96075   1.000 104.21173 ? 109 SER C C   1 
ATOM 4228 O O   . SER C 1 109 ? 20.07633  2.73220   2.72638   1.000 104.01313 ? 109 SER C O   1 
ATOM 4229 C CB  . SER C 1 109 ? 19.64392  5.55705   1.19157   1.000 115.60304 ? 109 SER C CB  1 
ATOM 4230 O OG  . SER C 1 109 ? 19.10050  6.86245   1.08845   1.000 120.25755 ? 109 SER C OG  1 
ATOM 4231 N N   . GLN C 1 110 ? 18.68332  2.53108   0.97119   1.000 100.47869 ? 110 GLN C N   1 
ATOM 4232 C CA  . GLN C 1 110 ? 18.91929  1.11033   0.75428   1.000 99.65742  ? 110 GLN C CA  1 
ATOM 4233 C C   . GLN C 1 110 ? 19.71507  0.91283   -0.52883  1.000 94.17371  ? 110 GLN C C   1 
ATOM 4234 O O   . GLN C 1 110 ? 19.26266  1.30801   -1.60537  1.000 95.79410  ? 110 GLN C O   1 
ATOM 4235 C CB  . GLN C 1 110 ? 17.59498  0.35360   0.67235   1.000 100.41576 ? 110 GLN C CB  1 
ATOM 4236 C CG  . GLN C 1 110 ? 16.82737  0.30759   1.97972   1.000 105.31241 ? 110 GLN C CG  1 
ATOM 4237 C CD  . GLN C 1 110 ? 15.51536  -0.43835  1.84125   1.000 109.96994 ? 110 GLN C CD  1 
ATOM 4238 O OE1 . GLN C 1 110 ? 15.10924  -0.79980  0.73032   1.000 106.36753 ? 110 GLN C OE1 1 
ATOM 4239 N NE2 . GLN C 1 110 ? 14.85590  -0.69768  2.97083   1.000 110.73370 ? 110 GLN C NE2 1 
ATOM 4240 N N   . GLY C 1 111 ? 20.88668  0.29054   -0.41798  1.000 93.05432  ? 111 GLY C N   1 
ATOM 4241 C CA  . GLY C 1 111 ? 21.61385  -0.13230  -1.60346  1.000 89.71472  ? 111 GLY C CA  1 
ATOM 4242 C C   . GLY C 1 111 ? 21.09332  -1.46472  -2.12264  1.000 91.05013  ? 111 GLY C C   1 
ATOM 4243 O O   . GLY C 1 111 ? 20.77830  -2.37563  -1.35918  1.000 93.84212  ? 111 GLY C O   1 
ATOM 4244 N N   . TRP C 1 112 ? 21.01826  -1.57322  -3.44377  1.000 89.71726  ? 112 TRP C N   1 
ATOM 4245 C CA  . TRP C 1 112 ? 20.43422  -2.72398  -4.11746  1.000 90.87806  ? 112 TRP C CA  1 
ATOM 4246 C C   . TRP C 1 112 ? 21.43215  -3.29560  -5.11364  1.000 89.97112  ? 112 TRP C C   1 
ATOM 4247 O O   . TRP C 1 112 ? 22.26488  -2.56038  -5.64891  1.000 88.87236  ? 112 TRP C O   1 
ATOM 4248 C CB  . TRP C 1 112 ? 19.15217  -2.31719  -4.84683  1.000 94.23888  ? 112 TRP C CB  1 
ATOM 4249 C CG  . TRP C 1 112 ? 18.05336  -2.01193  -3.92793  1.000 92.20054  ? 112 TRP C CG  1 
ATOM 4250 C CD1 . TRP C 1 112 ? 17.76142  -0.80407  -3.37580  1.000 95.91324  ? 112 TRP C CD1 1 
ATOM 4251 C CD2 . TRP C 1 112 ? 17.05878  -2.92462  -3.46221  1.000 94.56469  ? 112 TRP C CD2 1 
ATOM 4252 N NE1 . TRP C 1 112 ? 16.65739  -0.91247  -2.55810  1.000 100.63924 ? 112 TRP C NE1 1 
ATOM 4253 C CE2 . TRP C 1 112 ? 16.20522  -2.20615  -2.59778  1.000 98.98862  ? 112 TRP C CE2 1 
ATOM 4254 C CE3 . TRP C 1 112 ? 16.81474  -4.28349  -3.67936  1.000 95.34321  ? 112 TRP C CE3 1 
ATOM 4255 C CZ2 . TRP C 1 112 ? 15.12653  -2.80197  -1.94568  1.000 100.47353 ? 112 TRP C CZ2 1 
ATOM 4256 C CZ3 . TRP C 1 112 ? 15.74072  -4.87365  -3.03841  1.000 100.00621 ? 112 TRP C CZ3 1 
ATOM 4257 C CH2 . TRP C 1 112 ? 14.91036  -4.13272  -2.17728  1.000 102.09278 ? 112 TRP C CH2 1 
ATOM 4258 N N   . CYS C 1 113 ? 21.34532  -4.60768  -5.35753  1.000 88.31065  ? 113 CYS C N   1 
ATOM 4259 C CA  . CYS C 1 113 ? 22.10675  -5.24075  -6.43402  1.000 93.47632  ? 113 CYS C CA  1 
ATOM 4260 C C   . CYS C 1 113 ? 21.60362  -6.66234  -6.66376  1.000 94.94340  ? 113 CYS C C   1 
ATOM 4261 O O   . CYS C 1 113 ? 21.16015  -7.33031  -5.72899  1.000 89.55684  ? 113 CYS C O   1 
ATOM 4262 C CB  . CYS C 1 113 ? 23.61002  -5.26549  -6.12997  1.000 87.73980  ? 113 CYS C CB  1 
ATOM 4263 S SG  . CYS C 1 113 ? 24.11522  -6.39204  -4.82882  1.000 89.46959  ? 113 CYS C SG  1 
ATOM 4264 N N   . ARG C 1 114 ? 21.66224  -7.11802  -7.91712  1.000 102.68211 ? 114 ARG C N   1 
ATOM 4265 C CA  . ARG C 1 114 ? 21.30470  -8.50350  -8.19505  1.000 104.26174 ? 114 ARG C CA  1 
ATOM 4266 C C   . ARG C 1 114 ? 22.47360  -9.40390  -7.80278  1.000 104.23473 ? 114 ARG C C   1 
ATOM 4267 O O   . ARG C 1 114 ? 23.55675  -9.31279  -8.39518  1.000 102.49391 ? 114 ARG C O   1 
ATOM 4268 C CB  . ARG C 1 114 ? 20.93411  -8.70897  -9.65831  1.000 104.51876 ? 114 ARG C CB  1 
ATOM 4269 C CG  . ARG C 1 114 ? 20.35913  -10.09517 -9.89637  1.000 106.88014 ? 114 ARG C CG  1 
ATOM 4270 C CD  . ARG C 1 114 ? 20.06053  -10.37885 -11.36073 1.000 115.67526 ? 114 ARG C CD  1 
ATOM 4271 N NE  . ARG C 1 114 ? 19.05411  -9.48790  -11.92450 1.000 119.85563 ? 114 ARG C NE  1 
ATOM 4272 C CZ  . ARG C 1 114 ? 17.75693  -9.57137  -11.65828 1.000 120.65300 ? 114 ARG C CZ  1 
ATOM 4273 N NH1 . ARG C 1 114 ? 17.29404  -10.38419 -10.71695 1.000 117.63457 ? 114 ARG C NH1 1 
ATOM 4274 N NH2 . ARG C 1 114 ? 16.90309  -8.81443  -12.34295 1.000 114.64980 ? 114 ARG C NH2 1 
ATOM 4275 N N   . GLY C 1 115 ? 22.24684  -10.28727 -6.82088  1.000 99.62101  ? 115 GLY C N   1 
ATOM 4276 C CA  . GLY C 1 115 ? 23.32091  -11.04139 -6.19330  1.000 91.78459  ? 115 GLY C CA  1 
ATOM 4277 C C   . GLY C 1 115 ? 24.08403  -10.30650 -5.10184  1.000 85.54948  ? 115 GLY C C   1 
ATOM 4278 O O   . GLY C 1 115 ? 25.27683  -10.02985 -5.26378  1.000 79.13987  ? 115 GLY C O   1 
ATOM 4279 N N   . MET C 1 116 ? 23.40164  -9.99490  -3.98389  1.000 87.61666  ? 116 MET C N   1 
ATOM 4280 C CA  . MET C 1 116 ? 23.96977  -9.22151  -2.86930  1.000 84.22534  ? 116 MET C CA  1 
ATOM 4281 C C   . MET C 1 116 ? 25.31189  -9.75523  -2.37941  1.000 78.07918  ? 116 MET C C   1 
ATOM 4282 O O   . MET C 1 116 ? 26.06774  -9.01146  -1.74561  1.000 74.44090  ? 116 MET C O   1 
ATOM 4283 C CB  . MET C 1 116 ? 23.01317  -9.20956  -1.66312  1.000 84.90997  ? 116 MET C CB  1 
ATOM 4284 C CG  . MET C 1 116 ? 23.31646  -8.12291  -0.60584  1.000 85.60795  ? 116 MET C CG  1 
ATOM 4285 S SD  . MET C 1 116 ? 22.46488  -8.22908  1.01752   1.000 79.58855  ? 116 MET C SD  1 
ATOM 4286 C CE  . MET C 1 116 ? 20.77737  -8.17184  0.53900   1.000 85.05629  ? 116 MET C CE  1 
ATOM 4287 N N   . SER C 1 117 ? 25.60602  -11.03328 -2.62386  1.000 77.84845  ? 117 SER C N   1 
ATOM 4288 C CA  . SER C 1 117 ? 26.87511  -11.63452 -2.23572  1.000 72.73311  ? 117 SER C CA  1 
ATOM 4289 C C   . SER C 1 117 ? 28.03454  -11.21081 -3.12595  1.000 70.59418  ? 117 SER C C   1 
ATOM 4290 O O   . SER C 1 117 ? 29.19518  -11.39863 -2.74521  1.000 67.72360  ? 117 SER C O   1 
ATOM 4291 C CB  . SER C 1 117 ? 26.74557  -13.15946 -2.26267  1.000 71.53350  ? 117 SER C CB  1 
ATOM 4292 O OG  . SER C 1 117 ? 27.99490  -13.79953 -2.07539  1.000 68.93167  ? 117 SER C OG  1 
ATOM 4293 N N   . PHE C 1 118 ? 27.75552  -10.66459 -4.30411  1.000 69.98350  ? 118 PHE C N   1 
ATOM 4294 C CA  . PHE C 1 118 ? 28.79490  -10.40451 -5.29164  1.000 71.37609  ? 118 PHE C CA  1 
ATOM 4295 C C   . PHE C 1 118 ? 29.21625  -8.94067  -5.30077  1.000 66.72579  ? 118 PHE C C   1 
ATOM 4296 O O   . PHE C 1 118 ? 30.35952  -8.61061  -4.96951  1.000 59.05278  ? 118 PHE C O   1 
ATOM 4297 C CB  . PHE C 1 118 ? 28.26533  -10.81865 -6.67538  1.000 74.60086  ? 118 PHE C CB  1 
ATOM 4298 C CG  . PHE C 1 118 ? 29.27559  -10.73681 -7.78134  1.000 71.96853  ? 118 PHE C CG  1 
ATOM 4299 C CD1 . PHE C 1 118 ? 30.21151  -11.75150 -7.95762  1.000 73.36621  ? 118 PHE C CD1 1 
ATOM 4300 C CD2 . PHE C 1 118 ? 29.28112  -9.65217  -8.65378  1.000 72.52546  ? 118 PHE C CD2 1 
ATOM 4301 C CE1 . PHE C 1 118 ? 31.14004  -11.69294 -8.97982  1.000 77.20211  ? 118 PHE C CE1 1 
ATOM 4302 C CE2 . PHE C 1 118 ? 30.19516  -9.58184  -9.68678  1.000 77.49578  ? 118 PHE C CE2 1 
ATOM 4303 C CZ  . PHE C 1 118 ? 31.13270  -10.60625 -9.85038  1.000 81.51990  ? 118 PHE C CZ  1 
ATOM 4304 N N   . ASP C 1 119 ? 28.27294  -8.05483  -5.63070  1.000 70.78606  ? 119 ASP C N   1 
ATOM 4305 C CA  . ASP C 1 119 ? 28.59613  -6.66022  -5.90025  1.000 67.06600  ? 119 ASP C CA  1 
ATOM 4306 C C   . ASP C 1 119 ? 29.14541  -5.97695  -4.66459  1.000 65.06432  ? 119 ASP C C   1 
ATOM 4307 O O   . ASP C 1 119 ? 30.23216  -5.39305  -4.69406  1.000 65.09056  ? 119 ASP C O   1 
ATOM 4308 C CB  . ASP C 1 119 ? 27.35230  -5.93168  -6.40463  1.000 71.79107  ? 119 ASP C CB  1 
ATOM 4309 C CG  . ASP C 1 119 ? 26.97645  -6.32448  -7.81709  1.000 77.80917  ? 119 ASP C CG  1 
ATOM 4310 O OD1 . ASP C 1 119 ? 27.89880  -6.58042  -8.61503  1.000 79.68854  ? 119 ASP C OD1 1 
ATOM 4311 O OD2 . ASP C 1 119 ? 25.76643  -6.38848  -8.12844  1.000 82.64527  ? 119 ASP C OD2 1 
ATOM 4312 N N   . PHE C 1 120 ? 28.41981  -6.05931  -3.55655  1.000 66.78561  ? 120 PHE C N   1 
ATOM 4313 C CA  . PHE C 1 120 ? 28.83132  -5.29530  -2.38836  1.000 64.42592  ? 120 PHE C CA  1 
ATOM 4314 C C   . PHE C 1 120 ? 30.20122  -5.69755  -1.86215  1.000 63.21209  ? 120 PHE C C   1 
ATOM 4315 O O   . PHE C 1 120 ? 30.97233  -4.79084  -1.50173  1.000 66.02218  ? 120 PHE C O   1 
ATOM 4316 C CB  . PHE C 1 120 ? 27.74119  -5.35176  -1.32007  1.000 65.93418  ? 120 PHE C CB  1 
ATOM 4317 C CG  . PHE C 1 120 ? 26.58672  -4.43889  -1.60583  1.000 69.10201  ? 120 PHE C CG  1 
ATOM 4318 C CD1 . PHE C 1 120 ? 26.69504  -3.07947  -1.36524  1.000 70.06253  ? 120 PHE C CD1 1 
ATOM 4319 C CD2 . PHE C 1 120 ? 25.39513  -4.93063  -2.11127  1.000 74.19964  ? 120 PHE C CD2 1 
ATOM 4320 C CE1 . PHE C 1 120 ? 25.63544  -2.22578  -1.62140  1.000 73.76532  ? 120 PHE C CE1 1 
ATOM 4321 C CE2 . PHE C 1 120 ? 24.32508  -4.08069  -2.36781  1.000 76.13649  ? 120 PHE C CE2 1 
ATOM 4322 C CZ  . PHE C 1 120 ? 24.45041  -2.72780  -2.12862  1.000 77.38921  ? 120 PHE C CZ  1 
ATOM 4323 N N   . PRO C 1 121 ? 30.58085  -6.97625  -1.79251  1.000 62.60253  ? 121 PRO C N   1 
ATOM 4324 C CA  . PRO C 1 121 ? 31.98581  -7.27421  -1.46896  1.000 62.30712  ? 121 PRO C CA  1 
ATOM 4325 C C   . PRO C 1 121 ? 32.98795  -6.57989  -2.38159  1.000 63.52541  ? 121 PRO C C   1 
ATOM 4326 O O   . PRO C 1 121 ? 34.01322  -6.09572  -1.88639  1.000 64.91208  ? 121 PRO C O   1 
ATOM 4327 C CB  . PRO C 1 121 ? 32.04774  -8.80256  -1.58504  1.000 57.88161  ? 121 PRO C CB  1 
ATOM 4328 C CG  . PRO C 1 121 ? 30.71069  -9.22613  -1.21543  1.000 58.87722  ? 121 PRO C CG  1 
ATOM 4329 C CD  . PRO C 1 121 ? 29.75543  -8.19390  -1.73990  1.000 63.19883  ? 121 PRO C CD  1 
ATOM 4330 N N   . ILE C 1 122 ? 32.73061  -6.49146  -3.68713  1.000 59.96007  ? 122 ILE C N   1 
ATOM 4331 C CA  . ILE C 1 122 ? 33.67400  -5.77455  -4.53624  1.000 62.09852  ? 122 ILE C CA  1 
ATOM 4332 C C   . ILE C 1 122 ? 33.68213  -4.29341  -4.18568  1.000 62.02289  ? 122 ILE C C   1 
ATOM 4333 O O   . ILE C 1 122 ? 34.74649  -3.67243  -4.07027  1.000 61.49271  ? 122 ILE C O   1 
ATOM 4334 C CB  . ILE C 1 122 ? 33.35522  -6.01298  -6.02367  1.000 65.27388  ? 122 ILE C CB  1 
ATOM 4335 C CG1 . ILE C 1 122 ? 33.59696  -7.47787  -6.38037  1.000 65.16809  ? 122 ILE C CG1 1 
ATOM 4336 C CG2 . ILE C 1 122 ? 34.20058  -5.10977  -6.90474  1.000 64.72170  ? 122 ILE C CG2 1 
ATOM 4337 C CD1 . ILE C 1 122 ? 33.02213  -7.88536  -7.69368  1.000 65.41132  ? 122 ILE C CD1 1 
ATOM 4338 N N   . LEU C 1 123 ? 32.49672  -3.71142  -3.99182  1.000 62.52520  ? 123 LEU C N   1 
ATOM 4339 C CA  . LEU C 1 123 ? 32.39366  -2.27738  -3.76043  1.000 58.86776  ? 123 LEU C CA  1 
ATOM 4340 C C   . LEU C 1 123 ? 33.06413  -1.86585  -2.46009  1.000 60.08885  ? 123 LEU C C   1 
ATOM 4341 O O   . LEU C 1 123 ? 33.74899  -0.83880  -2.41142  1.000 61.99472  ? 123 LEU C O   1 
ATOM 4342 C CB  . LEU C 1 123 ? 30.93225  -1.85401  -3.77856  1.000 57.82095  ? 123 LEU C CB  1 
ATOM 4343 C CG  . LEU C 1 123 ? 30.69167  -0.36261  -3.51636  1.000 60.41764  ? 123 LEU C CG  1 
ATOM 4344 C CD1 . LEU C 1 123 ? 31.40735  0.52070   -4.48944  1.000 60.00165  ? 123 LEU C CD1 1 
ATOM 4345 C CD2 . LEU C 1 123 ? 29.19869  -0.04971  -3.53922  1.000 65.23279  ? 123 LEU C CD2 1 
ATOM 4346 N N   . VAL C 1 124 ? 32.87883  -2.65003  -1.39425  1.000 62.33773  ? 124 VAL C N   1 
ATOM 4347 C CA  . VAL C 1 124 ? 33.53528  -2.35999  -0.11994  1.000 61.11638  ? 124 VAL C CA  1 
ATOM 4348 C C   . VAL C 1 124 ? 35.04678  -2.51770  -0.24052  1.000 60.33615  ? 124 VAL C C   1 
ATOM 4349 O O   . VAL C 1 124 ? 35.80481  -1.78756  0.40262   1.000 61.21583  ? 124 VAL C O   1 
ATOM 4350 C CB  . VAL C 1 124 ? 32.95040  -3.25106  0.99776   1.000 60.75046  ? 124 VAL C CB  1 
ATOM 4351 C CG1 . VAL C 1 124 ? 33.70339  -3.06714  2.31742   1.000 58.97852  ? 124 VAL C CG1 1 
ATOM 4352 C CG2 . VAL C 1 124 ? 31.47752  -2.95913  1.19467   1.000 58.29442  ? 124 VAL C CG2 1 
ATOM 4353 N N   . ASP C 1 125 ? 35.51305  -3.46647  -1.05284  1.000 59.56832  ? 125 ASP C N   1 
ATOM 4354 C CA  . ASP C 1 125 ? 36.95034  -3.65187  -1.21385  1.000 59.72433  ? 125 ASP C CA  1 
ATOM 4355 C C   . ASP C 1 125 ? 37.58244  -2.51989  -2.01796  1.000 65.90093  ? 125 ASP C C   1 
ATOM 4356 O O   . ASP C 1 125 ? 38.76306  -2.20894  -1.82184  1.000 68.77918  ? 125 ASP C O   1 
ATOM 4357 C CB  . ASP C 1 125 ? 37.25159  -4.99638  -1.87838  1.000 56.79365  ? 125 ASP C CB  1 
ATOM 4358 C CG  . ASP C 1 125 ? 38.72857  -5.29427  -1.89776  1.000 60.26143  ? 125 ASP C CG  1 
ATOM 4359 O OD1 . ASP C 1 125 ? 39.26540  -5.67018  -0.84609  1.000 65.99137  ? 125 ASP C OD1 1 
ATOM 4360 O OD2 . ASP C 1 125 ? 39.38199  -5.10622  -2.93857  1.000 62.62088  ? 125 ASP C OD2 1 
ATOM 4361 N N   . LEU C 1 126 ? 36.83496  -1.91131  -2.94273  1.000 61.94687  ? 126 LEU C N   1 
ATOM 4362 C CA  . LEU C 1 126 ? 37.32975  -0.70098  -3.58758  1.000 65.83588  ? 126 LEU C CA  1 
ATOM 4363 C C   . LEU C 1 126 ? 37.33517  0.48264   -2.61533  1.000 66.79107  ? 126 LEU C C   1 
ATOM 4364 O O   . LEU C 1 126 ? 38.25549  1.31082   -2.64316  1.000 69.40209  ? 126 LEU C O   1 
ATOM 4365 C CB  . LEU C 1 126 ? 36.50185  -0.39609  -4.84006  1.000 64.59435  ? 126 LEU C CB  1 
ATOM 4366 C CG  . LEU C 1 126 ? 36.65038  -1.43849  -5.94507  1.000 60.86088  ? 126 LEU C CG  1 
ATOM 4367 C CD1 . LEU C 1 126 ? 35.70906  -1.15672  -7.07839  1.000 63.36486  ? 126 LEU C CD1 1 
ATOM 4368 C CD2 . LEU C 1 126 ? 38.08230  -1.49689  -6.44230  1.000 60.19215  ? 126 LEU C CD2 1 
ATOM 4369 N N   . ILE C 1 127 ? 36.32860  0.57718   -1.74029  1.000 61.89116  ? 127 ILE C N   1 
ATOM 4370 C CA  . ILE C 1 127 ? 36.33820  1.61606   -0.70796  1.000 66.43460  ? 127 ILE C CA  1 
ATOM 4371 C C   . ILE C 1 127 ? 37.45652  1.37998   0.31153   1.000 67.95368  ? 127 ILE C C   1 
ATOM 4372 O O   . ILE C 1 127 ? 38.08565  2.32769   0.78881   1.000 69.83640  ? 127 ILE C O   1 
ATOM 4373 C CB  . ILE C 1 127 ? 34.97201  1.70045   -0.01390  1.000 67.69887  ? 127 ILE C CB  1 
ATOM 4374 C CG1 . ILE C 1 127 ? 33.87945  2.05252   -1.01188  1.000 65.66234  ? 127 ILE C CG1 1 
ATOM 4375 C CG2 . ILE C 1 127 ? 35.01302  2.73376   1.08203   1.000 70.86305  ? 127 ILE C CG2 1 
ATOM 4376 C CD1 . ILE C 1 127 ? 32.48674  1.89259   -0.43932  1.000 65.12889  ? 127 ILE C CD1 1 
ATOM 4377 N N   . ARG C 1 128 ? 37.71185  0.12634   0.68431   1.000 71.68288  ? 128 ARG C N   1 
ATOM 4378 C CA  . ARG C 1 128 ? 38.85299  -0.14242  1.55316   1.000 71.45367  ? 128 ARG C CA  1 
ATOM 4379 C C   . ARG C 1 128 ? 40.18017  0.28166   0.90531   1.000 73.40077  ? 128 ARG C C   1 
ATOM 4380 O O   . ARG C 1 128 ? 41.15851  0.49361   1.62787   1.000 74.11186  ? 128 ARG C O   1 
ATOM 4381 C CB  . ARG C 1 128 ? 38.89217  -1.63921  1.96444   1.000 69.54426  ? 128 ARG C CB  1 
ATOM 4382 C CG  . ARG C 1 128 ? 37.67212  -2.18602  2.80627   1.000 69.68059  ? 128 ARG C CG  1 
ATOM 4383 C CD  . ARG C 1 128 ? 37.84238  -3.67553  3.27920   1.000 72.68191  ? 128 ARG C CD  1 
ATOM 4384 N NE  . ARG C 1 128 ? 36.62605  -4.36397  3.74187   1.000 76.83126  ? 128 ARG C NE  1 
ATOM 4385 C CZ  . ARG C 1 128 ? 36.11499  -4.31795  4.97556   1.000 81.79154  ? 128 ARG C CZ  1 
ATOM 4386 N NH1 . ARG C 1 128 ? 36.61868  -3.52861  5.92088   1.000 77.47588  ? 128 ARG C NH1 1 
ATOM 4387 N NH2 . ARG C 1 128 ? 35.05382  -5.06819  5.26594   1.000 78.71827  ? 128 ARG C NH2 1 
ATOM 4388 N N   . ASP C 1 129 ? 40.24605  0.41188   -0.43586  1.000 71.44245  ? 129 ASP C N   1 
ATOM 4389 C CA  . ASP C 1 129 ? 41.48075  0.87466   -1.08549  1.000 72.97636  ? 129 ASP C CA  1 
ATOM 4390 C C   . ASP C 1 129 ? 41.79973  2.33127   -0.76799  1.000 73.58236  ? 129 ASP C C   1 
ATOM 4391 O O   . ASP C 1 129 ? 42.97807  2.70707   -0.73064  1.000 73.33544  ? 129 ASP C O   1 
ATOM 4392 C CB  . ASP C 1 129 ? 41.42462  0.73153   -2.61213  1.000 79.09704  ? 129 ASP C CB  1 
ATOM 4393 C CG  . ASP C 1 129 ? 41.74931  -0.67027  -3.10512  1.000 79.48882  ? 129 ASP C CG  1 
ATOM 4394 O OD1 . ASP C 1 129 ? 42.38928  -1.44116  -2.35211  1.000 77.85427  ? 129 ASP C OD1 1 
ATOM 4395 O OD2 . ASP C 1 129 ? 41.42346  -0.95684  -4.29006  1.000 79.07452  ? 129 ASP C OD2 1 
ATOM 4396 N N   . ILE C 1 130 ? 40.77022  3.17170   -0.61112  1.000 73.15812  ? 130 ILE C N   1 
ATOM 4397 C CA  . ILE C 1 130 ? 40.96098  4.53473   -0.11379  1.000 68.87555  ? 130 ILE C CA  1 
ATOM 4398 C C   . ILE C 1 130 ? 41.83032  4.52390   1.13220   1.000 71.08234  ? 130 ILE C C   1 
ATOM 4399 O O   . ILE C 1 130 ? 42.82936  5.24686   1.22754   1.000 71.50469  ? 130 ILE C O   1 
ATOM 4400 C CB  . ILE C 1 130 ? 39.60318  5.17536   0.19763   1.000 67.45832  ? 130 ILE C CB  1 
ATOM 4401 C CG1 . ILE C 1 130 ? 38.73432  5.26143   -1.04535  1.000 71.69836  ? 130 ILE C CG1 1 
ATOM 4402 C CG2 . ILE C 1 130 ? 39.81766  6.52523   0.79597   1.000 76.63899  ? 130 ILE C CG2 1 
ATOM 4403 C CD1 . ILE C 1 130 ? 37.27871  5.48998   -0.70866  1.000 72.61189  ? 130 ILE C CD1 1 
ATOM 4404 N N   . GLN C 1 131 ? 41.45568  3.68620   2.10593   1.000 69.96032  ? 131 GLN C N   1 
ATOM 4405 C CA  . GLN C 1 131 ? 42.16565  3.62885   3.37386   1.000 67.98588  ? 131 GLN C CA  1 
ATOM 4406 C C   . GLN C 1 131 ? 43.53404  2.99218   3.22130   1.000 67.95146  ? 131 GLN C C   1 
ATOM 4407 O O   . GLN C 1 131 ? 44.51522  3.47962   3.79149   1.000 69.40705  ? 131 GLN C O   1 
ATOM 4408 C CB  . GLN C 1 131 ? 41.32334  2.87745   4.39647   1.000 71.66718  ? 131 GLN C CB  1 
ATOM 4409 C CG  . GLN C 1 131 ? 40.04762  3.63124   4.71831   1.000 75.41366  ? 131 GLN C CG  1 
ATOM 4410 C CD  . GLN C 1 131 ? 39.23137  2.99467   5.80807   1.000 74.75162  ? 131 GLN C CD  1 
ATOM 4411 O OE1 . GLN C 1 131 ? 39.56423  1.92375   6.29400   1.000 78.88756  ? 131 GLN C OE1 1 
ATOM 4412 N NE2 . GLN C 1 131 ? 38.15635  3.66225   6.21187   1.000 77.00001  ? 131 GLN C NE2 1 
ATOM 4413 N N   . ARG C 1 132 ? 43.62651  1.90266   2.46068   1.000 70.84955  ? 132 ARG C N   1 
ATOM 4414 C CA  . ARG C 1 132 ? 44.93970  1.34945   2.15377   1.000 69.21501  ? 132 ARG C CA  1 
ATOM 4415 C C   . ARG C 1 132 ? 45.83254  2.40562   1.50994   1.000 68.47303  ? 132 ARG C C   1 
ATOM 4416 O O   . ARG C 1 132 ? 47.01823  2.51358   1.84140   1.000 63.62125  ? 132 ARG C O   1 
ATOM 4417 C CB  . ARG C 1 132 ? 44.78061  0.10466   1.28332   1.000 62.90427  ? 132 ARG C CB  1 
ATOM 4418 C CG  . ARG C 1 132 ? 44.36989  -1.10444  2.10906   1.000 71.25293  ? 132 ARG C CG  1 
ATOM 4419 C CD  . ARG C 1 132 ? 44.43598  -2.44302  1.37739   1.000 70.61450  ? 132 ARG C CD  1 
ATOM 4420 N NE  . ARG C 1 132 ? 43.30913  -2.64743  0.47968   1.000 73.94537  ? 132 ARG C NE  1 
ATOM 4421 C CZ  . ARG C 1 132 ? 42.22288  -3.34486  0.78072   1.000 70.91962  ? 132 ARG C CZ  1 
ATOM 4422 N NH1 . ARG C 1 132 ? 42.12386  -4.00522  1.92059   1.000 73.50383  ? 132 ARG C NH1 1 
ATOM 4423 N NH2 . ARG C 1 132 ? 41.22039  -3.39957  -0.09563  1.000 69.37226  ? 132 ARG C NH2 1 
ATOM 4424 N N   . LEU C 1 133 ? 45.25423  3.24297   0.64426   1.000 70.84023  ? 133 LEU C N   1 
ATOM 4425 C CA  . LEU C 1 133 ? 45.99054  4.35427   0.04766   1.000 72.02394  ? 133 LEU C CA  1 
ATOM 4426 C C   . LEU C 1 133 ? 46.47619  5.34710   1.09609   1.000 74.08297  ? 133 LEU C C   1 
ATOM 4427 O O   . LEU C 1 133 ? 47.47753  6.04260   0.87011   1.000 73.45031  ? 133 LEU C O   1 
ATOM 4428 C CB  . LEU C 1 133 ? 45.10894  5.06117   -0.98745  1.000 74.96865  ? 133 LEU C CB  1 
ATOM 4429 C CG  . LEU C 1 133 ? 45.60040  6.27147   -1.78816  1.000 72.84221  ? 133 LEU C CG  1 
ATOM 4430 C CD1 . LEU C 1 133 ? 46.81335  5.92606   -2.62278  1.000 66.72095  ? 133 LEU C CD1 1 
ATOM 4431 C CD2 . LEU C 1 133 ? 44.46971  6.77871   -2.66436  1.000 71.08017  ? 133 LEU C CD2 1 
ATOM 4432 N N   . ASN C 1 134 ? 45.77619  5.44396   2.23299   1.000 70.96620  ? 134 ASN C N   1 
ATOM 4433 C CA  . ASN C 1 134 ? 46.24466  6.23863   3.36138   1.000 67.08758  ? 134 ASN C CA  1 
ATOM 4434 C C   . ASN C 1 134 ? 47.27599  5.53473   4.22291   1.000 69.27264  ? 134 ASN C C   1 
ATOM 4435 O O   . ASN C 1 134 ? 47.86620  6.17784   5.08959   1.000 73.47645  ? 134 ASN C O   1 
ATOM 4436 C CB  . ASN C 1 134 ? 45.07399  6.64156   4.23022   1.000 69.73694  ? 134 ASN C CB  1 
ATOM 4437 C CG  . ASN C 1 134 ? 44.42678  7.88857   3.75676   1.000 74.82740  ? 134 ASN C CG  1 
ATOM 4438 O OD1 . ASN C 1 134 ? 45.08339  8.92430   3.62818   1.000 76.49549  ? 134 ASN C OD1 1 
ATOM 4439 N ND2 . ASN C 1 134 ? 43.14389  7.80233   3.43189   1.000 77.31834  ? 134 ASN C ND2 1 
ATOM 4440 N N   . GLY C 1 135 ? 47.52466  4.25356   4.01042   1.000 72.14499  ? 135 GLY C N   1 
ATOM 4441 C CA  . GLY C 1 135 ? 48.49725  3.55967   4.81572   1.000 70.46205  ? 135 GLY C CA  1 
ATOM 4442 C C   . GLY C 1 135 ? 47.92363  2.82935   5.99914   1.000 70.68520  ? 135 GLY C C   1 
ATOM 4443 O O   . GLY C 1 135 ? 48.68671  2.41476   6.87822   1.000 74.54637  ? 135 GLY C O   1 
ATOM 4444 N N   . VAL C 1 136 ? 46.60525  2.65362   6.05346   1.000 68.72796  ? 136 VAL C N   1 
ATOM 4445 C CA  . VAL C 1 136 ? 46.01735  1.89812   7.14677   1.000 74.73573  ? 136 VAL C CA  1 
ATOM 4446 C C   . VAL C 1 136 ? 46.48719  0.44681   7.07164   1.000 76.39619  ? 136 VAL C C   1 
ATOM 4447 O O   . VAL C 1 136 ? 46.69056  -0.10832  5.98749   1.000 75.60197  ? 136 VAL C O   1 
ATOM 4448 C CB  . VAL C 1 136 ? 44.48276  2.01282   7.09993   1.000 75.18380  ? 136 VAL C CB  1 
ATOM 4449 C CG1 . VAL C 1 136 ? 43.85182  1.21240   8.19711   1.000 72.91688  ? 136 VAL C CG1 1 
ATOM 4450 C CG2 . VAL C 1 136 ? 44.04690  3.46653   7.19692   1.000 69.19436  ? 136 VAL C CG2 1 
ATOM 4451 N N   . SER C 1 137 ? 46.70762  -0.15746  8.23662   1.000 79.57464  ? 137 SER C N   1 
ATOM 4452 C CA  . SER C 1 137 ? 47.02359  -1.57767  8.32464   1.000 79.79476  ? 137 SER C CA  1 
ATOM 4453 C C   . SER C 1 137 ? 45.77626  -2.40612  8.02602   1.000 81.37705  ? 137 SER C C   1 
ATOM 4454 O O   . SER C 1 137 ? 44.66371  -2.01223  8.38166   1.000 83.00903  ? 137 SER C O   1 
ATOM 4455 C CB  . SER C 1 137 ? 47.57003  -1.88882  9.72267   1.000 80.23841  ? 137 SER C CB  1 
ATOM 4456 O OG  . SER C 1 137 ? 47.87634  -3.25849  9.89634   1.000 83.27154  ? 137 SER C OG  1 
ATOM 4457 N N   . GLU C 1 138 ? 45.97055  -3.57073  7.38237   1.000 81.06476  ? 138 GLU C N   1 
ATOM 4458 C CA  . GLU C 1 138 ? 44.85339  -4.37101  6.85194   1.000 79.68244  ? 138 GLU C CA  1 
ATOM 4459 C C   . GLU C 1 138 ? 43.86673  -4.81835  7.93118   1.000 78.82824  ? 138 GLU C C   1 
ATOM 4460 O O   . GLU C 1 138 ? 42.66548  -4.95247  7.65675   1.000 75.35710  ? 138 GLU C O   1 
ATOM 4461 C CB  . GLU C 1 138 ? 45.39040  -5.60165  6.11160   1.000 78.30560  ? 138 GLU C CB  1 
ATOM 4462 C CG  . GLU C 1 138 ? 44.33085  -6.46090  5.40187   1.000 73.21545  ? 138 GLU C CG  1 
ATOM 4463 C CD  . GLU C 1 138 ? 43.64465  -5.73526  4.24139   1.000 75.41040  ? 138 GLU C CD  1 
ATOM 4464 O OE1 . GLU C 1 138 ? 44.22478  -4.75434  3.72459   1.000 77.00005  ? 138 GLU C OE1 1 
ATOM 4465 O OE2 . GLU C 1 138 ? 42.53762  -6.15330  3.82797   1.000 76.99449  ? 138 GLU C OE2 1 
ATOM 4466 N N   . ASN C 1 139 ? 44.35273  -5.09150  9.14158   1.000 78.54915  ? 139 ASN C N   1 
ATOM 4467 C CA  . ASN C 1 139 ? 43.50769  -5.40432  10.28149  1.000 75.53414  ? 139 ASN C CA  1 
ATOM 4468 C C   . ASN C 1 139 ? 42.96726  -4.15565  10.97644  1.000 76.11428  ? 139 ASN C C   1 
ATOM 4469 O O   . ASN C 1 139 ? 42.40285  -4.26425  12.06879  1.000 75.13580  ? 139 ASN C O   1 
ATOM 4470 C CB  . ASN C 1 139 ? 44.29187  -6.26297  11.27400  1.000 77.10361  ? 139 ASN C CB  1 
ATOM 4471 C CG  . ASN C 1 139 ? 45.54147  -5.56555  11.77796  1.000 78.07022  ? 139 ASN C CG  1 
ATOM 4472 O OD1 . ASN C 1 139 ? 45.79079  -4.40508  11.44311  1.000 80.13134  ? 139 ASN C OD1 1 
ATOM 4473 N ND2 . ASN C 1 139 ? 46.33776  -6.26911  12.58058  1.000 69.53479  ? 139 ASN C ND2 1 
ATOM 4474 N N   . GLU C 1 140 ? 43.16352  -2.97290  10.39622  1.000 75.74403  ? 140 GLU C N   1 
ATOM 4475 C CA  . GLU C 1 140 ? 42.64151  -1.73386  10.95981  1.000 76.15266  ? 140 GLU C CA  1 
ATOM 4476 C C   . GLU C 1 140 ? 41.80429  -0.94302  9.96805   1.000 73.34371  ? 140 GLU C C   1 
ATOM 4477 O O   . GLU C 1 140 ? 41.51861  0.23042   10.21520  1.000 75.57826  ? 140 GLU C O   1 
ATOM 4478 C CB  . GLU C 1 140 ? 43.77652  -0.85661  11.48733  1.000 77.11084  ? 140 GLU C CB  1 
ATOM 4479 C CG  . GLU C 1 140 ? 44.44435  -1.40303  12.72637  1.000 80.14650  ? 140 GLU C CG  1 
ATOM 4480 C CD  . GLU C 1 140 ? 45.61715  -0.55732  13.17933  1.000 89.22119  ? 140 GLU C CD  1 
ATOM 4481 O OE1 . GLU C 1 140 ? 46.03476  0.34791   12.41722  1.000 91.81676  ? 140 GLU C OE1 1 
ATOM 4482 O OE2 . GLU C 1 140 ? 46.11332  -0.78648  14.30638  1.000 96.27308  ? 140 GLU C OE2 1 
ATOM 4483 N N   . LEU C 1 141 ? 41.40877  -1.54825  8.85872   1.000 73.75772  ? 141 LEU C N   1 
ATOM 4484 C CA  . LEU C 1 141 ? 40.43826  -0.93727  7.96380   1.000 71.63432  ? 141 LEU C CA  1 
ATOM 4485 C C   . LEU C 1 141 ? 39.08538  -0.81467  8.64893   1.000 77.86840  ? 141 LEU C C   1 
ATOM 4486 O O   . LEU C 1 141 ? 38.54275  -1.79974  9.17196   1.000 80.52047  ? 141 LEU C O   1 
ATOM 4487 C CB  . LEU C 1 141 ? 40.30274  -1.77952  6.70312   1.000 71.66523  ? 141 LEU C CB  1 
ATOM 4488 C CG  . LEU C 1 141 ? 41.24296  -1.57080  5.52995   1.000 73.50099  ? 141 LEU C CG  1 
ATOM 4489 C CD1 . LEU C 1 141 ? 42.69077  -1.70179  5.90177   1.000 74.15202  ? 141 LEU C CD1 1 
ATOM 4490 C CD2 . LEU C 1 141 ? 40.89343  -2.70580  4.63741   1.000 74.64653  ? 141 LEU C CD2 1 
ATOM 4491 N N   . ASP C 1 142 ? 38.52854  0.39394   8.63381   1.000 74.62842  ? 142 ASP C N   1 
ATOM 4492 C CA  . ASP C 1 142 ? 37.16929  0.61288   9.11675   1.000 75.65374  ? 142 ASP C CA  1 
ATOM 4493 C C   . ASP C 1 142 ? 36.46872  1.53129   8.13509   1.000 73.84657  ? 142 ASP C C   1 
ATOM 4494 O O   . ASP C 1 142 ? 36.75376  2.72705   8.08957   1.000 77.29524  ? 142 ASP C O   1 
ATOM 4495 C CB  . ASP C 1 142 ? 37.15747  1.20057   10.52263  1.000 81.15170  ? 142 ASP C CB  1 
ATOM 4496 C CG  . ASP C 1 142 ? 35.75767  1.37766   11.05440  1.000 84.42590  ? 142 ASP C CG  1 
ATOM 4497 O OD1 . ASP C 1 142 ? 35.11234  0.35167   11.37962  1.000 86.11370  ? 142 ASP C OD1 1 
ATOM 4498 O OD2 . ASP C 1 142 ? 35.30627  2.54448   11.13883  1.000 87.73676  ? 142 ASP C OD2 1 
ATOM 4499 N N   . THR C 1 143 ? 35.55528  0.97487   7.35395   1.000 75.25354  ? 143 THR C N   1 
ATOM 4500 C CA  . THR C 1 143 ? 34.94770  1.69175   6.24651   1.000 78.18533  ? 143 THR C CA  1 
ATOM 4501 C C   . THR C 1 143 ? 33.48213  1.99390   6.51305   1.000 82.52723  ? 143 THR C C   1 
ATOM 4502 O O   . THR C 1 143 ? 32.73512  2.27539   5.56966   1.000 80.55491  ? 143 THR C O   1 
ATOM 4503 C CB  . THR C 1 143 ? 35.10392  0.89166   4.94963   1.000 76.52704  ? 143 THR C CB  1 
ATOM 4504 O OG1 . THR C 1 143 ? 34.24067  -0.25389  4.96839   1.000 76.76364  ? 143 THR C OG1 1 
ATOM 4505 C CG2 . THR C 1 143 ? 36.53147  0.40107   4.82253   1.000 71.12014  ? 143 THR C CG2 1 
ATOM 4506 N N   . PHE C 1 144 ? 33.06297  1.93972   7.78641   1.000 81.20906  ? 144 PHE C N   1 
ATOM 4507 C CA  . PHE C 1 144 ? 31.65388  2.12212   8.13273   1.000 79.16496  ? 144 PHE C CA  1 
ATOM 4508 C C   . PHE C 1 144 ? 31.11140  3.44524   7.60150   1.000 80.50002  ? 144 PHE C C   1 
ATOM 4509 O O   . PHE C 1 144 ? 30.09671  3.47514   6.89212   1.000 80.08694  ? 144 PHE C O   1 
ATOM 4510 C CB  . PHE C 1 144 ? 31.47731  2.03236   9.65144   1.000 80.69420  ? 144 PHE C CB  1 
ATOM 4511 C CG  . PHE C 1 144 ? 30.04033  2.16665   10.11828  1.000 81.60475  ? 144 PHE C CG  1 
ATOM 4512 C CD1 . PHE C 1 144 ? 29.10810  1.17584   9.84140   1.000 79.14187  ? 144 PHE C CD1 1 
ATOM 4513 C CD2 . PHE C 1 144 ? 29.63898  3.26410   10.87299  1.000 81.11000  ? 144 PHE C CD2 1 
ATOM 4514 C CE1 . PHE C 1 144 ? 27.80445  1.29962   10.26544  1.000 78.81571  ? 144 PHE C CE1 1 
ATOM 4515 C CE2 . PHE C 1 144 ? 28.33179  3.38843   11.31087  1.000 78.02849  ? 144 PHE C CE2 1 
ATOM 4516 C CZ  . PHE C 1 144 ? 27.41370  2.41060   11.00836  1.000 79.11754  ? 144 PHE C CZ  1 
ATOM 4517 N N   . LYS C 1 145 ? 31.78621  4.55261   7.90536   1.000 79.67507  ? 145 LYS C N   1 
ATOM 4518 C CA  . LYS C 1 145 ? 31.25874  5.82587   7.43971   1.000 78.36526  ? 145 LYS C CA  1 
ATOM 4519 C C   . LYS C 1 145 ? 31.39419  5.96981   5.92786   1.000 83.80836  ? 145 LYS C C   1 
ATOM 4520 O O   . LYS C 1 145 ? 30.60985  6.69419   5.30491   1.000 90.37380  ? 145 LYS C O   1 
ATOM 4521 C CB  . LYS C 1 145 ? 31.94081  6.98697   8.16366   1.000 78.09322  ? 145 LYS C CB  1 
ATOM 4522 C CG  . LYS C 1 145 ? 33.41418  7.08726   7.90466   1.000 82.34016  ? 145 LYS C CG  1 
ATOM 4523 C CD  . LYS C 1 145 ? 34.00913  8.35495   8.50428   1.000 88.04908  ? 145 LYS C CD  1 
ATOM 4524 C CE  . LYS C 1 145 ? 35.46871  8.51734   8.07312   1.000 88.65192  ? 145 LYS C CE  1 
ATOM 4525 N NZ  . LYS C 1 145 ? 36.02547  9.84135   8.45378   1.000 91.70749  ? 145 LYS C NZ  1 
ATOM 4526 N N   . LEU C 1 146 ? 32.35148  5.27683   5.30996   1.000 82.86060  ? 146 LEU C N   1 
ATOM 4527 C CA  . LEU C 1 146 ? 32.59314  5.46972   3.88225   1.000 80.61523  ? 146 LEU C CA  1 
ATOM 4528 C C   . LEU C 1 146 ? 31.59959  4.72539   2.98540   1.000 77.98456  ? 146 LEU C C   1 
ATOM 4529 O O   . LEU C 1 146 ? 31.43092  5.11307   1.82902   1.000 81.18594  ? 146 LEU C O   1 
ATOM 4530 C CB  . LEU C 1 146 ? 34.02892  5.05198   3.52960   1.000 77.33431  ? 146 LEU C CB  1 
ATOM 4531 C CG  . LEU C 1 146 ? 35.20386  5.99134   3.84857   1.000 76.95762  ? 146 LEU C CG  1 
ATOM 4532 C CD1 . LEU C 1 146 ? 35.51477  6.04795   5.33301   1.000 80.80142  ? 146 LEU C CD1 1 
ATOM 4533 C CD2 . LEU C 1 146 ? 36.44633  5.57608   3.09242   1.000 75.82552  ? 146 LEU C CD2 1 
ATOM 4534 N N   . GLU C 1 147 ? 30.95100  3.67678   3.47182   1.000 75.54620  ? 147 GLU C N   1 
ATOM 4535 C CA  . GLU C 1 147 ? 30.05440  2.89389   2.63106   1.000 74.67920  ? 147 GLU C CA  1 
ATOM 4536 C C   . GLU C 1 147 ? 28.83189  3.73405   2.26833   1.000 77.98138  ? 147 GLU C C   1 
ATOM 4537 O O   . GLU C 1 147 ? 28.32623  4.47405   3.11637   1.000 82.15693  ? 147 GLU C O   1 
ATOM 4538 C CB  . GLU C 1 147 ? 29.62804  1.62196   3.37925   1.000 80.35559  ? 147 GLU C CB  1 
ATOM 4539 C CG  . GLU C 1 147 ? 30.79031  0.67315   3.71208   1.000 75.80425  ? 147 GLU C CG  1 
ATOM 4540 C CD  . GLU C 1 147 ? 30.48926  -0.29373  4.86456   1.000 84.32718  ? 147 GLU C CD  1 
ATOM 4541 O OE1 . GLU C 1 147 ? 29.38383  -0.22374  5.46864   1.000 82.93014  ? 147 GLU C OE1 1 
ATOM 4542 O OE2 . GLU C 1 147 ? 31.39807  -1.09137  5.21134   1.000 85.37305  ? 147 GLU C OE2 1 
ATOM 4543 N N   . PRO C 1 148 ? 28.33377  3.64963   1.02258   1.000 82.90092  ? 148 PRO C N   1 
ATOM 4544 C CA  . PRO C 1 148 ? 27.15665  4.45941   0.63983   1.000 83.26010  ? 148 PRO C CA  1 
ATOM 4545 C C   . PRO C 1 148 ? 25.86595  4.05380   1.33303   1.000 81.98371  ? 148 PRO C C   1 
ATOM 4546 O O   . PRO C 1 148 ? 24.88850  4.80451   1.25761   1.000 83.93476  ? 148 PRO C O   1 
ATOM 4547 C CB  . PRO C 1 148 ? 27.05302  4.24735   -0.87717  1.000 77.82303  ? 148 PRO C CB  1 
ATOM 4548 C CG  . PRO C 1 148 ? 27.68269  2.93550   -1.11726  1.000 76.09934  ? 148 PRO C CG  1 
ATOM 4549 C CD  . PRO C 1 148 ? 28.81319  2.83243   -0.10851  1.000 79.66542  ? 148 PRO C CD  1 
ATOM 4550 N N   . CYS C 1 149 ? 25.81547  2.89288   1.97509   1.000 81.02986  ? 149 CYS C N   1 
ATOM 4551 C CA  . CYS C 1 149 ? 24.66967  2.54569   2.79439   1.000 82.95981  ? 149 CYS C CA  1 
ATOM 4552 C C   . CYS C 1 149 ? 25.15343  1.66109   3.93845   1.000 83.34807  ? 149 CYS C C   1 
ATOM 4553 O O   . CYS C 1 149 ? 26.19318  1.00325   3.84426   1.000 84.98209  ? 149 CYS C O   1 
ATOM 4554 C CB  . CYS C 1 149 ? 23.56771  1.85600   1.96955   1.000 83.35334  ? 149 CYS C CB  1 
ATOM 4555 S SG  . CYS C 1 149 ? 23.85763  0.11772   1.50454   1.000 83.45060  ? 149 CYS C SG  1 
ATOM 4556 N N   . LYS C 1 150 ? 24.39754  1.67435   5.03434   1.000 86.68244  ? 150 LYS C N   1 
ATOM 4557 C CA  . LYS C 1 150 ? 24.69177  0.80888   6.17123   1.000 83.16169  ? 150 LYS C CA  1 
ATOM 4558 C C   . LYS C 1 150 ? 24.50423  -0.64834  5.77813   1.000 82.16465  ? 150 LYS C C   1 
ATOM 4559 O O   . LYS C 1 150 ? 23.54060  -0.99856  5.08904   1.000 84.51994  ? 150 LYS C O   1 
ATOM 4560 C CB  . LYS C 1 150 ? 23.78214  1.15805   7.34717   1.000 77.08076  ? 150 LYS C CB  1 
ATOM 4561 C CG  . LYS C 1 150 ? 23.91009  2.59316   7.74892   1.000 74.63110  ? 150 LYS C CG  1 
ATOM 4562 C CD  . LYS C 1 150 ? 25.31950  2.85504   8.16616   1.000 71.68351  ? 150 LYS C CD  1 
ATOM 4563 C CE  . LYS C 1 150 ? 25.51082  4.29987   8.48890   1.000 76.23887  ? 150 LYS C CE  1 
ATOM 4564 N NZ  . LYS C 1 150 ? 26.93072  4.61281   8.77959   1.000 75.86206  ? 150 LYS C NZ  1 
ATOM 4565 N N   . PHE C 1 151 ? 25.41338  -1.51212  6.23755   1.000 76.40372  ? 151 PHE C N   1 
ATOM 4566 C CA  . PHE C 1 151 ? 25.37057  -2.88377  5.75126   1.000 76.11013  ? 151 PHE C CA  1 
ATOM 4567 C C   . PHE C 1 151 ? 24.04873  -3.56869  6.08926   1.000 81.02270  ? 151 PHE C C   1 
ATOM 4568 O O   . PHE C 1 151 ? 23.72695  -4.60035  5.48784   1.000 79.56140  ? 151 PHE C O   1 
ATOM 4569 C CB  . PHE C 1 151 ? 26.54248  -3.68128  6.30865   1.000 70.43168  ? 151 PHE C CB  1 
ATOM 4570 C CG  . PHE C 1 151 ? 26.41940  -3.98996  7.74989   1.000 76.20226  ? 151 PHE C CG  1 
ATOM 4571 C CD1 . PHE C 1 151 ? 26.93648  -3.12333  8.70395   1.000 77.91006  ? 151 PHE C CD1 1 
ATOM 4572 C CD2 . PHE C 1 151 ? 25.77306  -5.15234  8.17200   1.000 77.85494  ? 151 PHE C CD2 1 
ATOM 4573 C CE1 . PHE C 1 151 ? 26.81025  -3.40818  10.06680  1.000 73.28965  ? 151 PHE C CE1 1 
ATOM 4574 C CE2 . PHE C 1 151 ? 25.64263  -5.43649  9.52156   1.000 73.97428  ? 151 PHE C CE2 1 
ATOM 4575 C CZ  . PHE C 1 151 ? 26.16852  -4.56270  10.47053  1.000 68.66024  ? 151 PHE C CZ  1 
ATOM 4576 N N   . TRP C 1 152 ? 23.27807  -3.02622  7.04488   1.000 82.39624  ? 152 TRP C N   1 
ATOM 4577 C CA  . TRP C 1 152 ? 21.93551  -3.53330  7.29883   1.000 81.97049  ? 152 TRP C CA  1 
ATOM 4578 C C   . TRP C 1 152 ? 20.90259  -2.95711  6.34354   1.000 86.76727  ? 152 TRP C C   1 
ATOM 4579 O O   . TRP C 1 152 ? 19.78359  -3.47144  6.30375   1.000 89.97162  ? 152 TRP C O   1 
ATOM 4580 C CB  . TRP C 1 152 ? 21.49715  -3.28128  8.76140   1.000 81.44784  ? 152 TRP C CB  1 
ATOM 4581 C CG  . TRP C 1 152 ? 21.37777  -1.83973  9.22289   1.000 77.28408  ? 152 TRP C CG  1 
ATOM 4582 C CD1 . TRP C 1 152 ? 20.29304  -1.00778  9.07815   1.000 78.39765  ? 152 TRP C CD1 1 
ATOM 4583 C CD2 . TRP C 1 152 ? 22.35907  -1.08894  9.94654   1.000 72.27527  ? 152 TRP C CD2 1 
ATOM 4584 N NE1 . TRP C 1 152 ? 20.56288  0.22538   9.63002   1.000 72.50736  ? 152 TRP C NE1 1 
ATOM 4585 C CE2 . TRP C 1 152 ? 21.82280  0.19796   10.17091  1.000 70.64062  ? 152 TRP C CE2 1 
ATOM 4586 C CE3 . TRP C 1 152 ? 23.65201  -1.37021  10.40160  1.000 70.34027  ? 152 TRP C CE3 1 
ATOM 4587 C CZ2 . TRP C 1 152 ? 22.53559  1.19337   10.82991  1.000 70.89622  ? 152 TRP C CZ2 1 
ATOM 4588 C CZ3 . TRP C 1 152 ? 24.35700  -0.38092  11.05204  1.000 67.60970  ? 152 TRP C CZ3 1 
ATOM 4589 C CH2 . TRP C 1 152 ? 23.79999  0.88364   11.26200  1.000 70.15492  ? 152 TRP C CH2 1 
ATOM 4590 N N   . ASN C 1 153 ? 21.24874  -1.92710  5.56350   1.000 97.44533  ? 153 ASN C N   1 
ATOM 4591 C CA  . ASN C 1 153 ? 20.34576  -1.38995  4.54535   1.000 98.99867  ? 153 ASN C CA  1 
ATOM 4592 C C   . ASN C 1 153 ? 20.52496  -2.00461  3.15894   1.000 99.91311  ? 153 ASN C C   1 
ATOM 4593 O O   . ASN C 1 153 ? 19.68032  -1.76576  2.28956   1.000 102.32000 ? 153 ASN C O   1 
ATOM 4594 C CB  . ASN C 1 153 ? 20.50631  0.12570   4.40726   1.000 98.53509  ? 153 ASN C CB  1 
ATOM 4595 C CG  . ASN C 1 153 ? 20.03997  0.86867   5.62063   1.000 99.39079  ? 153 ASN C CG  1 
ATOM 4596 O OD1 . ASN C 1 153 ? 20.81339  1.57248   6.26383   1.000 99.31224  ? 153 ASN C OD1 1 
ATOM 4597 N ND2 . ASN C 1 153 ? 18.76884  0.70625   5.95571   1.000 100.69931 ? 153 ASN C ND2 1 
ATOM 4598 N N   . GLN C 1 154 ? 21.59424  -2.76409  2.92137   1.000 91.22238  ? 154 GLN C N   1 
ATOM 4599 C CA  . GLN C 1 154 ? 21.75791  -3.44039  1.64114   1.000 87.28861  ? 154 GLN C CA  1 
ATOM 4600 C C   . GLN C 1 154 ? 20.60478  -4.40477  1.41825   1.000 91.20108  ? 154 GLN C C   1 
ATOM 4601 O O   . GLN C 1 154 ? 20.12588  -5.04088  2.35608   1.000 96.48026  ? 154 GLN C O   1 
ATOM 4602 C CB  . GLN C 1 154 ? 23.06392  -4.21553  1.61467   1.000 80.59638  ? 154 GLN C CB  1 
ATOM 4603 C CG  . GLN C 1 154 ? 24.29759  -3.39000  1.81535   1.000 79.13401  ? 154 GLN C CG  1 
ATOM 4604 C CD  . GLN C 1 154 ? 25.51608  -4.26772  1.90096   1.000 74.75795  ? 154 GLN C CD  1 
ATOM 4605 O OE1 . GLN C 1 154 ? 25.41192  -5.47924  1.76196   1.000 71.24716  ? 154 GLN C OE1 1 
ATOM 4606 N NE2 . GLN C 1 154 ? 26.66657  -3.67539  2.18921   1.000 75.05950  ? 154 GLN C NE2 1 
ATOM 4607 N N   . ARG C 1 155 ? 20.14986  -4.51249  0.17489   1.000 88.77157  ? 155 ARG C N   1 
ATOM 4608 C CA  . ARG C 1 155 ? 19.02951  -5.38302  -0.13949  1.000 90.81186  ? 155 ARG C CA  1 
ATOM 4609 C C   . ARG C 1 155 ? 19.31618  -6.14074  -1.42255  1.000 92.98990  ? 155 ARG C C   1 
ATOM 4610 O O   . ARG C 1 155 ? 20.14150  -5.73014  -2.24294  1.000 93.88402  ? 155 ARG C O   1 
ATOM 4611 C CB  . ARG C 1 155 ? 17.71602  -4.61459  -0.25665  1.000 96.39767  ? 155 ARG C CB  1 
ATOM 4612 C CG  . ARG C 1 155 ? 17.23234  -4.04671  1.05683   1.000 103.60435 ? 155 ARG C CG  1 
ATOM 4613 C CD  . ARG C 1 155 ? 16.92330  -5.16545  2.04548   1.000 103.82388 ? 155 ARG C CD  1 
ATOM 4614 N NE  . ARG C 1 155 ? 16.26813  -4.68110  3.25442   1.000 106.39936 ? 155 ARG C NE  1 
ATOM 4615 C CZ  . ARG C 1 155 ? 16.90030  -4.18527  4.31031   1.000 106.67140 ? 155 ARG C CZ  1 
ATOM 4616 N NH1 . ARG C 1 155 ? 18.20763  -3.97391  4.29770   1.000 101.73612 ? 155 ARG C NH1 1 
ATOM 4617 N NH2 . ARG C 1 155 ? 16.20156  -3.88553  5.40413   1.000 108.15727 ? 155 ARG C NH2 1 
ATOM 4618 N N   . ASP C 1 156 ? 18.62664  -7.26721  -1.57258  1.000 94.96703  ? 156 ASP C N   1 
ATOM 4619 C CA  . ASP C 1 156 ? 18.88592  -8.22851  -2.63460  1.000 94.67954  ? 156 ASP C CA  1 
ATOM 4620 C C   . ASP C 1 156 ? 17.79818  -8.10775  -3.69327  1.000 100.63923 ? 156 ASP C C   1 
ATOM 4621 O O   . ASP C 1 156 ? 16.60935  -8.10912  -3.36250  1.000 103.02934 ? 156 ASP C O   1 
ATOM 4622 C CB  . ASP C 1 156 ? 18.91719  -9.64508  -2.06255  1.000 97.66097  ? 156 ASP C CB  1 
ATOM 4623 C CG  . ASP C 1 156 ? 19.40324  -10.67049 -3.05429  1.000 97.18240  ? 156 ASP C CG  1 
ATOM 4624 O OD1 . ASP C 1 156 ? 20.62536  -10.72250 -3.28907  1.000 95.35118  ? 156 ASP C OD1 1 
ATOM 4625 O OD2 . ASP C 1 156 ? 18.57055  -11.43178 -3.59106  1.000 100.14930 ? 156 ASP C OD2 1 
ATOM 4626 N N   . ILE C 1 157 ? 18.20427  -7.98833  -4.96090  1.000 101.42106 ? 157 ILE C N   1 
ATOM 4627 C CA  . ILE C 1 157 ? 17.23206  -7.83208  -6.03907  1.000 97.88508  ? 157 ILE C CA  1 
ATOM 4628 C C   . ILE C 1 157 ? 16.39543  -9.09178  -6.20122  1.000 101.04379 ? 157 ILE C C   1 
ATOM 4629 O O   . ILE C 1 157 ? 15.16399  -9.02426  -6.28527  1.000 101.50216 ? 157 ILE C O   1 
ATOM 4630 C CB  . ILE C 1 157 ? 17.93050  -7.45538  -7.35508  1.000 101.12332 ? 157 ILE C CB  1 
ATOM 4631 C CG1 . ILE C 1 157 ? 18.56165  -6.06691  -7.26094  1.000 99.44414  ? 157 ILE C CG1 1 
ATOM 4632 C CG2 . ILE C 1 157 ? 16.95055  -7.51820  -8.50374  1.000 104.90862 ? 157 ILE C CG2 1 
ATOM 4633 C CD1 . ILE C 1 157 ? 17.59406  -4.97117  -7.03620  1.000 96.41486  ? 157 ILE C CD1 1 
ATOM 4634 N N   . ARG C 1 158 ? 17.03901  -10.26118 -6.25237  1.000 101.76445 ? 158 ARG C N   1 
ATOM 4635 C CA  . ARG C 1 158 ? 16.25730  -11.45647 -6.55119  1.000 105.82409 ? 158 ARG C CA  1 
ATOM 4636 C C   . ARG C 1 158 ? 15.61288  -12.08172 -5.31623  1.000 109.49107 ? 158 ARG C C   1 
ATOM 4637 O O   . ARG C 1 158 ? 14.83515  -13.02667 -5.46935  1.000 113.60975 ? 158 ARG C O   1 
ATOM 4638 C CB  . ARG C 1 158 ? 17.09731  -12.50789 -7.29591  1.000 108.10097 ? 158 ARG C CB  1 
ATOM 4639 C CG  . ARG C 1 158 ? 18.10405  -13.29510 -6.48412  1.000 109.04848 ? 158 ARG C CG  1 
ATOM 4640 C CD  . ARG C 1 158 ? 18.74875  -14.40761 -7.34273  1.000 109.94726 ? 158 ARG C CD  1 
ATOM 4641 N NE  . ARG C 1 158 ? 19.68072  -13.92404 -8.36025  1.000 108.94058 ? 158 ARG C NE  1 
ATOM 4642 C CZ  . ARG C 1 158 ? 20.99037  -13.80090 -8.17397  1.000 107.52155 ? 158 ARG C CZ  1 
ATOM 4643 N NH1 . ARG C 1 158 ? 21.55957  -14.14255 -7.02816  1.000 107.52647 ? 158 ARG C NH1 1 
ATOM 4644 N NH2 . ARG C 1 158 ? 21.74926  -13.32679 -9.16004  1.000 104.44796 ? 158 ARG C NH2 1 
ATOM 4645 N N   . THR C 1 159 ? 15.91107  -11.59037 -4.10706  1.000 108.32305 ? 159 THR C N   1 
ATOM 4646 C CA  . THR C 1 159 ? 15.10637  -11.93581 -2.93573  1.000 110.28558 ? 159 THR C CA  1 
ATOM 4647 C C   . THR C 1 159 ? 13.85991  -11.06096 -2.84127  1.000 111.98171 ? 159 THR C C   1 
ATOM 4648 O O   . THR C 1 159 ? 12.75830  -11.56196 -2.59186  1.000 114.92719 ? 159 THR C O   1 
ATOM 4649 C CB  . THR C 1 159 ? 15.93985  -11.81443 -1.65164  1.000 110.92641 ? 159 THR C CB  1 
ATOM 4650 O OG1 . THR C 1 159 ? 16.93946  -12.83946 -1.62608  1.000 111.82937 ? 159 THR C OG1 1 
ATOM 4651 C CG2 . THR C 1 159 ? 15.06451  -11.93579 -0.40398  1.000 109.21271 ? 159 THR C CG2 1 
ATOM 4652 N N   . ARG C 1 160 ? 14.02248  -9.75083  -3.03080  1.000 110.02328 ? 160 ARG C N   1 
ATOM 4653 C CA  . ARG C 1 160 ? 12.88820  -8.83332  -3.04166  1.000 109.88048 ? 160 ARG C CA  1 
ATOM 4654 C C   . ARG C 1 160 ? 11.79589  -9.30981  -3.98314  1.000 116.48434 ? 160 ARG C C   1 
ATOM 4655 O O   . ARG C 1 160 ? 10.62624  -9.39000  -3.60462  1.000 120.15684 ? 160 ARG C O   1 
ATOM 4656 C CB  . ARG C 1 160 ? 13.35663  -7.45322  -3.48069  1.000 107.64479 ? 160 ARG C CB  1 
ATOM 4657 C CG  . ARG C 1 160 ? 12.27738  -6.41248  -3.57103  1.000 106.03375 ? 160 ARG C CG  1 
ATOM 4658 C CD  . ARG C 1 160 ? 11.95557  -5.88902  -2.21967  1.000 107.31997 ? 160 ARG C CD  1 
ATOM 4659 N NE  . ARG C 1 160 ? 11.10563  -4.71248  -2.29473  1.000 105.47166 ? 160 ARG C NE  1 
ATOM 4660 C CZ  . ARG C 1 160 ? 10.77251  -3.98045  -1.24176  1.000 105.82364 ? 160 ARG C CZ  1 
ATOM 4661 N NH1 . ARG C 1 160 ? 11.24088  -4.25635  -0.03441  1.000 107.07084 ? 160 ARG C NH1 1 
ATOM 4662 N NH2 . ARG C 1 160 ? 9.97815   -2.92715  -1.40830  1.000 100.48667 ? 160 ARG C NH2 1 
ATOM 4663 N N   . ILE C 1 161 ? 12.16558  -9.63479  -5.22142  1.000 122.12139 ? 161 ILE C N   1 
ATOM 4664 C CA  . ILE C 1 161 ? 11.16776  -9.93845  -6.24315  1.000 124.88949 ? 161 ILE C CA  1 
ATOM 4665 C C   . ILE C 1 161 ? 10.46069  -11.25217 -5.94054  1.000 127.15699 ? 161 ILE C C   1 
ATOM 4666 O O   . ILE C 1 161 ? 9.22914   -11.34116 -6.00845  1.000 128.86570 ? 161 ILE C O   1 
ATOM 4667 C CB  . ILE C 1 161 ? 11.81997  -9.95079  -7.63560  1.000 123.14096 ? 161 ILE C CB  1 
ATOM 4668 C CG1 . ILE C 1 161 ? 12.35921  -8.56018  -7.94524  1.000 119.73937 ? 161 ILE C CG1 1 
ATOM 4669 C CG2 . ILE C 1 161 ? 10.83238  -10.40460 -8.69266  1.000 128.72123 ? 161 ILE C CG2 1 
ATOM 4670 C CD1 . ILE C 1 161 ? 11.30608  -7.50162  -7.85106  1.000 120.18699 ? 161 ILE C CD1 1 
ATOM 4671 N N   . GLU C 1 162 ? 11.22664  -12.29069 -5.60746  1.000 121.31543 ? 162 GLU C N   1 
ATOM 4672 C CA  . GLU C 1 162 ? 10.62634  -13.58615 -5.31759  1.000 123.05340 ? 162 GLU C CA  1 
ATOM 4673 C C   . GLU C 1 162 ? 9.66607   -13.49906 -4.13432  1.000 124.69253 ? 162 GLU C C   1 
ATOM 4674 O O   . GLU C 1 162 ? 8.67741   -14.24110 -4.07865  1.000 125.15296 ? 162 GLU C O   1 
ATOM 4675 C CB  . GLU C 1 162 ? 11.73877  -14.60739 -5.07652  1.000 123.74914 ? 162 GLU C CB  1 
ATOM 4676 C CG  . GLU C 1 162 ? 11.29252  -16.02676 -4.80898  1.000 125.48597 ? 162 GLU C CG  1 
ATOM 4677 C CD  . GLU C 1 162 ? 12.46194  -17.00747 -4.74988  1.000 124.19633 ? 162 GLU C CD  1 
ATOM 4678 O OE1 . GLU C 1 162 ? 13.61903  -16.59068 -4.96465  1.000 123.84999 ? 162 GLU C OE1 1 
ATOM 4679 O OE2 . GLU C 1 162 ? 12.22978  -18.20533 -4.48705  1.000 126.08477 ? 162 GLU C OE2 1 
ATOM 4680 N N   . ALA C 1 163 ? 9.93062   -12.59182 -3.18758  1.000 122.33449 ? 163 ALA C N   1 
ATOM 4681 C CA  . ALA C 1 163 ? 8.96401   -12.31586 -2.12857  1.000 119.19892 ? 163 ALA C CA  1 
ATOM 4682 C C   . ALA C 1 163 ? 7.77027   -11.52679 -2.65577  1.000 122.08100 ? 163 ALA C C   1 
ATOM 4683 O O   . ALA C 1 163 ? 6.62855   -11.78250 -2.25920  1.000 123.88493 ? 163 ALA C O   1 
ATOM 4684 C CB  . ALA C 1 163 ? 9.63917   -11.55890 -0.98795  1.000 115.26066 ? 163 ALA C CB  1 
ATOM 4685 N N   . LEU C 1 164 ? 8.01604   -10.56693 -3.55413  1.000 123.77564 ? 164 LEU C N   1 
ATOM 4686 C CA  . LEU C 1 164 ? 6.94417   -9.71389  -4.06206  1.000 121.94529 ? 164 LEU C CA  1 
ATOM 4687 C C   . LEU C 1 164 ? 5.90810   -10.51427 -4.83682  1.000 124.89926 ? 164 LEU C C   1 
ATOM 4688 O O   . LEU C 1 164 ? 4.71548   -10.18337 -4.82545  1.000 127.05680 ? 164 LEU C O   1 
ATOM 4689 C CB  . LEU C 1 164 ? 7.52633   -8.61116  -4.94406  1.000 118.31872 ? 164 LEU C CB  1 
ATOM 4690 C CG  . LEU C 1 164 ? 8.32720   -7.55659  -4.18505  1.000 118.93117 ? 164 LEU C CG  1 
ATOM 4691 C CD1 . LEU C 1 164 ? 9.01592   -6.59699  -5.13096  1.000 120.20368 ? 164 LEU C CD1 1 
ATOM 4692 C CD2 . LEU C 1 164 ? 7.43753   -6.81239  -3.21285  1.000 118.25218 ? 164 LEU C CD2 1 
ATOM 4693 N N   . LEU C 1 165 ? 6.33993   -11.55668 -5.53045  1.000 125.70202 ? 165 LEU C N   1 
ATOM 4694 C CA  . LEU C 1 165 ? 5.44057   -12.32355 -6.37287  1.000 126.93361 ? 165 LEU C CA  1 
ATOM 4695 C C   . LEU C 1 165 ? 4.93384   -13.59273 -5.69349  1.000 126.44633 ? 165 LEU C C   1 
ATOM 4696 O O   . LEU C 1 165 ? 4.09238   -14.28965 -6.26687  1.000 128.44160 ? 165 LEU C O   1 
ATOM 4697 C CB  . LEU C 1 165 ? 6.14153   -12.64317 -7.69761  1.000 123.51222 ? 165 LEU C CB  1 
ATOM 4698 C CG  . LEU C 1 165 ? 6.60526   -11.32412 -8.33990  1.000 122.08853 ? 165 LEU C CG  1 
ATOM 4699 C CD1 . LEU C 1 165 ? 7.40552   -11.54949 -9.60803  1.000 126.39264 ? 165 LEU C CD1 1 
ATOM 4700 C CD2 . LEU C 1 165 ? 5.45288   -10.35227 -8.58311  1.000 118.78054 ? 165 LEU C CD2 1 
ATOM 4701 N N   . LEU C 1 166 ? 5.40171   -13.88962 -4.47839  1.000 124.41275 ? 166 LEU C N   1 
ATOM 4702 C CA  . LEU C 1 166 ? 4.94682   -15.05508 -3.71541  1.000 124.58839 ? 166 LEU C CA  1 
ATOM 4703 C C   . LEU C 1 166 ? 5.03096   -16.33454 -4.55321  1.000 124.95686 ? 166 LEU C C   1 
ATOM 4704 O O   . LEU C 1 166 ? 4.11809   -17.16390 -4.56020  1.000 125.83895 ? 166 LEU C O   1 
ATOM 4705 C CB  . LEU C 1 166 ? 3.52466   -14.84142 -3.17876  1.000 126.62856 ? 166 LEU C CB  1 
ATOM 4706 C CG  . LEU C 1 166 ? 3.21662   -14.01469 -1.90644  1.000 128.40143 ? 166 LEU C CG  1 
ATOM 4707 C CD1 . LEU C 1 166 ? 3.90879   -14.57259 -0.66315  1.000 128.98099 ? 166 LEU C CD1 1 
ATOM 4708 C CD2 . LEU C 1 166 ? 3.48450   -12.50907 -2.04767  1.000 125.85241 ? 166 LEU C CD2 1 
ATOM 4709 N N   . VAL C 1 167 ? 6.13249   -16.48503 -5.28728  1.000 124.58745 ? 167 VAL C N   1 
ATOM 4710 C CA  . VAL C 1 167 ? 6.37006   -17.64845 -6.13418  1.000 124.10930 ? 167 VAL C CA  1 
ATOM 4711 C C   . VAL C 1 167 ? 7.81615   -18.08463 -5.95949  1.000 125.88894 ? 167 VAL C C   1 
ATOM 4712 O O   . VAL C 1 167 ? 8.71693   -17.24451 -5.89926  1.000 127.17512 ? 167 VAL C O   1 
ATOM 4713 C CB  . VAL C 1 167 ? 6.07923   -17.34293 -7.61783  1.000 126.46197 ? 167 VAL C CB  1 
ATOM 4714 C CG1 . VAL C 1 167 ? 6.41688   -18.55171 -8.49530  1.000 125.04948 ? 167 VAL C CG1 1 
ATOM 4715 C CG2 . VAL C 1 167 ? 4.63183   -16.92689 -7.80628  1.000 126.03460 ? 167 VAL C CG2 1 
ATOM 4716 N N   . ARG C 1 168 ? 8.03800   -19.39845 -5.88647  1.000 127.93625 ? 168 ARG C N   1 
ATOM 4717 C CA  . ARG C 1 168 ? 9.39200   -19.93844 -5.79441  1.000 127.52192 ? 168 ARG C CA  1 
ATOM 4718 C C   . ARG C 1 168 ? 10.22308  -19.53898 -7.01587  1.000 127.47177 ? 168 ARG C C   1 
ATOM 4719 O O   . ARG C 1 168 ? 9.71166   -19.46504 -8.13330  1.000 127.08910 ? 168 ARG C O   1 
ATOM 4720 C CB  . ARG C 1 168 ? 9.33821   -21.46675 -5.63508  1.000 125.08288 ? 168 ARG C CB  1 
ATOM 4721 C CG  . ARG C 1 168 ? 10.69682  -22.17961 -5.60780  1.000 122.13301 ? 168 ARG C CG  1 
ATOM 4722 C CD  . ARG C 1 168 ? 11.54056  -21.79128 -4.39944  1.000 121.25310 ? 168 ARG C CD  1 
ATOM 4723 N NE  . ARG C 1 168 ? 12.88117  -22.37269 -4.44278  1.000 122.43708 ? 168 ARG C NE  1 
ATOM 4724 C CZ  . ARG C 1 168 ? 13.24886  -23.49147 -3.83075  1.000 121.04665 ? 168 ARG C CZ  1 
ATOM 4725 N NH1 . ARG C 1 168 ? 12.40474  -24.17681 -3.07652  1.000 126.32970 ? 168 ARG C NH1 1 
ATOM 4726 N NH2 . ARG C 1 168 ? 14.50306  -23.92035 -3.95967  1.000 114.80168 ? 168 ARG C NH2 1 
ATOM 4727 N N   . ASP C 1 169 ? 11.49422  -19.19751 -6.75610  1.000 129.57500 ? 169 ASP C N   1 
ATOM 4728 C CA  . ASP C 1 169 ? 12.54622  -18.71514 -7.66042  1.000 127.31022 ? 169 ASP C CA  1 
ATOM 4729 C C   . ASP C 1 169 ? 12.01274  -17.81477 -8.76811  1.000 130.44089 ? 169 ASP C C   1 
ATOM 4730 O O   . ASP C 1 169 ? 12.47912  -17.87625 -9.90885  1.000 131.37707 ? 169 ASP C O   1 
ATOM 4731 C CB  . ASP C 1 169 ? 13.39674  -19.86567 -8.23631  1.000 122.47864 ? 169 ASP C CB  1 
ATOM 4732 C CG  . ASP C 1 169 ? 12.70181  -20.67597 -9.31462  1.000 127.33915 ? 169 ASP C CG  1 
ATOM 4733 O OD1 . ASP C 1 169 ? 11.51750  -20.46065 -9.61236  1.000 130.79479 ? 169 ASP C OD1 1 
ATOM 4734 O OD2 . ASP C 1 169 ? 13.38402  -21.53062 -9.91452  1.000 128.85629 ? 169 ASP C OD2 1 
ATOM 4735 N N   . MET C 1 170 ? 11.07693  -16.93144 -8.42868  1.000 136.10254 ? 170 MET C N   1 
ATOM 4736 C CA  . MET C 1 170 ? 10.50188  -16.01257 -9.40853  1.000 139.09477 ? 170 MET C CA  1 
ATOM 4737 C C   . MET C 1 170 ? 11.33437  -14.73632 -9.40041  1.000 141.65400 ? 170 MET C C   1 
ATOM 4738 O O   . MET C 1 170 ? 11.00995  -13.74032 -8.74840  1.000 140.87559 ? 170 MET C O   1 
ATOM 4739 C CB  . MET C 1 170 ? 9.03796   -15.73539 -9.09461  1.000 138.91162 ? 170 MET C CB  1 
ATOM 4740 C CG  . MET C 1 170 ? 8.28381   -14.95576 -10.17093 1.000 138.39416 ? 170 MET C CG  1 
ATOM 4741 S SD  . MET C 1 170 ? 7.98532   -15.88031 -11.69458 1.000 142.90734 ? 170 MET C SD  1 
ATOM 4742 C CE  . MET C 1 170 ? 7.69586   -14.55410 -12.86753 1.000 138.24997 ? 170 MET C CE  1 
ATOM 4743 N N   . THR C 1 171 ? 12.44549  -14.78235 -10.13174 1.000 139.08770 ? 171 THR C N   1 
ATOM 4744 C CA  . THR C 1 171 ? 13.31482  -13.61860 -10.23830 1.000 138.13118 ? 171 THR C CA  1 
ATOM 4745 C C   . THR C 1 171 ? 12.93810  -12.72014 -11.41610 1.000 137.99045 ? 171 THR C C   1 
ATOM 4746 O O   . THR C 1 171 ? 12.98628  -11.49306 -11.28613 1.000 137.27542 ? 171 THR C O   1 
ATOM 4747 C CB  . THR C 1 171 ? 14.77897  -14.06441 -10.33700 1.000 135.16916 ? 171 THR C CB  1 
ATOM 4748 O OG1 . THR C 1 171 ? 14.96669  -14.87207 -11.50549 1.000 138.48819 ? 171 THR C OG1 1 
ATOM 4749 C CG2 . THR C 1 171 ? 15.16243  -14.87553 -9.10879  1.000 128.52953 ? 171 THR C CG2 1 
ATOM 4750 N N   . THR C 1 172 ? 12.54900  -13.29715 -12.55553 1.000 135.10774 ? 172 THR C N   1 
ATOM 4751 C CA  . THR C 1 172 ? 12.10891  -12.49940 -13.69634 1.000 134.51513 ? 172 THR C CA  1 
ATOM 4752 C C   . THR C 1 172 ? 10.77076  -11.83007 -13.38309 1.000 135.27606 ? 172 THR C C   1 
ATOM 4753 O O   . THR C 1 172 ? 9.98406   -12.31810 -12.56736 1.000 134.58304 ? 172 THR C O   1 
ATOM 4754 C CB  . THR C 1 172 ? 11.99971  -13.37500 -14.95390 1.000 129.72621 ? 172 THR C CB  1 
ATOM 4755 O OG1 . THR C 1 172 ? 13.27586  -13.95381 -15.24660 1.000 126.10862 ? 172 THR C OG1 1 
ATOM 4756 C CG2 . THR C 1 172 ? 11.55615  -12.56737 -16.16597 1.000 126.39750 ? 172 THR C CG2 1 
ATOM 4757 N N   . CYS C 1 173 ? 10.52577  -10.68694 -14.02106 1.000 132.99990 ? 173 CYS C N   1 
ATOM 4758 C CA  . CYS C 1 173 ? 9.33341   -9.90086  -13.73315 1.000 130.87857 ? 173 CYS C CA  1 
ATOM 4759 C C   . CYS C 1 173 ? 8.98608   -8.94893  -14.87727 1.000 128.67974 ? 173 CYS C C   1 
ATOM 4760 O O   . CYS C 1 173 ? 7.91945   -9.05401  -15.48889 1.000 131.77370 ? 173 CYS C O   1 
ATOM 4761 C CB  . CYS C 1 173 ? 9.53645   -9.12221  -12.43122 1.000 127.22567 ? 173 CYS C CB  1 
ATOM 4762 S SG  . CYS C 1 173 ? 8.11080   -8.17758  -11.87110 1.000 130.26601 ? 173 CYS C SG  1 
ATOM 4763 N N   . THR C 1 179 ? 7.17359   -1.36465  -20.74409 1.000 128.95009 ? 179 THR C N   1 
ATOM 4764 C CA  . THR C 1 179 ? 7.66332   0.00817   -20.81711 1.000 131.52353 ? 179 THR C CA  1 
ATOM 4765 C C   . THR C 1 179 ? 8.85131   0.19228   -21.75336 1.000 133.25588 ? 179 THR C C   1 
ATOM 4766 O O   . THR C 1 179 ? 8.78856   0.95720   -22.73161 1.000 132.93536 ? 179 THR C O   1 
ATOM 4767 C CB  . THR C 1 179 ? 8.06507   0.51319   -19.43119 1.000 122.54152 ? 179 THR C CB  1 
ATOM 4768 O OG1 . THR C 1 179 ? 6.89261   0.61169   -18.62150 1.000 119.90103 ? 179 THR C OG1 1 
ATOM 4769 C CG2 . THR C 1 179 ? 8.74743   1.87211   -19.51616 1.000 123.13850 ? 179 THR C CG2 1 
ATOM 4770 N N   . LEU C 1 180 ? 9.91198   -0.55248  -21.46040 1.000 128.68729 ? 180 LEU C N   1 
ATOM 4771 C CA  . LEU C 1 180 ? 11.24615  -0.30070  -21.99361 1.000 128.27481 ? 180 LEU C CA  1 
ATOM 4772 C C   . LEU C 1 180 ? 11.23565  -0.50723  -23.49977 1.000 136.69523 ? 180 LEU C C   1 
ATOM 4773 O O   . LEU C 1 180 ? 11.23829  -1.64428  -23.98460 1.000 137.76406 ? 180 LEU C O   1 
ATOM 4774 C CB  . LEU C 1 180 ? 12.25805  -1.24194  -21.35883 1.000 126.48579 ? 180 LEU C CB  1 
ATOM 4775 C CG  . LEU C 1 180 ? 12.62926  -1.03660  -19.89788 1.000 124.64099 ? 180 LEU C CG  1 
ATOM 4776 C CD1 . LEU C 1 180 ? 11.49335  -1.47855  -19.00385 1.000 131.59092 ? 180 LEU C CD1 1 
ATOM 4777 C CD2 . LEU C 1 180 ? 13.87758  -1.82454  -19.57959 1.000 121.43994 ? 180 LEU C CD2 1 
ATOM 4778 N N   . ASP C 1 181 ? 11.24261  0.58751   -24.25294 1.000 133.60560 ? 181 ASP C N   1 
ATOM 4779 C CA  . ASP C 1 181 ? 11.58324  0.49935   -25.66001 1.000 129.45563 ? 181 ASP C CA  1 
ATOM 4780 C C   . ASP C 1 181 ? 13.07503  0.76196   -25.81137 1.000 124.37686 ? 181 ASP C C   1 
ATOM 4781 O O   . ASP C 1 181 ? 13.62571  1.67412   -25.18313 1.000 124.33252 ? 181 ASP C O   1 
ATOM 4782 C CB  . ASP C 1 181 ? 10.78223  1.48756   -26.51218 1.000 126.92308 ? 181 ASP C CB  1 
ATOM 4783 C CG  . ASP C 1 181 ? 9.28676   1.25523   -26.42424 1.000 134.63153 ? 181 ASP C CG  1 
ATOM 4784 O OD1 . ASP C 1 181 ? 8.88923   0.20709   -25.86065 1.000 142.03862 ? 181 ASP C OD1 1 
ATOM 4785 O OD2 . ASP C 1 181 ? 8.51902   2.08008   -26.98151 1.000 125.02189 ? 181 ASP C OD2 1 
ATOM 4786 N N   . GLY C 1 182 ? 13.72576  -0.05930  -26.63544 1.000 121.74567 ? 182 GLY C N   1 
ATOM 4787 C CA  . GLY C 1 182 ? 15.13878  0.09251   -26.92108 1.000 117.30535 ? 182 GLY C CA  1 
ATOM 4788 C C   . GLY C 1 182 ? 16.05561  -0.33102  -25.79307 1.000 127.75619 ? 182 GLY C C   1 
ATOM 4789 O O   . GLY C 1 182 ? 16.89370  0.45132   -25.33743 1.000 130.25473 ? 182 GLY C O   1 
ATOM 4790 N N   . PHE C 1 183 ? 15.89804  -1.56138  -25.32074 1.000 128.15921 ? 183 PHE C N   1 
ATOM 4791 C CA  . PHE C 1 183 ? 16.84944  -2.12726  -24.38169 1.000 126.75419 ? 183 PHE C CA  1 
ATOM 4792 C C   . PHE C 1 183 ? 18.08884  -2.59941  -25.13390 1.000 129.07468 ? 183 PHE C C   1 
ATOM 4793 O O   . PHE C 1 183 ? 18.00341  -3.08288  -26.26695 1.000 132.04110 ? 183 PHE C O   1 
ATOM 4794 C CB  . PHE C 1 183 ? 16.21526  -3.28669  -23.60616 1.000 131.91785 ? 183 PHE C CB  1 
ATOM 4795 C CG  . PHE C 1 183 ? 17.12919  -3.90083  -22.57770 1.000 129.74763 ? 183 PHE C CG  1 
ATOM 4796 C CD1 . PHE C 1 183 ? 17.36391  -3.26165  -21.37199 1.000 123.11689 ? 183 PHE C CD1 1 
ATOM 4797 C CD2 . PHE C 1 183 ? 17.76395  -5.11386  -22.82822 1.000 126.87996 ? 183 PHE C CD2 1 
ATOM 4798 C CE1 . PHE C 1 183 ? 18.20952  -3.81827  -20.44478 1.000 122.52513 ? 183 PHE C CE1 1 
ATOM 4799 C CE2 . PHE C 1 183 ? 18.61599  -5.67681  -21.90186 1.000 118.30904 ? 183 PHE C CE2 1 
ATOM 4800 C CZ  . PHE C 1 183 ? 18.83988  -5.02934  -20.71449 1.000 122.57831 ? 183 PHE C CZ  1 
ATOM 4801 N N   . VAL C 1 184 ? 19.25042  -2.44613  -24.49887 1.000 128.73719 ? 184 VAL C N   1 
ATOM 4802 C CA  . VAL C 1 184 ? 20.53058  -2.83539  -25.08174 1.000 128.10881 ? 184 VAL C CA  1 
ATOM 4803 C C   . VAL C 1 184 ? 21.12857  -3.96220  -24.24840 1.000 128.75146 ? 184 VAL C C   1 
ATOM 4804 O O   . VAL C 1 184 ? 21.07882  -3.92725  -23.01061 1.000 129.59690 ? 184 VAL C O   1 
ATOM 4805 C CB  . VAL C 1 184 ? 21.49890  -1.63870  -25.17640 1.000 128.09015 ? 184 VAL C CB  1 
ATOM 4806 C CG1 . VAL C 1 184 ? 22.85330  -2.07961  -25.72678 1.000 130.22242 ? 184 VAL C CG1 1 
ATOM 4807 C CG2 . VAL C 1 184 ? 20.89606  -0.55463  -26.04235 1.000 130.69834 ? 184 VAL C CG2 1 
ATOM 4808 N N   . ALA C 1 185 ? 21.71669  -4.94852  -24.93575 1.000 116.68934 ? 185 ALA C N   1 
ATOM 4809 C CA  . ALA C 1 185 ? 22.01352  -6.24931  -24.34698 1.000 117.17120 ? 185 ALA C CA  1 
ATOM 4810 C C   . ALA C 1 185 ? 22.87227  -6.17102  -23.08798 1.000 121.38156 ? 185 ALA C C   1 
ATOM 4811 O O   . ALA C 1 185 ? 22.38310  -6.38066  -21.96786 1.000 113.32112 ? 185 ALA C O   1 
ATOM 4812 C CB  . ALA C 1 185 ? 22.72463  -7.12222  -25.38305 1.000 105.08664 ? 185 ALA C CB  1 
ATOM 4813 N N   . HIS C 1 186 ? 24.13755  -5.80290  -23.26661 1.000 118.60894 ? 186 HIS C N   1 
ATOM 4814 C CA  . HIS C 1 186 ? 25.10855  -5.70611  -22.18251 1.000 114.68584 ? 186 HIS C CA  1 
ATOM 4815 C C   . HIS C 1 186 ? 25.36752  -4.25737  -21.82740 1.000 110.87128 ? 186 HIS C C   1 
ATOM 4816 O O   . HIS C 1 186 ? 26.50927  -3.83857  -21.62528 1.000 108.45592 ? 186 HIS C O   1 
ATOM 4817 C CB  . HIS C 1 186 ? 26.40293  -6.42088  -22.55301 1.000 118.28681 ? 186 HIS C CB  1 
ATOM 4818 N N   . ASP C 1 187 ? 24.30699  -3.46151  -21.81580 1.000 111.57558 ? 187 ASP C N   1 
ATOM 4819 C CA  . ASP C 1 187 ? 24.36376  -2.09982  -21.30676 1.000 114.11639 ? 187 ASP C CA  1 
ATOM 4820 C C   . ASP C 1 187 ? 24.05935  -2.14290  -19.80916 1.000 110.80000 ? 187 ASP C C   1 
ATOM 4821 O O   . ASP C 1 187 ? 22.91384  -2.36955  -19.40558 1.000 109.04222 ? 187 ASP C O   1 
ATOM 4822 C CB  . ASP C 1 187 ? 23.37639  -1.21426  -22.05540 1.000 116.53678 ? 187 ASP C CB  1 
ATOM 4823 C CG  . ASP C 1 187 ? 23.62228  0.25423   -21.81781 1.000 115.99717 ? 187 ASP C CG  1 
ATOM 4824 O OD1 . ASP C 1 187 ? 24.58211  0.58815   -21.09198 1.000 112.50577 ? 187 ASP C OD1 1 
ATOM 4825 O OD2 . ASP C 1 187 ? 22.84890  1.07582   -22.35234 1.000 119.32020 ? 187 ASP C OD2 1 
ATOM 4826 N N   . SER C 1 188 ? 25.09047  -1.93342  -18.98636 1.000 106.34494 ? 188 SER C N   1 
ATOM 4827 C CA  . SER C 1 188 ? 24.93120  -2.08404  -17.54787 1.000 105.54221 ? 188 SER C CA  1 
ATOM 4828 C C   . SER C 1 188 ? 24.00241  -1.02942  -16.96414 1.000 105.36354 ? 188 SER C C   1 
ATOM 4829 O O   . SER C 1 188 ? 23.38363  -1.26550  -15.92142 1.000 102.50411 ? 188 SER C O   1 
ATOM 4830 C CB  . SER C 1 188 ? 26.29461  -2.03113  -16.86974 1.000 104.84563 ? 188 SER C CB  1 
ATOM 4831 O OG  . SER C 1 188 ? 27.09300  -3.10817  -17.31402 1.000 108.31824 ? 188 SER C OG  1 
ATOM 4832 N N   . ILE C 1 189 ? 23.90457  0.14090   -17.59784 1.000 107.93663 ? 189 ILE C N   1 
ATOM 4833 C CA  . ILE C 1 189 ? 22.92857  1.12899   -17.14825 1.000 103.54870 ? 189 ILE C CA  1 
ATOM 4834 C C   . ILE C 1 189 ? 21.51936  0.66210   -17.48552 1.000 105.62683 ? 189 ILE C C   1 
ATOM 4835 O O   . ILE C 1 189 ? 20.58486  0.85151   -16.70168 1.000 103.97823 ? 189 ILE C O   1 
ATOM 4836 C CB  . ILE C 1 189 ? 23.23402  2.51425   -17.75298 1.000 100.86772 ? 189 ILE C CB  1 
ATOM 4837 C CG1 . ILE C 1 189 ? 24.64689  2.97600   -17.38640 1.000 94.41217  ? 189 ILE C CG1 1 
ATOM 4838 C CG2 . ILE C 1 189 ? 22.20861  3.54430   -17.30621 1.000 98.31644  ? 189 ILE C CG2 1 
ATOM 4839 C CD1 . ILE C 1 189 ? 24.89340  3.04364   -15.91171 1.000 98.31025  ? 189 ILE C CD1 1 
ATOM 4840 N N   . HIS C 1 190 ? 21.34097  0.04737   -18.65909 1.000 108.55170 ? 190 HIS C N   1 
ATOM 4841 C CA  . HIS C 1 190 ? 20.03507  -0.50262  -19.00712 1.000 111.31864 ? 190 HIS C CA  1 
ATOM 4842 C C   . HIS C 1 190 ? 19.66308  -1.67537  -18.11296 1.000 110.13309 ? 190 HIS C C   1 
ATOM 4843 O O   . HIS C 1 190 ? 18.47794  -1.89784  -17.83869 1.000 110.68315 ? 190 HIS C O   1 
ATOM 4844 C CB  . HIS C 1 190 ? 20.01162  -0.92543  -20.47325 1.000 114.45603 ? 190 HIS C CB  1 
ATOM 4845 C CG  . HIS C 1 190 ? 19.94158  0.22446   -21.42762 1.000 120.34503 ? 190 HIS C CG  1 
ATOM 4846 N ND1 . HIS C 1 190 ? 20.01064  0.06638   -22.79644 1.000 123.99774 ? 190 HIS C ND1 1 
ATOM 4847 C CD2 . HIS C 1 190 ? 19.80503  1.55357   -21.20836 1.000 117.21003 ? 190 HIS C CD2 1 
ATOM 4848 C CE1 . HIS C 1 190 ? 19.91524  1.24811   -23.37828 1.000 122.32573 ? 190 HIS C CE1 1 
ATOM 4849 N NE2 . HIS C 1 190 ? 19.78991  2.16658   -22.43667 1.000 120.74033 ? 190 HIS C NE2 1 
ATOM 4850 N N   . ASP C 1 191 ? 20.65700  -2.43540  -17.65982 1.000 110.00905 ? 191 ASP C N   1 
ATOM 4851 C CA  . ASP C 1 191 ? 20.39565  -3.55918  -16.76933 1.000 108.90583 ? 191 ASP C CA  1 
ATOM 4852 C C   . ASP C 1 191 ? 19.90915  -3.09053  -15.39921 1.000 103.31935 ? 191 ASP C C   1 
ATOM 4853 O O   . ASP C 1 191 ? 18.93944  -3.63917  -14.86288 1.000 102.43689 ? 191 ASP C O   1 
ATOM 4854 C CB  . ASP C 1 191 ? 21.66066  -4.40811  -16.66782 1.000 110.20621 ? 191 ASP C CB  1 
ATOM 4855 C CG  . ASP C 1 191 ? 21.96160  -5.13402  -17.96681 1.000 107.09314 ? 191 ASP C CG  1 
ATOM 4856 O OD1 . ASP C 1 191 ? 20.97722  -5.57118  -18.59485 1.000 105.68975 ? 191 ASP C OD1 1 
ATOM 4857 O OD2 . ASP C 1 191 ? 23.14760  -5.22101  -18.37771 1.000 104.23758 ? 191 ASP C OD2 1 
ATOM 4858 N N   . CYS C 1 192 ? 20.55354  -2.07141  -14.82175 1.000 101.24316 ? 192 CYS C N   1 
ATOM 4859 C CA  . CYS C 1 192 ? 20.06606  -1.51923  -13.55854 1.000 102.03820 ? 192 CYS C CA  1 
ATOM 4860 C C   . CYS C 1 192 ? 18.64183  -0.99825  -13.70502 1.000 102.33444 ? 192 CYS C C   1 
ATOM 4861 O O   . CYS C 1 192 ? 17.75159  -1.37966  -12.94299 1.000 104.37862 ? 192 CYS C O   1 
ATOM 4862 C CB  . CYS C 1 192 ? 20.98241  -0.39488  -13.05253 1.000 100.83978 ? 192 CYS C CB  1 
ATOM 4863 S SG  . CYS C 1 192 ? 22.64376  -0.82492  -12.43160 1.000 91.70863  ? 192 CYS C SG  1 
ATOM 4864 N N   . ALA C 1 193 ? 18.40274  -0.14265  -14.70084 1.000 103.94554 ? 193 ALA C N   1 
ATOM 4865 C CA  . ALA C 1 193 ? 17.09489  0.49320   -14.84011 1.000 105.68904 ? 193 ALA C CA  1 
ATOM 4866 C C   . ALA C 1 193 ? 15.98974  -0.53463  -15.03784 1.000 105.29270 ? 193 ALA C C   1 
ATOM 4867 O O   . ALA C 1 193 ? 14.87140  -0.35885  -14.54103 1.000 106.09508 ? 193 ALA C O   1 
ATOM 4868 C CB  . ALA C 1 193 ? 17.10998  1.48445   -16.00271 1.000 110.83407 ? 193 ALA C CB  1 
ATOM 4869 N N   . LYS C 1 194 ? 16.27335  -1.60761  -15.77259 1.000 104.99259 ? 194 LYS C N   1 
ATOM 4870 C CA  . LYS C 1 194 ? 15.29794  -2.68467  -15.87242 1.000 104.93111 ? 194 LYS C CA  1 
ATOM 4871 C C   . LYS C 1 194 ? 14.99986  -3.27169  -14.49527 1.000 108.51366 ? 194 LYS C C   1 
ATOM 4872 O O   . LYS C 1 194 ? 13.83440  -3.45588  -14.12912 1.000 110.48568 ? 194 LYS C O   1 
ATOM 4873 C CB  . LYS C 1 194 ? 15.80035  -3.76169  -16.83027 1.000 101.66243 ? 194 LYS C CB  1 
ATOM 4874 C CG  . LYS C 1 194 ? 14.86303  -4.93375  -16.98400 1.000 97.68376  ? 194 LYS C CG  1 
ATOM 4875 C CD  . LYS C 1 194 ? 15.43479  -5.94431  -17.95103 1.000 97.86547  ? 194 LYS C CD  1 
ATOM 4876 C CE  . LYS C 1 194 ? 16.72671  -6.53296  -17.39357 1.000 110.45119 ? 194 LYS C CE  1 
ATOM 4877 N NZ  . LYS C 1 194 ? 16.54298  -7.28342  -16.08932 1.000 110.91221 ? 194 LYS C NZ  1 
ATOM 4878 N N   . ASP C 1 195 ? 16.04311  -3.53990  -13.69909 1.000 105.12500 ? 195 ASP C N   1 
ATOM 4879 C CA  . ASP C 1 195 ? 15.81501  -4.06481  -12.35383 1.000 106.69131 ? 195 ASP C CA  1 
ATOM 4880 C C   . ASP C 1 195 ? 15.13301  -3.04144  -11.43397 1.000 108.04039 ? 195 ASP C C   1 
ATOM 4881 O O   . ASP C 1 195 ? 14.30289  -3.42962  -10.60570 1.000 107.95568 ? 195 ASP C O   1 
ATOM 4882 C CB  . ASP C 1 195 ? 17.12904  -4.56625  -11.72744 1.000 107.82661 ? 195 ASP C CB  1 
ATOM 4883 C CG  . ASP C 1 195 ? 17.58715  -5.91990  -12.29483 1.000 109.63345 ? 195 ASP C CG  1 
ATOM 4884 O OD1 . ASP C 1 195 ? 16.73072  -6.64352  -12.85059 1.000 111.24900 ? 195 ASP C OD1 1 
ATOM 4885 O OD2 . ASP C 1 195 ? 18.78072  -6.28978  -12.13642 1.000 104.50647 ? 195 ASP C OD2 1 
ATOM 4886 N N   . ILE C 1 196 ? 15.44970  -1.74321  -11.55459 1.000 109.42376 ? 196 ILE C N   1 
ATOM 4887 C CA  . ILE C 1 196 ? 14.75403  -0.73520  -10.74650 1.000 106.38656 ? 196 ILE C CA  1 
ATOM 4888 C C   . ILE C 1 196 ? 13.26121  -0.78032  -11.03190 1.000 110.98528 ? 196 ILE C C   1 
ATOM 4889 O O   . ILE C 1 196 ? 12.43289  -0.79259  -10.11669 1.000 114.08478 ? 196 ILE C O   1 
ATOM 4890 C CB  . ILE C 1 196 ? 15.30249  0.68072   -11.01659 1.000 107.97464 ? 196 ILE C CB  1 
ATOM 4891 C CG1 . ILE C 1 196 ? 16.79704  0.79662   -10.72563 1.000 107.38810 ? 196 ILE C CG1 1 
ATOM 4892 C CG2 . ILE C 1 196 ? 14.54947  1.70769   -10.17744 1.000 105.06631 ? 196 ILE C CG2 1 
ATOM 4893 C CD1 . ILE C 1 196 ? 17.38794  2.11238   -11.19604 1.000 103.88913 ? 196 ILE C CD1 1 
ATOM 4894 N N   . LEU C 1 197 ? 12.90053  -0.80185  -12.31634 1.000 114.70048 ? 197 LEU C N   1 
ATOM 4895 C CA  . LEU C 1 197 ? 11.49591  -0.79053  -12.70752 1.000 114.77109 ? 197 LEU C CA  1 
ATOM 4896 C C   . LEU C 1 197 ? 10.78201  -2.06133  -12.25844 1.000 116.16300 ? 197 LEU C C   1 
ATOM 4897 O O   . LEU C 1 197 ? 9.68814   -1.99594  -11.68591 1.000 119.56202 ? 197 LEU C O   1 
ATOM 4898 C CB  . LEU C 1 197 ? 11.38701  -0.61338  -14.22333 1.000 117.23736 ? 197 LEU C CB  1 
ATOM 4899 C CG  . LEU C 1 197 ? 11.85152  0.72875   -14.78862 1.000 118.48428 ? 197 LEU C CG  1 
ATOM 4900 C CD1 . LEU C 1 197 ? 11.89987  0.65625   -16.29218 1.000 117.42066 ? 197 LEU C CD1 1 
ATOM 4901 C CD2 . LEU C 1 197 ? 10.94149  1.87103   -14.33296 1.000 121.07914 ? 197 LEU C CD2 1 
ATOM 4902 N N   . MET C 1 198 ? 11.40073  -3.22785  -12.49040 1.000 113.83478 ? 198 MET C N   1 
ATOM 4903 C CA  . MET C 1 198 ? 10.74690  -4.50671  -12.20819 1.000 115.64421 ? 198 MET C CA  1 
ATOM 4904 C C   . MET C 1 198 ? 10.31957  -4.61572  -10.74464 1.000 121.22506 ? 198 MET C C   1 
ATOM 4905 O O   . MET C 1 198 ? 9.25918   -5.17839  -10.43892 1.000 122.80764 ? 198 MET C O   1 
ATOM 4906 C CB  . MET C 1 198 ? 11.68660  -5.65694  -12.55775 1.000 112.84248 ? 198 MET C CB  1 
ATOM 4907 C CG  . MET C 1 198 ? 11.98030  -5.84627  -14.00835 1.000 106.91034 ? 198 MET C CG  1 
ATOM 4908 S SD  . MET C 1 198 ? 13.42981  -6.90428  -14.19519 1.000 109.78149 ? 198 MET C SD  1 
ATOM 4909 C CE  . MET C 1 198 ? 12.77955  -8.51782  -13.79887 1.000 115.10667 ? 198 MET C CE  1 
ATOM 4910 N N   . MET C 1 199 ? 11.14531  -4.10803  -9.82430  1.000 116.11310 ? 199 MET C N   1 
ATOM 4911 C CA  . MET C 1 199 ? 10.77755  -4.09772  -8.40978  1.000 116.08657 ? 199 MET C CA  1 
ATOM 4912 C C   . MET C 1 199 ? 9.50923   -3.29136  -8.17604  1.000 122.76530 ? 199 MET C C   1 
ATOM 4913 O O   . MET C 1 199 ? 8.60353   -3.72526  -7.45324  1.000 123.81272 ? 199 MET C O   1 
ATOM 4914 C CB  . MET C 1 199 ? 11.92688  -3.53212  -7.58264  1.000 108.67526 ? 199 MET C CB  1 
ATOM 4915 C CG  . MET C 1 199 ? 13.07838  -4.48276  -7.36437  1.000 106.54094 ? 199 MET C CG  1 
ATOM 4916 S SD  . MET C 1 199 ? 14.50706  -3.59116  -6.72937  1.000 106.24499 ? 199 MET C SD  1 
ATOM 4917 C CE  . MET C 1 199 ? 13.86415  -2.95221  -5.18569  1.000 105.54525 ? 199 MET C CE  1 
ATOM 4918 N N   . LYS C 1 200 ? 9.42765   -2.11216  -8.79426  1.000 126.04996 ? 200 LYS C N   1 
ATOM 4919 C CA  . LYS C 1 200 ? 8.27406   -1.24082  -8.60698  1.000 128.50715 ? 200 LYS C CA  1 
ATOM 4920 C C   . LYS C 1 200 ? 7.00463   -1.89201  -9.15279  1.000 129.11059 ? 200 LYS C C   1 
ATOM 4921 O O   . LYS C 1 200 ? 5.91720   -1.72418  -8.58808  1.000 130.51059 ? 200 LYS C O   1 
ATOM 4922 C CB  . LYS C 1 200 ? 8.54650   0.10497   -9.28383  1.000 128.84526 ? 200 LYS C CB  1 
ATOM 4923 C CG  . LYS C 1 200 ? 7.64522   1.24689   -8.85938  1.000 129.96108 ? 200 LYS C CG  1 
ATOM 4924 C CD  . LYS C 1 200 ? 7.89238   1.60470   -7.40375  1.000 127.52949 ? 200 LYS C CD  1 
ATOM 4925 C CE  . LYS C 1 200 ? 9.31473   2.09798   -7.18429  1.000 124.78695 ? 200 LYS C CE  1 
ATOM 4926 N NZ  . LYS C 1 200 ? 9.56948   3.41506   -7.82171  1.000 127.22173 ? 200 LYS C NZ  1 
ATOM 4927 N N   . TYR C 1 201 ? 7.12148   -2.63343  -10.25892 1.000 136.67934 ? 201 TYR C N   1 
ATOM 4928 C CA  . TYR C 1 201 ? 5.97242   -3.36241  -10.79063 1.000 138.08792 ? 201 TYR C CA  1 
ATOM 4929 C C   . TYR C 1 201 ? 5.69154   -4.63276  -9.99207  1.000 140.49464 ? 201 TYR C C   1 
ATOM 4930 O O   . TYR C 1 201 ? 4.52628   -4.99390  -9.79255  1.000 144.21884 ? 201 TYR C O   1 
ATOM 4931 C CB  . TYR C 1 201 ? 6.18430   -3.68922  -12.27650 1.000 140.22079 ? 201 TYR C CB  1 
ATOM 4932 N N   . ALA C 1 202 ? 6.73579   -5.33312  -9.53812  1.000 127.89112 ? 202 ALA C N   1 
ATOM 4933 C CA  . ALA C 1 202 ? 6.50819   -6.46759  -8.64777  1.000 126.81540 ? 202 ALA C CA  1 
ATOM 4934 C C   . ALA C 1 202 ? 5.99076   -6.01961  -7.28923  1.000 126.24317 ? 202 ALA C C   1 
ATOM 4935 O O   . ALA C 1 202 ? 5.34103   -6.80603  -6.59072  1.000 126.68581 ? 202 ALA C O   1 
ATOM 4936 C CB  . ALA C 1 202 ? 7.78399   -7.28477  -8.47055  1.000 124.72501 ? 202 ALA C CB  1 
ATOM 4937 N N   . LEU C 1 203 ? 6.27538   -4.77429  -6.89297  1.000 123.69235 ? 203 LEU C N   1 
ATOM 4938 C CA  . LEU C 1 203 ? 5.78906   -4.27477  -5.60856  1.000 124.78964 ? 203 LEU C CA  1 
ATOM 4939 C C   . LEU C 1 203 ? 4.29846   -3.96741  -5.66228  1.000 129.58614 ? 203 LEU C C   1 
ATOM 4940 O O   . LEU C 1 203 ? 3.52574   -4.44154  -4.81876  1.000 127.87502 ? 203 LEU C O   1 
ATOM 4941 C CB  . LEU C 1 203 ? 6.56714   -3.02588  -5.18772  1.000 122.18087 ? 203 LEU C CB  1 
ATOM 4942 C CG  . LEU C 1 203 ? 6.15354   -2.45256  -3.82637  1.000 113.90764 ? 203 LEU C CG  1 
ATOM 4943 C CD1 . LEU C 1 203 ? 6.41216   -3.48280  -2.77165  1.000 114.46807 ? 203 LEU C CD1 1 
ATOM 4944 C CD2 . LEU C 1 203 ? 6.88378   -1.16550  -3.47632  1.000 108.86976 ? 203 LEU C CD2 1 
ATOM 4945 N N   . ARG C 1 204 ? 3.87852   -3.16670  -6.64893  1.000 131.46087 ? 204 ARG C N   1 
ATOM 4946 C CA  . ARG C 1 204 ? 2.47152   -2.79987  -6.76588  1.000 131.20504 ? 204 ARG C CA  1 
ATOM 4947 C C   . ARG C 1 204 ? 1.58414   -4.02755  -6.91924  1.000 133.53612 ? 204 ARG C C   1 
ATOM 4948 O O   . ARG C 1 204 ? 0.45029   -4.03050  -6.42518  1.000 139.28095 ? 204 ARG C O   1 
ATOM 4949 C CB  . ARG C 1 204 ? 2.26752   -1.84663  -7.94862  1.000 131.86502 ? 204 ARG C CB  1 
ATOM 4950 N N   . TYR C 1 205 ? 2.09333   -5.08371  -7.56797  1.000 131.64594 ? 205 TYR C N   1 
ATOM 4951 C CA  . TYR C 1 205 ? 1.27438   -6.24832  -7.90388  1.000 131.87797 ? 205 TYR C CA  1 
ATOM 4952 C C   . TYR C 1 205 ? 0.56827   -6.82417  -6.67534  1.000 134.18484 ? 205 TYR C C   1 
ATOM 4953 O O   . TYR C 1 205 ? -0.62517  -7.14283  -6.72653  1.000 139.61567 ? 205 TYR C O   1 
ATOM 4954 C CB  . TYR C 1 205 ? 2.13594   -7.31345  -8.58936  1.000 127.24371 ? 205 TYR C CB  1 
ATOM 4955 N N   . ALA C 1 206 ? 1.27786   -6.95855  -5.55945  1.000 132.07941 ? 206 ALA C N   1 
ATOM 4956 C CA  . ALA C 1 206 ? 0.62607   -7.41846  -4.33307  1.000 128.72787 ? 206 ALA C CA  1 
ATOM 4957 C C   . ALA C 1 206 ? 1.05793   -6.57891  -3.13408  1.000 128.40800 ? 206 ALA C C   1 
ATOM 4958 O O   . ALA C 1 206 ? 0.98539   -5.34888  -3.16890  1.000 128.45103 ? 206 ALA C O   1 
ATOM 4959 C CB  . ALA C 1 206 ? 0.91904   -8.89825  -4.09046  1.000 124.70284 ? 206 ALA C CB  1 
ATOM 4960 N N   . MET D 1 1   ? 13.87882  -32.92040 0.83453   1.000 139.82409 ? 1   MET D N   1 
ATOM 4961 C CA  . MET D 1 1   ? 14.62512  -31.88313 0.12667   1.000 140.83652 ? 1   MET D CA  1 
ATOM 4962 C C   . MET D 1 1   ? 14.34993  -30.52143 0.78791   1.000 138.61665 ? 1   MET D C   1 
ATOM 4963 O O   . MET D 1 1   ? 13.19406  -30.16274 1.02556   1.000 138.63680 ? 1   MET D O   1 
ATOM 4964 C CB  . MET D 1 1   ? 14.25746  -31.90376 -1.36189  1.000 140.79754 ? 1   MET D CB  1 
ATOM 4965 C CG  . MET D 1 1   ? 15.08742  -31.00102 -2.26311  1.000 137.33780 ? 1   MET D CG  1 
ATOM 4966 S SD  . MET D 1 1   ? 14.34519  -29.38621 -2.54302  1.000 140.05883 ? 1   MET D SD  1 
ATOM 4967 C CE  . MET D 1 1   ? 15.67309  -28.55972 -3.37464  1.000 124.77912 ? 1   MET D CE  1 
ATOM 4968 N N   . PHE D 1 2   ? 15.41173  -29.76787 1.09048   1.000 138.63006 ? 2   PHE D N   1 
ATOM 4969 C CA  . PHE D 1 2   ? 15.33824  -28.71124 2.09514   1.000 138.37877 ? 2   PHE D CA  1 
ATOM 4970 C C   . PHE D 1 2   ? 16.07975  -27.45036 1.66500   1.000 132.61666 ? 2   PHE D C   1 
ATOM 4971 O O   . PHE D 1 2   ? 16.87384  -27.44277 0.72129   1.000 128.59503 ? 2   PHE D O   1 
ATOM 4972 C CB  . PHE D 1 2   ? 15.92435  -29.19119 3.42460   1.000 137.21134 ? 2   PHE D CB  1 
ATOM 4973 C CG  . PHE D 1 2   ? 15.16936  -30.31483 4.03276   1.000 139.59431 ? 2   PHE D CG  1 
ATOM 4974 C CD1 . PHE D 1 2   ? 14.08595  -30.06821 4.85337   1.000 136.41263 ? 2   PHE D CD1 1 
ATOM 4975 C CD2 . PHE D 1 2   ? 15.51603  -31.62814 3.74783   1.000 143.20965 ? 2   PHE D CD2 1 
ATOM 4976 C CE1 . PHE D 1 2   ? 13.38071  -31.10872 5.40844   1.000 135.40338 ? 2   PHE D CE1 1 
ATOM 4977 C CE2 . PHE D 1 2   ? 14.81089  -32.67887 4.29469   1.000 141.73458 ? 2   PHE D CE2 1 
ATOM 4978 C CZ  . PHE D 1 2   ? 13.74101  -32.41824 5.12796   1.000 138.29180 ? 2   PHE D CZ  1 
ATOM 4979 N N   . ASP D 1 3   ? 15.80426  -26.37538 2.39785   1.000 131.34385 ? 3   ASP D N   1 
ATOM 4980 C CA  . ASP D 1 3   ? 16.62356  -25.17650 2.41260   1.000 126.96677 ? 3   ASP D CA  1 
ATOM 4981 C C   . ASP D 1 3   ? 17.74431  -25.35370 3.43894   1.000 123.95597 ? 3   ASP D C   1 
ATOM 4982 O O   . ASP D 1 3   ? 17.89493  -26.41572 4.04364   1.000 124.30849 ? 3   ASP D O   1 
ATOM 4983 C CB  . ASP D 1 3   ? 15.76789  -23.95263 2.74268   1.000 124.14375 ? 3   ASP D CB  1 
ATOM 4984 C CG  . ASP D 1 3   ? 14.77106  -23.61410 1.64636   1.000 125.12576 ? 3   ASP D CG  1 
ATOM 4985 O OD1 . ASP D 1 3   ? 15.05304  -23.90358 0.46166   1.000 124.94871 ? 3   ASP D OD1 1 
ATOM 4986 O OD2 . ASP D 1 3   ? 13.70632  -23.04688 1.97683   1.000 124.41275 ? 3   ASP D OD2 1 
ATOM 4987 N N   . PHE D 1 4   ? 18.55400  -24.31373 3.63321   1.000 113.51342 ? 4   PHE D N   1 
ATOM 4988 C CA  . PHE D 1 4   ? 19.43874  -24.26428 4.78790   1.000 106.78094 ? 4   PHE D CA  1 
ATOM 4989 C C   . PHE D 1 4   ? 19.64144  -22.81051 5.18631   1.000 100.65841 ? 4   PHE D C   1 
ATOM 4990 O O   . PHE D 1 4   ? 19.23957  -21.88826 4.47449   1.000 100.90188 ? 4   PHE D O   1 
ATOM 4991 C CB  . PHE D 1 4   ? 20.77382  -24.97141 4.52503   1.000 103.15177 ? 4   PHE D CB  1 
ATOM 4992 C CG  . PHE D 1 4   ? 21.64900  -24.28852 3.52689   1.000 100.77649 ? 4   PHE D CG  1 
ATOM 4993 C CD1 . PHE D 1 4   ? 21.55436  -24.58641 2.17596   1.000 106.86714 ? 4   PHE D CD1 1 
ATOM 4994 C CD2 . PHE D 1 4   ? 22.59709  -23.37813 3.94106   1.000 94.38844  ? 4   PHE D CD2 1 
ATOM 4995 C CE1 . PHE D 1 4   ? 22.38108  -23.96533 1.25190   1.000 101.74448 ? 4   PHE D CE1 1 
ATOM 4996 C CE2 . PHE D 1 4   ? 23.41916  -22.75553 3.03171   1.000 96.01592  ? 4   PHE D CE2 1 
ATOM 4997 C CZ  . PHE D 1 4   ? 23.31484  -23.04643 1.68407   1.000 96.90694  ? 4   PHE D CZ  1 
ATOM 4998 N N   . ILE D 1 5   ? 20.23123  -22.61551 6.36510   1.000 98.98877  ? 5   ILE D N   1 
ATOM 4999 C CA  . ILE D 1 5   ? 20.60547  -21.29141 6.84554   1.000 93.79879  ? 5   ILE D CA  1 
ATOM 5000 C C   . ILE D 1 5   ? 21.93790  -21.38813 7.57992   1.000 92.30827  ? 5   ILE D C   1 
ATOM 5001 O O   . ILE D 1 5   ? 22.29340  -22.43957 8.12107   1.000 94.32279  ? 5   ILE D O   1 
ATOM 5002 C CB  . ILE D 1 5   ? 19.52683  -20.68598 7.75159   1.000 89.78130  ? 5   ILE D CB  1 
ATOM 5003 C CG1 . ILE D 1 5   ? 19.79454  -19.20597 7.96616   1.000 88.20903  ? 5   ILE D CG1 1 
ATOM 5004 C CG2 . ILE D 1 5   ? 19.51596  -21.38279 9.07641   1.000 100.17760 ? 5   ILE D CG2 1 
ATOM 5005 C CD1 . ILE D 1 5   ? 18.65706  -18.50634 8.58645   1.000 91.24721  ? 5   ILE D CD1 1 
ATOM 5006 N N   . ILE D 1 6   ? 22.69857  -20.28615 7.56871   1.000 84.84036  ? 6   ILE D N   1 
ATOM 5007 C CA  . ILE D 1 6   ? 24.00782  -20.24039 8.20278   1.000 79.59684  ? 6   ILE D CA  1 
ATOM 5008 C C   . ILE D 1 6   ? 24.13981  -18.94905 8.99818   1.000 81.54576  ? 6   ILE D C   1 
ATOM 5009 O O   . ILE D 1 6   ? 23.43570  -17.96287 8.76190   1.000 80.67576  ? 6   ILE D O   1 
ATOM 5010 C CB  . ILE D 1 6   ? 25.16272  -20.34283 7.18987   1.000 81.93018  ? 6   ILE D CB  1 
ATOM 5011 C CG1 . ILE D 1 6   ? 25.23058  -19.08668 6.33066   1.000 82.91585  ? 6   ILE D CG1 1 
ATOM 5012 C CG2 . ILE D 1 6   ? 25.01638  -21.57758 6.28844   1.000 84.75998  ? 6   ILE D CG2 1 
ATOM 5013 C CD1 . ILE D 1 6   ? 26.44636  -19.07230 5.40955   1.000 82.48651  ? 6   ILE D CD1 1 
ATOM 5014 N N   . ASP D 1 7   ? 25.04824  -18.98159 9.97255   1.000 79.81832  ? 7   ASP D N   1 
ATOM 5015 C CA  . ASP D 1 7   ? 25.43762  -17.79161 10.72058  1.000 74.55001  ? 7   ASP D CA  1 
ATOM 5016 C C   . ASP D 1 7   ? 26.86635  -17.99591 11.19821  1.000 74.07054  ? 7   ASP D C   1 
ATOM 5017 O O   . ASP D 1 7   ? 27.15590  -18.97965 11.88352  1.000 74.75777  ? 7   ASP D O   1 
ATOM 5018 C CB  . ASP D 1 7   ? 24.50452  -17.53270 11.90260  1.000 78.87191  ? 7   ASP D CB  1 
ATOM 5019 C CG  . ASP D 1 7   ? 24.68300  -16.13602 12.49064  1.000 86.22209  ? 7   ASP D CG  1 
ATOM 5020 O OD1 . ASP D 1 7   ? 25.53566  -15.38285 11.95802  1.000 89.36718  ? 7   ASP D OD1 1 
ATOM 5021 O OD2 . ASP D 1 7   ? 23.97564  -15.78259 13.46818  1.000 84.38011  ? 7   ASP D OD2 1 
ATOM 5022 N N   . PHE D 1 8   ? 27.76225  -17.10145 10.79922  1.000 72.88641  ? 8   PHE D N   1 
ATOM 5023 C CA  . PHE D 1 8   ? 29.12423  -17.08058 11.30250  1.000 68.07674  ? 8   PHE D CA  1 
ATOM 5024 C C   . PHE D 1 8   ? 29.20392  -16.02927 12.38187  1.000 67.07482  ? 8   PHE D C   1 
ATOM 5025 O O   . PHE D 1 8   ? 28.54659  -14.98924 12.30228  1.000 69.89175  ? 8   PHE D O   1 
ATOM 5026 C CB  . PHE D 1 8   ? 30.16529  -16.72185 10.23037  1.000 66.33992  ? 8   PHE D CB  1 
ATOM 5027 C CG  . PHE D 1 8   ? 30.38583  -17.76660 9.19023   1.000 65.23447  ? 8   PHE D CG  1 
ATOM 5028 C CD1 . PHE D 1 8   ? 31.24547  -18.82144 9.42703   1.000 65.86571  ? 8   PHE D CD1 1 
ATOM 5029 C CD2 . PHE D 1 8   ? 29.76314  -17.67226 7.94963   1.000 67.27097  ? 8   PHE D CD2 1 
ATOM 5030 C CE1 . PHE D 1 8   ? 31.45662  -19.79633 8.45154   1.000 67.52447  ? 8   PHE D CE1 1 
ATOM 5031 C CE2 . PHE D 1 8   ? 29.97093  -18.63781 6.96199   1.000 66.02197  ? 8   PHE D CE2 1 
ATOM 5032 C CZ  . PHE D 1 8   ? 30.81654  -19.69667 7.20805   1.000 64.95135  ? 8   PHE D CZ  1 
ATOM 5033 N N   . GLU D 1 9   ? 30.02935  -16.29218 13.37857  1.000 63.26343  ? 9   GLU D N   1 
ATOM 5034 C CA  . GLU D 1 9   ? 30.51717  -15.23587 14.24027  1.000 63.94706  ? 9   GLU D CA  1 
ATOM 5035 C C   . GLU D 1 9   ? 31.98341  -15.04822 13.90688  1.000 62.18245  ? 9   GLU D C   1 
ATOM 5036 O O   . GLU D 1 9   ? 32.70865  -16.02640 13.68851  1.000 58.06380  ? 9   GLU D O   1 
ATOM 5037 C CB  . GLU D 1 9   ? 30.29064  -15.55310 15.71833  1.000 64.12792  ? 9   GLU D CB  1 
ATOM 5038 C CG  . GLU D 1 9   ? 28.81204  -15.49894 16.08682  1.000 68.02186  ? 9   GLU D CG  1 
ATOM 5039 C CD  . GLU D 1 9   ? 28.54214  -15.88520 17.53046  1.000 76.42629  ? 9   GLU D CD  1 
ATOM 5040 O OE1 . GLU D 1 9   ? 29.46392  -16.40347 18.19517  1.000 75.55976  ? 9   GLU D OE1 1 
ATOM 5041 O OE2 . GLU D 1 9   ? 27.40639  -15.66022 18.00774  1.000 81.32482  ? 9   GLU D OE2 1 
ATOM 5042 N N   . THR D 1 10  ? 32.39492  -13.79083 13.78946  1.000 59.72307  ? 10  THR D N   1 
ATOM 5043 C CA  . THR D 1 10  ? 33.69517  -13.49540 13.23257  1.000 59.50917  ? 10  THR D CA  1 
ATOM 5044 C C   . THR D 1 10  ? 34.47539  -12.58220 14.15197  1.000 59.17631  ? 10  THR D C   1 
ATOM 5045 O O   . THR D 1 10  ? 33.93435  -11.98325 15.08215  1.000 56.32528  ? 10  THR D O   1 
ATOM 5046 C CB  . THR D 1 10  ? 33.59019  -12.85952 11.85139  1.000 58.79374  ? 10  THR D CB  1 
ATOM 5047 O OG1 . THR D 1 10  ? 32.83323  -11.65206 11.94419  1.000 58.63460  ? 10  THR D OG1 1 
ATOM 5048 C CG2 . THR D 1 10  ? 32.90465  -13.81327 10.88474  1.000 59.98368  ? 10  THR D CG2 1 
ATOM 5049 N N   . MET D 1 11  ? 35.77899  -12.54360 13.88290  1.000 59.02416  ? 11  MET D N   1 
ATOM 5050 C CA  . MET D 1 11  ? 36.71445  -11.58849 14.44779  1.000 57.98351  ? 11  MET D CA  1 
ATOM 5051 C C   . MET D 1 11  ? 37.19356  -10.58013 13.42541  1.000 60.03112  ? 11  MET D C   1 
ATOM 5052 O O   . MET D 1 11  ? 38.14923  -9.84292  13.69943  1.000 59.07029  ? 11  MET D O   1 
ATOM 5053 C CB  . MET D 1 11  ? 37.90871  -12.31757 15.04565  1.000 57.17742  ? 11  MET D CB  1 
ATOM 5054 C CG  . MET D 1 11  ? 37.57290  -12.95869 16.33145  1.000 62.03846  ? 11  MET D CG  1 
ATOM 5055 S SD  . MET D 1 11  ? 37.23894  -11.68608 17.55358  1.000 70.36290  ? 11  MET D SD  1 
ATOM 5056 C CE  . MET D 1 11  ? 38.90947  -11.20961 17.92071  1.000 63.78255  ? 11  MET D CE  1 
ATOM 5057 N N   . GLY D 1 12  ? 36.56978  -10.54492 12.24831  1.000 60.47366  ? 12  GLY D N   1 
ATOM 5058 C CA  . GLY D 1 12  ? 36.99485  -9.65157  11.19672  1.000 60.11403  ? 12  GLY D CA  1 
ATOM 5059 C C   . GLY D 1 12  ? 35.82534  -9.25440  10.33387  1.000 63.12743  ? 12  GLY D C   1 
ATOM 5060 O O   . GLY D 1 12  ? 34.70013  -9.70985  10.52644  1.000 61.14843  ? 12  GLY D O   1 
ATOM 5061 N N   . SER D 1 13  ? 36.12473  -8.43099  9.33365   1.000 86.35004  ? 13  SER D N   1 
ATOM 5062 C CA  . SER D 1 13  ? 35.13553  -7.79665  8.47459   1.000 86.07258  ? 13  SER D CA  1 
ATOM 5063 C C   . SER D 1 13  ? 34.97479  -8.46962  7.11867   1.000 85.96605  ? 13  SER D C   1 
ATOM 5064 O O   . SER D 1 13  ? 33.83670  -8.68296  6.68465   1.000 88.75614  ? 13  SER D O   1 
ATOM 5065 C CB  . SER D 1 13  ? 35.50875  -6.32363  8.26652   1.000 87.02410  ? 13  SER D CB  1 
ATOM 5066 O OG  . SER D 1 13  ? 36.74289  -6.19954  7.55898   1.000 87.99474  ? 13  SER D OG  1 
ATOM 5067 N N   . GLY D 1 14  ? 36.07477  -8.80895  6.43417   1.000 68.28838  ? 14  GLY D N   1 
ATOM 5068 C CA  . GLY D 1 14  ? 36.00844  -9.17931  5.03063   1.000 69.83002  ? 14  GLY D CA  1 
ATOM 5069 C C   . GLY D 1 14  ? 35.69612  -10.64340 4.77217   1.000 68.21558  ? 14  GLY D C   1 
ATOM 5070 O O   . GLY D 1 14  ? 35.13783  -11.34891 5.61392   1.000 68.01581  ? 14  GLY D O   1 
ATOM 5071 N N   . GLU D 1 15  ? 36.05765  -11.11021 3.57205   1.000 67.73903  ? 15  GLU D N   1 
ATOM 5072 C CA  . GLU D 1 15  ? 35.95303  -12.54724 3.30992   1.000 65.62935  ? 15  GLU D CA  1 
ATOM 5073 C C   . GLU D 1 15  ? 37.14537  -13.31917 3.86149   1.000 62.04994  ? 15  GLU D C   1 
ATOM 5074 O O   . GLU D 1 15  ? 37.17762  -14.54462 3.73313   1.000 63.30168  ? 15  GLU D O   1 
ATOM 5075 C CB  . GLU D 1 15  ? 35.79483  -12.85190 1.80177   1.000 64.60307  ? 15  GLU D CB  1 
ATOM 5076 C CG  . GLU D 1 15  ? 37.07470  -12.76985 0.92288   1.000 66.45999  ? 15  GLU D CG  1 
ATOM 5077 C CD  . GLU D 1 15  ? 36.80518  -12.90630 -0.60138  1.000 67.62206  ? 15  GLU D CD  1 
ATOM 5078 O OE1 . GLU D 1 15  ? 35.62898  -13.04958 -1.02605  1.000 66.79960  ? 15  GLU D OE1 1 
ATOM 5079 O OE2 . GLU D 1 15  ? 37.78327  -12.84312 -1.38740  1.000 71.86095  ? 15  GLU D OE2 1 
ATOM 5080 N N   . LYS D 1 16  ? 38.13565  -12.63429 4.43290   1.000 61.77282  ? 16  LYS D N   1 
ATOM 5081 C CA  . LYS D 1 16  ? 39.24584  -13.27549 5.11803   1.000 60.88655  ? 16  LYS D CA  1 
ATOM 5082 C C   . LYS D 1 16  ? 39.10912  -13.17899 6.62735   1.000 59.90232  ? 16  LYS D C   1 
ATOM 5083 O O   . LYS D 1 16  ? 40.04407  -13.53067 7.35675   1.000 58.82824  ? 16  LYS D O   1 
ATOM 5084 C CB  . LYS D 1 16  ? 40.58469  -12.67595 4.67122   1.000 59.00689  ? 16  LYS D CB  1 
ATOM 5085 C CG  . LYS D 1 16  ? 40.88648  -12.82050 3.19221   1.000 55.41748  ? 16  LYS D CG  1 
ATOM 5086 C CD  . LYS D 1 16  ? 40.73292  -14.24525 2.68814   1.000 60.89315  ? 16  LYS D CD  1 
ATOM 5087 C CE  . LYS D 1 16  ? 41.74647  -15.23459 3.25742   1.000 63.83661  ? 16  LYS D CE  1 
ATOM 5088 N NZ  . LYS D 1 16  ? 41.53175  -16.58597 2.62938   1.000 66.71373  ? 16  LYS D NZ  1 
ATOM 5089 N N   . ALA D 1 17  ? 37.95291  -12.72792 7.10012   1.000 61.24378  ? 17  ALA D N   1 
ATOM 5090 C CA  . ALA D 1 17  ? 37.68233  -12.61025 8.52204   1.000 57.65045  ? 17  ALA D CA  1 
ATOM 5091 C C   . ALA D 1 17  ? 37.86830  -13.93843 9.24887   1.000 57.91885  ? 17  ALA D C   1 
ATOM 5092 O O   . ALA D 1 17  ? 37.41906  -14.98832 8.77678   1.000 54.96777  ? 17  ALA D O   1 
ATOM 5093 C CB  . ALA D 1 17  ? 36.25696  -12.11882 8.69161   1.000 60.49145  ? 17  ALA D CB  1 
ATOM 5094 N N   . ALA D 1 18  ? 38.53046  -13.88617 10.41342  1.000 59.67730  ? 18  ALA D N   1 
ATOM 5095 C CA  . ALA D 1 18  ? 38.59991  -15.05350 11.29432  1.000 58.23436  ? 18  ALA D CA  1 
ATOM 5096 C C   . ALA D 1 18  ? 37.20792  -15.44543 11.75718  1.000 56.53571  ? 18  ALA D C   1 
ATOM 5097 O O   . ALA D 1 18  ? 36.37151  -14.59420 12.05626  1.000 56.51847  ? 18  ALA D O   1 
ATOM 5098 C CB  . ALA D 1 18  ? 39.48248  -14.78632 12.50789  1.000 57.18852  ? 18  ALA D CB  1 
ATOM 5099 N N   . VAL D 1 19  ? 36.94897  -16.74259 11.78274  1.000 55.46525  ? 19  VAL D N   1 
ATOM 5100 C CA  . VAL D 1 19  ? 35.63696  -17.27832 12.11909  1.000 57.14191  ? 19  VAL D CA  1 
ATOM 5101 C C   . VAL D 1 19  ? 35.69747  -17.85062 13.52259  1.000 61.03878  ? 19  VAL D C   1 
ATOM 5102 O O   . VAL D 1 19  ? 36.61070  -18.62525 13.84888  1.000 60.54732  ? 19  VAL D O   1 
ATOM 5103 C CB  . VAL D 1 19  ? 35.16655  -18.33728 11.10651  1.000 59.77570  ? 19  VAL D CB  1 
ATOM 5104 C CG1 . VAL D 1 19  ? 34.63362  -17.67244 9.89053   1.000 60.09353  ? 19  VAL D CG1 1 
ATOM 5105 C CG2 . VAL D 1 19  ? 36.33638  -19.23183 10.70017  1.000 59.01896  ? 19  VAL D CG2 1 
ATOM 5106 N N   . ILE D 1 20  ? 34.74153  -17.43850 14.35384  1.000 60.41536  ? 20  ILE D N   1 
ATOM 5107 C CA  . ILE D 1 20  ? 34.59840  -17.95966 15.70832  1.000 62.67506  ? 20  ILE D CA  1 
ATOM 5108 C C   . ILE D 1 20  ? 33.76297  -19.22345 15.71587  1.000 62.81982  ? 20  ILE D C   1 
ATOM 5109 O O   . ILE D 1 20  ? 34.18152  -20.24048 16.27218  1.000 64.02122  ? 20  ILE D O   1 
ATOM 5110 C CB  . ILE D 1 20  ? 33.97351  -16.89248 16.62369  1.000 63.61635  ? 20  ILE D CB  1 
ATOM 5111 C CG1 . ILE D 1 20  ? 34.79520  -15.61889 16.60810  1.000 60.36602  ? 20  ILE D CG1 1 
ATOM 5112 C CG2 . ILE D 1 20  ? 33.89604  -17.40740 18.02583  1.000 65.54652  ? 20  ILE D CG2 1 
ATOM 5113 C CD1 . ILE D 1 20  ? 34.01111  -14.46379 17.10521  1.000 61.75585  ? 20  ILE D CD1 1 
ATOM 5114 N N   . ASP D 1 21  ? 32.57719  -19.17042 15.09829  1.000 63.54629  ? 21  ASP D N   1 
ATOM 5115 C CA  . ASP D 1 21  ? 31.74688  -20.35687 14.90953  1.000 67.52610  ? 21  ASP D CA  1 
ATOM 5116 C C   . ASP D 1 21  ? 30.85013  -20.19817 13.68776  1.000 66.15575  ? 21  ASP D C   1 
ATOM 5117 O O   . ASP D 1 21  ? 30.62966  -19.09802 13.17844  1.000 66.07516  ? 21  ASP D O   1 
ATOM 5118 C CB  . ASP D 1 21  ? 30.86680  -20.69127 16.13215  1.000 65.40671  ? 21  ASP D CB  1 
ATOM 5119 C CG  . ASP D 1 21  ? 29.77914  -19.64615 16.40665  1.000 72.35822  ? 21  ASP D CG  1 
ATOM 5120 O OD1 . ASP D 1 21  ? 29.78373  -18.55398 15.81750  1.000 75.12794  ? 21  ASP D OD1 1 
ATOM 5121 O OD2 . ASP D 1 21  ? 28.87109  -19.92730 17.20673  1.000 81.72155  ? 21  ASP D OD2 1 
ATOM 5122 N N   . LEU D 1 22  ? 30.32436  -21.33567 13.25095  1.000 70.49009  ? 22  LEU D N   1 
ATOM 5123 C CA  . LEU D 1 22  ? 29.36315  -21.46601 12.16808  1.000 74.03518  ? 22  LEU D CA  1 
ATOM 5124 C C   . LEU D 1 22  ? 28.16126  -22.27267 12.65302  1.000 76.88287  ? 22  LEU D C   1 
ATOM 5125 O O   . LEU D 1 22  ? 28.32488  -23.32093 13.28453  1.000 73.63004  ? 22  LEU D O   1 
ATOM 5126 C CB  . LEU D 1 22  ? 30.01071  -22.15236 10.94102  1.000 69.00214  ? 22  LEU D CB  1 
ATOM 5127 C CG  . LEU D 1 22  ? 29.08794  -22.53571 9.78737   1.000 66.02595  ? 22  LEU D CG  1 
ATOM 5128 C CD1 . LEU D 1 22  ? 28.32725  -21.32749 9.31420   1.000 71.27643  ? 22  LEU D CD1 1 
ATOM 5129 C CD2 . LEU D 1 22  ? 29.90587  -23.13605 8.65797   1.000 66.43002  ? 22  LEU D CD2 1 
ATOM 5130 N N   . ALA D 1 23  ? 26.95532  -21.79249 12.33912  1.000 76.66378  ? 23  ALA D N   1 
ATOM 5131 C CA  . ALA D 1 23  ? 25.70936  -22.46002 12.70895  1.000 79.60546  ? 23  ALA D CA  1 
ATOM 5132 C C   . ALA D 1 23  ? 24.89571  -22.74197 11.44960  1.000 83.26296  ? 23  ALA D C   1 
ATOM 5133 O O   . ALA D 1 23  ? 24.24280  -21.84029 10.92287  1.000 84.50836  ? 23  ALA D O   1 
ATOM 5134 C CB  . ALA D 1 23  ? 24.91450  -21.60675 13.69218  1.000 84.46149  ? 23  ALA D CB  1 
ATOM 5135 N N   . VAL D 1 24  ? 24.89980  -23.99337 10.98878  1.000 87.03692  ? 24  VAL D N   1 
ATOM 5136 C CA  . VAL D 1 24  ? 24.09174  -24.42186 9.84846   1.000 94.10727  ? 24  VAL D CA  1 
ATOM 5137 C C   . VAL D 1 24  ? 22.86477  -25.18496 10.34829  1.000 105.82977 ? 24  VAL D C   1 
ATOM 5138 O O   . VAL D 1 24  ? 22.98772  -26.14332 11.12369  1.000 107.11498 ? 24  VAL D O   1 
ATOM 5139 C CB  . VAL D 1 24  ? 24.92041  -25.26915 8.86081   1.000 92.72045  ? 24  VAL D CB  1 
ATOM 5140 C CG1 . VAL D 1 24  ? 25.53397  -26.48514 9.53416   1.000 93.55579  ? 24  VAL D CG1 1 
ATOM 5141 C CG2 . VAL D 1 24  ? 24.06304  -25.70492 7.69381   1.000 92.63190  ? 24  VAL D CG2 1 
ATOM 5142 N N   . ILE D 1 25  ? 21.67632  -24.75406 9.91477   1.000 115.20337 ? 25  ILE D N   1 
ATOM 5143 C CA  . ILE D 1 25  ? 20.40570  -25.40210 10.25790  1.000 116.03051 ? 25  ILE D CA  1 
ATOM 5144 C C   . ILE D 1 25  ? 19.60515  -25.61721 8.97231   1.000 116.49634 ? 25  ILE D C   1 
ATOM 5145 O O   . ILE D 1 25  ? 19.13225  -24.64756 8.36273   1.000 116.16103 ? 25  ILE D O   1 
ATOM 5146 C CB  . ILE D 1 25  ? 19.58828  -24.58430 11.27513  1.000 112.37211 ? 25  ILE D CB  1 
ATOM 5147 C CG1 . ILE D 1 25  ? 20.27657  -24.54204 12.63878  1.000 108.40708 ? 25  ILE D CG1 1 
ATOM 5148 C CG2 . ILE D 1 25  ? 18.18065  -25.13894 11.42666  1.000 114.31390 ? 25  ILE D CG2 1 
ATOM 5149 C CD1 . ILE D 1 25  ? 19.57977  -23.63624 13.59987  1.000 108.20252 ? 25  ILE D CD1 1 
ATOM 5150 N N   . ALA D 1 26  ? 19.44513  -26.88133 8.56509   1.000 117.53683 ? 26  ALA D N   1 
ATOM 5151 C CA  . ALA D 1 26  ? 18.54721  -27.21951 7.46331   1.000 117.89608 ? 26  ALA D CA  1 
ATOM 5152 C C   . ALA D 1 26  ? 17.09818  -27.00187 7.88289   1.000 120.74476 ? 26  ALA D C   1 
ATOM 5153 O O   . ALA D 1 26  ? 16.75482  -27.09781 9.06395   1.000 121.59987 ? 26  ALA D O   1 
ATOM 5154 C CB  . ALA D 1 26  ? 18.74188  -28.67360 7.02363   1.000 113.83216 ? 26  ALA D CB  1 
ATOM 5155 N N   . PHE D 1 27  ? 16.24239  -26.68815 6.91127   1.000 123.31119 ? 27  PHE D N   1 
ATOM 5156 C CA  . PHE D 1 27  ? 14.83407  -26.49432 7.23157   1.000 125.23239 ? 27  PHE D CA  1 
ATOM 5157 C C   . PHE D 1 27  ? 13.99096  -26.65955 5.97613   1.000 132.80662 ? 27  PHE D C   1 
ATOM 5158 O O   . PHE D 1 27  ? 14.48194  -26.53924 4.84890   1.000 132.29890 ? 27  PHE D O   1 
ATOM 5159 C CB  . PHE D 1 27  ? 14.59050  -25.13229 7.88737   1.000 122.68186 ? 27  PHE D CB  1 
ATOM 5160 C CG  . PHE D 1 27  ? 14.76908  -23.96516 6.96929   1.000 123.34703 ? 27  PHE D CG  1 
ATOM 5161 C CD1 . PHE D 1 27  ? 16.03338  -23.46863 6.68869   1.000 121.51231 ? 27  PHE D CD1 1 
ATOM 5162 C CD2 . PHE D 1 27  ? 13.66554  -23.31683 6.44211   1.000 123.73503 ? 27  PHE D CD2 1 
ATOM 5163 C CE1 . PHE D 1 27  ? 16.19446  -22.37508 5.85990   1.000 119.87996 ? 27  PHE D CE1 1 
ATOM 5164 C CE2 . PHE D 1 27  ? 13.81727  -22.22089 5.62001   1.000 124.44724 ? 27  PHE D CE2 1 
ATOM 5165 C CZ  . PHE D 1 27  ? 15.08295  -21.74685 5.32915   1.000 120.63951 ? 27  PHE D CZ  1 
ATOM 5166 N N   . ASP D 1 28  ? 12.68830  -26.93736 6.19841   1.000 136.52537 ? 28  ASP D N   1 
ATOM 5167 C CA  . ASP D 1 28  ? 11.80798  -27.37429 5.11948   1.000 138.73155 ? 28  ASP D CA  1 
ATOM 5168 C C   . ASP D 1 28  ? 11.20983  -26.17694 4.38893   1.000 137.64138 ? 28  ASP D C   1 
ATOM 5169 O O   . ASP D 1 28  ? 10.60210  -25.30399 5.02740   1.000 134.41751 ? 28  ASP D O   1 
ATOM 5170 C CB  . ASP D 1 28  ? 10.69614  -28.26676 5.64878   1.000 139.40985 ? 28  ASP D CB  1 
ATOM 5171 C CG  . ASP D 1 28  ? 9.90621   -28.93138 4.53328   1.000 139.35690 ? 28  ASP D CG  1 
ATOM 5172 O OD1 . ASP D 1 28  ? 10.44893  -29.85011 3.88024   1.000 140.52031 ? 28  ASP D OD1 1 
ATOM 5173 O OD2 . ASP D 1 28  ? 8.74511   -28.53676 4.30613   1.000 140.82203 ? 28  ASP D OD2 1 
ATOM 5174 N N   . PRO D 1 29  ? 11.34928  -26.12701 3.05998   1.000 136.68711 ? 29  PRO D N   1 
ATOM 5175 C CA  . PRO D 1 29  ? 10.87663  -24.95095 2.31292   1.000 135.71638 ? 29  PRO D CA  1 
ATOM 5176 C C   . PRO D 1 29  ? 9.35925   -24.85627 2.18803   1.000 135.65173 ? 29  PRO D C   1 
ATOM 5177 O O   . PRO D 1 29  ? 8.82297   -23.74166 2.23785   1.000 137.25047 ? 29  PRO D O   1 
ATOM 5178 C CB  . PRO D 1 29  ? 11.55129  -25.12284 0.94470   1.000 140.37846 ? 29  PRO D CB  1 
ATOM 5179 C CG  . PRO D 1 29  ? 11.77799  -26.60925 0.81269   1.000 138.91684 ? 29  PRO D CG  1 
ATOM 5180 C CD  . PRO D 1 29  ? 12.04790  -27.10384 2.20483   1.000 136.58449 ? 29  PRO D CD  1 
ATOM 5181 N N   . ASN D 1 30  ? 8.65507   -25.97631 2.03619   1.000 135.54675 ? 30  ASN D N   1 
ATOM 5182 C CA  . ASN D 1 30  ? 7.19426   -25.98603 1.95159   1.000 134.11511 ? 30  ASN D CA  1 
ATOM 5183 C C   . ASN D 1 30  ? 6.58598   -25.41431 3.24005   1.000 138.15641 ? 30  ASN D C   1 
ATOM 5184 O O   . ASN D 1 30  ? 6.83265   -25.95899 4.32602   1.000 136.35836 ? 30  ASN D O   1 
ATOM 5185 C CB  . ASN D 1 30  ? 6.75200   -27.42843 1.69521   1.000 127.74718 ? 30  ASN D CB  1 
ATOM 5186 C CG  . ASN D 1 30  ? 5.28489   -27.55356 1.34680   1.000 124.54058 ? 30  ASN D CG  1 
ATOM 5187 O OD1 . ASN D 1 30  ? 4.53106   -26.58386 1.38898   1.000 125.21243 ? 30  ASN D OD1 1 
ATOM 5188 N ND2 . ASN D 1 30  ? 4.87520   -28.76310 0.97524   1.000 117.96366 ? 30  ASN D ND2 1 
ATOM 5189 N N   . PRO D 1 31  ? 5.79004   -24.32429 3.17029   1.000 139.05855 ? 31  PRO D N   1 
ATOM 5190 C CA  . PRO D 1 31  ? 5.62087   -23.45711 4.35144   1.000 138.20266 ? 31  PRO D CA  1 
ATOM 5191 C C   . PRO D 1 31  ? 4.71418   -23.95091 5.47449   1.000 140.80792 ? 31  PRO D C   1 
ATOM 5192 O O   . PRO D 1 31  ? 5.08351   -23.82821 6.64828   1.000 141.87283 ? 31  PRO D O   1 
ATOM 5193 C CB  . PRO D 1 31  ? 5.05500   -22.16585 3.74385   1.000 138.93257 ? 31  PRO D CB  1 
ATOM 5194 C CG  . PRO D 1 31  ? 4.34161   -22.61341 2.52184   1.000 140.38887 ? 31  PRO D CG  1 
ATOM 5195 C CD  . PRO D 1 31  ? 5.13900   -23.75882 1.97370   1.000 139.30833 ? 31  PRO D CD  1 
ATOM 5196 N N   . GLU D 1 32  ? 3.54090   -24.48964 5.14775   1.000 140.49619 ? 32  GLU D N   1 
ATOM 5197 C CA  . GLU D 1 32  ? 2.45658   -24.62650 6.13109   1.000 137.78977 ? 32  GLU D CA  1 
ATOM 5198 C C   . GLU D 1 32  ? 2.86193   -25.36669 7.40145   1.000 133.64670 ? 32  GLU D C   1 
ATOM 5199 O O   . GLU D 1 32  ? 2.85830   -24.78322 8.48615   1.000 128.59505 ? 32  GLU D O   1 
ATOM 5200 C CB  . GLU D 1 32  ? 1.24854   -25.32378 5.50014   1.000 139.48119 ? 32  GLU D CB  1 
ATOM 5201 C CG  . GLU D 1 32  ? 1.47187   -26.78483 5.13090   1.000 144.25113 ? 32  GLU D CG  1 
ATOM 5202 C CD  . GLU D 1 32  ? 0.25641   -27.41347 4.44867   1.000 152.13163 ? 32  GLU D CD  1 
ATOM 5203 O OE1 . GLU D 1 32  ? -0.73299  -26.68910 4.20124   1.000 155.90214 ? 32  GLU D OE1 1 
ATOM 5204 O OE2 . GLU D 1 32  ? 0.28060   -28.63520 4.17362   1.000 152.13249 ? 32  GLU D OE2 1 
ATOM 5205 N N   . THR D 1 36  ? 6.56904   -23.44179 20.38632  1.000 143.95436 ? 36  THR D N   1 
ATOM 5206 C CA  . THR D 1 36  ? 6.88334   -22.25699 19.59316  1.000 139.23641 ? 36  THR D CA  1 
ATOM 5207 C C   . THR D 1 36  ? 8.28779   -22.29744 18.94466  1.000 137.92581 ? 36  THR D C   1 
ATOM 5208 O O   . THR D 1 36  ? 8.40568   -22.25365 17.71371  1.000 135.95212 ? 36  THR D O   1 
ATOM 5209 C CB  . THR D 1 36  ? 6.72267   -20.97292 20.45872  1.000 138.27874 ? 36  THR D CB  1 
ATOM 5210 O OG1 . THR D 1 36  ? 7.17096   -19.82445 19.72559  1.000 138.78179 ? 36  THR D OG1 1 
ATOM 5211 C CG2 . THR D 1 36  ? 7.42879   -21.09632 21.82991  1.000 136.17404 ? 36  THR D CG2 1 
ATOM 5212 N N   . PHE D 1 37  ? 9.33085   -22.42731 19.76641  1.000 138.83103 ? 37  PHE D N   1 
ATOM 5213 C CA  . PHE D 1 37  ? 10.72283  -22.23597 19.36714  1.000 134.21460 ? 37  PHE D CA  1 
ATOM 5214 C C   . PHE D 1 37  ? 11.52729  -23.53130 19.26595  1.000 132.39373 ? 37  PHE D C   1 
ATOM 5215 O O   . PHE D 1 37  ? 12.39630  -23.64984 18.39578  1.000 129.75221 ? 37  PHE D O   1 
ATOM 5216 C CB  . PHE D 1 37  ? 11.38036  -21.27690 20.37121  1.000 135.77904 ? 37  PHE D CB  1 
ATOM 5217 C CG  . PHE D 1 37  ? 12.84491  -21.02886 20.14196  1.000 134.02189 ? 37  PHE D CG  1 
ATOM 5218 C CD1 . PHE D 1 37  ? 13.27832  -20.31438 19.04595  1.000 126.97373 ? 37  PHE D CD1 1 
ATOM 5219 C CD2 . PHE D 1 37  ? 13.78491  -21.44465 21.07702  1.000 134.85520 ? 37  PHE D CD2 1 
ATOM 5220 C CE1 . PHE D 1 37  ? 14.62159  -20.06090 18.85773  1.000 124.46085 ? 37  PHE D CE1 1 
ATOM 5221 C CE2 . PHE D 1 37  ? 15.13278  -21.18593 20.89574  1.000 131.67669 ? 37  PHE D CE2 1 
ATOM 5222 C CZ  . PHE D 1 37  ? 15.54884  -20.49534 19.78424  1.000 127.34218 ? 37  PHE D CZ  1 
ATOM 5223 N N   . ASP D 1 38  ? 11.22854  -24.52014 20.11520  1.000 137.11753 ? 38  ASP D N   1 
ATOM 5224 C CA  . ASP D 1 38  ? 12.19230  -25.56590 20.45828  1.000 133.94084 ? 38  ASP D CA  1 
ATOM 5225 C C   . ASP D 1 38  ? 12.46361  -26.56780 19.34068  1.000 131.91465 ? 38  ASP D C   1 
ATOM 5226 O O   . ASP D 1 38  ? 13.43196  -27.32757 19.43987  1.000 131.76492 ? 38  ASP D O   1 
ATOM 5227 C CB  . ASP D 1 38  ? 11.71634  -26.31768 21.70868  1.000 136.28617 ? 38  ASP D CB  1 
ATOM 5228 N N   . GLU D 1 39  ? 11.64873  -26.60869 18.29112  1.000 127.22214 ? 39  GLU D N   1 
ATOM 5229 C CA  . GLU D 1 39  ? 11.72654  -27.77316 17.41680  1.000 124.10092 ? 39  GLU D CA  1 
ATOM 5230 C C   . GLU D 1 39  ? 12.87058  -27.66144 16.41010  1.000 124.62060 ? 39  GLU D C   1 
ATOM 5231 O O   . GLU D 1 39  ? 13.59410  -28.64197 16.20197  1.000 126.15980 ? 39  GLU D O   1 
ATOM 5232 C CB  . GLU D 1 39  ? 10.37556  -28.00779 16.73222  1.000 120.63546 ? 39  GLU D CB  1 
ATOM 5233 C CG  . GLU D 1 39  ? 10.01825  -27.12763 15.53856  1.000 121.08973 ? 39  GLU D CG  1 
ATOM 5234 C CD  . GLU D 1 39  ? 9.63425   -25.70199 15.91215  1.000 119.56671 ? 39  GLU D CD  1 
ATOM 5235 O OE1 . GLU D 1 39  ? 10.14954  -25.17519 16.91564  1.000 124.91678 ? 39  GLU D OE1 1 
ATOM 5236 O OE2 . GLU D 1 39  ? 8.77339   -25.11702 15.22530  1.000 113.04523 ? 39  GLU D OE2 1 
ATOM 5237 N N   . LEU D 1 40  ? 13.07840  -26.48269 15.79919  1.000 123.50663 ? 40  LEU D N   1 
ATOM 5238 C CA  . LEU D 1 40  ? 14.17552  -26.32574 14.83328  1.000 125.09800 ? 40  LEU D CA  1 
ATOM 5239 C C   . LEU D 1 40  ? 15.51935  -26.17649 15.52643  1.000 122.34424 ? 40  LEU D C   1 
ATOM 5240 O O   . LEU D 1 40  ? 16.56763  -26.43156 14.91530  1.000 117.17820 ? 40  LEU D O   1 
ATOM 5241 C CB  . LEU D 1 40  ? 13.94701  -25.11365 13.92900  1.000 119.16660 ? 40  LEU D CB  1 
ATOM 5242 C CG  . LEU D 1 40  ? 12.77771  -25.17636 12.96016  1.000 115.47102 ? 40  LEU D CG  1 
ATOM 5243 C CD1 . LEU D 1 40  ? 12.60863  -23.81828 12.33930  1.000 109.25282 ? 40  LEU D CD1 1 
ATOM 5244 C CD2 . LEU D 1 40  ? 13.02392  -26.23690 11.91445  1.000 117.19263 ? 40  LEU D CD2 1 
ATOM 5245 N N   . VAL D 1 41  ? 15.49250  -25.74327 16.78942  1.000 122.05350 ? 41  VAL D N   1 
ATOM 5246 C CA  . VAL D 1 41  ? 16.70407  -25.55709 17.58061  1.000 119.28020 ? 41  VAL D CA  1 
ATOM 5247 C C   . VAL D 1 41  ? 17.42411  -26.88428 17.76758  1.000 118.39888 ? 41  VAL D C   1 
ATOM 5248 O O   . VAL D 1 41  ? 18.65262  -26.93743 17.89692  1.000 114.89230 ? 41  VAL D O   1 
ATOM 5249 C CB  . VAL D 1 41  ? 16.33336  -24.91916 18.93121  1.000 122.94313 ? 41  VAL D CB  1 
ATOM 5250 C CG1 . VAL D 1 41  ? 17.57312  -24.56629 19.73718  1.000 119.94310 ? 41  VAL D CG1 1 
ATOM 5251 C CG2 . VAL D 1 41  ? 15.43466  -23.72387 18.71368  1.000 124.87415 ? 41  VAL D CG2 1 
ATOM 5252 N N   . SER D 1 42  ? 16.66369  -27.97256 17.82882  1.000 120.44367 ? 42  SER D N   1 
ATOM 5253 C CA  . SER D 1 42  ? 17.26421  -29.29422 17.90919  1.000 119.97459 ? 42  SER D CA  1 
ATOM 5254 C C   . SER D 1 42  ? 17.90269  -29.69804 16.59208  1.000 117.80676 ? 42  SER D C   1 
ATOM 5255 O O   . SER D 1 42  ? 18.90116  -30.42520 16.58062  1.000 118.56669 ? 42  SER D O   1 
ATOM 5256 C CB  . SER D 1 42  ? 16.19754  -30.30805 18.31880  1.000 123.21564 ? 42  SER D CB  1 
ATOM 5257 O OG  . SER D 1 42  ? 15.17396  -30.37933 17.33933  1.000 123.39961 ? 42  SER D OG  1 
ATOM 5258 N N   . ARG D 1 43  ? 17.35625  -29.21477 15.48073  1.000 118.91117 ? 43  ARG D N   1 
ATOM 5259 C CA  . ARG D 1 43  ? 17.60998  -29.85564 14.20112  1.000 120.02958 ? 43  ARG D CA  1 
ATOM 5260 C C   . ARG D 1 43  ? 19.05000  -29.65929 13.74439  1.000 123.25362 ? 43  ARG D C   1 
ATOM 5261 O O   . ARG D 1 43  ? 19.67234  -30.60127 13.23395  1.000 123.35136 ? 43  ARG D O   1 
ATOM 5262 C CB  . ARG D 1 43  ? 16.60606  -29.33559 13.17530  1.000 118.90533 ? 43  ARG D CB  1 
ATOM 5263 C CG  . ARG D 1 43  ? 15.20112  -29.63312 13.63681  1.000 121.45354 ? 43  ARG D CG  1 
ATOM 5264 C CD  . ARG D 1 43  ? 14.12136  -29.46571 12.59117  1.000 127.65882 ? 43  ARG D CD  1 
ATOM 5265 N NE  . ARG D 1 43  ? 12.82599  -29.82053 13.16966  1.000 130.69293 ? 43  ARG D NE  1 
ATOM 5266 C CZ  . ARG D 1 43  ? 11.69521  -29.96217 12.48868  1.000 131.57161 ? 43  ARG D CZ  1 
ATOM 5267 N NH1 . ARG D 1 43  ? 11.66572  -29.87426 11.16844  1.000 132.75439 ? 43  ARG D NH1 1 
ATOM 5268 N NH2 . ARG D 1 43  ? 10.56924  -30.22638 13.14840  1.000 131.30701 ? 43  ARG D NH2 1 
ATOM 5269 N N   . GLY D 1 44  ? 19.60814  -28.46048 13.95040  1.000 122.70989 ? 44  GLY D N   1 
ATOM 5270 C CA  . GLY D 1 44  ? 20.88066  -28.08758 13.37031  1.000 119.40994 ? 44  GLY D CA  1 
ATOM 5271 C C   . GLY D 1 44  ? 22.06480  -28.24809 14.31849  1.000 117.26025 ? 44  GLY D C   1 
ATOM 5272 O O   . GLY D 1 44  ? 21.92563  -28.60855 15.48570  1.000 116.98666 ? 44  GLY D O   1 
ATOM 5273 N N   . ILE D 1 45  ? 23.25845  -27.95971 13.77954  1.000 104.56796 ? 45  ILE D N   1 
ATOM 5274 C CA  . ILE D 1 45  ? 24.52154  -28.14473 14.48827  1.000 97.59160  ? 45  ILE D CA  1 
ATOM 5275 C C   . ILE D 1 45  ? 25.33490  -26.84963 14.41684  1.000 91.34028  ? 45  ILE D C   1 
ATOM 5276 O O   . ILE D 1 45  ? 24.97112  -25.90284 13.72431  1.000 90.50286  ? 45  ILE D O   1 
ATOM 5277 C CB  . ILE D 1 45  ? 25.32015  -29.34859 13.93827  1.000 92.78628  ? 45  ILE D CB  1 
ATOM 5278 C CG1 . ILE D 1 45  ? 25.81734  -29.10757 12.51980  1.000 99.35222  ? 45  ILE D CG1 1 
ATOM 5279 C CG2 . ILE D 1 45  ? 24.45735  -30.57179 13.89252  1.000 95.80361  ? 45  ILE D CG2 1 
ATOM 5280 C CD1 . ILE D 1 45  ? 27.24937  -28.63723 12.44910  1.000 94.05753  ? 45  ILE D CD1 1 
ATOM 5281 N N   . LYS D 1 46  ? 26.43385  -26.80427 15.17765  1.000 89.10719  ? 46  LYS D N   1 
ATOM 5282 C CA  . LYS D 1 46  ? 27.28126  -25.61283 15.26503  1.000 82.43247  ? 46  LYS D CA  1 
ATOM 5283 C C   . LYS D 1 46  ? 28.74623  -26.02520 15.32389  1.000 81.80252  ? 46  LYS D C   1 
ATOM 5284 O O   . LYS D 1 46  ? 29.17617  -26.65422 16.29320  1.000 79.35890  ? 46  LYS D O   1 
ATOM 5285 C CB  . LYS D 1 46  ? 26.93137  -24.75028 16.48346  1.000 69.74260  ? 46  LYS D CB  1 
ATOM 5286 N N   . ILE D 1 47  ? 29.51989  -25.65035 14.28911  1.000 82.01324  ? 47  ILE D N   1 
ATOM 5287 C CA  . ILE D 1 47  ? 30.95760  -25.89590 14.24357  1.000 75.63011  ? 47  ILE D CA  1 
ATOM 5288 C C   . ILE D 1 47  ? 31.65590  -24.75178 14.96238  1.000 70.26659  ? 47  ILE D C   1 
ATOM 5289 O O   . ILE D 1 47  ? 31.20794  -23.60560 14.90302  1.000 69.40264  ? 47  ILE D O   1 
ATOM 5290 C CB  . ILE D 1 47  ? 31.46582  -26.00978 12.79301  1.000 74.25442  ? 47  ILE D CB  1 
ATOM 5291 C CG1 . ILE D 1 47  ? 30.67243  -27.02644 11.96806  1.000 77.58453  ? 47  ILE D CG1 1 
ATOM 5292 C CG2 . ILE D 1 47  ? 32.92244  -26.40428 12.79276  1.000 75.90443  ? 47  ILE D CG2 1 
ATOM 5293 C CD1 . ILE D 1 47  ? 29.58716  -26.40735 11.10537  1.000 77.08143  ? 47  ILE D CD1 1 
ATOM 5294 N N   . LYS D 1 48  ? 32.75459  -25.04415 15.63829  1.000 71.19867  ? 48  LYS D N   1 
ATOM 5295 C CA  . LYS D 1 48  ? 33.49826  -24.00932 16.33596  1.000 71.32061  ? 48  LYS D CA  1 
ATOM 5296 C C   . LYS D 1 48  ? 34.95924  -24.11274 15.93289  1.000 72.08304  ? 48  LYS D C   1 
ATOM 5297 O O   . LYS D 1 48  ? 35.49457  -25.21965 15.82204  1.000 73.25849  ? 48  LYS D O   1 
ATOM 5298 C CB  . LYS D 1 48  ? 33.30594  -24.12374 17.86494  1.000 65.86127  ? 48  LYS D CB  1 
ATOM 5299 C CG  . LYS D 1 48  ? 33.95169  -22.99907 18.66038  1.000 68.68394  ? 48  LYS D CG  1 
ATOM 5300 C CD  . LYS D 1 48  ? 33.46424  -22.97359 20.09873  1.000 73.45126  ? 48  LYS D CD  1 
ATOM 5301 C CE  . LYS D 1 48  ? 34.05442  -21.81683 20.88752  1.000 69.97235  ? 48  LYS D CE  1 
ATOM 5302 N NZ  . LYS D 1 48  ? 35.47899  -22.07135 21.19502  1.000 73.06753  ? 48  LYS D NZ  1 
ATOM 5303 N N   . PHE D 1 49  ? 35.59420  -22.95717 15.70080  1.000 68.94567  ? 49  PHE D N   1 
ATOM 5304 C CA  . PHE D 1 49  ? 36.89560  -22.88093 15.03961  1.000 71.84112  ? 49  PHE D CA  1 
ATOM 5305 C C   . PHE D 1 49  ? 37.99286  -22.45428 16.00492  1.000 72.73065  ? 49  PHE D C   1 
ATOM 5306 O O   . PHE D 1 49  ? 37.78979  -21.57061 16.83707  1.000 76.21146  ? 49  PHE D O   1 
ATOM 5307 C CB  . PHE D 1 49  ? 36.87982  -21.88995 13.86899  1.000 67.08127  ? 49  PHE D CB  1 
ATOM 5308 C CG  . PHE D 1 49  ? 35.89233  -22.22503 12.81195  1.000 65.63153  ? 49  PHE D CG  1 
ATOM 5309 C CD1 . PHE D 1 49  ? 36.12652  -23.25599 11.93908  1.000 65.98284  ? 49  PHE D CD1 1 
ATOM 5310 C CD2 . PHE D 1 49  ? 34.72600  -21.49472 12.68643  1.000 64.80853  ? 49  PHE D CD2 1 
ATOM 5311 C CE1 . PHE D 1 49  ? 35.20836  -23.56320 10.97583  1.000 67.84810  ? 49  PHE D CE1 1 
ATOM 5312 C CE2 . PHE D 1 49  ? 33.80632  -21.79845 11.72179  1.000 64.17410  ? 49  PHE D CE2 1 
ATOM 5313 C CZ  . PHE D 1 49  ? 34.04714  -22.84114 10.86658  1.000 64.15677  ? 49  PHE D CZ  1 
ATOM 5314 N N   . ASP D 1 50  ? 39.16801  -23.05466 15.85496  1.000 72.89763  ? 50  ASP D N   1 
ATOM 5315 C CA  . ASP D 1 50  ? 40.35665  -22.65142 16.59872  1.000 74.62593  ? 50  ASP D CA  1 
ATOM 5316 C C   . ASP D 1 50  ? 40.82377  -21.27311 16.13051  1.000 75.96119  ? 50  ASP D C   1 
ATOM 5317 O O   . ASP D 1 50  ? 41.41425  -21.14574 15.05676  1.000 79.55507  ? 50  ASP D O   1 
ATOM 5318 C CB  . ASP D 1 50  ? 41.42987  -23.72405 16.41436  1.000 76.43911  ? 50  ASP D CB  1 
ATOM 5319 C CG  . ASP D 1 50  ? 42.78811  -23.34600 17.00039  1.000 81.32410  ? 50  ASP D CG  1 
ATOM 5320 O OD1 . ASP D 1 50  ? 43.00700  -22.19398 17.42059  1.000 86.09352  ? 50  ASP D OD1 1 
ATOM 5321 O OD2 . ASP D 1 50  ? 43.66950  -24.22541 17.03526  1.000 84.42584  ? 50  ASP D OD2 1 
ATOM 5322 N N   . LEU D 1 51  ? 40.60184  -20.24055 16.95447  1.000 78.41364  ? 51  LEU D N   1 
ATOM 5323 C CA  . LEU D 1 51  ? 41.05939  -18.89608 16.59760  1.000 79.42085  ? 51  LEU D CA  1 
ATOM 5324 C C   . LEU D 1 51  ? 42.56816  -18.82967 16.43523  1.000 81.12371  ? 51  LEU D C   1 
ATOM 5325 O O   . LEU D 1 51  ? 43.07006  -18.09043 15.58472  1.000 81.63611  ? 51  LEU D O   1 
ATOM 5326 C CB  . LEU D 1 51  ? 40.63671  -17.85754 17.64092  1.000 74.41881  ? 51  LEU D CB  1 
ATOM 5327 C CG  . LEU D 1 51  ? 39.20641  -17.35300 17.64423  1.000 67.56123  ? 51  LEU D CG  1 
ATOM 5328 C CD1 . LEU D 1 51  ? 39.09958  -16.20014 18.59253  1.000 67.73544  ? 51  LEU D CD1 1 
ATOM 5329 C CD2 . LEU D 1 51  ? 38.80912  -16.91339 16.25646  1.000 70.71590  ? 51  LEU D CD2 1 
ATOM 5330 N N   . LYS D 1 52  ? 43.30852  -19.52991 17.29317  1.000 90.64202  ? 52  LYS D N   1 
ATOM 5331 C CA  . LYS D 1 52  ? 44.75723  -19.37460 17.30322  1.000 89.56047  ? 52  LYS D CA  1 
ATOM 5332 C C   . LYS D 1 52  ? 45.37360  -19.96080 16.04965  1.000 90.39029  ? 52  LYS D C   1 
ATOM 5333 O O   . LYS D 1 52  ? 46.32652  -19.39462 15.50392  1.000 90.50360  ? 52  LYS D O   1 
ATOM 5334 C CB  . LYS D 1 52  ? 45.34679  -20.01252 18.55998  1.000 92.18286  ? 52  LYS D CB  1 
ATOM 5335 C CG  . LYS D 1 52  ? 45.14554  -19.16087 19.79014  1.000 95.31003  ? 52  LYS D CG  1 
ATOM 5336 C CD  . LYS D 1 52  ? 43.76024  -19.35361 20.39942  1.000 94.09469  ? 52  LYS D CD  1 
ATOM 5337 C CE  . LYS D 1 52  ? 43.60594  -18.51654 21.67542  1.000 97.90515  ? 52  LYS D CE  1 
ATOM 5338 N NZ  . LYS D 1 52  ? 43.65822  -17.04260 21.40099  1.000 95.47791  ? 52  LYS D NZ  1 
ATOM 5339 N N   . SER D 1 53  ? 44.82942  -21.08222 15.56336  1.000 85.01953  ? 53  SER D N   1 
ATOM 5340 C CA  . SER D 1 53  ? 45.36242  -21.68109 14.34051  1.000 85.66538  ? 53  SER D CA  1 
ATOM 5341 C C   . SER D 1 53  ? 45.21898  -20.73534 13.15558  1.000 82.53852  ? 53  SER D C   1 
ATOM 5342 O O   . SER D 1 53  ? 46.06112  -20.74321 12.25062  1.000 87.36613  ? 53  SER D O   1 
ATOM 5343 C CB  . SER D 1 53  ? 44.68090  -23.02642 14.05038  1.000 80.58210  ? 53  SER D CB  1 
ATOM 5344 O OG  . SER D 1 53  ? 43.33468  -22.89586 13.62930  1.000 74.99543  ? 53  SER D OG  1 
ATOM 5345 N N   . GLN D 1 54  ? 44.19193  -19.88619 13.17255  1.000 79.39825  ? 54  GLN D N   1 
ATOM 5346 C CA  . GLN D 1 54  ? 43.91265  -18.96806 12.08634  1.000 78.03975  ? 54  GLN D CA  1 
ATOM 5347 C C   . GLN D 1 54  ? 44.81273  -17.73897 12.09380  1.000 85.16209  ? 54  GLN D C   1 
ATOM 5348 O O   . GLN D 1 54  ? 44.68786  -16.90232 11.19267  1.000 83.23835  ? 54  GLN D O   1 
ATOM 5349 C CB  . GLN D 1 54  ? 42.46605  -18.50648 12.14783  1.000 68.70531  ? 54  GLN D CB  1 
ATOM 5350 C CG  . GLN D 1 54  ? 41.45764  -19.59508 12.30134  1.000 68.23457  ? 54  GLN D CG  1 
ATOM 5351 C CD  . GLN D 1 54  ? 40.05489  -19.03709 12.29335  1.000 68.82339  ? 54  GLN D CD  1 
ATOM 5352 O OE1 . GLN D 1 54  ? 39.84591  -17.91038 11.87318  1.000 69.34599  ? 54  GLN D OE1 1 
ATOM 5353 N NE2 . GLN D 1 54  ? 39.10926  -19.76808 12.86719  1.000 69.33566  ? 54  GLN D NE2 1 
ATOM 5354 N N   . LYS D 1 55  ? 45.67811  -17.57747 13.09455  1.000 99.57177  ? 55  LYS D N   1 
ATOM 5355 C CA  . LYS D 1 55  ? 46.60410  -16.45007 13.08983  1.000 100.32967 ? 55  LYS D CA  1 
ATOM 5356 C C   . LYS D 1 55  ? 47.50073  -16.50010 11.85651  1.000 102.00103 ? 55  LYS D C   1 
ATOM 5357 O O   . LYS D 1 55  ? 48.00749  -17.56224 11.47760  1.000 102.90217 ? 55  LYS D O   1 
ATOM 5358 C CB  . LYS D 1 55  ? 47.45442  -16.44093 14.36039  1.000 100.51274 ? 55  LYS D CB  1 
ATOM 5359 C CG  . LYS D 1 55  ? 46.71314  -16.03977 15.61912  1.000 100.17811 ? 55  LYS D CG  1 
ATOM 5360 C CD  . LYS D 1 55  ? 47.63609  -16.09541 16.83653  1.000 104.55232 ? 55  LYS D CD  1 
ATOM 5361 C CE  . LYS D 1 55  ? 46.96373  -15.52557 18.07285  1.000 103.07576 ? 55  LYS D CE  1 
ATOM 5362 N NZ  . LYS D 1 55  ? 45.78509  -16.32747 18.47829  1.000 99.86509  ? 55  LYS D NZ  1 
ATOM 5363 N N   . GLY D 1 56  ? 47.68664  -15.33681 11.22732  1.000 90.35659  ? 56  GLY D N   1 
ATOM 5364 C CA  . GLY D 1 56  ? 48.43403  -15.22765 9.98601   1.000 90.28690  ? 56  GLY D CA  1 
ATOM 5365 C C   . GLY D 1 56  ? 47.58836  -15.50796 8.75444   1.000 88.12370  ? 56  GLY D C   1 
ATOM 5366 O O   . GLY D 1 56  ? 47.66783  -14.79756 7.74857   1.000 88.40448  ? 56  GLY D O   1 
ATOM 5367 N N   . HIS D 1 57  ? 46.74755  -16.53600 8.84463   1.000 86.07997  ? 57  HIS D N   1 
ATOM 5368 C CA  . HIS D 1 57  ? 45.93954  -16.97593 7.71898   1.000 79.81328  ? 57  HIS D CA  1 
ATOM 5369 C C   . HIS D 1 57  ? 44.68672  -16.12387 7.53168   1.000 76.55607  ? 57  HIS D C   1 
ATOM 5370 O O   . HIS D 1 57  ? 44.31335  -15.82669 6.39337   1.000 75.62272  ? 57  HIS D O   1 
ATOM 5371 C CB  . HIS D 1 57  ? 45.56538  -18.43970 7.92395   1.000 85.85112  ? 57  HIS D CB  1 
ATOM 5372 C CG  . HIS D 1 57  ? 46.74981  -19.33240 8.12574   1.000 93.87482  ? 57  HIS D CG  1 
ATOM 5373 N ND1 . HIS D 1 57  ? 47.26949  -19.60424 9.37549   1.000 94.03214  ? 57  HIS D ND1 1 
ATOM 5374 C CD2 . HIS D 1 57  ? 47.53082  -19.99441 7.23767   1.000 96.27699  ? 57  HIS D CD2 1 
ATOM 5375 C CE1 . HIS D 1 57  ? 48.31203  -20.40668 9.24809   1.000 100.60089 ? 57  HIS D CE1 1 
ATOM 5376 N NE2 . HIS D 1 57  ? 48.49087  -20.65902 7.96213   1.000 102.36400 ? 57  HIS D NE2 1 
ATOM 5377 N N   . ARG D 1 58  ? 44.01133  -15.73431 8.62229   1.000 77.67038  ? 58  ARG D N   1 
ATOM 5378 C CA  . ARG D 1 58  ? 42.75040  -14.99635 8.54110   1.000 68.81974  ? 58  ARG D CA  1 
ATOM 5379 C C   . ARG D 1 58  ? 42.80477  -13.72711 9.38841   1.000 64.03397  ? 58  ARG D C   1 
ATOM 5380 O O   . ARG D 1 58  ? 43.63970  -13.58025 10.28002  1.000 67.61795  ? 58  ARG D O   1 
ATOM 5381 C CB  . ARG D 1 58  ? 41.56245  -15.87858 8.93201   1.000 61.29203  ? 58  ARG D CB  1 
ATOM 5382 C CG  . ARG D 1 58  ? 41.44399  -17.02728 7.97002   1.000 60.21140  ? 58  ARG D CG  1 
ATOM 5383 C CD  . ARG D 1 58  ? 40.25394  -17.89057 8.17000   1.000 55.76926  ? 58  ARG D CD  1 
ATOM 5384 N NE  . ARG D 1 58  ? 39.03835  -17.13394 7.93197   1.000 58.39508  ? 58  ARG D NE  1 
ATOM 5385 C CZ  . ARG D 1 58  ? 38.52421  -16.88376 6.73727   1.000 58.82888  ? 58  ARG D CZ  1 
ATOM 5386 N NH1 . ARG D 1 58  ? 39.13393  -17.25629 5.63522   1.000 57.17974  ? 58  ARG D NH1 1 
ATOM 5387 N NH2 . ARG D 1 58  ? 37.37108  -16.22469 6.65011   1.000 61.77729  ? 58  ARG D NH2 1 
ATOM 5388 N N   . LEU D 1 59  ? 41.90049  -12.80348 9.06780   1.000 63.63569  ? 59  LEU D N   1 
ATOM 5389 C CA  . LEU D 1 59  ? 42.00380  -11.37685 9.37996   1.000 61.78149  ? 59  LEU D CA  1 
ATOM 5390 C C   . LEU D 1 59  ? 41.23763  -11.02162 10.64326  1.000 60.19600  ? 59  LEU D C   1 
ATOM 5391 O O   . LEU D 1 59  ? 40.00934  -11.16416 10.67304  1.000 57.41836  ? 59  LEU D O   1 
ATOM 5392 C CB  . LEU D 1 59  ? 41.42553  -10.58708 8.21143   1.000 63.03401  ? 59  LEU D CB  1 
ATOM 5393 C CG  . LEU D 1 59  ? 41.20390  -9.09402  8.36110   1.000 68.51161  ? 59  LEU D CG  1 
ATOM 5394 C CD1 . LEU D 1 59  ? 42.53370  -8.35635  8.32076   1.000 71.99893  ? 59  LEU D CD1 1 
ATOM 5395 C CD2 . LEU D 1 59  ? 40.18837  -8.58227  7.32375   1.000 65.58500  ? 59  LEU D CD2 1 
ATOM 5396 N N   . PHE D 1 60  ? 41.94595  -10.50502 11.66432  1.000 66.90105  ? 60  PHE D N   1 
ATOM 5397 C CA  . PHE D 1 60  ? 41.30367  -10.07615 12.92799  1.000 66.62193  ? 60  PHE D CA  1 
ATOM 5398 C C   . PHE D 1 60  ? 41.13503  -8.54729  12.89438  1.000 67.59105  ? 60  PHE D C   1 
ATOM 5399 O O   . PHE D 1 60  ? 42.01524  -7.79421  13.31025  1.000 67.42471  ? 60  PHE D O   1 
ATOM 5400 C CB  . PHE D 1 60  ? 42.06748  -10.47275 14.20376  1.000 60.71028  ? 60  PHE D CB  1 
ATOM 5401 C CG  . PHE D 1 60  ? 42.38611  -11.96362 14.36946  1.000 65.17643  ? 60  PHE D CG  1 
ATOM 5402 C CD1 . PHE D 1 60  ? 42.49886  -12.83692 13.30744  1.000 66.50629  ? 60  PHE D CD1 1 
ATOM 5403 C CD2 . PHE D 1 60  ? 42.44002  -12.50767 15.64158  1.000 69.90282  ? 60  PHE D CD2 1 
ATOM 5404 C CE1 . PHE D 1 60  ? 42.78050  -14.19145 13.51281  1.000 67.28804  ? 60  PHE D CE1 1 
ATOM 5405 C CE2 . PHE D 1 60  ? 42.69715  -13.86824 15.83934  1.000 73.58982  ? 60  PHE D CE2 1 
ATOM 5406 C CZ  . PHE D 1 60  ? 42.85930  -14.70204 14.77274  1.000 70.47065  ? 60  PHE D CZ  1 
ATOM 5407 N N   . THR D 1 61  ? 39.98674  -8.08533  12.40394  1.000 74.14289  ? 61  THR D N   1 
ATOM 5408 C CA  . THR D 1 61  ? 39.67263  -6.66081  12.40818  1.000 72.46928  ? 61  THR D CA  1 
ATOM 5409 C C   . THR D 1 61  ? 39.49568  -6.16123  13.83889  1.000 72.68284  ? 61  THR D C   1 
ATOM 5410 O O   . THR D 1 61  ? 38.69976  -6.71811  14.60454  1.000 71.77079  ? 61  THR D O   1 
ATOM 5411 C CB  . THR D 1 61  ? 38.39953  -6.41204  11.58949  1.000 70.39145  ? 61  THR D CB  1 
ATOM 5412 O OG1 . THR D 1 61  ? 38.68129  -6.57120  10.19594  1.000 69.97802  ? 61  THR D OG1 1 
ATOM 5413 C CG2 . THR D 1 61  ? 37.80907  -5.04108  11.85393  1.000 70.88823  ? 61  THR D CG2 1 
ATOM 5414 N N   . LYS D 1 62  ? 40.22754  -5.09833  14.20159  1.000 71.03649  ? 62  LYS D N   1 
ATOM 5415 C CA  . LYS D 1 62  ? 40.17567  -4.62809  15.58477  1.000 70.01039  ? 62  LYS D CA  1 
ATOM 5416 C C   . LYS D 1 62  ? 38.88629  -3.88015  15.89948  1.000 68.04319  ? 62  LYS D C   1 
ATOM 5417 O O   . LYS D 1 62  ? 38.45715  -3.86889  17.05435  1.000 68.00258  ? 62  LYS D O   1 
ATOM 5418 C CB  . LYS D 1 62  ? 41.36643  -3.73836  15.92193  1.000 70.78282  ? 62  LYS D CB  1 
ATOM 5419 C CG  . LYS D 1 62  ? 41.37370  -2.43663  15.20808  1.000 74.76208  ? 62  LYS D CG  1 
ATOM 5420 C CD  . LYS D 1 62  ? 42.48590  -1.55024  15.71887  1.000 79.03813  ? 62  LYS D CD  1 
ATOM 5421 C CE  . LYS D 1 62  ? 42.08555  -0.90058  17.02619  1.000 87.10574  ? 62  LYS D CE  1 
ATOM 5422 N NZ  . LYS D 1 62  ? 40.93711  0.04509   16.82373  1.000 87.85890  ? 62  LYS D NZ  1 
ATOM 5423 N N   . SER D 1 63  ? 38.25257  -3.24924  14.91812  1.000 62.89671  ? 63  SER D N   1 
ATOM 5424 C CA  . SER D 1 63  ? 36.95592  -2.68662  15.24091  1.000 60.30449  ? 63  SER D CA  1 
ATOM 5425 C C   . SER D 1 63  ? 35.90071  -3.76470  15.40023  1.000 60.59798  ? 63  SER D C   1 
ATOM 5426 O O   . SER D 1 63  ? 34.76508  -3.44615  15.75874  1.000 62.53460  ? 63  SER D O   1 
ATOM 5427 C CB  . SER D 1 63  ? 36.49984  -1.69549  14.18350  1.000 64.79450  ? 63  SER D CB  1 
ATOM 5428 O OG  . SER D 1 63  ? 36.02757  -2.37969  13.03903  1.000 73.52661  ? 63  SER D OG  1 
ATOM 5429 N N   . THR D 1 64  ? 36.22799  -5.01644  15.09008  1.000 63.24279  ? 64  THR D N   1 
ATOM 5430 C CA  . THR D 1 64  ? 35.40946  -6.14921  15.50830  1.000 64.01056  ? 64  THR D CA  1 
ATOM 5431 C C   . THR D 1 64  ? 35.83106  -6.66722  16.87857  1.000 60.27054  ? 64  THR D C   1 
ATOM 5432 O O   . THR D 1 64  ? 34.97861  -7.08267  17.66773  1.000 54.96527  ? 64  THR D O   1 
ATOM 5433 C CB  . THR D 1 64  ? 35.48141  -7.26427  14.45375  1.000 58.87562  ? 64  THR D CB  1 
ATOM 5434 O OG1 . THR D 1 64  ? 35.02832  -6.73643  13.20863  1.000 63.81585  ? 64  THR D OG1 1 
ATOM 5435 C CG2 . THR D 1 64  ? 34.57099  -8.43134  14.81088  1.000 57.45009  ? 64  THR D CG2 1 
ATOM 5436 N N   . ILE D 1 65  ? 37.12787  -6.62493  17.17947  1.000 56.71685  ? 65  ILE D N   1 
ATOM 5437 C CA  . ILE D 1 65  ? 37.58004  -6.93733  18.52308  1.000 60.23553  ? 65  ILE D CA  1 
ATOM 5438 C C   . ILE D 1 65  ? 37.00998  -5.94232  19.52734  1.000 62.74735  ? 65  ILE D C   1 
ATOM 5439 O O   . ILE D 1 65  ? 36.59776  -6.32068  20.62452  1.000 61.17139  ? 65  ILE D O   1 
ATOM 5440 C CB  . ILE D 1 65  ? 39.10945  -6.95049  18.57863  1.000 61.04330  ? 65  ILE D CB  1 
ATOM 5441 C CG1 . ILE D 1 65  ? 39.65332  -7.97496  17.61658  1.000 61.52059  ? 65  ILE D CG1 1 
ATOM 5442 C CG2 . ILE D 1 65  ? 39.58014  -7.25462  19.98581  1.000 54.57767  ? 65  ILE D CG2 1 
ATOM 5443 C CD1 . ILE D 1 65  ? 41.14433  -7.94990  17.54326  1.000 58.93093  ? 65  ILE D CD1 1 
ATOM 5444 N N   . GLU D 1 66  ? 37.02419  -4.65046  19.19093  1.000 63.82147  ? 66  GLU D N   1 
ATOM 5445 C CA  . GLU D 1 66  ? 36.40846  -3.65731  20.05793  1.000 56.74416  ? 66  GLU D CA  1 
ATOM 5446 C C   . GLU D 1 66  ? 34.93338  -3.96748  20.26023  1.000 62.56787  ? 66  GLU D C   1 
ATOM 5447 O O   . GLU D 1 66  ? 34.41348  -3.87620  21.38009  1.000 64.02858  ? 66  GLU D O   1 
ATOM 5448 C CB  . GLU D 1 66  ? 36.58914  -2.26192  19.47032  1.000 51.21767  ? 66  GLU D CB  1 
ATOM 5449 N N   . TRP D 1 67  ? 34.24702  -4.36393  19.19307  1.000 58.98596  ? 67  TRP D N   1 
ATOM 5450 C CA  . TRP D 1 67  ? 32.83453  -4.70719  19.30979  1.000 56.85925  ? 67  TRP D CA  1 
ATOM 5451 C C   . TRP D 1 67  ? 32.60392  -5.83251  20.32028  1.000 62.25624  ? 67  TRP D C   1 
ATOM 5452 O O   . TRP D 1 67  ? 31.75868  -5.71149  21.21480  1.000 64.32678  ? 67  TRP D O   1 
ATOM 5453 C CB  . TRP D 1 67  ? 32.31936  -5.11986  17.95700  1.000 52.34710  ? 67  TRP D CB  1 
ATOM 5454 C CG  . TRP D 1 67  ? 30.89061  -5.31424  17.86648  1.000 52.92460  ? 67  TRP D CG  1 
ATOM 5455 C CD1 . TRP D 1 67  ? 29.93982  -4.36158  17.63410  1.000 55.59360  ? 67  TRP D CD1 1 
ATOM 5456 C CD2 . TRP D 1 67  ? 30.19860  -6.55302  18.01317  1.000 56.29518  ? 67  TRP D CD2 1 
ATOM 5457 N NE1 . TRP D 1 67  ? 28.68641  -4.94686  17.58258  1.000 58.13579  ? 67  TRP D NE1 1 
ATOM 5458 C CE2 . TRP D 1 67  ? 28.81936  -6.28769  17.83269  1.000 54.93324  ? 67  TRP D CE2 1 
ATOM 5459 C CE3 . TRP D 1 67  ? 30.61094  -7.86676  18.25876  1.000 56.93117  ? 67  TRP D CE3 1 
ATOM 5460 C CZ2 . TRP D 1 67  ? 27.86012  -7.27924  17.89277  1.000 53.13978  ? 67  TRP D CZ2 1 
ATOM 5461 C CZ3 . TRP D 1 67  ? 29.65376  -8.84915  18.33069  1.000 58.98347  ? 67  TRP D CZ3 1 
ATOM 5462 C CH2 . TRP D 1 67  ? 28.29164  -8.55215  18.14165  1.000 58.25653  ? 67  TRP D CH2 1 
ATOM 5463 N N   . TRP D 1 68  ? 33.32602  -6.95377  20.17744  1.000 61.56470  ? 68  TRP D N   1 
ATOM 5464 C CA  . TRP D 1 68  ? 33.14832  -8.06079  21.11606  1.000 61.44800  ? 68  TRP D CA  1 
ATOM 5465 C C   . TRP D 1 68  ? 33.42657  -7.63452  22.54664  1.000 65.75360  ? 68  TRP D C   1 
ATOM 5466 O O   . TRP D 1 68  ? 32.79856  -8.15135  23.48396  1.000 65.41606  ? 68  TRP D O   1 
ATOM 5467 C CB  . TRP D 1 68  ? 34.04903  -9.25236  20.76255  1.000 61.25841  ? 68  TRP D CB  1 
ATOM 5468 C CG  . TRP D 1 68  ? 33.51178  -10.06601 19.65022  1.000 65.20908  ? 68  TRP D CG  1 
ATOM 5469 C CD1 . TRP D 1 68  ? 33.93013  -10.08587 18.33612  1.000 62.53801  ? 68  TRP D CD1 1 
ATOM 5470 C CD2 . TRP D 1 68  ? 32.40109  -10.95414 19.73261  1.000 66.00735  ? 68  TRP D CD2 1 
ATOM 5471 N NE1 . TRP D 1 68  ? 33.14892  -10.95112 17.61320  1.000 60.51326  ? 68  TRP D NE1 1 
ATOM 5472 C CE2 . TRP D 1 68  ? 32.19985  -11.49278 18.44405  1.000 61.96919  ? 68  TRP D CE2 1 
ATOM 5473 C CE3 . TRP D 1 68  ? 31.55959  -11.35423 20.77533  1.000 61.90360  ? 68  TRP D CE3 1 
ATOM 5474 C CZ2 . TRP D 1 68  ? 31.19079  -12.40152 18.17452  1.000 61.51960  ? 68  TRP D CZ2 1 
ATOM 5475 C CZ3 . TRP D 1 68  ? 30.56378  -12.24410 20.50212  1.000 63.56807  ? 68  TRP D CZ3 1 
ATOM 5476 C CH2 . TRP D 1 68  ? 30.38415  -12.76376 19.20841  1.000 62.29878  ? 68  TRP D CH2 1 
ATOM 5477 N N   . LYS D 1 69  ? 34.36470  -6.70716  22.73944  1.000 63.23456  ? 69  LYS D N   1 
ATOM 5478 C CA  . LYS D 1 69  ? 34.72595  -6.33829  24.09382  1.000 68.77962  ? 69  LYS D CA  1 
ATOM 5479 C C   . LYS D 1 69  ? 33.61469  -5.52877  24.76411  1.000 69.82878  ? 69  LYS D C   1 
ATOM 5480 O O   . LYS D 1 69  ? 33.57588  -5.43686  25.99877  1.000 69.89874  ? 69  LYS D O   1 
ATOM 5481 C CB  . LYS D 1 69  ? 36.06939  -5.59659  24.09204  1.000 68.66534  ? 69  LYS D CB  1 
ATOM 5482 C CG  . LYS D 1 69  ? 36.54966  -5.31642  25.51314  1.000 85.29126  ? 69  LYS D CG  1 
ATOM 5483 C CD  . LYS D 1 69  ? 36.75518  -6.64178  26.27545  1.000 84.94923  ? 69  LYS D CD  1 
ATOM 5484 C CE  . LYS D 1 69  ? 37.06337  -6.41372  27.73054  1.000 81.14296  ? 69  LYS D CE  1 
ATOM 5485 N NZ  . LYS D 1 69  ? 35.81392  -5.88930  28.35520  1.000 79.69712  ? 69  LYS D NZ  1 
ATOM 5486 N N   . ASN D 1 70  ? 32.68663  -4.99039  23.97280  1.000 68.66114  ? 70  ASN D N   1 
ATOM 5487 C CA  . ASN D 1 70  ? 31.49046  -4.32978  24.46986  1.000 70.68030  ? 70  ASN D CA  1 
ATOM 5488 C C   . ASN D 1 70  ? 30.27409  -5.24617  24.41098  1.000 72.21845  ? 70  ASN D C   1 
ATOM 5489 O O   . ASN D 1 70  ? 29.15758  -4.79399  24.12275  1.000 75.21316  ? 70  ASN D O   1 
ATOM 5490 C CB  . ASN D 1 70  ? 31.22041  -3.03714  23.69636  1.000 69.02108  ? 70  ASN D CB  1 
ATOM 5491 C CG  . ASN D 1 70  ? 32.31110  -1.99802  23.90060  1.000 72.37591  ? 70  ASN D CG  1 
ATOM 5492 O OD1 . ASN D 1 70  ? 32.90030  -1.87533  24.98850  1.000 71.09453  ? 70  ASN D OD1 1 
ATOM 5493 N ND2 . ASN D 1 70  ? 32.57712  -1.22845  22.85520  1.000 77.15973  ? 70  ASN D ND2 1 
ATOM 5494 N N   . GLN D 1 71  ? 30.46862  -6.53101  24.66841  1.000 69.38875  ? 71  GLN D N   1 
ATOM 5495 C CA  . GLN D 1 71  ? 29.37946  -7.48588  24.69580  1.000 69.38801  ? 71  GLN D CA  1 
ATOM 5496 C C   . GLN D 1 71  ? 29.29182  -8.09285  26.08254  1.000 67.72629  ? 71  GLN D C   1 
ATOM 5497 O O   . GLN D 1 71  ? 30.26861  -8.10828  26.83440  1.000 65.41882  ? 71  GLN D O   1 
ATOM 5498 C CB  . GLN D 1 71  ? 29.57227  -8.60841  23.66908  1.000 69.18736  ? 71  GLN D CB  1 
ATOM 5499 C CG  . GLN D 1 71  ? 29.60868  -8.16312  22.24347  1.000 66.19922  ? 71  GLN D CG  1 
ATOM 5500 C CD  . GLN D 1 71  ? 28.35899  -7.41955  21.81944  1.000 66.59708  ? 71  GLN D CD  1 
ATOM 5501 O OE1 . GLN D 1 71  ? 28.41720  -6.22828  21.48190  1.000 64.12724  ? 71  GLN D OE1 1 
ATOM 5502 N NE2 . GLN D 1 71  ? 27.21922  -8.11432  21.83195  1.000 65.67726  ? 71  GLN D NE2 1 
ATOM 5503 N N   . SER D 1 72  ? 28.12611  -8.66260  26.37202  1.000 69.95407  ? 72  SER D N   1 
ATOM 5504 C CA  . SER D 1 72  ? 27.87400  -9.20194  27.68891  1.000 73.20133  ? 72  SER D CA  1 
ATOM 5505 C C   . SER D 1 72  ? 28.89781  -10.28609 27.99730  1.000 74.21463  ? 72  SER D C   1 
ATOM 5506 O O   . SER D 1 72  ? 29.48444  -10.87426 27.08606  1.000 73.80890  ? 72  SER D O   1 
ATOM 5507 C CB  . SER D 1 72  ? 26.46174  -9.77379  27.78748  1.000 77.64901  ? 72  SER D CB  1 
ATOM 5508 O OG  . SER D 1 72  ? 26.32562  -10.98086 27.08179  1.000 78.99165  ? 72  SER D OG  1 
ATOM 5509 N N   . PRO D 1 73  ? 29.17046  -10.52877 29.27654  1.000 74.21879  ? 73  PRO D N   1 
ATOM 5510 C CA  . PRO D 1 73  ? 30.10631  -11.60510 29.62411  1.000 74.96409  ? 73  PRO D CA  1 
ATOM 5511 C C   . PRO D 1 73  ? 29.73008  -12.94731 29.02334  1.000 76.48515  ? 73  PRO D C   1 
ATOM 5512 O O   . PRO D 1 73  ? 30.62696  -13.70403 28.63823  1.000 78.38166  ? 73  PRO D O   1 
ATOM 5513 C CB  . PRO D 1 73  ? 30.04302  -11.63071 31.15794  1.000 71.85665  ? 73  PRO D CB  1 
ATOM 5514 C CG  . PRO D 1 73  ? 29.67111  -10.24658 31.52947  1.000 66.98947  ? 73  PRO D CG  1 
ATOM 5515 C CD  . PRO D 1 73  ? 28.73534  -9.76752  30.45741  1.000 67.61547  ? 73  PRO D CD  1 
ATOM 5516 N N   . GLU D 1 74  ? 28.43550  -13.26863 28.92641  1.000 80.57615  ? 74  GLU D N   1 
ATOM 5517 C CA  . GLU D 1 74  ? 28.04226  -14.56015 28.37270  1.000 80.93551  ? 74  GLU D CA  1 
ATOM 5518 C C   . GLU D 1 74  ? 28.46970  -14.68154 26.91737  1.000 80.58738  ? 74  GLU D C   1 
ATOM 5519 O O   . GLU D 1 74  ? 29.01678  -15.71385 26.50593  1.000 81.25839  ? 74  GLU D O   1 
ATOM 5520 C CB  . GLU D 1 74  ? 26.53115  -14.76255 28.51355  1.000 83.53340  ? 74  GLU D CB  1 
ATOM 5521 N N   . ALA D 1 75  ? 28.25092  -13.62934 26.12885  1.000 81.26290  ? 75  ALA D N   1 
ATOM 5522 C CA  . ALA D 1 75  ? 28.64988  -13.66022 24.72578  1.000 83.62986  ? 75  ALA D CA  1 
ATOM 5523 C C   . ALA D 1 75  ? 30.16530  -13.80348 24.57763  1.000 79.85452  ? 75  ALA D C   1 
ATOM 5524 O O   . ALA D 1 75  ? 30.64277  -14.58354 23.74344  1.000 74.89302  ? 75  ALA D O   1 
ATOM 5525 C CB  . ALA D 1 75  ? 28.14425  -12.40272 24.01833  1.000 81.88389  ? 75  ALA D CB  1 
ATOM 5526 N N   . ARG D 1 76  ? 30.93791  -13.06246 25.38602  1.000 77.13038  ? 76  ARG D N   1 
ATOM 5527 C CA  . ARG D 1 76  ? 32.39633  -13.15453 25.34942  1.000 74.71103  ? 76  ARG D CA  1 
ATOM 5528 C C   . ARG D 1 76  ? 32.91542  -14.46348 25.95359  1.000 80.52463  ? 76  ARG D C   1 
ATOM 5529 O O   . ARG D 1 76  ? 34.08229  -14.81390 25.73595  1.000 77.59642  ? 76  ARG D O   1 
ATOM 5530 C CB  . ARG D 1 76  ? 33.02090  -11.94071 26.05884  1.000 62.64270  ? 76  ARG D CB  1 
ATOM 5531 N N   . LYS D 1 77  ? 32.08598  -15.18236 26.72283  1.000 80.94117  ? 77  LYS D N   1 
ATOM 5532 C CA  . LYS D 1 77  ? 32.46392  -16.50209 27.22315  1.000 77.12207  ? 77  LYS D CA  1 
ATOM 5533 C C   . LYS D 1 77  ? 32.26683  -17.57589 26.16075  1.000 78.90324  ? 77  LYS D C   1 
ATOM 5534 O O   . LYS D 1 77  ? 33.06344  -18.51017 26.06980  1.000 78.34221  ? 77  LYS D O   1 
ATOM 5535 C CB  . LYS D 1 77  ? 31.66484  -16.83695 28.47831  1.000 76.68750  ? 77  LYS D CB  1 
ATOM 5536 N N   . ASN D 1 78  ? 31.22299  -17.45000 25.34087  1.000 87.72218  ? 78  ASN D N   1 
ATOM 5537 C CA  . ASN D 1 78  ? 31.04883  -18.29625 24.16655  1.000 88.20284  ? 78  ASN D CA  1 
ATOM 5538 C C   . ASN D 1 78  ? 32.04133  -17.97735 23.04951  1.000 90.51358  ? 78  ASN D C   1 
ATOM 5539 O O   . ASN D 1 78  ? 32.05826  -18.68269 22.03688  1.000 91.59519  ? 78  ASN D O   1 
ATOM 5540 C CB  . ASN D 1 78  ? 29.61860  -18.16129 23.63977  1.000 87.44566  ? 78  ASN D CB  1 
ATOM 5541 N N   . ILE D 1 79  ? 32.84642  -16.92907 23.18216  1.000 83.32390  ? 79  ILE D N   1 
ATOM 5542 C CA  . ILE D 1 79  ? 33.88626  -16.62902 22.20163  1.000 79.41309  ? 79  ILE D CA  1 
ATOM 5543 C C   . ILE D 1 79  ? 35.25114  -17.15365 22.65613  1.000 75.40427  ? 79  ILE D C   1 
ATOM 5544 O O   . ILE D 1 79  ? 36.27593  -16.67051 22.19494  1.000 80.37108  ? 79  ILE D O   1 
ATOM 5545 C CB  . ILE D 1 79  ? 33.94844  -15.12211 21.88069  1.000 69.23205  ? 79  ILE D CB  1 
ATOM 5546 N N   . ALA D 1 80  ? 35.28102  -18.11928 23.55997  1.000 74.08115  ? 80  ALA D N   1 
ATOM 5547 C CA  . ALA D 1 80  ? 36.52721  -18.48921 24.22495  1.000 73.10378  ? 80  ALA D CA  1 
ATOM 5548 C C   . ALA D 1 80  ? 36.97993  -19.88245 23.80801  1.000 75.80246  ? 80  ALA D C   1 
ATOM 5549 O O   . ALA D 1 80  ? 36.14104  -20.71218 23.43962  1.000 78.99129  ? 80  ALA D O   1 
ATOM 5550 C CB  . ALA D 1 80  ? 36.34559  -18.45713 25.74405  1.000 77.67455  ? 80  ALA D CB  1 
ATOM 5551 N N   . PRO D 1 81  ? 38.28723  -20.18376 23.87118  1.000 75.91750  ? 81  PRO D N   1 
ATOM 5552 C CA  . PRO D 1 81  ? 38.76164  -21.48742 23.38979  1.000 73.81730  ? 81  PRO D CA  1 
ATOM 5553 C C   . PRO D 1 81  ? 38.09270  -22.62122 24.13302  1.000 79.25001  ? 81  PRO D C   1 
ATOM 5554 O O   . PRO D 1 81  ? 37.72842  -22.49466 25.30698  1.000 83.14410  ? 81  PRO D O   1 
ATOM 5555 C CB  . PRO D 1 81  ? 40.26924  -21.45567 23.67517  1.000 67.10695  ? 81  PRO D CB  1 
ATOM 5556 C CG  . PRO D 1 81  ? 40.62057  -20.03692 23.67335  1.000 71.97735  ? 81  PRO D CG  1 
ATOM 5557 C CD  . PRO D 1 81  ? 39.41466  -19.32451 24.26636  1.000 76.57837  ? 81  PRO D CD  1 
ATOM 5558 N N   . SER D 1 82  ? 37.89438  -23.72630 23.42199  1.000 79.15458  ? 82  SER D N   1 
ATOM 5559 C CA  . SER D 1 82  ? 37.50016  -24.96816 24.06454  1.000 87.79541  ? 82  SER D CA  1 
ATOM 5560 C C   . SER D 1 82  ? 38.27131  -26.10067 23.40734  1.000 93.13883  ? 82  SER D C   1 
ATOM 5561 O O   . SER D 1 82  ? 39.10853  -25.88592 22.52646  1.000 93.96852  ? 82  SER D O   1 
ATOM 5562 C CB  . SER D 1 82  ? 35.98431  -25.20596 23.99932  1.000 85.93380  ? 82  SER D CB  1 
ATOM 5563 O OG  . SER D 1 82  ? 35.56212  -25.64438 22.72958  1.000 88.26134  ? 82  SER D OG  1 
ATOM 5564 N N   . ASP D 1 83  ? 38.00961  -27.31420 23.86016  1.000 103.95535 ? 83  ASP D N   1 
ATOM 5565 C CA  . ASP D 1 83  ? 38.66576  -28.47135 23.28492  1.000 105.54911 ? 83  ASP D CA  1 
ATOM 5566 C C   . ASP D 1 83  ? 37.91097  -29.04901 22.10038  1.000 107.93157 ? 83  ASP D C   1 
ATOM 5567 O O   . ASP D 1 83  ? 38.45414  -29.91364 21.40448  1.000 111.88152 ? 83  ASP D O   1 
ATOM 5568 C CB  . ASP D 1 83  ? 38.87513  -29.52901 24.36153  1.000 108.43442 ? 83  ASP D CB  1 
ATOM 5569 C CG  . ASP D 1 83  ? 39.95562  -29.13005 25.34101  1.000 116.56660 ? 83  ASP D CG  1 
ATOM 5570 O OD1 . ASP D 1 83  ? 40.89900  -28.42505 24.92189  1.000 117.02849 ? 83  ASP D OD1 1 
ATOM 5571 O OD2 . ASP D 1 83  ? 39.86327  -29.50788 26.52788  1.000 125.54413 ? 83  ASP D OD2 1 
ATOM 5572 N N   . GLU D 1 84  ? 36.69186  -28.58229 21.84375  1.000 97.17851  ? 84  GLU D N   1 
ATOM 5573 C CA  . GLU D 1 84  ? 35.94582  -28.96313 20.65318  1.000 98.89395  ? 84  GLU D CA  1 
ATOM 5574 C C   . GLU D 1 84  ? 36.12369  -27.96612 19.50018  1.000 91.98767  ? 84  GLU D C   1 
ATOM 5575 O O   . GLU D 1 84  ? 35.37916  -28.02203 18.51346  1.000 90.23349  ? 84  GLU D O   1 
ATOM 5576 C CB  . GLU D 1 84  ? 34.46889  -29.14920 21.00389  1.000 99.58196  ? 84  GLU D CB  1 
ATOM 5577 C CG  . GLU D 1 84  ? 33.76834  -27.88578 21.43816  1.000 104.99399 ? 84  GLU D CG  1 
ATOM 5578 C CD  . GLU D 1 84  ? 32.36140  -28.16025 21.92379  1.000 110.64032 ? 84  GLU D CD  1 
ATOM 5579 O OE1 . GLU D 1 84  ? 31.97981  -29.35578 21.94536  1.000 107.24022 ? 84  GLU D OE1 1 
ATOM 5580 O OE2 . GLU D 1 84  ? 31.64809  -27.18756 22.28627  1.000 112.03702 ? 84  GLU D OE2 1 
ATOM 5581 N N   . ASP D 1 85  ? 37.09420  -27.06480 19.60422  1.000 86.82384  ? 85  ASP D N   1 
ATOM 5582 C CA  . ASP D 1 85  ? 37.51002  -26.29128 18.44788  1.000 82.15686  ? 85  ASP D CA  1 
ATOM 5583 C C   . ASP D 1 85  ? 38.09440  -27.22635 17.39820  1.000 81.35374  ? 85  ASP D C   1 
ATOM 5584 O O   . ASP D 1 85  ? 38.60457  -28.30222 17.71902  1.000 85.02627  ? 85  ASP D O   1 
ATOM 5585 C CB  . ASP D 1 85  ? 38.55569  -25.24672 18.84632  1.000 84.43240  ? 85  ASP D CB  1 
ATOM 5586 C CG  . ASP D 1 85  ? 38.02298  -24.20838 19.84521  1.000 80.53777  ? 85  ASP D CG  1 
ATOM 5587 O OD1 . ASP D 1 85  ? 36.79514  -23.95597 19.89306  1.000 75.51330  ? 85  ASP D OD1 1 
ATOM 5588 O OD2 . ASP D 1 85  ? 38.86189  -23.62428 20.56598  1.000 80.56983  ? 85  ASP D OD2 1 
ATOM 5589 N N   . VAL D 1 86  ? 37.98482  -26.82159 16.12346  1.000 83.99457  ? 86  VAL D N   1 
ATOM 5590 C CA  . VAL D 1 86  ? 38.57909  -27.53184 14.98801  1.000 80.72721  ? 86  VAL D CA  1 
ATOM 5591 C C   . VAL D 1 86  ? 39.18278  -26.50959 14.03287  1.000 71.49689  ? 86  VAL D C   1 
ATOM 5592 O O   . VAL D 1 86  ? 38.79578  -25.34150 14.01923  1.000 72.54596  ? 86  VAL D O   1 
ATOM 5593 C CB  . VAL D 1 86  ? 37.55135  -28.38758 14.22081  1.000 80.30571  ? 86  VAL D CB  1 
ATOM 5594 C CG1 . VAL D 1 86  ? 36.83283  -29.34528 15.15140  1.000 81.59712  ? 86  VAL D CG1 1 
ATOM 5595 C CG2 . VAL D 1 86  ? 36.56887  -27.49730 13.48823  1.000 80.53540  ? 86  VAL D CG2 1 
ATOM 5596 N N   . SER D 1 87  ? 40.12806  -26.95657 13.21461  1.000 74.29913  ? 87  SER D N   1 
ATOM 5597 C CA  . SER D 1 87  ? 40.61970  -26.08906 12.14792  1.000 77.28375  ? 87  SER D CA  1 
ATOM 5598 C C   . SER D 1 87  ? 39.49371  -25.70215 11.18992  1.000 75.52060  ? 87  SER D C   1 
ATOM 5599 O O   . SER D 1 87  ? 38.43415  -26.33160 11.13257  1.000 75.59327  ? 87  SER D O   1 
ATOM 5600 C CB  . SER D 1 87  ? 41.74047  -26.75077 11.34199  1.000 78.88288  ? 87  SER D CB  1 
ATOM 5601 O OG  . SER D 1 87  ? 42.97798  -26.78145 12.03406  1.000 79.71565  ? 87  SER D OG  1 
ATOM 5602 N N   . THR D 1 88  ? 39.74447  -24.62812 10.43864  1.000 74.51183  ? 88  THR D N   1 
ATOM 5603 C CA  . THR D 1 88  ? 38.81630  -24.17338 9.40387   1.000 76.77809  ? 88  THR D CA  1 
ATOM 5604 C C   . THR D 1 88  ? 38.59844  -25.21709 8.30718   1.000 78.08261  ? 88  THR D C   1 
ATOM 5605 O O   . THR D 1 88  ? 37.50529  -25.28156 7.72780   1.000 73.60637  ? 88  THR D O   1 
ATOM 5606 C CB  . THR D 1 88  ? 39.33585  -22.86620 8.81938   1.000 69.75854  ? 88  THR D CB  1 
ATOM 5607 O OG1 . THR D 1 88  ? 40.73262  -23.00726 8.56759   1.000 72.01638  ? 88  THR D OG1 1 
ATOM 5608 C CG2 . THR D 1 88  ? 39.13811  -21.74065 9.78392   1.000 67.81064  ? 88  THR D CG2 1 
ATOM 5609 N N   . ILE D 1 89  ? 39.62010  -26.03316 8.01064   1.000 81.09913  ? 89  ILE D N   1 
ATOM 5610 C CA  . ILE D 1 89  ? 39.43955  -27.21818 7.16237   1.000 81.82803  ? 89  ILE D CA  1 
ATOM 5611 C C   . ILE D 1 89  ? 38.45701  -28.19480 7.79182   1.000 82.22140  ? 89  ILE D C   1 
ATOM 5612 O O   . ILE D 1 89  ? 37.46295  -28.59309 7.16588   1.000 80.60349  ? 89  ILE D O   1 
ATOM 5613 C CB  . ILE D 1 89  ? 40.78089  -27.92311 6.90389   1.000 81.77268  ? 89  ILE D CB  1 
ATOM 5614 C CG1 . ILE D 1 89  ? 41.65733  -27.14240 5.92059   1.000 86.22304  ? 89  ILE D CG1 1 
ATOM 5615 C CG2 . ILE D 1 89  ? 40.51739  -29.32813 6.42667   1.000 82.14009  ? 89  ILE D CG2 1 
ATOM 5616 C CD1 . ILE D 1 89  ? 43.08059  -27.67400 5.82461   1.000 86.03703  ? 89  ILE D CD1 1 
ATOM 5617 N N   . ASP D 1 90  ? 38.76256  -28.64490 9.02012   1.000 78.08894  ? 90  ASP D N   1 
ATOM 5618 C CA  . ASP D 1 90  ? 37.88242  -29.59291 9.69508   1.000 79.53474  ? 90  ASP D CA  1 
ATOM 5619 C C   . ASP D 1 90  ? 36.47176  -29.04714 9.76659   1.000 82.63402  ? 90  ASP D C   1 
ATOM 5620 O O   . ASP D 1 90  ? 35.50210  -29.76229 9.49623   1.000 84.28565  ? 90  ASP D O   1 
ATOM 5621 C CB  . ASP D 1 90  ? 38.36230  -29.90130 11.12067  1.000 83.13483  ? 90  ASP D CB  1 
ATOM 5622 C CG  . ASP D 1 90  ? 39.64408  -30.74194 11.17344  1.000 88.25887  ? 90  ASP D CG  1 
ATOM 5623 O OD1 . ASP D 1 90  ? 40.00565  -31.39841 10.15900  1.000 88.75578  ? 90  ASP D OD1 1 
ATOM 5624 O OD2 . ASP D 1 90  ? 40.25115  -30.79343 12.27640  1.000 83.74489  ? 90  ASP D OD2 1 
ATOM 5625 N N   . GLY D 1 91  ? 36.34347  -27.77222 10.13323  1.000 84.13911  ? 91  GLY D N   1 
ATOM 5626 C CA  . GLY D 1 91  ? 35.02688  -27.18370 10.28830  1.000 83.94444  ? 91  GLY D CA  1 
ATOM 5627 C C   . GLY D 1 91  ? 34.23328  -27.15857 8.99797   1.000 84.59980  ? 91  GLY D C   1 
ATOM 5628 O O   . GLY D 1 91  ? 33.03976  -27.47674 8.98936   1.000 85.59958  ? 91  GLY D O   1 
ATOM 5629 N N   . ILE D 1 92  ? 34.87801  -26.76050 7.89118   1.000 83.00495  ? 92  ILE D N   1 
ATOM 5630 C CA  . ILE D 1 92  ? 34.16977  -26.73474 6.61306   1.000 83.99849  ? 92  ILE D CA  1 
ATOM 5631 C C   . ILE D 1 92  ? 33.87269  -28.15547 6.14103   1.000 87.76410  ? 92  ILE D C   1 
ATOM 5632 O O   . ILE D 1 92  ? 32.80269  -28.41987 5.58037   1.000 90.11825  ? 92  ILE D O   1 
ATOM 5633 C CB  . ILE D 1 92  ? 34.95043  -25.93257 5.55921   1.000 83.38819  ? 92  ILE D CB  1 
ATOM 5634 C CG1 . ILE D 1 92  ? 34.00196  -25.45369 4.46260   1.000 79.85909  ? 92  ILE D CG1 1 
ATOM 5635 C CG2 . ILE D 1 92  ? 36.04092  -26.78306 4.91503   1.000 85.30567  ? 92  ILE D CG2 1 
ATOM 5636 C CD1 . ILE D 1 92  ? 33.03790  -24.39764 4.91603   1.000 77.02947  ? 92  ILE D CD1 1 
ATOM 5637 N N   . ALA D 1 93  ? 34.79642  -29.09742 6.37848   1.000 87.04716  ? 93  ALA D N   1 
ATOM 5638 C CA  . ALA D 1 93  ? 34.50312  -30.50357 6.11017   1.000 88.75785  ? 93  ALA D CA  1 
ATOM 5639 C C   . ALA D 1 93  ? 33.29106  -30.97531 6.91229   1.000 94.12055  ? 93  ALA D C   1 
ATOM 5640 O O   . ALA D 1 93  ? 32.37595  -31.59691 6.36443   1.000 98.45146  ? 93  ALA D O   1 
ATOM 5641 C CB  . ALA D 1 93  ? 35.72808  -31.36260 6.41944   1.000 81.57676  ? 93  ALA D CB  1 
ATOM 5642 N N   . LYS D 1 94  ? 33.25859  -30.66741 8.21399   1.000 90.04441  ? 94  LYS D N   1 
ATOM 5643 C CA  . LYS D 1 94  ? 32.06576  -30.92576 9.01670   1.000 91.80367  ? 94  LYS D CA  1 
ATOM 5644 C C   . LYS D 1 94  ? 30.82980  -30.22488 8.45411   1.000 96.26963  ? 94  LYS D C   1 
ATOM 5645 O O   . LYS D 1 94  ? 29.71217  -30.73309 8.60509   1.000 97.92923  ? 94  LYS D O   1 
ATOM 5646 C CB  . LYS D 1 94  ? 32.28629  -30.48018 10.46993  1.000 91.26703  ? 94  LYS D CB  1 
ATOM 5647 C CG  . LYS D 1 94  ? 33.16042  -31.38616 11.34789  1.000 95.90747  ? 94  LYS D CG  1 
ATOM 5648 C CD  . LYS D 1 94  ? 33.19529  -30.87000 12.80815  1.000 95.80577  ? 94  LYS D CD  1 
ATOM 5649 C CE  . LYS D 1 94  ? 33.91122  -31.82542 13.77302  1.000 93.94782  ? 94  LYS D CE  1 
ATOM 5650 N NZ  . LYS D 1 94  ? 33.11016  -33.05930 14.03451  1.000 87.48020  ? 94  LYS D NZ  1 
ATOM 5651 N N   . PHE D 1 95  ? 30.99970  -29.04179 7.84160   1.000 98.07885  ? 95  PHE D N   1 
ATOM 5652 C CA  . PHE D 1 95  ? 29.86104  -28.33624 7.24945   1.000 97.10550  ? 95  PHE D CA  1 
ATOM 5653 C C   . PHE D 1 95  ? 29.26407  -29.11379 6.08474   1.000 101.19584 ? 95  PHE D C   1 
ATOM 5654 O O   . PHE D 1 95  ? 28.03787  -29.14177 5.91335   1.000 102.33037 ? 95  PHE D O   1 
ATOM 5655 C CB  . PHE D 1 95  ? 30.25940  -26.93311 6.77809   1.000 89.78877  ? 95  PHE D CB  1 
ATOM 5656 C CG  . PHE D 1 95  ? 29.19361  -26.26245 5.95630   1.000 85.49425  ? 95  PHE D CG  1 
ATOM 5657 C CD1 . PHE D 1 95  ? 28.05740  -25.75395 6.55094   1.000 83.37196  ? 95  PHE D CD1 1 
ATOM 5658 C CD2 . PHE D 1 95  ? 29.31131  -26.18633 4.57606   1.000 88.12868  ? 95  PHE D CD2 1 
ATOM 5659 C CE1 . PHE D 1 95  ? 27.06712  -25.16615 5.78895   1.000 84.22993  ? 95  PHE D CE1 1 
ATOM 5660 C CE2 . PHE D 1 95  ? 28.32499  -25.60132 3.81082   1.000 84.12388  ? 95  PHE D CE2 1 
ATOM 5661 C CZ  . PHE D 1 95  ? 27.19962  -25.09561 4.41726   1.000 85.35469  ? 95  PHE D CZ  1 
ATOM 5662 N N   . ASN D 1 96  ? 30.11333  -29.71506 5.24808   1.000 99.06732  ? 96  ASN D N   1 
ATOM 5663 C CA  . ASN D 1 96  ? 29.59073  -30.48758 4.12954   1.000 104.26147 ? 96  ASN D CA  1 
ATOM 5664 C C   . ASN D 1 96  ? 28.94833  -31.78615 4.60934   1.000 109.22900 ? 96  ASN D C   1 
ATOM 5665 O O   . ASN D 1 96  ? 27.85504  -32.14441 4.15535   1.000 111.95428 ? 96  ASN D O   1 
ATOM 5666 C CB  . ASN D 1 96  ? 30.69583  -30.75902 3.10659   1.000 103.61667 ? 96  ASN D CB  1 
ATOM 5667 C CG  . ASN D 1 96  ? 31.25529  -29.47166 2.48361   1.000 104.86895 ? 96  ASN D CG  1 
ATOM 5668 O OD1 . ASN D 1 96  ? 32.47288  -29.24043 2.46182   1.000 97.92833  ? 96  ASN D OD1 1 
ATOM 5669 N ND2 . ASN D 1 96  ? 30.35579  -28.60743 2.01723   1.000 104.20138 ? 96  ASN D ND2 1 
ATOM 5670 N N   . ASP D 1 97  ? 29.59264  -32.48665 5.55409   1.000 109.25706 ? 97  ASP D N   1 
ATOM 5671 C CA  . ASP D 1 97  ? 29.05502  -33.76284 6.02229   1.000 110.46558 ? 97  ASP D CA  1 
ATOM 5672 C C   . ASP D 1 97  ? 27.69183  -33.58516 6.66554   1.000 108.74068 ? 97  ASP D C   1 
ATOM 5673 O O   . ASP D 1 97  ? 26.89669  -34.52680 6.71575   1.000 112.35488 ? 97  ASP D O   1 
ATOM 5674 C CB  . ASP D 1 97  ? 30.02279  -34.44843 6.99589   1.000 107.46744 ? 97  ASP D CB  1 
ATOM 5675 C CG  . ASP D 1 97  ? 31.30992  -34.93312 6.30787   1.000 110.03535 ? 97  ASP D CG  1 
ATOM 5676 O OD1 . ASP D 1 97  ? 31.33020  -35.04154 5.05987   1.000 106.76639 ? 97  ASP D OD1 1 
ATOM 5677 O OD2 . ASP D 1 97  ? 32.28652  -35.25990 7.01937   1.000 107.78313 ? 97  ASP D OD2 1 
ATOM 5678 N N   . TYR D 1 98  ? 27.40995  -32.39625 7.17724   1.000 111.38451 ? 98  TYR D N   1 
ATOM 5679 C CA  . TYR D 1 98  ? 26.04671  -32.07825 7.57630   1.000 116.45496 ? 98  TYR D CA  1 
ATOM 5680 C C   . TYR D 1 98  ? 25.16336  -31.85298 6.35522   1.000 119.27803 ? 98  TYR D C   1 
ATOM 5681 O O   . TYR D 1 98  ? 24.08308  -32.44500 6.23666   1.000 121.46785 ? 98  TYR D O   1 
ATOM 5682 C CB  . TYR D 1 98  ? 26.05473  -30.84513 8.47150   1.000 108.32629 ? 98  TYR D CB  1 
ATOM 5683 C CG  . TYR D 1 98  ? 24.70122  -30.38632 8.92631   1.000 108.15901 ? 98  TYR D CG  1 
ATOM 5684 C CD1 . TYR D 1 98  ? 24.10166  -30.93594 10.03539  1.000 113.11707 ? 98  TYR D CD1 1 
ATOM 5685 C CD2 . TYR D 1 98  ? 24.01443  -29.40651 8.23085   1.000 112.77271 ? 98  TYR D CD2 1 
ATOM 5686 C CE1 . TYR D 1 98  ? 22.85623  -30.50207 10.46530  1.000 117.39637 ? 98  TYR D CE1 1 
ATOM 5687 C CE2 . TYR D 1 98  ? 22.77232  -28.96869 8.64329   1.000 113.13075 ? 98  TYR D CE2 1 
ATOM 5688 C CZ  . TYR D 1 98  ? 22.19347  -29.52148 9.76058   1.000 116.43269 ? 98  TYR D CZ  1 
ATOM 5689 O OH  . TYR D 1 98  ? 20.95303  -29.08808 10.18248  1.000 118.14489 ? 98  TYR D OH  1 
ATOM 5690 N N   . ILE D 1 99  ? 25.62675  -31.01797 5.41948   1.000 121.54154 ? 99  ILE D N   1 
ATOM 5691 C CA  . ILE D 1 99  ? 24.75573  -30.54037 4.34878   1.000 123.76659 ? 99  ILE D CA  1 
ATOM 5692 C C   . ILE D 1 99  ? 24.46936  -31.65326 3.33858   1.000 126.69167 ? 99  ILE D C   1 
ATOM 5693 O O   . ILE D 1 99  ? 23.39362  -31.67602 2.72494   1.000 129.91658 ? 99  ILE D O   1 
ATOM 5694 C CB  . ILE D 1 99  ? 25.35859  -29.28237 3.68502   1.000 116.54653 ? 99  ILE D CB  1 
ATOM 5695 C CG1 . ILE D 1 99  ? 24.26090  -28.45593 3.02416   1.000 117.11662 ? 99  ILE D CG1 1 
ATOM 5696 C CG2 . ILE D 1 99  ? 26.42713  -29.63439 2.66778   1.000 115.38655 ? 99  ILE D CG2 1 
ATOM 5697 C CD1 . ILE D 1 99  ? 23.36440  -27.79076 4.03414   1.000 117.23748 ? 99  ILE D CD1 1 
ATOM 5698 N N   . ASN D 1 100 ? 25.41015  -32.58781 3.14439   1.000 125.03778 ? 100 ASN D N   1 
ATOM 5699 C CA  . ASN D 1 100 ? 25.11299  -33.78762 2.36267   1.000 125.63610 ? 100 ASN D CA  1 
ATOM 5700 C C   . ASN D 1 100 ? 24.04009  -34.62510 3.04417   1.000 128.00376 ? 100 ASN D C   1 
ATOM 5701 O O   . ASN D 1 100 ? 23.07364  -35.06276 2.40809   1.000 130.22871 ? 100 ASN D O   1 
ATOM 5702 C CB  . ASN D 1 100 ? 26.37551  -34.63192 2.16625   1.000 124.32505 ? 100 ASN D CB  1 
ATOM 5703 C CG  . ASN D 1 100 ? 27.32785  -34.03766 1.16453   1.000 123.79694 ? 100 ASN D CG  1 
ATOM 5704 O OD1 . ASN D 1 100 ? 26.91761  -33.55461 0.10865   1.000 125.24274 ? 100 ASN D OD1 1 
ATOM 5705 N ND2 . ASN D 1 100 ? 28.61449  -34.07950 1.48251   1.000 119.17771 ? 100 ASN D ND2 1 
ATOM 5706 N N   . ALA D 1 101 ? 24.18975  -34.83956 4.35267   1.000 129.33705 ? 101 ALA D N   1 
ATOM 5707 C CA  . ALA D 1 101 ? 23.35899  -35.75125 5.12044   1.000 125.13131 ? 101 ALA D CA  1 
ATOM 5708 C C   . ALA D 1 101 ? 22.06814  -35.12201 5.58399   1.000 126.10087 ? 101 ALA D C   1 
ATOM 5709 O O   . ALA D 1 101 ? 21.49080  -35.60300 6.56164   1.000 127.40798 ? 101 ALA D O   1 
ATOM 5710 C CB  . ALA D 1 101 ? 24.13721  -36.28693 6.32585   1.000 118.51255 ? 101 ALA D CB  1 
ATOM 5711 N N   . HIS D 1 102 ? 21.59841  -34.06012 4.93587   1.000 124.75874 ? 102 HIS D N   1 
ATOM 5712 C CA  . HIS D 1 102 ? 20.31732  -33.47679 5.30796   1.000 132.38625 ? 102 HIS D CA  1 
ATOM 5713 C C   . HIS D 1 102 ? 19.52006  -33.06356 4.07875   1.000 141.39137 ? 102 HIS D C   1 
ATOM 5714 O O   . HIS D 1 102 ? 18.86191  -32.01666 4.06689   1.000 141.06104 ? 102 HIS D O   1 
ATOM 5715 C CB  . HIS D 1 102 ? 20.50723  -32.32194 6.29006   1.000 131.02287 ? 102 HIS D CB  1 
ATOM 5716 C CG  . HIS D 1 102 ? 20.80238  -32.78131 7.68807   1.000 129.96330 ? 102 HIS D CG  1 
ATOM 5717 N ND1 . HIS D 1 102 ? 22.07669  -33.07085 8.12924   1.000 128.52461 ? 102 HIS D ND1 1 
ATOM 5718 C CD2 . HIS D 1 102 ? 19.97846  -33.03369 8.73341   1.000 127.59171 ? 102 HIS D CD2 1 
ATOM 5719 C CE1 . HIS D 1 102 ? 22.02593  -33.47033 9.38799   1.000 125.47663 ? 102 HIS D CE1 1 
ATOM 5720 N NE2 . HIS D 1 102 ? 20.76453  -33.45376 9.77943   1.000 128.40572 ? 102 HIS D NE2 1 
ATOM 5721 N N   . ASN D 1 103 ? 19.57433  -33.89463 3.03419   1.000 161.25015 ? 103 ASN D N   1 
ATOM 5722 C CA  . ASN D 1 103 ? 18.62925  -33.89273 1.91167   1.000 161.99894 ? 103 ASN D CA  1 
ATOM 5723 C C   . ASN D 1 103 ? 18.46092  -32.48968 1.31833   1.000 161.61791 ? 103 ASN D C   1 
ATOM 5724 O O   . ASN D 1 103 ? 17.40772  -31.85981 1.39696   1.000 161.92393 ? 103 ASN D O   1 
ATOM 5725 C CB  . ASN D 1 103 ? 17.28141  -34.48713 2.34080   1.000 158.68785 ? 103 ASN D CB  1 
ATOM 5726 N N   . ILE D 1 104 ? 19.55161  -32.00300 0.73914   1.000 141.16278 ? 104 ILE D N   1 
ATOM 5727 C CA  . ILE D 1 104 ? 19.57045  -30.70415 0.07954   1.000 135.66669 ? 104 ILE D CA  1 
ATOM 5728 C C   . ILE D 1 104 ? 20.18671  -30.87280 -1.30388  1.000 132.83161 ? 104 ILE D C   1 
ATOM 5729 O O   . ILE D 1 104 ? 21.34508  -31.29289 -1.42888  1.000 131.28852 ? 104 ILE D O   1 
ATOM 5730 C CB  . ILE D 1 104 ? 20.32119  -29.65117 0.91594   1.000 134.79174 ? 104 ILE D CB  1 
ATOM 5731 C CG1 . ILE D 1 104 ? 19.42247  -29.15730 2.05586   1.000 133.86752 ? 104 ILE D CG1 1 
ATOM 5732 C CG2 . ILE D 1 104 ? 20.87143  -28.51980 0.05398   1.000 128.73320 ? 104 ILE D CG2 1 
ATOM 5733 C CD1 . ILE D 1 104 ? 20.10590  -28.24839 3.01824   1.000 125.36746 ? 104 ILE D CD1 1 
ATOM 5734 N N   . ASP D 1 105 ? 19.39673  -30.56288 -2.35142  1.000 127.68868 ? 105 ASP D N   1 
ATOM 5735 C CA  . ASP D 1 105 ? 19.86421  -30.69278 -3.72437  1.000 121.60211 ? 105 ASP D CA  1 
ATOM 5736 C C   . ASP D 1 105 ? 20.82711  -29.55844 -4.05380  1.000 121.13578 ? 105 ASP D C   1 
ATOM 5737 O O   . ASP D 1 105 ? 20.53895  -28.39623 -3.75692  1.000 119.57760 ? 105 ASP D O   1 
ATOM 5738 C CB  . ASP D 1 105 ? 18.69912  -30.66004 -4.70958  1.000 121.78794 ? 105 ASP D CB  1 
ATOM 5739 C CG  . ASP D 1 105 ? 19.13476  -30.98427 -6.13396  1.000 123.70200 ? 105 ASP D CG  1 
ATOM 5740 O OD1 . ASP D 1 105 ? 19.33228  -32.18781 -6.42240  1.000 127.36182 ? 105 ASP D OD1 1 
ATOM 5741 O OD2 . ASP D 1 105 ? 19.30743  -30.04547 -6.95346  1.000 120.03095 ? 105 ASP D OD2 1 
ATOM 5742 N N   . PRO D 1 106 ? 21.95980  -29.86216 -4.68593  1.000 117.09479 ? 106 PRO D N   1 
ATOM 5743 C CA  . PRO D 1 106 ? 22.91855  -28.79202 -5.00276  1.000 111.88901 ? 106 PRO D CA  1 
ATOM 5744 C C   . PRO D 1 106 ? 22.30446  -27.67707 -5.82403  1.000 111.05530 ? 106 PRO D C   1 
ATOM 5745 O O   . PRO D 1 106 ? 22.67239  -26.50715 -5.64691  1.000 104.43095 ? 106 PRO D O   1 
ATOM 5746 C CB  . PRO D 1 106 ? 24.02024  -29.52803 -5.77939  1.000 110.91006 ? 106 PRO D CB  1 
ATOM 5747 C CG  . PRO D 1 106 ? 23.88641  -30.97213 -5.36283  1.000 112.59706 ? 106 PRO D CG  1 
ATOM 5748 C CD  . PRO D 1 106 ? 22.42143  -31.18689 -5.13489  1.000 115.44724 ? 106 PRO D CD  1 
ATOM 5749 N N   . TRP D 1 107 ? 21.36017  -28.00681 -6.70738  1.000 113.55376 ? 107 TRP D N   1 
ATOM 5750 C CA  . TRP D 1 107 ? 20.79749  -27.02349 -7.62540  1.000 113.16944 ? 107 TRP D CA  1 
ATOM 5751 C C   . TRP D 1 107 ? 19.52889  -26.39218 -7.05032  1.000 113.36904 ? 107 TRP D C   1 
ATOM 5752 O O   . TRP D 1 107 ? 19.50115  -25.19233 -6.76017  1.000 113.16652 ? 107 TRP D O   1 
ATOM 5753 C CB  . TRP D 1 107 ? 20.50552  -27.68426 -8.98305  1.000 108.75784 ? 107 TRP D CB  1 
ATOM 5754 C CG  . TRP D 1 107 ? 21.70045  -28.33762 -9.66139  1.000 104.83473 ? 107 TRP D CG  1 
ATOM 5755 C CD1 . TRP D 1 107 ? 22.09801  -29.63652 -9.51550  1.000 108.07691 ? 107 TRP D CD1 1 
ATOM 5756 C CD2 . TRP D 1 107 ? 22.59904  -27.75598 -10.62962 1.000 105.67760 ? 107 TRP D CD2 1 
ATOM 5757 N NE1 . TRP D 1 107 ? 23.19943  -29.89533 -10.29692 1.000 104.73451 ? 107 TRP D NE1 1 
ATOM 5758 C CE2 . TRP D 1 107 ? 23.52807  -28.76200 -10.99478 1.000 106.17928 ? 107 TRP D CE2 1 
ATOM 5759 C CE3 . TRP D 1 107 ? 22.71787  -26.48771 -11.21338 1.000 102.35289 ? 107 TRP D CE3 1 
ATOM 5760 C CZ2 . TRP D 1 107 ? 24.56551  -28.53550 -11.91408 1.000 97.29464  ? 107 TRP D CZ2 1 
ATOM 5761 C CZ3 . TRP D 1 107 ? 23.75491  -26.26644 -12.12529 1.000 99.73516  ? 107 TRP D CZ3 1 
ATOM 5762 C CH2 . TRP D 1 107 ? 24.66083  -27.28763 -12.46189 1.000 96.57230  ? 107 TRP D CH2 1 
ATOM 5763 N N   . LYS D 1 108 ? 18.49413  -27.20017 -6.82206  1.000 116.80456 ? 108 LYS D N   1 
ATOM 5764 C CA  . LYS D 1 108 ? 17.17864  -26.65580 -6.50347  1.000 117.82967 ? 108 LYS D CA  1 
ATOM 5765 C C   . LYS D 1 108 ? 17.08866  -26.04644 -5.10490  1.000 118.43720 ? 108 LYS D C   1 
ATOM 5766 O O   . LYS D 1 108 ? 16.11076  -25.34176 -4.82312  1.000 118.95881 ? 108 LYS D O   1 
ATOM 5767 C CB  . LYS D 1 108 ? 16.10518  -27.74440 -6.65460  1.000 124.83914 ? 108 LYS D CB  1 
ATOM 5768 C CG  . LYS D 1 108 ? 15.82728  -28.25555 -8.08103  1.000 125.87864 ? 108 LYS D CG  1 
ATOM 5769 C CD  . LYS D 1 108 ? 14.66000  -29.26197 -8.03695  1.000 130.01735 ? 108 LYS D CD  1 
ATOM 5770 C CE  . LYS D 1 108 ? 14.29723  -29.85110 -9.39957  1.000 130.68537 ? 108 LYS D CE  1 
ATOM 5771 N NZ  . LYS D 1 108 ? 13.16019  -30.82598 -9.29926  1.000 124.02646 ? 108 LYS D NZ  1 
ATOM 5772 N N   . SER D 1 109 ? 18.05670  -26.29922 -4.22373  1.000 118.17383 ? 109 SER D N   1 
ATOM 5773 C CA  . SER D 1 109 ? 17.95833  -25.83644 -2.84355  1.000 117.85108 ? 109 SER D CA  1 
ATOM 5774 C C   . SER D 1 109 ? 18.40491  -24.38991 -2.70424  1.000 112.76714 ? 109 SER D C   1 
ATOM 5775 O O   . SER D 1 109 ? 19.23691  -23.89817 -3.46942  1.000 109.50888 ? 109 SER D O   1 
ATOM 5776 C CB  . SER D 1 109 ? 18.80801  -26.69676 -1.91328  1.000 120.29291 ? 109 SER D CB  1 
ATOM 5777 O OG  . SER D 1 109 ? 18.35274  -28.03498 -1.85918  1.000 124.22382 ? 109 SER D OG  1 
ATOM 5778 N N   . GLN D 1 110 ? 17.87180  -23.72266 -1.68363  1.000 111.82543 ? 110 GLN D N   1 
ATOM 5779 C CA  . GLN D 1 110 ? 18.22408  -22.34487 -1.37787  1.000 112.82092 ? 110 GLN D CA  1 
ATOM 5780 C C   . GLN D 1 110 ? 18.79147  -22.23122 0.03252   1.000 108.52861 ? 110 GLN D C   1 
ATOM 5781 O O   . GLN D 1 110 ? 18.27847  -22.84577 0.97005   1.000 110.39728 ? 110 GLN D O   1 
ATOM 5782 C CB  . GLN D 1 110 ? 17.01474  -21.41697 -1.52104  1.000 114.66334 ? 110 GLN D CB  1 
ATOM 5783 C CG  . GLN D 1 110 ? 16.49171  -21.28789 -2.94656  1.000 113.57971 ? 110 GLN D CG  1 
ATOM 5784 C CD  . GLN D 1 110 ? 15.42140  -20.21799 -3.06412  1.000 115.70145 ? 110 GLN D CD  1 
ATOM 5785 O OE1 . GLN D 1 110 ? 15.05546  -19.57636 -2.07133  1.000 115.72505 ? 110 GLN D OE1 1 
ATOM 5786 N NE2 . GLN D 1 110 ? 14.90977  -20.02080 -4.27604  1.000 115.12129 ? 110 GLN D NE2 1 
ATOM 5787 N N   . GLY D 1 111 ? 19.84113  -21.42677 0.17463   1.000 106.20056 ? 111 GLY D N   1 
ATOM 5788 C CA  . GLY D 1 111 ? 20.46994  -21.16669 1.45853   1.000 100.55849 ? 111 GLY D CA  1 
ATOM 5789 C C   . GLY D 1 111 ? 20.19754  -19.74885 1.93555   1.000 96.52063  ? 111 GLY D C   1 
ATOM 5790 O O   . GLY D 1 111 ? 20.32916  -18.78778 1.17740   1.000 93.62231  ? 111 GLY D O   1 
ATOM 5791 N N   . TRP D 1 112 ? 19.84041  -19.63826 3.20513   1.000 96.31376  ? 112 TRP D N   1 
ATOM 5792 C CA  . TRP D 1 112 ? 19.43037  -18.37575 3.79395   1.000 94.56092  ? 112 TRP D CA  1 
ATOM 5793 C C   . TRP D 1 112 ? 20.50269  -17.83571 4.72549   1.000 92.95683  ? 112 TRP D C   1 
ATOM 5794 O O   . TRP D 1 112 ? 21.46881  -18.52008 5.07148   1.000 88.97496  ? 112 TRP D O   1 
ATOM 5795 C CB  . TRP D 1 112 ? 18.08214  -18.54274 4.49512   1.000 93.38946  ? 112 TRP D CB  1 
ATOM 5796 C CG  . TRP D 1 112 ? 16.98993  -18.49432 3.49595   1.000 95.67671  ? 112 TRP D CG  1 
ATOM 5797 C CD1 . TRP D 1 112 ? 16.54243  -19.52200 2.70164   1.000 98.56175  ? 112 TRP D CD1 1 
ATOM 5798 C CD2 . TRP D 1 112 ? 16.18605  -17.35494 3.17546   1.000 96.89583  ? 112 TRP D CD2 1 
ATOM 5799 N NE1 . TRP D 1 112 ? 15.51987  -19.07893 1.88932   1.000 100.77964 ? 112 TRP D NE1 1 
ATOM 5800 C CE2 . TRP D 1 112 ? 15.27874  -17.75439 2.16192   1.000 100.44177 ? 112 TRP D CE2 1 
ATOM 5801 C CE3 . TRP D 1 112 ? 16.15343  -16.02908 3.63333   1.000 94.02552  ? 112 TRP D CE3 1 
ATOM 5802 C CZ2 . TRP D 1 112 ? 14.34020  -16.87403 1.60889   1.000 98.43773  ? 112 TRP D CZ2 1 
ATOM 5803 C CZ3 . TRP D 1 112 ? 15.22157  -15.15497 3.08052   1.000 97.50326  ? 112 TRP D CZ3 1 
ATOM 5804 C CH2 . TRP D 1 112 ? 14.32429  -15.58382 2.08258   1.000 97.61903  ? 112 TRP D CH2 1 
ATOM 5805 N N   . CYS D 1 113 ? 20.33543  -16.56117 5.07994   1.000 100.53411 ? 113 CYS D N   1 
ATOM 5806 C CA  . CYS D 1 113 ? 21.41189  -15.78324 5.67289   1.000 98.34296  ? 113 CYS D CA  1 
ATOM 5807 C C   . CYS D 1 113 ? 20.92995  -14.38899 6.07719   1.000 99.93576  ? 113 CYS D C   1 
ATOM 5808 O O   . CYS D 1 113 ? 20.13750  -13.79419 5.34383   1.000 102.47598 ? 113 CYS D O   1 
ATOM 5809 C CB  . CYS D 1 113 ? 22.53568  -15.71767 4.64389   1.000 96.42681  ? 113 CYS D CB  1 
ATOM 5810 S SG  . CYS D 1 113 ? 23.96349  -14.83200 5.11189   1.000 101.66962 ? 113 CYS D SG  1 
ATOM 5811 N N   . ARG D 1 114 ? 21.37629  -13.84259 7.21547   1.000 97.51130  ? 114 ARG D N   1 
ATOM 5812 C CA  . ARG D 1 114 ? 21.17513  -12.42224 7.52479   1.000 98.33178  ? 114 ARG D CA  1 
ATOM 5813 C C   . ARG D 1 114 ? 22.45849  -11.67934 7.19527   1.000 98.39612  ? 114 ARG D C   1 
ATOM 5814 O O   . ARG D 1 114 ? 23.51437  -11.98908 7.75738   1.000 101.40907 ? 114 ARG D O   1 
ATOM 5815 C CB  . ARG D 1 114 ? 20.81074  -12.13762 8.98901   1.000 99.31193  ? 114 ARG D CB  1 
ATOM 5816 C CG  . ARG D 1 114 ? 19.39583  -12.48008 9.45232   1.000 99.01416  ? 114 ARG D CG  1 
ATOM 5817 C CD  . ARG D 1 114 ? 19.09435  -11.94681 10.87973  1.000 99.04369  ? 114 ARG D CD  1 
ATOM 5818 N NE  . ARG D 1 114 ? 18.77671  -10.52083 10.95730  1.000 96.17661  ? 114 ARG D NE  1 
ATOM 5819 C CZ  . ARG D 1 114 ? 17.54368  -10.02527 10.93998  1.000 95.57809  ? 114 ARG D CZ  1 
ATOM 5820 N NH1 . ARG D 1 114 ? 16.48080  -10.81441 10.87163  1.000 95.58192  ? 114 ARG D NH1 1 
ATOM 5821 N NH2 . ARG D 1 114 ? 17.37199  -8.70593  11.00357  1.000 89.92528  ? 114 ARG D NH2 1 
ATOM 5822 N N   . GLY D 1 115 ? 22.36028  -10.67538 6.32644   1.000 99.23677  ? 115 GLY D N   1 
ATOM 5823 C CA  . GLY D 1 115 ? 23.55026  -10.03678 5.79930   1.000 96.75159  ? 115 GLY D CA  1 
ATOM 5824 C C   . GLY D 1 115 ? 24.26923  -10.93709 4.81515   1.000 95.07299  ? 115 GLY D C   1 
ATOM 5825 O O   . GLY D 1 115 ? 25.39632  -11.36699 5.07358   1.000 93.56109  ? 115 GLY D O   1 
ATOM 5826 N N   . MET D 1 116 ? 23.61371  -11.22885 3.68357   1.000 89.42503  ? 116 MET D N   1 
ATOM 5827 C CA  . MET D 1 116 ? 24.16427  -12.10055 2.64972   1.000 83.17302  ? 116 MET D CA  1 
ATOM 5828 C C   . MET D 1 116 ? 25.47153  -11.57383 2.07896   1.000 76.57214  ? 116 MET D C   1 
ATOM 5829 O O   . MET D 1 116 ? 26.23348  -12.34802 1.49196   1.000 74.43431  ? 116 MET D O   1 
ATOM 5830 C CB  . MET D 1 116 ? 23.11977  -12.26477 1.55427   1.000 85.06933  ? 116 MET D CB  1 
ATOM 5831 C CG  . MET D 1 116 ? 23.51859  -13.05833 0.34518   1.000 78.91874  ? 116 MET D CG  1 
ATOM 5832 S SD  . MET D 1 116 ? 22.07623  -13.10774 -0.74473  1.000 90.88563  ? 116 MET D SD  1 
ATOM 5833 C CE  . MET D 1 116 ? 22.82902  -13.58177 -2.29846  1.000 86.41777  ? 116 MET D CE  1 
ATOM 5834 N N   . SER D 1 117 ? 25.73838  -10.27449 2.24770   1.000 74.94715  ? 117 SER D N   1 
ATOM 5835 C CA  . SER D 1 117 ? 27.02774  -9.66521  1.92829   1.000 72.18439  ? 117 SER D CA  1 
ATOM 5836 C C   . SER D 1 117 ? 28.16074  -10.27941 2.72192   1.000 75.55302  ? 117 SER D C   1 
ATOM 5837 O O   . SER D 1 117 ? 29.32648  -10.13185 2.34036   1.000 73.05091  ? 117 SER D O   1 
ATOM 5838 C CB  . SER D 1 117 ? 27.02756  -8.17936  2.29030   1.000 74.49366  ? 117 SER D CB  1 
ATOM 5839 O OG  . SER D 1 117 ? 25.87762  -7.50060  1.83157   1.000 79.83689  ? 117 SER D OG  1 
ATOM 5840 N N   . PHE D 1 118 ? 27.83526  -10.91623 3.84637   1.000 76.77661  ? 118 PHE D N   1 
ATOM 5841 C CA  . PHE D 1 118 ? 28.77085  -11.20510 4.92220   1.000 73.72173  ? 118 PHE D CA  1 
ATOM 5842 C C   . PHE D 1 118 ? 29.05549  -12.69468 5.08122   1.000 71.63877  ? 118 PHE D C   1 
ATOM 5843 O O   . PHE D 1 118 ? 30.22257  -13.10808 5.06661   1.000 68.63474  ? 118 PHE D O   1 
ATOM 5844 C CB  . PHE D 1 118 ? 28.20697  -10.61673 6.23075   1.000 75.06036  ? 118 PHE D CB  1 
ATOM 5845 C CG  . PHE D 1 118 ? 29.06966  -10.88369 7.41524   1.000 73.77286  ? 118 PHE D CG  1 
ATOM 5846 C CD1 . PHE D 1 118 ? 30.19424  -10.10934 7.65636   1.000 73.25771  ? 118 PHE D CD1 1 
ATOM 5847 C CD2 . PHE D 1 118 ? 28.80215  -11.95757 8.24429   1.000 72.51812  ? 118 PHE D CD2 1 
ATOM 5848 C CE1 . PHE D 1 118 ? 31.01957  -10.37487 8.72180   1.000 71.23165  ? 118 PHE D CE1 1 
ATOM 5849 C CE2 . PHE D 1 118 ? 29.61860  -12.22811 9.31330   1.000 74.34928  ? 118 PHE D CE2 1 
ATOM 5850 C CZ  . PHE D 1 118 ? 30.73209  -11.42740 9.55455   1.000 75.45537  ? 118 PHE D CZ  1 
ATOM 5851 N N   . ASP D 1 119 ? 28.01531  -13.52233 5.24212   1.000 73.22916  ? 119 ASP D N   1 
ATOM 5852 C CA  . ASP D 1 119 ? 28.22180  -14.93498 5.54232   1.000 70.72628  ? 119 ASP D CA  1 
ATOM 5853 C C   . ASP D 1 119 ? 28.69323  -15.70334 4.31742   1.000 69.04160  ? 119 ASP D C   1 
ATOM 5854 O O   . ASP D 1 119 ? 29.77077  -16.30228 4.33224   1.000 69.18421  ? 119 ASP D O   1 
ATOM 5855 C CB  . ASP D 1 119 ? 26.94394  -15.55014 6.11497   1.000 79.21060  ? 119 ASP D CB  1 
ATOM 5856 C CG  . ASP D 1 119 ? 26.66596  -15.12233 7.57083   1.000 80.66521  ? 119 ASP D CG  1 
ATOM 5857 O OD1 . ASP D 1 119 ? 27.62992  -15.01151 8.35910   1.000 78.74439  ? 119 ASP D OD1 1 
ATOM 5858 O OD2 . ASP D 1 119 ? 25.48803  -14.87117 7.92344   1.000 84.38398  ? 119 ASP D OD2 1 
ATOM 5859 N N   . PHE D 1 120 ? 27.91366  -15.69610 3.23848   1.000 70.32672  ? 120 PHE D N   1 
ATOM 5860 C CA  . PHE D 1 120 ? 28.32838  -16.45044 2.05600   1.000 66.64511  ? 120 PHE D CA  1 
ATOM 5861 C C   . PHE D 1 120 ? 29.70320  -16.08227 1.51742   1.000 62.59539  ? 120 PHE D C   1 
ATOM 5862 O O   . PHE D 1 120 ? 30.42482  -16.99982 1.09481   1.000 61.90298  ? 120 PHE D O   1 
ATOM 5863 C CB  . PHE D 1 120 ? 27.27213  -16.36051 0.95644   1.000 66.47807  ? 120 PHE D CB  1 
ATOM 5864 C CG  . PHE D 1 120 ? 26.19635  -17.38220 1.09275   1.000 74.36672  ? 120 PHE D CG  1 
ATOM 5865 C CD1 . PHE D 1 120 ? 26.48453  -18.71828 0.86076   1.000 76.69215  ? 120 PHE D CD1 1 
ATOM 5866 C CD2 . PHE D 1 120 ? 24.90232  -17.02803 1.41483   1.000 79.12457  ? 120 PHE D CD2 1 
ATOM 5867 C CE1 . PHE D 1 120 ? 25.51372  -19.68340 0.97997   1.000 79.29408  ? 120 PHE D CE1 1 
ATOM 5868 C CE2 . PHE D 1 120 ? 23.91884  -17.99443 1.51995   1.000 82.69051  ? 120 PHE D CE2 1 
ATOM 5869 C CZ  . PHE D 1 120 ? 24.22920  -19.32171 1.30034   1.000 83.49034  ? 120 PHE D CZ  1 
ATOM 5870 N N   . PRO D 1 121 ? 30.12449  -14.81637 1.47633   1.000 65.15823  ? 121 PRO D N   1 
ATOM 5871 C CA  . PRO D 1 121 ? 31.52073  -14.54273 1.08606   1.000 63.11635  ? 121 PRO D CA  1 
ATOM 5872 C C   . PRO D 1 121 ? 32.54678  -15.24606 1.95614   1.000 65.31616  ? 121 PRO D C   1 
ATOM 5873 O O   . PRO D 1 121 ? 33.59942  -15.65517 1.43839   1.000 62.49015  ? 121 PRO D O   1 
ATOM 5874 C CB  . PRO D 1 121 ? 31.61804  -13.02035 1.21560   1.000 61.75292  ? 121 PRO D CB  1 
ATOM 5875 C CG  . PRO D 1 121 ? 30.24149  -12.55990 0.98567   1.000 63.48725  ? 121 PRO D CG  1 
ATOM 5876 C CD  . PRO D 1 121 ? 29.33959  -13.57434 1.58196   1.000 65.49055  ? 121 PRO D CD  1 
ATOM 5877 N N   . ILE D 1 122 ? 32.26639  -15.38998 3.26313   1.000 61.56148  ? 122 ILE D N   1 
ATOM 5878 C CA  . ILE D 1 122 ? 33.15394  -16.10884 4.17722   1.000 60.55751  ? 122 ILE D CA  1 
ATOM 5879 C C   . ILE D 1 122 ? 33.01531  -17.61869 4.01006   1.000 59.29990  ? 122 ILE D C   1 
ATOM 5880 O O   . ILE D 1 122 ? 33.99328  -18.35542 4.18276   1.000 59.27681  ? 122 ILE D O   1 
ATOM 5881 C CB  . ILE D 1 122 ? 32.89613  -15.68876 5.63845   1.000 63.42145  ? 122 ILE D CB  1 
ATOM 5882 C CG1 . ILE D 1 122 ? 33.26021  -14.23799 5.87421   1.000 60.83807  ? 122 ILE D CG1 1 
ATOM 5883 C CG2 . ILE D 1 122 ? 33.71548  -16.49297 6.59736   1.000 61.09958  ? 122 ILE D CG2 1 
ATOM 5884 C CD1 . ILE D 1 122 ? 32.80374  -13.76954 7.20238   1.000 61.90073  ? 122 ILE D CD1 1 
ATOM 5885 N N   . LEU D 1 123 ? 31.81494  -18.11127 3.69295   1.000 60.25950  ? 123 LEU D N   1 
ATOM 5886 C CA  . LEU D 1 123 ? 31.64704  -19.54337 3.46338   1.000 58.92074  ? 123 LEU D CA  1 
ATOM 5887 C C   . LEU D 1 123 ? 32.46338  -19.97883 2.26783   1.000 63.54968  ? 123 LEU D C   1 
ATOM 5888 O O   . LEU D 1 123 ? 33.23588  -20.94033 2.34174   1.000 66.64750  ? 123 LEU D O   1 
ATOM 5889 C CB  . LEU D 1 123 ? 30.17091  -19.89152 3.25036   1.000 63.01314  ? 123 LEU D CB  1 
ATOM 5890 C CG  . LEU D 1 123 ? 29.77988  -21.37415 3.07618   1.000 67.40929  ? 123 LEU D CG  1 
ATOM 5891 C CD1 . LEU D 1 123 ? 30.12769  -22.21890 4.29995   1.000 63.61562  ? 123 LEU D CD1 1 
ATOM 5892 C CD2 . LEU D 1 123 ? 28.29671  -21.52084 2.74002   1.000 67.05423  ? 123 LEU D CD2 1 
ATOM 5893 N N   . VAL D 1 124 ? 32.34348  -19.23731 1.16651   1.000 65.12231  ? 124 VAL D N   1 
ATOM 5894 C CA  . VAL D 1 124 ? 33.00498  -19.61436 -0.06786  1.000 62.01708  ? 124 VAL D CA  1 
ATOM 5895 C C   . VAL D 1 124 ? 34.52275  -19.50733 0.07013   1.000 64.92948  ? 124 VAL D C   1 
ATOM 5896 O O   . VAL D 1 124 ? 35.26523  -20.33375 -0.47925  1.000 65.32201  ? 124 VAL D O   1 
ATOM 5897 C CB  . VAL D 1 124 ? 32.44557  -18.76174 -1.21788  1.000 65.24925  ? 124 VAL D CB  1 
ATOM 5898 C CG1 . VAL D 1 124 ? 33.20386  -19.02373 -2.52211  1.000 68.02653  ? 124 VAL D CG1 1 
ATOM 5899 C CG2 . VAL D 1 124 ? 30.97614  -19.06231 -1.39710  1.000 63.35797  ? 124 VAL D CG2 1 
ATOM 5900 N N   . ASP D 1 125 ? 35.01830  -18.51302 0.81254   1.000 59.20608  ? 125 ASP D N   1 
ATOM 5901 C CA  . ASP D 1 125 ? 36.46700  -18.40877 0.96245   1.000 61.53413  ? 125 ASP D CA  1 
ATOM 5902 C C   . ASP D 1 125 ? 37.04363  -19.62199 1.69052   1.000 66.75377  ? 125 ASP D C   1 
ATOM 5903 O O   . ASP D 1 125 ? 38.18790  -20.02248 1.44652   1.000 64.69108  ? 125 ASP D O   1 
ATOM 5904 C CB  . ASP D 1 125 ? 36.84223  -17.12497 1.69046   1.000 59.47937  ? 125 ASP D CB  1 
ATOM 5905 C CG  . ASP D 1 125 ? 38.33558  -16.83851 1.61396   1.000 63.85093  ? 125 ASP D CG  1 
ATOM 5906 O OD1 . ASP D 1 125 ? 38.81683  -16.38882 0.54600   1.000 68.28325  ? 125 ASP D OD1 1 
ATOM 5907 O OD2 . ASP D 1 125 ? 39.04933  -17.08673 2.59464   1.000 60.59530  ? 125 ASP D OD2 1 
ATOM 5908 N N   . LEU D 1 126 ? 36.27337  -20.19485 2.61879   1.000 67.60145  ? 126 LEU D N   1 
ATOM 5909 C CA  . LEU D 1 126 ? 36.69359  -21.40232 3.31840   1.000 67.10507  ? 126 LEU D CA  1 
ATOM 5910 C C   . LEU D 1 126 ? 36.63252  -22.61814 2.39801   1.000 70.55945  ? 126 LEU D C   1 
ATOM 5911 O O   . LEU D 1 126 ? 37.53034  -23.46835 2.41443   1.000 72.19031  ? 126 LEU D O   1 
ATOM 5912 C CB  . LEU D 1 126 ? 35.81344  -21.60531 4.55371   1.000 66.00637  ? 126 LEU D CB  1 
ATOM 5913 C CG  . LEU D 1 126 ? 35.90180  -20.55513 5.66774   1.000 62.35799  ? 126 LEU D CG  1 
ATOM 5914 C CD1 . LEU D 1 126 ? 34.76947  -20.71319 6.66781   1.000 58.72191  ? 126 LEU D CD1 1 
ATOM 5915 C CD2 . LEU D 1 126 ? 37.24454  -20.61087 6.37424   1.000 59.61640  ? 126 LEU D CD2 1 
ATOM 5916 N N   . ILE D 1 127 ? 35.58003  -22.71275 1.58538   1.000 68.62366  ? 127 ILE D N   1 
ATOM 5917 C CA  . ILE D 1 127 ? 35.50773  -23.75312 0.56190   1.000 70.59908  ? 127 ILE D CA  1 
ATOM 5918 C C   . ILE D 1 127 ? 36.66631  -23.62377 -0.42333  1.000 70.36741  ? 127 ILE D C   1 
ATOM 5919 O O   . ILE D 1 127 ? 37.28627  -24.62006 -0.80002  1.000 72.18819  ? 127 ILE D O   1 
ATOM 5920 C CB  . ILE D 1 127 ? 34.14193  -23.69051 -0.14588  1.000 70.99889  ? 127 ILE D CB  1 
ATOM 5921 C CG1 . ILE D 1 127 ? 33.02285  -23.98547 0.86384   1.000 68.71056  ? 127 ILE D CG1 1 
ATOM 5922 C CG2 . ILE D 1 127 ? 34.11112  -24.60961 -1.35403  1.000 66.87575  ? 127 ILE D CG2 1 
ATOM 5923 C CD1 . ILE D 1 127 ? 31.62484  -23.65244 0.36494   1.000 70.99463  ? 127 ILE D CD1 1 
ATOM 5924 N N   . ARG D 1 128 ? 36.98585  -22.39459 -0.84598  1.000 72.56270  ? 128 ARG D N   1 
ATOM 5925 C CA  . ARG D 1 128 ? 38.16879  -22.15821 -1.67712  1.000 76.24128  ? 128 ARG D CA  1 
ATOM 5926 C C   . ARG D 1 128 ? 39.47004  -22.59585 -1.00719  1.000 77.59074  ? 128 ARG D C   1 
ATOM 5927 O O   . ARG D 1 128 ? 40.46986  -22.81447 -1.70193  1.000 79.30435  ? 128 ARG D O   1 
ATOM 5928 C CB  . ARG D 1 128 ? 38.28058  -20.67303 -2.04008  1.000 75.49835  ? 128 ARG D CB  1 
ATOM 5929 C CG  . ARG D 1 128 ? 37.30821  -20.17921 -3.08988  1.000 77.08388  ? 128 ARG D CG  1 
ATOM 5930 C CD  . ARG D 1 128 ? 37.40232  -18.68466 -3.14786  1.000 75.82146  ? 128 ARG D CD  1 
ATOM 5931 N NE  . ARG D 1 128 ? 36.35395  -18.06854 -3.94756  1.000 77.58423  ? 128 ARG D NE  1 
ATOM 5932 C CZ  . ARG D 1 128 ? 35.93265  -16.82415 -3.75540  1.000 78.44323  ? 128 ARG D CZ  1 
ATOM 5933 N NH1 . ARG D 1 128 ? 36.39980  -16.08460 -2.75578  1.000 72.41424  ? 128 ARG D NH1 1 
ATOM 5934 N NH2 . ARG D 1 128 ? 34.97669  -16.33169 -4.54262  1.000 80.28023  ? 128 ARG D NH2 1 
ATOM 5935 N N   . ASP D 1 129 ? 39.50410  -22.69068 0.32539   1.000 81.74635  ? 129 ASP D N   1 
ATOM 5936 C CA  . ASP D 1 129 ? 40.74932  -23.08047 0.96730   1.000 81.45372  ? 129 ASP D CA  1 
ATOM 5937 C C   . ASP D 1 129 ? 40.98690  -24.56504 0.82915   1.000 81.60940  ? 129 ASP D C   1 
ATOM 5938 O O   . ASP D 1 129 ? 42.12633  -25.01035 0.98538   1.000 84.27945  ? 129 ASP D O   1 
ATOM 5939 C CB  . ASP D 1 129 ? 40.75299  -22.66598 2.43649   1.000 82.85229  ? 129 ASP D CB  1 
ATOM 5940 C CG  . ASP D 1 129 ? 40.85506  -21.14777 2.62761   1.000 84.31723  ? 129 ASP D CG  1 
ATOM 5941 O OD1 . ASP D 1 129 ? 41.59177  -20.47659 1.87092   1.000 83.79753  ? 129 ASP D OD1 1 
ATOM 5942 O OD2 . ASP D 1 129 ? 40.15262  -20.62063 3.52987   1.000 82.05045  ? 129 ASP D OD2 1 
ATOM 5943 N N   . ILE D 1 130 ? 39.93382  -25.32980 0.52490   1.000 78.04355  ? 130 ILE D N   1 
ATOM 5944 C CA  . ILE D 1 130 ? 40.08705  -26.74935 0.20059   1.000 76.49179  ? 130 ILE D CA  1 
ATOM 5945 C C   . ILE D 1 130 ? 40.92206  -26.91445 -1.05463  1.000 78.78157  ? 130 ILE D C   1 
ATOM 5946 O O   . ILE D 1 130 ? 41.77334  -27.80577 -1.13415  1.000 75.72532  ? 130 ILE D O   1 
ATOM 5947 C CB  . ILE D 1 130 ? 38.71032  -27.42003 0.05355   1.000 69.96847  ? 130 ILE D CB  1 
ATOM 5948 C CG1 . ILE D 1 130 ? 38.02934  -27.51942 1.41285   1.000 72.48645  ? 130 ILE D CG1 1 
ATOM 5949 C CG2 . ILE D 1 130 ? 38.84972  -28.78013 -0.50915  1.000 74.32524  ? 130 ILE D CG2 1 
ATOM 5950 C CD1 . ILE D 1 130 ? 36.58273  -27.87804 1.32952   1.000 78.26399  ? 130 ILE D CD1 1 
ATOM 5951 N N   . GLN D 1 131 ? 40.68865  -26.04499 -2.05254  1.000 81.03916  ? 131 GLN D N   1 
ATOM 5952 C CA  . GLN D 1 131 ? 41.41212  -26.04434 -3.31629  1.000 76.08018  ? 131 GLN D CA  1 
ATOM 5953 C C   . GLN D 1 131 ? 42.77748  -25.37694 -3.21532  1.000 77.47296  ? 131 GLN D C   1 
ATOM 5954 O O   . GLN D 1 131 ? 43.69667  -25.74042 -3.95837  1.000 78.60146  ? 131 GLN D O   1 
ATOM 5955 C CB  . GLN D 1 131 ? 40.58717  -25.34037 -4.38774  1.000 79.77289  ? 131 GLN D CB  1 
ATOM 5956 C CG  . GLN D 1 131 ? 39.26489  -26.00572 -4.74411  1.000 83.19596  ? 131 GLN D CG  1 
ATOM 5957 C CD  . GLN D 1 131 ? 38.71819  -25.47819 -6.06798  1.000 90.49872  ? 131 GLN D CD  1 
ATOM 5958 O OE1 . GLN D 1 131 ? 39.32673  -24.60477 -6.69033  1.000 92.05191  ? 131 GLN D OE1 1 
ATOM 5959 N NE2 . GLN D 1 131 ? 37.59193  -26.02623 -6.51896  1.000 89.68138  ? 131 GLN D NE2 1 
ATOM 5960 N N   . ARG D 1 132 ? 42.92141  -24.37240 -2.35042  1.000 79.50641  ? 132 ARG D N   1 
ATOM 5961 C CA  . ARG D 1 132 ? 44.24611  -23.83194 -2.05794  1.000 81.15781  ? 132 ARG D CA  1 
ATOM 5962 C C   . ARG D 1 132 ? 45.13683  -24.84929 -1.36256  1.000 79.52358  ? 132 ARG D C   1 
ATOM 5963 O O   . ARG D 1 132 ? 46.36534  -24.72931 -1.41871  1.000 80.47324  ? 132 ARG D O   1 
ATOM 5964 C CB  . ARG D 1 132 ? 44.12763  -22.56363 -1.20875  1.000 80.44325  ? 132 ARG D CB  1 
ATOM 5965 C CG  . ARG D 1 132 ? 43.95623  -21.30766 -2.01942  1.000 84.71175  ? 132 ARG D CG  1 
ATOM 5966 C CD  . ARG D 1 132 ? 44.03627  -20.06891 -1.14108  1.000 81.95565  ? 132 ARG D CD  1 
ATOM 5967 N NE  . ARG D 1 132 ? 42.80182  -19.88598 -0.39602  1.000 81.85102  ? 132 ARG D NE  1 
ATOM 5968 C CZ  . ARG D 1 132 ? 41.78904  -19.13551 -0.81088  1.000 81.13943  ? 132 ARG D CZ  1 
ATOM 5969 N NH1 . ARG D 1 132 ? 41.87905  -18.39813 -1.90871  1.000 79.09032  ? 132 ARG D NH1 1 
ATOM 5970 N NH2 . ARG D 1 132 ? 40.65919  -19.12206 -0.10501  1.000 77.63615  ? 132 ARG D NH2 1 
ATOM 5971 N N   . LEU D 1 133 ? 44.53486  -25.83199 -0.69405  1.000 78.04067  ? 133 LEU D N   1 
ATOM 5972 C CA  . LEU D 1 133 ? 45.26417  -26.96818 -0.14873  1.000 79.40138  ? 133 LEU D CA  1 
ATOM 5973 C C   . LEU D 1 133 ? 45.76653  -27.91098 -1.24707  1.000 80.27164  ? 133 LEU D C   1 
ATOM 5974 O O   . LEU D 1 133 ? 46.71189  -28.67881 -1.02791  1.000 73.51735  ? 133 LEU D O   1 
ATOM 5975 C CB  . LEU D 1 133 ? 44.34332  -27.69902 0.82319   1.000 75.45020  ? 133 LEU D CB  1 
ATOM 5976 C CG  . LEU D 1 133 ? 44.91441  -28.85655 1.61819   1.000 75.56892  ? 133 LEU D CG  1 
ATOM 5977 C CD1 . LEU D 1 133 ? 46.00345  -28.33971 2.53788   1.000 72.54129  ? 133 LEU D CD1 1 
ATOM 5978 C CD2 . LEU D 1 133 ? 43.79080  -29.53921 2.36651   1.000 74.32761  ? 133 LEU D CD2 1 
ATOM 5979 N N   . ASN D 1 134 ? 45.16970  -27.83672 -2.42834  1.000 79.76951  ? 134 ASN D N   1 
ATOM 5980 C CA  . ASN D 1 134 ? 45.50201  -28.67495 -3.55432  1.000 76.35916  ? 134 ASN D CA  1 
ATOM 5981 C C   . ASN D 1 134 ? 46.52454  -28.01103 -4.47941  1.000 80.93985  ? 134 ASN D C   1 
ATOM 5982 O O   . ASN D 1 134 ? 46.85167  -28.57009 -5.53199  1.000 85.69875  ? 134 ASN D O   1 
ATOM 5983 C CB  . ASN D 1 134 ? 44.20666  -29.00090 -4.30413  1.000 78.47382  ? 134 ASN D CB  1 
ATOM 5984 C CG  . ASN D 1 134 ? 44.23127  -30.36344 -4.97877  1.000 80.73381  ? 134 ASN D CG  1 
ATOM 5985 O OD1 . ASN D 1 134 ? 45.18732  -31.13642 -4.84324  1.000 80.86353  ? 134 ASN D OD1 1 
ATOM 5986 N ND2 . ASN D 1 134 ? 43.16237  -30.66915 -5.70717  1.000 78.94910  ? 134 ASN D ND2 1 
ATOM 5987 N N   . GLY D 1 135 ? 47.03742  -26.83252 -4.11880  1.000 82.73220  ? 135 GLY D N   1 
ATOM 5988 C CA  . GLY D 1 135 ? 48.00676  -26.12196 -4.94086  1.000 86.61742  ? 135 GLY D CA  1 
ATOM 5989 C C   . GLY D 1 135 ? 47.41685  -25.30186 -6.06839  1.000 88.40362  ? 135 GLY D C   1 
ATOM 5990 O O   . GLY D 1 135 ? 48.17555  -24.70793 -6.84699  1.000 87.10522  ? 135 GLY D O   1 
ATOM 5991 N N   . VAL D 1 136 ? 46.08809  -25.26343 -6.17865  1.000 88.07356  ? 136 VAL D N   1 
ATOM 5992 C CA  . VAL D 1 136 ? 45.40216  -24.46317 -7.18189  1.000 87.83499  ? 136 VAL D CA  1 
ATOM 5993 C C   . VAL D 1 136 ? 45.65955  -22.98800 -6.91332  1.000 88.99870  ? 136 VAL D C   1 
ATOM 5994 O O   . VAL D 1 136 ? 45.59317  -22.53180 -5.76593  1.000 90.76469  ? 136 VAL D O   1 
ATOM 5995 C CB  . VAL D 1 136 ? 43.89686  -24.78696 -7.14411  1.000 86.60313  ? 136 VAL D CB  1 
ATOM 5996 C CG1 . VAL D 1 136 ? 43.13002  -23.95210 -8.14010  1.000 88.65157  ? 136 VAL D CG1 1 
ATOM 5997 C CG2 . VAL D 1 136 ? 43.65487  -26.27607 -7.37192  1.000 86.16406  ? 136 VAL D CG2 1 
ATOM 5998 N N   . SER D 1 137 ? 45.94118  -22.23009 -7.97161  1.000 91.54649  ? 137 SER D N   1 
ATOM 5999 C CA  . SER D 1 137 ? 46.25127  -20.81003 -7.85915  1.000 88.49704  ? 137 SER D CA  1 
ATOM 6000 C C   . SER D 1 137 ? 44.98318  -19.97354 -7.66732  1.000 89.49515  ? 137 SER D C   1 
ATOM 6001 O O   . SER D 1 137 ? 43.86609  -20.42034 -7.93824  1.000 90.34780  ? 137 SER D O   1 
ATOM 6002 C CB  . SER D 1 137 ? 46.99899  -20.34045 -9.09915  1.000 91.52187  ? 137 SER D CB  1 
ATOM 6003 O OG  . SER D 1 137 ? 48.22475  -21.03840 -9.24402  1.000 97.46695  ? 137 SER D OG  1 
ATOM 6004 N N   . GLU D 1 138 ? 45.17346  -18.73864 -7.18442  1.000 87.90887  ? 138 GLU D N   1 
ATOM 6005 C CA  . GLU D 1 138 ? 44.04953  -17.82731 -6.95172  1.000 86.03713  ? 138 GLU D CA  1 
ATOM 6006 C C   . GLU D 1 138 ? 43.20623  -17.61920 -8.20231  1.000 85.83964  ? 138 GLU D C   1 
ATOM 6007 O O   . GLU D 1 138 ? 41.97092  -17.54249 -8.12800  1.000 80.45559  ? 138 GLU D O   1 
ATOM 6008 C CB  . GLU D 1 138 ? 44.56849  -16.47788 -6.46188  1.000 87.68856  ? 138 GLU D CB  1 
ATOM 6009 C CG  . GLU D 1 138 ? 45.00932  -16.46293 -5.03429  1.000 88.14250  ? 138 GLU D CG  1 
ATOM 6010 C CD  . GLU D 1 138 ? 43.83057  -16.54844 -4.09337  1.000 93.25503  ? 138 GLU D CD  1 
ATOM 6011 O OE1 . GLU D 1 138 ? 42.76095  -15.98723 -4.42527  1.000 94.84838  ? 138 GLU D OE1 1 
ATOM 6012 O OE2 . GLU D 1 138 ? 43.96087  -17.18844 -3.02945  1.000 96.07928  ? 138 GLU D OE2 1 
ATOM 6013 N N   . ASN D 1 139 ? 43.86407  -17.46847 -9.35366  1.000 86.01265  ? 139 ASN D N   1 
ATOM 6014 C CA  . ASN D 1 139 ? 43.17268  -17.34442 -10.62901 1.000 86.86816  ? 139 ASN D CA  1 
ATOM 6015 C C   . ASN D 1 139 ? 42.65771  -18.67797 -11.15469 1.000 85.77440  ? 139 ASN D C   1 
ATOM 6016 O O   . ASN D 1 139 ? 41.74747  -18.69117 -11.98842 1.000 84.06009  ? 139 ASN D O   1 
ATOM 6017 C CB  . ASN D 1 139 ? 44.10902  -16.69648 -11.64485 1.000 86.65430  ? 139 ASN D CB  1 
ATOM 6018 C CG  . ASN D 1 139 ? 45.39135  -17.46640 -11.81794 1.000 89.14348  ? 139 ASN D CG  1 
ATOM 6019 O OD1 . ASN D 1 139 ? 45.52818  -18.58030 -11.32716 1.000 94.51789  ? 139 ASN D OD1 1 
ATOM 6020 N ND2 . ASN D 1 139 ? 46.35443  -16.86342 -12.49251 1.000 93.63308  ? 139 ASN D ND2 1 
ATOM 6021 N N   . GLU D 1 140 ? 43.22099  -19.79340 -10.69226 1.000 86.44841  ? 140 GLU D N   1 
ATOM 6022 C CA  . GLU D 1 140 ? 42.73958  -21.10762 -11.08785 1.000 87.90883  ? 140 GLU D CA  1 
ATOM 6023 C C   . GLU D 1 140 ? 41.57889  -21.61920 -10.23984 1.000 87.47521  ? 140 GLU D C   1 
ATOM 6024 O O   . GLU D 1 140 ? 40.99244  -22.64238 -10.59782 1.000 87.70934  ? 140 GLU D O   1 
ATOM 6025 C CB  . GLU D 1 140 ? 43.87292  -22.12126 -11.01904 1.000 90.91063  ? 140 GLU D CB  1 
ATOM 6026 C CG  . GLU D 1 140 ? 44.96192  -21.92978 -12.03816 1.000 97.23632  ? 140 GLU D CG  1 
ATOM 6027 C CD  . GLU D 1 140 ? 46.06457  -22.96552 -11.88383 1.000 102.98990 ? 140 GLU D CD  1 
ATOM 6028 O OE1 . GLU D 1 140 ? 46.02478  -23.74607 -10.89133 1.000 97.33965  ? 140 GLU D OE1 1 
ATOM 6029 O OE2 . GLU D 1 140 ? 46.96538  -22.99418 -12.75703 1.000 106.41938 ? 140 GLU D OE2 1 
ATOM 6030 N N   . LEU D 1 141 ? 41.23713  -20.95887 -9.13469  1.000 87.75704  ? 141 LEU D N   1 
ATOM 6031 C CA  . LEU D 1 141 ? 40.16074  -21.45308 -8.28593  1.000 89.38080  ? 141 LEU D CA  1 
ATOM 6032 C C   . LEU D 1 141 ? 38.84308  -21.50119 -9.04649  1.000 97.01664  ? 141 LEU D C   1 
ATOM 6033 O O   . LEU D 1 141 ? 38.55977  -20.66018 -9.90563  1.000 98.56893  ? 141 LEU D O   1 
ATOM 6034 C CB  . LEU D 1 141 ? 39.98954  -20.58002 -7.03905  1.000 86.93101  ? 141 LEU D CB  1 
ATOM 6035 C CG  . LEU D 1 141 ? 41.02485  -20.62409 -5.91687  1.000 84.63392  ? 141 LEU D CG  1 
ATOM 6036 C CD1 . LEU D 1 141 ? 40.76467  -19.52638 -4.91305  1.000 80.06066  ? 141 LEU D CD1 1 
ATOM 6037 C CD2 . LEU D 1 141 ? 40.96195  -21.96135 -5.23568  1.000 83.00370  ? 141 LEU D CD2 1 
ATOM 6038 N N   . ASP D 1 142 ? 38.04686  -22.52417 -8.73451  1.000 106.23444 ? 142 ASP D N   1 
ATOM 6039 C CA  . ASP D 1 142 ? 36.65209  -22.58330 -9.16663  1.000 107.36527 ? 142 ASP D CA  1 
ATOM 6040 C C   . ASP D 1 142 ? 35.91588  -23.54890 -8.24856  1.000 106.88432 ? 142 ASP D C   1 
ATOM 6041 O O   . ASP D 1 142 ? 36.18135  -24.75456 -8.26640  1.000 107.43546 ? 142 ASP D O   1 
ATOM 6042 C CB  . ASP D 1 142 ? 36.52618  -23.01390 -10.61933 1.000 108.92857 ? 142 ASP D CB  1 
ATOM 6043 C CG  . ASP D 1 142 ? 35.09423  -22.94224 -11.10388 1.000 112.02714 ? 142 ASP D CG  1 
ATOM 6044 O OD1 . ASP D 1 142 ? 34.61199  -21.81508 -11.35208 1.000 113.14045 ? 142 ASP D OD1 1 
ATOM 6045 O OD2 . ASP D 1 142 ? 34.43535  -24.00190 -11.19139 1.000 115.18211 ? 142 ASP D OD2 1 
ATOM 6046 N N   . THR D 1 143 ? 34.98001  -23.02777 -7.46716  1.000 99.01486  ? 143 THR D N   1 
ATOM 6047 C CA  . THR D 1 143 ? 34.30173  -23.83500 -6.46596  1.000 91.69913  ? 143 THR D CA  1 
ATOM 6048 C C   . THR D 1 143 ? 32.80771  -23.92915 -6.73248  1.000 91.25689  ? 143 THR D C   1 
ATOM 6049 O O   . THR D 1 143 ? 32.03800  -24.20662 -5.81452  1.000 91.75905  ? 143 THR D O   1 
ATOM 6050 C CB  . THR D 1 143 ? 34.57846  -23.27972 -5.06889  1.000 86.63071  ? 143 THR D CB  1 
ATOM 6051 O OG1 . THR D 1 143 ? 34.04708  -21.95513 -4.95526  1.000 86.61623  ? 143 THR D OG1 1 
ATOM 6052 C CG2 . THR D 1 143 ? 36.07809  -23.22769 -4.82424  1.000 84.74037  ? 143 THR D CG2 1 
ATOM 6053 N N   . PHE D 1 144 ? 32.39324  -23.72095 -7.98268  1.000 94.43963  ? 144 PHE D N   1 
ATOM 6054 C CA  . PHE D 1 144 ? 30.98854  -23.85210 -8.36235  1.000 95.78111  ? 144 PHE D CA  1 
ATOM 6055 C C   . PHE D 1 144 ? 30.41802  -25.17797 -7.87118  1.000 96.28005  ? 144 PHE D C   1 
ATOM 6056 O O   . PHE D 1 144 ? 29.36268  -25.22496 -7.22570  1.000 93.56260  ? 144 PHE D O   1 
ATOM 6057 C CB  . PHE D 1 144 ? 30.88889  -23.73625 -9.89131  1.000 99.33044  ? 144 PHE D CB  1 
ATOM 6058 C CG  . PHE D 1 144 ? 29.49915  -23.90908 -10.45543 1.000 96.99073  ? 144 PHE D CG  1 
ATOM 6059 C CD1 . PHE D 1 144 ? 28.57541  -22.87695 -10.40713 1.000 96.77032  ? 144 PHE D CD1 1 
ATOM 6060 C CD2 . PHE D 1 144 ? 29.13557  -25.09800 -11.07319 1.000 97.15467  ? 144 PHE D CD2 1 
ATOM 6061 C CE1 . PHE D 1 144 ? 27.30378  -23.02958 -10.94598 1.000 97.23837  ? 144 PHE D CE1 1 
ATOM 6062 C CE2 . PHE D 1 144 ? 27.86589  -25.26022 -11.60756 1.000 99.69629  ? 144 PHE D CE2 1 
ATOM 6063 C CZ  . PHE D 1 144 ? 26.94753  -24.22161 -11.54445 1.000 98.83476  ? 144 PHE D CZ  1 
ATOM 6064 N N   . LYS D 1 145 ? 31.14406  -26.26254 -8.12850  1.000 101.52662 ? 145 LYS D N   1 
ATOM 6065 C CA  . LYS D 1 145 ? 30.70927  -27.61532 -7.82727  1.000 98.50613  ? 145 LYS D CA  1 
ATOM 6066 C C   . LYS D 1 145 ? 30.82940  -27.98257 -6.35503  1.000 97.16293  ? 145 LYS D C   1 
ATOM 6067 O O   . LYS D 1 145 ? 30.29329  -29.01712 -5.94830  1.000 99.13349  ? 145 LYS D O   1 
ATOM 6068 C CB  . LYS D 1 145 ? 31.50716  -28.58302 -8.70568  1.000 100.50809 ? 145 LYS D CB  1 
ATOM 6069 C CG  . LYS D 1 145 ? 33.01794  -28.38953 -8.62185  1.000 100.74380 ? 145 LYS D CG  1 
ATOM 6070 C CD  . LYS D 1 145 ? 33.71603  -29.15054 -9.75414  1.000 112.11891 ? 145 LYS D CD  1 
ATOM 6071 C CE  . LYS D 1 145 ? 35.21182  -28.85052 -9.82944  1.000 107.32013 ? 145 LYS D CE  1 
ATOM 6072 N NZ  . LYS D 1 145 ? 35.82654  -29.55690 -10.98103 1.000 102.07377 ? 145 LYS D NZ  1 
ATOM 6073 N N   . LEU D 1 146 ? 31.48797  -27.17085 -5.54134  1.000 91.15399  ? 146 LEU D N   1 
ATOM 6074 C CA  . LEU D 1 146 ? 31.69177  -27.51013 -4.14322  1.000 84.34350  ? 146 LEU D CA  1 
ATOM 6075 C C   . LEU D 1 146 ? 30.72767  -26.79589 -3.19186  1.000 87.47413  ? 146 LEU D C   1 
ATOM 6076 O O   . LEU D 1 146 ? 30.85177  -26.96913 -1.97541  1.000 90.65196  ? 146 LEU D O   1 
ATOM 6077 C CB  . LEU D 1 146 ? 33.13506  -27.19599 -3.74623  1.000 76.97600  ? 146 LEU D CB  1 
ATOM 6078 C CG  . LEU D 1 146 ? 34.26893  -27.86491 -4.51953  1.000 75.69264  ? 146 LEU D CG  1 
ATOM 6079 C CD1 . LEU D 1 146 ? 35.60929  -27.35295 -4.03697  1.000 73.51580  ? 146 LEU D CD1 1 
ATOM 6080 C CD2 . LEU D 1 146 ? 34.21869  -29.37094 -4.43406  1.000 77.35012  ? 146 LEU D CD2 1 
ATOM 6081 N N   . GLU D 1 147 ? 29.68066  -25.97415 -3.73447  1.000 85.60154  ? 147 GLU D N   1 
ATOM 6082 C CA  . GLU D 1 147 ? 28.99763  -25.07798 -2.80002  1.000 87.06836  ? 147 GLU D CA  1 
ATOM 6083 C C   . GLU D 1 147 ? 27.61855  -25.60883 -2.40094  1.000 89.09574  ? 147 GLU D C   1 
ATOM 6084 O O   . GLU D 1 147 ? 26.93215  -26.24063 -3.20878  1.000 87.92442  ? 147 GLU D O   1 
ATOM 6085 C CB  . GLU D 1 147 ? 28.84016  -23.67167 -3.40136  1.000 87.62517  ? 147 GLU D CB  1 
ATOM 6086 C CG  . GLU D 1 147 ? 30.16911  -22.97451 -3.72950  1.000 89.20664  ? 147 GLU D CG  1 
ATOM 6087 C CD  . GLU D 1 147 ? 30.03857  -21.47909 -4.12865  1.000 91.49922  ? 147 GLU D CD  1 
ATOM 6088 O OE1 . GLU D 1 147 ? 28.91811  -20.89891 -4.06725  1.000 90.70282  ? 147 GLU D OE1 1 
ATOM 6089 O OE2 . GLU D 1 147 ? 31.07570  -20.89599 -4.53737  1.000 84.90584  ? 147 GLU D OE2 1 
ATOM 6090 N N   . PRO D 1 148 ? 27.18136  -25.33400 -1.15970  1.000 93.37642  ? 148 PRO D N   1 
ATOM 6091 C CA  . PRO D 1 148 ? 25.87367  -25.84387 -0.70322  1.000 91.52212  ? 148 PRO D CA  1 
ATOM 6092 C C   . PRO D 1 148 ? 24.69327  -25.36674 -1.52911  1.000 93.14525  ? 148 PRO D C   1 
ATOM 6093 O O   . PRO D 1 148 ? 23.68116  -26.07010 -1.61233  1.000 95.20032  ? 148 PRO D O   1 
ATOM 6094 C CB  . PRO D 1 148 ? 25.78684  -25.33074 0.74049   1.000 93.55378  ? 148 PRO D CB  1 
ATOM 6095 C CG  . PRO D 1 148 ? 26.68364  -24.14533 0.78470   1.000 87.71207  ? 148 PRO D CG  1 
ATOM 6096 C CD  . PRO D 1 148 ? 27.81865  -24.47641 -0.14269  1.000 88.54455  ? 148 PRO D CD  1 
ATOM 6097 N N   . CYS D 1 149 ? 24.76832  -24.17810 -2.11093  1.000 99.91548  ? 149 CYS D N   1 
ATOM 6098 C CA  . CYS D 1 149 ? 23.77559  -23.73620 -3.07546  1.000 100.89143 ? 149 CYS D CA  1 
ATOM 6099 C C   . CYS D 1 149 ? 24.48474  -22.94038 -4.15574  1.000 100.00734 ? 149 CYS D C   1 
ATOM 6100 O O   . CYS D 1 149 ? 25.52490  -22.32577 -3.90582  1.000 99.60879  ? 149 CYS D O   1 
ATOM 6101 C CB  . CYS D 1 149 ? 22.69077  -22.86958 -2.43737  1.000 104.16088 ? 149 CYS D CB  1 
ATOM 6102 S SG  . CYS D 1 149 ? 23.30495  -21.27295 -1.88287  1.000 101.39960 ? 149 CYS D SG  1 
ATOM 6103 N N   . LYS D 1 150 ? 23.92035  -22.95389 -5.35821  1.000 99.65168  ? 150 LYS D N   1 
ATOM 6104 C CA  . LYS D 1 150 ? 24.44849  -22.08461 -6.39573  1.000 101.40828 ? 150 LYS D CA  1 
ATOM 6105 C C   . LYS D 1 150 ? 24.15762  -20.63162 -6.02962  1.000 100.32635 ? 150 LYS D C   1 
ATOM 6106 O O   . LYS D 1 150 ? 23.20441  -20.33164 -5.30562  1.000 100.51910 ? 150 LYS D O   1 
ATOM 6107 C CB  . LYS D 1 150 ? 23.85380  -22.44175 -7.76153  1.000 100.16419 ? 150 LYS D CB  1 
ATOM 6108 C CG  . LYS D 1 150 ? 24.06312  -23.89387 -8.13948  1.000 96.95005  ? 150 LYS D CG  1 
ATOM 6109 C CD  . LYS D 1 150 ? 25.54103  -24.22670 -8.20844  1.000 99.57219  ? 150 LYS D CD  1 
ATOM 6110 C CE  . LYS D 1 150 ? 25.77528  -25.65200 -8.69728  1.000 101.66483 ? 150 LYS D CE  1 
ATOM 6111 N NZ  . LYS D 1 150 ? 25.35075  -26.68371 -7.70701  1.000 102.74560 ? 150 LYS D NZ  1 
ATOM 6112 N N   . PHE D 1 151 ? 24.99920  -19.72038 -6.53484  1.000 98.71720  ? 151 PHE D N   1 
ATOM 6113 C CA  . PHE D 1 151 ? 24.95703  -18.34108 -6.05683  1.000 95.71739  ? 151 PHE D CA  1 
ATOM 6114 C C   . PHE D 1 151 ? 23.63327  -17.65753 -6.34337  1.000 95.88385  ? 151 PHE D C   1 
ATOM 6115 O O   . PHE D 1 151 ? 23.31557  -16.65831 -5.69164  1.000 93.88137  ? 151 PHE D O   1 
ATOM 6116 C CB  . PHE D 1 151 ? 26.07827  -17.51264 -6.66857  1.000 93.69138  ? 151 PHE D CB  1 
ATOM 6117 C CG  . PHE D 1 151 ? 25.96077  -17.32131 -8.14909  1.000 95.83286  ? 151 PHE D CG  1 
ATOM 6118 C CD1 . PHE D 1 151 ? 26.63821  -18.15943 -9.02127  1.000 96.16220  ? 151 PHE D CD1 1 
ATOM 6119 C CD2 . PHE D 1 151 ? 25.18921  -16.28748 -8.67074  1.000 98.15351  ? 151 PHE D CD2 1 
ATOM 6120 C CE1 . PHE D 1 151 ? 26.55454  -17.97464 -10.39108 1.000 99.09749  ? 151 PHE D CE1 1 
ATOM 6121 C CE2 . PHE D 1 151 ? 25.08484  -16.09901 -10.02924 1.000 100.60203 ? 151 PHE D CE2 1 
ATOM 6122 C CZ  . PHE D 1 151 ? 25.77385  -16.94357 -10.90076 1.000 100.70877 ? 151 PHE D CZ  1 
ATOM 6123 N N   . TRP D 1 152 ? 22.87021  -18.15015 -7.31496  1.000 99.42723  ? 152 TRP D N   1 
ATOM 6124 C CA  . TRP D 1 152 ? 21.53464  -17.62190 -7.54411  1.000 100.65574 ? 152 TRP D CA  1 
ATOM 6125 C C   . TRP D 1 152 ? 20.48960  -18.20281 -6.59480  1.000 98.95582  ? 152 TRP D C   1 
ATOM 6126 O O   . TRP D 1 152 ? 19.34293  -17.74198 -6.60142  1.000 99.21174  ? 152 TRP D O   1 
ATOM 6127 C CB  . TRP D 1 152 ? 21.13449  -17.84802 -9.00248  1.000 101.81340 ? 152 TRP D CB  1 
ATOM 6128 C CG  . TRP D 1 152 ? 21.27152  -19.25578 -9.51012  1.000 98.36474  ? 152 TRP D CG  1 
ATOM 6129 C CD1 . TRP D 1 152 ? 20.38137  -20.26548 -9.34404  1.000 99.87297  ? 152 TRP D CD1 1 
ATOM 6130 C CD2 . TRP D 1 152 ? 22.33025  -19.78607 -10.33021 1.000 97.35071  ? 152 TRP D CD2 1 
ATOM 6131 N NE1 . TRP D 1 152 ? 20.83099  -21.40520 -9.97695  1.000 101.70130 ? 152 TRP D NE1 1 
ATOM 6132 C CE2 . TRP D 1 152 ? 22.02026  -21.13294 -10.59663 1.000 99.90874  ? 152 TRP D CE2 1 
ATOM 6133 C CE3 . TRP D 1 152 ? 23.50724  -19.25576 -10.85705 1.000 100.35529 ? 152 TRP D CE3 1 
ATOM 6134 C CZ2 . TRP D 1 152 ? 22.84735  -21.95953 -11.36932 1.000 101.99239 ? 152 TRP D CZ2 1 
ATOM 6135 C CZ3 . TRP D 1 152 ? 24.33636  -20.08402 -11.62840 1.000 99.06635  ? 152 TRP D CZ3 1 
ATOM 6136 C CH2 . TRP D 1 152 ? 24.00002  -21.41641 -11.87202 1.000 98.07996  ? 152 TRP D CH2 1 
ATOM 6137 N N   . ASN D 1 153 ? 20.85854  -19.17757 -5.76592  1.000 101.05516 ? 153 ASN D N   1 
ATOM 6138 C CA  . ASN D 1 153 ? 19.95197  -19.70177 -4.74995  1.000 107.00014 ? 153 ASN D CA  1 
ATOM 6139 C C   . ASN D 1 153 ? 20.10566  -19.02410 -3.38456  1.000 103.65089 ? 153 ASN D C   1 
ATOM 6140 O O   . ASN D 1 153 ? 19.20868  -19.15171 -2.54037  1.000 99.50198  ? 153 ASN D O   1 
ATOM 6141 C CB  . ASN D 1 153 ? 20.15801  -21.21297 -4.58933  1.000 106.39496 ? 153 ASN D CB  1 
ATOM 6142 C CG  . ASN D 1 153 ? 19.71742  -21.99986 -5.80908  1.000 100.70277 ? 153 ASN D CG  1 
ATOM 6143 O OD1 . ASN D 1 153 ? 18.71967  -21.67416 -6.45333  1.000 94.10154  ? 153 ASN D OD1 1 
ATOM 6144 N ND2 . ASN D 1 153 ? 20.44440  -23.06564 -6.10665  1.000 101.38135 ? 153 ASN D ND2 1 
ATOM 6145 N N   . GLN D 1 154 ? 21.21422  -18.32216 -3.14970  1.000 95.92245  ? 154 GLN D N   1 
ATOM 6146 C CA  . GLN D 1 154 ? 21.39352  -17.58723 -1.90794  1.000 92.60361  ? 154 GLN D CA  1 
ATOM 6147 C C   . GLN D 1 154 ? 20.31087  -16.52349 -1.79048  1.000 97.68394  ? 154 GLN D C   1 
ATOM 6148 O O   . GLN D 1 154 ? 19.93947  -15.88923 -2.77961  1.000 99.97308  ? 154 GLN D O   1 
ATOM 6149 C CB  . GLN D 1 154 ? 22.76781  -16.92491 -1.88796  1.000 89.98741  ? 154 GLN D CB  1 
ATOM 6150 C CG  . GLN D 1 154 ? 23.95050  -17.85789 -2.08829  1.000 90.42909  ? 154 GLN D CG  1 
ATOM 6151 C CD  . GLN D 1 154 ? 25.25161  -17.09884 -2.34778  1.000 82.70625  ? 154 GLN D CD  1 
ATOM 6152 O OE1 . GLN D 1 154 ? 25.27316  -15.87104 -2.37887  1.000 76.02095  ? 154 GLN D OE1 1 
ATOM 6153 N NE2 . GLN D 1 154 ? 26.32579  -17.83298 -2.57849  1.000 82.75154  ? 154 GLN D NE2 1 
ATOM 6154 N N   . ARG D 1 155 ? 19.79516  -16.33137 -0.57556  1.000 100.84909 ? 155 ARG D N   1 
ATOM 6155 C CA  . ARG D 1 155 ? 18.73543  -15.36193 -0.33033  1.000 99.34502  ? 155 ARG D CA  1 
ATOM 6156 C C   . ARG D 1 155 ? 19.05149  -14.59670 0.94195   1.000 97.48147  ? 155 ARG D C   1 
ATOM 6157 O O   . ARG D 1 155 ? 19.85371  -15.03424 1.76657   1.000 97.86108  ? 155 ARG D O   1 
ATOM 6158 C CB  . ARG D 1 155 ? 17.35973  -16.03037 -0.22431  1.000 100.85782 ? 155 ARG D CB  1 
ATOM 6159 C CG  . ARG D 1 155 ? 16.92495  -16.76378 -1.49881  1.000 109.79712 ? 155 ARG D CG  1 
ATOM 6160 C CD  . ARG D 1 155 ? 16.60504  -15.82126 -2.67255  1.000 109.12846 ? 155 ARG D CD  1 
ATOM 6161 N NE  . ARG D 1 155 ? 16.10484  -16.54721 -3.84033  1.000 111.58601 ? 155 ARG D NE  1 
ATOM 6162 C CZ  . ARG D 1 155 ? 16.84450  -16.95074 -4.86714  1.000 110.78917 ? 155 ARG D CZ  1 
ATOM 6163 N NH1 . ARG D 1 155 ? 18.13896  -16.68134 -4.94045  1.000 107.93058 ? 155 ARG D NH1 1 
ATOM 6164 N NH2 . ARG D 1 155 ? 16.26776  -17.63313 -5.85293  1.000 113.36719 ? 155 ARG D NH2 1 
ATOM 6165 N N   . ASP D 1 156 ? 18.41235  -13.44170 1.08899   1.000 98.58178  ? 156 ASP D N   1 
ATOM 6166 C CA  . ASP D 1 156 ? 18.67307  -12.53328 2.19454   1.000 99.51641  ? 156 ASP D CA  1 
ATOM 6167 C C   . ASP D 1 156 ? 17.44703  -12.43516 3.09357   1.000 104.30298 ? 156 ASP D C   1 
ATOM 6168 O O   . ASP D 1 156 ? 16.32604  -12.23178 2.61304   1.000 106.44691 ? 156 ASP D O   1 
ATOM 6169 C CB  . ASP D 1 156 ? 19.07605  -11.15411 1.67458   1.000 100.59520 ? 156 ASP D CB  1 
ATOM 6170 C CG  . ASP D 1 156 ? 19.52984  -10.21967 2.78256   1.000 100.06240 ? 156 ASP D CG  1 
ATOM 6171 O OD1 . ASP D 1 156 ? 20.57897  -10.50450 3.39800   1.000 96.61829  ? 156 ASP D OD1 1 
ATOM 6172 O OD2 . ASP D 1 156 ? 18.88052  -9.17138  2.99740   1.000 98.52778  ? 156 ASP D OD2 1 
ATOM 6173 N N   . ILE D 1 157 ? 17.67366  -12.59630 4.39991   1.000 104.13239 ? 157 ILE D N   1 
ATOM 6174 C CA  . ILE D 1 157 ? 16.59627  -12.57019 5.38813   1.000 103.70125 ? 157 ILE D CA  1 
ATOM 6175 C C   . ILE D 1 157 ? 16.04418  -11.16212 5.57812   1.000 103.17854 ? 157 ILE D C   1 
ATOM 6176 O O   . ILE D 1 157 ? 14.82789  -10.97684 5.70240   1.000 105.78395 ? 157 ILE D O   1 
ATOM 6177 C CB  . ILE D 1 157 ? 17.08678  -13.16056 6.72336   1.000 103.40111 ? 157 ILE D CB  1 
ATOM 6178 C CG1 . ILE D 1 157 ? 17.31429  -14.66894 6.59998   1.000 100.77213 ? 157 ILE D CG1 1 
ATOM 6179 C CG2 . ILE D 1 157 ? 16.12387  -12.81457 7.85620   1.000 102.22354 ? 157 ILE D CG2 1 
ATOM 6180 C CD1 . ILE D 1 157 ? 18.06717  -15.25172 7.74891   1.000 96.77958  ? 157 ILE D CD1 1 
ATOM 6181 N N   . ARG D 1 158 ? 16.91604  -10.15321 5.65603   1.000 101.09356 ? 158 ARG D N   1 
ATOM 6182 C CA  . ARG D 1 158 ? 16.41843  -8.80537  5.91295   1.000 102.90061 ? 158 ARG D CA  1 
ATOM 6183 C C   . ARG D 1 158 ? 15.53398  -8.33860  4.76721   1.000 108.84603 ? 158 ARG D C   1 
ATOM 6184 O O   . ARG D 1 158 ? 14.54443  -7.62640  4.98392   1.000 109.90156 ? 158 ARG D O   1 
ATOM 6185 C CB  . ARG D 1 158 ? 17.56990  -7.82222  6.12071   1.000 99.59378  ? 158 ARG D CB  1 
ATOM 6186 C CG  . ARG D 1 158 ? 18.58651  -8.22966  7.16564   1.000 92.86709  ? 158 ARG D CG  1 
ATOM 6187 C CD  . ARG D 1 158 ? 19.51928  -7.07303  7.49027   1.000 92.71759  ? 158 ARG D CD  1 
ATOM 6188 N NE  . ARG D 1 158 ? 20.69707  -7.51851  8.22921   1.000 96.04471  ? 158 ARG D NE  1 
ATOM 6189 C CZ  . ARG D 1 158 ? 21.90846  -7.65748  7.70158   1.000 95.92685  ? 158 ARG D CZ  1 
ATOM 6190 N NH1 . ARG D 1 158 ? 22.18159  -7.24380  6.47186   1.000 99.95630  ? 158 ARG D NH1 1 
ATOM 6191 N NH2 . ARG D 1 158 ? 22.87952  -8.19356  8.43454   1.000 94.34082  ? 158 ARG D NH2 1 
ATOM 6192 N N   . THR D 1 159 ? 15.88625  -8.73021  3.53602   1.000 119.45495 ? 159 THR D N   1 
ATOM 6193 C CA  . THR D 1 159 ? 15.07791  -8.39100  2.37167   1.000 119.92987 ? 159 THR D CA  1 
ATOM 6194 C C   . THR D 1 159 ? 13.71908  -9.07012  2.43373   1.000 119.41978 ? 159 THR D C   1 
ATOM 6195 O O   . THR D 1 159 ? 12.69012  -8.43170  2.19170   1.000 121.33919 ? 159 THR D O   1 
ATOM 6196 C CB  . THR D 1 159 ? 15.81033  -8.79411  1.08948   1.000 119.97464 ? 159 THR D CB  1 
ATOM 6197 O OG1 . THR D 1 159 ? 17.10858  -8.19244  1.06647   1.000 118.15407 ? 159 THR D OG1 1 
ATOM 6198 C CG2 . THR D 1 159 ? 15.03336  -8.34543  -0.15057  1.000 119.30920 ? 159 THR D CG2 1 
ATOM 6199 N N   . ARG D 1 160 ? 13.69521  -10.35924 2.77327   1.000 108.08505 ? 160 ARG D N   1 
ATOM 6200 C CA  . ARG D 1 160 ? 12.44811  -11.11298 2.72915   1.000 107.54324 ? 160 ARG D CA  1 
ATOM 6201 C C   . ARG D 1 160 ? 11.41496  -10.54062 3.69957   1.000 106.59568 ? 160 ARG D C   1 
ATOM 6202 O O   . ARG D 1 160 ? 10.23847  -10.38832 3.35246   1.000 107.30851 ? 160 ARG D O   1 
ATOM 6203 C CB  . ARG D 1 160 ? 12.73350  -12.58138 3.03433   1.000 101.35337 ? 160 ARG D CB  1 
ATOM 6204 C CG  . ARG D 1 160 ? 11.55517  -13.47614 2.83387   1.000 100.31120 ? 160 ARG D CG  1 
ATOM 6205 C CD  . ARG D 1 160 ? 11.27652  -13.54908 1.37086   1.000 104.16900 ? 160 ARG D CD  1 
ATOM 6206 N NE  . ARG D 1 160 ? 10.14590  -14.40430 1.04326   1.000 106.01626 ? 160 ARG D NE  1 
ATOM 6207 C CZ  . ARG D 1 160 ? 10.22847  -15.71922 0.90056   1.000 104.91201 ? 160 ARG D CZ  1 
ATOM 6208 N NH1 . ARG D 1 160 ? 11.33786  -16.37733 1.19265   1.000 101.53227 ? 160 ARG D NH1 1 
ATOM 6209 N NH2 . ARG D 1 160 ? 9.17116   -16.39147 0.45862   1.000 107.35762 ? 160 ARG D NH2 1 
ATOM 6210 N N   . ILE D 1 161 ? 11.83432  -10.20014 4.91459   1.000 106.56243 ? 161 ILE D N   1 
ATOM 6211 C CA  . ILE D 1 161 ? 10.88003  -9.67641  5.88296   1.000 110.52144 ? 161 ILE D CA  1 
ATOM 6212 C C   . ILE D 1 161 ? 10.37960  -8.30343  5.45186   1.000 110.60828 ? 161 ILE D C   1 
ATOM 6213 O O   . ILE D 1 161 ? 9.16946   -8.05599  5.43497   1.000 110.66632 ? 161 ILE D O   1 
ATOM 6214 C CB  . ILE D 1 161 ? 11.47484  -9.66965  7.30875   1.000 108.86254 ? 161 ILE D CB  1 
ATOM 6215 C CG1 . ILE D 1 161 ? 11.53274  -11.09628 7.86261   1.000 106.71622 ? 161 ILE D CG1 1 
ATOM 6216 C CG2 . ILE D 1 161 ? 10.66266  -8.81000  8.25321   1.000 106.51779 ? 161 ILE D CG2 1 
ATOM 6217 C CD1 . ILE D 1 161 ? 12.09241  -11.18472 9.26717   1.000 108.52587 ? 161 ILE D CD1 1 
ATOM 6218 N N   . GLU D 1 162 ? 11.28399  -7.39866  5.05703   1.000 110.05155 ? 162 GLU D N   1 
ATOM 6219 C CA  . GLU D 1 162 ? 10.76988  -6.09481  4.64075   1.000 111.01765 ? 162 GLU D CA  1 
ATOM 6220 C C   . GLU D 1 162 ? 9.97850   -6.19968  3.34441   1.000 110.64253 ? 162 GLU D C   1 
ATOM 6221 O O   . GLU D 1 162 ? 9.30497   -5.23638  2.95439   1.000 111.11960 ? 162 GLU D O   1 
ATOM 6222 C CB  . GLU D 1 162 ? 11.87361  -5.05086  4.44330   1.000 108.65004 ? 162 GLU D CB  1 
ATOM 6223 C CG  . GLU D 1 162 ? 12.51638  -5.12757  3.07608   1.000 111.02357 ? 162 GLU D CG  1 
ATOM 6224 C CD  . GLU D 1 162 ? 13.39618  -3.93242  2.75513   1.000 110.96007 ? 162 GLU D CD  1 
ATOM 6225 O OE1 . GLU D 1 162 ? 13.63923  -3.08507  3.64393   1.000 110.52411 ? 162 GLU D OE1 1 
ATOM 6226 O OE2 . GLU D 1 162 ? 13.80371  -3.81740  1.58148   1.000 111.33319 ? 162 GLU D OE2 1 
ATOM 6227 N N   . ALA D 1 163 ? 10.06847  -7.33660  2.65940   1.000 109.42326 ? 163 ALA D N   1 
ATOM 6228 C CA  . ALA D 1 163 ? 9.23074   -7.58836  1.50064   1.000 108.92225 ? 163 ALA D CA  1 
ATOM 6229 C C   . ALA D 1 163 ? 7.95520   -8.30622  1.92245   1.000 110.10832 ? 163 ALA D C   1 
ATOM 6230 O O   . ALA D 1 163 ? 6.85325   -7.80559  1.68007   1.000 110.93894 ? 163 ALA D O   1 
ATOM 6231 C CB  . ALA D 1 163 ? 10.00488  -8.38754  0.44671   1.000 110.35887 ? 163 ALA D CB  1 
ATOM 6232 N N   . LEU D 1 164 ? 8.08689   -9.46324  2.57918   1.000 110.29507 ? 164 LEU D N   1 
ATOM 6233 C CA  . LEU D 1 164 ? 6.89412   -10.18811 3.00482   1.000 111.13444 ? 164 LEU D CA  1 
ATOM 6234 C C   . LEU D 1 164 ? 5.97985   -9.26927  3.80301   1.000 111.72122 ? 164 LEU D C   1 
ATOM 6235 O O   . LEU D 1 164 ? 4.81673   -9.06475  3.43581   1.000 109.62746 ? 164 LEU D O   1 
ATOM 6236 C CB  . LEU D 1 164 ? 7.28379   -11.41909 3.82697   1.000 108.96140 ? 164 LEU D CB  1 
ATOM 6237 N N   . LEU D 1 165 ? 6.53272   -8.62281  4.84127   1.000 111.50976 ? 165 LEU D N   1 
ATOM 6238 C CA  . LEU D 1 165 ? 5.81412   -7.66115  5.67956   1.000 110.21896 ? 165 LEU D CA  1 
ATOM 6239 C C   . LEU D 1 165 ? 5.48898   -6.35095  4.97405   1.000 109.46271 ? 165 LEU D C   1 
ATOM 6240 O O   . LEU D 1 165 ? 4.78570   -5.52372  5.56601   1.000 109.74748 ? 165 LEU D O   1 
ATOM 6241 C CB  . LEU D 1 165 ? 6.60839   -7.32558  6.94901   1.000 112.82864 ? 165 LEU D CB  1 
ATOM 6242 C CG  . LEU D 1 165 ? 6.47871   -8.10346  8.26558   1.000 112.18631 ? 165 LEU D CG  1 
ATOM 6243 C CD1 . LEU D 1 165 ? 7.07171   -9.50140  8.19521   1.000 110.94755 ? 165 LEU D CD1 1 
ATOM 6244 C CD2 . LEU D 1 165 ? 7.12859   -7.29127  9.38639   1.000 109.42743 ? 165 LEU D CD2 1 
ATOM 6245 N N   . LEU D 1 166 ? 6.01985   -6.11779  3.77195   1.000 109.09503 ? 166 LEU D N   1 
ATOM 6246 C CA  . LEU D 1 166 ? 5.68716   -4.93447  2.97465   1.000 106.61932 ? 166 LEU D CA  1 
ATOM 6247 C C   . LEU D 1 166 ? 5.74645   -3.63921  3.78979   1.000 104.09108 ? 166 LEU D C   1 
ATOM 6248 O O   . LEU D 1 166 ? 4.90753   -2.74733  3.64707   1.000 101.40895 ? 166 LEU D O   1 
ATOM 6249 C CB  . LEU D 1 166 ? 4.32309   -5.10302  2.30309   1.000 104.21075 ? 166 LEU D CB  1 
ATOM 6250 C CG  . LEU D 1 166 ? 4.36803   -6.06921  1.11367   1.000 109.57231 ? 166 LEU D CG  1 
ATOM 6251 C CD1 . LEU D 1 166 ? 2.99656   -6.35536  0.47602   1.000 106.86320 ? 166 LEU D CD1 1 
ATOM 6252 C CD2 . LEU D 1 166 ? 5.34204   -5.52160  0.07423   1.000 104.06977 ? 166 LEU D CD2 1 
ATOM 6253 N N   . VAL D 1 167 ? 6.73692   -3.53671  4.67120   1.000 103.79714 ? 167 VAL D N   1 
ATOM 6254 C CA  . VAL D 1 167 ? 7.02649   -2.29206  5.37276   1.000 106.44933 ? 167 VAL D CA  1 
ATOM 6255 C C   . VAL D 1 167 ? 8.53425   -2.09723  5.37965   1.000 110.49937 ? 167 VAL D C   1 
ATOM 6256 O O   . VAL D 1 167 ? 9.27987   -3.00674  5.76056   1.000 111.09211 ? 167 VAL D O   1 
ATOM 6257 C CB  . VAL D 1 167 ? 6.47658   -2.28108  6.81156   1.000 106.74556 ? 167 VAL D CB  1 
ATOM 6258 C CG1 . VAL D 1 167 ? 6.80283   -0.95317  7.48307   1.000 104.32860 ? 167 VAL D CG1 1 
ATOM 6259 C CG2 . VAL D 1 167 ? 4.98093   -2.53073  6.81944   1.000 103.05367 ? 167 VAL D CG2 1 
ATOM 6260 N N   . ARG D 1 168 ? 8.97851   -0.91440  4.96791   1.000 114.70356 ? 168 ARG D N   1 
ATOM 6261 C CA  . ARG D 1 168 ? 10.40078  -0.66777  4.79793   1.000 115.85908 ? 168 ARG D CA  1 
ATOM 6262 C C   . ARG D 1 168 ? 11.10088  -0.64485  6.15269   1.000 116.34869 ? 168 ARG D C   1 
ATOM 6263 O O   . ARG D 1 168 ? 10.51537  -0.27882  7.17494   1.000 113.95355 ? 168 ARG D O   1 
ATOM 6264 C CB  . ARG D 1 168 ? 10.62517  0.64856   4.04327   1.000 113.93652 ? 168 ARG D CB  1 
ATOM 6265 C CG  . ARG D 1 168 ? 12.06515  0.92559   3.59085   1.000 114.39739 ? 168 ARG D CG  1 
ATOM 6266 C CD  . ARG D 1 168 ? 12.10718  2.17959   2.72281   1.000 118.81098 ? 168 ARG D CD  1 
ATOM 6267 N NE  . ARG D 1 168 ? 13.42775  2.49618   2.18947   1.000 116.97248 ? 168 ARG D NE  1 
ATOM 6268 C CZ  . ARG D 1 168 ? 14.30249  3.30386   2.77592   1.000 116.25108 ? 168 ARG D CZ  1 
ATOM 6269 N NH1 . ARG D 1 168 ? 14.04383  3.88031   3.93586   1.000 116.26288 ? 168 ARG D NH1 1 
ATOM 6270 N NH2 . ARG D 1 168 ? 15.46501  3.54468   2.17971   1.000 117.58173 ? 168 ARG D NH2 1 
ATOM 6271 N N   . ASP D 1 169 ? 12.36254  -1.08111  6.14724   1.000 114.47078 ? 169 ASP D N   1 
ATOM 6272 C CA  . ASP D 1 169 ? 13.24909  -1.08795  7.30732   1.000 110.64377 ? 169 ASP D CA  1 
ATOM 6273 C C   . ASP D 1 169 ? 12.83876  -2.13125  8.33689   1.000 110.07735 ? 169 ASP D C   1 
ATOM 6274 O O   . ASP D 1 169 ? 13.57471  -2.36322  9.30044   1.000 107.72997 ? 169 ASP D O   1 
ATOM 6275 C CB  . ASP D 1 169 ? 13.30139  0.29510   7.96727   1.000 105.93175 ? 169 ASP D CB  1 
ATOM 6276 N N   . MET D 1 170 ? 11.69750  -2.79359  8.12861   1.000 110.00212 ? 170 MET D N   1 
ATOM 6277 C CA  . MET D 1 170 ? 11.18540  -3.77249  9.08754   1.000 106.55655 ? 170 MET D CA  1 
ATOM 6278 C C   . MET D 1 170 ? 11.79403  -5.12268  8.75470   1.000 104.09982 ? 170 MET D C   1 
ATOM 6279 O O   . MET D 1 170 ? 11.28628  -5.87777  7.92979   1.000 104.73335 ? 170 MET D O   1 
ATOM 6280 C CB  . MET D 1 170 ? 9.66307   -3.80540  9.08422   1.000 110.07789 ? 170 MET D CB  1 
ATOM 6281 C CG  . MET D 1 170 ? 9.01353   -2.56322  9.72066   1.000 112.88992 ? 170 MET D CG  1 
ATOM 6282 S SD  . MET D 1 170 ? 9.40250   -2.31895  11.47850  1.000 119.30994 ? 170 MET D SD  1 
ATOM 6283 C CE  . MET D 1 170 ? 10.55660  -0.94008  11.43676  1.000 108.24026 ? 170 MET D CE  1 
ATOM 6284 N N   . THR D 1 171 ? 12.90140  -5.41636  9.42444   1.000 106.53240 ? 171 THR D N   1 
ATOM 6285 C CA  . THR D 1 171 ? 13.69522  -6.61484  9.21966   1.000 106.84245 ? 171 THR D CA  1 
ATOM 6286 C C   . THR D 1 171 ? 13.32090  -7.75827  10.15503  1.000 108.87044 ? 171 THR D C   1 
ATOM 6287 O O   . THR D 1 171 ? 13.86780  -8.85612  10.00859  1.000 106.78514 ? 171 THR D O   1 
ATOM 6288 C CB  . THR D 1 171 ? 15.17480  -6.26069  9.40077   1.000 103.35758 ? 171 THR D CB  1 
ATOM 6289 O OG1 . THR D 1 171 ? 15.39376  -5.78728  10.73556  1.000 101.54811 ? 171 THR D OG1 1 
ATOM 6290 C CG2 . THR D 1 171 ? 15.55925  -5.15410  8.43900   1.000 103.10247 ? 171 THR D CG2 1 
ATOM 6291 N N   . THR D 1 172 ? 12.41326  -7.52291  11.10949  1.000 119.20304 ? 172 THR D N   1 
ATOM 6292 C CA  . THR D 1 172 ? 12.05682  -8.47319  12.16117  1.000 118.96922 ? 172 THR D CA  1 
ATOM 6293 C C   . THR D 1 172 ? 10.54564  -8.65064  12.24749  1.000 119.59654 ? 172 THR D C   1 
ATOM 6294 O O   . THR D 1 172 ? 9.78333   -7.68195  12.15468  1.000 117.91409 ? 172 THR D O   1 
ATOM 6295 C CB  . THR D 1 172 ? 12.57173  -8.01517  13.52003  1.000 114.00464 ? 172 THR D CB  1 
ATOM 6296 O OG1 . THR D 1 172 ? 12.07715  -6.69500  13.77633  1.000 112.22115 ? 172 THR D OG1 1 
ATOM 6297 C CG2 . THR D 1 172 ? 14.09617  -8.02453  13.56292  1.000 111.34199 ? 172 THR D CG2 1 
ATOM 6298 N N   . CYS D 1 173 ? 10.12639  -9.88627  12.47253  1.000 117.33636 ? 173 CYS D N   1 
ATOM 6299 C CA  . CYS D 1 173 ? 8.74035   -10.31462 12.47740  1.000 117.44482 ? 173 CYS D CA  1 
ATOM 6300 C C   . CYS D 1 173 ? 8.27586   -10.65487 13.89367  1.000 123.17648 ? 173 CYS D C   1 
ATOM 6301 O O   . CYS D 1 173 ? 9.08131   -11.07621 14.73086  1.000 122.17153 ? 173 CYS D O   1 
ATOM 6302 C CB  . CYS D 1 173 ? 8.58859   -11.54177 11.57275  1.000 113.64716 ? 173 CYS D CB  1 
ATOM 6303 S SG  . CYS D 1 173 ? 6.94863   -12.24027 11.45314  1.000 109.72115 ? 173 CYS D SG  1 
ATOM 6304 N N   . PRO D 1 174 ? 6.99731   -10.44345 14.20752  1.000 124.17385 ? 174 PRO D N   1 
ATOM 6305 C CA  . PRO D 1 174 ? 6.43381   -10.95833 15.45994  1.000 123.40689 ? 174 PRO D CA  1 
ATOM 6306 C C   . PRO D 1 174 ? 5.93143   -12.39034 15.31001  1.000 125.19643 ? 174 PRO D C   1 
ATOM 6307 O O   . PRO D 1 174 ? 5.56794   -12.84516 14.22414  1.000 126.71782 ? 174 PRO D O   1 
ATOM 6308 C CB  . PRO D 1 174 ? 5.26555   -9.99878  15.73444  1.000 122.81799 ? 174 PRO D CB  1 
ATOM 6309 C CG  . PRO D 1 174 ? 4.82543   -9.57807  14.38278  1.000 123.33487 ? 174 PRO D CG  1 
ATOM 6310 C CD  . PRO D 1 174 ? 6.08098   -9.49971  13.54090  1.000 122.31064 ? 174 PRO D CD  1 
ATOM 6311 N N   . LEU D 1 175 ? 5.88571   -13.09098 16.43630  1.000 127.90970 ? 175 LEU D N   1 
ATOM 6312 C CA  . LEU D 1 175 ? 5.54562   -14.50497 16.47116  1.000 129.36830 ? 175 LEU D CA  1 
ATOM 6313 C C   . LEU D 1 175 ? 4.23463   -14.75882 17.22212  1.000 129.11263 ? 175 LEU D C   1 
ATOM 6314 O O   . LEU D 1 175 ? 3.76809   -13.90493 17.98826  1.000 128.72938 ? 175 LEU D O   1 
ATOM 6315 C CB  . LEU D 1 175 ? 6.69051   -15.29719 17.12141  1.000 124.74569 ? 175 LEU D CB  1 
ATOM 6316 N N   . PRO D 1 176 ? 3.58597   -15.92163 16.99282  1.000 129.23824 ? 176 PRO D N   1 
ATOM 6317 C CA  . PRO D 1 176 ? 2.41639   -16.31575 17.79277  1.000 128.12233 ? 176 PRO D CA  1 
ATOM 6318 C C   . PRO D 1 176 ? 2.79193   -16.77340 19.19726  1.000 126.34911 ? 176 PRO D C   1 
ATOM 6319 O O   . PRO D 1 176 ? 3.82108   -17.43452 19.35096  1.000 125.89083 ? 176 PRO D O   1 
ATOM 6320 C CB  . PRO D 1 176 ? 1.81323   -17.47673 16.99154  1.000 126.56574 ? 176 PRO D CB  1 
ATOM 6321 C CG  . PRO D 1 176 ? 2.95458   -18.04185 16.22831  1.000 125.87151 ? 176 PRO D CG  1 
ATOM 6322 C CD  . PRO D 1 176 ? 3.83928   -16.87006 15.89034  1.000 128.43518 ? 176 PRO D CD  1 
ATOM 6323 N N   . VAL D 1 184 ? 17.98433  -18.51144 24.77627  1.000 115.97212 ? 184 VAL D N   1 
ATOM 6324 C CA  . VAL D 1 184 ? 19.31503  -17.99538 25.07966  1.000 115.34127 ? 184 VAL D CA  1 
ATOM 6325 C C   . VAL D 1 184 ? 19.77904  -17.06476 23.96384  1.000 113.31160 ? 184 VAL D C   1 
ATOM 6326 O O   . VAL D 1 184 ? 19.73350  -17.41906 22.79311  1.000 116.12284 ? 184 VAL D O   1 
ATOM 6327 C CB  . VAL D 1 184 ? 20.31583  -19.14023 25.29922  1.000 113.31838 ? 184 VAL D CB  1 
ATOM 6328 N N   . ALA D 1 185 ? 20.23086  -15.86957 24.34032  1.000 109.46091 ? 185 ALA D N   1 
ATOM 6329 C CA  . ALA D 1 185 ? 20.48292  -14.82476 23.35027  1.000 114.06127 ? 185 ALA D CA  1 
ATOM 6330 C C   . ALA D 1 185 ? 21.75283  -15.08511 22.54989  1.000 114.96034 ? 185 ALA D C   1 
ATOM 6331 O O   . ALA D 1 185 ? 21.78562  -14.86177 21.33467  1.000 115.78525 ? 185 ALA D O   1 
ATOM 6332 C CB  . ALA D 1 185 ? 20.56934  -13.46112 24.03640  1.000 114.44174 ? 185 ALA D CB  1 
ATOM 6333 N N   . HIS D 1 186 ? 22.81307  -15.53681 23.21195  1.000 114.15947 ? 186 HIS D N   1 
ATOM 6334 C CA  . HIS D 1 186 ? 24.14104  -15.58214 22.62115  1.000 112.49650 ? 186 HIS D CA  1 
ATOM 6335 C C   . HIS D 1 186 ? 24.45858  -16.94287 22.03014  1.000 112.89545 ? 186 HIS D C   1 
ATOM 6336 O O   . HIS D 1 186 ? 25.63333  -17.31074 21.91547  1.000 113.06331 ? 186 HIS D O   1 
ATOM 6337 C CB  . HIS D 1 186 ? 25.16174  -15.18082 23.67527  1.000 109.47410 ? 186 HIS D CB  1 
ATOM 6338 C CG  . HIS D 1 186 ? 24.80345  -13.90139 24.35467  1.000 109.93955 ? 186 HIS D CG  1 
ATOM 6339 N ND1 . HIS D 1 186 ? 24.92623  -12.67321 23.74215  1.000 109.39200 ? 186 HIS D ND1 1 
ATOM 6340 C CD2 . HIS D 1 186 ? 24.25302  -13.66550 25.57010  1.000 110.55110 ? 186 HIS D CD2 1 
ATOM 6341 C CE1 . HIS D 1 186 ? 24.50122  -11.73185 24.56689  1.000 112.03570 ? 186 HIS D CE1 1 
ATOM 6342 N NE2 . HIS D 1 186 ? 24.08660  -12.30714 25.68297  1.000 112.08985 ? 186 HIS D NE2 1 
ATOM 6343 N N   . ASP D 1 187 ? 23.42609  -17.70011 21.68311  1.000 110.27722 ? 187 ASP D N   1 
ATOM 6344 C CA  . ASP D 1 187 ? 23.54962  -18.94167 20.94008  1.000 109.98846 ? 187 ASP D CA  1 
ATOM 6345 C C   . ASP D 1 187 ? 23.20608  -18.68144 19.48230  1.000 108.94851 ? 187 ASP D C   1 
ATOM 6346 O O   . ASP D 1 187 ? 22.18298  -18.05770 19.18539  1.000 110.82720 ? 187 ASP D O   1 
ATOM 6347 C CB  . ASP D 1 187 ? 22.62660  -20.00955 21.52233  1.000 112.86146 ? 187 ASP D CB  1 
ATOM 6348 C CG  . ASP D 1 187 ? 22.79234  -21.34866 20.84758  1.000 113.42661 ? 187 ASP D CG  1 
ATOM 6349 O OD1 . ASP D 1 187 ? 23.58265  -21.43468 19.88047  1.000 111.40868 ? 187 ASP D OD1 1 
ATOM 6350 O OD2 . ASP D 1 187 ? 22.13393  -22.31811 21.28463  1.000 111.37523 ? 187 ASP D OD2 1 
ATOM 6351 N N   . SER D 1 188 ? 24.06468  -19.16749 18.58149  1.000 107.50050 ? 188 SER D N   1 
ATOM 6352 C CA  . SER D 1 188 ? 23.87766  -18.97539 17.14658  1.000 102.95477 ? 188 SER D CA  1 
ATOM 6353 C C   . SER D 1 188 ? 22.78309  -19.86621 16.57904  1.000 107.83790 ? 188 SER D C   1 
ATOM 6354 O O   . SER D 1 188 ? 22.22055  -19.54003 15.52746  1.000 104.48171 ? 188 SER D O   1 
ATOM 6355 C CB  . SER D 1 188 ? 25.18090  -19.26290 16.41528  1.000 91.50484  ? 188 SER D CB  1 
ATOM 6356 O OG  . SER D 1 188 ? 26.20692  -18.45045 16.93348  1.000 92.51856  ? 188 SER D OG  1 
ATOM 6357 N N   . ILE D 1 189 ? 22.50630  -21.00417 17.22526  1.000 108.30563 ? 189 ILE D N   1 
ATOM 6358 C CA  . ILE D 1 189 ? 21.39395  -21.85221 16.80937  1.000 107.96057 ? 189 ILE D CA  1 
ATOM 6359 C C   . ILE D 1 189 ? 20.07094  -21.20346 17.18236  1.000 111.37337 ? 189 ILE D C   1 
ATOM 6360 O O   . ILE D 1 189 ? 19.08683  -21.28362 16.43628  1.000 110.99864 ? 189 ILE D O   1 
ATOM 6361 C CB  . ILE D 1 189 ? 21.52825  -23.25645 17.42277  1.000 105.11891 ? 189 ILE D CB  1 
ATOM 6362 C CG1 . ILE D 1 189 ? 22.83076  -23.92248 16.97547  1.000 104.56690 ? 189 ILE D CG1 1 
ATOM 6363 C CG2 . ILE D 1 189 ? 20.35339  -24.11755 17.01429  1.000 106.77088 ? 189 ILE D CG2 1 
ATOM 6364 C CD1 . ILE D 1 189 ? 22.92915  -24.16898 15.45474  1.000 103.86718 ? 189 ILE D CD1 1 
ATOM 6365 N N   . HIS D 1 190 ? 20.02214  -20.55716 18.34662  1.000 120.02479 ? 190 HIS D N   1 
ATOM 6366 C CA  . HIS D 1 190 ? 18.83553  -19.78974 18.69724  1.000 123.72946 ? 190 HIS D CA  1 
ATOM 6367 C C   . HIS D 1 190 ? 18.62926  -18.63732 17.72896  1.000 123.77117 ? 190 HIS D C   1 
ATOM 6368 O O   . HIS D 1 190 ? 17.48775  -18.30334 17.38648  1.000 124.28816 ? 190 HIS D O   1 
ATOM 6369 C CB  . HIS D 1 190 ? 18.92936  -19.27169 20.13274  1.000 125.17101 ? 190 HIS D CB  1 
ATOM 6370 C CG  . HIS D 1 190 ? 18.75739  -20.33581 21.17103  1.000 127.00382 ? 190 HIS D CG  1 
ATOM 6371 N ND1 . HIS D 1 190 ? 18.85380  -20.07868 22.52144  1.000 124.25040 ? 190 HIS D ND1 1 
ATOM 6372 C CD2 . HIS D 1 190 ? 18.50934  -21.66249 21.05428  1.000 128.19510 ? 190 HIS D CD2 1 
ATOM 6373 C CE1 . HIS D 1 190 ? 18.66022  -21.19985 23.19220  1.000 126.16941 ? 190 HIS D CE1 1 
ATOM 6374 N NE2 . HIS D 1 190 ? 18.45259  -22.17640 22.32558  1.000 128.00869 ? 190 HIS D NE2 1 
ATOM 6375 N N   . ASP D 1 191 ? 19.72598  -18.01878 17.27805  1.000 116.49372 ? 191 ASP D N   1 
ATOM 6376 C CA  . ASP D 1 191 ? 19.63122  -16.92863 16.31191  1.000 110.84330 ? 191 ASP D CA  1 
ATOM 6377 C C   . ASP D 1 191 ? 18.96679  -17.40126 15.02134  1.000 107.27464 ? 191 ASP D C   1 
ATOM 6378 O O   . ASP D 1 191 ? 18.03832  -16.75599 14.52137  1.000 107.05095 ? 191 ASP D O   1 
ATOM 6379 C CB  . ASP D 1 191 ? 21.02674  -16.35824 16.04174  1.000 109.55457 ? 191 ASP D CB  1 
ATOM 6380 C CG  . ASP D 1 191 ? 20.99226  -15.03646 15.27436  1.000 115.39295 ? 191 ASP D CG  1 
ATOM 6381 O OD1 . ASP D 1 191 ? 20.58182  -14.02448 15.88791  1.000 122.89294 ? 191 ASP D OD1 1 
ATOM 6382 O OD2 . ASP D 1 191 ? 21.39862  -14.99497 14.08112  1.000 106.63014 ? 191 ASP D OD2 1 
ATOM 6383 N N   . CYS D 1 192 ? 19.40218  -18.55354 14.48931  1.000 107.59400 ? 192 CYS D N   1 
ATOM 6384 C CA  . CYS D 1 192 ? 18.85566  -19.04634 13.22449  1.000 105.23937 ? 192 CYS D CA  1 
ATOM 6385 C C   . CYS D 1 192 ? 17.37763  -19.38705 13.34722  1.000 107.15552 ? 192 CYS D C   1 
ATOM 6386 O O   . CYS D 1 192 ? 16.57160  -19.01357 12.48599  1.000 106.24748 ? 192 CYS D O   1 
ATOM 6387 C CB  . CYS D 1 192 ? 19.63430  -20.26887 12.73522  1.000 103.89970 ? 192 CYS D CB  1 
ATOM 6388 S SG  . CYS D 1 192 ? 21.29015  -19.92660 12.07798  1.000 103.43390 ? 192 CYS D SG  1 
ATOM 6389 N N   . ALA D 1 193 ? 17.00315  -20.10547 14.40891  1.000 108.80660 ? 193 ALA D N   1 
ATOM 6390 C CA  . ALA D 1 193 ? 15.62265  -20.55334 14.53915  1.000 103.28784 ? 193 ALA D CA  1 
ATOM 6391 C C   . ALA D 1 193 ? 14.66906  -19.37110 14.65732  1.000 99.77545  ? 193 ALA D C   1 
ATOM 6392 O O   . ALA D 1 193 ? 13.60139  -19.36604 14.03713  1.000 99.32435  ? 193 ALA D O   1 
ATOM 6393 C CB  . ALA D 1 193 ? 15.49257  -21.49311 15.73224  1.000 111.35824 ? 193 ALA D CB  1 
ATOM 6394 N N   . LYS D 1 194 ? 15.04256  -18.34760 15.42756  1.000 102.60389 ? 194 LYS D N   1 
ATOM 6395 C CA  . LYS D 1 194 ? 14.22862  -17.13533 15.46757  1.000 99.14031  ? 194 LYS D CA  1 
ATOM 6396 C C   . LYS D 1 194 ? 14.14352  -16.47129 14.09042  1.000 106.42205 ? 194 LYS D C   1 
ATOM 6397 O O   . LYS D 1 194 ? 13.11554  -15.87093 13.75048  1.000 106.00310 ? 194 LYS D O   1 
ATOM 6398 C CB  . LYS D 1 194 ? 14.77772  -16.16297 16.51073  1.000 91.24935  ? 194 LYS D CB  1 
ATOM 6399 N N   . ASP D 1 195 ? 15.21886  -16.55015 13.28772  1.000 102.54004 ? 195 ASP D N   1 
ATOM 6400 C CA  . ASP D 1 195 ? 15.13171  -16.13638 11.88439  1.000 99.00443  ? 195 ASP D CA  1 
ATOM 6401 C C   . ASP D 1 195 ? 14.24985  -17.08385 11.07128  1.000 100.71909 ? 195 ASP D C   1 
ATOM 6402 O O   . ASP D 1 195 ? 13.32131  -16.63693 10.38643  1.000 103.37170 ? 195 ASP D O   1 
ATOM 6403 C CB  . ASP D 1 195 ? 16.52615  -16.04147 11.24984  1.000 97.26082  ? 195 ASP D CB  1 
ATOM 6404 C CG  . ASP D 1 195 ? 17.24466  -14.72606 11.55592  1.000 96.70778  ? 195 ASP D CG  1 
ATOM 6405 O OD1 . ASP D 1 195 ? 16.56321  -13.68363 11.70416  1.000 94.52288  ? 195 ASP D OD1 1 
ATOM 6406 O OD2 . ASP D 1 195 ? 18.49923  -14.74259 11.62224  1.000 92.40273  ? 195 ASP D OD2 1 
ATOM 6407 N N   . ILE D 1 196 ? 14.51274  -18.39779 11.13953  1.000 99.06890  ? 196 ILE D N   1 
ATOM 6408 C CA  . ILE D 1 196 ? 13.75145  -19.34430 10.31988  1.000 101.35455 ? 196 ILE D CA  1 
ATOM 6409 C C   . ILE D 1 196 ? 12.26811  -19.24920 10.64013  1.000 107.44271 ? 196 ILE D C   1 
ATOM 6410 O O   . ILE D 1 196 ? 11.41729  -19.52442 9.78044   1.000 110.06727 ? 196 ILE D O   1 
ATOM 6411 C CB  . ILE D 1 196 ? 14.24980  -20.79215 10.50876  1.000 101.64821 ? 196 ILE D CB  1 
ATOM 6412 C CG1 . ILE D 1 196 ? 15.72482  -20.92320 10.17160  1.000 101.95709 ? 196 ILE D CG1 1 
ATOM 6413 C CG2 . ILE D 1 196 ? 13.48275  -21.74490 9.60280   1.000 101.37815 ? 196 ILE D CG2 1 
ATOM 6414 C CD1 . ILE D 1 196 ? 16.28494  -22.26178 10.55972  1.000 106.21315 ? 196 ILE D CD1 1 
ATOM 6415 N N   . LEU D 1 197 ? 11.93069  -18.87062 11.87779  1.000 102.39844 ? 197 LEU D N   1 
ATOM 6416 C CA  . LEU D 1 197 ? 10.52803  -18.73976 12.24834  1.000 106.84991 ? 197 LEU D CA  1 
ATOM 6417 C C   . LEU D 1 197 ? 9.94992   -17.40726 11.79762  1.000 112.36708 ? 197 LEU D C   1 
ATOM 6418 O O   . LEU D 1 197 ? 8.86211   -17.37571 11.21483  1.000 120.23062 ? 197 LEU D O   1 
ATOM 6419 C CB  . LEU D 1 197 ? 10.33144  -18.91810 13.75916  1.000 106.97777 ? 197 LEU D CB  1 
ATOM 6420 C CG  . LEU D 1 197 ? 10.54665  -20.31164 14.36786  1.000 107.06762 ? 197 LEU D CG  1 
ATOM 6421 C CD1 . LEU D 1 197 ? 10.27397  -20.29461 15.86830  1.000 108.06919 ? 197 LEU D CD1 1 
ATOM 6422 C CD2 . LEU D 1 197 ? 9.73490   -21.39720 13.65330  1.000 103.87742 ? 197 LEU D CD2 1 
ATOM 6423 N N   . MET D 1 198 ? 10.64725  -16.29476 12.06409  1.000 111.06559 ? 198 MET D N   1 
ATOM 6424 C CA  . MET D 1 198 ? 10.09688  -14.99713 11.67937  1.000 110.67596 ? 198 MET D CA  1 
ATOM 6425 C C   . MET D 1 198 ? 9.72172   -14.97242 10.20472  1.000 117.63353 ? 198 MET D C   1 
ATOM 6426 O O   . MET D 1 198 ? 8.67739   -14.42626 9.83620   1.000 123.52707 ? 198 MET D O   1 
ATOM 6427 C CB  . MET D 1 198 ? 11.07258  -13.85998 11.96764  1.000 107.63020 ? 198 MET D CB  1 
ATOM 6428 C CG  . MET D 1 198 ? 11.29886  -13.52812 13.40552  1.000 105.97877 ? 198 MET D CG  1 
ATOM 6429 S SD  . MET D 1 198 ? 12.08883  -11.90706 13.51093  1.000 117.08121 ? 198 MET D SD  1 
ATOM 6430 C CE  . MET D 1 198 ? 13.69266  -12.22875 12.76993  1.000 110.01344 ? 198 MET D CE  1 
ATOM 6431 N N   . MET D 1 199 ? 10.55665  -15.56634 9.34455   1.000 115.53563 ? 199 MET D N   1 
ATOM 6432 C CA  . MET D 1 199 ? 10.24054  -15.60519 7.91917   1.000 118.34712 ? 199 MET D CA  1 
ATOM 6433 C C   . MET D 1 199 ? 9.08407   -16.55826 7.63889   1.000 120.29512 ? 199 MET D C   1 
ATOM 6434 O O   . MET D 1 199 ? 8.13591   -16.20220 6.92771   1.000 121.70543 ? 199 MET D O   1 
ATOM 6435 C CB  . MET D 1 199 ? 11.47979  -15.99890 7.10807   1.000 116.32048 ? 199 MET D CB  1 
ATOM 6436 N N   . LYS D 1 200 ? 9.13840   -17.77413 8.20034   1.000 120.98590 ? 200 LYS D N   1 
ATOM 6437 C CA  . LYS D 1 200 ? 8.06048   -18.73795 7.98441   1.000 123.54427 ? 200 LYS D CA  1 
ATOM 6438 C C   . LYS D 1 200 ? 6.73096   -18.21225 8.50746   1.000 126.80713 ? 200 LYS D C   1 
ATOM 6439 O O   . LYS D 1 200 ? 5.67252   -18.57254 7.97974   1.000 127.41413 ? 200 LYS D O   1 
ATOM 6440 C CB  . LYS D 1 200 ? 8.40027   -20.07716 8.64029   1.000 117.48799 ? 200 LYS D CB  1 
ATOM 6441 N N   . TYR D 1 201 ? 6.76914   -17.36866 9.54567   1.000 140.86278 ? 201 TYR D N   1 
ATOM 6442 C CA  . TYR D 1 201 ? 5.57681   -16.68623 10.04426  1.000 140.94034 ? 201 TYR D CA  1 
ATOM 6443 C C   . TYR D 1 201 ? 5.21106   -15.48542 9.17919   1.000 141.62170 ? 201 TYR D C   1 
ATOM 6444 O O   . TYR D 1 201 ? 4.02501   -15.17367 9.01604   1.000 142.27985 ? 201 TYR D O   1 
ATOM 6445 C CB  . TYR D 1 201 ? 5.78668   -16.24490 11.49718  1.000 140.33299 ? 201 TYR D CB  1 
ATOM 6446 N N   . ALA D 1 202 ? 6.21553   -14.78097 8.64755   1.000 131.07156 ? 202 ALA D N   1 
ATOM 6447 C CA  . ALA D 1 202 ? 5.94413   -13.70659 7.69836   1.000 123.56851 ? 202 ALA D CA  1 
ATOM 6448 C C   . ALA D 1 202 ? 5.37236   -14.25841 6.40295   1.000 124.22969 ? 202 ALA D C   1 
ATOM 6449 O O   . ALA D 1 202 ? 4.44039   -13.67850 5.83870   1.000 126.76555 ? 202 ALA D O   1 
ATOM 6450 C CB  . ALA D 1 202 ? 7.21229   -12.90434 7.42533   1.000 114.89035 ? 202 ALA D CB  1 
ATOM 6451 N N   . LEU D 1 203 ? 5.90616   -15.38935 5.92890   1.000 123.14778 ? 203 LEU D N   1 
ATOM 6452 C CA  . LEU D 1 203 ? 5.40584   -15.99358 4.69695   1.000 123.46785 ? 203 LEU D CA  1 
ATOM 6453 C C   . LEU D 1 203 ? 3.94436   -16.39897 4.83216   1.000 130.15271 ? 203 LEU D C   1 
ATOM 6454 O O   . LEU D 1 203 ? 3.14715   -16.19148 3.90934   1.000 130.23159 ? 203 LEU D O   1 
ATOM 6455 C CB  . LEU D 1 203 ? 6.25683   -17.20478 4.31998   1.000 117.84964 ? 203 LEU D CB  1 
ATOM 6456 N N   . ARG D 1 204 ? 3.57341   -16.98615 5.97393   1.000 133.25414 ? 204 ARG D N   1 
ATOM 6457 C CA  . ARG D 1 204 ? 2.17300   -17.32984 6.20162   1.000 132.11526 ? 204 ARG D CA  1 
ATOM 6458 C C   . ARG D 1 204 ? 1.30322   -16.07837 6.24719   1.000 133.19905 ? 204 ARG D C   1 
ATOM 6459 O O   . ARG D 1 204 ? 0.22318   -16.04309 5.64615   1.000 132.88430 ? 204 ARG D O   1 
ATOM 6460 C CB  . ARG D 1 204 ? 2.03347   -18.13865 7.49236   1.000 129.92164 ? 204 ARG D CB  1 
ATOM 6461 N N   . TYR D 1 205 ? 1.76352   -15.03425 6.94460   1.000 132.45853 ? 205 TYR D N   1 
ATOM 6462 C CA  . TYR D 1 205 ? 1.02210   -13.77763 6.96051   1.000 131.00896 ? 205 TYR D CA  1 
ATOM 6463 C C   . TYR D 1 205 ? 0.97928   -13.14928 5.57389   1.000 133.21693 ? 205 TYR D C   1 
ATOM 6464 O O   . TYR D 1 205 ? -0.05954  -12.62872 5.15499   1.000 133.40071 ? 205 TYR D O   1 
ATOM 6465 C CB  . TYR D 1 205 ? 1.63420   -12.81217 7.97533   1.000 126.62043 ? 205 TYR D CB  1 
ATOM 6466 N N   . ALA D 1 206 ? 2.09545   -13.20114 4.83909   1.000 139.40765 ? 206 ALA D N   1 
ATOM 6467 C CA  . ALA D 1 206 ? 2.12971   -12.62964 3.49191   1.000 139.19267 ? 206 ALA D CA  1 
ATOM 6468 C C   . ALA D 1 206 ? 1.22870   -13.38942 2.52633   1.000 139.65466 ? 206 ALA D C   1 
ATOM 6469 O O   . ALA D 1 206 ? 0.71902   -12.79761 1.56934   1.000 139.13187 ? 206 ALA D O   1 
ATOM 6470 C CB  . ALA D 1 206 ? 3.56393   -12.58997 2.95457   1.000 134.89237 ? 206 ALA D CB  1 
ATOM 6471 N N   . MET D 1 207 ? 1.02896   -14.68945 2.74462   1.000 135.40889 ? 207 MET D N   1 
ATOM 6472 C CA  . MET D 1 207 ? 0.06244   -15.44976 1.96292   1.000 135.37537 ? 207 MET D CA  1 
ATOM 6473 C C   . MET D 1 207 ? -1.33415  -15.45781 2.58483   1.000 142.20626 ? 207 MET D C   1 
ATOM 6474 O O   . MET D 1 207 ? -2.27938  -15.90318 1.92297   1.000 139.33680 ? 207 MET D O   1 
ATOM 6475 C CB  . MET D 1 207 ? 0.55434   -16.88876 1.76249   1.000 130.27109 ? 207 MET D CB  1 
ATOM 6476 N N   . GLY D 1 208 ? -1.48745  -14.96978 3.82930   1.000 154.02858 ? 208 GLY D N   1 
ATOM 6477 C CA  . GLY D 1 208 ? -2.78536  -14.68140 4.42486   1.000 152.16893 ? 208 GLY D CA  1 
ATOM 6478 C C   . GLY D 1 208 ? -3.30431  -15.64164 5.48409   1.000 153.27390 ? 208 GLY D C   1 
ATOM 6479 O O   . GLY D 1 208 ? -4.36358  -15.37038 6.07003   1.000 154.30539 ? 208 GLY D O   1 
ATOM 6480 N N   . LEU D 1 209 ? -2.60543  -16.74787 5.75328   1.000 139.78028 ? 209 LEU D N   1 
ATOM 6481 C CA  . LEU D 1 209 ? -3.06723  -17.69136 6.76876   1.000 134.09793 ? 209 LEU D CA  1 
ATOM 6482 C C   . LEU D 1 209 ? -2.79462  -17.20569 8.19248   1.000 129.66799 ? 209 LEU D C   1 
ATOM 6483 O O   . LEU D 1 209 ? -3.60765  -17.44486 9.09202   1.000 126.21643 ? 209 LEU D O   1 
ATOM 6484 C CB  . LEU D 1 209 ? -2.41812  -19.06209 6.53980   1.000 129.05729 ? 209 LEU D CB  1 
ATOM 6485 N N   . GLU D 1 210 ? -1.68219  -16.51814 8.41846   1.000 130.80894 ? 210 GLU D N   1 
ATOM 6486 C CA  . GLU D 1 210 ? -1.26632  -16.19630 9.77392   1.000 132.04296 ? 210 GLU D CA  1 
ATOM 6487 C C   . GLU D 1 210 ? -2.09387  -15.05022 10.34425  1.000 134.42168 ? 210 GLU D C   1 
ATOM 6488 O O   . GLU D 1 210 ? -2.40272  -14.07457 9.65143   1.000 130.72281 ? 210 GLU D O   1 
ATOM 6489 C CB  . GLU D 1 210 ? 0.22265   -15.83819 9.80828   1.000 130.56535 ? 210 GLU D CB  1 
ATOM 6490 N N   . ASP D 1 211 ? -2.47657  -15.19458 11.61075  1.000 140.70291 ? 211 ASP D N   1 
ATOM 6491 C CA  . ASP D 1 211 ? -3.12300  -14.12523 12.34960  1.000 141.18349 ? 211 ASP D CA  1 
ATOM 6492 C C   . ASP D 1 211 ? -2.08056  -13.12142 12.82558  1.000 141.25985 ? 211 ASP D C   1 
ATOM 6493 O O   . ASP D 1 211 ? -0.88549  -13.42140 12.91208  1.000 142.26027 ? 211 ASP D O   1 
ATOM 6494 C CB  . ASP D 1 211 ? -3.90107  -14.68211 13.54505  1.000 142.07420 ? 211 ASP D CB  1 
ATOM 6495 N N   . ALA D 1 212 ? -2.54962  -11.91593 13.13239  1.000 138.62361 ? 212 ALA D N   1 
ATOM 6496 C CA  . ALA D 1 212 ? -1.67761  -10.88581 13.68083  1.000 137.46081 ? 212 ALA D CA  1 
ATOM 6497 C C   . ALA D 1 212 ? -1.40613  -11.16860 15.15466  1.000 139.67277 ? 212 ALA D C   1 
ATOM 6498 O O   . ALA D 1 212 ? -2.34960  -11.37448 15.92616  1.000 142.67111 ? 212 ALA D O   1 
ATOM 6499 C CB  . ALA D 1 212 ? -2.30243  -9.50480  13.51859  1.000 134.78057 ? 212 ALA D CB  1 
ATOM 6500 N N   . PRO D 1 213 ? -0.14640  -11.21083 15.57637  1.000 138.28779 ? 213 PRO D N   1 
ATOM 6501 C CA  . PRO D 1 213 ? 0.14806   -11.36370 17.00727  1.000 139.41012 ? 213 PRO D CA  1 
ATOM 6502 C C   . PRO D 1 213 ? -0.45594  -10.22486 17.81598  1.000 140.43083 ? 213 PRO D C   1 
ATOM 6503 O O   . PRO D 1 213 ? -0.93189  -9.22196  17.28023  1.000 139.41927 ? 213 PRO D O   1 
ATOM 6504 C CB  . PRO D 1 213 ? 1.67897   -11.34711 17.06269  1.000 136.96278 ? 213 PRO D CB  1 
ATOM 6505 C CG  . PRO D 1 213 ? 2.10029   -11.78310 15.69175  1.000 139.56997 ? 213 PRO D CG  1 
ATOM 6506 C CD  . PRO D 1 213 ? 1.07165   -11.22296 14.75174  1.000 138.59033 ? 213 PRO D CD  1 
ATOM 6507 N N   . SER D 1 214 ? -0.42291  -10.38811 19.13721  1.000 141.45309 ? 214 SER D N   1 
ATOM 6508 C CA  . SER D 1 214 ? -1.07381  -9.44279  20.03239  1.000 136.38910 ? 214 SER D CA  1 
ATOM 6509 C C   . SER D 1 214 ? -0.49768  -8.02901  19.86051  1.000 132.20567 ? 214 SER D C   1 
ATOM 6510 O O   . SER D 1 214 ? 0.56831   -7.81652  19.26919  1.000 128.40058 ? 214 SER D O   1 
ATOM 6511 C CB  . SER D 1 214 ? -0.94837  -9.92391  21.47873  1.000 133.23267 ? 214 SER D CB  1 
ATOM 6512 O OG  . SER D 1 214 ? 0.40986   -10.02470 21.86585  1.000 134.46659 ? 214 SER D OG  1 
ATOM 6513 N N   . GLU D 1 215 ? -1.24592  -7.05298  20.37274  1.000 128.81436 ? 215 GLU D N   1 
ATOM 6514 C CA  . GLU D 1 215 ? -0.89956  -5.63738  20.25545  1.000 119.43628 ? 215 GLU D CA  1 
ATOM 6515 C C   . GLU D 1 215 ? 0.38776   -5.29748  21.00532  1.000 114.10122 ? 215 GLU D C   1 
ATOM 6516 O O   . GLU D 1 215 ? 1.48138   -5.69504  20.60317  1.000 112.83888 ? 215 GLU D O   1 
ATOM 6517 C CB  . GLU D 1 215 ? -2.05422  -4.76532  20.77275  1.000 104.39075 ? 215 GLU D CB  1 
ATOM 6518 N N   . ASP D 1 219 ? 6.43436   -17.61403 20.19146  1.000 116.81623 ? 219 ASP D N   1 
ATOM 6519 C CA  . ASP D 1 219 ? 6.86113   -17.03150 21.45697  1.000 116.51436 ? 219 ASP D CA  1 
ATOM 6520 C C   . ASP D 1 219 ? 7.04255   -15.51933 21.31637  1.000 121.10531 ? 219 ASP D C   1 
ATOM 6521 O O   . ASP D 1 219 ? 8.16709   -15.05014 21.22635  1.000 121.75014 ? 219 ASP D O   1 
ATOM 6522 C CB  . ASP D 1 219 ? 8.16636   -17.67581 21.94431  1.000 104.51704 ? 219 ASP D CB  1 
ATOM 6523 N N   . PRO D 1 220 ? 5.93367   -14.74955 21.40361  1.000 129.61317 ? 220 PRO D N   1 
ATOM 6524 C CA  . PRO D 1 220 ? 5.95464   -13.31530 21.04698  1.000 127.65289 ? 220 PRO D CA  1 
ATOM 6525 C C   . PRO D 1 220 ? 6.95002   -12.42616 21.80028  1.000 125.38843 ? 220 PRO D C   1 
ATOM 6526 O O   . PRO D 1 220 ? 6.77327   -11.20091 21.84873  1.000 126.91446 ? 220 PRO D O   1 
ATOM 6527 C CB  . PRO D 1 220 ? 4.50694   -12.87502 21.30771  1.000 128.97880 ? 220 PRO D CB  1 
ATOM 6528 C CG  . PRO D 1 220 ? 3.70064   -14.11025 21.06741  1.000 131.02921 ? 220 PRO D CG  1 
ATOM 6529 C CD  . PRO D 1 220 ? 4.55746   -15.24338 21.59145  1.000 131.74490 ? 220 PRO D CD  1 
ATOM 6530 N N   . LEU D 1 221 ? 7.95297   -13.02680 22.45234  1.000 117.70722 ? 221 LEU D N   1 
ATOM 6531 C CA  . LEU D 1 221 ? 9.14855   -12.28027 22.85308  1.000 119.15144 ? 221 LEU D CA  1 
ATOM 6532 C C   . LEU D 1 221 ? 9.77134   -11.48583 21.69420  1.000 125.31111 ? 221 LEU D C   1 
ATOM 6533 O O   . LEU D 1 221 ? 10.47162  -10.49177 21.93038  1.000 124.28925 ? 221 LEU D O   1 
ATOM 6534 C CB  . LEU D 1 221 ? 10.18044  -13.25197 23.43173  1.000 115.64950 ? 221 LEU D CB  1 
ATOM 6535 N N   . SER D 1 222 ? 9.53247   -11.90314 20.44585  1.000 125.56112 ? 222 SER D N   1 
ATOM 6536 C CA  . SER D 1 222 ? 10.16136  -11.33150 19.24646  1.000 124.16531 ? 222 SER D CA  1 
ATOM 6537 C C   . SER D 1 222 ? 9.62495   -9.92924  18.96351  1.000 123.92327 ? 222 SER D C   1 
ATOM 6538 O O   . SER D 1 222 ? 8.54014   -9.76887  18.40180  1.000 125.47352 ? 222 SER D O   1 
ATOM 6539 C CB  . SER D 1 222 ? 9.92210   -12.25226 18.05119  1.000 122.38541 ? 222 SER D CB  1 
ATOM 6540 O OG  . SER D 1 222 ? 8.54135   -12.36273 17.73179  1.000 121.03440 ? 222 SER D OG  1 
ATOM 6541 N N   . LEU D 1 223 ? 10.39284  -8.90314  19.32327  1.000 123.29437 ? 223 LEU D N   1 
ATOM 6542 C CA  . LEU D 1 223 ? 9.94371   -7.52523  19.18320  1.000 124.76752 ? 223 LEU D CA  1 
ATOM 6543 C C   . LEU D 1 223 ? 11.08079  -6.63047  18.71792  1.000 124.18448 ? 223 LEU D C   1 
ATOM 6544 O O   . LEU D 1 223 ? 12.25444  -6.90591  19.00206  1.000 122.23872 ? 223 LEU D O   1 
ATOM 6545 C CB  . LEU D 1 223 ? 9.38183   -6.98408  20.50944  1.000 127.31089 ? 223 LEU D CB  1 
ATOM 6546 N N   . PRO D 1 224 ? 10.76101  -5.52201  18.02355  1.000 125.02915 ? 224 PRO D N   1 
ATOM 6547 C CA  . PRO D 1 224 ? 11.65131  -4.47181  17.51101  1.000 124.55903 ? 224 PRO D CA  1 
ATOM 6548 C C   . PRO D 1 224 ? 12.46811  -3.79447  18.61392  1.000 121.24061 ? 224 PRO D C   1 
ATOM 6549 O O   . PRO D 1 224 ? 13.30817  -2.94626  18.30913  1.000 118.33162 ? 224 PRO D O   1 
ATOM 6550 C CB  . PRO D 1 224 ? 10.68042  -3.47723  16.86201  1.000 118.01594 ? 224 PRO D CB  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   . MET A 1   ? 1.00247 0.73596 0.78637 0.25031  0.04258  0.10004  1   MET A N   
2    C CA  . MET A 1   ? 1.09180 0.84912 0.90156 0.23590  0.03224  0.09423  1   MET A CA  
3    C C   . MET A 1   ? 0.98246 0.78692 0.84222 0.21549  0.01436  0.08522  1   MET A C   
4    O O   . MET A 1   ? 0.95915 0.80506 0.83855 0.22571  0.00053  0.08081  1   MET A O   
5    C CB  . MET A 1   ? 1.04523 0.81767 0.84091 0.26229  0.02700  0.09581  1   MET A CB  
6    C CG  . MET A 1   ? 1.01272 0.80727 0.83083 0.25013  0.01761  0.08996  1   MET A CG  
7    S SD  . MET A 1   ? 1.18919 1.05452 1.05683 0.24608  -0.00714 0.07819  1   MET A SD  
8    C CE  . MET A 1   ? 0.90823 0.77713 0.78589 0.23396  -0.01000 0.07445  1   MET A CE  
9    N N   . PHE A 2   ? 0.94224 0.74059 0.82117 0.18704  0.01569  0.08194  2   PHE A N   
10   C CA  . PHE A 2   ? 0.93669 0.76824 0.85596 0.16776  0.00325  0.07555  2   PHE A CA  
11   C C   . PHE A 2   ? 0.89473 0.75639 0.84415 0.15646  -0.00858 0.06948  2   PHE A C   
12   O O   . PHE A 2   ? 0.90630 0.76144 0.84756 0.15887  -0.00677 0.06973  2   PHE A O   
13   C CB  . PHE A 2   ? 0.95685 0.76695 0.87888 0.14480  0.01151  0.07550  2   PHE A CB  
14   C CG  . PHE A 2   ? 1.00670 0.79901 0.91238 0.15026  0.01925  0.07878  2   PHE A CG  
15   C CD1 . PHE A 2   ? 1.04375 0.83716 0.93152 0.17607  0.01953  0.08257  2   PHE A CD1 
16   C CD2 . PHE A 2   ? 1.00843 0.78889 0.91972 0.12985  0.02474  0.07717  2   PHE A CD2 
17   C CE1 . PHE A 2   ? 1.07038 0.84749 0.94335 0.18176  0.02696  0.08565  2   PHE A CE1 
18   C CE2 . PHE A 2   ? 1.03711 0.80177 0.93424 0.13391  0.03189  0.07954  2   PHE A CE2 
19   C CZ  . PHE A 2   ? 1.08110 0.84252 0.95884 0.15990  0.03337  0.08411  2   PHE A CZ  
20   N N   . ASP A 3   ? 0.79044 0.68282 0.77375 0.14369  -0.01947 0.06410  3   ASP A N   
21   C CA  . ASP A 3   ? 0.72304 0.63554 0.73506 0.12728  -0.02726 0.05897  3   ASP A CA  
22   C C   . ASP A 3   ? 0.72235 0.62441 0.74525 0.10568  -0.02376 0.05943  3   ASP A C   
23   O O   . ASP A 3   ? 0.77886 0.65988 0.78772 0.10251  -0.01563 0.06253  3   ASP A O   
24   C CB  . ASP A 3   ? 0.71221 0.66458 0.75214 0.12852  -0.03983 0.05206  3   ASP A CB  
25   C CG  . ASP A 3   ? 0.79288 0.76471 0.82663 0.14751  -0.04494 0.04862  3   ASP A CG  
26   O OD1 . ASP A 3   ? 0.79167 0.74629 0.80182 0.15876  -0.03997 0.05225  3   ASP A OD1 
27   O OD2 . ASP A 3   ? 0.79378 0.79987 0.84676 0.15035  -0.05357 0.04126  3   ASP A OD2 
28   N N   . PHE A 4   ? 0.66151 0.57920 0.70855 0.09156  -0.02950 0.05597  4   PHE A N   
29   C CA  . PHE A 4   ? 0.65577 0.57110 0.71513 0.07335  -0.02798 0.05594  4   PHE A CA  
30   C C   . PHE A 4   ? 0.59178 0.53361 0.68125 0.06495  -0.03737 0.05249  4   PHE A C   
31   O O   . PHE A 4   ? 0.57413 0.53337 0.67487 0.07024  -0.04357 0.04909  4   PHE A O   
32   C CB  . PHE A 4   ? 0.64735 0.54206 0.69479 0.06335  -0.01902 0.05663  4   PHE A CB  
33   C CG  . PHE A 4   ? 0.67901 0.58122 0.73436 0.06156  -0.02167 0.05457  4   PHE A CG  
34   C CD1 . PHE A 4   ? 0.72383 0.61536 0.76153 0.07353  -0.01851 0.05548  4   PHE A CD1 
35   C CD2 . PHE A 4   ? 0.61762 0.53698 0.69628 0.04947  -0.02679 0.05213  4   PHE A CD2 
36   C CE1 . PHE A 4   ? 0.63925 0.53744 0.68381 0.07174  -0.02066 0.05333  4   PHE A CE1 
37   C CE2 . PHE A 4   ? 0.61443 0.53981 0.69977 0.04833  -0.02852 0.05028  4   PHE A CE2 
38   C CZ  . PHE A 4   ? 0.69737 0.61218 0.76619 0.05867  -0.02553 0.05055  4   PHE A CZ  
39   N N   . ILE A 5   ? 0.58003 0.52397 0.68059 0.05212  -0.03727 0.05306  5   ILE A N   
40   C CA  . ILE A 5   ? 0.55448 0.51740 0.67915 0.04468  -0.04349 0.05146  5   ILE A CA  
41   C C   . ILE A 5   ? 0.59153 0.55230 0.72004 0.03277  -0.04107 0.05252  5   ILE A C   
42   O O   . ILE A 5   ? 0.56435 0.51252 0.68007 0.02738  -0.03499 0.05319  5   ILE A O   
43   C CB  . ILE A 5   ? 0.58535 0.55804 0.71938 0.04494  -0.04649 0.05130  5   ILE A CB  
44   C CG1 . ILE A 5   ? 0.57443 0.56226 0.72995 0.03883  -0.05062 0.04987  5   ILE A CG1 
45   C CG2 . ILE A 5   ? 0.58084 0.54255 0.70604 0.03946  -0.04220 0.05422  5   ILE A CG2 
46   C CD1 . ILE A 5   ? 0.60506 0.60248 0.76956 0.03960  -0.05236 0.04817  5   ILE A CD1 
47   N N   . ILE A 6   ? 0.63488 0.60890 0.78033 0.02888  -0.04501 0.05183  6   ILE A N   
48   C CA  . ILE A 6   ? 0.58171 0.56029 0.73254 0.02033  -0.04388 0.05232  6   ILE A CA  
49   C C   . ILE A 6   ? 0.51870 0.51114 0.68641 0.01922  -0.04815 0.05397  6   ILE A C   
50   O O   . ILE A 6   ? 0.49731 0.49362 0.67350 0.02331  -0.05068 0.05350  6   ILE A O   
51   C CB  . ILE A 6   ? 0.51772 0.49501 0.66699 0.01933  -0.04195 0.05046  6   ILE A CB  
52   C CG1 . ILE A 6   ? 0.55743 0.54205 0.71757 0.02511  -0.04617 0.04941  6   ILE A CG1 
53   C CG2 . ILE A 6   ? 0.50866 0.46781 0.63772 0.02101  -0.03552 0.04949  6   ILE A CG2 
54   C CD1 . ILE A 6   ? 0.57755 0.56434 0.74029 0.02343  -0.04496 0.04800  6   ILE A CD1 
55   N N   . ASP A 7   ? 0.54666 0.54677 0.71782 0.01379  -0.04786 0.05530  7   ASP A N   
56   C CA  . ASP A 7   ? 0.56889 0.57995 0.75188 0.01513  -0.05050 0.05830  7   ASP A CA  
57   C C   . ASP A 7   ? 0.56847 0.59286 0.75440 0.01213  -0.05058 0.05862  7   ASP A C   
58   O O   . ASP A 7   ? 0.56980 0.59866 0.74977 0.00582  -0.04895 0.05642  7   ASP A O   
59   C CB  . ASP A 7   ? 0.57576 0.58587 0.75829 0.01515  -0.05097 0.06064  7   ASP A CB  
60   C CG  . ASP A 7   ? 0.69260 0.70826 0.88405 0.01847  -0.05175 0.06446  7   ASP A CG  
61   O OD1 . ASP A 7   ? 0.70632 0.72424 0.90424 0.02183  -0.05152 0.06525  7   ASP A OD1 
62   O OD2 . ASP A 7   ? 0.78128 0.79734 0.97130 0.01813  -0.05152 0.06702  7   ASP A OD2 
63   N N   . PHE A 8   ? 0.52684 0.55880 0.72154 0.01675  -0.05177 0.06049  8   PHE A N   
64   C CA  . PHE A 8   ? 0.52062 0.56999 0.71934 0.01714  -0.05245 0.06084  8   PHE A CA  
65   C C   . PHE A 8   ? 0.57822 0.63511 0.78067 0.02421  -0.05384 0.06661  8   PHE A C   
66   O O   . PHE A 8   ? 0.61412 0.65949 0.81836 0.02925  -0.05266 0.07025  8   PHE A O   
67   C CB  . PHE A 8   ? 0.55323 0.60563 0.75714 0.02006  -0.05184 0.05959  8   PHE A CB  
68   C CG  . PHE A 8   ? 0.50399 0.55408 0.70305 0.01332  -0.04943 0.05396  8   PHE A CG  
69   C CD1 . PHE A 8   ? 0.50286 0.56887 0.70160 0.00692  -0.04784 0.04959  8   PHE A CD1 
70   C CD2 . PHE A 8   ? 0.49853 0.53181 0.69252 0.01350  -0.04792 0.05231  8   PHE A CD2 
71   C CE1 . PHE A 8   ? 0.47939 0.54004 0.67179 -0.00073 -0.04310 0.04382  8   PHE A CE1 
72   C CE2 . PHE A 8   ? 0.53735 0.56479 0.72338 0.00852  -0.04409 0.04804  8   PHE A CE2 
73   C CZ  . PHE A 8   ? 0.49702 0.53590 0.68187 0.00075  -0.04085 0.04391  8   PHE A CZ  
74   N N   . GLU A 9   ? 0.56809 0.64492 0.77062 0.02456  -0.05542 0.06670  9   GLU A N   
75   C CA  . GLU A 9   ? 0.55464 0.64229 0.75857 0.03496  -0.05650 0.07286  9   GLU A CA  
76   C C   . GLU A 9   ? 0.55821 0.66746 0.76702 0.03992  -0.05761 0.07162  9   GLU A C   
77   O O   . GLU A 9   ? 0.50240 0.62723 0.71293 0.03163  -0.05828 0.06439  9   GLU A O   
78   C CB  . GLU A 9   ? 0.62819 0.72570 0.82703 0.03355  -0.05822 0.07386  9   GLU A CB  
79   C CG  . GLU A 9   ? 0.70434 0.78114 0.89843 0.02900  -0.05671 0.07496  9   GLU A CG  
80   C CD  . GLU A 9   ? 0.85941 0.94445 1.04780 0.02955  -0.05788 0.07725  9   GLU A CD  
81   O OE1 . GLU A 9   ? 0.84962 0.95819 1.03727 0.03370  -0.06038 0.07761  9   GLU A OE1 
82   O OE2 . GLU A 9   ? 0.86358 0.93386 1.04811 0.02635  -0.05643 0.07820  9   GLU A OE2 
83   N N   . THR A 10  ? 0.58524 0.69348 0.79540 0.05323  -0.05630 0.07811  10  THR A N   
84   C CA  . THR A 10  ? 0.54212 0.66478 0.75733 0.05969  -0.05622 0.07734  10  THR A CA  
85   C C   . THR A 10  ? 0.54412 0.67781 0.75645 0.07759  -0.05564 0.08533  10  THR A C   
86   O O   . THR A 10  ? 0.68362 0.80140 0.88891 0.08558  -0.05277 0.09284  10  THR A O   
87   C CB  . THR A 10  ? 0.58337 0.68446 0.80149 0.05861  -0.05273 0.07654  10  THR A CB  
88   O OG1 . THR A 10  ? 0.61593 0.69329 0.83068 0.06563  -0.04835 0.08277  10  THR A OG1 
89   C CG2 . THR A 10  ? 0.56737 0.65608 0.78539 0.04454  -0.05288 0.06976  10  THR A CG2 
90   N N   . MET A 11  ? 0.52739 0.68767 0.74399 0.08474  -0.05735 0.08369  11  MET A N   
91   C CA  . MET A 11  ? 0.54418 0.71578 0.75682 0.10563  -0.05607 0.09166  11  MET A CA  
92   C C   . MET A 11  ? 0.61413 0.76711 0.82708 0.11468  -0.05031 0.09553  11  MET A C   
93   O O   . MET A 11  ? 0.58984 0.75418 0.79926 0.13307  -0.04850 0.10133  11  MET A O   
94   C CB  . MET A 11  ? 0.56272 0.78152 0.78016 0.11023  -0.06163 0.08663  11  MET A CB  
95   C CG  . MET A 11  ? 0.64072 0.88156 0.85508 0.10740  -0.06629 0.08447  11  MET A CG  
96   S SD  . MET A 11  ? 0.76718 0.99249 0.96593 0.12843  -0.06384 0.09912  11  MET A SD  
97   C CE  . MET A 11  ? 0.75941 1.00938 0.95683 0.11719  -0.06998 0.09274  11  MET A CE  
98   N N   . GLY A 12  ? 0.59868 0.72567 0.81505 0.10313  -0.04730 0.09192  12  GLY A N   
99   C CA  . GLY A 12  ? 0.59098 0.69952 0.80756 0.10933  -0.04131 0.09393  12  GLY A CA  
100  C C   . GLY A 12  ? 0.68030 0.75792 0.89765 0.09614  -0.03820 0.09044  12  GLY A C   
101  O O   . GLY A 12  ? 0.72152 0.79434 0.93894 0.08479  -0.04097 0.08744  12  GLY A O   
102  N N   . SER A 13  ? 0.81201 0.87031 1.02968 0.09810  -0.03223 0.09011  13  SER A N   
103  C CA  . SER A 13  ? 0.85550 0.88822 1.07396 0.08665  -0.02903 0.08557  13  SER A CA  
104  C C   . SER A 13  ? 0.86912 0.89720 1.09276 0.08100  -0.02804 0.07902  13  SER A C   
105  O O   . SER A 13  ? 0.91912 0.92837 1.14307 0.07377  -0.02469 0.07464  13  SER A O   
106  C CB  . SER A 13  ? 0.82824 0.83278 1.03874 0.09183  -0.01947 0.09062  13  SER A CB  
107  O OG  . SER A 13  ? 0.83560 0.82908 1.03955 0.10612  -0.01094 0.09656  13  SER A OG  
108  N N   . GLY A 14  ? 0.68372 0.73054 0.91162 0.08342  -0.03078 0.07712  14  GLY A N   
109  C CA  . GLY A 14  ? 0.68729 0.73201 0.91931 0.07597  -0.03104 0.07020  14  GLY A CA  
110  C C   . GLY A 14  ? 0.67208 0.73126 0.90640 0.06451  -0.03717 0.06427  14  GLY A C   
111  O O   . GLY A 14  ? 0.69596 0.76761 0.92955 0.06132  -0.04097 0.06468  14  GLY A O   
112  N N   . GLU A 15  ? 0.64910 0.70514 0.88447 0.05844  -0.03683 0.05851  15  GLU A N   
113  C CA  . GLU A 15  ? 0.59925 0.66207 0.83262 0.04785  -0.03981 0.05327  15  GLU A CA  
114  C C   . GLU A 15  ? 0.57609 0.66474 0.81253 0.04648  -0.04116 0.05175  15  GLU A C   
115  O O   . GLU A 15  ? 0.61119 0.70439 0.84440 0.03628  -0.04156 0.04700  15  GLU A O   
116  C CB  . GLU A 15  ? 0.61184 0.66425 0.84268 0.04319  -0.03805 0.04796  15  GLU A CB  
117  C CG  . GLU A 15  ? 0.63251 0.69534 0.86706 0.04536  -0.03543 0.04563  15  GLU A CG  
118  C CD  . GLU A 15  ? 0.66740 0.71663 0.89852 0.04322  -0.03301 0.04135  15  GLU A CD  
119  O OE1 . GLU A 15  ? 0.65799 0.69164 0.88431 0.04134  -0.03370 0.03975  15  GLU A OE1 
120  O OE2 . GLU A 15  ? 0.66919 0.72606 0.90256 0.04394  -0.03042 0.03898  15  GLU A OE2 
121  N N   . LYS A 16  ? 0.50026 0.60625 0.74181 0.05674  -0.04092 0.05497  16  LYS A N   
122  C CA  . LYS A 16  ? 0.46349 0.60183 0.70968 0.05729  -0.04287 0.05255  16  LYS A CA  
123  C C   . LYS A 16  ? 0.51897 0.66938 0.76396 0.06313  -0.04617 0.05727  16  LYS A C   
124  O O   . LYS A 16  ? 0.45316 0.63532 0.70220 0.06769  -0.04842 0.05592  16  LYS A O   
125  C CB  . LYS A 16  ? 0.47684 0.63179 0.72897 0.06781  -0.04092 0.05280  16  LYS A CB  
126  C CG  . LYS A 16  ? 0.52601 0.67300 0.77936 0.06131  -0.03752 0.04727  16  LYS A CG  
127  C CD  . LYS A 16  ? 0.57424 0.73322 0.82750 0.04564  -0.03713 0.03846  16  LYS A CD  
128  C CE  . LYS A 16  ? 0.54599 0.69539 0.79750 0.03806  -0.03268 0.03283  16  LYS A CE  
129  N NZ  . LYS A 16  ? 0.53721 0.68975 0.78391 0.02202  -0.03010 0.02523  16  LYS A NZ  
130  N N   . ALA A 17  ? 0.52385 0.65153 0.76330 0.06387  -0.04629 0.06232  17  ALA A N   
131  C CA  . ALA A 17  ? 0.54495 0.68006 0.78133 0.06714  -0.04896 0.06637  17  ALA A CA  
132  C C   . ALA A 17  ? 0.52603 0.68934 0.76458 0.05772  -0.05231 0.05951  17  ALA A C   
133  O O   . ALA A 17  ? 0.46615 0.62522 0.70363 0.04297  -0.05138 0.05233  17  ALA A O   
134  C CB  . ALA A 17  ? 0.56014 0.66695 0.79101 0.06203  -0.04823 0.06878  17  ALA A CB  
135  N N   . ALA A 18  ? 0.50258 0.69476 0.74272 0.06676  -0.05516 0.06123  18  ALA A N   
136  C CA  . ALA A 18  ? 0.46485 0.68363 0.70597 0.05712  -0.05815 0.05423  18  ALA A CA  
137  C C   . ALA A 18  ? 0.47106 0.66697 0.70491 0.04839  -0.05837 0.05572  18  ALA A C   
138  O O   . ALA A 18  ? 0.47431 0.64647 0.70331 0.05588  -0.05791 0.06409  18  ALA A O   
139  C CB  . ALA A 18  ? 0.45678 0.71283 0.69993 0.07157  -0.06196 0.05638  18  ALA A CB  
140  N N   . VAL A 19  ? 0.44239 0.64262 0.67462 0.03169  -0.05750 0.04694  19  VAL A N   
141  C CA  . VAL A 19  ? 0.47064 0.64537 0.69487 0.02272  -0.05643 0.04759  19  VAL A CA  
142  C C   . VAL A 19  ? 0.46794 0.66297 0.68967 0.01742  -0.05838 0.04395  19  VAL A C   
143  O O   . VAL A 19  ? 0.41536 0.63834 0.63999 0.00816  -0.05760 0.03409  19  VAL A O   
144  C CB  . VAL A 19  ? 0.44455 0.59685 0.66394 0.00920  -0.05151 0.04176  19  VAL A CB  
145  C CG1 . VAL A 19  ? 0.46434 0.59447 0.68463 0.01562  -0.05050 0.04613  19  VAL A CG1 
146  C CG2 . VAL A 19  ? 0.43110 0.60336 0.65241 -0.00286 -0.04762 0.03081  19  VAL A CG2 
147  N N   . ILE A 20  ? 0.48738 0.66973 0.70389 0.02263  -0.06029 0.05089  20  ILE A N   
148  C CA  . ILE A 20  ? 0.50722 0.70748 0.72023 0.01920  -0.06242 0.04844  20  ILE A CA  
149  C C   . ILE A 20  ? 0.48925 0.67337 0.69516 0.00191  -0.05844 0.04164  20  ILE A C   
150  O O   . ILE A 20  ? 0.45934 0.66346 0.66402 -0.01004 -0.05677 0.03184  20  ILE A O   
151  C CB  . ILE A 20  ? 0.41384 0.60801 0.62283 0.03411  -0.06523 0.05955  20  ILE A CB  
152  N N   . ASP A 21  ? 0.45743 0.60626 0.65791 0.00042  -0.05593 0.04573  21  ASP A N   
153  C CA  . ASP A 21  ? 0.48165 0.61106 0.67256 -0.01273 -0.05096 0.04064  21  ASP A CA  
154  C C   . ASP A 21  ? 0.51956 0.61660 0.70644 -0.01064 -0.04855 0.04432  21  ASP A C   
155  O O   . ASP A 21  ? 0.51134 0.60033 0.70325 -0.00019 -0.05134 0.05089  21  ASP A O   
156  C CB  . ASP A 21  ? 0.52618 0.65545 0.71132 -0.01425 -0.05209 0.04209  21  ASP A CB  
157  C CG  . ASP A 21  ? 0.65453 0.76160 0.83811 -0.00418 -0.05430 0.05207  21  ASP A CG  
158  O OD1 . ASP A 21  ? 0.64008 0.72469 0.82364 -0.00076 -0.05319 0.05540  21  ASP A OD1 
159  O OD2 . ASP A 21  ? 0.68872 0.80403 0.87152 0.00084  -0.05705 0.05609  21  ASP A OD2 
160  N N   . LEU A 22  ? 0.54513 0.62364 0.72135 -0.02037 -0.04238 0.03945  22  LEU A N   
161  C CA  . LEU A 22  ? 0.54658 0.59694 0.71601 -0.01707 -0.03996 0.04220  22  LEU A CA  
162  C C   . LEU A 22  ? 0.54814 0.57817 0.70424 -0.02050 -0.03603 0.04219  22  LEU A C   
163  O O   . LEU A 22  ? 0.52730 0.55561 0.67403 -0.03110 -0.02999 0.03644  22  LEU A O   
164  C CB  . LEU A 22  ? 0.50514 0.54893 0.67054 -0.02167 -0.03453 0.03742  22  LEU A CB  
165  C CG  . LEU A 22  ? 0.50083 0.51667 0.65553 -0.01707 -0.03143 0.03969  22  LEU A CG  
166  C CD1 . LEU A 22  ? 0.45416 0.46705 0.61693 -0.00487 -0.03807 0.04581  22  LEU A CD1 
167  C CD2 . LEU A 22  ? 0.51134 0.51960 0.65907 -0.02206 -0.02459 0.03499  22  LEU A CD2 
168  N N   . ALA A 23  ? 0.54667 0.56210 0.70170 -0.01187 -0.03853 0.04761  23  ALA A N   
169  C CA  . ALA A 23  ? 0.52891 0.52696 0.67226 -0.01178 -0.03559 0.04855  23  ALA A CA  
170  C C   . ALA A 23  ? 0.54498 0.52326 0.67967 -0.00465 -0.03350 0.04988  23  ALA A C   
171  O O   . ALA A 23  ? 0.53285 0.51429 0.67623 0.00319  -0.03821 0.05215  23  ALA A O   
172  C CB  . ALA A 23  ? 0.59649 0.60110 0.74717 -0.00687 -0.04084 0.05311  23  ALA A CB  
173  N N   . VAL A 24  ? 0.52475 0.48268 0.64093 -0.00662 -0.02577 0.04822  24  VAL A N   
174  C CA  . VAL A 24  ? 0.60504 0.54438 0.70869 0.00286  -0.02300 0.04989  24  VAL A CA  
175  C C   . VAL A 24  ? 0.60722 0.52871 0.69434 0.00668  -0.01801 0.05139  24  VAL A C   
176  O O   . VAL A 24  ? 0.61822 0.53001 0.69434 -0.00217 -0.01070 0.04906  24  VAL A O   
177  C CB  . VAL A 24  ? 0.56179 0.48891 0.65390 -0.00040 -0.01558 0.04703  24  VAL A CB  
178  C CG1 . VAL A 24  ? 0.56096 0.47651 0.63909 -0.01375 -0.00447 0.04208  24  VAL A CG1 
179  C CG2 . VAL A 24  ? 0.50628 0.41482 0.58295 0.01238  -0.01292 0.04960  24  VAL A CG2 
180  N N   . ILE A 25  ? 0.58962 0.50876 0.67520 0.01976  -0.02156 0.05435  25  ILE A N   
181  C CA  . ILE A 25  ? 0.63062 0.53312 0.69872 0.02757  -0.01664 0.05626  25  ILE A CA  
182  C C   . ILE A 25  ? 0.66106 0.55384 0.71592 0.04311  -0.01549 0.05799  25  ILE A C   
183  O O   . ILE A 25  ? 0.66023 0.56993 0.72819 0.05029  -0.02352 0.05746  25  ILE A O   
184  C CB  . ILE A 25  ? 0.69069 0.60669 0.77080 0.03015  -0.02282 0.05753  25  ILE A CB  
185  C CG1 . ILE A 25  ? 0.63424 0.56101 0.72578 0.01711  -0.02441 0.05659  25  ILE A CG1 
186  C CG2 . ILE A 25  ? 0.67524 0.57443 0.73618 0.03955  -0.01707 0.05938  25  ILE A CG2 
187  C CD1 . ILE A 25  ? 0.61231 0.55318 0.71755 0.01934  -0.03054 0.05816  25  ILE A CD1 
188  N N   . ALA A 26  ? 0.73983 0.60503 0.76712 0.04882  -0.00462 0.05970  26  ALA A N   
189  C CA  . ALA A 26  ? 0.74044 0.59497 0.74962 0.06786  -0.00256 0.06259  26  ALA A CA  
190  C C   . ALA A 26  ? 0.80772 0.66809 0.81484 0.08062  -0.00553 0.06447  26  ALA A C   
191  O O   . ALA A 26  ? 0.84388 0.70108 0.85188 0.07417  -0.00333 0.06457  26  ALA A O   
192  C CB  . ALA A 26  ? 0.75592 0.57337 0.73218 0.06956  0.01303  0.06442  26  ALA A CB  
193  N N   . PHE A 27  ? 0.81106 0.68280 0.81579 0.09893  -0.01063 0.06514  27  PHE A N   
194  C CA  . PHE A 27  ? 0.82479 0.71786 0.84044 0.10771  -0.01758 0.06405  27  PHE A CA  
195  C C   . PHE A 27  ? 0.90966 0.80662 0.90911 0.13192  -0.01823 0.06522  27  PHE A C   
196  O O   . PHE A 27  ? 0.91083 0.80409 0.90074 0.13939  -0.01769 0.06570  27  PHE A O   
197  C CB  . PHE A 27  ? 0.77322 0.69701 0.82361 0.09441  -0.02855 0.05925  27  PHE A CB  
198  C CG  . PHE A 27  ? 0.76146 0.71497 0.82918 0.10147  -0.03812 0.05425  27  PHE A CG  
199  C CD1 . PHE A 27  ? 0.78327 0.74572 0.84072 0.11982  -0.04005 0.05290  27  PHE A CD1 
200  C CD2 . PHE A 27  ? 0.69956 0.66872 0.79144 0.08815  -0.04374 0.05072  27  PHE A CD2 
201  C CE1 . PHE A 27  ? 0.75093 0.74349 0.82611 0.12277  -0.04847 0.04609  27  PHE A CE1 
202  C CE2 . PHE A 27  ? 0.62782 0.62112 0.73524 0.09099  -0.05049 0.04482  27  PHE A CE2 
203  C CZ  . PHE A 27  ? 0.61412 0.62023 0.71417 0.10696  -0.05299 0.04174  27  PHE A CZ  
204  N N   . ASP A 28  ? 0.96691 0.87262 0.96211 0.14543  -0.01922 0.06559  28  ASP A N   
205  C CA  . ASP A 28  ? 0.99083 0.90504 0.96956 0.17151  -0.02030 0.06645  28  ASP A CA  
206  C C   . ASP A 28  ? 0.97382 0.93567 0.98102 0.17478  -0.03406 0.05802  28  ASP A C   
207  O O   . ASP A 28  ? 0.98313 0.96807 1.01138 0.16882  -0.03928 0.05337  28  ASP A O   
208  C CB  . ASP A 28  ? 1.05155 0.95044 1.00698 0.18781  -0.01277 0.07113  28  ASP A CB  
209  C CG  . ASP A 28  ? 1.11499 1.01882 1.04625 0.21935  -0.01203 0.07372  28  ASP A CG  
210  O OD1 . ASP A 28  ? 1.07406 0.99467 1.00687 0.22800  -0.01788 0.07134  28  ASP A OD1 
211  O OD2 . ASP A 28  ? 1.16936 1.06146 1.07908 0.23699  -0.00554 0.07813  28  ASP A OD2 
212  N N   . PRO A 29  ? 0.98002 0.95755 0.98812 0.18318  -0.03913 0.05487  29  PRO A N   
213  C CA  . PRO A 29  ? 0.93933 0.96320 0.97575 0.18254  -0.05096 0.04431  29  PRO A CA  
214  C C   . PRO A 29  ? 0.96467 1.02009 0.99859 0.20431  -0.05549 0.03972  29  PRO A C   
215  O O   . PRO A 29  ? 0.98422 1.08186 1.04125 0.20350  -0.06439 0.02863  29  PRO A O   
216  C CB  . PRO A 29  ? 0.90406 0.92973 0.93844 0.18363  -0.05331 0.04265  29  PRO A CB  
217  C CG  . PRO A 29  ? 0.87697 0.86519 0.87371 0.19881  -0.04343 0.05249  29  PRO A CG  
218  C CD  . PRO A 29  ? 0.92253 0.87501 0.90660 0.19040  -0.03322 0.05977  29  PRO A CD  
219  N N   . ASN A 30  ? 1.00877 1.04619 1.01488 0.22390  -0.04890 0.04698  30  ASN A N   
220  C CA  . ASN A 30  ? 1.06657 1.13672 1.06947 0.24727  -0.05313 0.04286  30  ASN A CA  
221  C C   . ASN A 30  ? 1.10491 1.20564 1.13793 0.23467  -0.05818 0.03443  30  ASN A C   
222  O O   . ASN A 30  ? 1.03281 1.11058 1.06620 0.22298  -0.05256 0.03916  30  ASN A O   
223  C CB  . ASN A 30  ? 1.11455 1.15041 1.07703 0.27154  -0.04238 0.05440  30  ASN A CB  
224  C CG  . ASN A 30  ? 1.11422 1.18389 1.06833 0.30138  -0.04635 0.05148  30  ASN A CG  
225  O OD1 . ASN A 30  ? 1.08993 1.21330 1.07027 0.30290  -0.05771 0.03916  30  ASN A OD1 
226  N ND2 . ASN A 30  ? 1.05874 1.09746 0.97529 0.32547  -0.03592 0.06213  30  ASN A ND2 
227  N N   . PRO A 31  ? 1.06212 1.21462 1.11972 0.23618  -0.06768 0.02113  31  PRO A N   
228  C CA  . PRO A 31  ? 1.03328 1.21369 1.11967 0.22190  -0.07058 0.01193  31  PRO A CA  
229  C C   . PRO A 31  ? 1.10013 1.28108 1.17517 0.23685  -0.06696 0.01533  31  PRO A C   
230  O O   . PRO A 31  ? 1.05275 1.24594 1.14799 0.22301  -0.06691 0.01028  31  PRO A O   
231  C CB  . PRO A 31  ? 1.01309 1.24942 1.12421 0.22170  -0.07975 -0.00488 31  PRO A CB  
232  C CG  . PRO A 31  ? 1.05808 1.30316 1.14703 0.24731  -0.08274 -0.00337 31  PRO A CG  
233  C CD  . PRO A 31  ? 1.06889 1.25728 1.12973 0.24852  -0.07532 0.01245  31  PRO A CD  
234  N N   . GLU A 32  ? 1.24509 1.41188 1.28717 0.26532  -0.06290 0.02387  32  GLU A N   
235  C CA  . GLU A 32  ? 1.25855 1.41598 1.28604 0.27897  -0.05712 0.02920  32  GLU A CA  
236  C C   . GLU A 32  ? 1.26962 1.36973 1.28012 0.26646  -0.04595 0.04151  32  GLU A C   
237  O O   . GLU A 32  ? 1.28759 1.37654 1.28817 0.27299  -0.04020 0.04543  32  GLU A O   
238  C CB  . GLU A 32  ? 1.25319 1.41727 1.24910 0.31746  -0.05552 0.03379  32  GLU A CB  
239  C CG  . GLU A 32  ? 1.28349 1.51516 1.29625 0.33470  -0.06629 0.01987  32  GLU A CG  
240  C CD  . GLU A 32  ? 1.39903 1.65885 1.41585 0.34051  -0.07437 0.01282  32  GLU A CD  
241  O OE1 . GLU A 32  ? 1.38374 1.60718 1.38747 0.33364  -0.07112 0.02034  32  GLU A OE1 
242  O OE2 . GLU A 32  ? 1.43784 1.75845 1.47100 0.35187  -0.08375 -0.00126 32  GLU A OE2 
243  N N   . VAL A 33  ? 1.13607 1.20237 1.14363 0.24835  -0.04252 0.04655  33  VAL A N   
244  C CA  . VAL A 33  ? 1.14477 1.16130 1.13755 0.23426  -0.03191 0.05587  33  VAL A CA  
245  C C   . VAL A 33  ? 1.06467 1.08893 1.08974 0.20338  -0.03591 0.05080  33  VAL A C   
246  O O   . VAL A 33  ? 1.09008 1.11724 1.13092 0.18689  -0.03998 0.04809  33  VAL A O   
247  C CB  . VAL A 33  ? 1.09849 1.07338 1.06413 0.23573  -0.02392 0.06410  33  VAL A CB  
248  C CG1 . VAL A 33  ? 1.09021 1.01759 1.04152 0.21890  -0.01202 0.07100  33  VAL A CG1 
249  C CG2 . VAL A 33  ? 1.05503 1.02242 0.98675 0.26865  -0.01939 0.06949  33  VAL A CG2 
250  N N   . VAL A 34  ? 0.99283 1.01963 1.02651 0.19647  -0.03421 0.04991  34  VAL A N   
251  C CA  . VAL A 34  ? 0.99615 1.02847 1.05680 0.16985  -0.03686 0.04617  34  VAL A CA  
252  C C   . VAL A 34  ? 0.99088 0.98212 1.03681 0.15758  -0.02797 0.05412  34  VAL A C   
253  O O   . VAL A 34  ? 0.96777 0.94208 0.99642 0.16532  -0.02093 0.05816  34  VAL A O   
254  C CB  . VAL A 34  ? 0.95572 1.02599 1.04077 0.16782  -0.04168 0.03721  34  VAL A CB  
255  C CG1 . VAL A 34  ? 1.00978 1.07556 1.07999 0.18234  -0.03635 0.04015  34  VAL A CG1 
256  C CG2 . VAL A 34  ? 0.91649 0.98885 1.02628 0.14153  -0.04309 0.03412  34  VAL A CG2 
257  N N   . GLU A 35  ? 0.98632 0.96341 1.03892 0.13864  -0.02801 0.05550  35  GLU A N   
258  C CA  . GLU A 35  ? 0.95480 0.89525 0.99130 0.12706  -0.01952 0.06143  35  GLU A CA  
259  C C   . GLU A 35  ? 0.89361 0.84019 0.95042 0.10639  -0.02187 0.05968  35  GLU A C   
260  O O   . GLU A 35  ? 0.87587 0.84766 0.95793 0.09828  -0.02926 0.05511  35  GLU A O   
261  C CB  . GLU A 35  ? 0.97908 0.90089 1.00537 0.12293  -0.01711 0.06381  35  GLU A CB  
262  C CG  . GLU A 35  ? 1.02544 0.93075 1.02324 0.14430  -0.01136 0.06754  35  GLU A CG  
263  C CD  . GLU A 35  ? 1.07828 0.96889 1.06838 0.14009  -0.00937 0.06889  35  GLU A CD  
264  O OE1 . GLU A 35  ? 1.05509 0.95736 1.06671 0.12308  -0.01523 0.06582  35  GLU A OE1 
265  O OE2 . GLU A 35  ? 1.11648 0.98198 1.07724 0.15442  -0.00082 0.07337  35  GLU A OE2 
266  N N   . THR A 36  ? 0.92288 0.84592 0.96705 0.09850  -0.01456 0.06296  36  THR A N   
267  C CA  . THR A 36  ? 0.88313 0.81643 0.94543 0.08311  -0.01739 0.06137  36  THR A CA  
268  C C   . THR A 36  ? 0.84479 0.77639 0.91695 0.06640  -0.01985 0.06153  36  THR A C   
269  O O   . THR A 36  ? 0.83740 0.75470 0.89918 0.06417  -0.01713 0.06276  36  THR A O   
270  C CB  . THR A 36  ? 0.86590 0.78106 0.91365 0.08110  -0.00969 0.06353  36  THR A CB  
271  O OG1 . THR A 36  ? 0.89752 0.78389 0.92625 0.07231  -0.00161 0.06571  36  THR A OG1 
272  C CG2 . THR A 36  ? 0.76936 0.68206 0.80214 0.10101  -0.00560 0.06439  36  THR A CG2 
273  N N   . PHE A 37  ? 0.84160 0.78870 0.93347 0.05569  -0.02445 0.06018  37  PHE A N   
274  C CA  . PHE A 37  ? 0.78331 0.73041 0.88323 0.04191  -0.02649 0.06105  37  PHE A CA  
275  C C   . PHE A 37  ? 0.87636 0.80264 0.95863 0.03401  -0.02001 0.06252  37  PHE A C   
276  O O   . PHE A 37  ? 0.86892 0.79040 0.94858 0.02832  -0.01945 0.06217  37  PHE A O   
277  C CB  . PHE A 37  ? 0.71953 0.68105 0.83667 0.03456  -0.02972 0.06074  37  PHE A CB  
278  C CG  . PHE A 37  ? 0.74164 0.70554 0.86590 0.02397  -0.03190 0.06249  37  PHE A CG  
279  C CD1 . PHE A 37  ? 0.73450 0.70758 0.87103 0.02303  -0.03600 0.06198  37  PHE A CD1 
280  C CD2 . PHE A 37  ? 0.77192 0.73050 0.88987 0.01592  -0.02970 0.06427  37  PHE A CD2 
281  C CE1 . PHE A 37  ? 0.73457 0.71082 0.87636 0.01598  -0.03771 0.06419  37  PHE A CE1 
282  C CE2 . PHE A 37  ? 0.82807 0.79344 0.95196 0.00878  -0.03230 0.06576  37  PHE A CE2 
283  C CZ  . PHE A 37  ? 0.75575 0.72962 0.89126 0.00971  -0.03625 0.06621  37  PHE A CZ  
284  N N   . ASP A 38  ? 1.06011 0.97431 1.12975 0.03285  -0.01407 0.06298  38  ASP A N   
285  C CA  . ASP A 38  ? 1.08554 0.98060 1.13803 0.02277  -0.00621 0.06206  38  ASP A CA  
286  C C   . ASP A 38  ? 1.10402 0.97802 1.13778 0.02612  0.00102  0.06168  38  ASP A C   
287  O O   . ASP A 38  ? 1.11602 0.98045 1.14209 0.01452  0.00610  0.05901  38  ASP A O   
288  C CB  . ASP A 38  ? 1.12627 1.00898 1.16575 0.02259  0.00051  0.06204  38  ASP A CB  
289  C CG  . ASP A 38  ? 1.23703 1.13697 1.29140 0.01667  -0.00464 0.06228  38  ASP A CG  
290  O OD1 . ASP A 38  ? 1.22674 1.14249 1.29553 0.00858  -0.01072 0.06223  38  ASP A OD1 
291  O OD2 . ASP A 38  ? 1.29271 1.18939 1.34273 0.02128  -0.00180 0.06286  38  ASP A OD2 
292  N N   . GLU A 39  ? 0.97705 0.84486 1.00250 0.04238  0.00220  0.06379  39  GLU A N   
293  C CA  . GLU A 39  ? 0.94183 0.78625 0.94535 0.04962  0.01034  0.06482  39  GLU A CA  
294  C C   . GLU A 39  ? 0.91951 0.77209 0.93264 0.04473  0.00580  0.06367  39  GLU A C   
295  O O   . GLU A 39  ? 0.93787 0.77093 0.93598 0.03818  0.01414  0.06239  39  GLU A O   
296  C CB  . GLU A 39  ? 0.94237 0.78502 0.93603 0.07182  0.01077  0.06781  39  GLU A CB  
297  C CG  . GLU A 39  ? 1.01713 0.83143 0.98124 0.08578  0.02116  0.07081  39  GLU A CG  
298  C CD  . GLU A 39  ? 1.07849 0.89941 1.03514 0.11021  0.01975  0.07359  39  GLU A CD  
299  O OE1 . GLU A 39  ? 1.02467 0.87325 1.00162 0.11227  0.01112  0.07169  39  GLU A OE1 
300  O OE2 . GLU A 39  ? 1.19805 0.99814 1.12836 0.12796  0.02759  0.07735  39  GLU A OE2 
301  N N   . LEU A 40  ? 0.86655 0.74677 0.90402 0.04692  -0.00602 0.06338  40  LEU A N   
302  C CA  . LEU A 40  ? 0.76205 0.65088 0.80974 0.04245  -0.01046 0.06226  40  LEU A CA  
303  C C   . LEU A 40  ? 0.76827 0.65900 0.82159 0.02474  -0.00948 0.05996  40  LEU A C   
304  O O   . LEU A 40  ? 0.76716 0.64997 0.81431 0.01889  -0.00551 0.05822  40  LEU A O   
305  C CB  . LEU A 40  ? 0.71944 0.63584 0.79138 0.04697  -0.02159 0.06151  40  LEU A CB  
306  C CG  . LEU A 40  ? 0.77290 0.69713 0.84322 0.06394  -0.02405 0.06120  40  LEU A CG  
307  C CD1 . LEU A 40  ? 0.69794 0.65094 0.79432 0.06311  -0.03321 0.05782  40  LEU A CD1 
308  C CD2 . LEU A 40  ? 0.76927 0.68035 0.82176 0.07528  -0.02045 0.06232  40  LEU A CD2 
309  N N   . VAL A 41  ? 0.76159 0.66474 0.82618 0.01667  -0.01283 0.05949  41  VAL A N   
310  C CA  . VAL A 41  ? 0.72720 0.63996 0.79883 0.00219  -0.01369 0.05691  41  VAL A CA  
311  C C   . VAL A 41  ? 0.78956 0.68350 0.84187 -0.00808 -0.00264 0.05252  41  VAL A C   
312  O O   . VAL A 41  ? 0.80398 0.70409 0.85927 -0.01756 -0.00175 0.04878  41  VAL A O   
313  C CB  . VAL A 41  ? 0.74620 0.67288 0.82790 -0.00205 -0.01781 0.05772  41  VAL A CB  
314  C CG1 . VAL A 41  ? 0.69861 0.63684 0.78323 -0.01516 -0.01792 0.05439  41  VAL A CG1 
315  C CG2 . VAL A 41  ? 0.75847 0.70239 0.85942 0.00487  -0.02647 0.06085  41  VAL A CG2 
316  N N   . SER A 42  ? 0.79263 0.66292 0.82417 -0.00690 0.00731  0.05207  42  SER A N   
317  C CA  . SER A 42  ? 0.79129 0.64001 0.80257 -0.01883 0.02074  0.04649  42  SER A CA  
318  C C   . SER A 42  ? 0.77324 0.60323 0.77143 -0.01465 0.02751  0.04666  42  SER A C   
319  O O   . SER A 42  ? 0.71285 0.53080 0.69979 -0.02771 0.03784  0.04063  42  SER A O   
320  C CB  . SER A 42  ? 0.77486 0.59940 0.76493 -0.01972 0.03188  0.04560  42  SER A CB  
321  O OG  . SER A 42  ? 0.89034 0.69630 0.86708 -0.00132 0.03470  0.05169  42  SER A OG  
322  N N   . ARG A 43  ? 0.73053 0.56028 0.73053 0.00237  0.02213  0.05241  43  ARG A N   
323  C CA  . ARG A 43  ? 0.71047 0.52458 0.69815 0.00750  0.02761  0.05303  43  ARG A CA  
324  C C   . ARG A 43  ? 0.77672 0.61245 0.78364 -0.00131 0.02064  0.05007  43  ARG A C   
325  O O   . ARG A 43  ? 0.77443 0.59638 0.77034 -0.00370 0.02789  0.04828  43  ARG A O   
326  C CB  . ARG A 43  ? 0.74062 0.55132 0.72301 0.03005  0.02366  0.05928  43  ARG A CB  
327  C CG  . ARG A 43  ? 0.74990 0.53377 0.70784 0.03889  0.03375  0.06110  43  ARG A CG  
328  C CD  . ARG A 43  ? 0.81510 0.60118 0.76743 0.06279  0.02886  0.06644  43  ARG A CD  
329  N NE  . ARG A 43  ? 0.89583 0.67776 0.83816 0.07823  0.02966  0.06995  43  ARG A NE  
330  C CZ  . ARG A 43  ? 0.94981 0.75845 0.90710 0.09262  0.01785  0.07123  43  ARG A CZ  
331  N NH1 . ARG A 43  ? 0.92087 0.75828 0.90078 0.09433  0.00558  0.06939  43  ARG A NH1 
332  N NH2 . ARG A 43  ? 0.96563 0.77217 0.91414 0.10549  0.01950  0.07348  43  ARG A NH2 
333  N N   . GLY A 44  ? 0.71184 0.57955 0.74561 -0.00562 0.00793  0.04971  44  GLY A N   
334  C CA  . GLY A 44  ? 0.67662 0.56401 0.72709 -0.01123 0.00189  0.04766  44  GLY A CA  
335  C C   . GLY A 44  ? 0.70188 0.59547 0.75234 -0.02923 0.00758  0.04022  44  GLY A C   
336  O O   . GLY A 44  ? 0.72832 0.61471 0.76848 -0.03996 0.01538  0.03551  44  GLY A O   
337  N N   . ILE A 45  ? 0.67721 0.58684 0.73998 -0.03288 0.00384  0.03803  45  ILE A N   
338  C CA  . ILE A 45  ? 0.64198 0.57164 0.71268 -0.04839 0.00526  0.03022  45  ILE A CA  
339  C C   . ILE A 45  ? 0.60495 0.56723 0.70037 -0.04424 -0.00776 0.03249  45  ILE A C   
340  O O   . ILE A 45  ? 0.55486 0.51845 0.65881 -0.03256 -0.01457 0.03833  45  ILE A O   
341  C CB  . ILE A 45  ? 0.67307 0.58740 0.72957 -0.05939 0.01833  0.02295  45  ILE A CB  
342  C CG1 . ILE A 45  ? 0.68214 0.59435 0.74261 -0.05051 0.01539  0.02650  45  ILE A CG1 
343  C CG2 . ILE A 45  ? 0.67728 0.55343 0.70526 -0.06242 0.03393  0.02139  45  ILE A CG2 
344  C CD1 . ILE A 45  ? 0.63833 0.53975 0.68799 -0.06189 0.02767  0.01912  45  ILE A CD1 
345  N N   . LYS A 46  ? 0.58176 0.57098 0.68749 -0.05320 -0.01061 0.02748  46  LYS A N   
346  C CA  . LYS A 46  ? 0.52098 0.54095 0.64631 -0.04927 -0.02031 0.02877  46  LYS A CA  
347  C C   . LYS A 46  ? 0.58438 0.62257 0.71174 -0.06228 -0.01545 0.01855  46  LYS A C   
348  O O   . LYS A 46  ? 0.57615 0.62158 0.69747 -0.07597 -0.00919 0.00953  46  LYS A O   
349  C CB  . LYS A 46  ? 0.44645 0.48707 0.58180 -0.04445 -0.02874 0.03261  46  LYS A CB  
350  N N   . ILE A 47  ? 0.60510 0.65096 0.74075 -0.05890 -0.01746 0.01881  47  ILE A N   
351  C CA  . ILE A 47  ? 0.56338 0.63198 0.70480 -0.06943 -0.01404 0.00914  47  ILE A CA  
352  C C   . ILE A 47  ? 0.54393 0.65140 0.70404 -0.06147 -0.02537 0.01124  47  ILE A C   
353  O O   . ILE A 47  ? 0.55608 0.66286 0.72422 -0.04636 -0.03346 0.02128  47  ILE A O   
354  C CB  . ILE A 47  ? 0.55258 0.60446 0.69054 -0.06831 -0.00912 0.00922  47  ILE A CB  
355  C CG1 . ILE A 47  ? 0.57406 0.58376 0.68907 -0.07187 0.00277  0.00926  47  ILE A CG1 
356  C CG2 . ILE A 47  ? 0.54103 0.61839 0.68647 -0.07950 -0.00509 -0.00147 47  ILE A CG2 
357  C CD1 . ILE A 47  ? 0.56959 0.55601 0.67795 -0.06277 0.00474  0.01446  47  ILE A CD1 
358  N N   . LYS A 48  ? 0.53432 0.67555 0.69996 -0.07066 -0.02532 0.00169  48  LYS A N   
359  C CA  . LYS A 48  ? 0.53313 0.71305 0.71365 -0.05985 -0.03576 0.00428  48  LYS A CA  
360  C C   . LYS A 48  ? 0.56469 0.77671 0.75531 -0.06486 -0.03470 -0.00512 48  LYS A C   
361  O O   . LYS A 48  ? 0.57805 0.80368 0.76638 -0.08277 -0.02680 -0.01938 48  LYS A O   
362  C CB  . LYS A 48  ? 0.43059 0.63195 0.61026 -0.06133 -0.03936 0.00204  48  LYS A CB  
363  N N   . PHE A 49  ? 0.55155 0.77537 0.75294 -0.04967 -0.04144 0.00203  49  PHE A N   
364  C CA  . PHE A 49  ? 0.52024 0.77197 0.73176 -0.05165 -0.04053 -0.00539 49  PHE A CA  
365  C C   . PHE A 49  ? 0.51899 0.82365 0.74194 -0.04428 -0.04792 -0.00926 49  PHE A C   
366  O O   . PHE A 49  ? 0.50493 0.81898 0.72856 -0.02909 -0.05569 -0.00027 49  PHE A O   
367  C CB  . PHE A 49  ? 0.44961 0.68331 0.66512 -0.03865 -0.04252 0.00406  49  PHE A CB  
368  C CG  . PHE A 49  ? 0.41441 0.60143 0.61904 -0.04153 -0.03714 0.00870  49  PHE A CG  
369  C CD1 . PHE A 49  ? 0.42891 0.59950 0.62571 -0.05544 -0.02722 0.00078  49  PHE A CD1 
370  C CD2 . PHE A 49  ? 0.45626 0.61695 0.65768 -0.02937 -0.04142 0.02069  49  PHE A CD2 
371  C CE1 . PHE A 49  ? 0.43520 0.56457 0.61967 -0.05476 -0.02257 0.00581  49  PHE A CE1 
372  C CE2 . PHE A 49  ? 0.47953 0.60338 0.67144 -0.03011 -0.03746 0.02412  49  PHE A CE2 
373  C CZ  . PHE A 49  ? 0.46658 0.57515 0.64930 -0.04156 -0.02848 0.01722  49  PHE A CZ  
374  N N   . ASP A 50  ? 0.51751 0.85762 0.74868 -0.05411 -0.04485 -0.02289 50  ASP A N   
375  C CA  . ASP A 50  ? 0.47310 0.87057 0.71640 -0.04503 -0.05204 -0.02796 50  ASP A CA  
376  C C   . ASP A 50  ? 0.51015 0.91232 0.76060 -0.02084 -0.05873 -0.01539 50  ASP A C   
377  O O   . ASP A 50  ? 0.52546 0.92070 0.78056 -0.02173 -0.05522 -0.01650 50  ASP A O   
378  C CB  . ASP A 50  ? 0.46348 0.89781 0.71367 -0.06627 -0.04493 -0.04911 50  ASP A CB  
379  C CG  . ASP A 50  ? 0.46301 0.96428 0.72765 -0.05674 -0.05228 -0.05683 50  ASP A CG  
380  O OD1 . ASP A 50  ? 0.52059 1.03526 0.78817 -0.03093 -0.06227 -0.04378 50  ASP A OD1 
381  O OD2 . ASP A 50  ? 0.48934 1.03147 0.76174 -0.07464 -0.04720 -0.07669 50  ASP A OD2 
382  N N   . LEU A 51  ? 0.49017 0.90216 0.73964 0.00105  -0.06706 -0.00343 51  LEU A N   
383  C CA  . LEU A 51  ? 0.48312 0.89722 0.73620 0.02545  -0.07141 0.00884  51  LEU A CA  
384  C C   . LEU A 51  ? 0.48439 0.94970 0.74966 0.03039  -0.07309 -0.00032 51  LEU A C   
385  O O   . LEU A 51  ? 0.47727 0.93550 0.74742 0.03669  -0.07117 0.00250  51  LEU A O   
386  C CB  . LEU A 51  ? 0.40497 0.81598 0.65057 0.04770  -0.07727 0.02324  51  LEU A CB  
387  C CG  . LEU A 51  ? 0.40538 0.76239 0.64043 0.04717  -0.07510 0.03468  51  LEU A CG  
388  C CD1 . LEU A 51  ? 0.41351 0.76594 0.63947 0.06834  -0.07881 0.04849  51  LEU A CD1 
389  C CD2 . LEU A 51  ? 0.45598 0.77129 0.69135 0.04603  -0.07055 0.04017  51  LEU A CD2 
390  N N   . LYS A 52  ? 0.40642 0.92629 0.67716 0.02747  -0.07656 -0.01240 52  LYS A N   
391  C CA  . LYS A 52  ? 0.43565 1.01222 0.71917 0.03423  -0.07896 -0.02205 52  LYS A CA  
392  C C   . LYS A 52  ? 0.52661 1.09595 0.81833 0.01800  -0.07124 -0.03169 52  LYS A C   
393  O O   . LYS A 52  ? 0.49504 1.08327 0.79477 0.03100  -0.07223 -0.03039 52  LYS A O   
394  C CB  . LYS A 52  ? 0.40409 1.04284 0.69336 0.02612  -0.08241 -0.03877 52  LYS A CB  
395  N N   . SER A 53  ? 0.49675 1.03501 0.78440 -0.00902 -0.06251 -0.04036 53  SER A N   
396  C CA  . SER A 53  ? 0.45919 0.99110 0.75196 -0.02607 -0.05344 -0.05091 53  SER A CA  
397  C C   . SER A 53  ? 0.47284 0.96352 0.76335 -0.01316 -0.05256 -0.03675 53  SER A C   
398  O O   . SER A 53  ? 0.46074 0.95817 0.75793 -0.01837 -0.04759 -0.04324 53  SER A O   
399  C CB  . SER A 53  ? 0.46098 0.96517 0.74503 -0.05617 -0.04245 -0.06254 53  SER A CB  
400  O OG  . SER A 53  ? 0.47495 0.91972 0.74449 -0.05452 -0.04146 -0.04879 53  SER A OG  
401  N N   . GLN A 54  ? 0.48601 0.93610 0.76745 0.00281  -0.05668 -0.01874 54  GLN A N   
402  C CA  . GLN A 54  ? 0.44824 0.86016 0.72713 0.01507  -0.05581 -0.00604 54  GLN A CA  
403  C C   . GLN A 54  ? 0.51643 0.95300 0.80188 0.04068  -0.06087 0.00173  54  GLN A C   
404  O O   . GLN A 54  ? 0.54212 0.95231 0.82661 0.05013  -0.05897 0.00998  54  GLN A O   
405  C CB  . GLN A 54  ? 0.39864 0.75990 0.66553 0.01985  -0.05685 0.00773  54  GLN A CB  
406  C CG  . GLN A 54  ? 0.45845 0.79645 0.71662 -0.00005 -0.05276 0.00249  54  GLN A CG  
407  C CD  . GLN A 54  ? 0.48277 0.77734 0.73047 0.00545  -0.05433 0.01498  54  GLN A CD  
408  O OE1 . GLN A 54  ? 0.47839 0.75114 0.72487 0.02020  -0.05641 0.02658  54  GLN A OE1 
409  N NE2 . GLN A 54  ? 0.47155 0.75704 0.71189 -0.00639 -0.05290 0.01168  54  GLN A NE2 
410  N N   . LYS A 55  ? 0.55768 1.04360 0.84821 0.05344  -0.06677 -0.00054 55  LYS A N   
411  C CA  . LYS A 55  ? 0.56312 1.06860 0.85569 0.08209  -0.07075 0.00913  55  LYS A CA  
412  C C   . LYS A 55  ? 0.54183 1.06221 0.84460 0.08166  -0.06707 0.00280  55  LYS A C   
413  O O   . LYS A 55  ? 0.54509 1.10270 0.85864 0.06533  -0.06488 -0.01395 55  LYS A O   
414  C CB  . LYS A 55  ? 0.63155 1.19357 0.92637 0.09697  -0.07792 0.00651  55  LYS A CB  
415  N N   . GLY A 56  ? 0.68280 1.17452 0.98184 0.09895  -0.06531 0.01533  56  GLY A N   
416  C CA  . GLY A 56  ? 0.67810 1.17704 0.98543 0.09875  -0.06115 0.01056  56  GLY A CA  
417  C C   . GLY A 56  ? 0.70516 1.16336 1.01130 0.07593  -0.05434 0.00596  56  GLY A C   
418  O O   . GLY A 56  ? 0.73751 1.19779 1.04942 0.07371  -0.05003 0.00163  56  GLY A O   
419  N N   . HIS A 57  ? 0.58302 1.00528 0.88069 0.06022  -0.05301 0.00687  57  HIS A N   
420  C CA  . HIS A 57  ? 0.50496 0.88316 0.79690 0.04246  -0.04678 0.00513  57  HIS A CA  
421  C C   . HIS A 57  ? 0.52472 0.85184 0.80552 0.04937  -0.04757 0.01887  57  HIS A C   
422  O O   . HIS A 57  ? 0.59093 0.88570 0.86841 0.04997  -0.04417 0.02287  57  HIS A O   
423  C CB  . HIS A 57  ? 0.52338 0.90553 0.81342 0.01673  -0.04273 -0.00792 57  HIS A CB  
424  C CG  . HIS A 57  ? 0.58815 1.01753 0.88909 0.00390  -0.03902 -0.02497 57  HIS A CG  
425  N ND1 . HIS A 57  ? 0.59160 1.07586 0.90168 0.00693  -0.04372 -0.03295 57  HIS A ND1 
426  C CD2 . HIS A 57  ? 0.65803 1.08963 0.96196 -0.01281 -0.03027 -0.03679 57  HIS A CD2 
427  C CE1 . HIS A 57  ? 0.62037 1.14142 0.94036 -0.00849 -0.03813 -0.05021 57  HIS A CE1 
428  N NE2 . HIS A 57  ? 0.64919 1.13726 0.96528 -0.02110 -0.02926 -0.05261 57  HIS A NE2 
429  N N   . ARG A 58  ? 0.52954 0.85033 0.80460 0.05353  -0.05158 0.02496  58  ARG A N   
430  C CA  . ARG A 58  ? 0.50465 0.78255 0.77033 0.06013  -0.05199 0.03680  58  ARG A CA  
431  C C   . ARG A 58  ? 0.50292 0.78507 0.76661 0.08450  -0.05431 0.04839  58  ARG A C   
432  O O   . ARG A 58  ? 0.47538 0.79488 0.74377 0.09767  -0.05663 0.04791  58  ARG A O   
433  C CB  . ARG A 58  ? 0.50725 0.77260 0.76631 0.04838  -0.05333 0.03590  58  ARG A CB  
434  C CG  . ARG A 58  ? 0.49798 0.76355 0.75568 0.02551  -0.04951 0.02399  58  ARG A CG  
435  C CD  . ARG A 58  ? 0.44092 0.66948 0.69234 0.01629  -0.04446 0.02358  58  ARG A CD  
436  N NE  . ARG A 58  ? 0.39575 0.58929 0.63918 0.02038  -0.04603 0.03251  58  ARG A NE  
437  C CZ  . ARG A 58  ? 0.47811 0.63960 0.71627 0.01941  -0.04357 0.03512  58  ARG A CZ  
438  N NH1 . ARG A 58  ? 0.41532 0.57135 0.65300 0.01393  -0.03915 0.03024  58  ARG A NH1 
439  N NH2 . ARG A 58  ? 0.53174 0.66819 0.76496 0.02426  -0.04538 0.04210  58  ARG A NH2 
440  N N   . LEU A 59  ? 0.48504 0.72896 0.74034 0.09082  -0.05277 0.05843  59  LEU A N   
441  C CA  . LEU A 59  ? 0.51610 0.74993 0.76551 0.11298  -0.05083 0.07007  59  LEU A CA  
442  C C   . LEU A 59  ? 0.50529 0.73493 0.74609 0.12092  -0.05267 0.07768  59  LEU A C   
443  O O   . LEU A 59  ? 0.50652 0.70952 0.74279 0.11079  -0.05221 0.07889  59  LEU A O   
444  C CB  . LEU A 59  ? 0.54461 0.73636 0.79025 0.11313  -0.04481 0.07418  59  LEU A CB  
445  C CG  . LEU A 59  ? 0.63764 0.81037 0.87463 0.13397  -0.03907 0.08534  59  LEU A CG  
446  C CD1 . LEU A 59  ? 0.53881 0.74239 0.77762 0.15321  -0.03880 0.08761  59  LEU A CD1 
447  C CD2 . LEU A 59  ? 0.63791 0.77023 0.87211 0.12888  -0.03238 0.08590  59  LEU A CD2 
448  N N   . PHE A 60  ? 0.50716 0.76275 0.74447 0.14080  -0.05431 0.08327  60  PHE A N   
449  C CA  . PHE A 60  ? 0.53474 0.78321 0.76081 0.15164  -0.05473 0.09218  60  PHE A CA  
450  C C   . PHE A 60  ? 0.56400 0.78037 0.77714 0.17289  -0.04653 0.10545  60  PHE A C   
451  O O   . PHE A 60  ? 0.56150 0.79397 0.77029 0.19482  -0.04469 0.11103  60  PHE A O   
452  C CB  . PHE A 60  ? 0.55735 0.85459 0.78401 0.16053  -0.06150 0.09000  60  PHE A CB  
453  C CG  . PHE A 60  ? 0.52902 0.86031 0.76736 0.13875  -0.06739 0.07506  60  PHE A CG  
454  C CD1 . PHE A 60  ? 0.54465 0.88363 0.79431 0.12188  -0.06656 0.06380  60  PHE A CD1 
455  C CD2 . PHE A 60  ? 0.53469 0.87967 0.77012 0.13201  -0.07160 0.07232  60  PHE A CD2 
456  C CE1 . PHE A 60  ? 0.51021 0.87448 0.76755 0.10059  -0.06884 0.04970  60  PHE A CE1 
457  C CE2 . PHE A 60  ? 0.53394 0.90405 0.77779 0.10987  -0.07448 0.05781  60  PHE A CE2 
458  C CZ  . PHE A 60  ? 0.53668 0.91515 0.79095 0.09394  -0.07234 0.04643  60  PHE A CZ  
459  N N   . THR A 61  ? 0.59555 0.76710 0.80153 0.16658  -0.04059 0.10991  61  THR A N   
460  C CA  . THR A 61  ? 0.63033 0.76270 0.82319 0.18080  -0.02951 0.12013  61  THR A CA  
461  C C   . THR A 61  ? 0.69848 0.82589 0.87484 0.19956  -0.02615 0.13143  61  THR A C   
462  O O   . THR A 61  ? 0.75588 0.88751 0.93062 0.19255  -0.03036 0.13107  61  THR A O   
463  C CB  . THR A 61  ? 0.68606 0.77718 0.87970 0.16281  -0.02417 0.11706  61  THR A CB  
464  O OG1 . THR A 61  ? 0.66429 0.76230 0.87144 0.14586  -0.02834 0.10661  61  THR A OG1 
465  C CG2 . THR A 61  ? 0.70936 0.75933 0.89051 0.17331  -0.01049 0.12435  61  THR A CG2 
466  N N   . LYS A 62  ? 0.70600 0.82089 0.86795 0.22413  -0.01728 0.14195  62  LYS A N   
467  C CA  . LYS A 62  ? 0.74526 0.85465 0.88737 0.24630  -0.01270 0.15423  62  LYS A CA  
468  C C   . LYS A 62  ? 0.80468 0.86972 0.93557 0.23755  -0.00429 0.15847  62  LYS A C   
469  O O   . LYS A 62  ? 0.84183 0.91140 0.96233 0.24474  -0.00559 0.16411  62  LYS A O   
470  C CB  . LYS A 62  ? 0.79147 0.89102 0.91713 0.27621  -0.00258 0.16534  62  LYS A CB  
471  C CG  . LYS A 62  ? 0.82569 0.97998 0.95150 0.29937  -0.01135 0.16738  62  LYS A CG  
472  C CD  . LYS A 62  ? 0.80463 1.00665 0.95596 0.28353  -0.02407 0.15279  62  LYS A CD  
473  C CE  . LYS A 62  ? 0.83679 1.10085 0.99068 0.30454  -0.03301 0.15192  62  LYS A CE  
474  N NZ  . LYS A 62  ? 0.89046 1.15167 1.02984 0.33750  -0.02472 0.16278  62  LYS A NZ  
475  N N   . SER A 63  ? 0.75981 0.78357 0.89208 0.22253  0.00492  0.15527  63  SER A N   
476  C CA  . SER A 63  ? 0.80887 0.79494 0.93216 0.21279  0.01341  0.15728  63  SER A CA  
477  C C   . SER A 63  ? 0.87408 0.88068 1.00863 0.19465  0.00154  0.15055  63  SER A C   
478  O O   . SER A 63  ? 0.97418 0.96931 1.09834 0.19610  0.00437  0.15543  63  SER A O   
479  C CB  . SER A 63  ? 0.85720 0.80250 0.98264 0.19759  0.02486  0.15178  63  SER A CB  
480  O OG  . SER A 63  ? 0.84209 0.80078 0.98842 0.17421  0.01542  0.13886  63  SER A OG  
481  N N   . THR A 64  ? 0.86553 0.90009 1.01953 0.17774  -0.01048 0.13948  64  THR A N   
482  C CA  . THR A 64  ? 0.81076 0.86321 0.97377 0.16092  -0.02053 0.13280  64  THR A CA  
483  C C   . THR A 64  ? 0.80120 0.88838 0.95939 0.17252  -0.02814 0.13643  64  THR A C   
484  O O   . THR A 64  ? 0.80699 0.89677 0.96314 0.16551  -0.03144 0.13588  64  THR A O   
485  C CB  . THR A 64  ? 0.78849 0.85782 0.96934 0.14201  -0.02875 0.12075  64  THR A CB  
486  O OG1 . THR A 64  ? 0.83241 0.87230 1.01668 0.13291  -0.02213 0.11715  64  THR A OG1 
487  C CG2 . THR A 64  ? 0.77694 0.85724 0.96399 0.12475  -0.03643 0.11413  64  THR A CG2 
488  N N   . ILE A 65  ? 0.73228 0.84929 0.88890 0.19038  -0.03120 0.13925  65  ILE A N   
489  C CA  . ILE A 65  ? 0.79907 0.95360 0.95021 0.20357  -0.03829 0.14197  65  ILE A CA  
490  C C   . ILE A 65  ? 0.90844 1.03864 1.03753 0.22127  -0.03026 0.15508  65  ILE A C   
491  O O   . ILE A 65  ? 0.90533 1.05134 1.02933 0.22223  -0.03515 0.15606  65  ILE A O   
492  C CB  . ILE A 65  ? 0.76438 0.96147 0.91970 0.21993  -0.04335 0.14078  65  ILE A CB  
493  C CG1 . ILE A 65  ? 0.72481 0.94992 0.90179 0.19836  -0.05147 0.12585  65  ILE A CG1 
494  C CG2 . ILE A 65  ? 0.67773 0.91478 0.82400 0.23941  -0.04932 0.14481  65  ILE A CG2 
495  C CD1 . ILE A 65  ? 0.66024 0.92689 0.84453 0.21056  -0.05536 0.12221  65  ILE A CD1 
496  N N   . GLU A 66  ? 0.97938 1.06858 1.09343 0.23498  -0.01642 0.16500  66  GLU A N   
497  C CA  . GLU A 66  ? 1.01477 1.07150 1.10523 0.24936  -0.00534 0.17728  66  GLU A CA  
498  C C   . GLU A 66  ? 1.00299 1.03804 1.09638 0.22728  -0.00443 0.17314  66  GLU A C   
499  O O   . GLU A 66  ? 1.02590 1.06182 1.10748 0.23306  -0.00446 0.17843  66  GLU A O   
500  C CB  . GLU A 66  ? 1.07421 1.08421 1.14706 0.26447  0.01267  0.18690  66  GLU A CB  
501  C CG  . GLU A 66  ? 1.17742 1.20413 1.23642 0.29732  0.01498  0.19669  66  GLU A CG  
502  C CD  . GLU A 66  ? 1.31137 1.28861 1.35236 0.31147  0.03449  0.20530  66  GLU A CD  
503  O OE1 . GLU A 66  ? 1.28268 1.21727 1.32635 0.29216  0.04523  0.20074  66  GLU A OE1 
504  O OE2 . GLU A 66  ? 1.28444 1.26649 1.30766 0.34257  0.03970  0.21612  66  GLU A OE2 
505  N N   . TRP A 67  ? 0.91750 0.93638 1.02658 0.20275  -0.00422 0.16328  67  TRP A N   
506  C CA  . TRP A 67  ? 0.91758 0.91667 1.03022 0.18262  -0.00275 0.15865  67  TRP A CA  
507  C C   . TRP A 67  ? 0.95570 0.98706 1.07338 0.17583  -0.01516 0.15498  67  TRP A C   
508  O O   . TRP A 67  ? 0.97032 0.98727 1.08090 0.17123  -0.01216 0.15710  67  TRP A O   
509  C CB  . TRP A 67  ? 0.89531 0.88331 1.02544 0.16028  -0.00330 0.14743  67  TRP A CB  
510  C CG  . TRP A 67  ? 0.88785 0.85983 1.02371 0.14033  -0.00231 0.14116  67  TRP A CG  
511  C CD1 . TRP A 67  ? 0.84030 0.77547 0.97007 0.13403  0.01050  0.14135  67  TRP A CD1 
512  C CD2 . TRP A 67  ? 0.89411 0.88774 1.04181 0.12467  -0.01375 0.13335  67  TRP A CD2 
513  N NE1 . TRP A 67  ? 0.83478 0.77099 0.97401 0.11580  0.00646  0.13367  67  TRP A NE1 
514  C CE2 . TRP A 67  ? 0.89055 0.86040 1.03956 0.11092  -0.00819 0.12960  67  TRP A CE2 
515  C CE3 . TRP A 67  ? 0.87394 0.90406 1.03060 0.12033  -0.02677 0.12824  67  TRP A CE3 
516  C CZ2 . TRP A 67  ? 0.87510 0.85593 1.03312 0.09567  -0.01584 0.12242  67  TRP A CZ2 
517  C CZ3 . TRP A 67  ? 0.91238 0.94905 1.07649 0.10370  -0.03284 0.12096  67  TRP A CZ3 
518  C CH2 . TRP A 67  ? 0.88920 0.90104 1.05347 0.09286  -0.02769 0.11886  67  TRP A CH2 
519  N N   . TRP A 68  ? 0.93666 1.01101 1.06684 0.17299  -0.02808 0.14808  68  TRP A N   
520  C CA  . TRP A 68  ? 0.91124 1.01720 1.04480 0.16618  -0.03839 0.14331  68  TRP A CA  
521  C C   . TRP A 68  ? 0.93692 1.05699 1.05297 0.18769  -0.03831 0.15287  68  TRP A C   
522  O O   . TRP A 68  ? 0.99922 1.13739 1.11398 0.18260  -0.04428 0.15027  68  TRP A O   
523  C CB  . TRP A 68  ? 0.87240 1.02086 1.02234 0.15643  -0.04977 0.13186  68  TRP A CB  
524  C CG  . TRP A 68  ? 0.86443 1.00392 1.02950 0.13238  -0.05179 0.12111  68  TRP A CG  
525  C CD1 . TRP A 68  ? 0.84201 0.97679 1.01712 0.12657  -0.05095 0.11637  68  TRP A CD1 
526  C CD2 . TRP A 68  ? 0.89433 1.02756 1.06390 0.11283  -0.05436 0.11434  68  TRP A CD2 
527  N NE1 . TRP A 68  ? 0.78793 0.91402 0.97232 0.10559  -0.05294 0.10748  68  TRP A NE1 
528  C CE2 . TRP A 68  ? 0.84629 0.97080 1.02723 0.09740  -0.05481 0.10628  68  TRP A CE2 
529  C CE3 . TRP A 68  ? 0.88780 1.02149 1.05157 0.10798  -0.05588 0.11455  68  TRP A CE3 
530  C CZ2 . TRP A 68  ? 0.81851 0.93433 1.00369 0.07939  -0.05637 0.09923  68  TRP A CZ2 
531  C CZ3 . TRP A 68  ? 0.89268 1.01756 1.06211 0.08880  -0.05735 0.10704  68  TRP A CZ3 
532  C CH2 . TRP A 68  ? 0.88674 1.00257 1.06616 0.07553  -0.05744 0.09976  68  TRP A CH2 
533  N N   . LYS A 69  ? 0.92084 1.03373 1.02198 0.21272  -0.03144 0.16382  69  LYS A N   
534  C CA  . LYS A 69  ? 0.98347 1.10824 1.06420 0.23697  -0.03053 0.17435  69  LYS A CA  
535  C C   . LYS A 69  ? 1.04702 1.12940 1.11031 0.23728  -0.01960 0.18269  69  LYS A C   
536  O O   . LYS A 69  ? 1.03185 1.12608 1.08120 0.24848  -0.02139 0.18812  69  LYS A O   
537  C CB  . LYS A 69  ? 0.98107 1.10997 1.04840 0.26678  -0.02541 0.18438  69  LYS A CB  
538  C CG  . LYS A 69  ? 0.91095 1.09029 0.99513 0.26876  -0.03684 0.17572  69  LYS A CG  
539  C CD  . LYS A 69  ? 0.90489 1.09240 0.97523 0.30101  -0.03221 0.18586  69  LYS A CD  
540  C CE  . LYS A 69  ? 0.85481 1.09626 0.94491 0.30037  -0.04362 0.17511  69  LYS A CE  
541  N NZ  . LYS A 69  ? 0.90638 1.16363 0.98389 0.33419  -0.04035 0.18436  69  LYS A NZ  
542  N N   . ASN A 70  ? 1.02814 1.06335 1.09230 0.22428  -0.00803 0.18259  70  ASN A N   
543  C CA  . ASN A 70  ? 1.03667 1.02928 1.08658 0.22068  0.00459  0.18815  70  ASN A CA  
544  C C   . ASN A 70  ? 1.09583 1.09283 1.15908 0.19579  -0.00187 0.17865  70  ASN A C   
545  O O   . ASN A 70  ? 1.15263 1.11875 1.20643 0.19059  0.00773  0.18158  70  ASN A O   
546  C CB  . ASN A 70  ? 1.01095 0.95411 1.05693 0.21608  0.02125  0.18964  70  ASN A CB  
547  C CG  . ASN A 70  ? 1.14623 1.07487 1.17489 0.24140  0.03149  0.20013  70  ASN A CG  
548  O OD1 . ASN A 70  ? 1.17999 1.11666 1.18782 0.26818  0.03327  0.21179  70  ASN A OD1 
549  N ND2 . ASN A 70  ? 1.19352 1.10080 1.22939 0.23434  0.03873  0.19605  70  ASN A ND2 
550  N N   . GLN A 71  ? 1.06767 1.09937 1.15157 0.18012  -0.01614 0.16712  71  GLN A N   
551  C CA  . GLN A 71  ? 1.08815 1.12386 1.18346 0.15786  -0.02189 0.15807  71  GLN A CA  
552  C C   . GLN A 71  ? 1.12138 1.18489 1.20918 0.16273  -0.02934 0.15919  71  GLN A C   
553  O O   . GLN A 71  ? 1.10342 1.19828 1.18448 0.17945  -0.03500 0.16251  71  GLN A O   
554  C CB  . GLN A 71  ? 1.04003 1.09366 1.15730 0.13937  -0.03091 0.14552  71  GLN A CB  
555  C CG  . GLN A 71  ? 1.01082 1.03714 1.13476 0.13369  -0.02366 0.14370  71  GLN A CG  
556  C CD  . GLN A 71  ? 1.05483 1.04538 1.17710 0.12257  -0.01399 0.14297  71  GLN A CD  
557  O OE1 . GLN A 71  ? 1.08265 1.07518 1.21011 0.10904  -0.01745 0.13768  71  GLN A OE1 
558  N NE2 . GLN A 71  ? 1.08199 1.03975 1.19589 0.12841  -0.00056 0.14782  71  GLN A NE2 
559  N N   . SER A 72  ? 1.11701 1.17123 1.20613 0.14817  -0.02934 0.15557  72  SER A N   
560  C CA  . SER A 72  ? 1.15283 1.22714 1.23224 0.15234  -0.03418 0.15706  72  SER A CA  
561  C C   . SER A 72  ? 1.13155 1.25510 1.22108 0.14824  -0.04787 0.14768  72  SER A C   
562  O O   . SER A 72  ? 1.15363 1.28982 1.25952 0.13579  -0.05295 0.13836  72  SER A O   
563  C CB  . SER A 72  ? 1.14754 1.20207 1.22850 0.13542  -0.03128 0.15350  72  SER A CB  
564  O OG  . SER A 72  ? 1.13423 1.19901 1.23365 0.11417  -0.03823 0.14120  72  SER A OG  
565  N N   . PRO A 73  ? 1.15806 1.31073 1.23738 0.15794  -0.05317 0.14900  73  PRO A N   
566  C CA  . PRO A 73  ? 1.11892 1.32064 1.20882 0.14975  -0.06493 0.13678  73  PRO A CA  
567  C C   . PRO A 73  ? 1.09810 1.29829 1.20198 0.12188  -0.06782 0.12379  73  PRO A C   
568  O O   . PRO A 73  ? 1.07059 1.30411 1.18481 0.11075  -0.07464 0.11175  73  PRO A O   
569  C CB  . PRO A 73  ? 1.16979 1.39914 1.24341 0.16573  -0.06849 0.14093  73  PRO A CB  
570  C CG  . PRO A 73  ? 1.21253 1.41266 1.26562 0.19126  -0.05902 0.15808  73  PRO A CG  
571  C CD  . PRO A 73  ? 1.19080 1.33634 1.24685 0.17981  -0.04796 0.16166  73  PRO A CD  
572  N N   . GLU A 74  ? 1.06501 1.22829 1.16850 0.11052  -0.06186 0.12521  74  GLU A N   
573  C CA  . GLU A 74  ? 1.11226 1.27109 1.22750 0.08697  -0.06356 0.11385  74  GLU A CA  
574  C C   . GLU A 74  ? 1.10658 1.25612 1.23566 0.07864  -0.06311 0.10915  74  GLU A C   
575  O O   . GLU A 74  ? 1.06174 1.22756 1.19989 0.06514  -0.06695 0.09846  74  GLU A O   
576  C CB  . GLU A 74  ? 1.08700 1.21406 1.19739 0.07943  -0.05780 0.11642  74  GLU A CB  
577  N N   . ALA A 75  ? 1.11189 1.23424 1.24134 0.08615  -0.05725 0.11652  75  ALA A N   
578  C CA  . ALA A 75  ? 1.04311 1.15807 1.18451 0.08028  -0.05689 0.11248  75  ALA A CA  
579  C C   . ALA A 75  ? 1.01443 1.16232 1.16106 0.08558  -0.06250 0.10879  75  ALA A C   
580  O O   . ALA A 75  ? 0.99418 1.15137 1.15127 0.07366  -0.06522 0.09981  75  ALA A O   
581  C CB  . ALA A 75  ? 1.00376 1.08551 1.14304 0.08778  -0.04847 0.12027  75  ALA A CB  
582  N N   . ARG A 76  ? 1.02126 1.18785 1.15952 0.10437  -0.06367 0.11553  76  ARG A N   
583  C CA  . ARG A 76  ? 0.97521 1.17947 1.11830 0.11216  -0.06925 0.11185  76  ARG A CA  
584  C C   . ARG A 76  ? 0.91296 1.15510 1.06343 0.09722  -0.07623 0.09801  76  ARG A C   
585  O O   . ARG A 76  ? 0.88034 1.15528 1.03902 0.09680  -0.08029 0.09060  76  ARG A O   
586  C CB  . ARG A 76  ? 0.99620 1.21320 1.12515 0.13861  -0.06868 0.12293  76  ARG A CB  
587  C CG  . ARG A 76  ? 0.97493 1.23267 1.10717 0.15238  -0.07393 0.12097  76  ARG A CG  
588  C CD  . ARG A 76  ? 1.03474 1.30324 1.14860 0.18155  -0.07286 0.13330  76  ARG A CD  
589  N NE  . ARG A 76  ? 1.09579 1.31549 1.19583 0.19562  -0.06149 0.14788  76  ARG A NE  
590  C CZ  . ARG A 76  ? 1.15991 1.35078 1.24213 0.20423  -0.05437 0.15821  76  ARG A CZ  
591  N NH1 . ARG A 76  ? 1.15302 1.35906 1.22861 0.20201  -0.05846 0.15681  76  ARG A NH1 
592  N NH2 . ARG A 76  ? 1.13934 1.28374 1.20935 0.21428  -0.04157 0.16948  76  ARG A NH2 
593  N N   . LYS A 77  ? 0.92941 1.16800 1.07662 0.08436  -0.07655 0.09350  77  LYS A N   
594  C CA  . LYS A 77  ? 0.93733 1.20755 1.08974 0.06772  -0.08059 0.07896  77  LYS A CA  
595  C C   . LYS A 77  ? 0.89617 1.15861 1.05970 0.04921  -0.07857 0.06891  77  LYS A C   
596  O O   . LYS A 77  ? 0.86666 1.15637 1.03498 0.03531  -0.07987 0.05559  77  LYS A O   
597  C CB  . LYS A 77  ? 1.01827 1.28102 1.16270 0.05813  -0.07971 0.07675  77  LYS A CB  
598  N N   . ASN A 78  ? 0.91971 1.14566 1.08628 0.04857  -0.07448 0.07436  78  ASN A N   
599  C CA  . ASN A 78  ? 0.88249 1.09872 1.05720 0.03415  -0.07216 0.06642  78  ASN A CA  
600  C C   . ASN A 78  ? 0.84852 1.09750 1.03163 0.03534  -0.07463 0.05976  78  ASN A C   
601  O O   . ASN A 78  ? 0.83089 1.08809 1.01884 0.01946  -0.07275 0.04826  78  ASN A O   
602  C CB  . ASN A 78  ? 0.87231 1.04920 1.04857 0.03689  -0.06829 0.07378  78  ASN A CB  
603  C CG  . ASN A 78  ? 0.88866 1.03489 1.05915 0.03206  -0.06511 0.07713  78  ASN A CG  
604  O OD1 . ASN A 78  ? 0.89519 1.04221 1.06127 0.02148  -0.06463 0.07183  78  ASN A OD1 
605  N ND2 . ASN A 78  ? 0.89714 1.01640 1.06810 0.03858  -0.06198 0.08453  78  ASN A ND2 
606  N N   . ILE A 79  ? 0.81661 1.08351 1.00033 0.05450  -0.07759 0.06674  79  ILE A N   
607  C CA  . ILE A 79  ? 0.75957 1.05214 0.95224 0.05828  -0.07920 0.06223  79  ILE A CA  
608  C C   . ILE A 79  ? 0.71324 1.06073 0.90934 0.05803  -0.08414 0.05179  79  ILE A C   
609  O O   . ILE A 79  ? 0.67581 1.05377 0.87955 0.06437  -0.08624 0.04786  79  ILE A O   
610  C CB  . ILE A 79  ? 0.76207 1.04113 0.95312 0.07992  -0.07812 0.07515  79  ILE A CB  
611  C CG1 . ILE A 79  ? 0.80384 1.09749 0.98447 0.10241  -0.08025 0.08510  79  ILE A CG1 
612  C CG2 . ILE A 79  ? 0.80214 1.03057 0.99014 0.07804  -0.07259 0.08305  79  ILE A CG2 
613  C CD1 . ILE A 79  ? 0.79350 1.07294 0.96951 0.12453  -0.07684 0.09732  79  ILE A CD1 
614  N N   . ALA A 80  ? 0.70984 1.07306 0.90105 0.05017  -0.08580 0.04589  80  ALA A N   
615  C CA  . ALA A 80  ? 0.65746 1.07824 0.85294 0.04877  -0.09048 0.03354  80  ALA A CA  
616  C C   . ALA A 80  ? 0.57543 1.01161 0.78010 0.02215  -0.08657 0.01453  80  ALA A C   
617  O O   . ALA A 80  ? 0.56952 0.97064 0.77156 0.00310  -0.08011 0.01063  80  ALA A O   
618  C CB  . ALA A 80  ? 0.65511 1.09166 0.84084 0.05166  -0.09372 0.03360  80  ALA A CB  
619  N N   . PRO A 81  ? 0.48760 0.97620 0.70174 0.02090  -0.08931 0.00210  81  PRO A N   
620  C CA  . PRO A 81  ? 0.46354 0.96733 0.68565 -0.00608 -0.08324 -0.01762 81  PRO A CA  
621  C C   . PRO A 81  ? 0.57744 1.07246 0.79249 -0.02983 -0.07769 -0.02908 81  PRO A C   
622  O O   . PRO A 81  ? 0.69653 1.20744 0.90527 -0.02642 -0.08159 -0.02919 81  PRO A O   
623  C CB  . PRO A 81  ? 0.42399 0.99704 0.65721 -0.00000 -0.08862 -0.02946 81  PRO A CB  
624  C CG  . PRO A 81  ? 0.44580 1.02447 0.67779 0.03297  -0.09586 -0.01203 81  PRO A CG  
625  C CD  . PRO A 81  ? 0.53649 1.07100 0.75400 0.04559  -0.09677 0.00590  81  PRO A CD  
626  N N   . SER A 82  ? 0.53903 1.00808 0.75351 -0.05352 -0.06748 -0.03902 82  SER A N   
627  C CA  . SER A 82  ? 0.56885 1.01384 0.77313 -0.07643 -0.05859 -0.04819 82  SER A CA  
628  C C   . SER A 82  ? 0.71581 1.17612 0.92328 -0.10384 -0.04761 -0.07000 82  SER A C   
629  O O   . SER A 82  ? 0.79459 1.26892 1.01149 -0.10577 -0.04571 -0.07514 82  SER A O   
630  C CB  . SER A 82  ? 0.62897 1.00779 0.82267 -0.07539 -0.05373 -0.03448 82  SER A CB  
631  O OG  . SER A 82  ? 0.68023 1.03250 0.86266 -0.09733 -0.04278 -0.04389 82  SER A OG  
632  N N   . ASP A 83  ? 0.84362 1.29918 1.04204 -0.12609 -0.03877 -0.08348 83  ASP A N   
633  C CA  . ASP A 83  ? 0.84784 1.30461 1.04465 -0.15547 -0.02381 -0.10445 83  ASP A CA  
634  C C   . ASP A 83  ? 0.85425 1.24451 1.03823 -0.16432 -0.01086 -0.09887 83  ASP A C   
635  O O   . ASP A 83  ? 0.86616 1.24730 1.04543 -0.18725 0.00404  -0.11408 83  ASP A O   
636  C CB  . ASP A 83  ? 0.90636 1.38538 1.09708 -0.17695 -0.01743 -0.12304 83  ASP A CB  
637  C CG  . ASP A 83  ? 0.98979 1.54737 1.19485 -0.17483 -0.02702 -0.13680 83  ASP A CG  
638  O OD1 . ASP A 83  ? 0.95561 1.55131 1.17548 -0.16428 -0.03370 -0.13785 83  ASP A OD1 
639  O OD2 . ASP A 83  ? 1.15572 1.73880 1.35685 -0.18344 -0.02755 -0.14736 83  ASP A OD2 
640  N N   . GLU A 84  ? 0.79259 1.13787 0.97005 -0.14614 -0.01559 -0.07800 84  GLU A N   
641  C CA  . GLU A 84  ? 0.76923 1.05492 0.93437 -0.14816 -0.00609 -0.07004 84  GLU A CA  
642  C C   . GLU A 84  ? 0.67338 0.95287 0.84745 -0.13395 -0.01075 -0.06014 84  GLU A C   
643  O O   . GLU A 84  ? 0.64149 0.87490 0.80703 -0.12725 -0.00781 -0.04874 84  GLU A O   
644  C CB  . GLU A 84  ? 0.76342 1.00762 0.91620 -0.13781 -0.00814 -0.05534 84  GLU A CB  
645  N N   . ASP A 85  ? 0.66790 0.99453 0.85847 -0.12859 -0.01780 -0.06480 85  ASP A N   
646  C CA  . ASP A 85  ? 0.65807 0.98179 0.85768 -0.11355 -0.02281 -0.05520 85  ASP A CA  
647  C C   . ASP A 85  ? 0.62053 0.93179 0.81844 -0.12912 -0.01046 -0.06522 85  ASP A C   
648  O O   . ASP A 85  ? 0.65278 0.98572 0.85123 -0.15068 -0.00050 -0.08400 85  ASP A O   
649  C CB  . ASP A 85  ? 0.66423 1.04275 0.88065 -0.09731 -0.03541 -0.05418 85  ASP A CB  
650  C CG  . ASP A 85  ? 0.65130 1.03326 0.86749 -0.07492 -0.04749 -0.03892 85  ASP A CG  
651  O OD1 . ASP A 85  ? 0.66108 0.99995 0.86747 -0.06904 -0.04761 -0.02639 85  ASP A OD1 
652  O OD2 . ASP A 85  ? 0.64118 1.06967 0.86669 -0.06153 -0.05641 -0.03915 85  ASP A OD2 
653  N N   . VAL A 86  ? 0.55551 0.83423 0.75167 -0.11825 -0.01074 -0.05347 86  VAL A N   
654  C CA  . VAL A 86  ? 0.60673 0.86774 0.79876 -0.13006 0.00101  -0.06034 86  VAL A CA  
655  C C   . VAL A 86  ? 0.52139 0.79677 0.72705 -0.11448 -0.00660 -0.05343 86  VAL A C   
656  O O   . VAL A 86  ? 0.53164 0.80440 0.74290 -0.09298 -0.01825 -0.03846 86  VAL A O   
657  C CB  . VAL A 86  ? 0.64562 0.84434 0.81627 -0.13349 0.01143  -0.05368 86  VAL A CB  
658  C CG1 . VAL A 86  ? 0.55656 0.73854 0.71081 -0.15291 0.02406  -0.06400 86  VAL A CG1 
659  C CG2 . VAL A 86  ? 0.55878 0.73257 0.72851 -0.11056 0.00002  -0.03400 86  VAL A CG2 
660  N N   . SER A 87  ? 0.49600 0.78533 0.70616 -0.12626 0.00149  -0.06512 87  SER A N   
661  C CA  . SER A 87  ? 0.44740 0.74346 0.66792 -0.11309 -0.00322 -0.05908 87  SER A CA  
662  C C   . SER A 87  ? 0.46270 0.70452 0.67123 -0.10280 -0.00229 -0.04427 87  SER A C   
663  O O   . SER A 87  ? 0.53783 0.73930 0.72959 -0.10747 0.00368  -0.04072 87  SER A O   
664  C CB  . SER A 87  ? 0.45614 0.77446 0.68221 -0.12995 0.00724  -0.07557 87  SER A CB  
665  O OG  . SER A 87  ? 0.54302 0.81620 0.75061 -0.14688 0.02347  -0.08023 87  SER A OG  
666  N N   . THR A 88  ? 0.43727 0.68020 0.65430 -0.08680 -0.00892 -0.03532 88  THR A N   
667  C CA  . THR A 88  ? 0.45655 0.65461 0.66418 -0.07496 -0.01041 -0.02147 88  THR A CA  
668  C C   . THR A 88  ? 0.50833 0.66814 0.69917 -0.08691 0.00305  -0.02532 88  THR A C   
669  O O   . THR A 88  ? 0.49532 0.61523 0.67189 -0.08153 0.00451  -0.01673 88  THR A O   
670  C CB  . THR A 88  ? 0.54976 0.75672 0.76955 -0.05547 -0.01971 -0.01166 88  THR A CB  
671  O OG1 . THR A 88  ? 0.50373 0.73181 0.73210 -0.05887 -0.01600 -0.01920 88  THR A OG1 
672  C CG2 . THR A 88  ? 0.45560 0.68901 0.68589 -0.03994 -0.03130 -0.00452 88  THR A CG2 
673  N N   . ILE A 89  ? 0.52010 0.69187 0.71122 -0.10237 0.01368  -0.03835 89  ILE A N   
674  C CA  . ILE A 89  ? 0.52892 0.66097 0.69947 -0.11533 0.02977  -0.04286 89  ILE A CA  
675  C C   . ILE A 89  ? 0.58087 0.68484 0.73235 -0.12580 0.03859  -0.04502 89  ILE A C   
676  O O   . ILE A 89  ? 0.61080 0.66964 0.74230 -0.12066 0.04364  -0.03687 89  ILE A O   
677  C CB  . ILE A 89  ? 0.49954 0.65118 0.67403 -0.13247 0.04161  -0.05827 89  ILE A CB  
678  C CG1 . ILE A 89  ? 0.53509 0.68321 0.71481 -0.12164 0.03932  -0.05285 89  ILE A CG1 
679  C CG2 . ILE A 89  ? 0.55086 0.66882 0.70210 -0.15378 0.06239  -0.06852 89  ILE A CG2 
680  C CD1 . ILE A 89  ? 0.50587 0.59977 0.66417 -0.11329 0.04390  -0.04175 89  ILE A CD1 
681  N N   . ASP A 90  ? 0.67198 0.80407 0.82901 -0.13915 0.04021  -0.05602 90  ASP A N   
682  C CA  . ASP A 90  ? 0.69303 0.80008 0.83213 -0.15025 0.04942  -0.05931 90  ASP A CA  
683  C C   . ASP A 90  ? 0.70281 0.77929 0.83330 -0.13213 0.04072  -0.04269 90  ASP A C   
684  O O   . ASP A 90  ? 0.73427 0.76695 0.84182 -0.13368 0.05076  -0.03934 90  ASP A O   
685  C CB  . ASP A 90  ? 0.70136 0.85373 0.85291 -0.16374 0.04780  -0.07289 90  ASP A CB  
686  C CG  . ASP A 90  ? 0.82369 0.95320 0.95676 -0.17922 0.05960  -0.07968 90  ASP A CG  
687  O OD1 . ASP A 90  ? 0.85275 0.92907 0.96204 -0.17763 0.06910  -0.07249 90  ASP A OD1 
688  O OD2 . ASP A 90  ? 0.82827 0.99586 0.97044 -0.19234 0.05941  -0.09286 90  ASP A OD2 
689  N N   . GLY A 91  ? 0.58197 0.67985 0.72942 -0.11402 0.02324  -0.03220 91  GLY A N   
690  C CA  . GLY A 91  ? 0.53117 0.60423 0.67268 -0.09838 0.01548  -0.01824 91  GLY A CA  
691  C C   . GLY A 91  ? 0.57892 0.60958 0.70455 -0.08961 0.01998  -0.00994 91  GLY A C   
692  O O   . GLY A 91  ? 0.59109 0.59131 0.70147 -0.08420 0.02205  -0.00362 91  GLY A O   
693  N N   . ILE A 92  ? 0.58830 0.61855 0.71715 -0.08647 0.02103  -0.00973 92  ILE A N   
694  C CA  . ILE A 92  ? 0.59568 0.58953 0.70953 -0.07545 0.02353  -0.00141 92  ILE A CA  
695  C C   . ILE A 92  ? 0.63900 0.59351 0.72418 -0.08510 0.04141  -0.00534 92  ILE A C   
696  O O   . ILE A 92  ? 0.66486 0.58584 0.73142 -0.07438 0.04393  0.00253  92  ILE A O   
697  C CB  . ILE A 92  ? 0.55791 0.56072 0.68184 -0.06835 0.01964  0.00034  92  ILE A CB  
698  C CG1 . ILE A 92  ? 0.54512 0.52131 0.65971 -0.05208 0.01580  0.01055  92  ILE A CG1 
699  C CG2 . ILE A 92  ? 0.56721 0.56439 0.68259 -0.08224 0.03392  -0.00940 92  ILE A CG2 
700  C CD1 . ILE A 92  ? 0.51714 0.49989 0.64193 -0.03867 0.00247  0.01907  92  ILE A CD1 
701  N N   . ALA A 93  ? 0.62345 0.58141 0.70331 -0.10503 0.05510  -0.01801 93  ALA A N   
702  C CA  . ALA A 93  ? 0.66210 0.57850 0.71176 -0.11574 0.07504  -0.02232 93  ALA A CA  
703  C C   . ALA A 93  ? 0.69706 0.59429 0.73429 -0.11142 0.07488  -0.01722 93  ALA A C   
704  O O   . ALA A 93  ? 0.70165 0.55662 0.71262 -0.10326 0.08371  -0.01066 93  ALA A O   
705  C CB  . ALA A 93  ? 0.64894 0.57763 0.69804 -0.14148 0.09046  -0.03963 93  ALA A CB  
706  N N   . LYS A 94  ? 0.70512 0.63383 0.76025 -0.11461 0.06451  -0.01945 94  LYS A N   
707  C CA  . LYS A 94  ? 0.65530 0.57004 0.70186 -0.10928 0.06228  -0.01405 94  LYS A CA  
708  C C   . LYS A 94  ? 0.63283 0.53249 0.67761 -0.08570 0.05104  0.00091  94  LYS A C   
709  O O   . LYS A 94  ? 0.64267 0.51327 0.66886 -0.07844 0.05537  0.00645  94  LYS A O   
710  C CB  . LYS A 94  ? 0.65442 0.61022 0.72227 -0.11562 0.05182  -0.01891 94  LYS A CB  
711  C CG  . LYS A 94  ? 0.70682 0.68042 0.77487 -0.13967 0.06318  -0.03568 94  LYS A CG  
712  C CD  . LYS A 94  ? 0.72610 0.74112 0.81291 -0.14221 0.05148  -0.03922 94  LYS A CD  
713  C CE  . LYS A 94  ? 0.85429 0.88969 0.94002 -0.16761 0.06344  -0.05827 94  LYS A CE  
714  N NZ  . LYS A 94  ? 0.88333 0.87758 0.94154 -0.18126 0.08207  -0.06386 94  LYS A NZ  
715  N N   . PHE A 95  ? 0.63535 0.55606 0.69940 -0.07364 0.03704  0.00669  95  PHE A N   
716  C CA  . PHE A 95  ? 0.65282 0.55990 0.71429 -0.05361 0.02860  0.01806  95  PHE A CA  
717  C C   . PHE A 95  ? 0.69486 0.56113 0.72737 -0.04740 0.04110  0.02097  95  PHE A C   
718  O O   . PHE A 95  ? 0.67714 0.52224 0.69491 -0.03449 0.04120  0.02782  95  PHE A O   
719  C CB  . PHE A 95  ? 0.57290 0.50557 0.65711 -0.04444 0.01513  0.02161  95  PHE A CB  
720  C CG  . PHE A 95  ? 0.57309 0.49574 0.65605 -0.02632 0.00721  0.03047  95  PHE A CG  
721  C CD1 . PHE A 95  ? 0.50523 0.43627 0.59744 -0.01772 -0.00280 0.03568  95  PHE A CD1 
722  C CD2 . PHE A 95  ? 0.56468 0.47042 0.63622 -0.01835 0.01064  0.03251  95  PHE A CD2 
723  C CE1 . PHE A 95  ? 0.53295 0.45902 0.62518 -0.00279 -0.00936 0.04132  95  PHE A CE1 
724  C CE2 . PHE A 95  ? 0.53417 0.43570 0.60479 -0.00198 0.00317  0.03866  95  PHE A CE2 
725  C CZ  . PHE A 95  ? 0.54928 0.46215 0.63089 0.00521  -0.00672 0.04234  95  PHE A CZ  
726  N N   . ASN A 96  ? 0.75253 0.60789 0.77546 -0.05521 0.05225  0.01590  96  ASN A N   
727  C CA  . ASN A 96  ? 0.77272 0.58836 0.76610 -0.04622 0.06416  0.02010  96  ASN A CA  
728  C C   . ASN A 96  ? 0.82473 0.60170 0.78685 -0.04984 0.08127  0.01954  96  ASN A C   
729  O O   . ASN A 96  ? 0.84541 0.59032 0.78213 -0.03376 0.08672  0.02730  96  ASN A O   
730  C CB  . ASN A 96  ? 0.78232 0.59442 0.77237 -0.05380 0.07286  0.01497  96  ASN A CB  
731  C CG  . ASN A 96  ? 0.79796 0.63747 0.81117 -0.04412 0.05759  0.01820  96  ASN A CG  
732  O OD1 . ASN A 96  ? 0.80493 0.65557 0.82900 -0.02853 0.04309  0.02553  96  ASN A OD1 
733  N ND2 . ASN A 96  ? 0.81178 0.65899 0.82999 -0.05327 0.06277  0.01220  96  ASN A ND2 
734  N N   . ASP A 97  ? 0.86566 0.64600 0.82829 -0.06991 0.09023  0.01008  97  ASP A N   
735  C CA  . ASP A 97  ? 0.88884 0.63319 0.82320 -0.07392 0.10618  0.00919  97  ASP A CA  
736  C C   . ASP A 97  ? 0.89464 0.63194 0.82461 -0.05357 0.09647  0.02016  97  ASP A C   
737  O O   . ASP A 97  ? 0.94911 0.64675 0.84786 -0.04129 0.10782  0.02627  97  ASP A O   
738  C CB  . ASP A 97  ? 0.90440 0.66466 0.84705 -0.09869 0.11280  -0.00378 97  ASP A CB  
739  C CG  . ASP A 97  ? 0.93202 0.69307 0.87201 -0.12110 0.12813  -0.01723 97  ASP A CG  
740  O OD1 . ASP A 97  ? 1.01934 0.74983 0.93865 -0.11849 0.14098  -0.01578 97  ASP A OD1 
741  O OD2 . ASP A 97  ? 0.94304 0.73576 0.90037 -0.14137 0.12824  -0.02996 97  ASP A OD2 
742  N N   . TYR A 98  ? 0.78244 0.55761 0.74218 -0.04869 0.07633  0.02284  98  TYR A N   
743  C CA  . TYR A 98  ? 0.72020 0.49122 0.67716 -0.03243 0.06849  0.03116  98  TYR A CA  
744  C C   . TYR A 98  ? 0.78121 0.54024 0.72791 -0.00863 0.06370  0.04068  98  TYR A C   
745  O O   . TYR A 98  ? 0.82203 0.55646 0.74648 0.00575  0.06883  0.04657  98  TYR A O   
746  C CB  . TYR A 98  ? 0.72852 0.53934 0.71685 -0.03570 0.05152  0.03051  98  TYR A CB  
747  C CG  . TYR A 98  ? 0.79704 0.61567 0.79265 -0.01944 0.03915  0.03843  98  TYR A CG  
748  C CD1 . TYR A 98  ? 0.84156 0.64399 0.82356 0.00071  0.03794  0.04597  98  TYR A CD1 
749  C CD2 . TYR A 98  ? 0.74300 0.57832 0.75100 -0.02591 0.03374  0.03687  98  TYR A CD2 
750  C CE1 . TYR A 98  ? 0.77821 0.59026 0.76701 0.01338  0.02837  0.05094  98  TYR A CE1 
751  C CE2 . TYR A 98  ? 0.76938 0.60938 0.78202 -0.01360 0.02530  0.04277  98  TYR A CE2 
752  C CZ  . TYR A 98  ? 0.77341 0.60207 0.77688 0.00544  0.02298  0.04931  98  TYR A CZ  
753  O OH  . TYR A 98  ? 0.77556 0.61231 0.78480 0.01690  0.01520  0.05356  98  TYR A OH  
754  N N   . ILE A 99  ? 0.78051 0.55576 0.74047 -0.00353 0.05530  0.04173  99  ILE A N   
755  C CA  . ILE A 99  ? 0.76377 0.53024 0.71277 0.01868  0.05119  0.04914  99  ILE A CA  
756  C C   . ILE A 99  ? 0.87682 0.59679 0.78427 0.02680  0.07040  0.05226  99  ILE A C   
757  O O   . ILE A 99  ? 0.89109 0.59586 0.77919 0.04793  0.07083  0.05936  99  ILE A O   
758  C CB  . ILE A 99  ? 0.77451 0.56557 0.74421 0.02041  0.04037  0.04831  99  ILE A CB  
759  C CG1 . ILE A 99  ? 0.70753 0.53906 0.71388 0.01578  0.02319  0.04674  99  ILE A CG1 
760  C CG2 . ILE A 99  ? 0.81853 0.60398 0.77667 0.04263  0.03610  0.05424  99  ILE A CG2 
761  C CD1 . ILE A 99  ? 0.66476 0.51010 0.68051 0.03040  0.01093  0.05133  99  ILE A CD1 
762  N N   . ASN A 100 ? 0.89540 0.59181 0.78695 0.01052  0.08785  0.04659  100 ASN A N   
763  C CA  . ASN A 100 ? 0.89764 0.54370 0.74600 0.01707  0.10965  0.04951  100 ASN A CA  
764  C C   . ASN A 100 ? 0.92308 0.53711 0.74454 0.02215  0.12193  0.05257  100 ASN A C   
765  O O   . ASN A 100 ? 0.97616 0.54554 0.75775 0.03505  0.13922  0.05797  100 ASN A O   
766  C CB  . ASN A 100 ? 0.93539 0.56359 0.77398 -0.00554 0.12788  0.04053  100 ASN A CB  
767  C CG  . ASN A 100 ? 0.92801 0.57487 0.78142 -0.00667 0.12146  0.03885  100 ASN A CG  
768  O OD1 . ASN A 100 ? 0.94559 0.59801 0.79866 0.01357  0.11137  0.04615  100 ASN A OD1 
769  N ND2 . ASN A 100 ? 0.93327 0.58966 0.79796 -0.03058 0.12872  0.02822  100 ASN A ND2 
770  N N   . ALA A 101 ? 0.93675 0.56978 0.77626 0.01337  0.11482  0.04965  101 ALA A N   
771  C CA  . ALA A 101 ? 0.97832 0.57948 0.79174 0.01635  0.12803  0.05163  101 ALA A CA  
772  C C   . ALA A 101 ? 1.00403 0.62209 0.82573 0.03740  0.11274  0.05940  101 ALA A C   
773  O O   . ALA A 101 ? 1.07835 0.68060 0.88745 0.03819  0.11946  0.06027  101 ALA A O   
774  C CB  . ALA A 101 ? 0.97104 0.57471 0.79229 -0.01258 0.13670  0.04039  101 ALA A CB  
775  N N   . HIS A 102 ? 0.91592 0.56613 0.75831 0.05361  0.09331  0.06399  102 HIS A N   
776  C CA  . HIS A 102 ? 0.90816 0.58230 0.76465 0.06906  0.07819  0.06839  102 HIS A CA  
777  C C   . HIS A 102 ? 0.90013 0.58447 0.75234 0.09620  0.06869  0.07487  102 HIS A C   
778  O O   . HIS A 102 ? 0.88457 0.60561 0.76244 0.10409  0.05108  0.07508  102 HIS A O   
779  C CB  . HIS A 102 ? 0.83187 0.55048 0.73062 0.05462  0.06051  0.06350  102 HIS A CB  
780  C CG  . HIS A 102 ? 0.86356 0.58002 0.76696 0.03434  0.06622  0.05806  102 HIS A CG  
781  N ND1 . HIS A 102 ? 0.87537 0.58629 0.77926 0.01123  0.07593  0.05019  102 HIS A ND1 
782  C CD2 . HIS A 102 ? 0.86711 0.59112 0.77706 0.03311  0.06263  0.05821  102 HIS A CD2 
783  C CE1 . HIS A 102 ? 0.89488 0.61083 0.80467 -0.00304 0.07790  0.04542  102 HIS A CE1 
784  N NE2 . HIS A 102 ? 0.92092 0.64310 0.83387 0.01002  0.07003  0.05074  102 HIS A NE2 
785  N N   . ASN A 103 ? 0.87592 0.52850 0.69442 0.11113  0.08103  0.07960  103 ASN A N   
786  C CA  . ASN A 103 ? 0.92625 0.58627 0.73302 0.14123  0.07409  0.08602  103 ASN A CA  
787  C C   . ASN A 103 ? 0.91205 0.61784 0.75223 0.14309  0.05383  0.08285  103 ASN A C   
788  O O   . ASN A 103 ? 0.91180 0.64771 0.76361 0.16008  0.04009  0.08362  103 ASN A O   
789  C CB  . ASN A 103 ? 1.02370 0.68699 0.82287 0.15962  0.07140  0.09023  103 ASN A CB  
790  C CG  . ASN A 103 ? 1.07334 0.68445 0.82493 0.17312  0.09333  0.09682  103 ASN A CG  
791  O OD1 . ASN A 103 ? 1.07290 0.66084 0.81484 0.16216  0.10467  0.09596  103 ASN A OD1 
792  N ND2 . ASN A 103 ? 1.19000 0.78057 0.90880 0.19849  0.10048  0.10365  103 ASN A ND2 
793  N N   . ILE A 104 ? 0.90737 0.61835 0.76191 0.12548  0.05320  0.07839  104 ILE A N   
794  C CA  . ILE A 104 ? 0.86207 0.60880 0.74331 0.12642  0.03758  0.07531  104 ILE A CA  
795  C C   . ILE A 104 ? 0.90506 0.63292 0.76025 0.14052  0.04466  0.07852  104 ILE A C   
796  O O   . ILE A 104 ? 0.93723 0.62902 0.76829 0.13336  0.06143  0.07954  104 ILE A O   
797  C CB  . ILE A 104 ? 0.81750 0.58459 0.73196 0.10010  0.03168  0.06874  104 ILE A CB  
798  C CG1 . ILE A 104 ? 0.87197 0.65457 0.80698 0.08877  0.02603  0.06663  104 ILE A CG1 
799  C CG2 . ILE A 104 ? 0.80748 0.60785 0.74778 0.10136  0.01723  0.06568  104 ILE A CG2 
800  C CD1 . ILE A 104 ? 0.81243 0.62354 0.76315 0.10235  0.01205  0.06749  104 ILE A CD1 
801  N N   . ASP A 105 ? 0.90693 0.65927 0.76555 0.16047  0.03292  0.07939  105 ASP A N   
802  C CA  . ASP A 105 ? 0.94004 0.68165 0.77631 0.17603  0.03675  0.08209  105 ASP A CA  
803  C C   . ASP A 105 ? 0.94761 0.71484 0.81224 0.16231  0.02702  0.07595  105 ASP A C   
804  O O   . ASP A 105 ? 0.90322 0.71136 0.80127 0.15923  0.01048  0.07061  105 ASP A O   
805  C CB  . ASP A 105 ? 0.97023 0.72830 0.79297 0.20707  0.02928  0.08535  105 ASP A CB  
806  C CG  . ASP A 105 ? 1.00712 0.76104 0.80711 0.22666  0.03076  0.08788  105 ASP A CG  
807  O OD1 . ASP A 105 ? 1.01586 0.75504 0.81240 0.21595  0.03676  0.08702  105 ASP A OD1 
808  O OD2 . ASP A 105 ? 1.05055 0.81984 0.83663 0.25411  0.02517  0.09021  105 ASP A OD2 
809  N N   . PRO A 106 ? 0.96360 0.70716 0.81498 0.15416  0.03791  0.07612  106 PRO A N   
810  C CA  . PRO A 106 ? 0.92062 0.68828 0.79958 0.14073  0.02929  0.07022  106 PRO A CA  
811  C C   . PRO A 106 ? 0.90829 0.71018 0.79986 0.15579  0.01409  0.06775  106 PRO A C   
812  O O   . PRO A 106 ? 0.87065 0.70044 0.79323 0.14378  0.00370  0.06174  106 PRO A O   
813  C CB  . PRO A 106 ? 0.92588 0.65704 0.77910 0.13471  0.04659  0.07170  106 PRO A CB  
814  C CG  . PRO A 106 ? 0.97268 0.66207 0.79525 0.13298  0.06503  0.07573  106 PRO A CG  
815  C CD  . PRO A 106 ? 0.97309 0.66529 0.78402 0.15470  0.06032  0.08093  106 PRO A CD  
816  N N   . TRP A 107 ? 0.91236 0.71421 0.78030 0.18202  0.01299  0.07151  107 TRP A N   
817  C CA  . TRP A 107 ? 0.91408 0.75187 0.79286 0.19572  -0.00081 0.06700  107 TRP A CA  
818  C C   . TRP A 107 ? 0.87744 0.75491 0.77649 0.20433  -0.01522 0.06241  107 TRP A C   
819  O O   . TRP A 107 ? 0.81920 0.73484 0.74286 0.20335  -0.02811 0.05426  107 TRP A O   
820  C CB  . TRP A 107 ? 0.97611 0.79528 0.81531 0.22099  0.00639  0.07243  107 TRP A CB  
821  C CG  . TRP A 107 ? 0.96050 0.74979 0.78496 0.21191  0.01832  0.07424  107 TRP A CG  
822  C CD1 . TRP A 107 ? 1.00480 0.74539 0.79964 0.20666  0.03806  0.08029  107 TRP A CD1 
823  C CD2 . TRP A 107 ? 0.95615 0.76224 0.79453 0.20612  0.01256  0.06895  107 TRP A CD2 
824  N NE1 . TRP A 107 ? 0.97586 0.70332 0.76640 0.19744  0.04481  0.07889  107 TRP A NE1 
825  C CE2 . TRP A 107 ? 0.97890 0.74583 0.79572 0.19775  0.02898  0.07253  107 TRP A CE2 
826  C CE3 . TRP A 107 ? 0.96569 0.81537 0.83231 0.20602  -0.00365 0.06062  107 TRP A CE3 
827  C CZ2 . TRP A 107 ? 0.98218 0.75320 0.80525 0.19066  0.02875  0.06888  107 TRP A CZ2 
828  C CZ3 . TRP A 107 ? 0.93718 0.78902 0.80907 0.19890  -0.00354 0.05708  107 TRP A CZ3 
829  C CH2 . TRP A 107 ? 0.96945 0.78268 0.81982 0.19208  0.01207  0.06167  107 TRP A CH2 
830  N N   . LYS A 108 ? 0.87505 0.74538 0.76540 0.21123  -0.01261 0.06621  108 LYS A N   
831  C CA  . LYS A 108 ? 0.84422 0.75380 0.75116 0.22172  -0.02529 0.06123  108 LYS A CA  
832  C C   . LYS A 108 ? 0.82918 0.75143 0.76614 0.20273  -0.02993 0.05790  108 LYS A C   
833  O O   . LYS A 108 ? 0.78251 0.74127 0.74025 0.20583  -0.04073 0.05143  108 LYS A O   
834  C CB  . LYS A 108 ? 0.81880 0.71864 0.68956 0.25273  -0.02050 0.06785  108 LYS A CB  
835  N N   . SER A 109 ? 0.80405 0.69971 0.74422 0.18286  -0.02190 0.06109  109 SER A N   
836  C CA  . SER A 109 ? 0.79956 0.70604 0.76489 0.16668  -0.02581 0.05872  109 SER A CA  
837  C C   . SER A 109 ? 0.76241 0.70126 0.76606 0.15000  -0.03699 0.05059  109 SER A C   
838  O O   . SER A 109 ? 0.76558 0.71274 0.77630 0.14704  -0.03986 0.04712  109 SER A O   
839  C CB  . SER A 109 ? 0.80984 0.68080 0.76537 0.15107  -0.01357 0.06352  109 SER A CB  
840  O OG  . SER A 109 ? 0.84580 0.68158 0.76337 0.16534  -0.00041 0.07059  109 SER A OG  
841  N N   . GLN A 110 ? 0.72601 0.68054 0.75272 0.13925  -0.04197 0.04778  110 GLN A N   
842  C CA  . GLN A 110 ? 0.65124 0.63147 0.71101 0.12427  -0.05006 0.04079  110 GLN A CA  
843  C C   . GLN A 110 ? 0.66054 0.62941 0.73334 0.10513  -0.04711 0.04332  110 GLN A C   
844  O O   . GLN A 110 ? 0.70593 0.65894 0.76911 0.10352  -0.04206 0.04780  110 GLN A O   
845  C CB  . GLN A 110 ? 0.64907 0.66392 0.72538 0.13006  -0.05870 0.03314  110 GLN A CB  
846  C CG  . GLN A 110 ? 0.66103 0.69885 0.73278 0.14513  -0.06398 0.02679  110 GLN A CG  
847  C CD  . GLN A 110 ? 0.71266 0.79039 0.79986 0.15131  -0.07189 0.01658  110 GLN A CD  
848  O OE1 . GLN A 110 ? 0.74147 0.82789 0.84004 0.14681  -0.07282 0.01510  110 GLN A OE1 
849  N NE2 . GLN A 110 ? 0.70503 0.80935 0.79309 0.16089  -0.07727 0.00827  110 GLN A NE2 
850  N N   . GLY A 111 ? 0.58757 0.56361 0.67956 0.09193  -0.04945 0.04055  111 GLY A N   
851  C CA  . GLY A 111 ? 0.55400 0.52571 0.66000 0.07588  -0.04801 0.04235  111 GLY A CA  
852  C C   . GLY A 111 ? 0.64702 0.64098 0.77889 0.06924  -0.05426 0.03758  111 GLY A C   
853  O O   . GLY A 111 ? 0.63565 0.64507 0.77782 0.07072  -0.05807 0.03172  111 GLY A O   
854  N N   . TRP A 112 ? 0.60076 0.59467 0.74151 0.06141  -0.05399 0.03967  112 TRP A N   
855  C CA  . TRP A 112 ? 0.52430 0.53414 0.68464 0.05626  -0.05734 0.03602  112 TRP A CA  
856  C C   . TRP A 112 ? 0.57556 0.58116 0.74666 0.04515  -0.05578 0.03949  112 TRP A C   
857  O O   . TRP A 112 ? 0.56485 0.55916 0.72833 0.04146  -0.05300 0.04426  112 TRP A O   
858  C CB  . TRP A 112 ? 0.54036 0.55475 0.69805 0.06065  -0.05798 0.03578  112 TRP A CB  
859  C CG  . TRP A 112 ? 0.52377 0.54773 0.67205 0.07399  -0.06007 0.03209  112 TRP A CG  
860  C CD1 . TRP A 112 ? 0.57299 0.58429 0.69836 0.08608  -0.05748 0.03613  112 TRP A CD1 
861  C CD2 . TRP A 112 ? 0.54072 0.59049 0.70065 0.07789  -0.06440 0.02298  112 TRP A CD2 
862  N NE1 . TRP A 112 ? 0.58972 0.61897 0.71095 0.10016  -0.06108 0.03116  112 TRP A NE1 
863  C CE2 . TRP A 112 ? 0.58608 0.64214 0.72990 0.09447  -0.06596 0.02202  112 TRP A CE2 
864  C CE3 . TRP A 112 ? 0.54368 0.61183 0.72496 0.06881  -0.06589 0.01467  112 TRP A CE3 
865  C CZ2 . TRP A 112 ? 0.58350 0.66971 0.73416 0.10248  -0.07075 0.01219  112 TRP A CZ2 
866  C CZ3 . TRP A 112 ? 0.52873 0.62444 0.71719 0.07386  -0.06924 0.00375  112 TRP A CZ3 
867  C CH2 . TRP A 112 ? 0.54044 0.64798 0.71482 0.09065  -0.07253 0.00218  112 TRP A CH2 
868  N N   . CYS A 113 ? 0.59359 0.60854 0.78109 0.04016  -0.05657 0.03649  113 CYS A N   
869  C CA  . CYS A 113 ? 0.62893 0.64053 0.82459 0.03312  -0.05468 0.04069  113 CYS A CA  
870  C C   . CYS A 113 ? 0.62083 0.63862 0.83015 0.02950  -0.05304 0.03667  113 CYS A C   
871  O O   . CYS A 113 ? 0.63391 0.66121 0.84846 0.03015  -0.05340 0.02894  113 CYS A O   
872  C CB  . CYS A 113 ? 0.64694 0.65373 0.84200 0.03083  -0.05355 0.04415  113 CYS A CB  
873  S SG  . CYS A 113 ? 0.72907 0.73899 0.93007 0.03208  -0.05337 0.03952  113 CYS A SG  
874  N N   . ARG A 114 ? 0.56953 0.58215 0.78331 0.02570  -0.05020 0.04135  114 ARG A N   
875  C CA  . ARG A 114 ? 0.69085 0.70221 0.91400 0.02191  -0.04530 0.03866  114 ARG A CA  
876  C C   . ARG A 114 ? 0.70334 0.70885 0.92910 0.02211  -0.04229 0.04030  114 ARG A C   
877  O O   . ARG A 114 ? 0.72014 0.72154 0.94283 0.02443  -0.04222 0.04763  114 ARG A O   
878  C CB  . ARG A 114 ? 0.66778 0.67377 0.89101 0.01980  -0.04205 0.04351  114 ARG A CB  
879  C CG  . ARG A 114 ? 0.64224 0.65411 0.86681 0.01800  -0.04221 0.03924  114 ARG A CG  
880  C CD  . ARG A 114 ? 0.69532 0.70025 0.92001 0.01521  -0.03745 0.04332  114 ARG A CD  
881  N NE  . ARG A 114 ? 0.65962 0.67195 0.88559 0.01369  -0.03793 0.03899  114 ARG A NE  
882  C CZ  . ARG A 114 ? 0.70494 0.72488 0.93918 0.00908  -0.03399 0.02968  114 ARG A CZ  
883  N NH1 . ARG A 114 ? 0.68753 0.70525 0.92873 0.00371  -0.02766 0.02348  114 ARG A NH1 
884  N NH2 . ARG A 114 ? 0.70478 0.73563 0.94018 0.00941  -0.03556 0.02547  114 ARG A NH2 
885  N N   . GLY A 115 ? 0.68266 0.68953 0.91409 0.01986  -0.03935 0.03277  115 GLY A N   
886  C CA  . GLY A 115 ? 0.77119 0.77220 1.00332 0.02126  -0.03682 0.03408  115 GLY A CA  
887  C C   . GLY A 115 ? 0.66433 0.67079 0.89173 0.02495  -0.04270 0.03461  115 GLY A C   
888  O O   . GLY A 115 ? 0.64355 0.64821 0.86707 0.02755  -0.04414 0.04106  115 GLY A O   
889  N N   . MET A 116 ? 0.69152 0.70618 0.91844 0.02532  -0.04558 0.02706  116 MET A N   
890  C CA  . MET A 116 ? 0.71081 0.72760 0.93091 0.02942  -0.04923 0.02674  116 MET A CA  
891  C C   . MET A 116 ? 0.68547 0.69648 0.90661 0.02970  -0.04686 0.02957  116 MET A C   
892  O O   . MET A 116 ? 0.68795 0.69765 0.90253 0.03191  -0.04858 0.03294  116 MET A O   
893  C CB  . MET A 116 ? 0.67898 0.70709 0.89923 0.03116  -0.05144 0.01704  116 MET A CB  
894  C CG  . MET A 116 ? 0.66653 0.69622 0.87698 0.03716  -0.05452 0.01623  116 MET A CG  
895  S SD  . MET A 116 ? 0.72587 0.77578 0.93668 0.04148  -0.05805 0.00419  116 MET A SD  
896  C CE  . MET A 116 ? 0.70925 0.75702 0.90681 0.04943  -0.05998 0.00431  116 MET A CE  
897  N N   . SER A 117 ? 0.66851 0.67476 0.89673 0.02748  -0.04158 0.02826  117 SER A N   
898  C CA  . SER A 117 ? 0.64017 0.64133 0.86907 0.02954  -0.03871 0.03109  117 SER A CA  
899  C C   . SER A 117 ? 0.67343 0.67262 0.90116 0.03281  -0.03814 0.04055  117 SER A C   
900  O O   . SER A 117 ? 0.66954 0.66728 0.89826 0.03620  -0.03561 0.04327  117 SER A O   
901  C CB  . SER A 117 ? 0.61840 0.61252 0.85267 0.02691  -0.03141 0.02555  117 SER A CB  
902  O OG  . SER A 117 ? 0.64802 0.63374 0.88468 0.02427  -0.02523 0.02657  117 SER A OG  
903  N N   . PHE A 118 ? 0.74057 0.74202 0.96615 0.03249  -0.04045 0.04499  118 PHE A N   
904  C CA  . PHE A 118 ? 0.73606 0.74133 0.96019 0.03559  -0.04102 0.05250  118 PHE A CA  
905  C C   . PHE A 118 ? 0.73088 0.74426 0.94993 0.03329  -0.04563 0.05309  118 PHE A C   
906  O O   . PHE A 118 ? 0.71388 0.73520 0.93252 0.03403  -0.04611 0.05475  118 PHE A O   
907  C CB  . PHE A 118 ? 0.77228 0.77296 0.99642 0.03660  -0.03845 0.05684  118 PHE A CB  
908  C CG  . PHE A 118 ? 0.81783 0.82654 1.03935 0.04086  -0.04007 0.06407  118 PHE A CG  
909  C CD1 . PHE A 118 ? 0.80964 0.82287 1.03146 0.04848  -0.03807 0.06872  118 PHE A CD1 
910  C CD2 . PHE A 118 ? 0.81145 0.82509 1.02976 0.03809  -0.04339 0.06569  118 PHE A CD2 
911  C CE1 . PHE A 118 ? 0.79192 0.81874 1.01153 0.05366  -0.04032 0.07417  118 PHE A CE1 
912  C CE2 . PHE A 118 ? 0.77935 0.80412 0.99527 0.04148  -0.04512 0.07080  118 PHE A CE2 
913  C CZ  . PHE A 118 ? 0.78065 0.81398 0.99755 0.04951  -0.04400 0.07473  118 PHE A CZ  
914  N N   . ASP A 119 ? 0.70576 0.71721 0.92021 0.03029  -0.04785 0.05096  119 ASP A N   
915  C CA  . ASP A 119 ? 0.66798 0.68158 0.87448 0.02744  -0.04954 0.05144  119 ASP A CA  
916  C C   . ASP A 119 ? 0.65137 0.66262 0.85161 0.02667  -0.04878 0.04820  119 ASP A C   
917  O O   . ASP A 119 ? 0.66267 0.67766 0.85972 0.02348  -0.04729 0.04835  119 ASP A O   
918  C CB  . ASP A 119 ? 0.69444 0.70380 0.89595 0.02644  -0.05073 0.05093  119 ASP A CB  
919  C CG  . ASP A 119 ? 0.71905 0.73083 0.92315 0.02556  -0.05082 0.05492  119 ASP A CG  
920  O OD1 . ASP A 119 ? 0.72760 0.74618 0.93179 0.02467  -0.05084 0.05801  119 ASP A OD1 
921  O OD2 . ASP A 119 ? 0.74384 0.75281 0.95018 0.02595  -0.05060 0.05434  119 ASP A OD2 
922  N N   . PHE A 120 ? 0.60340 0.60981 0.80126 0.02929  -0.04916 0.04444  120 PHE A N   
923  C CA  . PHE A 120 ? 0.59880 0.60060 0.78749 0.02996  -0.04766 0.04209  120 PHE A CA  
924  C C   . PHE A 120 ? 0.58653 0.59232 0.77997 0.02879  -0.04563 0.04179  120 PHE A C   
925  O O   . PHE A 120 ? 0.58365 0.58834 0.77042 0.02535  -0.04272 0.04146  120 PHE A O   
926  C CB  . PHE A 120 ? 0.57053 0.56991 0.75460 0.03512  -0.04923 0.03794  120 PHE A CB  
927  C CG  . PHE A 120 ? 0.61992 0.61532 0.79343 0.03836  -0.05020 0.03822  120 PHE A CG  
928  C CD1 . PHE A 120 ? 0.58358 0.56721 0.74000 0.03931  -0.04671 0.04034  120 PHE A CD1 
929  C CD2 . PHE A 120 ? 0.63962 0.64188 0.81892 0.04044  -0.05310 0.03596  120 PHE A CD2 
930  C CE1 . PHE A 120 ? 0.60799 0.58517 0.75203 0.04423  -0.04630 0.04141  120 PHE A CE1 
931  C CE2 . PHE A 120 ? 0.60963 0.60993 0.77881 0.04516  -0.05393 0.03634  120 PHE A CE2 
932  C CZ  . PHE A 120 ? 0.61170 0.59866 0.76263 0.04805  -0.05064 0.03968  120 PHE A CZ  
933  N N   . PRO A 121 ? 0.56879 0.57846 0.77256 0.03103  -0.04563 0.04138  121 PRO A N   
934  C CA  . PRO A 121 ? 0.50482 0.51968 0.71277 0.03123  -0.04341 0.04166  121 PRO A CA  
935  C C   . PRO A 121 ? 0.55988 0.58507 0.76867 0.02807  -0.04262 0.04385  121 PRO A C   
936  O O   . PRO A 121 ? 0.56730 0.59756 0.77530 0.02594  -0.04018 0.04174  121 PRO A O   
937  C CB  . PRO A 121 ? 0.51847 0.53331 0.73603 0.03516  -0.04227 0.04252  121 PRO A CB  
938  C CG  . PRO A 121 ? 0.55109 0.55947 0.76805 0.03479  -0.04309 0.03853  121 PRO A CG  
939  C CD  . PRO A 121 ? 0.59554 0.60380 0.80621 0.03306  -0.04601 0.03931  121 PRO A CD  
940  N N   . ILE A 122 ? 0.56043 0.59122 0.77112 0.02725  -0.04426 0.04695  122 ILE A N   
941  C CA  . ILE A 122 ? 0.53380 0.57927 0.74528 0.02329  -0.04375 0.04687  122 ILE A CA  
942  C C   . ILE A 122 ? 0.49275 0.53256 0.69325 0.01473  -0.04046 0.04257  122 ILE A C   
943  O O   . ILE A 122 ? 0.43736 0.48718 0.63749 0.00882  -0.03712 0.03870  122 ILE A O   
944  C CB  . ILE A 122 ? 0.53336 0.58667 0.74792 0.02510  -0.04629 0.05092  122 ILE A CB  
945  C CG1 . ILE A 122 ? 0.59521 0.65242 0.81731 0.03475  -0.04667 0.05584  122 ILE A CG1 
946  C CG2 . ILE A 122 ? 0.49649 0.56771 0.71042 0.01908  -0.04608 0.04850  122 ILE A CG2 
947  C CD1 . ILE A 122 ? 0.57931 0.63637 0.80137 0.03881  -0.04786 0.06118  122 ILE A CD1 
948  N N   . LEU A 123 ? 0.51916 0.54250 0.70943 0.01418  -0.04011 0.04273  123 LEU A N   
949  C CA  . LEU A 123 ? 0.51996 0.53213 0.69546 0.00749  -0.03476 0.03984  123 LEU A CA  
950  C C   . LEU A 123 ? 0.51506 0.52010 0.68342 0.00566  -0.02941 0.03644  123 LEU A C   
951  O O   . LEU A 123 ? 0.47803 0.48323 0.64016 -0.00314 -0.02274 0.03231  123 LEU A O   
952  C CB  . LEU A 123 ? 0.53009 0.52573 0.69441 0.01109  -0.03528 0.04177  123 LEU A CB  
953  C CG  . LEU A 123 ? 0.55559 0.53400 0.70041 0.00609  -0.02780 0.04013  123 LEU A CG  
954  C CD1 . LEU A 123 ? 0.53168 0.51676 0.67677 -0.00334 -0.02545 0.03862  123 LEU A CD1 
955  C CD2 . LEU A 123 ? 0.50485 0.46621 0.63604 0.01480  -0.02792 0.04240  123 LEU A CD2 
956  N N   . VAL A 124 ? 0.54239 0.54227 0.71187 0.01295  -0.03151 0.03713  124 VAL A N   
957  C CA  . VAL A 124 ? 0.52643 0.51949 0.68900 0.01268  -0.02679 0.03434  124 VAL A CA  
958  C C   . VAL A 124 ? 0.49191 0.50108 0.66425 0.00666  -0.02399 0.03124  124 VAL A C   
959  O O   . VAL A 124 ? 0.55932 0.56398 0.72311 -0.00029 -0.01649 0.02722  124 VAL A O   
960  C CB  . VAL A 124 ? 0.52986 0.51946 0.69445 0.02162  -0.03071 0.03476  124 VAL A CB  
961  C CG1 . VAL A 124 ? 0.58533 0.56838 0.74228 0.02190  -0.02596 0.03210  124 VAL A CG1 
962  C CG2 . VAL A 124 ? 0.49215 0.47172 0.64720 0.02783  -0.03340 0.03597  124 VAL A CG2 
963  N N   . ASP A 125 ? 0.42321 0.45160 0.61223 0.00953  -0.02884 0.03277  125 ASP A N   
964  C CA  . ASP A 125 ? 0.44202 0.49140 0.64077 0.00594  -0.02685 0.02961  125 ASP A CA  
965  C C   . ASP A 125 ? 0.50453 0.56308 0.69934 -0.00595 -0.02180 0.02428  125 ASP A C   
966  O O   . ASP A 125 ? 0.54025 0.60940 0.73617 -0.01329 -0.01608 0.01808  125 ASP A O   
967  C CB  . ASP A 125 ? 0.47552 0.54290 0.68924 0.01421  -0.03243 0.03358  125 ASP A CB  
968  C CG  . ASP A 125 ? 0.54256 0.63254 0.76639 0.01575  -0.03092 0.03092  125 ASP A CG  
969  O OD1 . ASP A 125 ? 0.61235 0.69782 0.83718 0.01874  -0.02871 0.02986  125 ASP A OD1 
970  O OD2 . ASP A 125 ? 0.51463 0.62906 0.74537 0.01460  -0.03198 0.02934  125 ASP A OD2 
971  N N   . LEU A 126 ? 0.53485 0.59089 0.72550 -0.00916 -0.02297 0.02536  126 LEU A N   
972  C CA  . LEU A 126 ? 0.54639 0.60862 0.73134 -0.02255 -0.01649 0.01862  126 LEU A CA  
973  C C   . LEU A 126 ? 0.53724 0.57383 0.70314 -0.03122 -0.00524 0.01425  126 LEU A C   
974  O O   . LEU A 126 ? 0.50925 0.55150 0.67126 -0.04468 0.00383  0.00584  126 LEU A O   
975  C CB  . LEU A 126 ? 0.50820 0.57071 0.69137 -0.02358 -0.01976 0.02094  126 LEU A CB  
976  C CG  . LEU A 126 ? 0.46275 0.55080 0.66104 -0.01654 -0.02848 0.02458  126 LEU A CG  
977  C CD1 . LEU A 126 ? 0.41655 0.49566 0.60872 -0.01754 -0.03031 0.02739  126 LEU A CD1 
978  C CD2 . LEU A 126 ? 0.41255 0.53657 0.62208 -0.02122 -0.02837 0.01806  126 LEU A CD2 
979  N N   . ILE A 127 ? 0.49767 0.50664 0.65044 -0.02347 -0.00476 0.01924  127 ILE A N   
980  C CA  . ILE A 127 ? 0.55377 0.53606 0.68564 -0.02723 0.00634  0.01689  127 ILE A CA  
981  C C   . ILE A 127 ? 0.65038 0.64110 0.78700 -0.03087 0.01086  0.01217  127 ILE A C   
982  O O   . ILE A 127 ? 0.69271 0.67298 0.81702 -0.04188 0.02334  0.00595  127 ILE A O   
983  C CB  . ILE A 127 ? 0.61591 0.57327 0.73358 -0.01411 0.00386  0.02359  127 ILE A CB  
984  C CG1 . ILE A 127 ? 0.58991 0.54108 0.70381 -0.00976 -0.00058 0.02785  127 ILE A CG1 
985  C CG2 . ILE A 127 ? 0.61697 0.54494 0.70920 -0.01460 0.01605  0.02250  127 ILE A CG2 
986  C CD1 . ILE A 127 ? 0.56450 0.50211 0.66359 -0.01951 0.00891  0.02515  127 ILE A CD1 
987  N N   . ARG A 128 ? 0.71418 0.72122 0.86708 -0.02192 0.00237  0.01476  128 ARG A N   
988  C CA  . ARG A 128 ? 0.71281 0.72754 0.87020 -0.02387 0.00648  0.01067  128 ARG A CA  
989  C C   . ARG A 128 ? 0.71458 0.75494 0.88165 -0.03717 0.01216  0.00176  128 ARG A C   
990  O O   . ARG A 128 ? 0.72557 0.76720 0.89005 -0.04459 0.02091  -0.00457 128 ARG A O   
991  C CB  . ARG A 128 ? 0.67173 0.69896 0.84471 -0.01155 -0.00296 0.01494  128 ARG A CB  
992  C CG  . ARG A 128 ? 0.66154 0.67041 0.82836 -0.00013 -0.00858 0.02089  128 ARG A CG  
993  C CD  . ARG A 128 ? 0.71513 0.73645 0.89745 0.00853  -0.01486 0.02282  128 ARG A CD  
994  N NE  . ARG A 128 ? 0.77829 0.79043 0.96073 0.01747  -0.02119 0.02667  128 ARG A NE  
995  C CZ  . ARG A 128 ? 0.85201 0.84945 1.02424 0.02241  -0.02121 0.02629  128 ARG A CZ  
996  N NH1 . ARG A 128 ? 0.90701 0.89202 1.06450 0.02096  -0.01498 0.02405  128 ARG A NH1 
997  N NH2 . ARG A 128 ? 0.79049 0.78648 0.96643 0.02885  -0.02693 0.02749  128 ARG A NH2 
998  N N   . ASP A 129 ? 0.68470 0.74824 0.86318 -0.04033 0.00744  0.00028  129 ASP A N   
999  C CA  . ASP A 129 ? 0.68349 0.77681 0.87103 -0.05369 0.01264  -0.01029 129 ASP A CA  
1000 C C   . ASP A 129 ? 0.71817 0.79290 0.88768 -0.07180 0.02806  -0.01926 129 ASP A C   
1001 O O   . ASP A 129 ? 0.72452 0.82030 0.89926 -0.08603 0.03633  -0.03097 129 ASP A O   
1002 C CB  . ASP A 129 ? 0.66432 0.78769 0.86586 -0.05171 0.00392  -0.01001 129 ASP A CB  
1003 C CG  . ASP A 129 ? 0.69129 0.84024 0.91117 -0.03554 -0.00749 -0.00385 129 ASP A CG  
1004 O OD1 . ASP A 129 ? 0.62825 0.78585 0.85523 -0.03045 -0.00707 -0.00446 129 ASP A OD1 
1005 O OD2 . ASP A 129 ? 0.69865 0.85765 0.92424 -0.02768 -0.01573 0.00168  129 ASP A OD2 
1006 N N   . ILE A 130 ? 0.64316 0.67886 0.79044 -0.07169 0.03357  -0.01483 130 ILE A N   
1007 C CA  . ILE A 130 ? 0.68433 0.69223 0.80898 -0.08627 0.05176  -0.02198 130 ILE A CA  
1008 C C   . ILE A 130 ? 0.71205 0.71417 0.83346 -0.08729 0.05907  -0.02482 130 ILE A C   
1009 O O   . ILE A 130 ? 0.70404 0.71209 0.82334 -0.10374 0.07239  -0.03627 130 ILE A O   
1010 C CB  . ILE A 130 ? 0.63544 0.59874 0.73302 -0.08093 0.05697  -0.01463 130 ILE A CB  
1011 C CG1 . ILE A 130 ? 0.65261 0.62085 0.75311 -0.08008 0.05034  -0.01199 130 ILE A CG1 
1012 C CG2 . ILE A 130 ? 0.66337 0.59388 0.73411 -0.09538 0.07847  -0.02164 130 ILE A CG2 
1013 C CD1 . ILE A 130 ? 0.64334 0.57306 0.72092 -0.06885 0.05155  -0.00262 130 ILE A CD1 
1014 N N   . GLN A 131 ? 0.66550 0.65777 0.78706 -0.07077 0.05107  -0.01566 131 GLN A N   
1015 C CA  . GLN A 131 ? 0.68340 0.66912 0.80046 -0.07180 0.05851  -0.01846 131 GLN A CA  
1016 C C   . GLN A 131 ? 0.68642 0.71438 0.82855 -0.07802 0.05640  -0.02676 131 GLN A C   
1017 O O   . GLN A 131 ? 0.65532 0.68361 0.79400 -0.08827 0.06816  -0.03483 131 GLN A O   
1018 C CB  . GLN A 131 ? 0.72599 0.69367 0.83703 -0.05340 0.05080  -0.00828 131 GLN A CB  
1019 C CG  . GLN A 131 ? 0.79759 0.72517 0.88067 -0.04555 0.05483  -0.00131 131 GLN A CG  
1020 C CD  . GLN A 131 ? 0.80099 0.70996 0.87169 -0.03221 0.05408  0.00397  131 GLN A CD  
1021 O OE1 . GLN A 131 ? 0.81758 0.74111 0.90040 -0.03064 0.05155  0.00204  131 GLN A OE1 
1022 N NE2 . GLN A 131 ? 0.83448 0.71233 0.87991 -0.02183 0.05673  0.01025  131 GLN A NE2 
1023 N N   . ARG A 132 ? 0.64978 0.71347 0.81593 -0.07090 0.04241  -0.02488 132 ARG A N   
1024 C CA  . ARG A 132 ? 0.57551 0.68156 0.76395 -0.07351 0.04041  -0.03226 132 ARG A CA  
1025 C C   . ARG A 132 ? 0.53763 0.66482 0.72813 -0.09482 0.05217  -0.04740 132 ARG A C   
1026 O O   . ARG A 132 ? 0.57791 0.73408 0.78067 -0.10179 0.05673  -0.05714 132 ARG A O   
1027 C CB  . ARG A 132 ? 0.53905 0.67572 0.74839 -0.05888 0.02448  -0.02598 132 ARG A CB  
1028 C CG  . ARG A 132 ? 0.56599 0.68275 0.77421 -0.04033 0.01462  -0.01312 132 ARG A CG  
1029 C CD  . ARG A 132 ? 0.55832 0.70257 0.78518 -0.02612 0.00232  -0.00738 132 ARG A CD  
1030 N NE  . ARG A 132 ? 0.56494 0.68865 0.79026 -0.01110 -0.00489 0.00313  132 ARG A NE  
1031 C CZ  . ARG A 132 ? 0.60867 0.71922 0.83084 -0.00510 -0.01120 0.01018  132 ARG A CZ  
1032 N NH1 . ARG A 132 ? 0.60617 0.72392 0.82790 -0.01002 -0.01298 0.00966  132 ARG A NH1 
1033 N NH2 . ARG A 132 ? 0.60417 0.69538 0.82394 0.00525  -0.01528 0.01682  132 ARG A NH2 
1034 N N   . LEU A 133 ? 0.61467 0.72770 0.79276 -0.10613 0.05835  -0.05067 133 LEU A N   
1035 C CA  . LEU A 133 ? 0.62242 0.75241 0.80016 -0.12949 0.07180  -0.06711 133 LEU A CA  
1036 C C   . LEU A 133 ? 0.60811 0.70899 0.76653 -0.14507 0.09241  -0.07539 133 LEU A C   
1037 O O   . LEU A 133 ? 0.58914 0.71489 0.75456 -0.16374 0.10388  -0.09135 133 LEU A O   
1038 C CB  . LEU A 133 ? 0.57281 0.69123 0.74080 -0.13592 0.07267  -0.06718 133 LEU A CB  
1039 C CG  . LEU A 133 ? 0.58869 0.72176 0.75431 -0.16142 0.08685  -0.08480 133 LEU A CG  
1040 C CD1 . LEU A 133 ? 0.56842 0.76613 0.76285 -0.16628 0.08068  -0.09697 133 LEU A CD1 
1041 C CD2 . LEU A 133 ? 0.61044 0.72976 0.76663 -0.16302 0.08477  -0.08172 133 LEU A CD2 
1042 N N   . ASN A 134 ? 0.60859 0.65858 0.74223 -0.13712 0.09773  -0.06522 134 ASN A N   
1043 C CA  . ASN A 134 ? 0.61790 0.63180 0.72777 -0.14720 0.11752  -0.06962 134 ASN A CA  
1044 C C   . ASN A 134 ? 0.66398 0.69441 0.78519 -0.14440 0.11770  -0.07220 134 ASN A C   
1045 O O   . ASN A 134 ? 0.73655 0.73457 0.83703 -0.14932 0.13300  -0.07368 134 ASN A O   
1046 C CB  . ASN A 134 ? 0.68273 0.64019 0.76147 -0.13413 0.12051  -0.05593 134 ASN A CB  
1047 C CG  . ASN A 134 ? 0.69097 0.61544 0.74490 -0.14556 0.13476  -0.05859 134 ASN A CG  
1048 O OD1 . ASN A 134 ? 0.73514 0.64194 0.77254 -0.16554 0.15647  -0.06996 134 ASN A OD1 
1049 N ND2 . ASN A 134 ? 0.72817 0.64687 0.78086 -0.13472 0.12363  -0.04966 134 ASN A ND2 
1050 N N   . GLY A 135 ? 0.65012 0.72819 0.80162 -0.13572 0.10222  -0.07244 135 GLY A N   
1051 C CA  . GLY A 135 ? 0.58238 0.67950 0.74628 -0.13226 0.10208  -0.07522 135 GLY A CA  
1052 C C   . GLY A 135 ? 0.59756 0.67115 0.75582 -0.11119 0.09316  -0.06100 135 GLY A C   
1053 O O   . GLY A 135 ? 0.60695 0.68696 0.76992 -0.10911 0.09599  -0.06312 135 GLY A O   
1054 N N   . VAL A 136 ? 0.60762 0.65658 0.75660 -0.09622 0.08286  -0.04783 136 VAL A N   
1055 C CA  . VAL A 136 ? 0.63500 0.66388 0.77855 -0.07733 0.07444  -0.03614 136 VAL A CA  
1056 C C   . VAL A 136 ? 0.70951 0.77412 0.88047 -0.06384 0.05861  -0.03250 136 VAL A C   
1057 O O   . VAL A 136 ? 0.72816 0.82345 0.91717 -0.06253 0.04985  -0.03320 136 VAL A O   
1058 C CB  . VAL A 136 ? 0.65261 0.64640 0.77672 -0.06729 0.07008  -0.02550 136 VAL A CB  
1059 C CG1 . VAL A 136 ? 0.68130 0.65747 0.79887 -0.04979 0.06266  -0.01619 136 VAL A CG1 
1060 C CG2 . VAL A 136 ? 0.71231 0.67006 0.80744 -0.07899 0.08707  -0.02853 136 VAL A CG2 
1061 N N   . SER A 137 ? 0.68450 0.74400 0.85685 -0.05302 0.05581  -0.02850 137 SER A N   
1062 C CA  . SER A 137 ? 0.67072 0.75664 0.86494 -0.03908 0.04333  -0.02437 137 SER A CA  
1063 C C   . SER A 137 ? 0.70119 0.76864 0.89212 -0.02360 0.03174  -0.01315 137 SER A C   
1064 O O   . SER A 137 ? 0.69300 0.72931 0.86504 -0.02186 0.03268  -0.00882 137 SER A O   
1065 C CB  . SER A 137 ? 0.74501 0.83872 0.94435 -0.03722 0.04802  -0.02802 137 SER A CB  
1066 O OG  . SER A 137 ? 0.81010 0.86874 0.99047 -0.03237 0.05149  -0.02375 137 SER A OG  
1067 N N   . GLU A 138 ? 0.71656 0.80422 0.92536 -0.01177 0.02174  -0.00898 138 GLU A N   
1068 C CA  . GLU A 138 ? 0.73037 0.80631 0.93933 -0.00025 0.01174  -0.00036 138 GLU A CA  
1069 C C   . GLU A 138 ? 0.73868 0.78524 0.93359 0.00584  0.01138  0.00311  138 GLU A C   
1070 O O   . GLU A 138 ? 0.72914 0.75899 0.91563 0.00967  0.00668  0.00748  138 GLU A O   
1071 C CB  . GLU A 138 ? 0.73152 0.83033 0.95902 0.01131  0.00457  0.00315  138 GLU A CB  
1072 C CG  . GLU A 138 ? 0.76299 0.89285 1.00298 0.00935  0.00217  0.00126  138 GLU A CG  
1073 C CD  . GLU A 138 ? 0.76618 0.88878 1.00065 0.00509  -0.00150 0.00377  138 GLU A CD  
1074 O OE1 . GLU A 138 ? 0.76679 0.86747 0.99497 0.01104  -0.00632 0.01032  138 GLU A OE1 
1075 O OE2 . GLU A 138 ? 0.75553 0.89520 0.99173 -0.00552 0.00138  -0.00217 138 GLU A OE2 
1076 N N   . ASN A 139 ? 0.73366 0.77703 0.92689 0.00764  0.01578  0.00064  139 ASN A N   
1077 C CA  . ASN A 139 ? 0.73561 0.75546 0.91543 0.01365  0.01559  0.00242  139 ASN A CA  
1078 C C   . ASN A 139 ? 0.69938 0.69414 0.85510 0.00907  0.02181  0.00204  139 ASN A C   
1079 O O   . ASN A 139 ? 0.69041 0.66690 0.83204 0.01592  0.02049  0.00394  139 ASN A O   
1080 C CB  . ASN A 139 ? 0.79599 0.82114 0.98089 0.01663  0.01922  -0.00052 139 ASN A CB  
1081 C CG  . ASN A 139 ? 0.84450 0.87839 1.02856 0.00680  0.02935  -0.00665 139 ASN A CG  
1082 O OD1 . ASN A 139 ? 0.84167 0.87359 1.01833 -0.00382 0.03533  -0.00958 139 ASN A OD1 
1083 N ND2 . ASN A 139 ? 0.82293 0.86665 1.01455 0.00936  0.03256  -0.00957 139 ASN A ND2 
1084 N N   . GLU A 140 ? 0.70664 0.70051 0.85627 -0.00170 0.02915  -0.00073 140 GLU A N   
1085 C CA  . GLU A 140 ? 0.78382 0.74952 0.90741 -0.00558 0.03748  -0.00025 140 GLU A CA  
1086 C C   . GLU A 140 ? 0.78223 0.74192 0.90072 -0.00743 0.03496  0.00268  140 GLU A C   
1087 O O   . GLU A 140 ? 0.79541 0.72923 0.89010 -0.00961 0.04317  0.00367  140 GLU A O   
1088 C CB  . GLU A 140 ? 0.78690 0.74872 0.90216 -0.01881 0.05251  -0.00715 140 GLU A CB  
1089 C CG  . GLU A 140 ? 0.86579 0.82702 0.98024 -0.01663 0.05693  -0.00969 140 GLU A CG  
1090 C CD  . GLU A 140 ? 1.00908 0.97218 1.11978 -0.03162 0.07233  -0.01816 140 GLU A CD  
1091 O OE1 . GLU A 140 ? 0.99767 0.96987 1.11174 -0.04487 0.07837  -0.02354 140 GLU A OE1 
1092 O OE2 . GLU A 140 ? 1.01605 0.97192 1.12007 -0.03109 0.07912  -0.02042 140 GLU A OE2 
1093 N N   . LEU A 141 ? 0.74331 0.72373 0.88107 -0.00591 0.02513  0.00444  141 LEU A N   
1094 C CA  . LEU A 141 ? 0.79412 0.76747 0.92596 -0.00714 0.02277  0.00735  141 LEU A CA  
1095 C C   . LEU A 141 ? 0.80491 0.75406 0.91825 0.00375  0.01981  0.01274  141 LEU A C   
1096 O O   . LEU A 141 ? 0.84359 0.79388 0.96006 0.01382  0.01299  0.01463  141 LEU A O   
1097 C CB  . LEU A 141 ? 0.75238 0.75080 0.90664 -0.00511 0.01224  0.00925  141 LEU A CB  
1098 C CG  . LEU A 141 ? 0.67324 0.70123 0.84510 -0.01339 0.01412  0.00382  141 LEU A CG  
1099 C CD1 . LEU A 141 ? 0.63321 0.68278 0.82339 -0.00678 0.00378  0.00748  141 LEU A CD1 
1100 C CD2 . LEU A 141 ? 0.66513 0.69156 0.82812 -0.02841 0.02424  -0.00250 141 LEU A CD2 
1101 N N   . ASP A 142 ? 0.81751 0.74533 0.91025 0.00189  0.02602  0.01432  142 ASP A N   
1102 C CA  . ASP A 142 ? 0.86269 0.76998 0.93568 0.01452  0.02359  0.01944  142 ASP A CA  
1103 C C   . ASP A 142 ? 0.84269 0.73454 0.90114 0.01241  0.02783  0.02184  142 ASP A C   
1104 O O   . ASP A 142 ? 0.83612 0.70529 0.87331 0.00569  0.04176  0.02056  142 ASP A O   
1105 C CB  . ASP A 142 ? 0.88827 0.77380 0.93771 0.02040  0.03181  0.01969  142 ASP A CB  
1106 C CG  . ASP A 142 ? 0.95598 0.82097 0.98024 0.03528  0.03091  0.02494  142 ASP A CG  
1107 O OD1 . ASP A 142 ? 1.00671 0.88471 1.03902 0.04634  0.01867  0.02637  142 ASP A OD1 
1108 O OD2 . ASP A 142 ? 0.95311 0.78914 0.94849 0.03617  0.04347  0.02711  142 ASP A OD2 
1109 N N   . THR A 143 ? 0.77857 0.68016 0.84662 0.01808  0.01731  0.02499  143 THR A N   
1110 C CA  . THR A 143 ? 0.79274 0.68468 0.85215 0.01531  0.01986  0.02694  143 THR A CA  
1111 C C   . THR A 143 ? 0.78750 0.66337 0.82786 0.03026  0.01719  0.03220  143 THR A C   
1112 O O   . THR A 143 ? 0.77276 0.64659 0.81146 0.03113  0.01522  0.03445  143 THR A O   
1113 C CB  . THR A 143 ? 0.75632 0.67412 0.84192 0.00917  0.01088  0.02613  143 THR A CB  
1114 O OG1 . THR A 143 ? 0.72345 0.65780 0.82601 0.01856  -0.00201 0.02833  143 THR A OG1 
1115 C CG2 . THR A 143 ? 0.73394 0.67118 0.83630 -0.00384 0.01396  0.02062  143 THR A CG2 
1116 N N   . PHE A 144 ? 0.80493 0.67126 0.83026 0.04282  0.01718  0.03382  144 PHE A N   
1117 C CA  . PHE A 144 ? 0.76483 0.62508 0.77500 0.05977  0.01229  0.03782  144 PHE A CA  
1118 C C   . PHE A 144 ? 0.88008 0.71356 0.86397 0.06281  0.02205  0.04204  144 PHE A C   
1119 O O   . PHE A 144 ? 0.88631 0.72394 0.87022 0.07023  0.01615  0.04458  144 PHE A O   
1120 C CB  . PHE A 144 ? 0.82338 0.67742 0.81730 0.07282  0.01289  0.03815  144 PHE A CB  
1121 C CG  . PHE A 144 ? 0.82006 0.67393 0.79798 0.09232  0.00736  0.04106  144 PHE A CG  
1122 C CD1 . PHE A 144 ? 0.74542 0.62888 0.74380 0.09815  -0.00703 0.03774  144 PHE A CD1 
1123 C CD2 . PHE A 144 ? 0.86931 0.69360 0.81020 0.10543  0.01776  0.04656  144 PHE A CD2 
1124 C CE1 . PHE A 144 ? 0.77840 0.66819 0.76353 0.11619  -0.01251 0.03855  144 PHE A CE1 
1125 C CE2 . PHE A 144 ? 0.85218 0.68018 0.77725 0.12645  0.01226  0.04929  144 PHE A CE2 
1126 C CZ  . PHE A 144 ? 0.82572 0.68951 0.77413 0.13173  -0.00364 0.04467  144 PHE A CZ  
1127 N N   . LYS A 145 ? 0.96158 0.76580 0.92163 0.05685  0.03850  0.04237  145 LYS A N   
1128 C CA  . LYS A 145 ? 0.98044 0.75150 0.90965 0.06003  0.05166  0.04634  145 LYS A CA  
1129 C C   . LYS A 145 ? 0.98314 0.75682 0.92389 0.04364  0.05456  0.04361  145 LYS A C   
1130 O O   . LYS A 145 ? 1.01388 0.76031 0.93073 0.04470  0.06570  0.04620  145 LYS A O   
1131 C CB  . LYS A 145 ? 1.02540 0.75904 0.92127 0.05851  0.07156  0.04694  145 LYS A CB  
1132 C CG  . LYS A 145 ? 1.09454 0.82245 0.97480 0.07425  0.07112  0.04951  145 LYS A CG  
1133 C CD  . LYS A 145 ? 1.13957 0.85986 0.99594 0.10124  0.06644  0.05665  145 LYS A CD  
1134 C CE  . LYS A 145 ? 1.16570 0.87690 1.00125 0.11584  0.06924  0.05859  145 LYS A CE  
1135 N NZ  . LYS A 145 ? 1.13465 0.84194 0.94388 0.14495  0.06496  0.06496  145 LYS A NZ  
1136 N N   . LEU A 146 ? 0.88816 0.69308 0.86289 0.02942  0.04574  0.03843  146 LEU A N   
1137 C CA  . LEU A 146 ? 0.78518 0.59917 0.77319 0.01432  0.04671  0.03504  146 LEU A CA  
1138 C C   . LEU A 146 ? 0.75318 0.58809 0.75948 0.02046  0.03201  0.03787  146 LEU A C   
1139 O O   . LEU A 146 ? 0.83009 0.66462 0.83820 0.01257  0.03404  0.03695  146 LEU A O   
1140 C CB  . LEU A 146 ? 0.77156 0.61020 0.78439 -0.00311 0.04623  0.02765  146 LEU A CB  
1141 C CG  . LEU A 146 ? 0.78142 0.60484 0.78111 -0.01488 0.06225  0.02200  146 LEU A CG  
1142 C CD1 . LEU A 146 ? 0.72009 0.57782 0.74919 -0.02877 0.05832  0.01443  146 LEU A CD1 
1143 C CD2 . LEU A 146 ? 0.78573 0.57684 0.75835 -0.02521 0.08107  0.01941  146 LEU A CD2 
1144 N N   . GLU A 147 ? 0.76439 0.61723 0.78367 0.03306  0.01845  0.04029  147 GLU A N   
1145 C CA  . GLU A 147 ? 0.69699 0.57162 0.73654 0.03610  0.00564  0.04147  147 GLU A CA  
1146 C C   . GLU A 147 ? 0.75478 0.61394 0.77594 0.04586  0.00745  0.04560  147 GLU A C   
1147 O O   . GLU A 147 ? 0.76473 0.60148 0.75866 0.05833  0.01410  0.04885  147 GLU A O   
1148 C CB  . GLU A 147 ? 0.68934 0.58565 0.74641 0.04458  -0.00650 0.04084  147 GLU A CB  
1149 C CG  . GLU A 147 ? 0.70584 0.61667 0.78137 0.03522  -0.00759 0.03726  147 GLU A CG  
1150 C CD  . GLU A 147 ? 0.71493 0.64345 0.80640 0.04152  -0.01683 0.03562  147 GLU A CD  
1151 O OE1 . GLU A 147 ? 0.69575 0.62951 0.78650 0.05209  -0.02338 0.03573  147 GLU A OE1 
1152 O OE2 . GLU A 147 ? 0.69718 0.63508 0.80138 0.03538  -0.01648 0.03319  147 GLU A OE2 
1153 N N   . PRO A 148 ? 0.79015 0.65992 0.82367 0.04171  0.00247  0.04595  148 PRO A N   
1154 C CA  . PRO A 148 ? 0.79382 0.64847 0.80952 0.05070  0.00523  0.04969  148 PRO A CA  
1155 C C   . PRO A 148 ? 0.79760 0.65805 0.80744 0.07044  -0.00217 0.05229  148 PRO A C   
1156 O O   . PRO A 148 ? 0.81858 0.66329 0.80671 0.08268  0.00204  0.05600  148 PRO A O   
1157 C CB  . PRO A 148 ? 0.74806 0.61930 0.78390 0.04104  -0.00059 0.04863  148 PRO A CB  
1158 C CG  . PRO A 148 ? 0.72277 0.62272 0.78832 0.03550  -0.01105 0.04600  148 PRO A CG  
1159 C CD  . PRO A 148 ? 0.74960 0.64606 0.81280 0.03140  -0.00624 0.04360  148 PRO A CD  
1160 N N   . CYS A 149 ? 0.70842 0.59209 0.73619 0.07424  -0.01241 0.04966  149 CYS A N   
1161 C CA  . CYS A 149 ? 0.71022 0.60415 0.73249 0.09195  -0.01898 0.04954  149 CYS A CA  
1162 C C   . CYS A 149 ? 0.72886 0.63804 0.76289 0.09212  -0.02425 0.04545  149 CYS A C   
1163 O O   . CYS A 149 ? 0.68329 0.60274 0.73827 0.07902  -0.02650 0.04269  149 CYS A O   
1164 C CB  . CYS A 149 ? 0.69373 0.61008 0.73276 0.09517  -0.02862 0.04790  149 CYS A CB  
1165 S SG  . CYS A 149 ? 0.68234 0.62740 0.76056 0.07985  -0.03828 0.04267  149 CYS A SG  
1166 N N   . LYS A 150 ? 0.73581 0.64782 0.75560 0.10829  -0.02623 0.04491  150 LYS A N   
1167 C CA  . LYS A 150 ? 0.72420 0.65211 0.75436 0.10897  -0.03140 0.03995  150 LYS A CA  
1168 C C   . LYS A 150 ? 0.67670 0.63486 0.73959 0.10084  -0.04180 0.03344  150 LYS A C   
1169 O O   . LYS A 150 ? 0.64811 0.62061 0.72063 0.10256  -0.04709 0.03172  150 LYS A O   
1170 C CB  . LYS A 150 ? 0.72310 0.65212 0.73048 0.12955  -0.03223 0.03991  150 LYS A CB  
1171 C CG  . LYS A 150 ? 0.76132 0.65420 0.73208 0.13870  -0.01925 0.04744  150 LYS A CG  
1172 C CD  . LYS A 150 ? 0.78640 0.66010 0.75780 0.12256  -0.01021 0.04802  150 LYS A CD  
1173 C CE  . LYS A 150 ? 0.85612 0.69070 0.79108 0.12792  0.00560  0.05408  150 LYS A CE  
1174 N NZ  . LYS A 150 ? 0.94245 0.75912 0.86730 0.12558  0.01231  0.05800  150 LYS A NZ  
1175 N N   . PHE A 151 ? 0.70456 0.67056 0.78318 0.09202  -0.04328 0.02963  151 PHE A N   
1176 C CA  . PHE A 151 ? 0.66710 0.65399 0.77413 0.08256  -0.04949 0.02425  151 PHE A CA  
1177 C C   . PHE A 151 ? 0.65498 0.66595 0.76988 0.08928  -0.05676 0.01703  151 PHE A C   
1178 O O   . PHE A 151 ? 0.66721 0.69172 0.80250 0.08124  -0.05984 0.01298  151 PHE A O   
1179 C CB  . PHE A 151 ? 0.65827 0.64694 0.77639 0.07501  -0.04835 0.02143  151 PHE A CB  
1180 C CG  . PHE A 151 ? 0.67508 0.66640 0.78216 0.08351  -0.04870 0.01755  151 PHE A CG  
1181 C CD1 . PHE A 151 ? 0.73844 0.71083 0.82575 0.08692  -0.04212 0.02158  151 PHE A CD1 
1182 C CD2 . PHE A 151 ? 0.69753 0.71072 0.81294 0.08753  -0.05470 0.00891  151 PHE A CD2 
1183 C CE1 . PHE A 151 ? 0.76790 0.74179 0.84263 0.09600  -0.04210 0.01851  151 PHE A CE1 
1184 C CE2 . PHE A 151 ? 0.78004 0.79824 0.88411 0.09609  -0.05544 0.00459  151 PHE A CE2 
1185 C CZ  . PHE A 151 ? 0.74079 0.73856 0.82379 0.10125  -0.04942 0.01017  151 PHE A CZ  
1186 N N   . TRP A 152 ? 0.66984 0.68775 0.76859 0.10394  -0.05889 0.01463  152 TRP A N   
1187 C CA  . TRP A 152 ? 0.66121 0.70884 0.76898 0.10987  -0.06604 0.00545  152 TRP A CA  
1188 C C   . TRP A 152 ? 0.59395 0.64648 0.69842 0.11617  -0.06779 0.00757  152 TRP A C   
1189 O O   . TRP A 152 ? 0.57276 0.65315 0.68831 0.11881  -0.07336 -0.00107 152 TRP A O   
1190 C CB  . TRP A 152 ? 0.67778 0.73851 0.77045 0.12492  -0.06889 0.00044  152 TRP A CB  
1191 C CG  . TRP A 152 ? 0.62801 0.66928 0.68767 0.14299  -0.06486 0.00932  152 TRP A CG  
1192 C CD1 . TRP A 152 ? 0.63329 0.67945 0.67573 0.16046  -0.06626 0.01175  152 TRP A CD1 
1193 C CD2 . TRP A 152 ? 0.69210 0.70375 0.73015 0.14580  -0.05698 0.01687  152 TRP A CD2 
1194 N NE1 . TRP A 152 ? 0.66869 0.68648 0.67790 0.17483  -0.05884 0.02126  152 TRP A NE1 
1195 C CE2 . TRP A 152 ? 0.73588 0.73170 0.74180 0.16514  -0.05263 0.02412  152 TRP A CE2 
1196 C CE3 . TRP A 152 ? 0.73843 0.73507 0.78028 0.13418  -0.05214 0.01794  152 TRP A CE3 
1197 C CZ2 . TRP A 152 ? 0.78306 0.74521 0.75927 0.17186  -0.04221 0.03224  152 TRP A CZ2 
1198 C CZ3 . TRP A 152 ? 0.75789 0.72535 0.77302 0.13992  -0.04295 0.02513  152 TRP A CZ3 
1199 C CH2 . TRP A 152 ? 0.79191 0.74090 0.77387 0.15806  -0.03744 0.03208  152 TRP A CH2 
1200 N N   . ASN A 153 ? 0.68488 0.71182 0.77350 0.11849  -0.06233 0.01773  153 ASN A N   
1201 C CA  . ASN A 153 ? 0.71582 0.74217 0.80039 0.12317  -0.06243 0.02100  153 ASN A CA  
1202 C C   . ASN A 153 ? 0.69957 0.72257 0.80384 0.10656  -0.06170 0.02248  153 ASN A C   
1203 O O   . ASN A 153 ? 0.71338 0.72954 0.81262 0.10820  -0.06012 0.02669  153 ASN A O   
1204 C CB  . ASN A 153 ? 0.73040 0.72738 0.78329 0.13518  -0.05483 0.03081  153 ASN A CB  
1205 C CG  . ASN A 153 ? 0.73314 0.73476 0.76206 0.15753  -0.05554 0.03076  153 ASN A CG  
1206 O OD1 . ASN A 153 ? 0.69187 0.72652 0.72941 0.16610  -0.06377 0.02248  153 ASN A OD1 
1207 N ND2 . ASN A 153 ? 0.77818 0.74710 0.77485 0.16810  -0.04595 0.03963  153 ASN A ND2 
1208 N N   . GLN A 154 ? 0.63196 0.65753 0.75571 0.09213  -0.06195 0.01987  154 GLN A N   
1209 C CA  . GLN A 154 ? 0.58803 0.61432 0.73074 0.07859  -0.06171 0.02050  154 GLN A CA  
1210 C C   . GLN A 154 ? 0.62799 0.67836 0.78715 0.07708  -0.06600 0.01217  154 GLN A C   
1211 O O   . GLN A 154 ? 0.57011 0.64118 0.73160 0.08288  -0.06959 0.00341  154 GLN A O   
1212 C CB  . GLN A 154 ? 0.58233 0.60330 0.73692 0.06748  -0.05961 0.02074  154 GLN A CB  
1213 C CG  . GLN A 154 ? 0.55889 0.56010 0.70153 0.06562  -0.05466 0.02719  154 GLN A CG  
1214 C CD  . GLN A 154 ? 0.60358 0.60474 0.76044 0.05592  -0.05320 0.02699  154 GLN A CD  
1215 O OE1 . GLN A 154 ? 0.64323 0.65503 0.81632 0.05165  -0.05496 0.02278  154 GLN A OE1 
1216 N NE2 . GLN A 154 ? 0.60277 0.59170 0.75290 0.05241  -0.04877 0.03109  154 GLN A NE2 
1217 N N   . ARG A 155 ? 0.64260 0.69154 0.81270 0.06885  -0.06500 0.01407  155 ARG A N   
1218 C CA  . ARG A 155 ? 0.56437 0.63336 0.74828 0.06631  -0.06705 0.00641  155 ARG A CA  
1219 C C   . ARG A 155 ? 0.54139 0.60370 0.73962 0.05349  -0.06374 0.00848  155 ARG A C   
1220 O O   . ARG A 155 ? 0.58025 0.62575 0.77390 0.05082  -0.06169 0.01749  155 ARG A O   
1221 C CB  . ARG A 155 ? 0.57546 0.65100 0.74881 0.07731  -0.06913 0.00743  155 ARG A CB  
1222 C CG  . ARG A 155 ? 0.61175 0.69866 0.77031 0.09336  -0.07231 0.00448  155 ARG A CG  
1223 C CD  . ARG A 155 ? 0.59414 0.71156 0.76701 0.09198  -0.07607 -0.00921 155 ARG A CD  
1224 N NE  . ARG A 155 ? 0.62442 0.75989 0.78314 0.10987  -0.08036 -0.01321 155 ARG A NE  
1225 C CZ  . ARG A 155 ? 0.64794 0.77541 0.79149 0.11844  -0.08049 -0.01065 155 ARG A CZ  
1226 N NH1 . ARG A 155 ? 0.60824 0.71018 0.74945 0.11013  -0.07643 -0.00424 155 ARG A NH1 
1227 N NH2 . ARG A 155 ? 0.69167 0.83826 0.82115 0.13684  -0.08452 -0.01457 155 ARG A NH2 
1228 N N   . ASP A 156 ? 0.57811 0.65374 0.79225 0.04567  -0.06229 -0.00053 156 ASP A N   
1229 C CA  . ASP A 156 ? 0.58820 0.65489 0.81351 0.03469  -0.05716 0.00128  156 ASP A CA  
1230 C C   . ASP A 156 ? 0.58863 0.66397 0.81838 0.03313  -0.05673 -0.00108 156 ASP A C   
1231 O O   . ASP A 156 ? 0.57044 0.66776 0.80527 0.03465  -0.05843 -0.01152 156 ASP A O   
1232 C CB  . ASP A 156 ? 0.58162 0.65081 0.81888 0.02572  -0.05217 -0.00712 156 ASP A CB  
1233 C CG  . ASP A 156 ? 0.61708 0.67068 0.86092 0.01691  -0.04469 -0.00319 156 ASP A CG  
1234 O OD1 . ASP A 156 ? 0.63852 0.67539 0.87745 0.01845  -0.04382 0.00779  156 ASP A OD1 
1235 O OD2 . ASP A 156 ? 0.58403 0.64261 0.83703 0.00871  -0.03884 -0.01167 156 ASP A OD2 
1236 N N   . ILE A 157 ? 0.54858 0.60935 0.77658 0.03032  -0.05451 0.00783  157 ILE A N   
1237 C CA  . ILE A 157 ? 0.62863 0.69594 0.85918 0.02942  -0.05392 0.00654  157 ILE A CA  
1238 C C   . ILE A 157 ? 0.60739 0.68435 0.85249 0.01930  -0.04815 -0.00380 157 ILE A C   
1239 O O   . ILE A 157 ? 0.62134 0.71792 0.87216 0.01905  -0.04865 -0.01282 157 ILE A O   
1240 C CB  . ILE A 157 ? 0.67119 0.72103 0.89464 0.02906  -0.05296 0.01826  157 ILE A CB  
1241 C CG1 . ILE A 157 ? 0.58230 0.62523 0.78998 0.03780  -0.05678 0.02490  157 ILE A CG1 
1242 C CG2 . ILE A 157 ? 0.61940 0.67323 0.84783 0.02534  -0.05029 0.01674  157 ILE A CG2 
1243 C CD1 . ILE A 157 ? 0.56813 0.59500 0.76863 0.03530  -0.05530 0.03462  157 ILE A CD1 
1244 N N   . ARG A 158 ? 0.58609 0.64976 0.83647 0.01105  -0.04143 -0.00355 158 ARG A N   
1245 C CA  . ARG A 158 ? 0.62103 0.68764 0.88241 -0.00030 -0.03243 -0.01375 158 ARG A CA  
1246 C C   . ARG A 158 ? 0.59112 0.68449 0.86145 -0.00348 -0.03321 -0.03073 158 ARG A C   
1247 O O   . ARG A 158 ? 0.61182 0.72046 0.89178 -0.01166 -0.02833 -0.04275 158 ARG A O   
1248 C CB  . ARG A 158 ? 0.59782 0.64081 0.85894 -0.00618 -0.02331 -0.00963 158 ARG A CB  
1249 C CG  . ARG A 158 ? 0.57886 0.60031 0.83141 -0.00178 -0.02254 0.00602  158 ARG A CG  
1250 C CD  . ARG A 158 ? 0.58520 0.58482 0.83598 -0.00484 -0.01231 0.00964  158 ARG A CD  
1251 N NE  . ARG A 158 ? 0.64265 0.62711 0.88462 0.00221  -0.01288 0.02446  158 ARG A NE  
1252 C CZ  . ARG A 158 ? 0.68645 0.66647 0.92372 0.00917  -0.01652 0.03230  158 ARG A CZ  
1253 N NH1 . ARG A 158 ? 0.75134 0.73527 0.99083 0.00985  -0.01844 0.02802  158 ARG A NH1 
1254 N NH2 . ARG A 158 ? 0.69959 0.67313 0.92992 0.01549  -0.01797 0.04391  158 ARG A NH2 
1255 N N   . THR A 159 ? 0.60578 0.70709 0.87310 0.00242  -0.03884 -0.03298 159 THR A N   
1256 C CA  . THR A 159 ? 0.62155 0.75315 0.89619 0.00131  -0.04104 -0.04965 159 THR A CA  
1257 C C   . THR A 159 ? 0.59108 0.75019 0.86565 0.00986  -0.04807 -0.05427 159 THR A C   
1258 O O   . THR A 159 ? 0.58812 0.77637 0.87386 0.00454  -0.04666 -0.07022 159 THR A O   
1259 C CB  . THR A 159 ? 0.57170 0.70420 0.84012 0.00806  -0.04599 -0.04921 159 THR A CB  
1260 O OG1 . THR A 159 ? 0.56569 0.67084 0.83270 0.00254  -0.03974 -0.04234 159 THR A OG1 
1261 C CG2 . THR A 159 ? 0.55658 0.71977 0.83341 0.00447  -0.04651 -0.06802 159 THR A CG2 
1262 N N   . ARG A 160 ? 0.61397 0.76411 0.87553 0.02287  -0.05453 -0.04099 160 ARG A N   
1263 C CA  . ARG A 160 ? 0.58892 0.75998 0.84584 0.03479  -0.06064 -0.04251 160 ARG A CA  
1264 C C   . ARG A 160 ? 0.61381 0.79838 0.88252 0.02673  -0.05632 -0.05002 160 ARG A C   
1265 O O   . ARG A 160 ? 0.61289 0.83210 0.89088 0.02709  -0.05772 -0.06476 160 ARG A O   
1266 C CB  . ARG A 160 ? 0.56299 0.71082 0.80176 0.04669  -0.06420 -0.02563 160 ARG A CB  
1267 C CG  . ARG A 160 ? 0.50057 0.66112 0.72912 0.06153  -0.06881 -0.02408 160 ARG A CG  
1268 C CD  . ARG A 160 ? 0.47276 0.66034 0.69666 0.07480  -0.07451 -0.03241 160 ARG A CD  
1269 N NE  . ARG A 160 ? 0.51468 0.70723 0.72231 0.09358  -0.07806 -0.02729 160 ARG A NE  
1270 C CZ  . ARG A 160 ? 0.57712 0.79726 0.77752 0.11050  -0.08328 -0.03367 160 ARG A CZ  
1271 N NH1 . ARG A 160 ? 0.65416 0.90317 0.86383 0.10964  -0.08649 -0.04685 160 ARG A NH1 
1272 N NH2 . ARG A 160 ? 0.57551 0.79438 0.75749 0.12968  -0.08479 -0.02685 160 ARG A NH2 
1273 N N   . ILE A 161 ? 0.62750 0.78681 0.89584 0.01949  -0.05078 -0.04060 161 ILE A N   
1274 C CA  . ILE A 161 ? 0.64215 0.80923 0.91950 0.01174  -0.04548 -0.04587 161 ILE A CA  
1275 C C   . ILE A 161 ? 0.66477 0.85097 0.95892 -0.00358 -0.03758 -0.06436 161 ILE A C   
1276 O O   . ILE A 161 ? 0.66285 0.87861 0.96724 -0.00662 -0.03652 -0.07764 161 ILE A O   
1277 C CB  . ILE A 161 ? 0.60387 0.73778 0.87571 0.00692  -0.04027 -0.03183 161 ILE A CB  
1278 C CG1 . ILE A 161 ? 0.60608 0.72723 0.86237 0.02008  -0.04715 -0.01734 161 ILE A CG1 
1279 C CG2 . ILE A 161 ? 0.68615 0.82510 0.96730 -0.00332 -0.03250 -0.03832 161 ILE A CG2 
1280 C CD1 . ILE A 161 ? 0.66966 0.76115 0.91921 0.01647  -0.04375 -0.00375 161 ILE A CD1 
1281 N N   . GLU A 162 ? 0.64747 0.81763 0.94434 -0.01383 -0.03090 -0.06651 162 GLU A N   
1282 C CA  . GLU A 162 ? 0.60058 0.78416 0.91144 -0.03065 -0.02058 -0.08523 162 GLU A CA  
1283 C C   . GLU A 162 ? 0.60260 0.83224 0.92273 -0.02838 -0.02668 -0.10399 162 GLU A C   
1284 O O   . GLU A 162 ? 0.61746 0.87250 0.95170 -0.04170 -0.01960 -0.12318 162 GLU A O   
1285 C CB  . GLU A 162 ? 0.60991 0.76465 0.91847 -0.03947 -0.01185 -0.08300 162 GLU A CB  
1286 C CG  . GLU A 162 ? 0.63516 0.79773 0.95569 -0.05896 0.00205  -0.10327 162 GLU A CG  
1287 C CD  . GLU A 162 ? 0.71198 0.84205 1.02765 -0.06656 0.01265  -0.10086 162 GLU A CD  
1288 O OE1 . GLU A 162 ? 0.68568 0.79121 0.99036 -0.05611 0.00810  -0.08411 162 GLU A OE1 
1289 O OE2 . GLU A 162 ? 0.75127 0.88029 1.07388 -0.08374 0.02705  -0.11683 162 GLU A OE2 
1290 N N   . ALA A 163 ? 0.62564 0.86794 0.93737 -0.01176 -0.03889 -0.09975 163 ALA A N   
1291 C CA  . ALA A 163 ? 0.63036 0.91951 0.94871 -0.00634 -0.04554 -0.11713 163 ALA A CA  
1292 C C   . ALA A 163 ? 0.65731 0.97793 0.97522 0.00760  -0.05328 -0.11921 163 ALA A C   
1293 O O   . ALA A 163 ? 0.65455 1.02220 0.98166 0.01034  -0.05712 -0.13711 163 ALA A O   
1294 C CB  . ALA A 163 ? 0.62803 0.91709 0.93548 0.00629  -0.05382 -0.11278 163 ALA A CB  
1295 N N   . LEU A 164 ? 0.67388 0.97156 0.98078 0.01719  -0.05551 -0.10199 164 LEU A N   
1296 C CA  . LEU A 164 ? 0.65449 0.97874 0.96058 0.02979  -0.06069 -0.10386 164 LEU A CA  
1297 C C   . LEU A 164 ? 0.66593 1.00853 0.98991 0.01367  -0.05231 -0.11773 164 LEU A C   
1298 O O   . LEU A 164 ? 0.67890 1.06549 1.01160 0.01880  -0.05550 -0.13165 164 LEU A O   
1299 C CB  . LEU A 164 ? 0.67131 0.96334 0.95822 0.04449  -0.06442 -0.08193 164 LEU A CB  
1300 C CG  . LEU A 164 ? 0.68363 0.96670 0.95062 0.06418  -0.07249 -0.07113 164 LEU A CG  
1301 C CD1 . LEU A 164 ? 0.70272 0.94756 0.95037 0.07356  -0.07279 -0.05067 164 LEU A CD1 
1302 C CD2 . LEU A 164 ? 0.64338 0.97034 0.90725 0.08294  -0.08038 -0.08144 164 LEU A CD2 
1303 N N   . LEU A 165 ? 0.65718 0.96769 0.98591 -0.00508 -0.04084 -0.11460 165 LEU A N   
1304 C CA  . LEU A 165 ? 0.61294 0.93413 0.95623 -0.02187 -0.03016 -0.12694 165 LEU A CA  
1305 C C   . LEU A 165 ? 0.59005 0.93656 0.95090 -0.04205 -0.02072 -0.15139 165 LEU A C   
1306 O O   . LEU A 165 ? 0.63962 1.00261 1.01390 -0.05726 -0.01085 -0.16614 165 LEU A O   
1307 C CB  . LEU A 165 ? 0.59244 0.86521 0.92920 -0.03109 -0.02057 -0.11159 165 LEU A CB  
1308 C CG  . LEU A 165 ? 0.66259 0.91042 0.98335 -0.01556 -0.02741 -0.08964 165 LEU A CG  
1309 C CD1 . LEU A 165 ? 0.69645 0.89987 1.01038 -0.02434 -0.01845 -0.07556 165 LEU A CD1 
1310 C CD2 . LEU A 165 ? 0.63886 0.91448 0.96080 -0.00459 -0.03275 -0.09241 165 LEU A CD2 
1311 N N   . LEU A 166 ? 0.58284 0.93351 0.94371 -0.04353 -0.02250 -0.15728 166 LEU A N   
1312 C CA  . LEU A 166 ? 0.57438 0.94651 0.95061 -0.06450 -0.01212 -0.18165 166 LEU A CA  
1313 C C   . LEU A 166 ? 0.56645 0.90574 0.94755 -0.08910 0.00796  -0.18551 166 LEU A C   
1314 O O   . LEU A 166 ? 0.57906 0.94219 0.97521 -0.10869 0.01982  -0.20824 166 LEU A O   
1315 C CB  . LEU A 166 ? 0.54833 0.98704 0.94058 -0.06432 -0.01676 -0.20657 166 LEU A CB  
1316 C CG  . LEU A 166 ? 0.63558 1.11935 1.02525 -0.04291 -0.03349 -0.21185 166 LEU A CG  
1317 C CD1 . LEU A 166 ? 0.62603 1.09551 1.00821 -0.04186 -0.03600 -0.20977 166 LEU A CD1 
1318 C CD2 . LEU A 166 ? 0.68162 1.16715 1.05651 -0.01394 -0.04754 -0.19307 166 LEU A CD2 
1319 N N   . VAL A 167 ? 0.56624 0.85079 0.93342 -0.08805 0.01299  -0.16392 167 VAL A N   
1320 C CA  . VAL A 167 ? 0.60211 0.84820 0.96828 -0.10765 0.03309  -0.16429 167 VAL A CA  
1321 C C   . VAL A 167 ? 0.60178 0.79931 0.95375 -0.10601 0.03757  -0.14824 167 VAL A C   
1322 O O   . VAL A 167 ? 0.65601 0.83150 0.99516 -0.08914 0.02720  -0.12623 167 VAL A O   
1323 C CB  . VAL A 167 ? 0.62189 0.85200 0.98455 -0.10689 0.03712  -0.15378 167 VAL A CB  
1324 C CG1 . VAL A 167 ? 0.61030 0.78924 0.96396 -0.12040 0.05651  -0.14649 167 VAL A CG1 
1325 C CG2 . VAL A 167 ? 0.55651 0.83247 0.93590 -0.11570 0.03960  -0.17498 167 VAL A CG2 
1326 N N   . ARG A 168 ? 0.57000 0.75014 0.92359 -0.12393 0.05444  -0.15967 168 ARG A N   
1327 C CA  . ARG A 168 ? 0.68808 0.82605 1.02844 -0.12104 0.05904  -0.14625 168 ARG A CA  
1328 C C   . ARG A 168 ? 0.73729 0.83006 1.06168 -0.11116 0.06116  -0.12069 168 ARG A C   
1329 O O   . ARG A 168 ? 0.74869 0.82662 1.07078 -0.11705 0.07113  -0.11816 168 ARG A O   
1330 C CB  . ARG A 168 ? 0.73198 0.85343 1.07437 -0.14302 0.08082  -0.16334 168 ARG A CB  
1331 C CG  . ARG A 168 ? 0.76738 0.84841 1.09602 -0.13838 0.08557  -0.15087 168 ARG A CG  
1332 C CD  . ARG A 168 ? 0.76658 0.82540 1.09406 -0.15978 0.10958  -0.16733 168 ARG A CD  
1333 N NE  . ARG A 168 ? 0.83906 0.86034 1.15250 -0.15217 0.11310  -0.15407 168 ARG A NE  
1334 C CZ  . ARG A 168 ? 0.84243 0.87787 1.15858 -0.14913 0.10533  -0.15945 168 ARG A CZ  
1335 N NH1 . ARG A 168 ? 0.78126 0.86718 1.11243 -0.15291 0.09407  -0.17826 168 ARG A NH1 
1336 N NH2 . ARG A 168 ? 0.81171 0.81119 1.11449 -0.14105 0.10912  -0.14579 168 ARG A NH2 
1337 N N   . ASP A 169 ? 0.86489 0.93783 1.17813 -0.09615 0.05202  -0.10260 169 ASP A N   
1338 C CA  . ASP A 169 ? 0.88052 0.91559 1.17846 -0.08493 0.05222  -0.07886 169 ASP A CA  
1339 C C   . ASP A 169 ? 0.86512 0.90599 1.16132 -0.07712 0.04448  -0.06883 169 ASP A C   
1340 O O   . ASP A 169 ? 0.89065 0.90225 1.17506 -0.07158 0.04816  -0.05263 169 ASP A O   
1341 C CB  . ASP A 169 ? 0.90589 0.89731 1.19333 -0.09414 0.07393  -0.07594 169 ASP A CB  
1342 C CG  . ASP A 169 ? 1.01438 0.98356 1.29373 -0.08978 0.07692  -0.07048 169 ASP A CG  
1343 O OD1 . ASP A 169 ? 1.03397 1.00576 1.30916 -0.07407 0.06179  -0.05679 169 ASP A OD1 
1344 O OD2 . ASP A 169 ? 1.06355 1.01359 1.34071 -0.10257 0.09489  -0.08096 169 ASP A OD2 
1345 N N   . MET A 170 ? 0.72339 0.80227 1.02975 -0.07474 0.03342  -0.07760 170 MET A N   
1346 C CA  . MET A 170 ? 0.71866 0.80297 1.02232 -0.06606 0.02567  -0.06796 170 MET A CA  
1347 C C   . MET A 170 ? 0.77343 0.86515 1.07032 -0.04776 0.00758  -0.05500 170 MET A C   
1348 O O   . MET A 170 ? 0.72418 0.84639 1.02594 -0.04109 -0.00319 -0.06219 170 MET A O   
1349 C CB  . MET A 170 ? 0.72089 0.83926 1.03772 -0.07365 0.02702  -0.08464 170 MET A CB  
1350 C CG  . MET A 170 ? 0.79399 0.91010 1.10578 -0.06544 0.02202  -0.07316 170 MET A CG  
1351 S SD  . MET A 170 ? 0.78759 0.93730 1.11316 -0.07415 0.02642  -0.08991 170 MET A SD  
1352 C CE  . MET A 170 ? 0.82240 0.95968 1.13596 -0.05894 0.01736  -0.06979 170 MET A CE  
1353 N N   . THR A 171 ? 0.79603 0.85998 1.08033 -0.03941 0.00531  -0.03626 171 THR A N   
1354 C CA  . THR A 171 ? 0.79181 0.85593 1.06791 -0.02510 -0.00823 -0.02420 171 THR A CA  
1355 C C   . THR A 171 ? 0.80672 0.86555 1.07460 -0.01691 -0.01411 -0.01175 171 THR A C   
1356 O O   . THR A 171 ? 0.81071 0.86635 1.07003 -0.00665 -0.02330 -0.00181 171 THR A O   
1357 C CB  . THR A 171 ? 0.81676 0.85680 1.08565 -0.02281 -0.00617 -0.01483 171 THR A CB  
1358 O OG1 . THR A 171 ? 0.90087 0.91394 1.16145 -0.02289 0.00112  -0.00285 171 THR A OG1 
1359 C CG2 . THR A 171 ? 0.76336 0.80331 1.03899 -0.03260 0.00275  -0.02739 171 THR A CG2 
1360 N N   . THR A 172 ? 0.80354 0.86014 1.07295 -0.02211 -0.00792 -0.01261 172 THR A N   
1361 C CA  . THR A 172 ? 0.75156 0.80969 1.01481 -0.01510 -0.01371 -0.00459 172 THR A CA  
1362 C C   . THR A 172 ? 0.76014 0.84424 1.03263 -0.01765 -0.01340 -0.01678 172 THR A C   
1363 O O   . THR A 172 ? 0.78699 0.88148 1.07049 -0.02898 -0.00457 -0.03016 172 THR A O   
1364 C CB  . THR A 172 ? 0.71992 0.75256 0.97420 -0.01628 -0.00781 0.00761  172 THR A CB  
1365 O OG1 . THR A 172 ? 0.76306 0.78933 1.02201 -0.02728 0.00529  0.00104  172 THR A OG1 
1366 C CG2 . THR A 172 ? 0.72590 0.73766 0.97162 -0.01237 -0.00785 0.01880  172 THR A CG2 
1367 N N   . CYS A 173 ? 0.78027 0.87487 1.04763 -0.00724 -0.02197 -0.01283 173 CYS A N   
1368 C CA  . CYS A 173 ? 0.78729 0.91075 1.06216 -0.00524 -0.02362 -0.02371 173 CYS A CA  
1369 C C   . CYS A 173 ? 0.79831 0.91450 1.06835 -0.00428 -0.02148 -0.01746 173 CYS A C   
1370 O O   . CYS A 173 ? 0.81950 0.91525 1.07644 0.00184  -0.02471 -0.00363 173 CYS A O   
1371 C CB  . CYS A 173 ? 0.78057 0.92424 1.05097 0.00965  -0.03461 -0.02513 173 CYS A CB  
1372 S SG  . CYS A 173 ? 0.79731 0.98009 1.07446 0.01750  -0.03773 -0.03728 173 CYS A SG  
1373 N N   . PRO A 174 ? 0.86730 1.00151 1.14801 -0.01118 -0.01553 -0.02868 174 PRO A N   
1374 C CA  . PRO A 174 ? 0.85022 0.97870 1.12692 -0.01082 -0.01263 -0.02382 174 PRO A CA  
1375 C C   . PRO A 174 ? 0.82587 0.96434 1.09369 0.00496  -0.02192 -0.01877 174 PRO A C   
1376 O O   . PRO A 174 ? 0.77162 0.93673 1.04239 0.01469  -0.02816 -0.02626 174 PRO A O   
1377 C CB  . PRO A 174 ? 0.88724 1.03778 1.17991 -0.02323 -0.00316 -0.04058 174 PRO A CB  
1378 C CG  . PRO A 174 ? 0.90025 1.05410 1.20250 -0.03460 0.00273  -0.05138 174 PRO A CG  
1379 C CD  . PRO A 174 ? 0.85467 1.01222 1.15203 -0.02324 -0.00856 -0.04727 174 PRO A CD  
1380 N N   . LEU A 175 ? 0.88803 1.00489 1.14347 0.00803  -0.02172 -0.00644 175 LEU A N   
1381 C CA  . LEU A 175 ? 0.89524 1.01229 1.13783 0.02236  -0.02818 0.00007  175 LEU A CA  
1382 C C   . LEU A 175 ? 0.87655 0.99921 1.11898 0.02310  -0.02449 -0.00112 175 LEU A C   
1383 O O   . LEU A 175 ? 0.79940 0.91092 1.04458 0.01242  -0.01735 0.00020  175 LEU A O   
1384 C CB  . LEU A 175 ? 0.82272 0.90977 1.04843 0.02565  -0.03113 0.01473  175 LEU A CB  
1385 C CG  . LEU A 175 ? 0.79854 0.88052 1.02293 0.02675  -0.03516 0.01645  175 LEU A CG  
1386 C CD1 . LEU A 175 ? 0.74253 0.79848 0.95307 0.02690  -0.03661 0.02881  175 LEU A CD1 
1387 C CD2 . LEU A 175 ? 0.72172 0.82241 0.94431 0.03903  -0.04090 0.01098  175 LEU A CD2 
1388 N N   . PRO A 176 ? 0.85937 0.99748 1.09654 0.03696  -0.02853 -0.00285 176 PRO A N   
1389 C CA  . PRO A 176 ? 0.79940 0.94069 1.03424 0.03940  -0.02504 -0.00274 176 PRO A CA  
1390 C C   . PRO A 176 ? 0.84820 0.95564 1.06909 0.03491  -0.02208 0.01031  176 PRO A C   
1391 O O   . PRO A 176 ? 0.80785 0.89250 1.01622 0.03617  -0.02483 0.02002  176 PRO A O   
1392 C CB  . PRO A 176 ? 0.77272 0.92933 0.99798 0.05942  -0.03037 -0.00344 176 PRO A CB  
1393 C CG  . PRO A 176 ? 0.83329 1.00908 1.06386 0.06509  -0.03598 -0.00994 176 PRO A CG  
1394 C CD  . PRO A 176 ? 0.82044 0.97322 1.05168 0.05278  -0.03567 -0.00473 176 PRO A CD  
1395 N N   . LYS A 177 ? 0.88808 0.99491 1.11167 0.02902  -0.01606 0.00929  177 LYS A N   
1396 C CA  . LYS A 177 ? 0.83194 0.91096 1.04559 0.02160  -0.01206 0.01940  177 LYS A CA  
1397 C C   . LYS A 177 ? 0.77238 0.83195 0.96595 0.03028  -0.01522 0.02960  177 LYS A C   
1398 O O   . LYS A 177 ? 0.80160 0.86684 0.98757 0.04194  -0.01652 0.02881  177 LYS A O   
1399 C CB  . LYS A 177 ? 0.86440 0.94880 1.08494 0.01403  -0.00408 0.01489  177 LYS A CB  
1400 N N   . GLY A 178 ? 0.77443 0.81127 0.95840 0.02469  -0.01540 0.03856  178 GLY A N   
1401 C CA  . GLY A 178 ? 0.77542 0.79389 0.94088 0.02922  -0.01715 0.04618  178 GLY A CA  
1402 C C   . GLY A 178 ? 0.87839 0.89106 1.03711 0.03411  -0.02183 0.04841  178 GLY A C   
1403 O O   . GLY A 178 ? 0.90777 0.90298 1.05081 0.03463  -0.02161 0.05382  178 GLY A O   
1404 N N   . THR A 179 ? 0.84965 0.87644 1.01915 0.03673  -0.02514 0.04345  179 THR A N   
1405 C CA  . THR A 179 ? 0.81517 0.83613 0.97744 0.04196  -0.02905 0.04549  179 THR A CA  
1406 C C   . THR A 179 ? 0.82034 0.82353 0.97603 0.03387  -0.02949 0.05218  179 THR A C   
1407 O O   . THR A 179 ? 0.80489 0.79301 0.94520 0.03556  -0.02892 0.05612  179 THR A O   
1408 C CB  . THR A 179 ? 0.79251 0.83298 0.96941 0.04356  -0.03241 0.03847  179 THR A CB  
1409 O OG1 . THR A 179 ? 0.82220 0.88531 1.00484 0.05258  -0.03281 0.03065  179 THR A OG1 
1410 C CG2 . THR A 179 ? 0.68293 0.71616 0.85232 0.04809  -0.03604 0.04102  179 THR A CG2 
1411 N N   . LEU A 180 ? 0.80060 0.80543 0.96665 0.02505  -0.02924 0.05305  180 LEU A N   
1412 C CA  . LEU A 180 ? 0.79670 0.79143 0.95888 0.01954  -0.03057 0.05855  180 LEU A CA  
1413 C C   . LEU A 180 ? 0.85420 0.83926 1.00641 0.01495  -0.02842 0.06350  180 LEU A C   
1414 O O   . LEU A 180 ? 0.85631 0.83860 1.00704 0.01070  -0.02947 0.06747  180 LEU A O   
1415 C CB  . LEU A 180 ? 0.83013 0.82994 1.00536 0.01513  -0.03041 0.05779  180 LEU A CB  
1416 C CG  . LEU A 180 ? 0.78766 0.79787 0.97221 0.01824  -0.03280 0.05186  180 LEU A CG  
1417 C CD1 . LEU A 180 ? 0.76160 0.77482 0.95853 0.01262  -0.02993 0.04939  180 LEU A CD1 
1418 C CD2 . LEU A 180 ? 0.73688 0.74174 0.91332 0.02195  -0.03691 0.05426  180 LEU A CD2 
1419 N N   . ASP A 181 ? 0.88875 0.87047 1.03363 0.01657  -0.02545 0.06296  181 ASP A N   
1420 C CA  . ASP A 181 ? 0.84391 0.81689 0.97756 0.01191  -0.02326 0.06655  181 ASP A CA  
1421 C C   . ASP A 181 ? 0.83774 0.80361 0.96059 0.00873  -0.02467 0.06805  181 ASP A C   
1422 O O   . ASP A 181 ? 0.81177 0.76941 0.92492 0.01146  -0.02324 0.06631  181 ASP A O   
1423 C CB  . ASP A 181 ? 0.91736 0.88558 1.04250 0.01500  -0.01916 0.06505  181 ASP A CB  
1424 C CG  . ASP A 181 ? 0.96861 0.92920 1.08293 0.00896  -0.01632 0.06776  181 ASP A CG  
1425 O OD1 . ASP A 181 ? 0.96153 0.92502 1.07777 0.00374  -0.01795 0.07080  181 ASP A OD1 
1426 O OD2 . ASP A 181 ? 0.95759 0.90912 1.05964 0.01028  -0.01225 0.06679  181 ASP A OD2 
1427 N N   . GLY A 182 ? 0.89470 0.86385 1.01759 0.00332  -0.02629 0.07087  182 GLY A N   
1428 C CA  . GLY A 182 ? 0.91456 0.88386 1.03070 -0.00128 -0.02785 0.07053  182 GLY A CA  
1429 C C   . GLY A 182 ? 0.90210 0.88032 1.02784 -0.00058 -0.03216 0.07218  182 GLY A C   
1430 O O   . GLY A 182 ? 0.93497 0.91819 1.05735 -0.00448 -0.03384 0.07136  182 GLY A O   
1431 N N   . PHE A 183 ? 0.80332 0.78444 0.94080 0.00363  -0.03308 0.07354  183 PHE A N   
1432 C CA  . PHE A 183 ? 0.79338 0.78004 0.93899 0.00511  -0.03592 0.07497  183 PHE A CA  
1433 C C   . PHE A 183 ? 0.83437 0.82799 0.97763 0.00465  -0.03731 0.07935  183 PHE A C   
1434 O O   . PHE A 183 ? 0.93397 0.92772 1.07280 0.00487  -0.03553 0.08239  183 PHE A O   
1435 C CB  . PHE A 183 ? 0.82701 0.81364 0.98423 0.00804  -0.03435 0.07423  183 PHE A CB  
1436 C CG  . PHE A 183 ? 0.83845 0.82788 1.00319 0.00967  -0.03616 0.07447  183 PHE A CG  
1437 C CD1 . PHE A 183 ? 0.78458 0.77547 0.95172 0.01095  -0.03871 0.07075  183 PHE A CD1 
1438 C CD2 . PHE A 183 ? 0.84436 0.83334 1.01138 0.01114  -0.03456 0.07896  183 PHE A CD2 
1439 C CE1 . PHE A 183 ? 0.82248 0.81578 0.99610 0.01218  -0.04016 0.07073  183 PHE A CE1 
1440 C CE2 . PHE A 183 ? 0.86615 0.85615 1.03882 0.01324  -0.03535 0.07930  183 PHE A CE2 
1441 C CZ  . PHE A 183 ? 0.86207 0.85498 1.03898 0.01303  -0.03844 0.07482  183 PHE A CZ  
1442 N N   . VAL A 184 ? 0.85961 0.86050 1.00502 0.00522  -0.04044 0.07963  184 VAL A N   
1443 C CA  . VAL A 184 ? 0.91621 0.92877 1.05959 0.00768  -0.04257 0.08345  184 VAL A CA  
1444 C C   . VAL A 184 ? 1.01620 1.03094 1.16729 0.01315  -0.04367 0.08597  184 VAL A C   
1445 O O   . VAL A 184 ? 0.91626 0.92886 1.07302 0.01193  -0.04466 0.08268  184 VAL A O   
1446 C CB  . VAL A 184 ? 0.87135 0.89654 1.00781 0.00181  -0.04492 0.07925  184 VAL A CB  
1447 C CG1 . VAL A 184 ? 0.86348 0.90799 1.00019 0.00608  -0.04846 0.08158  184 VAL A CG1 
1448 C CG2 . VAL A 184 ? 0.93903 0.96178 1.06618 -0.00279 -0.04268 0.07769  184 VAL A CG2 
1449 N N   . ALA A 185 ? 1.32610 1.34334 1.47543 0.02031  -0.04259 0.09223  185 ALA A N   
1450 C CA  . ALA A 185 ? 1.32620 1.33798 1.48064 0.02680  -0.04036 0.09579  185 ALA A CA  
1451 C C   . ALA A 185 ? 1.32586 1.34821 1.48534 0.02782  -0.04447 0.09367  185 ALA A C   
1452 O O   . ALA A 185 ? 1.30557 1.32163 1.47236 0.02572  -0.04405 0.09038  185 ALA A O   
1453 C CB  . ALA A 185 ? 1.33722 1.34664 1.48349 0.03650  -0.03666 0.10413  185 ALA A CB  
1454 N N   . HIS A 186 ? 1.12717 1.16809 1.28302 0.03096  -0.04843 0.09463  186 HIS A N   
1455 C CA  . HIS A 186 ? 1.04103 1.09349 1.20217 0.03326  -0.05132 0.09304  186 HIS A CA  
1456 C C   . HIS A 186 ? 0.93299 0.99290 1.09671 0.02253  -0.05410 0.08451  186 HIS A C   
1457 O O   . HIS A 186 ? 0.88663 0.96534 1.05158 0.02095  -0.05694 0.08086  186 HIS A O   
1458 C CB  . HIS A 186 ? 1.03655 1.10903 1.19296 0.04374  -0.05365 0.09766  186 HIS A CB  
1459 N N   . ASP A 187 ? 0.84355 0.88803 1.00739 0.01568  -0.05215 0.08092  187 ASP A N   
1460 C CA  . ASP A 187 ? 0.80267 0.84740 0.96365 0.00642  -0.05208 0.07381  187 ASP A CA  
1461 C C   . ASP A 187 ? 0.80835 0.84149 0.97372 0.00646  -0.05118 0.07179  187 ASP A C   
1462 O O   . ASP A 187 ? 0.75931 0.77960 0.92716 0.00912  -0.04985 0.07289  187 ASP A O   
1463 C CB  . ASP A 187 ? 0.79701 0.83248 0.94977 0.00048  -0.04957 0.07148  187 ASP A CB  
1464 C CG  . ASP A 187 ? 0.79353 0.82896 0.93869 -0.00943 -0.04706 0.06416  187 ASP A CG  
1465 O OD1 . ASP A 187 ? 0.84438 0.89236 0.99128 -0.01318 -0.04766 0.06017  187 ASP A OD1 
1466 O OD2 . ASP A 187 ? 0.81854 0.83960 0.95518 -0.01349 -0.04314 0.06195  187 ASP A OD2 
1467 N N   . SER A 188 ? 0.77588 0.81565 0.94191 0.00306  -0.05159 0.06779  188 SER A N   
1468 C CA  . SER A 188 ? 0.68724 0.71723 0.85588 0.00388  -0.05076 0.06596  188 SER A CA  
1469 C C   . SER A 188 ? 0.70784 0.72076 0.86837 0.00151  -0.04771 0.06338  188 SER A C   
1470 O O   . SER A 188 ? 0.69650 0.70072 0.85955 0.00627  -0.04785 0.06370  188 SER A O   
1471 C CB  . SER A 188 ? 0.70105 0.74213 0.87057 -0.00001 -0.05072 0.06196  188 SER A CB  
1472 O OG  . SER A 188 ? 0.78337 0.84464 0.95871 0.00392  -0.05377 0.06423  188 SER A OG  
1473 N N   . ILE A 189 ? 0.68152 0.69016 0.83121 -0.00511 -0.04431 0.06033  189 ILE A N   
1474 C CA  . ILE A 189 ? 0.65928 0.64902 0.79781 -0.00474 -0.03998 0.05877  189 ILE A CA  
1475 C C   . ILE A 189 ? 0.66412 0.64928 0.80493 0.00144  -0.04130 0.06180  189 ILE A C   
1476 O O   . ILE A 189 ? 0.67741 0.65324 0.81502 0.00721  -0.04032 0.06141  189 ILE A O   
1477 C CB  . ILE A 189 ? 0.68902 0.67060 0.81262 -0.01403 -0.03327 0.05416  189 ILE A CB  
1478 C CG1 . ILE A 189 ? 0.62106 0.60676 0.74263 -0.02153 -0.03014 0.04913  189 ILE A CG1 
1479 C CG2 . ILE A 189 ? 0.66216 0.62018 0.77038 -0.01060 -0.02719 0.05410  189 ILE A CG2 
1480 C CD1 . ILE A 189 ? 0.57997 0.55895 0.68740 -0.03403 -0.02145 0.04224  189 ILE A CD1 
1481 N N   . HIS A 190 ? 0.72707 0.72032 0.87311 0.00113  -0.04324 0.06448  190 HIS A N   
1482 C CA  . HIS A 190 ? 0.69556 0.68502 0.84442 0.00556  -0.04322 0.06634  190 HIS A CA  
1483 C C   . HIS A 190 ? 0.70132 0.69322 0.86172 0.01105  -0.04513 0.06651  190 HIS A C   
1484 O O   . HIS A 190 ? 0.63930 0.62847 0.80076 0.01487  -0.04451 0.06436  190 HIS A O   
1485 C CB  . HIS A 190 ? 0.73761 0.73282 0.88713 0.00370  -0.04342 0.06928  190 HIS A CB  
1486 C CG  . HIS A 190 ? 0.79572 0.78913 0.93350 -0.00249 -0.04091 0.06736  190 HIS A CG  
1487 N ND1 . HIS A 190 ? 0.80035 0.79952 0.93581 -0.00441 -0.04094 0.06921  190 HIS A ND1 
1488 C CD2 . HIS A 190 ? 0.75692 0.74218 0.88314 -0.00790 -0.03698 0.06308  190 HIS A CD2 
1489 C CE1 . HIS A 190 ? 0.76452 0.76150 0.88893 -0.01147 -0.03788 0.06530  190 HIS A CE1 
1490 N NE2 . HIS A 190 ? 0.78211 0.76930 0.90041 -0.01428 -0.03463 0.06137  190 HIS A NE2 
1491 N N   . ASP A 191 ? 0.75438 0.75275 0.92297 0.01168  -0.04689 0.06814  191 ASP A N   
1492 C CA  . ASP A 191 ? 0.68166 0.68083 0.86014 0.01509  -0.04725 0.06682  191 ASP A CA  
1493 C C   . ASP A 191 ? 0.66532 0.66215 0.84193 0.01763  -0.04802 0.06238  191 ASP A C   
1494 O O   . ASP A 191 ? 0.67725 0.67672 0.85973 0.02044  -0.04800 0.05883  191 ASP A O   
1495 C CB  . ASP A 191 ? 0.74152 0.74518 0.92533 0.01615  -0.04799 0.06933  191 ASP A CB  
1496 C CG  . ASP A 191 ? 0.88727 0.89197 1.07246 0.01809  -0.04606 0.07466  191 ASP A CG  
1497 O OD1 . ASP A 191 ? 0.88417 0.88377 1.06971 0.01783  -0.04301 0.07545  191 ASP A OD1 
1498 O OD2 . ASP A 191 ? 0.87755 0.88837 1.06251 0.02097  -0.04695 0.07813  191 ASP A OD2 
1499 N N   . CYS A 192 ? 0.61190 0.60455 0.77927 0.01677  -0.04790 0.06182  192 CYS A N   
1500 C CA  . CYS A 192 ? 0.63135 0.61893 0.79266 0.02148  -0.04759 0.05880  192 CYS A CA  
1501 C C   . CYS A 192 ? 0.66299 0.64682 0.81730 0.02677  -0.04632 0.05749  192 CYS A C   
1502 O O   . CYS A 192 ? 0.67342 0.66186 0.82936 0.03376  -0.04769 0.05435  192 CYS A O   
1503 C CB  . CYS A 192 ? 0.65138 0.63086 0.80118 0.01877  -0.04505 0.05859  192 CYS A CB  
1504 S SG  . CYS A 192 ? 0.64721 0.63444 0.80565 0.01572  -0.04678 0.05829  192 CYS A SG  
1505 N N   . ALA A 193 ? 0.72807 0.70570 0.87430 0.02428  -0.04369 0.05928  193 ALA A N   
1506 C CA  . ALA A 193 ? 0.68543 0.65974 0.82457 0.03059  -0.04194 0.05838  193 ALA A CA  
1507 C C   . ALA A 193 ? 0.66676 0.65566 0.82061 0.03314  -0.04458 0.05564  193 ALA A C   
1508 O O   . ALA A 193 ? 0.67508 0.67040 0.82829 0.04128  -0.04517 0.05223  193 ALA A O   
1509 C CB  . ALA A 193 ? 0.68245 0.64663 0.81044 0.02616  -0.03781 0.06043  193 ALA A CB  
1510 N N   . LYS A 194 ? 0.66968 0.66455 0.83590 0.02666  -0.04520 0.05649  194 LYS A N   
1511 C CA  . LYS A 194 ? 0.65294 0.65915 0.83267 0.02644  -0.04502 0.05242  194 LYS A CA  
1512 C C   . LYS A 194 ? 0.66204 0.67884 0.84973 0.02992  -0.04709 0.04638  194 LYS A C   
1513 O O   . LYS A 194 ? 0.64146 0.67172 0.83549 0.03311  -0.04731 0.03978  194 LYS A O   
1514 C CB  . LYS A 194 ? 0.64383 0.64857 0.83125 0.01972  -0.04286 0.05531  194 LYS A CB  
1515 C CG  . LYS A 194 ? 0.68543 0.69788 0.88531 0.01720  -0.03965 0.04985  194 LYS A CG  
1516 C CD  . LYS A 194 ? 0.80330 0.80848 1.00720 0.01205  -0.03484 0.05341  194 LYS A CD  
1517 C CE  . LYS A 194 ? 0.86535 0.86747 1.07247 0.01205  -0.03498 0.05451  194 LYS A CE  
1518 N NZ  . LYS A 194 ? 1.01871 1.01106 1.22781 0.00935  -0.02787 0.05755  194 LYS A NZ  
1519 N N   . ASP A 195 ? 0.63737 0.65094 0.82521 0.02921  -0.04858 0.04754  195 ASP A N   
1520 C CA  . ASP A 195 ? 0.64008 0.66364 0.83438 0.03227  -0.05050 0.04143  195 ASP A CA  
1521 C C   . ASP A 195 ? 0.66266 0.69211 0.84788 0.04272  -0.05272 0.03830  195 ASP A C   
1522 O O   . ASP A 195 ? 0.65451 0.70145 0.84698 0.04677  -0.05446 0.03055  195 ASP A O   
1523 C CB  . ASP A 195 ? 0.69322 0.71083 0.88791 0.03009  -0.05123 0.04386  195 ASP A CB  
1524 C CG  . ASP A 195 ? 0.72237 0.73875 0.92811 0.02344  -0.04843 0.04462  195 ASP A CG  
1525 O OD1 . ASP A 195 ? 0.70258 0.72419 0.91750 0.02001  -0.04522 0.03992  195 ASP A OD1 
1526 O OD2 . ASP A 195 ? 0.72566 0.73557 0.92981 0.02209  -0.04835 0.04952  195 ASP A OD2 
1527 N N   . ILE A 196 ? 0.63878 0.65419 0.80677 0.04766  -0.05170 0.04362  196 ILE A N   
1528 C CA  . ILE A 196 ? 0.66383 0.68003 0.81814 0.06067  -0.05194 0.04242  196 ILE A CA  
1529 C C   . ILE A 196 ? 0.68165 0.71346 0.84074 0.06602  -0.05250 0.03807  196 ILE A C   
1530 O O   . ILE A 196 ? 0.71532 0.76332 0.87315 0.07743  -0.05486 0.03292  196 ILE A O   
1531 C CB  . ILE A 196 ? 0.65682 0.64874 0.78873 0.06351  -0.04726 0.04896  196 ILE A CB  
1532 C CG1 . ILE A 196 ? 0.64517 0.62492 0.77298 0.05739  -0.04590 0.05145  196 ILE A CG1 
1533 C CG2 . ILE A 196 ? 0.61210 0.60011 0.72562 0.07974  -0.04553 0.04913  196 ILE A CG2 
1534 C CD1 . ILE A 196 ? 0.65304 0.60978 0.76196 0.05411  -0.03921 0.05573  196 ILE A CD1 
1535 N N   . LEU A 197 ? 0.64835 0.67804 0.81309 0.05842  -0.05036 0.03956  197 LEU A N   
1536 C CA  . LEU A 197 ? 0.66244 0.70682 0.83233 0.06210  -0.04991 0.03519  197 LEU A CA  
1537 C C   . LEU A 197 ? 0.63839 0.70934 0.82846 0.05870  -0.05173 0.02483  197 LEU A C   
1538 O O   . LEU A 197 ? 0.61792 0.71119 0.81123 0.06727  -0.05343 0.01751  197 LEU A O   
1539 C CB  . LEU A 197 ? 0.66595 0.69868 0.83501 0.05401  -0.04630 0.03982  197 LEU A CB  
1540 C CG  . LEU A 197 ? 0.62977 0.64094 0.77770 0.05834  -0.04301 0.04672  197 LEU A CG  
1541 C CD1 . LEU A 197 ? 0.69157 0.69086 0.83858 0.04773  -0.04014 0.05117  197 LEU A CD1 
1542 C CD2 . LEU A 197 ? 0.60090 0.61808 0.73998 0.07172  -0.04182 0.04483  197 LEU A CD2 
1543 N N   . MET A 198 ? 0.59230 0.66201 0.79520 0.04658  -0.05049 0.02325  198 MET A N   
1544 C CA  . MET A 198 ? 0.60312 0.69443 0.82407 0.04036  -0.04937 0.01194  198 MET A CA  
1545 C C   . MET A 198 ? 0.66279 0.77437 0.88654 0.04752  -0.05368 0.00358  198 MET A C   
1546 O O   . MET A 198 ? 0.64557 0.78388 0.88284 0.04526  -0.05338 -0.00896 198 MET A O   
1547 C CB  . MET A 198 ? 0.65191 0.73096 0.88154 0.02707  -0.04469 0.01326  198 MET A CB  
1548 C CG  . MET A 198 ? 0.69956 0.76385 0.92766 0.02061  -0.03987 0.01962  198 MET A CG  
1549 S SD  . MET A 198 ? 0.70857 0.75975 0.94485 0.00820  -0.03195 0.02010  198 MET A SD  
1550 C CE  . MET A 198 ? 0.73834 0.77310 0.96618 0.01132  -0.03561 0.02988  198 MET A CE  
1551 N N   . MET A 199 ? 0.68466 0.78540 0.89595 0.05523  -0.05703 0.00918  199 MET A N   
1552 C CA  . MET A 199 ? 0.64986 0.76983 0.86083 0.06429  -0.06134 0.00192  199 MET A CA  
1553 C C   . MET A 199 ? 0.67114 0.80950 0.87313 0.08114  -0.06447 -0.00096 199 MET A C   
1554 O O   . MET A 199 ? 0.68433 0.85447 0.89410 0.08698  -0.06778 -0.01234 199 MET A O   
1555 C CB  . MET A 199 ? 0.64430 0.74567 0.84286 0.06803  -0.06280 0.00896  199 MET A CB  
1556 C CG  . MET A 199 ? 0.70441 0.79470 0.91213 0.05515  -0.06077 0.00989  199 MET A CG  
1557 S SD  . MET A 199 ? 0.70746 0.78390 0.90151 0.06152  -0.06286 0.01514  199 MET A SD  
1558 C CE  . MET A 199 ? 0.67027 0.71798 0.84373 0.06505  -0.06021 0.02808  199 MET A CE  
1559 N N   . LYS A 200 ? 0.65919 0.77856 0.84342 0.09000  -0.06298 0.00883  200 LYS A N   
1560 C CA  . LYS A 200 ? 0.70731 0.83992 0.87918 0.10892  -0.06450 0.00791  200 LYS A CA  
1561 C C   . LYS A 200 ? 0.74044 0.90627 0.92954 0.10760  -0.06521 -0.00306 200 LYS A C   
1562 O O   . LYS A 200 ? 0.72903 0.92761 0.91988 0.12100  -0.06906 -0.01185 200 LYS A O   
1563 C CB  . LYS A 200 ? 0.75906 0.85801 0.90721 0.11573  -0.05988 0.02063  200 LYS A CB  
1564 C CG  . LYS A 200 ? 0.86008 0.96266 0.98877 0.13789  -0.05900 0.02271  200 LYS A CG  
1565 C CD  . LYS A 200 ? 0.91145 1.01821 1.02353 0.15671  -0.06119 0.02311  200 LYS A CD  
1566 C CE  . LYS A 200 ? 0.96419 1.03071 1.05569 0.15472  -0.05603 0.03346  200 LYS A CE  
1567 N NZ  . LYS A 200 ? 0.98321 1.01482 1.05063 0.15927  -0.04741 0.04329  200 LYS A NZ  
1568 N N   . TYR A 201 ? 0.70484 0.86511 0.90670 0.09186  -0.06118 -0.00351 201 TYR A N   
1569 C CA  . TYR A 201 ? 0.75386 0.94561 0.97300 0.08820  -0.06022 -0.01533 201 TYR A CA  
1570 C C   . TYR A 201 ? 0.73896 0.96439 0.97876 0.08002  -0.06161 -0.03147 201 TYR A C   
1571 O O   . TYR A 201 ? 0.73415 0.99891 0.98343 0.08630  -0.06385 -0.04441 201 TYR A O   
1572 C CB  . TYR A 201 ? 0.79392 0.96930 1.01965 0.07334  -0.05411 -0.01185 201 TYR A CB  
1573 C CG  . TYR A 201 ? 0.80622 0.96754 1.01657 0.08312  -0.05247 -0.00307 201 TYR A CG  
1574 C CD1 . TYR A 201 ? 0.80167 0.98898 1.01271 0.09537  -0.05319 -0.00923 201 TYR A CD1 
1575 C CD2 . TYR A 201 ? 0.75026 0.87459 0.94561 0.07997  -0.04970 0.01018  201 TYR A CD2 
1576 C CE1 . TYR A 201 ? 0.86431 1.03647 1.05972 0.10502  -0.05061 -0.00114 201 TYR A CE1 
1577 C CE2 . TYR A 201 ? 0.79450 0.90480 0.97492 0.08757  -0.04698 0.01693  201 TYR A CE2 
1578 C CZ  . TYR A 201 ? 0.86547 0.99743 1.04528 0.10023  -0.04707 0.01185  201 TYR A CZ  
1579 O OH  . TYR A 201 ? 0.86594 0.98088 1.02941 0.10797  -0.04317 0.01888  201 TYR A OH  
1580 N N   . ALA A 202 ? 0.73722 0.94978 0.98406 0.06613  -0.05975 -0.03201 202 ALA A N   
1581 C CA  . ALA A 202 ? 0.72636 0.96801 0.99066 0.05753  -0.05966 -0.04817 202 ALA A CA  
1582 C C   . ALA A 202 ? 0.70088 0.97720 0.96157 0.07519  -0.06736 -0.05639 202 ALA A C   
1583 O O   . ALA A 202 ? 0.66132 0.97957 0.93755 0.07299  -0.06828 -0.07392 202 ALA A O   
1584 C CB  . ALA A 202 ? 0.70655 0.92354 0.97274 0.04487  -0.05670 -0.04465 202 ALA A CB  
1585 N N   . LEU A 203 ? 0.71501 0.97491 0.95408 0.09301  -0.07212 -0.04448 203 LEU A N   
1586 C CA  . LEU A 203 ? 0.70578 0.99465 0.93537 0.11464  -0.07893 -0.04936 203 LEU A CA  
1587 C C   . LEU A 203 ? 0.73220 1.05202 0.96168 0.12914  -0.08078 -0.05478 203 LEU A C   
1588 O O   . LEU A 203 ? 0.74777 1.11426 0.98457 0.13923  -0.08564 -0.06885 203 LEU A O   
1589 C CB  . LEU A 203 ? 0.72611 0.98164 0.92831 0.13022  -0.08048 -0.03350 203 LEU A CB  
1590 C CG  . LEU A 203 ? 0.74576 1.01645 0.92813 0.15669  -0.08575 -0.03281 203 LEU A CG  
1591 C CD1 . LEU A 203 ? 0.66576 0.97062 0.85913 0.15620  -0.09092 -0.04664 203 LEU A CD1 
1592 C CD2 . LEU A 203 ? 0.80357 1.02684 0.95728 0.16607  -0.08245 -0.01498 203 LEU A CD2 
1593 N N   . ARG A 204 ? 0.75567 1.05258 0.97675 0.13103  -0.07700 -0.04443 204 ARG A N   
1594 C CA  . ARG A 204 ? 0.75492 1.08097 0.97751 0.14359  -0.07775 -0.04991 204 ARG A CA  
1595 C C   . ARG A 204 ? 0.71347 1.08428 0.96596 0.12792  -0.07677 -0.07033 204 ARG A C   
1596 O O   . ARG A 204 ? 0.71009 1.12957 0.96991 0.13992  -0.08078 -0.08369 204 ARG A O   
1597 C CB  . ARG A 204 ? 0.81112 1.10097 1.02088 0.14409  -0.07240 -0.03584 204 ARG A CB  
1598 C CG  . ARG A 204 ? 0.84831 1.09785 1.02559 0.16180  -0.07135 -0.01815 204 ARG A CG  
1599 C CD  . ARG A 204 ? 0.89416 1.10684 1.05941 0.15844  -0.06485 -0.00599 204 ARG A CD  
1600 N NE  . ARG A 204 ? 0.97295 1.20892 1.14396 0.16494  -0.06372 -0.01124 204 ARG A NE  
1601 C CZ  . ARG A 204 ? 0.96126 1.20972 1.11604 0.19026  -0.06428 -0.00976 204 ARG A CZ  
1602 N NH1 . ARG A 204 ? 0.99944 1.23899 1.12927 0.21304  -0.06548 -0.00309 204 ARG A NH1 
1603 N NH2 . ARG A 204 ? 0.97186 1.24175 1.13429 0.19392  -0.06278 -0.01492 204 ARG A NH2 
1604 N N   . TYR A 205 ? 0.73653 1.09215 1.00552 0.10131  -0.07051 -0.07372 205 TYR A N   
1605 C CA  . TYR A 205 ? 0.71301 1.10444 1.00876 0.08279  -0.06609 -0.09384 205 TYR A CA  
1606 C C   . TYR A 205 ? 0.64683 1.08326 0.95438 0.08377  -0.07066 -0.11215 205 TYR A C   
1607 O O   . TYR A 205 ? 0.62651 1.11426 0.95074 0.08288  -0.07123 -0.13146 205 TYR A O   
1608 C CB  . TYR A 205 ? 0.73392 1.09126 1.03914 0.05600  -0.05638 -0.09156 205 TYR A CB  
1609 C CG  . TYR A 205 ? 0.82958 1.14953 1.12646 0.05223  -0.05115 -0.07677 205 TYR A CG  
1610 C CD1 . TYR A 205 ? 0.86308 1.18540 1.14926 0.06815  -0.05356 -0.06996 205 TYR A CD1 
1611 C CD2 . TYR A 205 ? 0.88378 1.16628 1.18216 0.03370  -0.04328 -0.06974 205 TYR A CD2 
1612 C CE1 . TYR A 205 ? 0.88192 1.17076 1.16022 0.06366  -0.04855 -0.05743 205 TYR A CE1 
1613 C CE2 . TYR A 205 ? 0.86814 1.11959 1.15829 0.03084  -0.03894 -0.05689 205 TYR A CE2 
1614 C CZ  . TYR A 205 ? 0.85630 1.11159 1.13710 0.04482  -0.04176 -0.05136 205 TYR A CZ  
1615 O OH  . TYR A 205 ? 0.89710 1.12265 1.16963 0.04101  -0.03731 -0.03972 205 TYR A OH  
1616 N N   . ALA A 206 ? 0.69860 1.11900 0.99778 0.08554  -0.07389 -0.10733 206 ALA A N   
1617 C CA  . ALA A 206 ? 0.65280 1.11372 0.96220 0.08520  -0.07801 -0.12480 206 ALA A CA  
1618 C C   . ALA A 206 ? 0.64556 1.15181 0.94656 0.11355  -0.08795 -0.13025 206 ALA A C   
1619 O O   . ALA A 206 ? 0.65103 1.21196 0.96713 0.11318  -0.09121 -0.15137 206 ALA A O   
1620 C CB  . ALA A 206 ? 0.65034 1.07877 0.95106 0.08072  -0.07847 -0.11664 206 ALA A CB  
1621 N N   . MET A 207 ? 0.68638 1.17099 0.96201 0.13871  -0.09199 -0.11204 207 MET A N   
1622 C CA  . MET A 207 ? 0.67602 1.19864 0.93878 0.16993  -0.09984 -0.11438 207 MET A CA  
1623 C C   . MET A 207 ? 0.68867 1.25245 0.96343 0.17546  -0.09962 -0.12508 207 MET A C   
1624 O O   . MET A 207 ? 0.69964 1.30959 0.96923 0.20066  -0.10639 -0.13229 207 MET A O   
1625 C CB  . MET A 207 ? 0.77681 1.25401 1.00420 0.19465  -0.10103 -0.09043 207 MET A CB  
1626 C CG  . MET A 207 ? 0.86164 1.31719 1.07258 0.20090  -0.10379 -0.08308 207 MET A CG  
1627 S SD  . MET A 207 ? 1.01101 1.40955 1.17813 0.22773  -0.10150 -0.05636 207 MET A SD  
1628 C CE  . MET A 207 ? 0.95233 1.34131 1.10771 0.23131  -0.10477 -0.05472 207 MET A CE  
1629 N N   . GLY A 208 ? 0.71171 1.26234 1.00173 0.15390  -0.09188 -0.12672 208 GLY A N   
1630 C CA  . GLY A 208 ? 0.68009 1.26698 0.98013 0.15966  -0.09098 -0.13576 208 GLY A CA  
1631 C C   . GLY A 208 ? 0.77467 1.34425 1.04814 0.18952  -0.09314 -0.11822 208 GLY A C   
1632 O O   . GLY A 208 ? 0.78540 1.39907 1.06039 0.20842  -0.09634 -0.12621 208 GLY A O   
1633 N N   . LEU A 209 ? 0.79340 1.30079 1.04135 0.19500  -0.09077 -0.09524 209 LEU A N   
1634 C CA  . LEU A 209 ? 0.84398 1.32238 1.06699 0.21572  -0.08840 -0.07831 209 LEU A CA  
1635 C C   . LEU A 209 ? 0.93839 1.39761 1.17160 0.19791  -0.08095 -0.07586 209 LEU A C   
1636 O O   . LEU A 209 ? 0.96256 1.40607 1.17914 0.21340  -0.07824 -0.06555 209 LEU A O   
1637 C CB  . LEU A 209 ? 0.86583 1.28377 1.05766 0.22472  -0.08644 -0.05662 209 LEU A CB  
1638 C CG  . LEU A 209 ? 0.92374 1.33740 1.08658 0.25445  -0.09033 -0.04847 209 LEU A CG  
1639 C CD1 . LEU A 209 ? 0.91785 1.36178 1.09229 0.25044  -0.09692 -0.06038 209 LEU A CD1 
1640 C CD2 . LEU A 209 ? 1.02913 1.37300 1.16388 0.25431  -0.08354 -0.02716 209 LEU A CD2 
1641 N N   . GLU A 210 ? 0.92714 1.38328 1.18446 0.16651  -0.07649 -0.08419 210 GLU A N   
1642 C CA  . GLU A 210 ? 0.96796 1.40061 1.23302 0.14825  -0.06858 -0.08067 210 GLU A CA  
1643 C C   . GLU A 210 ? 0.98657 1.43554 1.28075 0.11756  -0.06355 -0.09687 210 GLU A C   
1644 O O   . GLU A 210 ? 0.94826 1.40106 1.25033 0.10680  -0.06474 -0.10338 210 GLU A O   
1645 C CB  . GLU A 210 ? 0.99076 1.35774 1.23405 0.14520  -0.06478 -0.05864 210 GLU A CB  
1646 C CG  . GLU A 210 ? 1.05507 1.39686 1.30108 0.13116  -0.05733 -0.05296 210 GLU A CG  
1647 C CD  . GLU A 210 ? 1.09277 1.37602 1.31632 0.12985  -0.05433 -0.03293 210 GLU A CD  
1648 O OE1 . GLU A 210 ? 1.03484 1.29690 1.24149 0.13876  -0.05726 -0.02411 210 GLU A OE1 
1649 O OE2 . GLU A 210 ? 1.08922 1.34931 1.31203 0.11930  -0.04862 -0.02701 210 GLU A OE2 
1650 N N   . ASP A 211 ? 1.03137 1.48909 1.34008 0.10383  -0.05660 -0.10386 211 ASP A N   
1651 C CA  . ASP A 211 ? 1.01439 1.48341 1.34799 0.07422  -0.04836 -0.11956 211 ASP A CA  
1652 C C   . ASP A 211 ? 1.08442 1.49479 1.41190 0.05538  -0.04043 -0.10509 211 ASP A C   
1653 O O   . ASP A 211 ? 1.07631 1.45292 1.38923 0.06040  -0.03883 -0.08929 211 ASP A O   
1654 C CB  . ASP A 211 ? 1.02923 1.54224 1.38199 0.06879  -0.04348 -0.13697 211 ASP A CB  
1655 N N   . ALA A 212 ? 1.13364 1.53253 1.47071 0.03506  -0.03531 -0.11056 212 ALA A N   
1656 C CA  . ALA A 212 ? 1.17991 1.52704 1.51108 0.01875  -0.02731 -0.09779 212 ALA A CA  
1657 C C   . ALA A 212 ? 1.18617 1.52911 1.52636 0.00304  -0.01584 -0.10231 212 ALA A C   
1658 O O   . ALA A 212 ? 1.13481 1.51421 1.49403 -0.00844 -0.00956 -0.12219 212 ALA A O   
1659 C CB  . ALA A 212 ? 1.17854 1.51483 1.51616 0.00310  -0.02343 -0.10292 212 ALA A CB  
1660 N N   . PRO A 213 ? 1.16878 1.46935 1.49556 0.00153  -0.01225 -0.08531 213 PRO A N   
1661 C CA  . PRO A 213 ? 1.17638 1.46834 1.50891 -0.01302 -0.00050 -0.08805 213 PRO A CA  
1662 C C   . PRO A 213 ? 1.17700 1.44951 1.51703 -0.03657 0.01280  -0.09393 213 PRO A C   
1663 O O   . PRO A 213 ? 1.15772 1.41750 1.49671 -0.04114 0.01264  -0.09313 213 PRO A O   
1664 C CB  . PRO A 213 ? 1.18189 1.43438 1.49406 -0.00391 -0.00275 -0.06659 213 PRO A CB  
1665 C CG  . PRO A 213 ? 1.10339 1.33104 1.40118 0.00508  -0.01101 -0.05295 213 PRO A CG  
1666 C CD  . PRO A 213 ? 1.08741 1.34903 1.39216 0.01409  -0.01882 -0.06365 213 PRO A CD  
1667 N N   . SER A 214 ? 1.20474 1.47479 1.55145 -0.05131 0.02586  -0.10064 214 SER A N   
1668 C CA  . SER A 214 ? 1.16180 1.39418 1.50512 -0.07004 0.04118  -0.09798 214 SER A CA  
1669 C C   . SER A 214 ? 1.24981 1.43962 1.57439 -0.06557 0.04297  -0.07709 214 SER A C   
1670 O O   . SER A 214 ? 1.24505 1.39776 1.56082 -0.07556 0.05397  -0.06981 214 SER A O   
1671 C CB  . SER A 214 ? 1.03054 1.28311 1.39079 -0.09121 0.05774  -0.11956 214 SER A CB  
1672 N N   . GLU A 215 ? 1.25942 1.45408 1.57619 -0.04965 0.03274  -0.06755 215 GLU A N   
1673 C CA  . GLU A 215 ? 1.24772 1.41048 1.54763 -0.04450 0.03314  -0.05023 215 GLU A CA  
1674 C C   . GLU A 215 ? 1.21650 1.36507 1.50095 -0.02735 0.01905  -0.03416 215 GLU A C   
1675 O O   . GLU A 215 ? 1.17437 1.33666 1.45442 -0.01297 0.01018  -0.03174 215 GLU A O   
1676 C CB  . GLU A 215 ? 1.26791 1.45041 1.57291 -0.04367 0.03655  -0.05653 215 GLU A CB  
1677 C CG  . GLU A 215 ? 1.29379 1.51380 1.60336 -0.02660 0.02482  -0.06186 215 GLU A CG  
1678 C CD  . GLU A 215 ? 1.26726 1.53527 1.59749 -0.02907 0.02386  -0.08304 215 GLU A CD  
1679 O OE1 . GLU A 215 ? 1.27663 1.54698 1.61725 -0.04443 0.03081  -0.09340 215 GLU A OE1 
1680 O OE2 . GLU A 215 ? 1.26398 1.56825 1.59897 -0.01469 0.01636  -0.08964 215 GLU A OE2 
1681 N N   . GLU A 216 ? 1.16597 1.28581 1.44098 -0.02892 0.01842  -0.02351 216 GLU A N   
1682 C CA  . GLU A 216 ? 1.13459 1.24506 1.39831 -0.01620 0.00655  -0.01235 216 GLU A CA  
1683 C C   . GLU A 216 ? 1.12291 1.20173 1.36889 -0.01296 0.00558  0.00438  216 GLU A C   
1684 O O   . GLU A 216 ? 1.13224 1.19445 1.37377 -0.01983 0.01378  0.00849  216 GLU A O   
1685 C CB  . GLU A 216 ? 1.13955 1.24649 1.40708 -0.01973 0.00540  -0.01424 216 GLU A CB  
1686 C CG  . GLU A 216 ? 1.13605 1.27545 1.42038 -0.02358 0.00579  -0.03161 216 GLU A CG  
1687 C CD  . GLU A 216 ? 1.20818 1.34974 1.50438 -0.04159 0.02035  -0.04402 216 GLU A CD  
1688 O OE1 . GLU A 216 ? 1.22869 1.34239 1.51745 -0.04905 0.03026  -0.03689 216 GLU A OE1 
1689 O OE2 . GLU A 216 ? 1.27821 1.44881 1.58991 -0.04851 0.02285  -0.06137 216 GLU A OE2 
1690 N N   . GLU A 217 ? 0.94482 1.01614 1.17989 -0.00264 -0.00392 0.01326  217 GLU A N   
1691 C CA  . GLU A 217 ? 0.95245 0.99681 1.17355 -0.00245 -0.00507 0.02670  217 GLU A CA  
1692 C C   . GLU A 217 ? 1.02396 1.05433 1.24783 -0.01171 0.00243  0.02790  217 GLU A C   
1693 O O   . GLU A 217 ? 0.99054 1.02697 1.22369 -0.01556 0.00401  0.02125  217 GLU A O   
1694 C CB  . GLU A 217 ? 0.90960 0.95037 1.12265 0.00600  -0.01427 0.03220  217 GLU A CB  
1695 C CG  . GLU A 217 ? 0.88188 0.90105 1.08344 0.00469  -0.01524 0.04353  217 GLU A CG  
1696 C CD  . GLU A 217 ? 0.97612 0.98533 1.16409 0.00720  -0.01619 0.05047  217 GLU A CD  
1697 O OE1 . GLU A 217 ? 0.99155 1.00495 1.17397 0.01365  -0.01926 0.04914  217 GLU A OE1 
1698 O OE2 . GLU A 217 ? 1.02372 1.02090 1.20524 0.00348  -0.01302 0.05683  217 GLU A OE2 
1699 N N   . CYS A 218 ? 1.08260 1.09341 1.29673 -0.01448 0.00801  0.03630  218 CYS A N   
1700 C CA  . CYS A 218 ? 1.08633 1.07986 1.29900 -0.02072 0.01734  0.03870  218 CYS A CA  
1701 C C   . CYS A 218 ? 1.01525 1.00110 1.22506 -0.01703 0.01275  0.04402  218 CYS A C   
1702 O O   . CYS A 218 ? 1.03591 1.00854 1.24547 -0.02109 0.02108  0.04432  218 CYS A O   
1703 C CB  . CYS A 218 ? 1.14182 1.11630 1.34114 -0.02105 0.02385  0.04796  218 CYS A CB  
1704 S SG  . CYS A 218 ? 1.60208 1.57107 1.78518 -0.01156 0.01332  0.06091  218 CYS A SG  
1705 N N   . ASP A 219 ? 1.01461 1.00727 1.22154 -0.00968 0.00120  0.04756  219 ASP A N   
1706 C CA  . ASP A 219 ? 0.99398 0.98103 1.19738 -0.00564 -0.00400 0.05310  219 ASP A CA  
1707 C C   . ASP A 219 ? 0.92653 0.92170 1.14094 -0.00763 -0.00438 0.04511  219 ASP A C   
1708 O O   . ASP A 219 ? 0.94967 0.93457 1.16244 -0.00747 -0.00232 0.04861  219 ASP A O   
1709 C CB  . ASP A 219 ? 0.95000 0.94008 1.14493 0.00083  -0.01399 0.05859  219 ASP A CB  
1710 N N   . PRO A 220 ? 0.91050 0.92542 1.13529 -0.00821 -0.00722 0.03434  220 PRO A N   
1711 C CA  . PRO A 220 ? 0.88413 0.90926 1.11989 -0.01149 -0.00630 0.02477  220 PRO A CA  
1712 C C   . PRO A 220 ? 0.93216 0.94369 1.17122 -0.02058 0.00558  0.02200  220 PRO A C   
1713 O O   . PRO A 220 ? 0.99758 1.00149 1.23621 -0.02022 0.00585  0.02345  220 PRO A O   
1714 C CB  . PRO A 220 ? 0.90009 0.95144 1.14641 -0.01194 -0.00764 0.01217  220 PRO A CB  
1715 C CG  . PRO A 220 ? 0.85331 0.90647 1.09057 -0.00302 -0.01437 0.01842  220 PRO A CG  
1716 C CD  . PRO A 220 ? 0.91840 0.94868 1.14381 -0.00386 -0.01186 0.03054  220 PRO A CD  
1717 N N   . LEU A 221 ? 0.92527 0.93186 1.16636 -0.02878 0.01678  0.01770  221 LEU A N   
1718 C CA  . LEU A 221 ? 0.86454 0.84889 1.10274 -0.03704 0.03177  0.01733  221 LEU A CA  
1719 C C   . LEU A 221 ? 0.91466 0.90359 1.16268 -0.04462 0.03709  0.00563  221 LEU A C   
1720 O O   . LEU A 221 ? 0.95603 0.92882 1.19843 -0.04211 0.03878  0.01107  221 LEU A O   
1721 C CB  . LEU A 221 ? 0.87007 0.82802 1.09159 -0.02893 0.03229  0.03406  221 LEU A CB  
1722 N N   . MET B 1   ? 1.01259 0.87257 1.29243 -0.29026 0.28070  -0.27435 1   MET B N   
1723 C CA  . MET B 1   ? 1.03249 0.89575 1.30865 -0.25667 0.25211  -0.24347 1   MET B CA  
1724 C C   . MET B 1   ? 1.02773 0.95487 1.32363 -0.24698 0.22055  -0.24924 1   MET B C   
1725 O O   . MET B 1   ? 0.98129 0.96468 1.29718 -0.25437 0.20781  -0.26623 1   MET B O   
1726 C CB  . MET B 1   ? 1.02314 0.88141 1.29625 -0.24058 0.24176  -0.22128 1   MET B CB  
1727 C CG  . MET B 1   ? 1.02440 0.88472 1.29291 -0.20841 0.21474  -0.19138 1   MET B CG  
1728 S SD  . MET B 1   ? 1.11410 0.99481 1.38723 -0.18923 0.19192  -0.17054 1   MET B SD  
1729 C CE  . MET B 1   ? 0.99503 0.95515 1.29669 -0.19624 0.16885  -0.19322 1   MET B CE  
1730 N N   . PHE B 2   ? 0.99190 0.90980 1.28059 -0.22798 0.20781  -0.23335 2   PHE B N   
1731 C CA  . PHE B 2   ? 0.92809 0.89724 1.23003 -0.21536 0.17925  -0.23465 2   PHE B CA  
1732 C C   . PHE B 2   ? 0.90098 0.86790 1.19754 -0.18529 0.15534  -0.20366 2   PHE B C   
1733 O O   . PHE B 2   ? 0.93840 0.86004 1.21893 -0.17211 0.16087  -0.18032 2   PHE B O   
1734 C CB  . PHE B 2   ? 0.91150 0.87793 1.21082 -0.22017 0.18366  -0.24546 2   PHE B CB  
1735 C CG  . PHE B 2   ? 0.89012 0.88144 1.20034 -0.24929 0.19894  -0.28110 2   PHE B CG  
1736 C CD1 . PHE B 2   ? 0.90777 0.92493 1.23055 -0.26956 0.20762  -0.30219 2   PHE B CD1 
1737 C CD2 . PHE B 2   ? 0.89952 0.89580 1.20926 -0.25635 0.20264  -0.29518 2   PHE B CD2 
1738 C CE1 . PHE B 2   ? 0.93626 0.98245 1.27073 -0.29800 0.22169  -0.33777 2   PHE B CE1 
1739 C CE2 . PHE B 2   ? 0.90695 0.93151 1.22764 -0.28449 0.21626  -0.33053 2   PHE B CE2 
1740 C CZ  . PHE B 2   ? 0.93381 0.98451 1.26728 -0.30576 0.22588  -0.35241 2   PHE B CZ  
1741 N N   . ASP B 3   ? 0.90089 0.91814 1.20993 -0.17432 0.12954  -0.20449 3   ASP B N   
1742 C CA  . ASP B 3   ? 0.88466 0.90446 1.18869 -0.14836 0.10713  -0.18048 3   ASP B CA  
1743 C C   . ASP B 3   ? 0.88373 0.90875 1.18560 -0.14365 0.10151  -0.18340 3   ASP B C   
1744 O O   . ASP B 3   ? 0.87372 0.91144 1.18062 -0.15966 0.11072  -0.20590 3   ASP B O   
1745 C CB  . ASP B 3   ? 0.86050 0.92584 1.17499 -0.13765 0.08455  -0.17860 3   ASP B CB  
1746 C CG  . ASP B 3   ? 0.87414 0.92926 1.18794 -0.13622 0.08662  -0.16851 3   ASP B CG  
1747 O OD1 . ASP B 3   ? 0.91305 0.92248 1.21444 -0.13384 0.09871  -0.15279 3   ASP B OD1 
1748 O OD2 . ASP B 3   ? 0.85174 0.94514 1.17628 -0.13568 0.07585  -0.17559 3   ASP B OD2 
1749 N N   . PHE B 4   ? 0.78786 0.80415 1.08216 -0.12226 0.08671  -0.16134 4   PHE B N   
1750 C CA  . PHE B 4   ? 0.71077 0.73024 1.00193 -0.11601 0.08086  -0.16170 4   PHE B CA  
1751 C C   . PHE B 4   ? 0.68008 0.72448 0.97138 -0.09559 0.05636  -0.14802 4   PHE B C   
1752 O O   . PHE B 4   ? 0.71138 0.76011 1.00226 -0.08468 0.04573  -0.13413 4   PHE B O   
1753 C CB  . PHE B 4   ? 0.73262 0.70244 1.00980 -0.11220 0.09512  -0.14885 4   PHE B CB  
1754 C CG  . PHE B 4   ? 0.73192 0.67705 0.99949 -0.09254 0.08855  -0.12097 4   PHE B CG  
1755 C CD1 . PHE B 4   ? 0.75235 0.67004 1.01358 -0.09186 0.09865  -0.11018 4   PHE B CD1 
1756 C CD2 . PHE B 4   ? 0.72237 0.67142 0.98635 -0.07535 0.07380  -0.10652 4   PHE B CD2 
1757 C CE1 . PHE B 4   ? 0.71457 0.61376 0.96697 -0.07365 0.09247  -0.08603 4   PHE B CE1 
1758 C CE2 . PHE B 4   ? 0.71448 0.64497 0.97073 -0.05896 0.06857  -0.08339 4   PHE B CE2 
1759 C CZ  . PHE B 4   ? 0.69766 0.60501 0.94847 -0.05790 0.07739  -0.07350 4   PHE B CZ  
1760 N N   . ILE B 5   ? 0.66819 0.72674 0.95849 -0.09112 0.04903  -0.15260 5   ILE B N   
1761 C CA  . ILE B 5   ? 0.66776 0.74580 0.95494 -0.07255 0.02874  -0.14107 5   ILE B CA  
1762 C C   . ILE B 5   ? 0.64661 0.70164 0.92486 -0.06518 0.03007  -0.13163 5   ILE B C   
1763 O O   . ILE B 5   ? 0.63263 0.67387 0.90984 -0.07560 0.04321  -0.14214 5   ILE B O   
1764 C CB  . ILE B 5   ? 0.66335 0.79140 0.95769 -0.07282 0.01682  -0.15881 5   ILE B CB  
1765 C CG1 . ILE B 5   ? 0.60491 0.74824 0.89189 -0.05180 -0.00230 -0.14518 5   ILE B CG1 
1766 C CG2 . ILE B 5   ? 0.66329 0.80364 0.96111 -0.08625 0.02499  -0.18078 5   ILE B CG2 
1767 C CD1 . ILE B 5   ? 0.65592 0.84770 0.94688 -0.04759 -0.01405 -0.15975 5   ILE B CD1 
1768 N N   . ILE B 6   ? 0.61151 0.66089 0.88295 -0.04820 0.01813  -0.11241 6   ILE B N   
1769 C CA  . ILE B 6   ? 0.63943 0.67118 0.90323 -0.04032 0.01826  -0.10339 6   ILE B CA  
1770 C C   . ILE B 6   ? 0.64974 0.70405 0.90931 -0.02701 0.00146  -0.09862 6   ILE B C   
1771 O O   . ILE B 6   ? 0.68232 0.75512 0.94178 -0.02002 -0.00965 -0.09489 6   ILE B O   
1772 C CB  . ILE B 6   ? 0.65404 0.65043 0.91157 -0.03281 0.02414  -0.08342 6   ILE B CB  
1773 C CG1 . ILE B 6   ? 0.65158 0.65287 0.90793 -0.02194 0.01247  -0.06774 6   ILE B CG1 
1774 C CG2 . ILE B 6   ? 0.65010 0.61870 0.90700 -0.04347 0.04303  -0.08691 6   ILE B CG2 
1775 C CD1 . ILE B 6   ? 0.61751 0.59415 0.86771 -0.01179 0.01428  -0.04856 6   ILE B CD1 
1776 N N   . ASP B 7   ? 0.64794 0.69854 0.90224 -0.02320 0.00103  -0.09885 7   ASP B N   
1777 C CA  . ASP B 7   ? 0.63600 0.69929 0.88246 -0.00992 -0.01179 -0.09221 7   ASP B CA  
1778 C C   . ASP B 7   ? 0.63772 0.67848 0.87824 -0.00529 -0.00770 -0.08308 7   ASP B C   
1779 O O   . ASP B 7   ? 0.67722 0.70730 0.91898 -0.01268 0.00247  -0.09119 7   ASP B O   
1780 C CB  . ASP B 7   ? 0.65062 0.74731 0.89656 -0.01027 -0.01839 -0.10899 7   ASP B CB  
1781 C CG  . ASP B 7   ? 0.73022 0.83940 0.96425 0.00614  -0.03152 -0.10060 7   ASP B CG  
1782 O OD1 . ASP B 7   ? 0.73098 0.82282 0.95841 0.01515  -0.03474 -0.08304 7   ASP B OD1 
1783 O OD2 . ASP B 7   ? 0.83258 0.96852 1.06242 0.01012  -0.03760 -0.11202 7   ASP B OD2 
1784 N N   . PHE B 8   ? 0.64404 0.67781 0.87800 0.00612  -0.01438 -0.06738 8   PHE B N   
1785 C CA  . PHE B 8   ? 0.62104 0.64136 0.84936 0.01156  -0.01246 -0.06041 8   PHE B CA  
1786 C C   . PHE B 8   ? 0.67228 0.70741 0.89112 0.01928  -0.02126 -0.06192 8   PHE B C   
1787 O O   . PHE B 8   ? 0.71328 0.76406 0.92703 0.02493  -0.03001 -0.06163 8   PHE B O   
1788 C CB  . PHE B 8   ? 0.62944 0.63334 0.85658 0.01817  -0.01232 -0.04309 8   PHE B CB  
1789 C CG  . PHE B 8   ? 0.60663 0.59028 0.83836 0.01534  -0.00165 -0.03867 8   PHE B CG  
1790 C CD1 . PHE B 8   ? 0.60064 0.56899 0.83095 0.01659  0.00700  -0.03768 8   PHE B CD1 
1791 C CD2 . PHE B 8   ? 0.66390 0.64230 0.89925 0.01350  0.00021  -0.03403 8   PHE B CD2 
1792 C CE1 . PHE B 8   ? 0.59689 0.54432 0.82786 0.01748  0.01784  -0.03196 8   PHE B CE1 
1793 C CE2 . PHE B 8   ? 0.63904 0.59605 0.87492 0.01364  0.01111  -0.02829 8   PHE B CE2 
1794 C CZ  . PHE B 8   ? 0.63928 0.58043 0.87218 0.01653  0.02006  -0.02692 8   PHE B CZ  
1795 N N   . GLU B 9   ? 0.67585 0.70397 0.89043 0.02074  -0.01790 -0.06287 9   GLU B N   
1796 C CA  . GLU B 9   ? 0.70219 0.73490 0.90491 0.02976  -0.02384 -0.05915 9   GLU B CA  
1797 C C   . GLU B 9   ? 0.68918 0.70310 0.89060 0.03321  -0.01983 -0.04658 9   GLU B C   
1798 O O   . GLU B 9   ? 0.64479 0.64620 0.85192 0.02969  -0.01161 -0.04685 9   GLU B O   
1799 C CB  . GLU B 9   ? 0.72392 0.76899 0.92207 0.02855  -0.02360 -0.07299 9   GLU B CB  
1800 C CG  . GLU B 9   ? 0.78695 0.85915 0.98607 0.02662  -0.02903 -0.08722 9   GLU B CG  
1801 C CD  . GLU B 9   ? 0.91404 1.00311 1.10834 0.02570  -0.02935 -0.10231 9   GLU B CD  
1802 O OE1 . GLU B 9   ? 0.97399 1.04971 1.16515 0.02476  -0.02389 -0.10197 9   GLU B OE1 
1803 O OE2 . GLU B 9   ? 0.97415 1.09227 1.16771 0.02650  -0.03524 -0.11510 9   GLU B OE2 
1804 N N   . THR B 10  ? 0.68473 0.69691 0.87823 0.04003  -0.02451 -0.03617 10  THR B N   
1805 C CA  . THR B 10  ? 0.69062 0.69061 0.88590 0.04171  -0.02103 -0.02512 10  THR B CA  
1806 C C   . THR B 10  ? 0.68272 0.68046 0.86601 0.04658  -0.02150 -0.02183 10  THR B C   
1807 O O   . THR B 10  ? 0.75332 0.75584 0.92383 0.05080  -0.02524 -0.02478 10  THR B O   
1808 C CB  . THR B 10  ? 0.68630 0.68490 0.88546 0.04196  -0.02349 -0.01583 10  THR B CB  
1809 O OG1 . THR B 10  ? 0.65692 0.66020 0.84540 0.04566  -0.02946 -0.01330 10  THR B OG1 
1810 C CG2 . THR B 10  ? 0.64668 0.64571 0.85580 0.03719  -0.02201 -0.01902 10  THR B CG2 
1811 N N   . MET B 11  ? 0.67609 0.66688 0.86280 0.04668  -0.01675 -0.01591 11  MET B N   
1812 C CA  . MET B 11  ? 0.69566 0.68305 0.87287 0.04914  -0.01469 -0.01275 11  MET B CA  
1813 C C   . MET B 11  ? 0.69805 0.68462 0.87516 0.04839  -0.01463 -0.00417 11  MET B C   
1814 O O   . MET B 11  ? 0.70600 0.69091 0.88031 0.04770  -0.01047 -0.00160 11  MET B O   
1815 C CB  . MET B 11  ? 0.70103 0.68510 0.88320 0.04889  -0.00832 -0.01529 11  MET B CB  
1816 C CG  . MET B 11  ? 0.74834 0.72934 0.92002 0.05061  -0.00503 -0.01498 11  MET B CG  
1817 S SD  . MET B 11  ? 0.93859 0.91889 1.09035 0.05450  -0.00816 -0.02122 11  MET B SD  
1818 C CE  . MET B 11  ? 0.75979 0.74354 0.91797 0.05273  -0.00617 -0.03243 11  MET B CE  
1819 N N   . GLY B 12  ? 0.71427 0.70334 0.89504 0.04739  -0.01850 -0.00090 12  GLY B N   
1820 C CA  . GLY B 12  ? 0.66591 0.65603 0.84772 0.04538  -0.01840 0.00573  12  GLY B CA  
1821 C C   . GLY B 12  ? 0.71006 0.70139 0.89161 0.04526  -0.02350 0.00742  12  GLY B C   
1822 O O   . GLY B 12  ? 0.67568 0.66871 0.85631 0.04687  -0.02690 0.00299  12  GLY B O   
1823 N N   . SER B 13  ? 0.71727 0.71005 0.90028 0.04276  -0.02371 0.01277  13  SER B N   
1824 C CA  . SER B 13  ? 0.69603 0.68818 0.87554 0.04276  -0.02784 0.01483  13  SER B CA  
1825 C C   . SER B 13  ? 0.72903 0.72721 0.92115 0.04045  -0.02930 0.01892  13  SER B C   
1826 O O   . SER B 13  ? 0.79402 0.79288 0.98837 0.04079  -0.03277 0.01919  13  SER B O   
1827 C CB  . SER B 13  ? 0.72975 0.71323 0.89182 0.04256  -0.02570 0.01697  13  SER B CB  
1828 O OG  . SER B 13  ? 0.72219 0.70577 0.88469 0.03690  -0.02035 0.01891  13  SER B OG  
1829 N N   . GLY B 14  ? 0.71621 0.72075 0.91630 0.03894  -0.02668 0.02177  14  GLY B N   
1830 C CA  . GLY B 14  ? 0.69962 0.71137 0.90898 0.03877  -0.02832 0.02615  14  GLY B CA  
1831 C C   . GLY B 14  ? 0.69484 0.70442 0.91274 0.04233  -0.02839 0.02673  14  GLY B C   
1832 O O   . GLY B 14  ? 0.68176 0.68469 0.89855 0.04263  -0.02790 0.02214  14  GLY B O   
1833 N N   . GLU B 15  ? 0.79033 0.80512 1.01542 0.04497  -0.02797 0.03168  15  GLU B N   
1834 C CA  . GLU B 15  ? 0.76259 0.76991 0.99262 0.04920  -0.02441 0.03266  15  GLU B CA  
1835 C C   . GLU B 15  ? 0.73683 0.74275 0.96952 0.05440  -0.01895 0.03236  15  GLU B C   
1836 O O   . GLU B 15  ? 0.75237 0.74630 0.98587 0.05699  -0.01345 0.03135  15  GLU B O   
1837 C CB  . GLU B 15  ? 0.72886 0.73856 0.96204 0.05279  -0.02450 0.03919  15  GLU B CB  
1838 C CG  . GLU B 15  ? 0.72166 0.74547 0.95835 0.05952  -0.02386 0.04450  15  GLU B CG  
1839 C CD  . GLU B 15  ? 0.73913 0.76805 0.97664 0.06406  -0.02505 0.05089  15  GLU B CD  
1840 O OE1 . GLU B 15  ? 0.74147 0.76060 0.97685 0.06075  -0.02587 0.05136  15  GLU B OE1 
1841 O OE2 . GLU B 15  ? 0.76102 0.80588 1.00112 0.07144  -0.02522 0.05503  15  GLU B OE2 
1842 N N   . LYS B 16  ? 0.63324 0.65033 0.86668 0.05541  -0.01903 0.03254  16  LYS B N   
1843 C CA  . LYS B 16  ? 0.65001 0.66765 0.88587 0.06080  -0.01391 0.03185  16  LYS B CA  
1844 C C   . LYS B 16  ? 0.64210 0.65155 0.87332 0.05665  -0.01238 0.02500  16  LYS B C   
1845 O O   . LYS B 16  ? 0.61259 0.62403 0.84489 0.05962  -0.00847 0.02356  16  LYS B O   
1846 C CB  . LYS B 16  ? 0.64283 0.68122 0.88335 0.06412  -0.01418 0.03421  16  LYS B CB  
1847 C CG  . LYS B 16  ? 0.58554 0.63779 0.83034 0.06998  -0.01621 0.04027  16  LYS B CG  
1848 C CD  . LYS B 16  ? 0.63465 0.67468 0.87877 0.08062  -0.01196 0.04598  16  LYS B CD  
1849 C CE  . LYS B 16  ? 0.66866 0.70982 0.91403 0.09237  -0.00561 0.04806  16  LYS B CE  
1850 N NZ  . LYS B 16  ? 0.65728 0.68045 0.89764 0.10342  0.00105  0.05446  16  LYS B NZ  
1851 N N   . ALA B 17  ? 0.62578 0.62792 0.85139 0.05105  -0.01542 0.02063  17  ALA B N   
1852 C CA  . ALA B 17  ? 0.61499 0.61160 0.83447 0.04869  -0.01466 0.01379  17  ALA B CA  
1853 C C   . ALA B 17  ? 0.62463 0.61338 0.84686 0.05121  -0.00829 0.01024  17  ALA B C   
1854 O O   . ALA B 17  ? 0.58832 0.56846 0.81382 0.05187  -0.00436 0.00964  17  ALA B O   
1855 C CB  . ALA B 17  ? 0.62650 0.62034 0.84038 0.04515  -0.01907 0.00931  17  ALA B CB  
1856 N N   . ALA B 18  ? 0.63802 0.62748 0.85743 0.05204  -0.00579 0.00747  18  ALA B N   
1857 C CA  . ALA B 18  ? 0.62594 0.60632 0.84511 0.05289  0.00025  0.00185  18  ALA B CA  
1858 C C   . ALA B 18  ? 0.64482 0.62052 0.86030 0.04740  -0.00115 -0.00682 18  ALA B C   
1859 O O   . ALA B 18  ? 0.63368 0.61554 0.84329 0.04505  -0.00749 -0.00945 18  ALA B O   
1860 C CB  . ALA B 18  ? 0.62237 0.60559 0.83799 0.05415  0.00249  -0.00009 18  ALA B CB  
1861 N N   . VAL B 19  ? 0.65104 0.61636 0.86913 0.04565  0.00577  -0.01190 19  VAL B N   
1862 C CA  . VAL B 19  ? 0.66340 0.62791 0.88090 0.03847  0.00580  -0.02204 19  VAL B CA  
1863 C C   . VAL B 19  ? 0.68847 0.64995 0.90265 0.03495  0.01080  -0.03327 19  VAL B C   
1864 O O   . VAL B 19  ? 0.69898 0.64790 0.91358 0.03657  0.01998  -0.03349 19  VAL B O   
1865 C CB  . VAL B 19  ? 0.60325 0.55727 0.82560 0.03593  0.01171  -0.02102 19  VAL B CB  
1866 C CG1 . VAL B 19  ? 0.62102 0.58190 0.84556 0.03810  0.00478  -0.01235 19  VAL B CG1 
1867 C CG2 . VAL B 19  ? 0.61427 0.55152 0.83707 0.04166  0.02250  -0.01536 19  VAL B CG2 
1868 N N   . ILE B 20  ? 0.68291 0.65691 0.89274 0.03125  0.00490  -0.04268 20  ILE B N   
1869 C CA  . ILE B 20  ? 0.67358 0.64953 0.87997 0.02694  0.00851  -0.05570 20  ILE B CA  
1870 C C   . ILE B 20  ? 0.69751 0.66726 0.90920 0.01715  0.01725  -0.06709 20  ILE B C   
1871 O O   . ILE B 20  ? 0.77229 0.72615 0.98412 0.01415  0.02866  -0.07112 20  ILE B O   
1872 C CB  . ILE B 20  ? 0.70661 0.70157 0.90466 0.02879  -0.00132 -0.06167 20  ILE B CB  
1873 C CG1 . ILE B 20  ? 0.69450 0.68916 0.88388 0.03737  -0.00629 -0.05079 20  ILE B CG1 
1874 C CG2 . ILE B 20  ? 0.75945 0.76145 0.95396 0.02428  0.00144  -0.07684 20  ILE B CG2 
1875 C CD1 . ILE B 20  ? 0.76677 0.77500 0.94466 0.04232  -0.01527 -0.05210 20  ILE B CD1 
1876 N N   . ASP B 21  ? 0.70982 0.69080 0.92518 0.01160  0.01352  -0.07293 21  ASP B N   
1877 C CA  . ASP B 21  ? 0.66562 0.64134 0.88623 -0.00015 0.02324  -0.08515 21  ASP B CA  
1878 C C   . ASP B 21  ? 0.68099 0.66015 0.90706 -0.00247 0.02059  -0.08173 21  ASP B C   
1879 O O   . ASP B 21  ? 0.62608 0.61267 0.85169 0.00517  0.01061  -0.07047 21  ASP B O   
1880 C CB  . ASP B 21  ? 0.66921 0.66450 0.88951 -0.00934 0.02287  -0.10543 21  ASP B CB  
1881 C CG  . ASP B 21  ? 0.79412 0.82119 1.01360 -0.00613 0.00830  -0.10977 21  ASP B CG  
1882 O OD1 . ASP B 21  ? 0.80372 0.83388 1.01920 0.00469  -0.00141 -0.09611 21  ASP B OD1 
1883 O OD2 . ASP B 21  ? 0.85079 0.90022 1.07349 -0.01453 0.00753  -0.12736 21  ASP B OD2 
1884 N N   . LEU B 22  ? 0.70191 0.67540 0.93242 -0.01449 0.03084  -0.09321 22  LEU B N   
1885 C CA  . LEU B 22  ? 0.62120 0.59555 0.85704 -0.01969 0.03198  -0.09321 22  LEU B CA  
1886 C C   . LEU B 22  ? 0.64689 0.63265 0.88774 -0.03604 0.03935  -0.11509 22  LEU B C   
1887 O O   . LEU B 22  ? 0.69100 0.66095 0.93034 -0.04582 0.05387  -0.12579 22  LEU B O   
1888 C CB  . LEU B 22  ? 0.64088 0.58374 0.87487 -0.01636 0.04296  -0.07978 22  LEU B CB  
1889 C CG  . LEU B 22  ? 0.61248 0.54663 0.84949 -0.02285 0.04954  -0.07979 22  LEU B CG  
1890 C CD1 . LEU B 22  ? 0.60444 0.56303 0.84659 -0.02094 0.03533  -0.07718 22  LEU B CD1 
1891 C CD2 . LEU B 22  ? 0.61248 0.51579 0.84356 -0.01400 0.05899  -0.06354 22  LEU B CD2 
1892 N N   . ALA B 23  ? 0.62133 0.63480 0.86787 -0.03934 0.03048  -0.12253 23  ALA B N   
1893 C CA  . ALA B 23  ? 0.65846 0.68847 0.91224 -0.05600 0.03734  -0.14444 23  ALA B CA  
1894 C C   . ALA B 23  ? 0.66642 0.68875 0.92538 -0.06178 0.04256  -0.14178 23  ALA B C   
1895 O O   . ALA B 23  ? 0.63719 0.66239 0.89615 -0.05134 0.03241  -0.12704 23  ALA B O   
1896 C CB  . ALA B 23  ? 0.67682 0.75184 0.93332 -0.05453 0.02311  -0.15806 23  ALA B CB  
1897 N N   . VAL B 24  ? 0.64403 0.65451 0.90620 -0.07918 0.05985  -0.15644 24  VAL B N   
1898 C CA  . VAL B 24  ? 0.64308 0.64604 0.90947 -0.08717 0.06736  -0.15690 24  VAL B CA  
1899 C C   . VAL B 24  ? 0.67306 0.69443 0.94766 -0.10949 0.07862  -0.18479 24  VAL B C   
1900 O O   . VAL B 24  ? 0.78844 0.80603 1.06179 -0.12141 0.09000  -0.20086 24  VAL B O   
1901 C CB  . VAL B 24  ? 0.69824 0.65215 0.95544 -0.08363 0.08247  -0.14014 24  VAL B CB  
1902 C CG1 . VAL B 24  ? 0.72751 0.64921 0.97687 -0.09221 0.10293  -0.14756 24  VAL B CG1 
1903 C CG2 . VAL B 24  ? 0.73346 0.67823 0.99296 -0.09075 0.09029  -0.13936 24  VAL B CG2 
1904 N N   . ILE B 25  ? 0.66462 0.70951 0.94814 -0.11567 0.07517  -0.19208 25  ILE B N   
1905 C CA  . ILE B 25  ? 0.69221 0.75810 0.98548 -0.13859 0.08682  -0.21978 25  ILE B CA  
1906 C C   . ILE B 25  ? 0.70706 0.76193 1.00366 -0.14507 0.09460  -0.21669 25  ILE B C   
1907 O O   . ILE B 25  ? 0.67335 0.73392 0.97044 -0.13068 0.08101  -0.19969 25  ILE B O   
1908 C CB  . ILE B 25  ? 0.71541 0.84301 1.01945 -0.13924 0.07037  -0.23884 25  ILE B CB  
1909 C CG1 . ILE B 25  ? 0.70372 0.84446 1.00256 -0.13012 0.06075  -0.24042 25  ILE B CG1 
1910 C CG2 . ILE B 25  ? 0.69350 0.84799 1.00971 -0.16530 0.08370  -0.27066 25  ILE B CG2 
1911 C CD1 . ILE B 25  ? 0.69695 0.89685 1.00138 -0.12166 0.04072  -0.25175 25  ILE B CD1 
1912 N N   . ALA B 26  ? 0.71522 0.75435 1.01335 -0.16766 0.11743  -0.23427 26  ALA B N   
1913 C CA  . ALA B 26  ? 0.72206 0.74822 1.02221 -0.17703 0.12874  -0.23439 26  ALA B CA  
1914 C C   . ALA B 26  ? 0.73187 0.80851 1.04880 -0.19575 0.12842  -0.26324 26  ALA B C   
1915 O O   . ALA B 26  ? 0.81607 0.89895 1.13736 -0.21906 0.14535  -0.28961 26  ALA B O   
1916 C CB  . ALA B 26  ? 0.79871 0.76485 1.08510 -0.18851 0.15804  -0.23239 26  ALA B CB  
1917 N N   . PHE B 27  ? 0.73390 0.84603 1.05986 -0.18635 0.11087  -0.25917 27  PHE B N   
1918 C CA  . PHE B 27  ? 0.71109 0.87995 1.05393 -0.19930 0.10663  -0.28519 27  PHE B CA  
1919 C C   . PHE B 27  ? 0.81138 0.97192 1.15902 -0.21139 0.11878  -0.28808 27  PHE B C   
1920 O O   . PHE B 27  ? 0.81681 0.93280 1.15403 -0.20384 0.12450  -0.26567 27  PHE B O   
1921 C CB  . PHE B 27  ? 0.71247 0.93191 1.06060 -0.17727 0.07750  -0.27955 27  PHE B CB  
1922 C CG  . PHE B 27  ? 0.68044 0.88488 1.02208 -0.15447 0.06316  -0.25001 27  PHE B CG  
1923 C CD1 . PHE B 27  ? 0.68462 0.85187 1.01249 -0.13638 0.05716  -0.22336 27  PHE B CD1 
1924 C CD2 . PHE B 27  ? 0.68427 0.91489 1.03395 -0.15165 0.05583  -0.25051 27  PHE B CD2 
1925 C CE1 . PHE B 27  ? 0.71264 0.86847 1.03478 -0.11767 0.04498  -0.19879 27  PHE B CE1 
1926 C CE2 . PHE B 27  ? 0.68431 0.90082 1.02721 -0.13195 0.04364  -0.22484 27  PHE B CE2 
1927 C CZ  . PHE B 27  ? 0.68419 0.86360 1.01331 -0.11559 0.03830  -0.19946 27  PHE B CZ  
1928 N N   . ASP B 28  ? 0.79241 0.99941 1.15606 -0.23011 0.12263  -0.31691 28  ASP B N   
1929 C CA  . ASP B 28  ? 0.76898 0.97415 1.13927 -0.24585 0.13642  -0.32539 28  ASP B CA  
1930 C C   . ASP B 28  ? 0.76219 1.00832 1.14147 -0.22859 0.11401  -0.31684 28  ASP B C   
1931 O O   . ASP B 28  ? 0.73333 1.04279 1.12610 -0.22571 0.09857  -0.33368 28  ASP B O   
1932 C CB  . ASP B 28  ? 0.82422 1.05856 1.20772 -0.27859 0.15562  -0.36443 28  ASP B CB  
1933 C CG  . ASP B 28  ? 0.90433 1.13391 1.29437 -0.29938 0.17455  -0.37660 28  ASP B CG  
1934 O OD1 . ASP B 28  ? 0.94029 1.15105 1.32611 -0.28670 0.16989  -0.35510 28  ASP B OD1 
1935 O OD2 . ASP B 28  ? 0.82826 1.07273 1.22729 -0.33003 0.19555  -0.40919 28  ASP B OD2 
1936 N N   . PRO B 29  ? 0.84302 1.05677 1.21451 -0.21652 0.11231  -0.29209 29  PRO B N   
1937 C CA  . PRO B 29  ? 0.79876 1.04588 1.17539 -0.19634 0.08971  -0.28013 29  PRO B CA  
1938 C C   . PRO B 29  ? 0.82803 1.12512 1.22214 -0.20846 0.09032  -0.30244 29  PRO B C   
1939 O O   . PRO B 29  ? 0.84240 1.16905 1.24025 -0.19099 0.07222  -0.29380 29  PRO B O   
1940 C CB  . PRO B 29  ? 0.73211 0.92452 1.09403 -0.18337 0.09153  -0.24885 29  PRO B CB  
1941 C CG  . PRO B 29  ? 0.80077 0.94143 1.15417 -0.20243 0.11939  -0.25171 29  PRO B CG  
1942 C CD  . PRO B 29  ? 0.81901 0.96272 1.17388 -0.21757 0.13019  -0.27198 29  PRO B CD  
1943 N N   . ASN B 30  ? 0.85015 1.15871 1.25468 -0.23761 0.11099  -0.33152 30  ASN B N   
1944 C CA  . ASN B 30  ? 0.89777 1.25670 1.32068 -0.25197 0.11382  -0.35570 30  ASN B CA  
1945 C C   . ASN B 30  ? 0.89663 1.33267 1.33289 -0.23705 0.08893  -0.36800 30  ASN B C   
1946 O O   . ASN B 30  ? 0.89917 1.36576 1.33873 -0.23790 0.08321  -0.38298 30  ASN B O   
1947 C CB  . ASN B 30  ? 0.97182 1.32898 1.40259 -0.28878 0.14266  -0.38804 30  ASN B CB  
1948 C CG  . ASN B 30  ? 0.98917 1.39637 1.43986 -0.30795 0.14965  -0.41547 30  ASN B CG  
1949 O OD1 . ASN B 30  ? 0.96340 1.41091 1.42295 -0.29238 0.13179  -0.41099 30  ASN B OD1 
1950 N ND2 . ASN B 30  ? 1.00991 1.41385 1.46709 -0.34262 0.17731  -0.44492 30  ASN B ND2 
1951 N N   . PRO B 31  ? 0.93036 1.39966 1.37302 -0.22222 0.07438  -0.36250 31  PRO B N   
1952 C CA  . PRO B 31  ? 0.93166 1.47427 1.38398 -0.20448 0.05147  -0.37340 31  PRO B CA  
1953 C C   . PRO B 31  ? 0.96021 1.57066 1.43349 -0.22636 0.05765  -0.41448 31  PRO B C   
1954 O O   . PRO B 31  ? 0.91572 1.59011 1.39557 -0.21143 0.03938  -0.42624 31  PRO B O   
1955 C CB  . PRO B 31  ? 0.86276 1.41389 1.31460 -0.18509 0.03923  -0.35633 31  PRO B CB  
1956 C CG  . PRO B 31  ? 0.88170 1.38286 1.33188 -0.20286 0.05943  -0.34966 31  PRO B CG  
1957 C CD  . PRO B 31  ? 0.92078 1.35790 1.35827 -0.21615 0.07670  -0.34196 31  PRO B CD  
1958 N N   . GLU B 32  ? 1.12102 1.72046 1.60377 -0.26091 0.08358  -0.43734 32  GLU B N   
1959 C CA  . GLU B 32  ? 1.10317 1.76756 1.60618 -0.28544 0.09148  -0.47957 32  GLU B CA  
1960 C C   . GLU B 32  ? 1.11673 1.77697 1.61441 -0.29410 0.09581  -0.49149 32  GLU B C   
1961 O O   . GLU B 32  ? 1.11595 1.83001 1.61378 -0.29141 0.08984  -0.51252 32  GLU B O   
1962 C CB  . GLU B 32  ? 1.11666 1.75906 1.61896 -0.31413 0.12018  -0.49523 32  GLU B CB  
1963 C CG  . GLU B 32  ? 1.17178 1.82429 1.68057 -0.30800 0.11710  -0.48763 32  GLU B CG  
1964 C CD  . GLU B 32  ? 1.31757 1.95293 1.82332 -0.33539 0.14571  -0.50552 32  GLU B CD  
1965 O OE1 . GLU B 32  ? 1.35832 1.97235 1.85594 -0.35862 0.16876  -0.52348 32  GLU B OE1 
1966 O OE2 . GLU B 32  ? 1.37314 2.01473 1.88354 -0.33348 0.14618  -0.50161 32  GLU B OE2 
1967 N N   . VAL B 33  ? 0.96280 1.54832 1.44317 -0.29656 0.10702  -0.47166 33  VAL B N   
1968 C CA  . VAL B 33  ? 0.92242 1.49651 1.39687 -0.30567 0.11324  -0.48156 33  VAL B CA  
1969 C C   . VAL B 33  ? 0.90312 1.49949 1.36934 -0.27216 0.08467  -0.46463 33  VAL B C   
1970 O O   . VAL B 33  ? 0.97374 1.53986 1.42651 -0.24394 0.06954  -0.43055 33  VAL B O   
1971 C CB  . VAL B 33  ? 0.88496 1.36779 1.34091 -0.31725 0.13668  -0.46429 33  VAL B CB  
1972 C CG1 . VAL B 33  ? 0.85966 1.32841 1.30829 -0.32490 0.14311  -0.47313 33  VAL B CG1 
1973 C CG2 . VAL B 33  ? 0.95591 1.41036 1.41557 -0.34866 0.16704  -0.47912 33  VAL B CG2 
1974 N N   . VAL B 34  ? 0.83497 1.48283 1.30790 -0.27566 0.07836  -0.48867 34  VAL B N   
1975 C CA  . VAL B 34  ? 0.78652 1.45642 1.24962 -0.24477 0.05322  -0.47510 34  VAL B CA  
1976 C C   . VAL B 34  ? 0.81124 1.46798 1.26915 -0.25871 0.06272  -0.48815 34  VAL B C   
1977 O O   . VAL B 34  ? 0.83312 1.54715 1.30323 -0.27376 0.06435  -0.52188 34  VAL B O   
1978 C CB  . VAL B 34  ? 0.69370 1.45297 1.16838 -0.22702 0.03091  -0.49060 34  VAL B CB  
1979 N N   . GLU B 35  ? 0.81391 1.39748 1.25372 -0.25348 0.06904  -0.46233 35  GLU B N   
1980 C CA  . GLU B 35  ? 0.80904 1.37390 1.24172 -0.26426 0.07822  -0.47145 35  GLU B CA  
1981 C C   . GLU B 35  ? 0.87295 1.47796 1.29964 -0.23766 0.05321  -0.46712 35  GLU B C   
1982 O O   . GLU B 35  ? 0.85116 1.45992 1.26929 -0.20603 0.03188  -0.44151 35  GLU B O   
1983 C CB  . GLU B 35  ? 0.80537 1.28010 1.22020 -0.26528 0.09358  -0.44467 35  GLU B CB  
1984 N N   . THR B 36  ? 0.87996 1.51264 1.30935 -0.25093 0.05736  -0.49252 36  THR B N   
1985 C CA  . THR B 36  ? 0.85222 1.52811 1.27549 -0.22875 0.03609  -0.49389 36  THR B CA  
1986 C C   . THR B 36  ? 0.84907 1.46480 1.25088 -0.20915 0.03122  -0.46184 36  THR B C   
1987 O O   . THR B 36  ? 0.87138 1.41705 1.26486 -0.21857 0.04758  -0.44641 36  THR B O   
1988 C CB  . THR B 36  ? 0.87105 1.60018 1.30566 -0.25296 0.04397  -0.53548 36  THR B CB  
1989 O OG1 . THR B 36  ? 0.89864 1.68139 1.34956 -0.26935 0.05066  -0.56338 36  THR B OG1 
1990 C CG2 . THR B 36  ? 0.80568 1.58448 1.23270 -0.22905 0.02177  -0.53866 36  THR B CG2 
1991 N N   . PHE B 37  ? 0.83581 1.48150 1.22769 -0.18044 0.00883  -0.45228 37  PHE B N   
1992 C CA  . PHE B 37  ? 0.83825 1.43805 1.21040 -0.16182 0.00304  -0.42607 37  PHE B CA  
1993 C C   . PHE B 37  ? 0.86095 1.42465 1.22989 -0.18402 0.02185  -0.43675 37  PHE B C   
1994 O O   . PHE B 37  ? 0.84359 1.34546 1.19898 -0.17776 0.02692  -0.41259 37  PHE B O   
1995 C CB  . PHE B 37  ? 0.76614 1.41463 1.12836 -0.13142 -0.02117 -0.42263 37  PHE B CB  
1996 C CG  . PHE B 37  ? 0.75932 1.36719 1.10102 -0.11232 -0.02733 -0.39826 37  PHE B CG  
1997 C CD1 . PHE B 37  ? 0.79123 1.33953 1.12052 -0.09725 -0.02892 -0.36329 37  PHE B CD1 
1998 C CD2 . PHE B 37  ? 0.80108 1.43422 1.13574 -0.10867 -0.03214 -0.41096 37  PHE B CD2 
1999 C CE1 . PHE B 37  ? 0.84524 1.35883 1.15647 -0.08069 -0.03389 -0.34222 37  PHE B CE1 
2000 C CE2 . PHE B 37  ? 0.84217 1.43795 1.15753 -0.09116 -0.03719 -0.38866 37  PHE B CE2 
2001 C CZ  . PHE B 37  ? 0.84403 1.38032 1.14813 -0.07759 -0.03777 -0.35458 37  PHE B CZ  
2002 N N   . ASP B 38  ? 0.85263 1.45496 1.23349 -0.21004 0.03299  -0.47353 38  ASP B N   
2003 C CA  . ASP B 38  ? 0.90083 1.47096 1.27628 -0.22948 0.05054  -0.48476 38  ASP B CA  
2004 C C   . ASP B 38  ? 0.93767 1.42878 1.30892 -0.24776 0.07598  -0.47292 38  ASP B C   
2005 O O   . ASP B 38  ? 0.94860 1.38379 1.30570 -0.24373 0.08336  -0.45552 38  ASP B O   
2006 C CB  . ASP B 38  ? 0.90061 1.53205 1.28961 -0.25527 0.05803  -0.52942 38  ASP B CB  
2007 N N   . GLU B 39  ? 1.10790 1.59285 1.48987 -0.26660 0.09025  -0.48164 39  GLU B N   
2008 C CA  . GLU B 39  ? 1.13379 1.54242 1.50845 -0.28274 0.11633  -0.47089 39  GLU B CA  
2009 C C   . GLU B 39  ? 1.14985 1.50653 1.51353 -0.25871 0.10927  -0.42996 39  GLU B C   
2010 O O   . GLU B 39  ? 1.17362 1.46314 1.52651 -0.26429 0.12794  -0.41501 39  GLU B O   
2011 C CB  . GLU B 39  ? 1.13326 1.55039 1.52121 -0.31591 0.13911  -0.49896 39  GLU B CB  
2012 C CG  . GLU B 39  ? 1.17183 1.62106 1.57173 -0.30918 0.12816  -0.49542 39  GLU B CG  
2013 C CD  . GLU B 39  ? 1.15426 1.69608 1.56988 -0.30301 0.10662  -0.51817 39  GLU B CD  
2014 O OE1 . GLU B 39  ? 1.09164 1.66820 1.50450 -0.29272 0.09297  -0.52560 39  GLU B OE1 
2015 O OE2 . GLU B 39  ? 1.17747 1.75804 1.60741 -0.30793 0.10403  -0.52910 39  GLU B OE2 
2016 N N   . LEU B 40  ? 0.95472 1.34057 1.31967 -0.23204 0.08400  -0.41215 40  LEU B N   
2017 C CA  . LEU B 40  ? 0.88174 1.22058 1.23394 -0.20706 0.07494  -0.37326 40  LEU B CA  
2018 C C   . LEU B 40  ? 0.88851 1.19348 1.22556 -0.19346 0.07200  -0.35634 40  LEU B C   
2019 O O   . LEU B 40  ? 0.83340 1.07910 1.15936 -0.18798 0.08052  -0.33307 40  LEU B O   
2020 C CB  . LEU B 40  ? 0.82798 1.20537 1.18302 -0.18246 0.05009  -0.36003 40  LEU B CB  
2021 C CG  . LEU B 40  ? 0.82327 1.20981 1.18961 -0.19150 0.05497  -0.36401 40  LEU B CG  
2022 C CD1 . LEU B 40  ? 0.77110 1.20236 1.14074 -0.16843 0.03165  -0.35567 40  LEU B CD1 
2023 C CD2 . LEU B 40  ? 0.74295 1.05954 1.10076 -0.19367 0.06946  -0.34046 40  LEU B CD2 
2024 N N   . VAL B 41  ? 0.88628 1.22987 1.22222 -0.18731 0.06030  -0.36827 41  VAL B N   
2025 C CA  . VAL B 41  ? 0.84691 1.15915 1.16878 -0.17635 0.05910  -0.35438 41  VAL B CA  
2026 C C   . VAL B 41  ? 0.82649 1.09132 1.14448 -0.19894 0.08571  -0.36344 41  VAL B C   
2027 O O   . VAL B 41  ? 0.80506 1.01681 1.11070 -0.19075 0.09212  -0.34216 41  VAL B O   
2028 C CB  . VAL B 41  ? 0.84740 1.21182 1.16716 -0.16456 0.04154  -0.36594 41  VAL B CB  
2029 C CG1 . VAL B 41  ? 0.87327 1.20533 1.17917 -0.15760 0.04360  -0.35581 41  VAL B CG1 
2030 C CG2 . VAL B 41  ? 0.82091 1.21727 1.13778 -0.13672 0.01710  -0.34982 41  VAL B CG2 
2031 N N   . SER B 42  ? 0.82661 1.10892 1.15425 -0.22767 0.10299  -0.39542 42  SER B N   
2032 C CA  . SER B 42  ? 0.88782 1.12091 1.20860 -0.24961 0.13112  -0.40506 42  SER B CA  
2033 C C   . SER B 42  ? 0.87217 1.03773 1.18427 -0.24947 0.14793  -0.38248 42  SER B C   
2034 O O   . SER B 42  ? 0.84739 0.95664 1.14598 -0.25171 0.16561  -0.37333 42  SER B O   
2035 C CB  . SER B 42  ? 0.91014 1.17490 1.24240 -0.28337 0.14886  -0.44623 42  SER B CB  
2036 O OG  . SER B 42  ? 0.91424 1.18021 1.25602 -0.29870 0.15981  -0.45423 42  SER B OG  
2037 N N   . ARG B 43  ? 0.85812 1.02895 1.17655 -0.24525 0.14276  -0.37297 43  ARG B N   
2038 C CA  . ARG B 43  ? 0.80643 0.91651 1.11586 -0.24509 0.15904  -0.35291 43  ARG B CA  
2039 C C   . ARG B 43  ? 0.81086 0.88305 1.10730 -0.21614 0.14764  -0.31575 43  ARG B C   
2040 O O   . ARG B 43  ? 0.83825 0.85267 1.12221 -0.21411 0.16410  -0.29926 43  ARG B O   
2041 C CB  . ARG B 43  ? 0.78110 0.91044 1.10148 -0.25125 0.15803  -0.35638 43  ARG B CB  
2042 C CG  . ARG B 43  ? 0.84456 0.91241 1.15456 -0.25405 0.17792  -0.33957 43  ARG B CG  
2043 C CD  . ARG B 43  ? 0.83921 0.92437 1.15913 -0.25757 0.17542  -0.33965 43  ARG B CD  
2044 N NE  . ARG B 43  ? 0.78980 0.91330 1.12453 -0.28603 0.18703  -0.37456 43  ARG B NE  
2045 C CZ  . ARG B 43  ? 0.81392 1.00256 1.16626 -0.28605 0.16958  -0.38832 43  ARG B CZ  
2046 N NH1 . ARG B 43  ? 0.78309 1.00161 1.13850 -0.25889 0.14081  -0.36934 43  ARG B NH1 
2047 N NH2 . ARG B 43  ? 0.86632 1.09102 1.23275 -0.31397 0.18248  -0.42258 43  ARG B NH2 
2048 N N   . GLY B 44  ? 0.77867 0.88200 1.07648 -0.19329 0.12091  -0.30259 44  GLY B N   
2049 C CA  . GLY B 44  ? 0.76641 0.83789 1.05319 -0.16819 0.11080  -0.26994 44  GLY B CA  
2050 C C   . GLY B 44  ? 0.84295 0.88540 1.11833 -0.16354 0.11715  -0.26471 44  GLY B C   
2051 O O   . GLY B 44  ? 0.83960 0.89247 1.11528 -0.17712 0.12517  -0.28604 44  GLY B O   
2052 N N   . ILE B 45  ? 0.87892 0.88590 1.14428 -0.14404 0.11374  -0.23642 45  ILE B N   
2053 C CA  . ILE B 45  ? 0.89950 0.87975 1.15416 -0.13581 0.11798  -0.22795 45  ILE B CA  
2054 C C   . ILE B 45  ? 0.90115 0.88705 1.15261 -0.11032 0.09680  -0.20291 45  ILE B C   
2055 O O   . ILE B 45  ? 0.88836 0.87728 1.14188 -0.09909 0.08602  -0.18664 45  ILE B O   
2056 C CB  . ILE B 45  ? 0.93073 0.85109 1.17323 -0.13987 0.14356  -0.22030 45  ILE B CB  
2057 C CG1 . ILE B 45  ? 0.94185 0.83475 1.17926 -0.12312 0.14128  -0.19268 45  ILE B CG1 
2058 C CG2 . ILE B 45  ? 0.94659 0.85431 1.18973 -0.16661 0.16809  -0.24442 45  ILE B CG2 
2059 C CD1 . ILE B 45  ? 0.97384 0.80887 1.19557 -0.11845 0.16327  -0.17970 45  ILE B CD1 
2060 N N   . LYS B 46  ? 0.78104 0.76818 1.02696 -0.10228 0.09186  -0.20081 46  LYS B N   
2061 C CA  . LYS B 46  ? 0.73998 0.72834 0.98135 -0.08029 0.07536  -0.17860 46  LYS B CA  
2062 C C   . LYS B 46  ? 0.72310 0.66966 0.95501 -0.07241 0.08670  -0.16403 46  LYS B C   
2063 O O   . LYS B 46  ? 0.73942 0.67012 0.96644 -0.08018 0.10029  -0.17453 46  LYS B O   
2064 C CB  . LYS B 46  ? 0.64731 0.67385 0.88843 -0.07433 0.05891  -0.18618 46  LYS B CB  
2065 N N   . ILE B 47  ? 0.72109 0.65132 0.95035 -0.05698 0.08178  -0.14077 47  ILE B N   
2066 C CA  . ILE B 47  ? 0.70078 0.59702 0.92176 -0.04581 0.09055  -0.12502 47  ILE B CA  
2067 C C   . ILE B 47  ? 0.67675 0.58877 0.89659 -0.03114 0.07479  -0.11407 47  ILE B C   
2068 O O   . ILE B 47  ? 0.74987 0.68384 0.97303 -0.02363 0.05853  -0.10613 47  ILE B O   
2069 C CB  . ILE B 47  ? 0.75470 0.62598 0.97316 -0.03780 0.09609  -0.10741 47  ILE B CB  
2070 C CG1 . ILE B 47  ? 0.75356 0.60559 0.97091 -0.05240 0.11339  -0.11739 47  ILE B CG1 
2071 C CG2 . ILE B 47  ? 0.82602 0.66827 1.03563 -0.02319 0.10399  -0.09138 47  ILE B CG2 
2072 C CD1 . ILE B 47  ? 0.75511 0.63274 0.98174 -0.05909 0.10352  -0.12215 47  ILE B CD1 
2073 N N   . LYS B 48  ? 0.76785 0.66757 0.98197 -0.02749 0.08067  -0.11404 48  LYS B N   
2074 C CA  . LYS B 48  ? 0.76704 0.68166 0.97931 -0.01586 0.06772  -0.10634 48  LYS B CA  
2075 C C   . LYS B 48  ? 0.78996 0.68204 0.99828 -0.00211 0.07264  -0.08869 48  LYS B C   
2076 O O   . LYS B 48  ? 0.84592 0.71035 1.04918 -0.00207 0.08873  -0.08870 48  LYS B O   
2077 C CB  . LYS B 48  ? 0.78565 0.71303 0.99495 -0.02265 0.06808  -0.12294 48  LYS B CB  
2078 C CG  . LYS B 48  ? 0.87952 0.82416 1.08510 -0.01147 0.05439  -0.11630 48  LYS B CG  
2079 C CD  . LYS B 48  ? 0.89175 0.84976 1.09266 -0.01700 0.05456  -0.13258 48  LYS B CD  
2080 C CE  . LYS B 48  ? 0.82486 0.79524 1.01942 -0.00475 0.04264  -0.12397 48  LYS B CE  
2081 N NZ  . LYS B 48  ? 0.82881 0.77615 1.02205 0.00453  0.04824  -0.10827 48  LYS B NZ  
2082 N N   . PHE B 49  ? 0.79431 0.69873 1.00417 0.00969  0.05979  -0.07439 49  PHE B N   
2083 C CA  . PHE B 49  ? 0.84592 0.73780 1.05453 0.02321  0.06219  -0.05784 49  PHE B CA  
2084 C C   . PHE B 49  ? 0.85083 0.74817 1.05661 0.02948  0.05975  -0.05647 49  PHE B C   
2085 O O   . PHE B 49  ? 0.86378 0.77864 1.06814 0.02630  0.05104  -0.06328 49  PHE B O   
2086 C CB  . PHE B 49  ? 0.75118 0.65493 0.96418 0.03009  0.05097  -0.04446 49  PHE B CB  
2087 C CG  . PHE B 49  ? 0.73055 0.62761 0.94582 0.02504  0.05395  -0.04438 49  PHE B CG  
2088 C CD1 . PHE B 49  ? 0.75724 0.62958 0.96919 0.02931  0.06688  -0.03772 49  PHE B CD1 
2089 C CD2 . PHE B 49  ? 0.73094 0.64575 0.95007 0.01714  0.04475  -0.05091 49  PHE B CD2 
2090 C CE1 . PHE B 49  ? 0.75544 0.61921 0.96778 0.02427  0.07114  -0.03775 49  PHE B CE1 
2091 C CE2 . PHE B 49  ? 0.70690 0.61598 0.92849 0.01179  0.04830  -0.05153 49  PHE B CE2 
2092 C CZ  . PHE B 49  ? 0.68651 0.56912 0.90462 0.01468  0.06182  -0.04499 49  PHE B CZ  
2093 N N   . ASP B 50  ? 0.93275 0.81527 1.13652 0.03956  0.06810  -0.04760 50  ASP B N   
2094 C CA  . ASP B 50  ? 0.95691 0.84537 1.15900 0.04615  0.06658  -0.04541 50  ASP B CA  
2095 C C   . ASP B 50  ? 0.92847 0.83682 1.13473 0.05387  0.05440  -0.03408 50  ASP B C   
2096 O O   . ASP B 50  ? 0.92550 0.83433 1.13536 0.06269  0.05450  -0.02270 50  ASP B O   
2097 C CB  . ASP B 50  ? 0.94387 0.81030 1.14191 0.05458  0.08142  -0.04175 50  ASP B CB  
2098 C CG  . ASP B 50  ? 1.01392 0.88994 1.21227 0.06338  0.07933  -0.03726 50  ASP B CG  
2099 O OD1 . ASP B 50  ? 1.05720 0.93929 1.25278 0.05787  0.07735  -0.04604 50  ASP B OD1 
2100 O OD2 . ASP B 50  ? 1.02577 0.90561 1.22707 0.07605  0.07961  -0.02541 50  ASP B OD2 
2101 N N   . LEU B 51  ? 0.87380 0.79814 1.07801 0.05085  0.04520  -0.03770 51  LEU B N   
2102 C CA  . LEU B 51  ? 0.82458 0.76482 1.03070 0.05534  0.03593  -0.02879 51  LEU B CA  
2103 C C   . LEU B 51  ? 0.87635 0.81896 1.08587 0.06454  0.04017  -0.02091 51  LEU B C   
2104 O O   . LEU B 51  ? 0.85862 0.81220 1.07342 0.06927  0.03632  -0.01225 51  LEU B O   
2105 C CB  . LEU B 51  ? 0.72202 0.67334 0.92087 0.05137  0.02814  -0.03390 51  LEU B CB  
2106 C CG  . LEU B 51  ? 0.71720 0.67533 0.91275 0.04573  0.02038  -0.03927 51  LEU B CG  
2107 C CD1 . LEU B 51  ? 0.64371 0.61155 0.82829 0.04639  0.01326  -0.04127 51  LEU B CD1 
2108 C CD2 . LEU B 51  ? 0.74711 0.70759 0.94888 0.04603  0.01633  -0.03188 51  LEU B CD2 
2109 N N   . LYS B 52  ? 0.85895 0.79431 1.06586 0.06715  0.04803  -0.02463 52  LYS B N   
2110 C CA  . LYS B 52  ? 0.85731 0.80190 1.06767 0.07530  0.05027  -0.01878 52  LYS B CA  
2111 C C   . LYS B 52  ? 0.86427 0.81255 1.08164 0.08600  0.05278  -0.00879 52  LYS B C   
2112 O O   . LYS B 52  ? 0.87522 0.84241 1.09846 0.09138  0.04999  -0.00343 52  LYS B O   
2113 C CB  . LYS B 52  ? 0.91753 0.85265 1.12360 0.07717  0.05919  -0.02451 52  LYS B CB  
2114 C CG  . LYS B 52  ? 0.90461 0.85295 1.11451 0.08442  0.06128  -0.02043 52  LYS B CG  
2115 C CD  . LYS B 52  ? 1.01473 0.95245 1.21978 0.08649  0.07065  -0.02627 52  LYS B CD  
2116 C CE  . LYS B 52  ? 1.00009 0.95380 1.20966 0.09298  0.07303  -0.02346 52  LYS B CE  
2117 N NZ  . LYS B 52  ? 0.79130 0.73380 0.99611 0.09609  0.08290  -0.02866 52  LYS B NZ  
2118 N N   . SER B 53  ? 0.85744 0.78914 1.07339 0.08917  0.05853  -0.00673 53  SER B N   
2119 C CA  . SER B 53  ? 0.85663 0.78914 1.07552 0.10283  0.06254  0.00357  53  SER B CA  
2120 C C   . SER B 53  ? 0.84933 0.79595 1.07320 0.10286  0.05344  0.01016  53  SER B C   
2121 O O   . SER B 53  ? 0.81880 0.77419 1.04557 0.11530  0.05434  0.01891  53  SER B O   
2122 C CB  . SER B 53  ? 0.86790 0.77034 1.07890 0.10786  0.07610  0.00378  53  SER B CB  
2123 O OG  . SER B 53  ? 0.89746 0.78690 1.10576 0.09653  0.07546  -0.00097 53  SER B OG  
2124 N N   . GLN B 54  ? 0.83147 0.78145 1.05549 0.09057  0.04494  0.00611  54  GLN B N   
2125 C CA  . GLN B 54  ? 0.80271 0.76821 1.03129 0.08942  0.03579  0.01156  54  GLN B CA  
2126 C C   . GLN B 54  ? 0.80735 0.79836 1.04122 0.08945  0.02957  0.01317  54  GLN B C   
2127 O O   . GLN B 54  ? 0.83457 0.83996 1.07206 0.08762  0.02284  0.01674  54  GLN B O   
2128 C CB  . GLN B 54  ? 0.67938 0.63966 0.90521 0.07736  0.02971  0.00647  54  GLN B CB  
2129 C CG  . GLN B 54  ? 0.64735 0.58575 0.86928 0.07414  0.03666  0.00227  54  GLN B CG  
2130 C CD  . GLN B 54  ? 0.63152 0.57094 0.85206 0.06247  0.03041  -0.00500 54  GLN B CD  
2131 O OE1 . GLN B 54  ? 0.63668 0.59046 0.85772 0.05924  0.02083  -0.00434 54  GLN B OE1 
2132 N NE2 . GLN B 54  ? 0.71066 0.63539 0.92846 0.05592  0.03685  -0.01331 54  GLN B NE2 
2133 N N   . LYS B 55  ? 0.88355 0.88004 1.11750 0.09004  0.03266  0.00962  55  LYS B N   
2134 C CA  . LYS B 55  ? 0.88266 0.90370 1.12202 0.08917  0.02952  0.00998  55  LYS B CA  
2135 C C   . LYS B 55  ? 0.87416 0.91582 1.12203 0.09984  0.02877  0.01677  55  LYS B C   
2136 O O   . LYS B 55  ? 0.83721 0.87356 1.08533 0.11302  0.03399  0.02176  55  LYS B O   
2137 C CB  . LYS B 55  ? 0.87036 0.89358 1.10883 0.08974  0.03512  0.00521  55  LYS B CB  
2138 C CG  . LYS B 55  ? 0.90293 0.91176 1.13167 0.07970  0.03503  -0.00188 55  LYS B CG  
2139 C CD  . LYS B 55  ? 1.03369 1.04815 1.26168 0.08010  0.04067  -0.00600 55  LYS B CD  
2140 C CE  . LYS B 55  ? 1.04059 1.04663 1.27000 0.09014  0.04911  -0.00623 55  LYS B CE  
2141 N NZ  . LYS B 55  ? 1.06923 1.08087 1.29794 0.09051  0.05485  -0.01063 55  LYS B NZ  
2142 N N   . GLY B 56  ? 0.85999 0.92431 1.11301 0.09441  0.02291  0.01672  56  GLY B N   
2143 C CA  . GLY B 56  ? 0.79367 0.88438 1.05520 0.10327  0.02072  0.02134  56  GLY B CA  
2144 C C   . GLY B 56  ? 0.77201 0.85464 1.03176 0.11093  0.01855  0.02871  56  GLY B C   
2145 O O   . GLY B 56  ? 0.78965 0.89368 1.05452 0.12192  0.01715  0.03351  56  GLY B O   
2146 N N   . HIS B 57  ? 0.77656 0.83088 1.02887 0.10598  0.01868  0.02922  57  HIS B N   
2147 C CA  . HIS B 57  ? 0.78325 0.82709 1.03281 0.11142  0.01800  0.03561  57  HIS B CA  
2148 C C   . HIS B 57  ? 0.76247 0.79663 1.00919 0.09827  0.01196  0.03357  57  HIS B C   
2149 O O   . HIS B 57  ? 0.74423 0.78332 0.99176 0.09957  0.00806  0.03811  57  HIS B O   
2150 C CB  . HIS B 57  ? 0.84830 0.86417 1.09064 0.12078  0.02779  0.03834  57  HIS B CB  
2151 C CG  . HIS B 57  ? 0.89228 0.91551 1.13466 0.13936  0.03461  0.04378  57  HIS B CG  
2152 N ND1 . HIS B 57  ? 0.90884 0.94661 1.15149 0.15510  0.03422  0.05235  57  HIS B ND1 
2153 C CD2 . HIS B 57  ? 0.88810 0.90737 1.12924 0.14643  0.04209  0.04205  57  HIS B CD2 
2154 C CE1 . HIS B 57  ? 0.95353 0.99680 1.19470 0.17246  0.04111  0.05598  57  HIS B CE1 
2155 N NE2 . HIS B 57  ? 0.91853 0.94984 1.15910 0.16713  0.04627  0.04984  57  HIS B NE2 
2156 N N   . ARG B 58  ? 0.70007 0.72168 0.94264 0.08706  0.01117  0.02691  58  ARG B N   
2157 C CA  . ARG B 58  ? 0.61930 0.63613 0.85847 0.07611  0.00503  0.02439  58  ARG B CA  
2158 C C   . ARG B 58  ? 0.66188 0.68725 0.89852 0.06773  0.00228  0.01951  58  ARG B C   
2159 O O   . ARG B 58  ? 0.70199 0.73677 0.94066 0.06919  0.00548  0.01764  58  ARG B O   
2160 C CB  . ARG B 58  ? 0.58238 0.57674 0.81645 0.07253  0.00755  0.02063  58  ARG B CB  
2161 C CG  . ARG B 58  ? 0.63082 0.61280 0.86510 0.08071  0.01389  0.02562  58  ARG B CG  
2162 C CD  . ARG B 58  ? 0.61182 0.57238 0.84188 0.07489  0.01836  0.02069  58  ARG B CD  
2163 N NE  . ARG B 58  ? 0.62836 0.59365 0.85862 0.06590  0.01050  0.01819  58  ARG B NE  
2164 C CZ  . ARG B 58  ? 0.56733 0.53711 0.79922 0.06683  0.00668  0.02388  58  ARG B CZ  
2165 N NH1 . ARG B 58  ? 0.56089 0.53284 0.79395 0.07658  0.00918  0.03240  58  ARG B NH1 
2166 N NH2 . ARG B 58  ? 0.60561 0.57924 0.83702 0.05910  0.00008  0.02105  58  ARG B NH2 
2167 N N   . LEU B 59  ? 0.64781 0.66940 0.87875 0.05964  -0.00258 0.01773  59  LEU B N   
2168 C CA  . LEU B 59  ? 0.62058 0.64820 0.84608 0.05251  -0.00366 0.01512  59  LEU B CA  
2169 C C   . LEU B 59  ? 0.65801 0.67087 0.87143 0.04856  -0.00399 0.01050  59  LEU B C   
2170 O O   . LEU B 59  ? 0.62686 0.63077 0.83636 0.04818  -0.00742 0.00952  59  LEU B O   
2171 C CB  . LEU B 59  ? 0.67232 0.70796 0.89792 0.04809  -0.00775 0.01783  59  LEU B CB  
2172 C CG  . LEU B 59  ? 0.68000 0.71466 0.89579 0.03935  -0.00664 0.01498  59  LEU B CG  
2173 C CD1 . LEU B 59  ? 0.67256 0.72046 0.89084 0.03562  -0.00084 0.01143  59  LEU B CD1 
2174 C CD2 . LEU B 59  ? 0.69512 0.73252 0.90950 0.03519  -0.01021 0.01745  59  LEU B CD2 
2175 N N   . PHE B 60  ? 0.70077 0.71297 0.90755 0.04601  -0.00017 0.00728  60  PHE B N   
2176 C CA  . PHE B 60  ? 0.68473 0.68388 0.87656 0.04438  -0.00003 0.00357  60  PHE B CA  
2177 C C   . PHE B 60  ? 0.70470 0.70068 0.88451 0.03915  0.00155  0.00448  60  PHE B C   
2178 O O   . PHE B 60  ? 0.77216 0.77457 0.95311 0.03459  0.00688  0.00383  60  PHE B O   
2179 C CB  . PHE B 60  ? 0.71169 0.70672 0.90011 0.04622  0.00483  -0.00078 60  PHE B CB  
2180 C CG  . PHE B 60  ? 0.67757 0.67418 0.87731 0.05088  0.00694  -0.00183 60  PHE B CG  
2181 C CD1 . PHE B 60  ? 0.66492 0.67157 0.87776 0.05463  0.00849  0.00220  60  PHE B CD1 
2182 C CD2 . PHE B 60  ? 0.63619 0.62345 0.83197 0.05220  0.00738  -0.00699 60  PHE B CD2 
2183 C CE1 . PHE B 60  ? 0.67285 0.67573 0.89201 0.06079  0.01238  0.00225  60  PHE B CE1 
2184 C CE2 . PHE B 60  ? 0.64163 0.62534 0.84518 0.05547  0.01155  -0.00845 60  PHE B CE2 
2185 C CZ  . PHE B 60  ? 0.69975 0.68887 0.91390 0.06040  0.01466  -0.00308 60  PHE B CZ  
2186 N N   . THR B 61  ? 0.74646 0.73276 0.91427 0.03970  -0.00190 0.00531  61  THR B N   
2187 C CA  . THR B 61  ? 0.74659 0.72493 0.90031 0.03573  0.00090  0.00712  61  THR B CA  
2188 C C   . THR B 61  ? 0.79397 0.75640 0.92605 0.03849  0.00552  0.00535  61  THR B C   
2189 O O   . THR B 61  ? 0.79486 0.75288 0.91899 0.04552  0.00126  0.00401  61  THR B O   
2190 C CB  . THR B 61  ? 0.78918 0.76599 0.94160 0.03704  -0.00521 0.01020  61  THR B CB  
2191 O OG1 . THR B 61  ? 0.70331 0.69390 0.87432 0.03528  -0.00875 0.01226  61  THR B OG1 
2192 C CG2 . THR B 61  ? 0.80763 0.77195 0.94249 0.03387  -0.00104 0.01234  61  THR B CG2 
2193 N N   . LYS B 62  ? 0.81060 0.76599 0.93294 0.03292  0.01488  0.00450  62  LYS B N   
2194 C CA  . LYS B 62  ? 0.84654 0.78192 0.94346 0.03534  0.02234  0.00399  62  LYS B CA  
2195 C C   . LYS B 62  ? 0.85853 0.77967 0.93487 0.04441  0.01887  0.00713  62  LYS B C   
2196 O O   . LYS B 62  ? 0.87141 0.78319 0.93029 0.05330  0.01911  0.00661  62  LYS B O   
2197 C CB  . LYS B 62  ? 0.84577 0.77278 0.93400 0.02477  0.03497  0.00280  62  LYS B CB  
2198 C CG  . LYS B 62  ? 0.84671 0.74813 0.90574 0.02617  0.04645  0.00267  62  LYS B CG  
2199 C CD  . LYS B 62  ? 0.85356 0.73060 0.88569 0.03053  0.05034  0.00726  62  LYS B CD  
2200 C CE  . LYS B 62  ? 1.02934 0.87709 1.02765 0.03604  0.06221  0.00873  62  LYS B CE  
2201 N NZ  . LYS B 62  ? 1.10724 0.93219 1.07798 0.04634  0.06378  0.01468  62  LYS B NZ  
2202 N N   . SER B 63  ? 0.87288 0.79411 0.95052 0.04330  0.01563  0.01022  63  SER B N   
2203 C CA  . SER B 63  ? 0.87070 0.78215 0.93077 0.05337  0.01170  0.01323  63  SER B CA  
2204 C C   . SER B 63  ? 0.89297 0.81694 0.95781 0.06311  0.00179  0.01019  63  SER B C   
2205 O O   . SER B 63  ? 0.94263 0.86012 0.98723 0.07446  0.00056  0.01040  63  SER B O   
2206 C CB  . SER B 63  ? 0.90218 0.81761 0.97030 0.04965  0.00811  0.01608  63  SER B CB  
2207 O OG  . SER B 63  ? 0.96082 0.87288 1.03189 0.03741  0.01643  0.01611  63  SER B OG  
2208 N N   . THR B 64  ? 0.89454 0.83696 0.98497 0.05911  -0.00446 0.00671  64  THR B N   
2209 C CA  . THR B 64  ? 0.85754 0.81297 0.95508 0.06475  -0.01250 0.00162  64  THR B CA  
2210 C C   . THR B 64  ? 0.89319 0.84870 0.98469 0.06811  -0.01048 -0.00340 64  THR B C   
2211 O O   . THR B 64  ? 0.90695 0.87057 0.99324 0.07499  -0.01551 -0.00866 64  THR B O   
2212 C CB  . THR B 64  ? 0.77545 0.74472 0.89937 0.05854  -0.01682 -0.00018 64  THR B CB  
2213 O OG1 . THR B 64  ? 0.81306 0.78249 0.94280 0.05488  -0.01804 0.00480  64  THR B OG1 
2214 C CG2 . THR B 64  ? 0.76759 0.74890 0.89732 0.06191  -0.02337 -0.00698 64  THR B CG2 
2215 N N   . ILE B 65  ? 0.90681 0.85654 1.00036 0.06291  -0.00326 -0.00301 65  ILE B N   
2216 C CA  . ILE B 65  ? 0.92449 0.87254 1.01113 0.06579  -0.00024 -0.00750 65  ILE B CA  
2217 C C   . ILE B 65  ? 0.94800 0.88330 1.00456 0.07570  0.00222  -0.00629 65  ILE B C   
2218 O O   . ILE B 65  ? 0.92785 0.86870 0.97562 0.08341  -0.00113 -0.01121 65  ILE B O   
2219 C CB  . ILE B 65  ? 0.87146 0.81713 0.96702 0.05821  0.00771  -0.00706 65  ILE B CB  
2220 C CG1 . ILE B 65  ? 0.86410 0.82349 0.98683 0.05262  0.00479  -0.00728 65  ILE B CG1 
2221 C CG2 . ILE B 65  ? 0.80732 0.74997 0.89493 0.06111  0.01148  -0.01157 65  ILE B CG2 
2222 C CD1 . ILE B 65  ? 0.82365 0.78689 0.95724 0.04627  0.01126  -0.00563 65  ILE B CD1 
2223 N N   . GLU B 66  ? 0.95270 0.87040 0.99139 0.07621  0.00885  -0.00000 66  GLU B N   
2224 C CA  . GLU B 66  ? 0.98137 0.88230 0.98685 0.08851  0.01259  0.00314  66  GLU B CA  
2225 C C   . GLU B 66  ? 1.01128 0.92669 1.01202 0.10121  0.00166  0.00080  66  GLU B C   
2226 O O   . GLU B 66  ? 1.05706 0.97361 1.03846 0.11375  0.00024  -0.00132 66  GLU B O   
2227 C CB  . GLU B 66  ? 0.90932 0.78699 0.89734 0.08603  0.02235  0.01009  66  GLU B CB  
2228 N N   . TRP B 67  ? 0.99864 0.92821 1.01754 0.09819  -0.00619 0.00023  67  TRP B N   
2229 C CA  . TRP B 67  ? 0.99971 0.94766 1.01719 0.10861  -0.01632 -0.00374 67  TRP B CA  
2230 C C   . TRP B 67  ? 1.01160 0.98054 1.03772 0.11015  -0.02209 -0.01414 67  TRP B C   
2231 O O   . TRP B 67  ? 1.02450 1.00586 1.03604 0.12295  -0.02710 -0.01852 67  TRP B O   
2232 C CB  . TRP B 67  ? 0.87953 0.83896 0.91837 0.10200  -0.02233 -0.00352 67  TRP B CB  
2233 C CG  . TRP B 67  ? 0.81711 0.79649 0.85480 0.11161  -0.03152 -0.00813 67  TRP B CG  
2234 C CD1 . TRP B 67  ? 0.83426 0.81093 0.84965 0.12614  -0.03297 -0.00414 67  TRP B CD1 
2235 C CD2 . TRP B 67  ? 0.85645 0.86315 0.91493 0.10794  -0.03951 -0.01894 67  TRP B CD2 
2236 N NE1 . TRP B 67  ? 0.87928 0.88443 0.90240 0.13223  -0.04280 -0.01199 67  TRP B NE1 
2237 C CE2 . TRP B 67  ? 0.87705 0.90106 0.92697 0.11977  -0.04652 -0.02200 67  TRP B CE2 
2238 C CE3 . TRP B 67  ? 0.88141 0.89850 0.96389 0.09564  -0.04001 -0.02673 67  TRP B CE3 
2239 C CZ2 . TRP B 67  ? 0.84112 0.89571 0.90778 0.11750  -0.05414 -0.03422 67  TRP B CZ2 
2240 C CZ3 . TRP B 67  ? 0.87977 0.92162 0.97628 0.09316  -0.04605 -0.03821 67  TRP B CZ3 
2241 C CH2 . TRP B 67  ? 0.83141 0.89333 0.92104 0.10292  -0.05314 -0.04264 67  TRP B CH2 
2242 N N   . TRP B 68  ? 0.94896 0.92336 0.99811 0.09778  -0.02107 -0.01883 68  TRP B N   
2243 C CA  . TRP B 68  ? 0.95669 0.94902 1.01426 0.09715  -0.02490 -0.02996 68  TRP B CA  
2244 C C   . TRP B 68  ? 1.05684 1.04411 1.09197 0.10606  -0.02166 -0.03179 68  TRP B C   
2245 O O   . TRP B 68  ? 1.07075 1.07641 1.10315 0.11103  -0.02654 -0.04157 68  TRP B O   
2246 C CB  . TRP B 68  ? 0.96071 0.95468 1.04456 0.08335  -0.02220 -0.03349 68  TRP B CB  
2247 C CG  . TRP B 68  ? 0.95040 0.95597 1.05630 0.07598  -0.02638 -0.03675 68  TRP B CG  
2248 C CD1 . TRP B 68  ? 0.93315 0.93256 1.05327 0.06930  -0.02504 -0.03016 68  TRP B CD1 
2249 C CD2 . TRP B 68  ? 0.95500 0.98081 1.07035 0.07403  -0.03152 -0.04838 68  TRP B CD2 
2250 N NE1 . TRP B 68  ? 0.84694 0.85802 0.98331 0.06411  -0.02845 -0.03571 68  TRP B NE1 
2251 C CE2 . TRP B 68  ? 0.89805 0.92522 1.03231 0.06581  -0.03189 -0.04750 68  TRP B CE2 
2252 C CE3 . TRP B 68  ? 1.01968 1.06433 1.12910 0.07787  -0.03527 -0.06062 68  TRP B CE3 
2253 C CZ2 . TRP B 68  ? 0.91456 0.95815 1.06156 0.06004  -0.03437 -0.05844 68  TRP B CZ2 
2254 C CZ3 . TRP B 68  ? 1.06240 1.12752 1.18622 0.07140  -0.03853 -0.07287 68  TRP B CZ3 
2255 C CH2 . TRP B 68  ? 1.00218 1.06516 1.14451 0.06192  -0.03735 -0.07174 68  TRP B CH2 
2256 N N   . LYS B 69  ? 1.07922 1.04269 1.09788 0.10740  -0.01272 -0.02360 69  LYS B N   
2257 C CA  . LYS B 69  ? 1.12726 1.08268 1.12209 0.11624  -0.00818 -0.02454 69  LYS B CA  
2258 C C   . LYS B 69  ? 1.17072 1.13138 1.13741 0.13518  -0.01265 -0.02420 69  LYS B C   
2259 O O   . LYS B 69  ? 1.26748 1.23223 1.21676 0.14486  -0.01263 -0.02829 69  LYS B O   
2260 C CB  . LYS B 69  ? 1.16177 1.08905 1.14457 0.11194  0.00449  -0.01644 69  LYS B CB  
2261 C CG  . LYS B 69  ? 1.09796 1.02621 1.10562 0.09695  0.00893  -0.01905 69  LYS B CG  
2262 C CD  . LYS B 69  ? 1.11707 1.02349 1.11286 0.09247  0.02190  -0.01432 69  LYS B CD  
2263 C CE  . LYS B 69  ? 1.11776 1.03147 1.13835 0.08081  0.02508  -0.01835 69  LYS B CE  
2264 N NZ  . LYS B 69  ? 1.11931 1.01733 1.13015 0.07602  0.03786  -0.01656 69  LYS B NZ  
2265 N N   . ASN B 70  ? 1.16628 1.12886 1.12794 0.14187  -0.01668 -0.01970 70  ASN B N   
2266 C CA  . ASN B 70  ? 1.19086 1.16252 1.12694 0.16244  -0.02179 -0.01915 70  ASN B CA  
2267 C C   . ASN B 70  ? 1.13950 1.15144 1.09326 0.16439  -0.03495 -0.03154 70  ASN B C   
2268 O O   . ASN B 70  ? 1.12742 1.15367 1.07096 0.17813  -0.04122 -0.03126 70  ASN B O   
2269 C CB  . ASN B 70  ? 1.24472 1.19443 1.16317 0.16965  -0.01720 -0.00735 70  ASN B CB  
2270 C CG  . ASN B 70  ? 1.32291 1.23257 1.22301 0.16519  -0.00195 0.00278  70  ASN B CG  
2271 O OD1 . ASN B 70  ? 1.41505 1.31084 1.29989 0.16676  0.00559  0.00312  70  ASN B OD1 
2272 N ND2 . ASN B 70  ? 1.23299 1.12445 1.13410 0.15867  0.00352  0.01002  70  ASN B ND2 
2273 N N   . GLN B 71  ? 1.11951 1.14991 1.09948 0.15043  -0.03810 -0.04307 71  GLN B N   
2274 C CA  . GLN B 71  ? 1.15870 1.22651 1.15748 0.14764  -0.04795 -0.05750 71  GLN B CA  
2275 C C   . GLN B 71  ? 1.22960 1.31682 1.22511 0.14930  -0.04986 -0.07044 71  GLN B C   
2276 O O   . GLN B 71  ? 1.21439 1.28615 1.21104 0.14182  -0.04321 -0.07048 71  GLN B O   
2277 C CB  . GLN B 71  ? 1.17517 1.24598 1.20861 0.12709  -0.04782 -0.06155 71  GLN B CB  
2278 C CG  . GLN B 71  ? 1.04769 1.10349 1.08837 0.12330  -0.04670 -0.05053 71  GLN B CG  
2279 C CD  . GLN B 71  ? 1.03042 1.09997 1.05987 0.13691  -0.05336 -0.04883 71  GLN B CD  
2280 O OE1 . GLN B 71  ? 1.01382 1.06314 1.02337 0.14699  -0.05028 -0.03660 71  GLN B OE1 
2281 N NE2 . GLN B 71  ? 1.07503 1.17940 1.11622 0.13723  -0.06145 -0.06201 71  GLN B NE2 
2282 N N   . SER B 72  ? 1.30360 1.42731 1.29564 0.15895  -0.05891 -0.08239 72  SER B N   
2283 C CA  . SER B 72  ? 1.29779 1.44767 1.28600 0.16137  -0.06209 -0.09740 72  SER B CA  
2284 C C   . SER B 72  ? 1.31284 1.46037 1.32708 0.13858  -0.05702 -0.10767 72  SER B C   
2285 O O   . SER B 72  ? 1.31924 1.45537 1.35749 0.12222  -0.05354 -0.10611 72  SER B O   
2286 C CB  . SER B 72  ? 1.31281 1.51083 1.30271 0.17028  -0.07322 -0.11214 72  SER B CB  
2287 O OG  . SER B 72  ? 1.30764 1.52318 1.32941 0.15209  -0.07540 -0.12250 72  SER B OG  
2288 N N   . PRO B 73  ? 1.38974 1.54576 1.39805 0.13803  -0.05556 -0.11764 73  PRO B N   
2289 C CA  . PRO B 73  ? 1.39935 1.55208 1.43084 0.11700  -0.04941 -0.12834 73  PRO B CA  
2290 C C   . PRO B 73  ? 1.36530 1.54259 1.42404 0.10102  -0.05159 -0.14396 73  PRO B C   
2291 O O   . PRO B 73  ? 1.36305 1.52505 1.44232 0.08309  -0.04392 -0.14672 73  PRO B O   
2292 C CB  . PRO B 73  ? 1.45119 1.61533 1.46679 0.12272  -0.04902 -0.13818 73  PRO B CB  
2293 C CG  . PRO B 73  ? 1.46871 1.62080 1.45042 0.14584  -0.05041 -0.12401 73  PRO B CG  
2294 C CD  . PRO B 73  ? 1.43651 1.59727 1.41340 0.15734  -0.05711 -0.11683 73  PRO B CD  
2295 N N   . GLU B 74  ? 1.28927 1.50385 1.34782 0.10746  -0.06073 -0.15441 74  GLU B N   
2296 C CA  . GLU B 74  ? 1.24651 1.48302 1.33109 0.09073  -0.06121 -0.16927 74  GLU B CA  
2297 C C   . GLU B 74  ? 1.25464 1.46253 1.35468 0.08164  -0.05670 -0.15582 74  GLU B C   
2298 O O   . GLU B 74  ? 1.24893 1.44990 1.37046 0.06278  -0.04983 -0.16272 74  GLU B O   
2299 C CB  . GLU B 74  ? 1.21321 1.49796 1.29415 0.10143  -0.07236 -0.18185 74  GLU B CB  
2300 N N   . ALA B 75  ? 1.24594 1.43549 1.33339 0.09515  -0.05937 -0.13669 75  ALA B N   
2301 C CA  . ALA B 75  ? 1.22412 1.38787 1.32444 0.08766  -0.05558 -0.12355 75  ALA B CA  
2302 C C   . ALA B 75  ? 1.23026 1.35940 1.33865 0.07643  -0.04540 -0.11573 75  ALA B C   
2303 O O   . ALA B 75  ? 1.18077 1.29792 1.30830 0.06293  -0.04003 -0.11512 75  ALA B O   
2304 C CB  . ALA B 75  ? 1.23457 1.38746 1.31686 0.10462  -0.05981 -0.10658 75  ALA B CB  
2305 N N   . ARG B 76  ? 1.24590 1.35903 1.33880 0.08300  -0.04210 -0.10955 76  ARG B N   
2306 C CA  . ARG B 76  ? 1.19866 1.28317 1.29918 0.07396  -0.03263 -0.10284 76  ARG B CA  
2307 C C   . ARG B 76  ? 1.18817 1.27635 1.30440 0.05938  -0.02635 -0.11735 76  ARG B C   
2308 O O   . ARG B 76  ? 1.18305 1.24913 1.30469 0.05349  -0.01787 -0.11302 76  ARG B O   
2309 C CB  . ARG B 76  ? 1.15008 1.21764 1.22950 0.08417  -0.02971 -0.09357 76  ARG B CB  
2310 N N   . LYS B 77  ? 1.18649 1.30241 1.30930 0.05345  -0.02926 -0.13524 77  LYS B N   
2311 C CA  . LYS B 77  ? 1.15838 1.27425 1.29575 0.03689  -0.02057 -0.15041 77  LYS B CA  
2312 C C   . LYS B 77  ? 1.13613 1.22813 1.29060 0.02592  -0.01229 -0.14382 77  LYS B C   
2313 O O   . LYS B 77  ? 1.09594 1.16827 1.25726 0.01664  -0.00125 -0.14628 77  LYS B O   
2314 C CB  . LYS B 77  ? 1.13777 1.29139 1.27965 0.03060  -0.02457 -0.17283 77  LYS B CB  
2315 N N   . ASN B 78  ? 1.13826 1.23073 1.29793 0.02833  -0.01695 -0.13486 78  ASN B N   
2316 C CA  . ASN B 78  ? 1.11094 1.18300 1.28518 0.01943  -0.00962 -0.12864 78  ASN B CA  
2317 C C   . ASN B 78  ? 1.06403 1.10543 1.23802 0.02193  -0.00242 -0.11394 78  ASN B C   
2318 O O   . ASN B 78  ? 1.04781 1.07063 1.23049 0.01414  0.00827  -0.11459 78  ASN B O   
2319 C CB  . ASN B 78  ? 1.04835 1.12753 1.22579 0.02358  -0.01706 -0.12047 78  ASN B CB  
2320 N N   . ILE B 79  ? 1.05278 1.08879 1.21565 0.03316  -0.00696 -0.10131 79  ILE B N   
2321 C CA  . ILE B 79  ? 1.00751 1.02053 1.17249 0.03565  -0.00138 -0.08708 79  ILE B CA  
2322 C C   . ILE B 79  ? 0.99250 0.99316 1.15685 0.03336  0.00781  -0.09072 79  ILE B C   
2323 O O   . ILE B 79  ? 0.91335 0.89732 1.08256 0.03471  0.01407  -0.08120 79  ILE B O   
2324 C CB  . ILE B 79  ? 0.93815 0.94952 1.09152 0.04593  -0.00743 -0.07393 79  ILE B CB  
2325 N N   . ALA B 80  ? 1.01779 1.02806 1.17632 0.03045  0.00891  -0.10477 80  ALA B N   
2326 C CA  . ALA B 80  ? 1.01143 1.01015 1.16627 0.02975  0.01714  -0.10785 80  ALA B CA  
2327 C C   . ALA B 80  ? 1.01431 0.99440 1.18013 0.02155  0.02991  -0.11102 80  ALA B C   
2328 O O   . ALA B 80  ? 1.02942 1.01149 1.20172 0.01186  0.03400  -0.12204 80  ALA B O   
2329 C CB  . ALA B 80  ? 0.99482 1.01097 1.13900 0.02910  0.01442  -0.12291 80  ALA B CB  
2330 N N   . PRO B 81  ? 0.86984 0.83113 1.03664 0.02558  0.03781  -0.10220 81  PRO B N   
2331 C CA  . PRO B 81  ? 0.86513 0.80501 1.03924 0.02173  0.05120  -0.10234 81  PRO B CA  
2332 C C   . PRO B 81  ? 0.91680 0.85186 1.09035 0.00994  0.06101  -0.12034 81  PRO B C   
2333 O O   . PRO B 81  ? 1.02074 0.97231 1.18887 0.00475  0.05740  -0.13442 81  PRO B O   
2334 C CB  . PRO B 81  ? 0.75391 0.68221 0.92575 0.03008  0.05656  -0.09317 81  PRO B CB  
2335 C CG  . PRO B 81  ? 0.79641 0.73740 0.96486 0.03732  0.04578  -0.08295 81  PRO B CG  
2336 C CD  . PRO B 81  ? 0.85347 0.81261 1.01426 0.03482  0.03540  -0.09077 81  PRO B CD  
2337 N N   . SER B 82  ? 0.90900 0.82118 1.08666 0.00579  0.07456  -0.12064 82  SER B N   
2338 C CA  . SER B 82  ? 0.95714 0.86266 1.13438 -0.00870 0.08592  -0.13901 82  SER B CA  
2339 C C   . SER B 82  ? 1.08878 0.95849 1.26481 -0.00886 0.10495  -0.13532 82  SER B C   
2340 O O   . SER B 82  ? 1.13106 0.98634 1.30837 0.00323  0.10682  -0.11799 82  SER B O   
2341 C CB  . SER B 82  ? 0.95649 0.87990 1.13958 -0.01797 0.07973  -0.14740 82  SER B CB  
2342 O OG  . SER B 82  ? 0.95297 0.86882 1.13690 -0.03416 0.09317  -0.16588 82  SER B OG  
2343 N N   . ASP B 83  ? 1.26224 1.11804 1.43431 -0.02206 0.11994  -0.15235 83  ASP B N   
2344 C CA  . ASP B 83  ? 1.31463 1.13093 1.48150 -0.02261 0.14132  -0.15015 83  ASP B CA  
2345 C C   . ASP B 83  ? 1.24664 1.05035 1.41604 -0.03044 0.14882  -0.15132 83  ASP B C   
2346 O O   . ASP B 83  ? 1.24864 1.01615 1.41142 -0.02780 0.16673  -0.14552 83  ASP B O   
2347 C CB  . ASP B 83  ? 1.39388 1.19515 1.55250 -0.03385 0.15739  -0.16828 83  ASP B CB  
2348 C CG  . ASP B 83  ? 1.45775 1.26741 1.61238 -0.02478 0.15191  -0.16583 83  ASP B CG  
2349 O OD1 . ASP B 83  ? 1.43946 1.25438 1.59613 -0.00823 0.14220  -0.14758 83  ASP B OD1 
2350 O OD2 . ASP B 83  ? 1.54334 1.35489 1.69261 -0.03506 0.15818  -0.18316 83  ASP B OD2 
2351 N N   . GLU B 84  ? 1.15604 0.98825 1.33348 -0.03833 0.13587  -0.15773 84  GLU B N   
2352 C CA  . GLU B 84  ? 1.11298 0.93768 1.29409 -0.04551 0.14080  -0.15817 84  GLU B CA  
2353 C C   . GLU B 84  ? 1.06194 0.88495 1.24656 -0.02956 0.13135  -0.13498 84  GLU B C   
2354 O O   . GLU B 84  ? 1.06561 0.87608 1.25122 -0.03265 0.13739  -0.13193 84  GLU B O   
2355 C CB  . GLU B 84  ? 1.09162 0.95178 1.28058 -0.06093 0.13114  -0.17694 84  GLU B CB  
2356 C CG  . GLU B 84  ? 1.08352 0.98155 1.27858 -0.05064 0.10626  -0.16878 84  GLU B CG  
2357 C CD  . GLU B 84  ? 1.15411 1.09160 1.35466 -0.06238 0.09622  -0.18845 84  GLU B CD  
2358 O OE1 . GLU B 84  ? 1.19335 1.13326 1.39474 -0.08035 0.10801  -0.21073 84  GLU B OE1 
2359 O OE2 . GLU B 84  ? 1.14726 1.11399 1.35059 -0.05344 0.07737  -0.18225 84  GLU B OE2 
2360 N N   . ASP B 85  ? 1.00306 0.83742 1.18889 -0.01346 0.11830  -0.11945 85  ASP B N   
2361 C CA  . ASP B 85  ? 0.98761 0.82440 1.17728 0.00046  0.10918  -0.09933 85  ASP B CA  
2362 C C   . ASP B 85  ? 0.98905 0.79225 1.17353 0.00707  0.12475  -0.08862 85  ASP B C   
2363 O O   . ASP B 85  ? 1.03841 0.81097 1.21400 0.00348  0.14432  -0.09438 85  ASP B O   
2364 C CB  . ASP B 85  ? 0.92403 0.77402 1.11450 0.01501  0.09786  -0.08658 85  ASP B CB  
2365 C CG  . ASP B 85  ? 0.89812 0.77867 1.09044 0.01166  0.08219  -0.09341 85  ASP B CG  
2366 O OD1 . ASP B 85  ? 0.86263 0.75872 1.05686 0.00075  0.07737  -0.10604 85  ASP B OD1 
2367 O OD2 . ASP B 85  ? 0.91088 0.80097 1.10202 0.02081  0.07476  -0.08572 85  ASP B OD2 
2368 N N   . VAL B 86  ? 1.01496 0.82251 1.20307 0.01675  0.11719  -0.07350 86  VAL B N   
2369 C CA  . VAL B 86  ? 1.01824 0.79780 1.19971 0.02812  0.12946  -0.05998 86  VAL B CA  
2370 C C   . VAL B 86  ? 1.00445 0.80227 1.19123 0.04498  0.11521  -0.04150 86  VAL B C   
2371 O O   . VAL B 86  ? 0.95723 0.78530 1.15253 0.04417  0.09755  -0.04041 86  VAL B O   
2372 C CB  . VAL B 86  ? 0.98253 0.74542 1.16150 0.01754  0.13927  -0.06483 86  VAL B CB  
2373 C CG1 . VAL B 86  ? 1.02288 0.77019 1.19744 -0.00202 0.15489  -0.08583 86  VAL B CG1 
2374 C CG2 . VAL B 86  ? 0.96929 0.76232 1.15922 0.01290  0.12123  -0.06402 86  VAL B CG2 
2375 N N   . SER B 87  ? 0.98044 0.75937 1.16056 0.06076  0.12417  -0.02742 87  SER B N   
2376 C CA  . SER B 87  ? 0.90448 0.70196 1.08962 0.07534  0.11225  -0.01149 87  SER B CA  
2377 C C   . SER B 87  ? 0.88789 0.69280 1.07731 0.06815  0.10501  -0.01057 87  SER B C   
2378 O O   . SER B 87  ? 0.90530 0.69261 1.09096 0.05622  0.11432  -0.01899 87  SER B O   
2379 C CB  . SER B 87  ? 0.88908 0.66670 1.06434 0.09603  0.12427  0.00257  87  SER B CB  
2380 O OG  . SER B 87  ? 0.89380 0.63853 1.05744 0.09563  0.13989  0.00403  87  SER B OG  
2381 N N   . THR B 88  ? 0.85520 0.68681 1.05254 0.07439  0.08920  -0.00135 88  THR B N   
2382 C CA  . THR B 88  ? 0.77464 0.61226 0.97514 0.06966  0.08286  0.00113  88  THR B CA  
2383 C C   . THR B 88  ? 0.86602 0.67367 1.05618 0.07539  0.09806  0.00727  88  THR B C   
2384 O O   . THR B 88  ? 0.89418 0.69463 1.08399 0.06533  0.10032  0.00316  88  THR B O   
2385 C CB  . THR B 88  ? 0.66566 0.53303 0.87404 0.07684  0.06626  0.01085  88  THR B CB  
2386 O OG1 . THR B 88  ? 0.71101 0.58382 0.91831 0.09342  0.06740  0.02108  88  THR B OG1 
2387 C CG2 . THR B 88  ? 0.63410 0.52549 0.84967 0.06691  0.05258  0.00343  88  THR B CG2 
2388 N N   . ILE B 89  ? 0.84675 0.63538 1.02681 0.09212  0.10991  0.01684  89  ILE B N   
2389 C CA  . ILE B 89  ? 0.85490 0.60856 1.02006 0.09981  0.12753  0.02350  89  ILE B CA  
2390 C C   . ILE B 89  ? 0.94954 0.67009 1.10661 0.08285  0.14570  0.00925  89  ILE B C   
2391 O O   . ILE B 89  ? 0.94322 0.64240 1.09348 0.07574  0.15611  0.00738  89  ILE B O   
2392 C CB  . ILE B 89  ? 0.86663 0.60772 1.02011 0.12495  0.13681  0.03748  89  ILE B CB  
2393 C CG1 . ILE B 89  ? 0.88660 0.66736 1.05033 0.13987  0.11907  0.04806  89  ILE B CG1 
2394 C CG2 . ILE B 89  ? 0.89510 0.60195 1.03079 0.13590  0.15324  0.04696  89  ILE B CG2 
2395 C CD1 . ILE B 89  ? 0.86647 0.67019 1.03962 0.14062  0.11154  0.04362  89  ILE B CD1 
2396 N N   . ASP B 90  ? 1.04360 0.75978 1.20097 0.07521  0.15082  -0.00206 90  ASP B N   
2397 C CA  . ASP B 90  ? 1.06237 0.75187 1.21342 0.05622  0.16804  -0.01903 90  ASP B CA  
2398 C C   . ASP B 90  ? 1.05861 0.76956 1.22194 0.03393  0.15842  -0.03376 90  ASP B C   
2399 O O   . ASP B 90  ? 1.03703 0.72790 1.19570 0.01792  0.17293  -0.04599 90  ASP B O   
2400 C CB  . ASP B 90  ? 1.05804 0.74369 1.20756 0.05372  0.17342  -0.02810 90  ASP B CB  
2401 C CG  . ASP B 90  ? 1.09085 0.74715 1.22487 0.07477  0.18897  -0.01604 90  ASP B CG  
2402 O OD1 . ASP B 90  ? 1.08038 0.70208 1.19817 0.08548  0.20594  -0.00653 90  ASP B OD1 
2403 O OD2 . ASP B 90  ? 1.03928 0.70699 1.17615 0.08169  0.18471  -0.01580 90  ASP B OD2 
2404 N N   . GLY B 91  ? 1.05464 0.80651 1.23277 0.03281  0.13511  -0.03345 91  GLY B N   
2405 C CA  . GLY B 91  ? 1.01617 0.79200 1.20508 0.01572  0.12445  -0.04581 91  GLY B CA  
2406 C C   . GLY B 91  ? 1.01705 0.78690 1.20558 0.01335  0.12623  -0.04135 91  GLY B C   
2407 O O   . GLY B 91  ? 1.03270 0.80568 1.22507 -0.00370 0.12946  -0.05518 91  GLY B O   
2408 N N   . ILE B 92  ? 0.93215 0.69654 1.11646 0.03040  0.12380  -0.02284 92  ILE B N   
2409 C CA  . ILE B 92  ? 0.94851 0.70570 1.13077 0.02952  0.12598  -0.01747 92  ILE B CA  
2410 C C   . ILE B 92  ? 0.97960 0.69288 1.14673 0.02435  0.15199  -0.02113 92  ILE B C   
2411 O O   . ILE B 92  ? 0.97089 0.67566 1.13670 0.01507  0.15791  -0.02437 92  ILE B O   
2412 C CB  . ILE B 92  ? 0.94882 0.71638 1.13037 0.04955  0.11523  0.00255  92  ILE B CB  
2413 C CG1 . ILE B 92  ? 0.88103 0.65289 1.06445 0.04627  0.11106  0.00632  92  ILE B CG1 
2414 C CG2 . ILE B 92  ? 0.95804 0.69631 1.12380 0.06907  0.13004  0.01592  92  ILE B CG2 
2415 C CD1 . ILE B 92  ? 0.82767 0.63164 1.02577 0.03169  0.09483  -0.00410 92  ILE B CD1 
2416 N N   . ALA B 93  ? 1.00748 0.69027 1.16170 0.02978  0.16939  -0.02106 93  ALA B N   
2417 C CA  . ALA B 93  ? 1.04286 0.67865 1.17984 0.02256  0.19752  -0.02658 93  ALA B CA  
2418 C C   . ALA B 93  ? 1.05488 0.69338 1.19884 -0.00642 0.20489  -0.05158 93  ALA B C   
2419 O O   . ALA B 93  ? 1.10870 0.72612 1.24682 -0.01978 0.22040  -0.05917 93  ALA B O   
2420 C CB  . ALA B 93  ? 1.04718 0.64757 1.16641 0.03718  0.21551  -0.01985 93  ALA B CB  
2421 N N   . LYS B 94  ? 1.01849 0.68471 1.17462 -0.01645 0.19432  -0.06540 94  LYS B N   
2422 C CA  . LYS B 94  ? 1.01557 0.69578 1.18064 -0.04303 0.19773  -0.09074 94  LYS B CA  
2423 C C   . LYS B 94  ? 1.02118 0.73015 1.19914 -0.05290 0.18521  -0.09537 94  LYS B C   
2424 O O   . LYS B 94  ? 0.99461 0.70287 1.17538 -0.07414 0.19614  -0.11390 94  LYS B O   
2425 C CB  . LYS B 94  ? 1.01074 0.72152 1.18577 -0.04701 0.18464  -0.10176 94  LYS B CB  
2426 C CG  . LYS B 94  ? 1.09897 0.77947 1.26135 -0.04366 0.20142  -0.10373 94  LYS B CG  
2427 C CD  . LYS B 94  ? 1.12682 0.83788 1.29791 -0.04435 0.18698  -0.11161 94  LYS B CD  
2428 C CE  . LYS B 94  ? 1.18519 0.86530 1.34377 -0.04576 0.20648  -0.11828 94  LYS B CE  
2429 N NZ  . LYS B 94  ? 1.21082 0.85541 1.35444 -0.02276 0.21720  -0.09734 94  LYS B NZ  
2430 N N   . PHE B 95  ? 0.99703 0.73230 1.18289 -0.03825 0.16309  -0.07963 95  PHE B N   
2431 C CA  . PHE B 95  ? 0.91827 0.67916 1.11489 -0.04444 0.15082  -0.08131 95  PHE B CA  
2432 C C   . PHE B 95  ? 0.96611 0.69550 1.15311 -0.04798 0.16829  -0.07762 95  PHE B C   
2433 O O   . PHE B 95  ? 0.95611 0.69751 1.15040 -0.06362 0.16937  -0.08969 95  PHE B O   
2434 C CB  . PHE B 95  ? 0.88109 0.67138 1.08524 -0.02740 0.12589  -0.06456 95  PHE B CB  
2435 C CG  . PHE B 95  ? 0.83094 0.64423 1.04405 -0.03112 0.11378  -0.06388 95  PHE B CG  
2436 C CD1 . PHE B 95  ? 0.76950 0.61566 0.99476 -0.04531 0.10442  -0.08080 95  PHE B CD1 
2437 C CD2 . PHE B 95  ? 0.79598 0.59959 1.00462 -0.01940 0.11192  -0.04675 95  PHE B CD2 
2438 C CE1 . PHE B 95  ? 0.68116 0.54792 0.91390 -0.04771 0.09430  -0.08041 95  PHE B CE1 
2439 C CE2 . PHE B 95  ? 0.80628 0.62951 1.02250 -0.02327 0.10184  -0.04673 95  PHE B CE2 
2440 C CZ  . PHE B 95  ? 0.76361 0.61781 0.99200 -0.03740 0.09317  -0.06345 95  PHE B CZ  
2441 N N   . ASN B 96  ? 1.04698 0.73751 1.21685 -0.03227 0.18194  -0.06062 96  ASN B N   
2442 C CA  . ASN B 96  ? 1.10378 0.76101 1.26120 -0.03496 0.20032  -0.05690 96  ASN B CA  
2443 C C   . ASN B 96  ? 1.15550 0.77934 1.30357 -0.05672 0.22880  -0.07654 96  ASN B C   
2444 O O   . ASN B 96  ? 1.15362 0.76124 1.29758 -0.06996 0.24310  -0.08334 96  ASN B O   
2445 C CB  . ASN B 96  ? 1.14093 0.76718 1.27990 -0.00898 0.20690  -0.03217 96  ASN B CB  
2446 C CG  . ASN B 96  ? 1.15855 0.81899 1.30674 0.01035  0.18070  -0.01469 96  ASN B CG  
2447 O OD1 . ASN B 96  ? 1.13390 0.83154 1.29845 0.00416  0.16101  -0.01780 96  ASN B OD1 
2448 N ND2 . ASN B 96  ? 1.21767 0.86554 1.35429 0.03441  0.18153  0.00353  96  ASN B ND2 
2449 N N   . ASP B 97  ? 1.15493 0.76736 1.29897 -0.06162 0.23858  -0.08655 97  ASP B N   
2450 C CA  . ASP B 97  ? 1.16373 0.75209 1.30194 -0.08686 0.26425  -0.11019 97  ASP B CA  
2451 C C   . ASP B 97  ? 1.14341 0.77219 1.30173 -0.11262 0.25645  -0.13380 97  ASP B C   
2452 O O   . ASP B 97  ? 1.14687 0.75799 1.30145 -0.13294 0.27675  -0.14865 97  ASP B O   
2453 C CB  . ASP B 97  ? 1.17619 0.75732 1.31080 -0.08834 0.27038  -0.11868 97  ASP B CB  
2454 C CG  . ASP B 97  ? 1.23222 0.76628 1.34361 -0.06472 0.28522  -0.09861 97  ASP B CG  
2455 O OD1 . ASP B 97  ? 1.28286 0.77614 1.37499 -0.05310 0.30170  -0.08393 97  ASP B OD1 
2456 O OD2 . ASP B 97  ? 1.23864 0.77646 1.34982 -0.05683 0.28120  -0.09774 97  ASP B OD2 
2457 N N   . TYR B 98  ? 1.01310 0.69683 1.19191 -0.11135 0.22784  -0.13772 98  TYR B N   
2458 C CA  . TYR B 98  ? 0.96002 0.68803 1.15767 -0.13173 0.21825  -0.15940 98  TYR B CA  
2459 C C   . TYR B 98  ? 1.00177 0.73029 1.20179 -0.13424 0.21855  -0.15461 98  TYR B C   
2460 O O   . TYR B 98  ? 1.01170 0.74511 1.21684 -0.15682 0.23104  -0.17474 98  TYR B O   
2461 C CB  . TYR B 98  ? 0.93072 0.71330 1.14509 -0.12367 0.18731  -0.15973 98  TYR B CB  
2462 C CG  . TYR B 98  ? 0.88721 0.71926 1.11941 -0.14147 0.17701  -0.18290 98  TYR B CG  
2463 C CD1 . TYR B 98  ? 0.83056 0.68112 1.06840 -0.16080 0.18375  -0.20967 98  TYR B CD1 
2464 C CD2 . TYR B 98  ? 0.86616 0.72720 1.10891 -0.13888 0.16178  -0.17902 98  TYR B CD2 
2465 C CE1 . TYR B 98  ? 0.81408 0.71483 1.06810 -0.17548 0.17425  -0.23193 98  TYR B CE1 
2466 C CE2 . TYR B 98  ? 0.83627 0.74481 1.09474 -0.15318 0.15294  -0.20053 98  TYR B CE2 
2467 C CZ  . TYR B 98  ? 0.82644 0.75645 1.09073 -0.17103 0.15895  -0.22720 98  TYR B CZ  
2468 O OH  . TYR B 98  ? 0.79976 0.78290 1.07985 -0.18377 0.14965  -0.24991 98  TYR B OH  
2469 N N   . ILE B 99  ? 0.98142 0.70618 1.17789 -0.11199 0.20556  -0.12909 99  ILE B N   
2470 C CA  . ILE B 99  ? 0.98823 0.71719 1.18752 -0.11303 0.20318  -0.12374 99  ILE B CA  
2471 C C   . ILE B 99  ? 1.04441 0.72610 1.22824 -0.12656 0.23489  -0.12963 99  ILE B C   
2472 O O   . ILE B 99  ? 1.04946 0.74122 1.24035 -0.14428 0.24097  -0.14341 99  ILE B O   
2473 C CB  . ILE B 99  ? 0.98051 0.71183 1.17675 -0.08661 0.18514  -0.09560 99  ILE B CB  
2474 C CG1 . ILE B 99  ? 0.91847 0.69686 1.12981 -0.07657 0.15532  -0.09195 99  ILE B CG1 
2475 C CG2 . ILE B 99  ? 0.89744 0.62816 1.09408 -0.08761 0.18511  -0.08972 99  ILE B CG2 
2476 C CD1 . ILE B 99  ? 0.83152 0.65683 1.06105 -0.08901 0.13999  -0.10750 99  ILE B CD1 
2477 N N   . ASN B 100 ? 1.04261 0.67107 1.20386 -0.11835 0.25704  -0.11980 100 ASN B N   
2478 C CA  . ASN B 100 ? 1.09065 0.66732 1.23256 -0.12977 0.28999  -0.12383 100 ASN B CA  
2479 C C   . ASN B 100 ? 1.09220 0.66797 1.23892 -0.16311 0.31063  -0.15616 100 ASN B C   
2480 O O   . ASN B 100 ? 1.12329 0.67452 1.26275 -0.18111 0.33375  -0.16703 100 ASN B O   
2481 C CB  . ASN B 100 ? 1.17381 0.69088 1.28655 -0.10955 0.31011  -0.10402 100 ASN B CB  
2482 C CG  . ASN B 100 ? 1.26498 0.78494 1.37217 -0.07696 0.29182  -0.07351 100 ASN B CG  
2483 O OD1 . ASN B 100 ? 1.32597 0.84512 1.42860 -0.05627 0.28332  -0.05962 100 ASN B OD1 
2484 N ND2 . ASN B 100 ? 1.17804 0.70568 1.28695 -0.07293 0.28488  -0.06425 100 ASN B ND2 
2485 N N   . ALA B 101 ? 1.09721 0.70097 1.25599 -0.17258 0.30320  -0.17290 101 ALA B N   
2486 C CA  . ALA B 101 ? 1.04665 0.65450 1.21065 -0.20500 0.32246  -0.20599 101 ALA B CA  
2487 C C   . ALA B 101 ? 1.00522 0.67184 1.19488 -0.22557 0.30896  -0.22860 101 ALA B C   
2488 O O   . ALA B 101 ? 1.03696 0.71215 1.23257 -0.25490 0.32598  -0.25867 101 ALA B O   
2489 C CB  . ALA B 101 ? 1.03236 0.64854 1.19806 -0.20663 0.32022  -0.21596 101 ALA B CB  
2490 N N   . HIS B 102 ? 0.99372 0.70187 1.19830 -0.21160 0.28017  -0.21641 102 HIS B N   
2491 C CA  . HIS B 102 ? 0.93187 0.70122 1.16088 -0.22750 0.26503  -0.23771 102 HIS B CA  
2492 C C   . HIS B 102 ? 0.94115 0.71494 1.17363 -0.22538 0.26144  -0.22911 102 HIS B C   
2493 O O   . HIS B 102 ? 0.91054 0.73397 1.16026 -0.21892 0.23598  -0.22783 102 HIS B O   
2494 C CB  . HIS B 102 ? 0.90642 0.73253 1.15216 -0.21492 0.23212  -0.23719 102 HIS B CB  
2495 C CG  . HIS B 102 ? 0.92651 0.76419 1.17436 -0.22539 0.23574  -0.25623 102 HIS B CG  
2496 N ND1 . HIS B 102 ? 0.96508 0.77304 1.19979 -0.21172 0.23793  -0.24333 102 HIS B ND1 
2497 C CD2 . HIS B 102 ? 0.88848 0.76495 1.14965 -0.24884 0.23877  -0.28847 102 HIS B CD2 
2498 C CE1 . HIS B 102 ? 0.95329 0.77926 1.19266 -0.22627 0.24185  -0.26606 102 HIS B CE1 
2499 N NE2 . HIS B 102 ? 0.93733 0.80587 1.19267 -0.24893 0.24219  -0.29398 102 HIS B NE2 
2500 N N   . ASN B 103 ? 1.01714 0.73657 1.23129 -0.23110 0.28900  -0.22384 103 ASN B N   
2501 C CA  . ASN B 103 ? 1.03073 0.74911 1.24665 -0.23708 0.29398  -0.22264 103 ASN B CA  
2502 C C   . ASN B 103 ? 1.00731 0.75886 1.23320 -0.21302 0.26175  -0.20052 103 ASN B C   
2503 O O   . ASN B 103 ? 0.97494 0.76855 1.21791 -0.21916 0.24871  -0.20880 103 ASN B O   
2504 C CB  . ASN B 103 ? 0.99660 0.74946 1.22986 -0.27048 0.30470  -0.25814 103 ASN B CB  
2505 N N   . ILE B 104 ? 1.03625 0.76984 1.25117 -0.18549 0.24933  -0.17307 104 ILE B N   
2506 C CA  . ILE B 104 ? 1.02519 0.78267 1.24589 -0.16215 0.22153  -0.15061 104 ILE B CA  
2507 C C   . ILE B 104 ? 1.06799 0.78092 1.26967 -0.15007 0.23358  -0.12900 104 ILE B C   
2508 O O   . ILE B 104 ? 1.11191 0.77397 1.29127 -0.14076 0.25197  -0.11636 104 ILE B O   
2509 C CB  . ILE B 104 ? 0.97779 0.74908 1.19962 -0.14076 0.19994  -0.13602 104 ILE B CB  
2510 C CG1 . ILE B 104 ? 0.93789 0.75328 1.17637 -0.15149 0.18814  -0.15716 104 ILE B CG1 
2511 C CG2 . ILE B 104 ? 0.96173 0.75501 1.18812 -0.11896 0.17400  -0.11432 104 ILE B CG2 
2512 C CD1 . ILE B 104 ? 0.90330 0.77596 1.16263 -0.15880 0.16937  -0.17079 104 ILE B CD1 
2513 N N   . ASP B 105 ? 1.15365 0.88582 1.36283 -0.14919 0.22384  -0.12494 105 ASP B N   
2514 C CA  . ASP B 105 ? 1.18362 0.87897 1.37569 -0.13924 0.23452  -0.10647 105 ASP B CA  
2515 C C   . ASP B 105 ? 1.18842 0.88851 1.37588 -0.10956 0.21229  -0.07834 105 ASP B C   
2516 O O   . ASP B 105 ? 1.16993 0.91495 1.37418 -0.10282 0.18535  -0.07598 105 ASP B O   
2517 C CB  . ASP B 105 ? 1.18053 0.89605 1.38371 -0.15516 0.23616  -0.11840 105 ASP B CB  
2518 C CG  . ASP B 105 ? 1.20804 0.88241 1.39192 -0.14855 0.25144  -0.10248 105 ASP B CG  
2519 O OD1 . ASP B 105 ? 1.25377 0.88988 1.41611 -0.12742 0.25624  -0.07938 105 ASP B OD1 
2520 O OD2 . ASP B 105 ? 1.22444 0.90572 1.41413 -0.16468 0.25976  -0.11412 105 ASP B OD2 
2521 N N   . PRO B 106 ? 1.11590 0.77223 1.28023 -0.09104 0.22321  -0.05747 106 PRO B N   
2522 C CA  . PRO B 106 ? 1.06248 0.72949 1.22398 -0.06378 0.20185  -0.03317 106 PRO B CA  
2523 C C   . PRO B 106 ? 1.02632 0.72201 1.19733 -0.05913 0.18354  -0.02581 106 PRO B C   
2524 O O   . PRO B 106 ? 1.01637 0.74076 1.19507 -0.04413 0.15967  -0.01425 106 PRO B O   
2525 C CB  . PRO B 106 ? 1.12900 0.74211 1.26142 -0.04643 0.22223  -0.01494 106 PRO B CB  
2526 C CG  . PRO B 106 ? 1.15335 0.72754 1.27415 -0.06316 0.25200  -0.03019 106 PRO B CG  
2527 C CD  . PRO B 106 ? 1.13457 0.73055 1.27301 -0.09317 0.25625  -0.05587 106 PRO B CD  
2528 N N   . TRP B 107 ? 1.00354 0.69213 1.17404 -0.07263 0.19498  -0.03319 107 TRP B N   
2529 C CA  . TRP B 107 ? 0.95563 0.66568 1.13219 -0.06768 0.18056  -0.02529 107 TRP B CA  
2530 C C   . TRP B 107 ? 0.89760 0.65363 1.09826 -0.08442 0.16735  -0.04369 107 TRP B C   
2531 O O   . TRP B 107 ? 0.81153 0.59964 1.02234 -0.07601 0.14542  -0.03708 107 TRP B O   
2532 C CB  . TRP B 107 ? 0.96305 0.63186 1.11936 -0.06693 0.20213  -0.01718 107 TRP B CB  
2533 C CG  . TRP B 107 ? 0.98145 0.61561 1.11370 -0.04226 0.20767  0.00603  107 TRP B CG  
2534 C CD1 . TRP B 107 ? 1.04597 0.63442 1.15630 -0.03627 0.23016  0.01060  107 TRP B CD1 
2535 C CD2 . TRP B 107 ? 0.91440 0.55932 1.04133 -0.01876 0.19040  0.02746  107 TRP B CD2 
2536 N NE1 . TRP B 107 ? 1.01673 0.58907 1.10840 -0.00821 0.22696  0.03442  107 TRP B NE1 
2537 C CE2 . TRP B 107 ? 0.91409 0.52263 1.01648 0.00205  0.20234  0.04426  107 TRP B CE2 
2538 C CE3 . TRP B 107 ? 0.87395 0.55623 1.01371 -0.01328 0.16677  0.03332  107 TRP B CE3 
2539 C CZ2 . TRP B 107 ? 0.87887 0.49257 0.97096 0.02777  0.19032  0.06548  107 TRP B CZ2 
2540 C CZ3 . TRP B 107 ? 0.83614 0.52061 0.96558 0.00991  0.15583  0.05370  107 TRP B CZ3 
2541 C CH2 . TRP B 107 ? 0.88022 0.53322 0.98686 0.03019  0.16696  0.06911  107 TRP B CH2 
2542 N N   . LYS B 108 ? 0.95329 0.71465 1.16271 -0.10742 0.18061  -0.06730 108 LYS B N   
2543 C CA  . LYS B 108 ? 0.94222 0.75030 1.17376 -0.12195 0.16935  -0.08566 108 LYS B CA  
2544 C C   . LYS B 108 ? 0.90223 0.75401 1.15094 -0.12202 0.14966  -0.09638 108 LYS B C   
2545 O O   . LYS B 108 ? 0.85568 0.75091 1.11979 -0.12116 0.13073  -0.10160 108 LYS B O   
2546 C CB  . LYS B 108 ? 1.00238 0.80009 1.23577 -0.14825 0.19442  -0.10811 108 LYS B CB  
2547 C CG  . LYS B 108 ? 1.05613 0.81744 1.27418 -0.14959 0.21242  -0.09919 108 LYS B CG  
2548 C CD  . LYS B 108 ? 1.13103 0.86964 1.34569 -0.17717 0.24394  -0.12114 108 LYS B CD  
2549 C CE  . LYS B 108 ? 1.16690 0.95602 1.40677 -0.19882 0.23940  -0.14709 108 LYS B CE  
2550 N NZ  . LYS B 108 ? 1.16432 0.93183 1.40095 -0.22758 0.27188  -0.16933 108 LYS B NZ  
2551 N N   . SER B 109 ? 0.95152 0.79136 1.19592 -0.12122 0.15405  -0.09877 109 SER B N   
2552 C CA  . SER B 109 ? 0.90605 0.78463 1.16458 -0.12244 0.13816  -0.11053 109 SER B CA  
2553 C C   . SER B 109 ? 0.88005 0.78456 1.14260 -0.10164 0.11064  -0.09441 109 SER B C   
2554 O O   . SER B 109 ? 0.87760 0.76334 1.12969 -0.08452 0.10512  -0.07248 109 SER B O   
2555 C CB  . SER B 109 ? 0.89900 0.75417 1.14982 -0.12588 0.15078  -0.11554 109 SER B CB  
2556 O OG  . SER B 109 ? 0.96547 0.80382 1.21484 -0.14908 0.17603  -0.13620 109 SER B OG  
2557 N N   . GLN B 110 ? 0.79421 0.74253 1.07082 -0.10329 0.09450  -0.10652 110 GLN B N   
2558 C CA  . GLN B 110 ? 0.75610 0.72976 1.03553 -0.08591 0.07046  -0.09481 110 GLN B CA  
2559 C C   . GLN B 110 ? 0.77435 0.75735 1.05422 -0.08179 0.06380  -0.09842 110 GLN B C   
2560 O O   . GLN B 110 ? 0.75485 0.74686 1.03983 -0.09496 0.07178  -0.11737 110 GLN B O   
2561 C CB  . GLN B 110 ? 0.74009 0.75556 1.03165 -0.08730 0.05725  -0.10371 110 GLN B CB  
2562 C CG  . GLN B 110 ? 0.78773 0.79435 1.07770 -0.08701 0.06002  -0.09552 110 GLN B CG  
2563 C CD  . GLN B 110 ? 0.74861 0.79580 1.05052 -0.08910 0.04964  -0.10588 110 GLN B CD  
2564 O OE1 . GLN B 110 ? 0.69932 0.78423 1.01105 -0.09120 0.04127  -0.12118 110 GLN B OE1 
2565 N NE2 . GLN B 110 ? 0.75834 0.79905 1.05849 -0.08713 0.05019  -0.09747 110 GLN B NE2 
2566 N N   . GLY B 111 ? 0.75732 0.73837 1.03150 -0.06440 0.05002  -0.08103 111 GLY B N   
2567 C CA  . GLY B 111 ? 0.68672 0.67577 0.95998 -0.05852 0.04267  -0.08198 111 GLY B CA  
2568 C C   . GLY B 111 ? 0.62220 0.64649 0.89959 -0.04905 0.02265  -0.08191 111 GLY B C   
2569 O O   . GLY B 111 ? 0.59306 0.61697 0.86580 -0.03600 0.01147  -0.06621 111 GLY B O   
2570 N N   . TRP B 112 ? 0.62402 0.67840 0.90846 -0.05514 0.01904  -0.09987 112 TRP B N   
2571 C CA  . TRP B 112 ? 0.61889 0.70666 0.90420 -0.04434 0.00165  -0.10086 112 TRP B CA  
2572 C C   . TRP B 112 ? 0.63292 0.71723 0.91049 -0.03364 -0.00555 -0.09386 112 TRP B C   
2573 O O   . TRP B 112 ? 0.64191 0.70524 0.91651 -0.03677 0.00272  -0.09303 112 TRP B O   
2574 C CB  . TRP B 112 ? 0.60662 0.73368 0.90217 -0.05336 0.00035  -0.12384 112 TRP B CB  
2575 C CG  . TRP B 112 ? 0.59055 0.72796 0.89347 -0.06010 0.00334  -0.12885 112 TRP B CG  
2576 C CD1 . TRP B 112 ? 0.61172 0.73937 0.92127 -0.07791 0.01947  -0.14005 112 TRP B CD1 
2577 C CD2 . TRP B 112 ? 0.61723 0.77457 0.92035 -0.04925 -0.00868 -0.12273 112 TRP B CD2 
2578 N NE1 . TRP B 112 ? 0.62518 0.76813 0.94054 -0.07924 0.01745  -0.14169 112 TRP B NE1 
2579 C CE2 . TRP B 112 ? 0.58865 0.75041 0.90040 -0.06124 -0.00018 -0.13096 112 TRP B CE2 
2580 C CE3 . TRP B 112 ? 0.63984 0.80913 0.93497 -0.03055 -0.02428 -0.11111 112 TRP B CE3 
2581 C CZ2 . TRP B 112 ? 0.58320 0.76339 0.89720 -0.05452 -0.00800 -0.12794 112 TRP B CZ2 
2582 C CZ3 . TRP B 112 ? 0.58772 0.77244 0.88349 -0.02365 -0.03101 -0.10781 112 TRP B CZ3 
2583 C CH2 . TRP B 112 ? 0.54720 0.73836 0.85299 -0.03525 -0.02353 -0.11609 112 TRP B CH2 
2584 N N   . CYS B 113 ? 0.60180 0.70514 0.87452 -0.02026 -0.02001 -0.08842 113 CYS B N   
2585 C CA  . CYS B 113 ? 0.58010 0.67560 0.84262 -0.00811 -0.02705 -0.07730 113 CYS B CA  
2586 C C   . CYS B 113 ? 0.57976 0.69541 0.83449 0.00592  -0.04038 -0.07318 113 CYS B C   
2587 O O   . CYS B 113 ? 0.65109 0.77443 0.90609 0.00940  -0.04441 -0.06988 113 CYS B O   
2588 C CB  . CYS B 113 ? 0.59293 0.65586 0.85079 -0.00498 -0.02298 -0.05952 113 CYS B CB  
2589 S SG  . CYS B 113 ? 0.68692 0.74234 0.93334 0.00871  -0.03139 -0.04499 113 CYS B SG  
2590 N N   . ARG B 114 ? 0.62396 0.74651 0.86991 0.01472  -0.04613 -0.07324 114 ARG B N   
2591 C CA  . ARG B 114 ? 0.63949 0.77569 0.87297 0.03024  -0.05652 -0.06833 114 ARG B CA  
2592 C C   . ARG B 114 ? 0.67695 0.78625 0.89814 0.03792  -0.05726 -0.05108 114 ARG B C   
2593 O O   . ARG B 114 ? 0.78518 0.88740 1.00042 0.04019  -0.05647 -0.05014 114 ARG B O   
2594 C CB  . ARG B 114 ? 0.63646 0.80140 0.86613 0.03575  -0.06148 -0.08196 114 ARG B CB  
2595 C CG  . ARG B 114 ? 0.71269 0.88703 0.92427 0.05519  -0.07053 -0.07526 114 ARG B CG  
2596 C CD  . ARG B 114 ? 0.78031 0.98757 0.98593 0.06402  -0.07629 -0.08878 114 ARG B CD  
2597 N NE  . ARG B 114 ? 0.77635 1.02442 0.99162 0.06361  -0.08022 -0.10513 114 ARG B NE  
2598 C CZ  . ARG B 114 ? 0.75940 1.02704 0.96723 0.07827  -0.08703 -0.10343 114 ARG B CZ  
2599 N NH1 . ARG B 114 ? 0.69824 0.94360 0.88812 0.09315  -0.08925 -0.08563 114 ARG B NH1 
2600 N NH2 . ARG B 114 ? 0.76210 1.07337 0.98029 0.07785  -0.09074 -0.12091 114 ARG B NH2 
2601 N N   . GLY B 115 ? 0.65606 0.75186 0.87351 0.04105  -0.05821 -0.03867 115 GLY B N   
2602 C CA  . GLY B 115 ? 0.65986 0.73129 0.86977 0.04341  -0.05647 -0.02483 115 GLY B CA  
2603 C C   . GLY B 115 ? 0.65427 0.70911 0.87398 0.03471  -0.05055 -0.01873 115 GLY B C   
2604 O O   . GLY B 115 ? 0.66263 0.70394 0.88331 0.03264  -0.04646 -0.01442 115 GLY B O   
2605 N N   . MET B 116 ? 0.66791 0.72473 0.89406 0.03082  -0.04974 -0.01844 116 MET B N   
2606 C CA  . MET B 116 ? 0.66968 0.71186 0.90385 0.02360  -0.04308 -0.01383 116 MET B CA  
2607 C C   . MET B 116 ? 0.65467 0.68013 0.88441 0.02671  -0.04208 -0.00081 116 MET B C   
2608 O O   . MET B 116 ? 0.63697 0.65053 0.87116 0.02385  -0.03592 0.00269  116 MET B O   
2609 C CB  . MET B 116 ? 0.64477 0.69194 0.88329 0.02074  -0.04317 -0.01436 116 MET B CB  
2610 C CG  . MET B 116 ? 0.70274 0.73385 0.94624 0.01518  -0.03596 -0.00862 116 MET B CG  
2611 S SD  . MET B 116 ? 0.77942 0.81673 1.02857 0.00988  -0.03412 -0.01190 116 MET B SD  
2612 C CE  . MET B 116 ? 0.73379 0.74694 0.98091 0.00967  -0.02766 0.00165  116 MET B CE  
2613 N N   . SER B 117 ? 0.60483 0.62953 0.82486 0.03280  -0.04695 0.00586  117 SER B N   
2614 C CA  . SER B 117 ? 0.58278 0.59702 0.80015 0.03392  -0.04559 0.01551  117 SER B CA  
2615 C C   . SER B 117 ? 0.63409 0.64515 0.84948 0.03535  -0.04373 0.01492  117 SER B C   
2616 O O   . SER B 117 ? 0.58843 0.59496 0.80266 0.03614  -0.04240 0.02131  117 SER B O   
2617 C CB  . SER B 117 ? 0.60835 0.62106 0.81599 0.03681  -0.04896 0.02183  117 SER B CB  
2618 O OG  . SER B 117 ? 0.63412 0.64897 0.83018 0.04196  -0.05160 0.01913  117 SER B OG  
2619 N N   . PHE B 118 ? 0.71519 0.73095 0.93070 0.03539  -0.04345 0.00645  118 PHE B N   
2620 C CA  . PHE B 118 ? 0.69346 0.70604 0.90750 0.03634  -0.04098 0.00464  118 PHE B CA  
2621 C C   . PHE B 118 ? 0.70082 0.70826 0.92412 0.03207  -0.03436 0.00045  118 PHE B C   
2622 O O   . PHE B 118 ? 0.70100 0.70031 0.92602 0.03337  -0.03022 0.00542  118 PHE B O   
2623 C CB  . PHE B 118 ? 0.73390 0.75459 0.93891 0.04036  -0.04455 -0.00213 118 PHE B CB  
2624 C CG  . PHE B 118 ? 0.78555 0.80327 0.98770 0.04137  -0.04201 -0.00480 118 PHE B CG  
2625 C CD1 . PHE B 118 ? 0.79409 0.80357 0.98939 0.04375  -0.04055 0.00198  118 PHE B CD1 
2626 C CD2 . PHE B 118 ? 0.76378 0.78767 0.97029 0.03871  -0.04014 -0.01526 118 PHE B CD2 
2627 C CE1 . PHE B 118 ? 0.76905 0.77585 0.96192 0.04456  -0.03767 -0.00051 118 PHE B CE1 
2628 C CE2 . PHE B 118 ? 0.76653 0.78698 0.96995 0.03963  -0.03745 -0.01770 118 PHE B CE2 
2629 C CZ  . PHE B 118 ? 0.78644 0.79807 0.98295 0.04315  -0.03646 -0.00977 118 PHE B CZ  
2630 N N   . ASP B 119 ? 0.60699 0.61901 0.83564 0.02696  -0.03210 -0.00910 119 ASP B N   
2631 C CA  . ASP B 119 ? 0.57994 0.58400 0.81435 0.02139  -0.02325 -0.01576 119 ASP B CA  
2632 C C   . ASP B 119 ? 0.59236 0.57948 0.82989 0.02087  -0.01538 -0.00804 119 ASP B C   
2633 O O   . ASP B 119 ? 0.57778 0.55283 0.81435 0.02401  -0.00951 -0.00361 119 ASP B O   
2634 C CB  . ASP B 119 ? 0.55307 0.56947 0.79199 0.01400  -0.02208 -0.03039 119 ASP B CB  
2635 C CG  . ASP B 119 ? 0.65581 0.68838 0.89093 0.01575  -0.02707 -0.04001 119 ASP B CG  
2636 O OD1 . ASP B 119 ? 0.72829 0.75466 0.95976 0.01797  -0.02527 -0.03941 119 ASP B OD1 
2637 O OD2 . ASP B 119 ? 0.68871 0.74149 0.92339 0.01647  -0.03305 -0.04781 119 ASP B OD2 
2638 N N   . PHE B 120 ? 0.56660 0.55258 0.80654 0.01835  -0.01464 -0.00612 120 PHE B N   
2639 C CA  . PHE B 120 ? 0.56148 0.53034 0.80137 0.01971  -0.00655 0.00183  120 PHE B CA  
2640 C C   . PHE B 120 ? 0.55902 0.52373 0.79554 0.02938  -0.00817 0.01480  120 PHE B C   
2641 O O   . PHE B 120 ? 0.50418 0.45408 0.73860 0.03373  0.00046  0.01987  120 PHE B O   
2642 C CB  . PHE B 120 ? 0.59215 0.56247 0.83380 0.01633  -0.00701 0.00281  120 PHE B CB  
2643 C CG  . PHE B 120 ? 0.58591 0.55856 0.83225 0.00567  -0.00114 -0.01078 120 PHE B CG  
2644 C CD1 . PHE B 120 ? 0.56139 0.51520 0.80745 -0.00067 0.01333  -0.01598 120 PHE B CD1 
2645 C CD2 . PHE B 120 ? 0.56640 0.56021 0.81648 0.00212  -0.00876 -0.01913 120 PHE B CD2 
2646 C CE1 . PHE B 120 ? 0.58795 0.54538 0.83891 -0.01313 0.02041  -0.03095 120 PHE B CE1 
2647 C CE2 . PHE B 120 ? 0.59846 0.60016 0.85457 -0.00838 -0.00332 -0.03368 120 PHE B CE2 
2648 C CZ  . PHE B 120 ? 0.61689 0.60107 0.87423 -0.01749 0.01150  -0.04049 120 PHE B CZ  
2649 N N   . PRO B 121 ? 0.57405 0.55115 0.80897 0.03327  -0.01755 0.02003  121 PRO B N   
2650 C CA  . PRO B 121 ? 0.54616 0.52444 0.77965 0.04071  -0.01818 0.02914  121 PRO B CA  
2651 C C   . PRO B 121 ? 0.56798 0.54121 0.80135 0.04407  -0.01307 0.02775  121 PRO B C   
2652 O O   . PRO B 121 ? 0.58582 0.55734 0.81882 0.05175  -0.00986 0.03488  121 PRO B O   
2653 C CB  . PRO B 121 ? 0.48815 0.47973 0.71916 0.04021  -0.02710 0.03072  121 PRO B CB  
2654 C CG  . PRO B 121 ? 0.48637 0.48032 0.71647 0.03586  -0.03066 0.02718  121 PRO B CG  
2655 C CD  . PRO B 121 ? 0.50519 0.49501 0.73829 0.03142  -0.02644 0.01809  121 PRO B CD  
2656 N N   . ILE B 122 ? 0.49270 0.46553 0.72590 0.03964  -0.01236 0.01864  122 ILE B N   
2657 C CA  . ILE B 122 ? 0.57552 0.54114 0.80818 0.04223  -0.00604 0.01655  122 ILE B CA  
2658 C C   . ILE B 122 ? 0.57554 0.52184 0.80750 0.04209  0.00610  0.01535  122 ILE B C   
2659 O O   . ILE B 122 ? 0.55019 0.48598 0.77970 0.04952  0.01341  0.02031  122 ILE B O   
2660 C CB  . ILE B 122 ? 0.64186 0.61374 0.87301 0.03778  -0.00901 0.00683  122 ILE B CB  
2661 C CG1 . ILE B 122 ? 0.62201 0.60554 0.84957 0.04043  -0.01676 0.00995  122 ILE B CG1 
2662 C CG2 . ILE B 122 ? 0.62160 0.58356 0.85225 0.03794  -0.00077 0.00186  122 ILE B CG2 
2663 C CD1 . ILE B 122 ? 0.59568 0.58512 0.81815 0.03782  -0.02049 0.00147  122 ILE B CD1 
2664 N N   . LEU B 123 ? 0.58023 0.52091 0.81320 0.03383  0.00973  0.00831  123 LEU B N   
2665 C CA  . LEU B 123 ? 0.54887 0.46676 0.77882 0.03167  0.02412  0.00650  123 LEU B CA  
2666 C C   . LEU B 123 ? 0.57482 0.48002 0.79938 0.04323  0.02923  0.02040  123 LEU B C   
2667 O O   . LEU B 123 ? 0.64746 0.53271 0.86546 0.04979  0.04110  0.02394  123 LEU B O   
2668 C CB  . LEU B 123 ? 0.52453 0.44211 0.75726 0.01985  0.02694  -0.00317 123 LEU B CB  
2669 C CG  . LEU B 123 ? 0.60493 0.49461 0.83246 0.01522  0.04529  -0.00704 123 LEU B CG  
2670 C CD1 . LEU B 123 ? 0.67377 0.55539 0.89970 0.01151  0.05315  -0.01651 123 LEU B CD1 
2671 C CD2 . LEU B 123 ? 0.57952 0.46730 0.80981 0.00215  0.05110  -0.01704 123 LEU B CD2 
2672 N N   . VAL B 124 ? 0.57965 0.49615 0.80536 0.04706  0.02097  0.02842  124 VAL B N   
2673 C CA  . VAL B 124 ? 0.57622 0.48407 0.79583 0.05928  0.02540  0.04104  124 VAL B CA  
2674 C C   . VAL B 124 ? 0.55434 0.46895 0.77265 0.07203  0.02427  0.04801  124 VAL B C   
2675 O O   . VAL B 124 ? 0.58618 0.48677 0.79676 0.08430  0.03358  0.05564  124 VAL B O   
2676 C CB  . VAL B 124 ? 0.56492 0.48546 0.78607 0.05956  0.01677  0.04673  124 VAL B CB  
2677 C CG1 . VAL B 124 ? 0.53002 0.44750 0.74432 0.07408  0.01953  0.05972  124 VAL B CG1 
2678 C CG2 . VAL B 124 ? 0.59262 0.50375 0.81424 0.04848  0.02093  0.04012  124 VAL B CG2 
2679 N N   . ASP B 125 ? 0.54244 0.47772 0.76694 0.07009  0.01421  0.04524  125 ASP B N   
2680 C CA  . ASP B 125 ? 0.57604 0.52124 0.80073 0.08115  0.01354  0.05056  125 ASP B CA  
2681 C C   . ASP B 125 ? 0.63366 0.55950 0.85362 0.08587  0.02548  0.04868  125 ASP B C   
2682 O O   . ASP B 125 ? 0.62973 0.55474 0.84590 0.10001  0.03030  0.05592  125 ASP B O   
2683 C CB  . ASP B 125 ? 0.62878 0.59711 0.85973 0.07599  0.00264  0.04678  125 ASP B CB  
2684 C CG  . ASP B 125 ? 0.69302 0.67874 0.92616 0.08623  0.00101  0.05181  125 ASP B CG  
2685 O OD1 . ASP B 125 ? 0.72928 0.72971 0.96317 0.09336  -0.00240 0.05853  125 ASP B OD1 
2686 O OD2 . ASP B 125 ? 0.62457 0.61134 0.85882 0.08734  0.00336  0.04843  125 ASP B OD2 
2687 N N   . LEU B 126 ? 0.60017 0.51177 0.81980 0.07469  0.03079  0.03834  126 LEU B N   
2688 C CA  . LEU B 126 ? 0.63261 0.52120 0.84598 0.07742  0.04469  0.03549  126 LEU B CA  
2689 C C   . LEU B 126 ? 0.65486 0.51545 0.85688 0.08606  0.05943  0.04264  126 LEU B C   
2690 O O   . LEU B 126 ? 0.64249 0.48684 0.83585 0.09869  0.07033  0.04814  126 LEU B O   
2691 C CB  . LEU B 126 ? 0.64516 0.52805 0.86084 0.06175  0.04723  0.02067  126 LEU B CB  
2692 C CG  . LEU B 126 ? 0.60033 0.50436 0.82207 0.05730  0.03650  0.01441  126 LEU B CG  
2693 C CD1 . LEU B 126 ? 0.59944 0.50002 0.82195 0.04392  0.03939  -0.00050 126 LEU B CD1 
2694 C CD2 . LEU B 126 ? 0.55338 0.46010 0.77401 0.06814  0.03805  0.01950  126 LEU B CD2 
2695 N N   . ILE B 127 ? 0.63511 0.48818 0.83520 0.08061  0.06101  0.04314  127 ILE B N   
2696 C CA  . ILE B 127 ? 0.65946 0.48340 0.84586 0.08949  0.07605  0.05103  127 ILE B CA  
2697 C C   . ILE B 127 ? 0.66456 0.49554 0.84437 0.11223  0.07426  0.06682  127 ILE B C   
2698 O O   . ILE B 127 ? 0.64694 0.45371 0.81254 0.12709  0.08852  0.07425  127 ILE B O   
2699 C CB  . ILE B 127 ? 0.66881 0.48692 0.85544 0.07822  0.07700  0.04797  127 ILE B CB  
2700 C CG1 . ILE B 127 ? 0.65436 0.46753 0.84686 0.05716  0.08113  0.03075  127 ILE B CG1 
2701 C CG2 . ILE B 127 ? 0.75204 0.53855 0.92210 0.08843  0.09315  0.05739  127 ILE B CG2 
2702 C CD1 . ILE B 127 ? 0.67589 0.49260 0.87239 0.04488  0.07925  0.02557  127 ILE B CD1 
2703 N N   . ARG B 128 ? 0.62338 0.48816 0.81214 0.11611  0.05772  0.07166  128 ARG B N   
2704 C CA  . ARG B 128 ? 0.63105 0.50765 0.81397 0.13783  0.05633  0.08473  128 ARG B CA  
2705 C C   . ARG B 128 ? 0.68871 0.56813 0.86946 0.15157  0.06050  0.08727  128 ARG B C   
2706 O O   . ARG B 128 ? 0.69360 0.57499 0.86503 0.17323  0.06465  0.09822  128 ARG B O   
2707 C CB  . ARG B 128 ? 0.63299 0.54783 0.82547 0.13921  0.03931  0.08815  128 ARG B CB  
2708 C CG  . ARG B 128 ? 0.62685 0.56727 0.83398 0.12241  0.02486  0.07926  128 ARG B CG  
2709 C CD  . ARG B 128 ? 0.62570 0.57728 0.83489 0.11684  0.01667  0.08111  128 ARG B CD  
2710 N NE  . ARG B 128 ? 0.71435 0.67806 0.93295 0.09946  0.00670  0.07234  128 ARG B NE  
2711 C CZ  . ARG B 128 ? 0.73275 0.72153 0.95911 0.09440  -0.00357 0.06882  128 ARG B CZ  
2712 N NH1 . ARG B 128 ? 0.69312 0.70209 0.92248 0.10260  -0.00607 0.07089  128 ARG B NH1 
2713 N NH2 . ARG B 128 ? 0.69243 0.68522 0.92264 0.08078  -0.01016 0.06234  128 ARG B NH2 
2714 N N   . ASP B 129 ? 0.85497 0.73445 1.04271 0.14104  0.06024  0.07755  129 ASP B N   
2715 C CA  . ASP B 129 ? 0.86237 0.74299 1.04802 0.15334  0.06525  0.07919  129 ASP B CA  
2716 C C   . ASP B 129 ? 0.89930 0.74232 1.06639 0.16854  0.08502  0.08576  129 ASP B C   
2717 O O   . ASP B 129 ? 0.90562 0.75216 1.06774 0.18685  0.08936  0.09182  129 ASP B O   
2718 C CB  . ASP B 129 ? 0.86428 0.74835 1.05900 0.13803  0.06242  0.06701  129 ASP B CB  
2719 C CG  . ASP B 129 ? 0.87022 0.79169 1.07931 0.13058  0.04550  0.06322  129 ASP B CG  
2720 O OD1 . ASP B 129 ? 0.87139 0.81896 1.08409 0.14040  0.03774  0.06998  129 ASP B OD1 
2721 O OD2 . ASP B 129 ? 0.88940 0.81409 1.10471 0.11561  0.04110  0.05316  129 ASP B OD2 
2722 N N   . ILE B 130 ? 0.74990 0.55614 0.90562 0.16147  0.09852  0.08419  130 ILE B N   
2723 C CA  . ILE B 130 ? 0.71226 0.47707 0.84580 0.17718  0.12022  0.09187  130 ILE B CA  
2724 C C   . ILE B 130 ? 0.75902 0.53319 0.88170 0.20442  0.11932  0.10843  130 ILE B C   
2725 O O   . ILE B 130 ? 0.75802 0.51423 0.86367 0.22772  0.13223  0.11824  130 ILE B O   
2726 C CB  . ILE B 130 ? 0.73471 0.45935 0.85817 0.16140  0.13581  0.08557  130 ILE B CB  
2727 C CG1 . ILE B 130 ? 0.71646 0.44417 0.85382 0.13363  0.13268  0.06735  130 ILE B CG1 
2728 C CG2 . ILE B 130 ? 0.78713 0.46155 0.88523 0.17439  0.16214  0.09116  130 ILE B CG2 
2729 C CD1 . ILE B 130 ? 0.75089 0.45679 0.88542 0.11460  0.14160  0.05882  130 ILE B CD1 
2730 N N   . GLN B 131 ? 0.74262 0.54587 0.87384 0.20283  0.10428  0.11162  131 GLN B N   
2731 C CA  . GLN B 131 ? 0.70961 0.52841 0.83162 0.22765  0.10134  0.12585  131 GLN B CA  
2732 C C   . GLN B 131 ? 0.69021 0.55622 0.82372 0.24169  0.08751  0.12831  131 GLN B C   
2733 O O   . GLN B 131 ? 0.71140 0.58491 0.83305 0.26928  0.09129  0.13963  131 GLN B O   
2734 C CB  . GLN B 131 ? 0.71693 0.54645 0.84233 0.21932  0.09236  0.12717  131 GLN B CB  
2735 C CG  . GLN B 131 ? 0.72614 0.50939 0.83275 0.21752  0.10968  0.13058  131 GLN B CG  
2736 C CD  . GLN B 131 ? 0.81132 0.60681 0.92366 0.20643  0.10003  0.13011  131 GLN B CD  
2737 O OE1 . GLN B 131 ? 0.79216 0.62871 0.92286 0.19807  0.08063  0.12610  131 GLN B OE1 
2738 N NE2 . GLN B 131 ? 0.89256 0.65054 0.98817 0.20554  0.11489  0.13376  131 GLN B NE2 
2739 N N   . ARG B 132 ? 0.65265 0.55144 0.80792 0.22404  0.07239  0.11766  132 ARG B N   
2740 C CA  . ARG B 132 ? 0.63776 0.57891 0.80392 0.23493  0.06243  0.11771  132 ARG B CA  
2741 C C   . ARG B 132 ? 0.66687 0.59222 0.82201 0.25451  0.07563  0.12222  132 ARG B C   
2742 O O   . ARG B 132 ? 0.67474 0.62651 0.82757 0.27812  0.07384  0.12934  132 ARG B O   
2743 C CB  . ARG B 132 ? 0.60073 0.56769 0.78775 0.21142  0.04917  0.10488  132 ARG B CB  
2744 C CG  . ARG B 132 ? 0.57362 0.55823 0.77059 0.19441  0.03652  0.10061  132 ARG B CG  
2745 C CD  . ARG B 132 ? 0.54483 0.54916 0.75749 0.17473  0.02662  0.08924  132 ARG B CD  
2746 N NE  . ARG B 132 ? 0.62046 0.64243 0.84117 0.15975  0.01499  0.08546  132 ARG B NE  
2747 C CZ  . ARG B 132 ? 0.64171 0.64896 0.86471 0.14088  0.01258  0.07907  132 ARG B CZ  
2748 N NH1 . ARG B 132 ? 0.66559 0.64598 0.88619 0.13187  0.01928  0.07337  132 ARG B NH1 
2749 N NH2 . ARG B 132 ? 0.64755 0.67001 0.87535 0.13103  0.00318  0.07745  132 ARG B NH2 
2750 N N   . LEU B 133 ? 0.68456 0.56806 0.83238 0.24518  0.08944  0.11739  133 LEU B N   
2751 C CA  . LEU B 133 ? 0.71724 0.57605 0.85165 0.26182  0.10525  0.12101  133 LEU B CA  
2752 C C   . LEU B 133 ? 0.75932 0.59790 0.86915 0.29347  0.11896  0.13672  133 LEU B C   
2753 O O   . LEU B 133 ? 0.78220 0.62112 0.88256 0.31739  0.12666  0.14327  133 LEU B O   
2754 C CB  . LEU B 133 ? 0.73065 0.54461 0.86004 0.24179  0.11882  0.11131  133 LEU B CB  
2755 C CG  . LEU B 133 ? 0.76738 0.54426 0.88149 0.25134  0.13862  0.11153  133 LEU B CG  
2756 C CD1 . LEU B 133 ? 0.75374 0.56053 0.87930 0.25814  0.13187  0.10875  133 LEU B CD1 
2757 C CD2 . LEU B 133 ? 0.77665 0.51414 0.88794 0.22532  0.15025  0.09884  133 LEU B CD2 
2758 N N   . ASN B 134 ? 0.77198 0.59216 0.86977 0.29516  0.12277  0.14322  134 ASN B N   
2759 C CA  . ASN B 134 ? 0.81238 0.61229 0.88419 0.32459  0.13502  0.15908  134 ASN B CA  
2760 C C   . ASN B 134 ? 0.80131 0.65498 0.87738 0.34951  0.12029  0.16785  134 ASN B C   
2761 O O   . ASN B 134 ? 0.83443 0.67827 0.88829 0.37761  0.12842  0.18182  134 ASN B O   
2762 C CB  . ASN B 134 ? 0.82260 0.58995 0.88401 0.31220  0.14164  0.16036  134 ASN B CB  
2763 C CG  . ASN B 134 ? 0.88243 0.59543 0.90763 0.33602  0.16668  0.17448  134 ASN B CG  
2764 O OD1 . ASN B 134 ? 0.92110 0.61453 0.92583 0.36332  0.18120  0.18411  134 ASN B OD1 
2765 N ND2 . ASN B 134 ? 0.89249 0.57833 0.90832 0.32527  0.17317  0.17547  134 ASN B ND2 
2766 N N   . GLY B 135 ? 0.76235 0.67264 0.86492 0.34001  0.09987  0.15947  135 GLY B N   
2767 C CA  . GLY B 135 ? 0.74507 0.71302 0.85488 0.35894  0.08521  0.16406  135 GLY B CA  
2768 C C   . GLY B 135 ? 0.73780 0.72800 0.85274 0.35117  0.07272  0.16465  135 GLY B C   
2769 O O   . GLY B 135 ? 0.73665 0.77684 0.85689 0.36624  0.06079  0.16736  135 GLY B O   
2770 N N   . VAL B 136 ? 0.71997 0.67696 0.83366 0.32822  0.07533  0.16130  136 VAL B N   
2771 C CA  . VAL B 136 ? 0.74907 0.72472 0.86781 0.31904  0.06396  0.16121  136 VAL B CA  
2772 C C   . VAL B 136 ? 0.76905 0.79992 0.91573 0.30032  0.04344  0.14920  136 VAL B C   
2773 O O   . VAL B 136 ? 0.63385 0.66473 0.79637 0.27678  0.03948  0.13775  136 VAL B O   
2774 C CB  . VAL B 136 ? 0.72788 0.65536 0.84049 0.29706  0.07247  0.15857  136 VAL B CB  
2775 C CG1 . VAL B 136 ? 0.69016 0.63570 0.80809 0.28706  0.06108  0.15824  136 VAL B CG1 
2776 C CG2 . VAL B 136 ? 0.75544 0.62498 0.83939 0.31249  0.09578  0.16854  136 VAL B CG2 
2777 N N   . SER B 137 ? 0.80836 0.88533 0.95950 0.31033  0.03138  0.15128  137 SER B N   
2778 C CA  . SER B 137 ? 0.74297 0.87138 0.91821 0.29204  0.01424  0.13921  137 SER B CA  
2779 C C   . SER B 137 ? 0.76381 0.87735 0.94815 0.26090  0.00882  0.13124  137 SER B C   
2780 O O   . SER B 137 ? 0.78721 0.86000 0.96043 0.25541  0.01599  0.13538  137 SER B O   
2781 C CB  . SER B 137 ? 0.73210 0.91424 0.90880 0.30963  0.00406  0.14182  137 SER B CB  
2782 O OG  . SER B 137 ? 0.85277 1.06394 1.02799 0.33526  0.00564  0.14486  137 SER B OG  
2783 N N   . GLU B 138 ? 0.72316 0.87006 0.92721 0.24049  -0.00284 0.11914  138 GLU B N   
2784 C CA  . GLU B 138 ? 0.68037 0.81133 0.89267 0.21155  -0.00692 0.11077  138 GLU B CA  
2785 C C   . GLU B 138 ? 0.65688 0.78777 0.86529 0.20627  -0.01163 0.11329  138 GLU B C   
2786 O O   . GLU B 138 ? 0.64024 0.74521 0.84927 0.18787  -0.01128 0.11001  138 GLU B O   
2787 C CB  . GLU B 138 ? 0.64144 0.80364 0.87171 0.19331  -0.01541 0.09805  138 GLU B CB  
2788 C CG  . GLU B 138 ? 0.61479 0.75818 0.85113 0.16586  -0.01830 0.08960  138 GLU B CG  
2789 C CD  . GLU B 138 ? 0.68230 0.78424 0.91506 0.15847  -0.01029 0.08813  138 GLU B CD  
2790 O OE1 . GLU B 138 ? 0.64917 0.74172 0.87893 0.16951  -0.00306 0.09015  138 GLU B OE1 
2791 O OE2 . GLU B 138 ? 0.66635 0.74723 0.89927 0.14166  -0.01121 0.08410  138 GLU B OE2 
2792 N N   . ASN B 139 ? 0.69453 0.85636 0.89882 0.22266  -0.01624 0.11853  139 ASN B N   
2793 C CA  . ASN B 139 ? 0.69745 0.85808 0.89547 0.22069  -0.01966 0.12218  139 ASN B CA  
2794 C C   . ASN B 139 ? 0.71192 0.83116 0.88893 0.23666  -0.00824 0.13509  139 ASN B C   
2795 O O   . ASN B 139 ? 0.71698 0.82712 0.88746 0.23339  -0.00915 0.13833  139 ASN B O   
2796 C CB  . ASN B 139 ? 0.66212 0.87634 0.86398 0.23045  -0.02965 0.12094  139 ASN B CB  
2797 C CG  . ASN B 139 ? 0.73032 0.96752 0.92452 0.26083  -0.02722 0.12835  139 ASN B CG  
2798 O OD1 . ASN B 139 ? 0.79485 1.00960 0.98294 0.27281  -0.01823 0.13321  139 ASN B OD1 
2799 N ND2 . ASN B 139 ? 0.77833 1.05892 0.97050 0.27565  -0.03431 0.12989  139 ASN B ND2 
2800 N N   . GLU B 140 ? 0.74135 0.83369 0.90623 0.25363  0.00384  0.14233  140 GLU B N   
2801 C CA  . GLU B 140 ? 0.70741 0.75551 0.84884 0.26943  0.01830  0.15456  140 GLU B CA  
2802 C C   . GLU B 140 ? 0.68757 0.68227 0.82466 0.25517  0.03164  0.15205  140 GLU B C   
2803 O O   . GLU B 140 ? 0.76136 0.71330 0.87789 0.26641  0.04753  0.16063  140 GLU B O   
2804 C CB  . GLU B 140 ? 0.66410 0.72232 0.78946 0.30444  0.02420  0.16611  140 GLU B CB  
2805 C CG  . GLU B 140 ? 0.77498 0.88268 0.90043 0.31888  0.01224  0.16908  140 GLU B CG  
2806 C CD  . GLU B 140 ? 0.93001 1.06706 1.04413 0.35485  0.01337  0.17797  140 GLU B CD  
2807 O OE1 . GLU B 140 ? 0.93369 1.06274 1.04544 0.36678  0.02070  0.17968  140 GLU B OE1 
2808 O OE2 . GLU B 140 ? 0.95523 1.12424 1.06164 0.37256  0.00708  0.18337  140 GLU B OE2 
2809 N N   . LEU B 141 ? 0.65413 0.65040 0.80884 0.23023  0.02633  0.13979  141 LEU B N   
2810 C CA  . LEU B 141 ? 0.70740 0.66012 0.86021 0.21386  0.03711  0.13462  141 LEU B CA  
2811 C C   . LEU B 141 ? 0.76009 0.68797 0.90649 0.20277  0.04102  0.13529  141 LEU B C   
2812 O O   . LEU B 141 ? 0.81582 0.76593 0.96831 0.19650  0.03008  0.13451  141 LEU B O   
2813 C CB  . LEU B 141 ? 0.70200 0.66856 0.87465 0.19128  0.02844  0.12120  141 LEU B CB  
2814 C CG  . LEU B 141 ? 0.69620 0.68713 0.87889 0.19500  0.02416  0.11694  141 LEU B CG  
2815 C CD1 . LEU B 141 ? 0.59905 0.60030 0.79809 0.17129  0.01577  0.10434  141 LEU B CD1 
2816 C CD2 . LEU B 141 ? 0.67141 0.63709 0.84250 0.21099  0.03851  0.12155  141 LEU B CD2 
2817 N N   . ASP B 142 ? 0.79211 0.67367 0.92579 0.19964  0.05783  0.13591  142 ASP B N   
2818 C CA  . ASP B 142 ? 0.80768 0.66564 0.93782 0.18492  0.06283  0.13347  142 ASP B CA  
2819 C C   . ASP B 142 ? 0.82848 0.64687 0.95583 0.16954  0.07799  0.12505  142 ASP B C   
2820 O O   . ASP B 142 ? 0.88149 0.66180 0.99014 0.17960  0.09706  0.13013  142 ASP B O   
2821 C CB  . ASP B 142 ? 0.82769 0.66934 0.93711 0.20246  0.07133  0.14628  142 ASP B CB  
2822 C CG  . ASP B 142 ? 0.87262 0.69162 0.97988 0.18559  0.07677  0.14255  142 ASP B CG  
2823 O OD1 . ASP B 142 ? 0.93139 0.77714 1.05339 0.17197  0.06210  0.13711  142 ASP B OD1 
2824 O OD2 . ASP B 142 ? 0.94966 0.72431 1.04129 0.18403  0.09636  0.14349  142 ASP B OD2 
2825 N N   . THR B 143 ? 0.80447 0.63102 0.94845 0.14553  0.07079  0.11192  143 THR B N   
2826 C CA  . THR B 143 ? 0.86438 0.66304 1.00916 0.12868  0.08292  0.10058  143 THR B CA  
2827 C C   . THR B 143 ? 0.90471 0.68824 1.04951 0.11183  0.08830  0.09421  143 THR B C   
2828 O O   . THR B 143 ? 0.92469 0.70001 1.07689 0.09278  0.09281  0.08066  143 THR B O   
2829 C CB  . THR B 143 ? 0.86282 0.68414 1.02573 0.11529  0.07173  0.08869  143 THR B CB  
2830 O OG1 . THR B 143 ? 0.89736 0.74991 1.07542 0.10351  0.05423  0.08365  143 THR B OG1 
2831 C CG2 . THR B 143 ? 0.74019 0.57698 0.90410 0.13045  0.06752  0.09356  143 THR B CG2 
2832 N N   . PHE B 144 ? 0.93896 0.72150 1.07603 0.11836  0.08776  0.10278  144 PHE B N   
2833 C CA  . PHE B 144 ? 0.95718 0.73033 1.09653 0.10146  0.09134  0.09596  144 PHE B CA  
2834 C C   . PHE B 144 ? 0.98579 0.71881 1.11611 0.08966  0.11371  0.08747  144 PHE B C   
2835 O O   . PHE B 144 ? 0.96464 0.70038 1.10659 0.06813  0.11443  0.07269  144 PHE B O   
2836 C CB  . PHE B 144 ? 0.96322 0.73466 1.09135 0.11244  0.09111  0.10771  144 PHE B CB  
2837 C CG  . PHE B 144 ? 0.93491 0.69933 1.06625 0.09537  0.09420  0.10076  144 PHE B CG  
2838 C CD1 . PHE B 144 ? 0.90960 0.70626 1.05933 0.08214  0.07695  0.09326  144 PHE B CD1 
2839 C CD2 . PHE B 144 ? 0.96953 0.69382 1.08459 0.09222  0.11585  0.10103  144 PHE B CD2 
2840 C CE1 . PHE B 144 ? 0.90748 0.70006 1.06076 0.06726  0.07984  0.08635  144 PHE B CE1 
2841 C CE2 . PHE B 144 ? 0.89751 0.61766 1.01673 0.07540  0.11939  0.09328  144 PHE B CE2 
2842 C CZ  . PHE B 144 ? 0.85791 0.61402 0.99711 0.06337  0.10070  0.08588  144 PHE B CZ  
2843 N N   . LYS B 145 ? 1.08580 0.78201 1.19439 0.10398  0.13302  0.09602  145 LYS B N   
2844 C CA  . LYS B 145 ? 1.11309 0.76363 1.20788 0.09466  0.15899  0.08890  145 LYS B CA  
2845 C C   . LYS B 145 ? 1.10838 0.75578 1.21009 0.08597  0.16305  0.07734  145 LYS B C   
2846 O O   . LYS B 145 ? 1.11723 0.72417 1.20441 0.08125  0.18652  0.07249  145 LYS B O   
2847 C CB  . LYS B 145 ? 1.16758 0.77541 1.23119 0.11728  0.17979  0.10509  145 LYS B CB  
2848 C CG  . LYS B 145 ? 1.21319 0.79975 1.26245 0.11733  0.19008  0.11084  145 LYS B CG  
2849 C CD  . LYS B 145 ? 1.26546 0.89051 1.32251 0.12785  0.16777  0.12068  145 LYS B CD  
2850 C CE  . LYS B 145 ? 1.30893 0.94280 1.35146 0.16039  0.16223  0.13952  145 LYS B CE  
2851 N NZ  . LYS B 145 ? 1.25886 0.93179 1.30919 0.16759  0.14156  0.14653  145 LYS B NZ  
2852 N N   . LEU B 146 ? 1.03544 0.72141 1.15668 0.08390  0.14272  0.07280  146 LEU B N   
2853 C CA  . LEU B 146 ? 0.99447 0.67848 1.12142 0.07654  0.14609  0.06216  146 LEU B CA  
2854 C C   . LEU B 146 ? 0.93314 0.65015 1.08339 0.05503  0.13119  0.04515  146 LEU B C   
2855 O O   . LEU B 146 ? 0.92528 0.64937 1.08232 0.05008  0.12929  0.03664  146 LEU B O   
2856 C CB  . LEU B 146 ? 0.92523 0.62175 1.05035 0.09758  0.13827  0.07296  146 LEU B CB  
2857 C CG  . LEU B 146 ? 0.98302 0.65593 1.08530 0.12476  0.14973  0.09098  146 LEU B CG  
2858 C CD1 . LEU B 146 ? 0.91141 0.60397 1.01705 0.14127  0.14118  0.09652  146 LEU B CD1 
2859 C CD2 . LEU B 146 ? 1.06765 0.68345 1.14531 0.12468  0.17995  0.09113  146 LEU B CD2 
2860 N N   . GLU B 147 ? 0.91872 0.65638 1.07981 0.04452  0.12060  0.04081  147 GLU B N   
2861 C CA  . GLU B 147 ? 0.87004 0.64142 1.05087 0.02881  0.10532  0.02665  147 GLU B CA  
2862 C C   . GLU B 147 ? 0.88245 0.64549 1.06729 0.00656  0.11716  0.00849  147 GLU B C   
2863 O O   . GLU B 147 ? 0.90437 0.64303 1.08003 0.00166  0.13231  0.00839  147 GLU B O   
2864 C CB  . GLU B 147 ? 0.88829 0.69272 1.07915 0.03233  0.08447  0.03271  147 GLU B CB  
2865 C CG  . GLU B 147 ? 0.91348 0.72952 1.10098 0.05214  0.07386  0.04860  147 GLU B CG  
2866 C CD  . GLU B 147 ? 0.97510 0.82046 1.17034 0.05437  0.05591  0.05395  147 GLU B CD  
2867 O OE1 . GLU B 147 ? 0.99747 0.85393 1.20045 0.04205  0.05060  0.04646  147 GLU B OE1 
2868 O OE2 . GLU B 147 ? 0.97870 0.83616 1.17149 0.06882  0.04821  0.06527  147 GLU B OE2 
2869 N N   . PRO B 148 ? 0.83051 0.61457 1.02838 -0.00729 0.11143  -0.00794 148 PRO B N   
2870 C CA  . PRO B 148 ? 0.80608 0.58774 1.00898 -0.02939 0.12336  -0.02824 148 PRO B CA  
2871 C C   . PRO B 148 ? 0.82935 0.62651 1.03973 -0.03852 0.11907  -0.03266 148 PRO B C   
2872 O O   . PRO B 148 ? 0.83447 0.62765 1.04787 -0.05692 0.13199  -0.04911 148 PRO B O   
2873 C CB  . PRO B 148 ? 0.78522 0.59587 1.00087 -0.03729 0.11275  -0.04270 148 PRO B CB  
2874 C CG  . PRO B 148 ? 0.80307 0.63764 1.02319 -0.02159 0.09124  -0.02985 148 PRO B CG  
2875 C CD  . PRO B 148 ? 0.80531 0.61759 1.01299 -0.00326 0.09448  -0.00949 148 PRO B CD  
2876 N N   . CYS B 149 ? 0.82406 0.63995 1.03782 -0.02728 0.10210  -0.01986 149 CYS B N   
2877 C CA  . CYS B 149 ? 0.79142 0.61863 1.01014 -0.03344 0.09879  -0.02156 149 CYS B CA  
2878 C C   . CYS B 149 ? 0.77226 0.59966 0.98491 -0.01600 0.08837  -0.00121 149 CYS B C   
2879 O O   . CYS B 149 ? 0.78346 0.61101 0.99159 -0.00083 0.08104  0.01141  149 CYS B O   
2880 C CB  . CYS B 149 ? 0.77020 0.63871 1.00636 -0.04429 0.08416  -0.03684 149 CYS B CB  
2881 S SG  . CYS B 149 ? 0.73700 0.64108 0.98097 -0.03173 0.05785  -0.03082 149 CYS B SG  
2882 N N   . LYS B 150 ? 0.78854 0.61652 1.00088 -0.01882 0.08895  0.00097  150 LYS B N   
2883 C CA  . LYS B 150 ? 0.73916 0.57114 0.94644 -0.00420 0.07864  0.01812  150 LYS B CA  
2884 C C   . LYS B 150 ? 0.73870 0.60823 0.95854 -0.00199 0.05600  0.01797  150 LYS B C   
2885 O O   . LYS B 150 ? 0.72032 0.61204 0.95180 -0.01276 0.04974  0.00476  150 LYS B O   
2886 C CB  . LYS B 150 ? 0.74347 0.55994 0.94426 -0.00845 0.08904  0.02006  150 LYS B CB  
2887 C CG  . LYS B 150 ? 0.75846 0.53183 0.94255 -0.00983 0.11422  0.02118  150 LYS B CG  
2888 C CD  . LYS B 150 ? 0.78677 0.54030 0.95477 0.01141  0.11674  0.03901  150 LYS B CD  
2889 C CE  . LYS B 150 ? 0.86968 0.57513 1.01636 0.01340  0.14365  0.04208  150 LYS B CE  
2890 N NZ  . LYS B 150 ? 0.92307 0.61054 1.05274 0.03696  0.14678  0.05925  150 LYS B NZ  
2891 N N   . PHE B 151 ? 0.70252 0.57969 0.91883 0.01241  0.04463  0.03207  151 PHE B N   
2892 C CA  . PHE B 151 ? 0.66098 0.56791 0.88627 0.01410  0.02633  0.03120  151 PHE B CA  
2893 C C   . PHE B 151 ? 0.64698 0.57289 0.87992 0.00614  0.01863  0.02430  151 PHE B C   
2894 O O   . PHE B 151 ? 0.64115 0.58863 0.88060 0.00482  0.00727  0.01887  151 PHE B O   
2895 C CB  . PHE B 151 ? 0.66657 0.58043 0.88721 0.02790  0.01693  0.04532  151 PHE B CB  
2896 C CG  . PHE B 151 ? 0.66344 0.57471 0.87799 0.03325  0.01636  0.05508  151 PHE B CG  
2897 C CD1 . PHE B 151 ? 0.70101 0.59269 0.90362 0.04359  0.02610  0.06552  151 PHE B CD1 
2898 C CD2 . PHE B 151 ? 0.69140 0.61941 0.91031 0.02940  0.00648  0.05418  151 PHE B CD2 
2899 C CE1 . PHE B 151 ? 0.76316 0.65387 0.95869 0.04967  0.02532  0.07464  151 PHE B CE1 
2900 C CE2 . PHE B 151 ? 0.70945 0.63563 0.92235 0.03391  0.00600  0.06263  151 PHE B CE2 
2901 C CZ  . PHE B 151 ? 0.71182 0.62038 0.91324 0.04391  0.01501  0.07277  151 PHE B CZ  
2902 N N   . TRP B 152 ? 0.66856 0.58598 0.89935 0.00192  0.02541  0.02463  152 TRP B N   
2903 C CA  . TRP B 152 ? 0.62384 0.55948 0.86213 -0.00550 0.01970  0.01712  152 TRP B CA  
2904 C C   . TRP B 152 ? 0.66131 0.60634 0.90896 -0.01912 0.02542  -0.00107 152 TRP B C   
2905 O O   . TRP B 152 ? 0.66559 0.63106 0.92063 -0.02428 0.02012  -0.00906 152 TRP B O   
2906 C CB  . TRP B 152 ? 0.66287 0.58700 0.89535 -0.00505 0.02517  0.02400  152 TRP B CB  
2907 C CG  . TRP B 152 ? 0.67520 0.57035 0.90029 -0.00999 0.04451  0.02279  152 TRP B CG  
2908 C CD1 . TRP B 152 ? 0.66992 0.55958 0.89928 -0.02469 0.05737  0.00884  152 TRP B CD1 
2909 C CD2 . TRP B 152 ? 0.67651 0.54315 0.88668 0.00015  0.05487  0.03565  152 TRP B CD2 
2910 N NE1 . TRP B 152 ? 0.66861 0.52335 0.88527 -0.02565 0.07673  0.01228  152 TRP B NE1 
2911 C CE2 . TRP B 152 ? 0.66514 0.50438 0.86873 -0.00883 0.07537  0.02972  152 TRP B CE2 
2912 C CE3 . TRP B 152 ? 0.70377 0.56686 0.90475 0.01656  0.04945  0.05101  152 TRP B CE3 
2913 C CZ2 . TRP B 152 ? 0.68416 0.48790 0.86939 0.00002  0.09130  0.04043  152 TRP B CZ2 
2914 C CZ3 . TRP B 152 ? 0.69632 0.53007 0.88106 0.02648  0.06335  0.06121  152 TRP B CZ3 
2915 C CH2 . TRP B 152 ? 0.69295 0.49502 0.86855 0.01917  0.08442  0.05677  152 TRP B CH2 
2916 N N   . ASN B 153 ? 0.72041 0.65268 0.96772 -0.02507 0.03664  -0.00872 153 ASN B N   
2917 C CA  . ASN B 153 ? 0.72310 0.67003 0.98033 -0.03898 0.04119  -0.02856 153 ASN B CA  
2918 C C   . ASN B 153 ? 0.71724 0.68439 0.97950 -0.03638 0.03073  -0.03471 153 ASN B C   
2919 O O   . ASN B 153 ? 0.70534 0.68762 0.97529 -0.04686 0.03386  -0.05195 153 ASN B O   
2920 C CB  . ASN B 153 ? 0.75373 0.67346 1.00680 -0.05062 0.06290  -0.03675 153 ASN B CB  
2921 C CG  . ASN B 153 ? 0.76871 0.66811 1.01593 -0.05565 0.07608  -0.03401 153 ASN B CG  
2922 O OD1 . ASN B 153 ? 0.78676 0.65108 1.01982 -0.05072 0.08931  -0.02321 153 ASN B OD1 
2923 N ND2 . ASN B 153 ? 0.76358 0.68463 1.02019 -0.06404 0.07305  -0.04327 153 ASN B ND2 
2924 N N   . GLN B 154 ? 0.65509 0.62333 0.91266 -0.02334 0.01944  -0.02201 154 GLN B N   
2925 C CA  . GLN B 154 ? 0.63377 0.62180 0.89431 -0.01970 0.00860  -0.02669 154 GLN B CA  
2926 C C   . GLN B 154 ? 0.62189 0.64003 0.88788 -0.01910 -0.00310 -0.03343 154 GLN B C   
2927 O O   . GLN B 154 ? 0.70751 0.72965 0.97336 -0.01723 -0.00655 -0.02868 154 GLN B O   
2928 C CB  . GLN B 154 ? 0.61370 0.59421 0.86717 -0.00715 0.00139  -0.01181 154 GLN B CB  
2929 C CG  . GLN B 154 ? 0.60367 0.55914 0.85141 -0.00453 0.01181  -0.00553 154 GLN B CG  
2930 C CD  . GLN B 154 ? 0.61747 0.57127 0.85985 0.00791  0.00427  0.00859  154 GLN B CD  
2931 O OE1 . GLN B 154 ? 0.57071 0.53987 0.81320 0.01251  -0.00765 0.01282  154 GLN B OE1 
2932 N NE2 . GLN B 154 ? 0.68740 0.62228 0.92406 0.01360  0.01240  0.01572  154 GLN B NE2 
2933 N N   . ARG B 155 ? 0.59900 0.63860 0.86863 -0.01970 -0.00858 -0.04479 155 ARG B N   
2934 C CA  . ARG B 155 ? 0.61380 0.68448 0.88720 -0.01717 -0.01838 -0.05302 155 ARG B CA  
2935 C C   . ARG B 155 ? 0.65048 0.73648 0.91920 -0.00788 -0.02847 -0.05443 155 ARG B C   
2936 O O   . ARG B 155 ? 0.64449 0.72420 0.91192 -0.00912 -0.02581 -0.05697 155 ARG B O   
2937 C CB  . ARG B 155 ? 0.61367 0.70388 0.89824 -0.03044 -0.01144 -0.07254 155 ARG B CB  
2938 C CG  . ARG B 155 ? 0.63310 0.71040 0.92124 -0.03994 -0.00087 -0.07256 155 ARG B CG  
2939 C CD  . ARG B 155 ? 0.61770 0.70307 0.90418 -0.03202 -0.00926 -0.06372 155 ARG B CD  
2940 N NE  . ARG B 155 ? 0.65409 0.73001 0.94414 -0.04156 0.00102  -0.06540 155 ARG B NE  
2941 C CZ  . ARG B 155 ? 0.65121 0.69624 0.93408 -0.04094 0.00796  -0.05174 155 ARG B CZ  
2942 N NH1 . ARG B 155 ? 0.60365 0.62695 0.87695 -0.03156 0.00555  -0.03609 155 ARG B NH1 
2943 N NH2 . ARG B 155 ? 0.66941 0.70705 0.95439 -0.04953 0.01790  -0.05446 155 ARG B NH2 
2944 N N   . ASP B 156 ? 0.60070 0.70498 0.86502 0.00229  -0.03902 -0.05242 156 ASP B N   
2945 C CA  . ASP B 156 ? 0.58247 0.69729 0.83731 0.01439  -0.04814 -0.05070 156 ASP B CA  
2946 C C   . ASP B 156 ? 0.60283 0.75373 0.86088 0.01739  -0.05339 -0.06611 156 ASP B C   
2947 O O   . ASP B 156 ? 0.63912 0.80786 0.90173 0.01777  -0.05520 -0.07097 156 ASP B O   
2948 C CB  . ASP B 156 ? 0.61094 0.71372 0.85328 0.02600  -0.05417 -0.03479 156 ASP B CB  
2949 C CG  . ASP B 156 ? 0.65497 0.76519 0.88359 0.03944  -0.06142 -0.03275 156 ASP B CG  
2950 O OD1 . ASP B 156 ? 0.65815 0.75827 0.88126 0.04115  -0.06092 -0.03000 156 ASP B OD1 
2951 O OD2 . ASP B 156 ? 0.63311 0.75852 0.85509 0.04924  -0.06677 -0.03376 156 ASP B OD2 
2952 N N   . ILE B 157 ? 0.58326 0.74732 0.83861 0.02052  -0.05606 -0.07406 157 ILE B N   
2953 C CA  . ILE B 157 ? 0.59967 0.80366 0.85966 0.02252  -0.06053 -0.09161 157 ILE B CA  
2954 C C   . ILE B 157 ? 0.61536 0.83692 0.86262 0.04205  -0.07091 -0.08654 157 ILE B C   
2955 O O   . ILE B 157 ? 0.63467 0.88897 0.88706 0.04548  -0.07461 -0.09713 157 ILE B O   
2956 C CB  . ILE B 157 ? 0.62791 0.84130 0.88917 0.01846  -0.05907 -0.10326 157 ILE B CB  
2957 C CG1 . ILE B 157 ? 0.60244 0.80108 0.87666 -0.00206 -0.04616 -0.11181 157 ILE B CG1 
2958 C CG2 . ILE B 157 ? 0.64452 0.90412 0.90775 0.02425  -0.06589 -0.12080 157 ILE B CG2 
2959 C CD1 . ILE B 157 ? 0.61857 0.81520 0.89282 -0.00776 -0.04203 -0.12031 157 ILE B CD1 
2960 N N   . ARG B 158 ? 0.63374 0.83356 0.86326 0.05540  -0.07450 -0.07067 158 ARG B N   
2961 C CA  . ARG B 158 ? 0.66412 0.87337 0.87716 0.07508  -0.08159 -0.06447 158 ARG B CA  
2962 C C   . ARG B 158 ? 0.64885 0.86194 0.86594 0.07560  -0.08178 -0.06173 158 ARG B C   
2963 O O   . ARG B 158 ? 0.67690 0.91898 0.89168 0.08684  -0.08682 -0.06804 158 ARG B O   
2964 C CB  . ARG B 158 ? 0.65052 0.82766 0.84253 0.08578  -0.08161 -0.04753 158 ARG B CB  
2965 C CG  . ARG B 158 ? 0.60927 0.78168 0.79382 0.08816  -0.08154 -0.04864 158 ARG B CG  
2966 C CD  . ARG B 158 ? 0.65448 0.79501 0.81798 0.09750  -0.07983 -0.03245 158 ARG B CD  
2967 N NE  . ARG B 158 ? 0.74896 0.88034 0.90459 0.09878  -0.07845 -0.03203 158 ARG B NE  
2968 C CZ  . ARG B 158 ? 0.76242 0.87354 0.92492 0.08692  -0.07355 -0.02845 158 ARG B CZ  
2969 N NH1 . ARG B 158 ? 0.75837 0.85559 0.93443 0.07407  -0.06962 -0.02419 158 ARG B NH1 
2970 N NH2 . ARG B 158 ? 0.80737 0.91276 0.96185 0.08945  -0.07240 -0.02891 158 ARG B NH2 
2971 N N   . THR B 159 ? 0.61310 0.79888 0.83563 0.06472  -0.07638 -0.05245 159 THR B N   
2972 C CA  . THR B 159 ? 0.64449 0.83259 0.87140 0.06361  -0.07576 -0.05019 159 THR B CA  
2973 C C   . THR B 159 ? 0.63630 0.86147 0.88010 0.05704  -0.07572 -0.06823 159 THR B C   
2974 O O   . THR B 159 ? 0.61586 0.86269 0.85864 0.06601  -0.07950 -0.07122 159 THR B O   
2975 C CB  . THR B 159 ? 0.59989 0.75705 0.83235 0.05081  -0.06927 -0.04036 159 THR B CB  
2976 O OG1 . THR B 159 ? 0.59607 0.72399 0.81493 0.05530  -0.06906 -0.02583 159 THR B OG1 
2977 C CG2 . THR B 159 ? 0.57311 0.73179 0.80791 0.05068  -0.06874 -0.03749 159 THR B CG2 
2978 N N   . ARG B 160 ? 0.61342 0.84612 0.87248 0.04082  -0.07024 -0.08122 160 ARG B N   
2979 C CA  . ARG B 160 ? 0.61548 0.88140 0.89234 0.02928  -0.06707 -0.10081 160 ARG B CA  
2980 C C   . ARG B 160 ? 0.64408 0.95742 0.92008 0.04262  -0.07578 -0.11405 160 ARG B C   
2981 O O   . ARG B 160 ? 0.65175 0.99467 0.93542 0.04424  -0.07743 -0.12291 160 ARG B O   
2982 C CB  . ARG B 160 ? 0.62142 0.88160 0.91052 0.00957  -0.05752 -0.11256 160 ARG B CB  
2983 C CG  . ARG B 160 ? 0.58380 0.87742 0.89116 -0.00641 -0.05133 -0.13626 160 ARG B CG  
2984 C CD  . ARG B 160 ? 0.59505 0.87693 0.91105 -0.01868 -0.04257 -0.13579 160 ARG B CD  
2985 N NE  . ARG B 160 ? 0.63873 0.94785 0.97209 -0.03799 -0.03313 -0.15994 160 ARG B NE  
2986 C CZ  . ARG B 160 ? 0.63093 0.93452 0.97348 -0.05229 -0.02264 -0.16483 160 ARG B CZ  
2987 N NH1 . ARG B 160 ? 0.63697 0.90840 0.97299 -0.04899 -0.02073 -0.14670 160 ARG B NH1 
2988 N NH2 . ARG B 160 ? 0.64340 0.97449 1.00150 -0.07121 -0.01290 -0.18937 160 ARG B NH2 
2989 N N   . ILE B 161 ? 0.65935 0.98293 0.92573 0.05322  -0.08133 -0.11612 161 ILE B N   
2990 C CA  . ILE B 161 ? 0.69821 1.07167 0.96330 0.06726  -0.08966 -0.13017 161 ILE B CA  
2991 C C   . ILE B 161 ? 0.72798 1.10678 0.97662 0.09145  -0.09688 -0.11859 161 ILE B C   
2992 O O   . ILE B 161 ? 0.70641 1.12841 0.95927 0.10096  -0.10185 -0.13000 161 ILE B O   
2993 C CB  . ILE B 161 ? 0.64932 1.03323 0.90662 0.07336  -0.09341 -0.13574 161 ILE B CB  
2994 C CG1 . ILE B 161 ? 0.67566 1.06599 0.95170 0.04862  -0.08542 -0.15342 161 ILE B CG1 
2995 C CG2 . ILE B 161 ? 0.72999 1.16371 0.97990 0.09459  -0.10350 -0.14595 161 ILE B CG2 
2996 C CD1 . ILE B 161 ? 0.73384 1.12862 1.00281 0.05149  -0.08755 -0.15859 161 ILE B CD1 
2997 N N   . GLU B 162 ? 0.72424 1.05998 0.95359 0.10154  -0.09654 -0.09669 162 GLU B N   
2998 C CA  . GLU B 162 ? 0.69512 1.02705 0.90647 0.12276  -0.10028 -0.08469 162 GLU B CA  
2999 C C   . GLU B 162 ? 0.72841 1.07402 0.95393 0.11614  -0.09845 -0.08911 162 GLU B C   
3000 O O   . GLU B 162 ? 0.71969 1.09693 0.94187 0.13190  -0.10321 -0.09384 162 GLU B O   
3001 C CB  . GLU B 162 ? 0.69664 0.97562 0.88742 0.12764  -0.09690 -0.06264 162 GLU B CB  
3002 C CG  . GLU B 162 ? 0.73830 1.00544 0.90127 0.15283  -0.09884 -0.04937 162 GLU B CG  
3003 C CD  . GLU B 162 ? 0.76323 0.97732 0.90839 0.15195  -0.09284 -0.03019 162 GLU B CD  
3004 O OE1 . GLU B 162 ? 0.71579 0.90637 0.87338 0.13219  -0.08832 -0.02636 162 GLU B OE1 
3005 O OE2 . GLU B 162 ? 0.80912 1.00535 0.92643 0.17137  -0.09180 -0.01960 162 GLU B OE2 
3006 N N   . ALA B 163 ? 0.70454 1.02780 0.94542 0.09371  -0.09109 -0.08801 163 ALA B N   
3007 C CA  . ALA B 163 ? 0.66099 0.99404 0.91512 0.08547  -0.08789 -0.09221 163 ALA B CA  
3008 C C   . ALA B 163 ? 0.67081 1.05861 0.94426 0.08017  -0.08914 -0.11600 163 ALA B C   
3009 O O   . ALA B 163 ? 0.73662 1.15190 1.01311 0.08846  -0.09168 -0.12087 163 ALA B O   
3010 C CB  . ALA B 163 ? 0.64097 0.93800 0.90511 0.06353  -0.07877 -0.08631 163 ALA B CB  
3011 N N   . LEU B 164 ? 0.66781 1.07384 0.95442 0.06614  -0.08682 -0.13218 164 LEU B N   
3012 C CA  . LEU B 164 ? 0.68784 1.15034 0.99363 0.05867  -0.08716 -0.15820 164 LEU B CA  
3013 C C   . LEU B 164 ? 0.70726 1.21791 1.00422 0.08531  -0.09877 -0.16402 164 LEU B C   
3014 O O   . LEU B 164 ? 0.70840 1.26846 1.01892 0.08589  -0.10064 -0.18115 164 LEU B O   
3015 C CB  . LEU B 164 ? 0.68304 1.15247 1.00057 0.03957  -0.08186 -0.17411 164 LEU B CB  
3016 C CG  . LEU B 164 ? 0.66938 1.09997 0.99791 0.01217  -0.06775 -0.17380 164 LEU B CG  
3017 C CD1 . LEU B 164 ? 0.68078 1.10988 1.01502 -0.00283 -0.06197 -0.18605 164 LEU B CD1 
3018 C CD2 . LEU B 164 ? 0.68198 1.13052 1.02866 -0.00473 -0.05932 -0.18773 164 LEU B CD2 
3019 N N   . LEU B 165 ? 0.74354 1.24133 1.01679 0.10834  -0.10585 -0.15034 165 LEU B N   
3020 C CA  . LEU B 165 ? 0.72872 1.26867 0.98836 0.13723  -0.11614 -0.15439 165 LEU B CA  
3021 C C   . LEU B 165 ? 0.76303 1.28460 0.99903 0.16377  -0.11926 -0.13483 165 LEU B C   
3022 O O   . LEU B 165 ? 0.79210 1.34800 1.01429 0.19119  -0.12673 -0.13693 165 LEU B O   
3023 C CB  . LEU B 165 ? 0.73888 1.27888 0.98466 0.14681  -0.12047 -0.15414 165 LEU B CB  
3024 C CG  . LEU B 165 ? 0.72519 1.31712 0.98945 0.13515  -0.12242 -0.18093 165 LEU B CG  
3025 C CD1 . LEU B 165 ? 0.76510 1.35343 1.05743 0.09930  -0.11202 -0.19554 165 LEU B CD1 
3026 C CD2 . LEU B 165 ? 0.80926 1.38495 1.05797 0.14158  -0.12469 -0.17598 165 LEU B CD2 
3027 N N   . LEU B 166 ? 0.70943 1.17833 0.93906 0.15710  -0.11313 -0.11638 166 LEU B N   
3028 C CA  . LEU B 166 ? 0.75751 1.20644 0.96712 0.17724  -0.11338 -0.09975 166 LEU B CA  
3029 C C   . LEU B 166 ? 0.80072 1.24468 0.97736 0.21013  -0.11811 -0.08826 166 LEU B C   
3030 O O   . LEU B 166 ? 0.83100 1.28690 0.99136 0.23502  -0.12050 -0.08337 166 LEU B O   
3031 C CB  . LEU B 166 ? 0.69383 1.18269 0.91852 0.17859  -0.11440 -0.11113 166 LEU B CB  
3032 C CG  . LEU B 166 ? 0.67706 1.15819 0.92810 0.14788  -0.10682 -0.11789 166 LEU B CG  
3033 C CD1 . LEU B 166 ? 0.66165 1.18621 0.92689 0.15032  -0.10759 -0.13057 166 LEU B CD1 
3034 C CD2 . LEU B 166 ? 0.65610 1.07414 0.89698 0.13940  -0.10029 -0.09679 166 LEU B CD2 
3035 N N   . VAL B 167 ? 0.81758 1.24159 0.98247 0.21106  -0.11827 -0.08352 167 VAL B N   
3036 C CA  . VAL B 167 ? 0.82146 1.22866 0.95146 0.23982  -0.11987 -0.07042 167 VAL B CA  
3037 C C   . VAL B 167 ? 0.82647 1.17187 0.94274 0.22980  -0.11283 -0.05360 167 VAL B C   
3038 O O   . VAL B 167 ? 0.83366 1.17197 0.96394 0.20987  -0.11178 -0.05842 167 VAL B O   
3039 C CB  . VAL B 167 ? 0.82685 1.28036 0.95404 0.25421  -0.12761 -0.08404 167 VAL B CB  
3040 C CG1 . VAL B 167 ? 0.82141 1.24697 0.90935 0.28226  -0.12694 -0.06822 167 VAL B CG1 
3041 C CG2 . VAL B 167 ? 0.77491 1.29541 0.91411 0.26708  -0.13493 -0.10144 167 VAL B CG2 
3042 N N   . ARG B 168 ? 0.85821 1.15997 0.94667 0.24350  -0.10713 -0.03491 168 ARG B N   
3043 C CA  . ARG B 168 ? 0.85292 1.09842 0.92718 0.23419  -0.09948 -0.02005 168 ARG B CA  
3044 C C   . ARG B 168 ? 0.88969 1.13475 0.95523 0.23758  -0.10100 -0.02189 168 ARG B C   
3045 O O   . ARG B 168 ? 0.87987 1.14944 0.92900 0.26093  -0.10548 -0.02533 168 ARG B O   
3046 C CB  . ARG B 168 ? 0.86011 1.06379 0.89998 0.25266  -0.09188 -0.00236 168 ARG B CB  
3047 C CG  . ARG B 168 ? 0.82282 0.96983 0.85215 0.23789  -0.08223 0.01110  168 ARG B CG  
3048 C CD  . ARG B 168 ? 0.84996 0.98489 0.89846 0.21701  -0.07950 0.01264  168 ARG B CD  
3049 N NE  . ARG B 168 ? 0.84816 0.93809 0.89222 0.19999  -0.07151 0.02251  168 ARG B NE  
3050 C CZ  . ARG B 168 ? 0.82516 0.87342 0.84069 0.20682  -0.06189 0.03487  168 ARG B CZ  
3051 N NH1 . ARG B 168 ? 0.86797 0.90648 0.85196 0.23260  -0.05783 0.04099  168 ARG B NH1 
3052 N NH2 . ARG B 168 ? 0.80542 0.82135 0.82288 0.18770  -0.05525 0.04062  168 ARG B NH2 
3053 N N   . ASP B 169 ? 0.88609 1.10447 0.96202 0.21534  -0.09722 -0.01960 169 ASP B N   
3054 C CA  . ASP B 169 ? 0.89785 1.11407 0.96949 0.21404  -0.09792 -0.02207 169 ASP B CA  
3055 C C   . ASP B 169 ? 0.90679 1.17761 0.99004 0.22054  -0.10672 -0.03988 169 ASP B C   
3056 O O   . ASP B 169 ? 0.95938 1.24175 1.02268 0.24057  -0.10961 -0.04050 169 ASP B O   
3057 C CB  . ASP B 169 ? 0.89145 1.06924 0.92516 0.23290  -0.09176 -0.00701 169 ASP B CB  
3058 N N   . MET B 170 ? 0.98997 1.29538 1.10483 0.20331  -0.11014 -0.05530 170 MET B N   
3059 C CA  . MET B 170 ? 0.97534 1.33475 1.10800 0.20083  -0.11681 -0.07642 170 MET B CA  
3060 C C   . MET B 170 ? 0.95493 1.30865 1.11539 0.16916  -0.11286 -0.08567 170 MET B C   
3061 O O   . MET B 170 ? 0.91734 1.28147 1.10174 0.15049  -0.11049 -0.09414 170 MET B O   
3062 C CB  . MET B 170 ? 0.96366 1.37258 1.10795 0.20869  -0.12216 -0.08916 170 MET B CB  
3063 C CG  . MET B 170 ? 1.00995 1.48121 1.17595 0.20267  -0.12820 -0.11474 170 MET B CG  
3064 S SD  . MET B 170 ? 1.16202 1.67884 1.30791 0.23250  -0.13762 -0.12344 170 MET B SD  
3065 C CE  . MET B 170 ? 1.03561 1.58610 1.16712 0.26497  -0.14332 -0.12117 170 MET B CE  
3066 N N   . THR B 171 ? 0.96322 1.29854 1.11858 0.16407  -0.11098 -0.08375 171 THR B N   
3067 C CA  . THR B 171 ? 0.90226 1.22415 1.07882 0.13700  -0.10560 -0.08961 171 THR B CA  
3068 C C   . THR B 171 ? 0.91859 1.27728 1.10799 0.12928  -0.10787 -0.11002 171 THR B C   
3069 O O   . THR B 171 ? 0.91388 1.25849 1.11660 0.10907  -0.10220 -0.11477 171 THR B O   
3070 C CB  . THR B 171 ? 0.92574 1.19568 1.08945 0.13353  -0.09999 -0.07212 171 THR B CB  
3071 O OG1 . THR B 171 ? 0.98795 1.25440 1.12983 0.14940  -0.10209 -0.06860 171 THR B OG1 
3072 C CG2 . THR B 171 ? 0.85617 1.09161 1.00809 0.13826  -0.09670 -0.05432 171 THR B CG2 
3073 N N   . THR B 172 ? 0.90509 1.31116 1.08984 0.14546  -0.11551 -0.12262 172 THR B N   
3074 C CA  . THR B 172 ? 0.90022 1.34984 1.10057 0.13549  -0.11756 -0.14615 172 THR B CA  
3075 C C   . THR B 172 ? 0.91601 1.42601 1.12896 0.14045  -0.12341 -0.16502 172 THR B C   
3076 O O   . THR B 172 ? 0.89917 1.42373 1.09834 0.16396  -0.12929 -0.15836 172 THR B O   
3077 C CB  . THR B 172 ? 0.86884 1.32289 1.04972 0.15052  -0.12168 -0.14588 172 THR B CB  
3078 O OG1 . THR B 172 ? 0.94859 1.42248 1.10447 0.18296  -0.12960 -0.13997 172 THR B OG1 
3079 C CG2 . THR B 172 ? 0.84863 1.24419 1.01689 0.14627  -0.11540 -0.12710 172 THR B CG2 
3080 N N   . CYS B 173 ? 0.86714 1.41159 1.10602 0.11764  -0.12045 -0.18920 173 CYS B N   
3081 C CA  . CYS B 173 ? 0.88947 1.49556 1.14522 0.11672  -0.12433 -0.21116 173 CYS B CA  
3082 C C   . CYS B 173 ? 0.94140 1.60675 1.19756 0.12478  -0.13173 -0.23302 173 CYS B C   
3083 O O   . CYS B 173 ? 0.97878 1.64364 1.24182 0.10819  -0.12766 -0.24460 173 CYS B O   
3084 C CB  . CYS B 173 ? 0.85646 1.46263 1.14150 0.08299  -0.11353 -0.22599 173 CYS B CB  
3085 S SG  . CYS B 173 ? 0.77267 1.45903 1.08148 0.07736  -0.11633 -0.25707 173 CYS B SG  
3086 N N   . PRO B 174 ? 1.04091 1.75883 1.28908 0.15069  -0.14231 -0.23949 174 PRO B N   
3087 C CA  . PRO B 174 ? 1.01588 1.80209 1.26836 0.15671  -0.14978 -0.26481 174 PRO B CA  
3088 C C   . PRO B 174 ? 1.00678 1.83278 1.29412 0.12164  -0.14292 -0.29650 174 PRO B C   
3089 O O   . PRO B 174 ? 1.02128 1.84898 1.32833 0.10395  -0.13651 -0.30249 174 PRO B O   
3090 C CB  . PRO B 174 ? 1.01274 1.84633 1.25097 0.19247  -0.16141 -0.26363 174 PRO B CB  
3091 C CG  . PRO B 174 ? 1.07338 1.84671 1.28899 0.21027  -0.15959 -0.23139 174 PRO B CG  
3092 C CD  . PRO B 174 ? 1.01291 1.73075 1.24582 0.17751  -0.14766 -0.22383 174 PRO B CD  
3093 N N   . LEU B 175 ? 1.00552 1.86228 1.29911 0.11105  -0.14302 -0.31740 175 LEU B N   
3094 C CA  . LEU B 175 ? 0.97732 1.86763 1.30103 0.07520  -0.13382 -0.34959 175 LEU B CA  
3095 C C   . LEU B 175 ? 0.99568 1.97968 1.32874 0.08334  -0.14350 -0.38088 175 LEU B C   
3096 O O   . LEU B 175 ? 1.02893 2.04829 1.34282 0.11927  -0.15775 -0.37525 175 LEU B O   
3097 C CB  . LEU B 175 ? 0.94783 1.79528 1.27169 0.05261  -0.12370 -0.35056 175 LEU B CB  
3098 C CG  . LEU B 175 ? 0.92282 1.68233 1.23784 0.04539  -0.11438 -0.32083 175 LEU B CG  
3099 C CD1 . LEU B 175 ? 0.85623 1.57814 1.17031 0.02649  -0.10484 -0.32227 175 LEU B CD1 
3100 C CD2 . LEU B 175 ? 0.86893 1.60606 1.20105 0.02555  -0.10406 -0.31897 175 LEU B CD2 
3101 N N   . PRO B 176 ? 0.94841 1.97372 1.30900 0.05102  -0.13462 -0.41434 176 PRO B N   
3102 C CA  . PRO B 176 ? 0.96442 2.04868 1.31783 0.05568  -0.13453 -0.43886 176 PRO B CA  
3103 C C   . PRO B 176 ? 0.93693 2.02891 1.27865 0.06008  -0.13844 -0.44492 176 PRO B C   
3104 O O   . PRO B 176 ? 0.90952 1.96279 1.25596 0.04609  -0.13646 -0.43910 176 PRO B O   
3105 C CB  . PRO B 176 ? 0.91168 2.01315 1.29103 0.01583  -0.11673 -0.46804 176 PRO B CB  
3106 C CG  . PRO B 176 ? 0.89463 1.93803 1.29257 -0.01350 -0.10601 -0.45995 176 PRO B CG  
3107 C CD  . PRO B 176 ? 0.88210 1.88468 1.26844 0.01277  -0.11781 -0.42491 176 PRO B CD  
3108 N N   . LYS B 177 ? 0.94399 2.08824 1.26995 0.08064  -0.14374 -0.45720 177 LYS B N   
3109 C CA  . LYS B 177 ? 0.95728 2.11306 1.26670 0.09328  -0.14965 -0.45987 177 LYS B CA  
3110 C C   . LYS B 177 ? 0.90314 2.05610 1.23192 0.05420  -0.13711 -0.48399 177 LYS B C   
3111 O O   . LYS B 177 ? 0.86871 2.04527 1.21755 0.02400  -0.12294 -0.51081 177 LYS B O   
3112 C CB  . LYS B 177 ? 0.94135 2.15858 1.23166 0.12247  -0.15568 -0.47061 177 LYS B CB  
3113 N N   . GLY B 178 ? 0.90302 2.02534 1.22372 0.05509  -0.14105 -0.47468 178 GLY B N   
3114 C CA  . GLY B 178 ? 0.91736 2.03602 1.25092 0.02218  -0.12942 -0.49673 178 GLY B CA  
3115 C C   . GLY B 178 ? 0.91083 1.97911 1.26766 -0.01751 -0.11423 -0.49968 178 GLY B C   
3116 O O   . GLY B 178 ? 0.94371 1.99822 1.30844 -0.04534 -0.10234 -0.51594 178 GLY B O   
3117 N N   . THR B 179 ? 0.97580 2.01316 1.34229 -0.02113 -0.11224 -0.48444 179 THR B N   
3118 C CA  . THR B 179 ? 0.99379 1.95319 1.36661 -0.05051 -0.09277 -0.47388 179 THR B CA  
3119 C C   . THR B 179 ? 1.01960 1.90689 1.36903 -0.03813 -0.09259 -0.44298 179 THR B C   
3120 O O   . THR B 179 ? 1.03255 1.86298 1.38480 -0.06192 -0.07655 -0.43929 179 THR B O   
3121 C CB  . THR B 179 ? 1.00683 1.93786 1.38853 -0.05498 -0.08740 -0.45988 179 THR B CB  
3122 O OG1 . THR B 179 ? 1.02376 1.88387 1.41096 -0.08401 -0.06725 -0.45285 179 THR B OG1 
3123 C CG2 . THR B 179 ? 1.01396 1.91678 1.37373 -0.01726 -0.10164 -0.42306 179 THR B CG2 
3124 N N   . LEU B 180 ? 0.97815 1.86727 1.30343 -0.00100 -0.10898 -0.42152 180 LEU B N   
3125 C CA  . LEU B 180 ? 0.97982 1.81007 1.28257 0.01078  -0.10906 -0.39629 180 LEU B CA  
3126 C C   . LEU B 180 ? 0.94519 1.78675 1.24787 -0.00362 -0.10417 -0.41601 180 LEU B C   
3127 O O   . LEU B 180 ? 0.90141 1.69009 1.18949 -0.00134 -0.10031 -0.39851 180 LEU B O   
3128 C CB  . LEU B 180 ? 1.00131 1.83460 1.27625 0.05359  -0.12592 -0.37169 180 LEU B CB  
3129 N N   . ASP B 181 ? 0.95976 1.87006 1.27886 -0.01920 -0.10367 -0.45291 181 ASP B N   
3130 C CA  . ASP B 181 ? 0.86421 1.79619 1.18146 -0.02982 -0.10111 -0.47431 181 ASP B CA  
3131 C C   . ASP B 181 ? 0.86933 1.73134 1.18940 -0.05836 -0.08159 -0.47021 181 ASP B C   
3132 O O   . ASP B 181 ? 0.82735 1.65868 1.16382 -0.08650 -0.06503 -0.47519 181 ASP B O   
3133 C CB  . ASP B 181 ? 0.77566 1.79481 1.11433 -0.04782 -0.10112 -0.51827 181 ASP B CB  
3134 N N   . GLY B 182 ? 0.88887 1.72636 1.19132 -0.04983 -0.08291 -0.46146 182 GLY B N   
3135 C CA  . GLY B 182 ? 0.88068 1.64938 1.18072 -0.06919 -0.06643 -0.45268 182 GLY B CA  
3136 C C   . GLY B 182 ? 0.91888 1.61508 1.20140 -0.05052 -0.06783 -0.41197 182 GLY B C   
3137 O O   . GLY B 182 ? 0.93718 1.57749 1.21517 -0.06145 -0.05591 -0.40199 182 GLY B O   
3138 N N   . PHE B 183 ? 0.87450 1.57130 1.14656 -0.02271 -0.08132 -0.38923 183 PHE B N   
3139 C CA  . PHE B 183 ? 0.89245 1.52231 1.15006 -0.00821 -0.08119 -0.35258 183 PHE B CA  
3140 C C   . PHE B 183 ? 0.88958 1.49331 1.12469 0.00783  -0.08464 -0.33791 183 PHE B C   
3141 O O   . PHE B 183 ? 0.93611 1.57942 1.15743 0.02624  -0.09576 -0.34490 183 PHE B O   
3142 C CB  . PHE B 183 ? 0.89143 1.53183 1.14201 0.01685  -0.09368 -0.33488 183 PHE B CB  
3143 C CG  . PHE B 183 ? 0.89366 1.46846 1.13348 0.02641  -0.09154 -0.30086 183 PHE B CG  
3144 C CD1 . PHE B 183 ? 0.87979 1.41514 1.13394 0.00726  -0.08000 -0.29375 183 PHE B CD1 
3145 C CD2 . PHE B 183 ? 0.92593 1.47819 1.14024 0.05393  -0.09985 -0.27681 183 PHE B CD2 
3146 C CE1 . PHE B 183 ? 0.89595 1.37596 1.14072 0.01590  -0.07853 -0.26408 183 PHE B CE1 
3147 C CE2 . PHE B 183 ? 0.93837 1.43317 1.14366 0.06041  -0.09693 -0.24794 183 PHE B CE2 
3148 C CZ  . PHE B 183 ? 0.92915 1.39032 1.15048 0.04150  -0.08704 -0.24203 183 PHE B CZ  
3149 N N   . VAL B 184 ? 0.93556 1.47432 1.16633 0.00162  -0.07481 -0.31798 184 VAL B N   
3150 C CA  . VAL B 184 ? 0.97790 1.48626 1.18759 0.01669  -0.07694 -0.30125 184 VAL B CA  
3151 C C   . VAL B 184 ? 1.01002 1.46781 1.20792 0.03234  -0.07861 -0.26773 184 VAL B C   
3152 O O   . VAL B 184 ? 1.01902 1.45368 1.22802 0.02425  -0.07388 -0.25852 184 VAL B O   
3153 C CB  . VAL B 184 ? 0.93125 1.41188 1.14559 -0.00499 -0.06285 -0.31055 184 VAL B CB  
3154 N N   . ALA B 185 ? 1.10977 1.55018 1.28431 0.05396  -0.08433 -0.25031 185 ALA B N   
3155 C CA  . ALA B 185 ? 1.14287 1.55275 1.30178 0.07431  -0.08907 -0.22237 185 ALA B CA  
3156 C C   . ALA B 185 ? 1.17692 1.52966 1.34295 0.06245  -0.07895 -0.20371 185 ALA B C   
3157 O O   . ALA B 185 ? 1.20446 1.54541 1.37886 0.06002  -0.07830 -0.19469 185 ALA B O   
3158 C CB  . ALA B 185 ? 1.18133 1.58755 1.31079 0.09980  -0.09558 -0.21067 185 ALA B CB  
3159 N N   . HIS B 186 ? 1.13021 1.44892 1.29275 0.05598  -0.07112 -0.19781 186 HIS B N   
3160 C CA  . HIS B 186 ? 1.16224 1.42983 1.32617 0.05211  -0.06381 -0.17666 186 HIS B CA  
3161 C C   . HIS B 186 ? 1.08777 1.33541 1.27222 0.02806  -0.05119 -0.18353 186 HIS B C   
3162 O O   . HIS B 186 ? 1.09708 1.30722 1.28184 0.02291  -0.04278 -0.17290 186 HIS B O   
3163 C CB  . HIS B 186 ? 1.23727 1.47703 1.38193 0.06388  -0.06289 -0.16187 186 HIS B CB  
3164 C CG  . HIS B 186 ? 1.25146 1.50151 1.37124 0.08867  -0.07228 -0.15250 186 HIS B CG  
3165 N ND1 . HIS B 186 ? 1.24702 1.52070 1.35006 0.10092  -0.07713 -0.16107 186 HIS B ND1 
3166 C CD2 . HIS B 186 ? 1.21962 1.45943 1.32639 0.10427  -0.07669 -0.13601 186 HIS B CD2 
3167 C CE1 . HIS B 186 ? 1.21975 1.49413 1.29876 0.12443  -0.08346 -0.14871 186 HIS B CE1 
3168 N NE2 . HIS B 186 ? 1.23957 1.49265 1.32033 0.12634  -0.08279 -0.13369 186 HIS B NE2 
3169 N N   . ASP B 187 ? 1.05356 1.32597 1.25423 0.01377  -0.04873 -0.20152 187 ASP B N   
3170 C CA  . ASP B 187 ? 1.00219 1.25455 1.21967 -0.00907 -0.03451 -0.20934 187 ASP B CA  
3171 C C   . ASP B 187 ? 1.02767 1.26134 1.25341 -0.01109 -0.03273 -0.19625 187 ASP B C   
3172 O O   . ASP B 187 ? 0.98398 1.24317 1.21252 -0.00558 -0.04077 -0.19788 187 ASP B O   
3173 C CB  . ASP B 187 ? 0.95939 1.24957 1.18862 -0.02627 -0.03023 -0.23956 187 ASP B CB  
3174 C CG  . ASP B 187 ? 0.94149 1.20548 1.18344 -0.05101 -0.01164 -0.24979 187 ASP B CG  
3175 O OD1 . ASP B 187 ? 0.93900 1.15636 1.18011 -0.05240 -0.00286 -0.23233 187 ASP B OD1 
3176 O OD2 . ASP B 187 ? 0.93225 1.22302 1.18397 -0.06881 -0.00491 -0.27605 187 ASP B OD2 
3177 N N   . SER B 188 ? 1.01085 1.20123 1.23961 -0.01766 -0.02219 -0.18324 188 SER B N   
3178 C CA  . SER B 188 ? 0.92249 1.09381 1.15815 -0.01975 -0.01956 -0.17091 188 SER B CA  
3179 C C   . SER B 188 ? 0.88126 1.06970 1.13128 -0.03659 -0.01295 -0.18874 188 SER B C   
3180 O O   . SER B 188 ? 0.90869 1.10442 1.16358 -0.03467 -0.01695 -0.18423 188 SER B O   
3181 C CB  . SER B 188 ? 0.90239 1.02773 1.13735 -0.02209 -0.00905 -0.15507 188 SER B CB  
3182 O OG  . SER B 188 ? 0.89634 1.00745 1.11975 -0.00732 -0.01498 -0.13803 188 SER B OG  
3183 N N   . ILE B 189 ? 0.85629 1.04913 1.11286 -0.05451 -0.00113 -0.20954 189 ILE B N   
3184 C CA  . ILE B 189 ? 0.82685 1.03474 1.09682 -0.07350 0.00797  -0.22873 189 ILE B CA  
3185 C C   . ILE B 189 ? 0.88018 1.14455 1.15552 -0.07002 -0.00494 -0.24437 189 ILE B C   
3186 O O   . ILE B 189 ? 0.89418 1.17579 1.18067 -0.07958 -0.00247 -0.25413 189 ILE B O   
3187 C CB  . ILE B 189 ? 0.79269 0.98735 1.06645 -0.09544 0.02682  -0.24834 189 ILE B CB  
3188 C CG1 . ILE B 189 ? 0.78118 0.91825 1.04881 -0.09676 0.04117  -0.23148 189 ILE B CG1 
3189 C CG2 . ILE B 189 ? 0.77102 0.98427 1.05799 -0.11791 0.03817  -0.27218 189 ILE B CG2 
3190 C CD1 . ILE B 189 ? 0.78137 0.89854 1.04858 -0.11577 0.06132  -0.24841 189 ILE B CD1 
3191 N N   . HIS B 190 ? 0.86483 1.15999 1.13154 -0.05538 -0.01835 -0.24728 190 HIS B N   
3192 C CA  . HIS B 190 ? 0.85687 1.20726 1.12606 -0.04675 -0.03178 -0.25955 190 HIS B CA  
3193 C C   . HIS B 190 ? 0.90157 1.24869 1.16680 -0.02941 -0.04213 -0.23928 190 HIS B C   
3194 O O   . HIS B 190 ? 0.90907 1.29122 1.18237 -0.02898 -0.04728 -0.24873 190 HIS B O   
3195 C CB  . HIS B 190 ? 0.89979 1.28273 1.15716 -0.03275 -0.04274 -0.26699 190 HIS B CB  
3196 C CG  . HIS B 190 ? 0.94713 1.34863 1.21035 -0.05107 -0.03409 -0.29342 190 HIS B CG  
3197 N ND1 . HIS B 190 ? 0.94115 1.36306 1.19289 -0.04160 -0.04065 -0.30017 190 HIS B ND1 
3198 C CD2 . HIS B 190 ? 0.92594 1.32758 1.20382 -0.07890 -0.01811 -0.31556 190 HIS B CD2 
3199 C CE1 . HIS B 190 ? 0.89219 1.32796 1.15244 -0.06317 -0.02995 -0.32578 190 HIS B CE1 
3200 N NE2 . HIS B 190 ? 0.87381 1.29647 1.14967 -0.08660 -0.01543 -0.33582 190 HIS B NE2 
3201 N N   . ASP B 191 ? 1.05431 1.36059 1.30757 -0.01597 -0.04441 -0.21249 191 ASP B N   
3202 C CA  . ASP B 191 ? 1.03966 1.33669 1.28891 -0.00251 -0.05154 -0.19341 191 ASP B CA  
3203 C C   . ASP B 191 ? 1.01520 1.30797 1.27996 -0.01747 -0.04395 -0.19727 191 ASP B C   
3204 O O   . ASP B 191 ? 1.00178 1.31954 1.27016 -0.01186 -0.05065 -0.19898 191 ASP B O   
3205 C CB  . ASP B 191 ? 1.08564 1.33675 1.32235 0.00804  -0.05134 -0.16715 191 ASP B CB  
3206 C CG  . ASP B 191 ? 1.18957 1.44403 1.40735 0.02711  -0.06012 -0.15915 191 ASP B CG  
3207 O OD1 . ASP B 191 ? 1.20925 1.50036 1.41962 0.03994  -0.06985 -0.16686 191 ASP B OD1 
3208 O OD2 . ASP B 191 ? 1.26594 1.48691 1.47529 0.03013  -0.05675 -0.14517 191 ASP B OD2 
3209 N N   . CYS B 192 ? 0.85568 1.11478 1.12788 -0.03529 -0.02904 -0.19782 192 CYS B N   
3210 C CA  . CYS B 192 ? 0.82219 1.06941 1.10578 -0.04889 -0.01961 -0.19916 192 CYS B CA  
3211 C C   . CYS B 192 ? 0.80927 1.10133 1.10659 -0.06193 -0.01812 -0.22514 192 CYS B C   
3212 O O   . CYS B 192 ? 0.76262 1.06586 1.06699 -0.06304 -0.01951 -0.22508 192 CYS B O   
3213 C CB  . CYS B 192 ? 0.77578 0.97744 1.06071 -0.06358 -0.00199 -0.19585 192 CYS B CB  
3214 S SG  . CYS B 192 ? 0.76007 0.91331 1.03207 -0.04817 -0.00350 -0.16478 192 CYS B SG  
3215 N N   . ALA B 193 ? 0.79581 1.11649 1.09751 -0.07241 -0.01510 -0.24873 193 ALA B N   
3216 C CA  . ALA B 193 ? 0.74285 1.11306 1.05909 -0.08643 -0.01337 -0.27691 193 ALA B CA  
3217 C C   . ALA B 193 ? 0.74752 1.16753 1.06310 -0.06677 -0.03188 -0.27758 193 ALA B C   
3218 O O   . ALA B 193 ? 0.75193 1.20670 1.08041 -0.07437 -0.03164 -0.29267 193 ALA B O   
3219 C CB  . ALA B 193 ? 0.74804 1.13997 1.06843 -0.10241 -0.00592 -0.30328 193 ALA B CB  
3220 N N   . LYS B 194 ? 0.74397 1.16779 1.04352 -0.04106 -0.04676 -0.26185 194 LYS B N   
3221 C CA  . LYS B 194 ? 0.70099 1.16250 0.99561 -0.01912 -0.06235 -0.25815 194 LYS B CA  
3222 C C   . LYS B 194 ? 0.78063 1.22056 1.07802 -0.01656 -0.06173 -0.24192 194 LYS B C   
3223 O O   . LYS B 194 ? 0.76027 1.23574 1.06687 -0.01590 -0.06540 -0.25165 194 LYS B O   
3224 C CB  . LYS B 194 ? 0.67748 1.13644 0.94973 0.00836  -0.07510 -0.24192 194 LYS B CB  
3225 N N   . ASP B 195 ? 0.75629 1.14001 1.04632 -0.01554 -0.05674 -0.21810 195 ASP B N   
3226 C CA  . ASP B 195 ? 0.72470 1.08649 1.01463 -0.01101 -0.05714 -0.20086 195 ASP B CA  
3227 C C   . ASP B 195 ? 0.75963 1.12813 1.06773 -0.03189 -0.04657 -0.21438 195 ASP B C   
3228 O O   . ASP B 195 ? 0.70474 1.08350 1.01600 -0.02669 -0.05040 -0.21015 195 ASP B O   
3229 C CB  . ASP B 195 ? 0.72391 1.02896 1.00338 -0.00743 -0.05330 -0.17561 195 ASP B CB  
3230 C CG  . ASP B 195 ? 0.75134 1.04784 1.01123 0.01656  -0.06458 -0.15693 195 ASP B CG  
3231 O OD1 . ASP B 195 ? 0.72643 1.05228 0.97906 0.03321  -0.07500 -0.15739 195 ASP B OD1 
3232 O OD2 . ASP B 195 ? 0.79406 1.05373 1.04486 0.01913  -0.06195 -0.14175 195 ASP B OD2 
3233 N N   . ILE B 196 ? 0.74569 1.10590 1.06431 -0.05570 -0.03180 -0.23057 196 ILE B N   
3234 C CA  . ILE B 196 ? 0.70038 1.06734 1.03484 -0.07760 -0.01902 -0.24646 196 ILE B CA  
3235 C C   . ILE B 196 ? 0.72762 1.16033 1.07423 -0.07872 -0.02600 -0.27046 196 ILE B C   
3236 O O   . ILE B 196 ? 0.73680 1.18420 1.09307 -0.08358 -0.02423 -0.27496 196 ILE B O   
3237 C CB  . ILE B 196 ? 0.69052 1.03095 1.03006 -0.10297 0.00106  -0.25974 196 ILE B CB  
3238 C CG1 . ILE B 196 ? 0.69846 0.97663 1.02565 -0.09958 0.00825  -0.23613 196 ILE B CG1 
3239 C CG2 . ILE B 196 ? 0.65997 1.00092 1.01270 -0.12563 0.01668  -0.27467 196 ILE B CG2 
3240 C CD1 . ILE B 196 ? 0.64855 0.90009 0.97628 -0.11988 0.02753  -0.24836 196 ILE B CD1 
3241 N N   . LEU B 197 ? 0.72205 1.19788 1.06857 -0.07417 -0.03371 -0.28723 197 LEU B N   
3242 C CA  . LEU B 197 ? 0.73572 1.28151 1.09360 -0.07252 -0.04170 -0.31103 197 LEU B CA  
3243 C C   . LEU B 197 ? 0.71791 1.28170 1.06883 -0.04593 -0.05722 -0.29552 197 LEU B C   
3244 O O   . LEU B 197 ? 0.72773 1.33087 1.09080 -0.04803 -0.05894 -0.30824 197 LEU B O   
3245 C CB  . LEU B 197 ? 0.70060 1.28995 1.05666 -0.06885 -0.04852 -0.33001 197 LEU B CB  
3246 C CG  . LEU B 197 ? 0.69886 1.28179 1.06559 -0.10002 -0.03081 -0.35339 197 LEU B CG  
3247 C CD1 . LEU B 197 ? 0.71952 1.33927 1.08250 -0.09695 -0.03692 -0.37066 197 LEU B CD1 
3248 C CD2 . LEU B 197 ? 0.64313 1.25497 1.03095 -0.12606 -0.01837 -0.37958 197 LEU B CD2 
3249 N N   . MET B 198 ? 0.70132 1.23583 1.03205 -0.02127 -0.06730 -0.26867 198 MET B N   
3250 C CA  . MET B 198 ? 0.75325 1.29718 1.07367 0.00432  -0.07970 -0.25264 198 MET B CA  
3251 C C   . MET B 198 ? 0.76350 1.28489 1.09201 -0.00397 -0.07331 -0.24386 198 MET B C   
3252 O O   . MET B 198 ? 0.77676 1.32920 1.10819 0.00659  -0.07977 -0.24602 198 MET B O   
3253 C CB  . MET B 198 ? 0.78589 1.29410 1.08159 0.02828  -0.08764 -0.22602 198 MET B CB  
3254 C CG  . MET B 198 ? 0.74781 1.28813 1.03052 0.04650  -0.09780 -0.23207 198 MET B CG  
3255 S SD  . MET B 198 ? 0.76871 1.25694 1.02116 0.07164  -0.10307 -0.19909 198 MET B SD  
3256 C CE  . MET B 198 ? 0.90956 1.44409 1.14455 0.09632  -0.11499 -0.20857 198 MET B CE  
3257 N N   . MET B 199 ? 0.73621 1.20406 1.06704 -0.02109 -0.06058 -0.23339 199 MET B N   
3258 C CA  . MET B 199 ? 0.72700 1.17261 1.06463 -0.02978 -0.05340 -0.22567 199 MET B CA  
3259 C C   . MET B 199 ? 0.77093 1.25712 1.12929 -0.04893 -0.04595 -0.25195 199 MET B C   
3260 O O   . MET B 199 ? 0.76915 1.26725 1.13258 -0.04587 -0.04755 -0.25019 199 MET B O   
3261 C CB  . MET B 199 ? 0.68516 1.06819 1.01961 -0.04301 -0.04050 -0.21055 199 MET B CB  
3262 C CG  . MET B 199 ? 0.72980 1.07012 1.04602 -0.02496 -0.04689 -0.18131 199 MET B CG  
3263 S SD  . MET B 199 ? 0.69101 0.96508 1.00381 -0.03703 -0.03297 -0.16324 199 MET B SD  
3264 C CE  . MET B 199 ? 0.70934 0.96998 1.02094 -0.04732 -0.02497 -0.17201 199 MET B CE  
3265 N N   . LYS B 200 ? 0.83539 1.34200 1.20592 -0.07037 -0.03631 -0.27732 200 LYS B N   
3266 C CA  . LYS B 200 ? 0.81754 1.36207 1.20852 -0.09271 -0.02633 -0.30510 200 LYS B CA  
3267 C C   . LYS B 200 ? 0.82298 1.43697 1.22089 -0.07725 -0.04081 -0.31816 200 LYS B C   
3268 O O   . LYS B 200 ? 0.83824 1.46997 1.24622 -0.08056 -0.03902 -0.32276 200 LYS B O   
3269 C CB  . LYS B 200 ? 0.76831 1.32170 1.16912 -0.11928 -0.01219 -0.33150 200 LYS B CB  
3270 N N   . TYR B 201 ? 0.77919 1.43288 1.17018 -0.05806 -0.05528 -0.32322 201 TYR B N   
3271 C CA  . TYR B 201 ? 0.78604 1.50667 1.17986 -0.03766 -0.07001 -0.33350 201 TYR B CA  
3272 C C   . TYR B 201 ? 0.80107 1.50466 1.18417 -0.01475 -0.07809 -0.30876 201 TYR B C   
3273 O O   . TYR B 201 ? 0.81042 1.55543 1.20362 -0.01065 -0.08129 -0.31855 201 TYR B O   
3274 C CB  . TYR B 201 ? 0.82298 1.57914 1.20459 -0.01583 -0.08415 -0.33741 201 TYR B CB  
3275 C CG  . TYR B 201 ? 0.80580 1.60707 1.20216 -0.03665 -0.07896 -0.37073 201 TYR B CG  
3276 C CD1 . TYR B 201 ? 0.82725 1.70599 1.24277 -0.04362 -0.08098 -0.40262 201 TYR B CD1 
3277 C CD2 . TYR B 201 ? 0.76419 1.53254 1.15591 -0.05027 -0.07127 -0.37172 201 TYR B CD2 
3278 C CE1 . TYR B 201 ? 0.86655 1.78985 1.29624 -0.06490 -0.07538 -0.43578 201 TYR B CE1 
3279 C CE2 . TYR B 201 ? 0.85759 1.66591 1.26198 -0.07060 -0.06533 -0.40324 201 TYR B CE2 
3280 C CZ  . TYR B 201 ? 0.89407 1.78046 1.31754 -0.07866 -0.06730 -0.43592 201 TYR B CZ  
3281 O OH  . TYR B 201 ? 0.91211 1.84130 1.34862 -0.10097 -0.06064 -0.46983 201 TYR B OH  
3282 N N   . ALA B 202 ? 0.85710 1.50126 1.21993 -0.00030 -0.08076 -0.27775 202 ALA B N   
3283 C CA  . ALA B 202 ? 0.81972 1.43918 1.17192 0.01700  -0.08531 -0.25436 202 ALA B CA  
3284 C C   . ALA B 202 ? 0.83543 1.45182 1.20509 -0.00326 -0.07450 -0.26108 202 ALA B C   
3285 O O   . ALA B 202 ? 0.79702 1.44084 1.16990 0.00736  -0.07937 -0.26202 202 ALA B O   
3286 C CB  . ALA B 202 ? 0.78934 1.34033 1.12139 0.02528  -0.08485 -0.22410 202 ALA B CB  
3287 N N   . LEU B 203 ? 0.84181 1.42501 1.22175 -0.03216 -0.05861 -0.26654 203 LEU B N   
3288 C CA  . LEU B 203 ? 0.86478 1.43945 1.25885 -0.05259 -0.04578 -0.27269 203 LEU B CA  
3289 C C   . LEU B 203 ? 0.86195 1.50535 1.27722 -0.06375 -0.04411 -0.30446 203 LEU B C   
3290 O O   . LEU B 203 ? 0.88425 1.54290 1.30784 -0.06489 -0.04251 -0.30700 203 LEU B O   
3291 C CB  . LEU B 203 ? 0.86231 1.38343 1.25857 -0.07894 -0.02726 -0.27125 203 LEU B CB  
3292 C CG  . LEU B 203 ? 0.86666 1.36742 1.27186 -0.09720 -0.01273 -0.27237 203 LEU B CG  
3293 C CD1 . LEU B 203 ? 0.82008 1.29635 1.21388 -0.07754 -0.02107 -0.24592 203 LEU B CD1 
3294 C CD2 . LEU B 203 ? 0.87688 1.32345 1.28080 -0.12120 0.00764  -0.27121 203 LEU B CD2 
3295 N N   . ARG B 204 ? 0.82115 1.50908 1.24596 -0.07277 -0.04412 -0.33015 204 ARG B N   
3296 C CA  . ARG B 204 ? 0.80659 1.56879 1.25273 -0.08313 -0.04343 -0.36313 204 ARG B CA  
3297 C C   . ARG B 204 ? 0.83151 1.64455 1.27400 -0.05125 -0.06186 -0.35942 204 ARG B C   
3298 O O   . ARG B 204 ? 0.86971 1.72851 1.32792 -0.05532 -0.06088 -0.37571 204 ARG B O   
3299 C CB  . ARG B 204 ? 0.74174 1.54421 1.19751 -0.09819 -0.04059 -0.39203 204 ARG B CB  
3300 N N   . TYR B 205 ? 0.80663 1.61042 1.22696 -0.01873 -0.07748 -0.33778 205 TYR B N   
3301 C CA  . TYR B 205 ? 0.81134 1.65570 1.22266 0.01515  -0.09340 -0.33134 205 TYR B CA  
3302 C C   . TYR B 205 ? 0.76736 1.58476 1.17685 0.02011  -0.09104 -0.31418 205 TYR B C   
3303 O O   . TYR B 205 ? 0.77848 1.64421 1.19665 0.02951  -0.09547 -0.32428 205 TYR B O   
3304 C CB  . TYR B 205 ? 0.83823 1.66582 1.22150 0.04795  -0.10699 -0.30956 205 TYR B CB  
3305 C CG  . TYR B 205 ? 0.83735 1.70303 1.21973 0.05036  -0.11257 -0.32671 205 TYR B CG  
3306 C CD1 . TYR B 205 ? 0.85816 1.78916 1.26423 0.03064  -0.10946 -0.36275 205 TYR B CD1 
3307 C CD2 . TYR B 205 ? 0.86655 1.70205 1.22417 0.07062  -0.11979 -0.30782 205 TYR B CD2 
3308 C CE1 . TYR B 205 ? 0.88023 1.84725 1.28508 0.03221  -0.11453 -0.37938 205 TYR B CE1 
3309 C CE2 . TYR B 205 ? 0.91576 1.78466 1.27127 0.07312  -0.12471 -0.32306 205 TYR B CE2 
3310 C CZ  . TYR B 205 ? 0.90447 1.83948 1.28354 0.05426  -0.12252 -0.35868 205 TYR B CZ  
3311 O OH  . TYR B 205 ? 0.91464 1.88373 1.29099 0.05656  -0.12749 -0.37436 205 TYR B OH  
3312 N N   . ALA B 206 ? 0.82883 1.57149 1.22730 0.01405  -0.08396 -0.28895 206 ALA B N   
3313 C CA  . ALA B 206 ? 0.84016 1.55341 1.23278 0.02196  -0.08306 -0.26974 206 ALA B CA  
3314 C C   . ALA B 206 ? 0.86481 1.60090 1.28047 -0.00060 -0.07223 -0.28787 206 ALA B C   
3315 O O   . ALA B 206 ? 0.82406 1.55574 1.23745 0.00901  -0.07350 -0.27761 206 ALA B O   
3316 C CB  . ALA B 206 ? 0.76807 1.40051 1.14490 0.01854  -0.07753 -0.24118 206 ALA B CB  
3317 N N   . MET B 207 ? 0.83618 1.59517 1.27292 -0.03097 -0.06031 -0.31510 207 MET B N   
3318 C CA  . MET B 207 ? 0.87068 1.64273 1.32810 -0.05682 -0.04610 -0.33267 207 MET B CA  
3319 C C   . MET B 207 ? 0.91887 1.77849 1.39738 -0.05809 -0.04962 -0.36458 207 MET B C   
3320 O O   . MET B 207 ? 0.91354 1.79005 1.40869 -0.07549 -0.03928 -0.37847 207 MET B O   
3321 C CB  . MET B 207 ? 0.88485 1.61863 1.35058 -0.09309 -0.02573 -0.34291 207 MET B CB  
3322 C CG  . MET B 207 ? 0.84390 1.49231 1.29248 -0.09569 -0.01829 -0.31318 207 MET B CG  
3323 S SD  . MET B 207 ? 0.87691 1.48098 1.33179 -0.13471 0.00747  -0.32559 207 MET B SD  
3324 C CE  . MET B 207 ? 0.81897 1.33181 1.25102 -0.12712 0.01133  -0.28647 207 MET B CE  
3325 N N   . GLY B 208 ? 0.93300 1.85009 1.41106 -0.04006 -0.06343 -0.37706 208 GLY B N   
3326 C CA  . GLY B 208 ? 0.92310 1.90663 1.40499 -0.03700 -0.06516 -0.40200 208 GLY B CA  
3327 C C   . GLY B 208 ? 0.91317 1.92221 1.39983 -0.06075 -0.05514 -0.43142 208 GLY B C   
3328 O O   . GLY B 208 ? 0.96222 2.01587 1.45152 -0.06746 -0.04985 -0.45508 208 GLY B O   
3329 N N   . LEU B 209 ? 0.92027 1.90358 1.40761 -0.07323 -0.05194 -0.43153 209 LEU B N   
3330 C CA  . LEU B 209 ? 0.90608 1.90398 1.39828 -0.10004 -0.03894 -0.45928 209 LEU B CA  
3331 C C   . LEU B 209 ? 0.93767 1.98262 1.41645 -0.07920 -0.05176 -0.46926 209 LEU B C   
3332 O O   . LEU B 209 ? 0.99433 2.08507 1.47465 -0.08871 -0.04554 -0.49692 209 LEU B O   
3333 C CB  . LEU B 209 ? 0.85731 1.79751 1.35641 -0.12664 -0.02585 -0.45465 209 LEU B CB  
3334 C CG  . LEU B 209 ? 0.83373 1.72213 1.34433 -0.15254 -0.00788 -0.44810 209 LEU B CG  
3335 C CD1 . LEU B 209 ? 0.80988 1.62908 1.31479 -0.16976 0.00434  -0.43641 209 LEU B CD1 
3336 C CD2 . LEU B 209 ? 0.79400 1.69772 1.31183 -0.17983 0.01212  -0.47410 209 LEU B CD2 
3337 N N   . GLU B 210 ? 0.92530 1.96092 1.38974 -0.05033 -0.06872 -0.44793 210 GLU B N   
3338 C CA  . GLU B 210 ? 0.97113 2.04341 1.42080 -0.03154 -0.07927 -0.45572 210 GLU B CA  
3339 C C   . GLU B 210 ? 1.03719 2.12731 1.46419 0.01451  -0.09909 -0.43492 210 GLU B C   
3340 O O   . GLU B 210 ? 0.98739 2.05489 1.41003 0.03134  -0.10482 -0.41244 210 GLU B O   
3341 C CB  . GLU B 210 ? 0.94453 1.98413 1.39401 -0.04236 -0.07784 -0.45208 210 GLU B CB  
3342 N N   . ASP B 211 ? 1.10789 2.23724 1.51833 0.03522  -0.10798 -0.44285 211 ASP B N   
3343 C CA  . ASP B 211 ? 1.08922 2.23629 1.47236 0.08021  -0.12405 -0.42559 211 ASP B CA  
3344 C C   . ASP B 211 ? 1.14223 2.25522 1.50733 0.10035  -0.13409 -0.40294 211 ASP B C   
3345 O O   . ASP B 211 ? 1.14120 2.25686 1.50801 0.08902  -0.13260 -0.41340 211 ASP B O   
3346 C CB  . ASP B 211 ? 1.01866 2.23360 1.39220 0.09288  -0.12623 -0.44938 211 ASP B CB  
3347 N N   . ALA B 212 ? 1.05513 2.13467 1.40213 0.12950  -0.14308 -0.37252 212 ALA B N   
3348 C CA  . ALA B 212 ? 1.00159 2.04823 1.32706 0.15210  -0.15198 -0.35013 212 ALA B CA  
3349 C C   . ALA B 212 ? 1.02504 2.11115 1.32606 0.17732  -0.15897 -0.35795 212 ALA B C   
3350 O O   . ALA B 212 ? 0.99168 2.11648 1.27826 0.19901  -0.16185 -0.36342 212 ALA B O   
3351 C CB  . ALA B 212 ? 1.02004 2.02323 1.32684 0.17991  -0.15784 -0.31710 212 ALA B CB  
3352 N N   . PRO B 213 ? 1.05191 2.13140 1.34776 0.17534  -0.16124 -0.35964 213 PRO B N   
3353 C CA  . PRO B 213 ? 1.07755 2.19937 1.35302 0.19550  -0.16627 -0.37109 213 PRO B CA  
3354 C C   . PRO B 213 ? 1.12898 2.24335 1.36456 0.24308  -0.17537 -0.34723 213 PRO B C   
3355 O O   . PRO B 213 ? 1.12077 2.18541 1.34048 0.26082  -0.17821 -0.31836 213 PRO B O   
3356 C CB  . PRO B 213 ? 1.07306 2.17771 1.35423 0.17903  -0.16566 -0.37519 213 PRO B CB  
3357 C CG  . PRO B 213 ? 1.01819 2.08927 1.33098 0.13999  -0.15650 -0.37856 213 PRO B CG  
3358 C CD  . PRO B 213 ? 1.03618 2.07619 1.34962 0.14844  -0.15714 -0.35728 213 PRO B CD  
3359 N N   . SER B 214 ? 1.28225 2.44652 1.50022 0.26375  -0.17821 -0.36052 214 SER B N   
3360 C CA  . SER B 214 ? 1.31913 2.47567 1.49486 0.30885  -0.18476 -0.34027 214 SER B CA  
3361 C C   . SER B 214 ? 1.34033 2.46488 1.50067 0.31546  -0.18815 -0.32820 214 SER B C   
3362 O O   . SER B 214 ? 1.33077 2.46254 1.51214 0.28802  -0.18653 -0.34405 214 SER B O   
3363 C CB  . SER B 214 ? 1.26421 2.48812 1.42681 0.32905  -0.18583 -0.36007 214 SER B CB  
3364 O OG  . SER B 214 ? 1.20442 2.47234 1.38041 0.31220  -0.18455 -0.38724 214 SER B OG  
3365 N N   . GLU B 215 ? 1.29711 2.38370 1.41857 0.35206  -0.19150 -0.30007 215 GLU B N   
3366 C CA  . GLU B 215 ? 1.30658 2.35943 1.40928 0.36117  -0.19408 -0.28670 215 GLU B CA  
3367 C C   . GLU B 215 ? 1.26027 2.36300 1.36300 0.35963  -0.19592 -0.31013 215 GLU B C   
3368 O O   . GLU B 215 ? 1.23649 2.32152 1.33858 0.35207  -0.19747 -0.30876 215 GLU B O   
3369 C CB  . GLU B 215 ? 1.32236 2.32833 1.37801 0.40281  -0.19429 -0.25456 215 GLU B CB  
3370 N N   . GLU B 216 ? 1.23911 2.40547 1.34238 0.36724  -0.19546 -0.33215 216 GLU B N   
3371 C CA  . GLU B 216 ? 1.18497 2.40708 1.29697 0.35856  -0.19558 -0.36021 216 GLU B CA  
3372 C C   . GLU B 216 ? 1.20429 2.44095 1.36065 0.30912  -0.19073 -0.38584 216 GLU B C   
3373 O O   . GLU B 216 ? 1.13081 2.38360 1.29559 0.29407  -0.18990 -0.40164 216 GLU B O   
3374 C CB  . GLU B 216 ? 1.10091 2.38962 1.20247 0.38055  -0.19535 -0.37759 216 GLU B CB  
3375 N N   . GLU B 217 ? 1.20242 2.43130 1.38607 0.28327  -0.18601 -0.39035 217 GLU B N   
3376 C CA  . GLU B 217 ? 1.15017 2.39640 1.37382 0.23659  -0.17765 -0.41765 217 GLU B CA  
3377 C C   . GLU B 217 ? 1.12199 2.31178 1.36424 0.20729  -0.17465 -0.40833 217 GLU B C   
3378 O O   . GLU B 217 ? 1.04530 2.24138 1.31787 0.16771  -0.16534 -0.43007 217 GLU B O   
3379 C CB  . GLU B 217 ? 1.10340 2.37417 1.34641 0.22297  -0.17189 -0.43029 217 GLU B CB  
3380 N N   . CYS B 218 ? 1.16751 2.30179 1.39178 0.22504  -0.18057 -0.37762 218 CYS B N   
3381 C CA  . CYS B 218 ? 1.15846 2.24131 1.40149 0.19887  -0.17766 -0.36848 218 CYS B CA  
3382 C C   . CYS B 218 ? 1.13903 2.20546 1.37236 0.19956  -0.18094 -0.36590 218 CYS B C   
3383 O O   . CYS B 218 ? 1.16908 2.24174 1.37138 0.23123  -0.18772 -0.35657 218 CYS B O   
3384 C CB  . CYS B 218 ? 1.20711 2.23729 1.44236 0.21310  -0.18024 -0.33723 218 CYS B CB  
3385 S SG  . CYS B 218 ? 1.36321 2.35656 1.54951 0.26457  -0.18892 -0.30127 218 CYS B SG  
3386 N N   . ASP B 219 ? 1.03817 2.08254 1.29730 0.16405  -0.17483 -0.37486 219 ASP B N   
3387 C CA  . ASP B 219 ? 1.03253 2.04759 1.28025 0.16020  -0.17359 -0.37087 219 ASP B CA  
3388 C C   . ASP B 219 ? 1.01181 1.95942 1.22388 0.18941  -0.17577 -0.33230 219 ASP B C   
3389 O O   . ASP B 219 ? 1.01466 1.90522 1.22351 0.18818  -0.17021 -0.30875 219 ASP B O   
3390 C CB  . ASP B 219 ? 1.03365 2.00664 1.30446 0.11543  -0.15733 -0.37985 219 ASP B CB  
3391 N N   . PRO B 220 ? 1.02606 1.97874 1.21004 0.21565  -0.18292 -0.32567 220 PRO B N   
3392 C CA  . PRO B 220 ? 1.01878 1.90594 1.16664 0.24279  -0.18277 -0.28999 220 PRO B CA  
3393 C C   . PRO B 220 ? 0.99269 1.79600 1.14302 0.21891  -0.17009 -0.27075 220 PRO B C   
3394 O O   . PRO B 220 ? 0.98647 1.73147 1.11407 0.23420  -0.16733 -0.24155 220 PRO B O   
3395 C CB  . PRO B 220 ? 1.01240 1.92767 1.13324 0.26921  -0.19090 -0.29324 220 PRO B CB  
3396 C CG  . PRO B 220 ? 0.92270 1.89833 1.07007 0.24404  -0.19196 -0.32925 220 PRO B CG  
3397 C CD  . PRO B 220 ? 0.95830 1.97731 1.14109 0.22134  -0.19054 -0.35136 220 PRO B CD  
3398 N N   . LEU B 221 ? 1.00497 1.80091 1.18108 0.18228  -0.16140 -0.28683 221 LEU B N   
3399 C CA  . LEU B 221 ? 1.00543 1.72575 1.18350 0.16178  -0.14954 -0.26913 221 LEU B CA  
3400 C C   . LEU B 221 ? 1.09808 1.77786 1.28526 0.15338  -0.14374 -0.25267 221 LEU B C   
3401 O O   . LEU B 221 ? 1.12461 1.74030 1.30726 0.14496  -0.13579 -0.23234 221 LEU B O   
3402 C CB  . LEU B 221 ? 0.93218 1.65556 1.13360 0.12669  -0.14041 -0.29111 221 LEU B CB  
3403 N N   . SER B 222 ? 1.11853 1.83664 1.31779 0.15667  -0.14781 -0.26122 222 SER B N   
3404 C CA  . SER B 222 ? 1.11824 1.80542 1.32801 0.14769  -0.14251 -0.24890 222 SER B CA  
3405 C C   . SER B 222 ? 1.16177 1.81850 1.34444 0.17816  -0.14688 -0.22080 222 SER B C   
3406 O O   . SER B 222 ? 1.14946 1.74959 1.32981 0.17156  -0.14016 -0.20045 222 SER B O   
3407 C CB  . SER B 222 ? 1.07654 1.82062 1.31363 0.13418  -0.14324 -0.27365 222 SER B CB  
3408 O OG  . SER B 222 ? 1.09555 1.90031 1.32311 0.16314  -0.15568 -0.28119 222 SER B OG  
3409 N N   . LEU B 223 ? 1.14013 1.83382 1.30134 0.21170  -0.15714 -0.21990 223 LEU B N   
3410 C CA  . LEU B 223 ? 1.17997 1.84207 1.31161 0.24193  -0.15902 -0.19369 223 LEU B CA  
3411 C C   . LEU B 223 ? 1.25966 1.85498 1.36449 0.24849  -0.15325 -0.16956 223 LEU B C   
3412 O O   . LEU B 223 ? 1.29988 1.89793 1.39338 0.25266  -0.15442 -0.17304 223 LEU B O   
3413 C CB  . LEU B 223 ? 1.10022 1.81810 1.21206 0.27900  -0.17014 -0.19882 223 LEU B CB  
3414 N N   . PRO B 224 ? 1.29574 1.83165 1.39034 0.24825  -0.14637 -0.14615 224 PRO B N   
3415 C CA  . PRO B 224 ? 1.31569 1.78852 1.38532 0.25301  -0.13945 -0.12394 224 PRO B CA  
3416 C C   . PRO B 224 ? 1.35532 1.79213 1.39322 0.27867  -0.13669 -0.10070 224 PRO B C   
3417 O O   . PRO B 224 ? 1.34971 1.81580 1.38204 0.29770  -0.14169 -0.10226 224 PRO B O   
3418 C CB  . PRO B 224 ? 1.21312 1.64729 1.30785 0.21827  -0.13091 -0.12185 224 PRO B CB  
3419 N N   . MET C 1   ? 1.68687 1.61301 1.28149 0.38172  0.06885  0.31225  1   MET C N   
3420 C CA  . MET C 1   ? 1.74180 1.66867 1.37215 0.34097  0.06430  0.29485  1   MET C CA  
3421 C C   . MET C 1   ? 1.76121 1.73187 1.39361 0.33286  0.04994  0.28463  1   MET C C   
3422 O O   . MET C 1   ? 1.74228 1.77445 1.38578 0.33555  0.02950  0.27483  1   MET C O   
3423 C CB  . MET C 1   ? 1.72778 1.67620 1.40112 0.31813  0.05198  0.28038  1   MET C CB  
3424 C CG  . MET C 1   ? 1.80703 1.75721 1.51677 0.27853  0.04698  0.26264  1   MET C CG  
3425 S SD  . MET C 1   ? 1.72108 1.74190 1.45674 0.26020  0.02122  0.24230  1   MET C SD  
3426 C CE  . MET C 1   ? 1.61156 1.66691 1.37794 0.25513  0.00678  0.23290  1   MET C CE  
3427 N N   . PHE C 2   ? 1.79753 1.73610 1.41924 0.32181  0.06187  0.28593  2   PHE C N   
3428 C CA  . PHE C 2   ? 1.76457 1.73436 1.38712 0.31102  0.05196  0.27622  2   PHE C CA  
3429 C C   . PHE C 2   ? 1.74777 1.72557 1.41142 0.27123  0.04475  0.25677  2   PHE C C   
3430 O O   . PHE C 2   ? 1.74101 1.68365 1.42542 0.25170  0.05393  0.25383  2   PHE C O   
3431 C CB  . PHE C 2   ? 1.76261 1.69117 1.34913 0.32156  0.07013  0.28869  2   PHE C CB  
3432 C CG  . PHE C 2   ? 1.78485 1.71632 1.32423 0.36318  0.07442  0.30666  2   PHE C CG  
3433 C CD1 . PHE C 2   ? 1.77172 1.75667 1.30418 0.38848  0.05784  0.30794  2   PHE C CD1 
3434 C CD2 . PHE C 2   ? 1.81605 1.69721 1.31657 0.37760  0.09591  0.32201  2   PHE C CD2 
3435 C CE1 . PHE C 2   ? 1.81650 1.80612 1.30360 0.42962  0.06175  0.32485  2   PHE C CE1 
3436 C CE2 . PHE C 2   ? 1.83151 1.71209 1.28484 0.41813  0.10118  0.33971  2   PHE C CE2 
3437 C CZ  . PHE C 2   ? 1.81320 1.74894 1.25948 0.44534  0.08360  0.34147  2   PHE C CZ  
3438 N N   . ASP C 3   ? 1.57145 1.59624 1.24501 0.26002  0.02901  0.24306  3   ASP C N   
3439 C CA  . ASP C 3   ? 1.45563 1.48121 1.15637 0.22636  0.02602  0.22707  3   ASP C CA  
3440 C C   . ASP C 3   ? 1.45519 1.45482 1.13532 0.22418  0.03763  0.23106  3   ASP C C   
3441 O O   . ASP C 3   ? 1.48011 1.45244 1.12663 0.24644  0.05051  0.24684  3   ASP C O   
3442 C CB  . ASP C 3   ? 1.38243 1.46788 1.10403 0.21333  0.00556  0.20897  3   ASP C CB  
3443 C CG  . ASP C 3   ? 1.40278 1.50544 1.15303 0.20499  -0.00351 0.20144  3   ASP C CG  
3444 O OD1 . ASP C 3   ? 1.37852 1.44365 1.14060 0.20002  0.00553  0.20642  3   ASP C OD1 
3445 O OD2 . ASP C 3   ? 1.36284 1.51720 1.12452 0.20137  -0.01904 0.18903  3   ASP C OD2 
3446 N N   . PHE C 4   ? 1.35865 1.36368 1.05658 0.19817  0.03470  0.21732  4   PHE C N   
3447 C CA  . PHE C 4   ? 1.32145 1.30482 1.00048 0.19582  0.04523  0.22022  4   PHE C CA  
3448 C C   . PHE C 4   ? 1.28443 1.29649 0.97836 0.17336  0.03532  0.20303  4   PHE C C   
3449 O O   . PHE C 4   ? 1.26934 1.29997 0.99293 0.15288  0.02585  0.18877  4   PHE C O   
3450 C CB  . PHE C 4   ? 1.32128 1.24542 1.00163 0.18676  0.06600  0.22696  4   PHE C CB  
3451 C CG  . PHE C 4   ? 1.29173 1.20605 1.00995 0.15801  0.06583  0.21424  4   PHE C CG  
3452 C CD1 . PHE C 4   ? 1.29506 1.19570 1.03210 0.15464  0.06782  0.21489  4   PHE C CD1 
3453 C CD2 . PHE C 4   ? 1.27582 1.19351 1.00881 0.13592  0.06461  0.20203  4   PHE C CD2 
3454 C CE1 . PHE C 4   ? 1.23270 1.12596 1.00233 0.13059  0.06773  0.20355  4   PHE C CE1 
3455 C CE2 . PHE C 4   ? 1.18213 1.09124 0.94701 0.11313  0.06495  0.19135  4   PHE C CE2 
3456 C CZ  . PHE C 4   ? 1.18176 1.07974 0.96472 0.11086  0.06619  0.19213  4   PHE C CZ  
3457 N N   . ILE C 5   ? 1.31505 1.32730 0.98571 0.17781  0.03917  0.20483  5   ILE C N   
3458 C CA  . ILE C 5   ? 1.29388 1.32537 0.97277 0.15741  0.03369  0.18978  5   ILE C CA  
3459 C C   . ILE C 5   ? 1.27404 1.26266 0.94415 0.14939  0.05018  0.19395  5   ILE C C   
3460 O O   . ILE C 5   ? 1.25151 1.20789 0.89595 0.16584  0.06408  0.20901  5   ILE C O   
3461 C CB  . ILE C 5   ? 1.28288 1.36516 0.94283 0.16824  0.02088  0.18418  5   ILE C CB  
3462 C CG1 . ILE C 5   ? 1.28927 1.38962 0.96065 0.14306  0.01623  0.16601  5   ILE C CG1 
3463 C CG2 . ILE C 5   ? 1.30201 1.37284 0.92164 0.19564  0.02906  0.20036  5   ILE C CG2 
3464 C CD1 . ILE C 5   ? 1.31468 1.47120 0.97346 0.14707  0.00283  0.15496  5   ILE C CD1 
3465 N N   . ILE C 6   ? 1.23549 1.22245 0.92616 0.12425  0.04989  0.18042  6   ILE C N   
3466 C CA  . ILE C 6   ? 1.15979 1.11045 0.84794 0.11370  0.06471  0.18157  6   ILE C CA  
3467 C C   . ILE C 6   ? 1.21066 1.18223 0.89958 0.09889  0.05936  0.16797  6   ILE C C   
3468 O O   . ILE C 6   ? 1.13216 1.13908 0.83327 0.08889  0.04603  0.15455  6   ILE C O   
3469 C CB  . ILE C 6   ? 1.17190 1.09074 0.88793 0.09735  0.07360  0.17918  6   ILE C CB  
3470 C CG1 . ILE C 6   ? 1.14053 1.08143 0.88797 0.07761  0.06178  0.16339  6   ILE C CG1 
3471 C CG2 . ILE C 6   ? 1.21354 1.10884 0.92817 0.10993  0.08100  0.19138  6   ILE C CG2 
3472 C CD1 . ILE C 6   ? 1.03360 0.94883 0.80745 0.06146  0.06952  0.15892  6   ILE C CD1 
3473 N N   . ASP C 7   ? 1.28736 1.23428 0.96218 0.09666  0.07172  0.17107  7   ASP C N   
3474 C CA  . ASP C 7   ? 1.21447 1.17682 0.88245 0.08613  0.06934  0.16046  7   ASP C CA  
3475 C C   . ASP C 7   ? 1.19527 1.11954 0.86010 0.07826  0.08599  0.16317  7   ASP C C   
3476 O O   . ASP C 7   ? 1.21840 1.11327 0.86495 0.09061  0.09925  0.17661  7   ASP C O   
3477 C CB  . ASP C 7   ? 1.20366 1.19622 0.84074 0.10371  0.06240  0.16347  7   ASP C CB  
3478 C CG  . ASP C 7   ? 1.29471 1.31394 0.92901 0.09008  0.05631  0.14827  7   ASP C CG  
3479 O OD1 . ASP C 7   ? 1.27695 1.28636 0.93195 0.06790  0.05878  0.13670  7   ASP C OD1 
3480 O OD2 . ASP C 7   ? 1.42626 1.47658 1.03681 0.10201  0.04957  0.14744  7   ASP C OD2 
3481 N N   . PHE C 8   ? 1.15588 1.07950 0.83789 0.05804  0.08655  0.15028  8   PHE C N   
3482 C CA  . PHE C 8   ? 1.17309 1.06661 0.85507 0.04910  0.10131  0.15017  8   PHE C CA  
3483 C C   . PHE C 8   ? 1.20997 1.11694 0.87740 0.04281  0.10006  0.14162  8   PHE C C   
3484 O O   . PHE C 8   ? 1.21867 1.15499 0.89064 0.03455  0.08844  0.12937  8   PHE C O   
3485 C CB  . PHE C 8   ? 1.14412 1.02325 0.85884 0.03207  0.10495  0.14232  8   PHE C CB  
3486 C CG  . PHE C 8   ? 1.13132 0.98876 0.85987 0.03538  0.11191  0.15009  8   PHE C CG  
3487 C CD1 . PHE C 8   ? 1.15572 0.98107 0.87697 0.03786  0.12929  0.15810  8   PHE C CD1 
3488 C CD2 . PHE C 8   ? 1.07894 0.94735 0.82788 0.03426  0.10250  0.14802  8   PHE C CD2 
3489 C CE1 . PHE C 8   ? 1.14542 0.95054 0.87918 0.03850  0.13754  0.16315  8   PHE C CE1 
3490 C CE2 . PHE C 8   ? 1.06280 0.91143 0.82426 0.03627  0.10954  0.15400  8   PHE C CE2 
3491 C CZ  . PHE C 8   ? 1.07237 0.88961 0.82638 0.03786  0.12725  0.16105  8   PHE C CZ  
3492 N N   . GLU C 9   ? 1.20715 1.09169 0.85640 0.04570  0.11330  0.14728  9   GLU C N   
3493 C CA  . GLU C 9   ? 1.20117 1.08861 0.84282 0.03521  0.11624  0.13798  9   GLU C CA  
3494 C C   . GLU C 9   ? 1.14125 1.00000 0.80199 0.02173  0.12925  0.13463  9   GLU C C   
3495 O O   . GLU C 9   ? 1.13185 0.96372 0.79564 0.02520  0.14154  0.14336  9   GLU C O   
3496 C CB  . GLU C 9   ? 1.29543 1.18327 0.90060 0.04911  0.12083  0.14575  9   GLU C CB  
3497 C CG  . GLU C 9   ? 1.35053 1.27705 0.93798 0.06237  0.10572  0.14570  9   GLU C CG  
3498 C CD  . GLU C 9   ? 1.42474 1.35825 0.97517 0.07667  0.10832  0.15138  9   GLU C CD  
3499 O OE1 . GLU C 9   ? 1.49744 1.39990 1.03449 0.07739  0.12340  0.15772  9   GLU C OE1 
3500 O OE2 . GLU C 9   ? 1.46805 1.44006 1.00280 0.08711  0.09548  0.14870  9   GLU C OE2 
3501 N N   . THR C 10  ? 1.11113 0.97648 0.78513 0.00641  0.12716  0.12116  10  THR C N   
3502 C CA  . THR C 10  ? 1.08711 0.93328 0.78502 -0.00506 0.13596  0.11623  10  THR C CA  
3503 C C   . THR C 10  ? 1.09385 0.93382 0.78451 -0.01391 0.14358  0.10835  10  THR C C   
3504 O O   . THR C 10  ? 1.12986 0.98310 0.80090 -0.01484 0.13986  0.10361  10  THR C O   
3505 C CB  . THR C 10  ? 1.11626 0.97270 0.84201 -0.01342 0.12672  0.10796  10  THR C CB  
3506 O OG1 . THR C 10  ? 1.10565 0.98132 0.82816 -0.02179 0.11802  0.09609  10  THR C OG1 
3507 C CG2 . THR C 10  ? 1.07841 0.94253 0.81091 -0.00478 0.11867  0.11520  10  THR C CG2 
3508 N N   . MET C 11  ? 1.08826 0.90951 0.79523 -0.02015 0.15474  0.10641  11  MET C N   
3509 C CA  . MET C 11  ? 1.10095 0.91388 0.80661 -0.02840 0.16356  0.09860  11  MET C CA  
3510 C C   . MET C 11  ? 1.14779 0.96272 0.87665 -0.03764 0.16147  0.08780  11  MET C C   
3511 O O   . MET C 11  ? 1.14462 0.95030 0.87579 -0.04280 0.17038  0.08186  11  MET C O   
3512 C CB  . MET C 11  ? 1.10655 0.89792 0.81163 -0.02696 0.17999  0.10423  11  MET C CB  
3513 C CG  . MET C 11  ? 1.23128 1.01415 0.90597 -0.01934 0.18693  0.11275  11  MET C CG  
3514 S SD  . MET C 11  ? 1.20341 0.99278 0.85649 -0.02460 0.18736  0.10409  11  MET C SD  
3515 C CE  . MET C 11  ? 1.26704 1.04875 0.88196 -0.01113 0.19357  0.11703  11  MET C CE  
3516 N N   . GLY C 12  ? 1.11826 0.94377 0.86308 -0.03844 0.15090  0.08568  12  GLY C N   
3517 C CA  . GLY C 12  ? 1.11422 0.93829 0.88016 -0.04424 0.15024  0.07757  12  GLY C CA  
3518 C C   . GLY C 12  ? 1.14753 0.98556 0.91891 -0.04647 0.13741  0.07361  12  GLY C C   
3519 O O   . GLY C 12  ? 1.15895 1.01098 0.92003 -0.04376 0.12856  0.07648  12  GLY C O   
3520 N N   . SER C 13  ? 1.19057 1.02526 0.97779 -0.05039 0.13705  0.06697  13  SER C N   
3521 C CA  . SER C 13  ? 1.18349 1.02751 0.97459 -0.05458 0.12755  0.06126  13  SER C CA  
3522 C C   . SER C 13  ? 1.13797 0.98764 0.94976 -0.04993 0.12027  0.06617  13  SER C C   
3523 O O   . SER C 13  ? 1.16367 1.02717 0.97391 -0.04942 0.11044  0.06755  13  SER C O   
3524 C CB  . SER C 13  ? 1.22539 1.05788 1.01608 -0.06085 0.13329  0.05120  13  SER C CB  
3525 O OG  . SER C 13  ? 1.23877 1.06095 1.04760 -0.05568 0.13904  0.05249  13  SER C OG  
3526 N N   . GLY C 14  ? 0.99220 0.83407 0.82345 -0.04637 0.12488  0.06806  14  GLY C N   
3527 C CA  . GLY C 14  ? 1.03977 0.88659 0.89137 -0.04358 0.11849  0.06957  14  GLY C CA  
3528 C C   . GLY C 14  ? 1.03030 0.88280 0.88873 -0.03844 0.11462  0.07845  14  GLY C C   
3529 O O   . GLY C 14  ? 1.06358 0.91849 0.90712 -0.03579 0.11384  0.08435  14  GLY C O   
3530 N N   . GLU C 15  ? 0.97740 0.83155 0.85712 -0.03604 0.11264  0.07934  15  GLU C N   
3531 C CA  . GLU C 15  ? 0.89115 0.74596 0.77894 -0.03187 0.11257  0.08686  15  GLU C CA  
3532 C C   . GLU C 15  ? 0.94686 0.79190 0.83788 -0.03162 0.12544  0.08906  15  GLU C C   
3533 O O   . GLU C 15  ? 0.99136 0.83189 0.88560 -0.02941 0.12920  0.09492  15  GLU C O   
3534 C CB  . GLU C 15  ? 0.87984 0.74063 0.78964 -0.03076 0.10679  0.08548  15  GLU C CB  
3535 C CG  . GLU C 15  ? 0.89495 0.75486 0.82372 -0.03118 0.11373  0.08021  15  GLU C CG  
3536 C CD  . GLU C 15  ? 0.96624 0.83449 0.91605 -0.02932 0.10778  0.07747  15  GLU C CD  
3537 O OE1 . GLU C 15  ? 0.96240 0.83489 0.91225 -0.02855 0.09821  0.07933  15  GLU C OE1 
3538 O OE2 . GLU C 15  ? 0.98167 0.85447 0.94828 -0.02838 0.11289  0.07280  15  GLU C OE2 
3539 N N   . LYS C 16  ? 0.94218 0.78307 0.83279 -0.03424 0.13356  0.08378  16  LYS C N   
3540 C CA  . LYS C 16  ? 0.89558 0.72880 0.78831 -0.03551 0.14704  0.08431  16  LYS C CA  
3541 C C   . LYS C 16  ? 0.92189 0.74544 0.78952 -0.03572 0.15335  0.08789  16  LYS C C   
3542 O O   . LYS C 16  ? 0.97998 0.79614 0.84647 -0.03780 0.16568  0.08671  16  LYS C O   
3543 C CB  . LYS C 16  ? 0.86005 0.69864 0.77103 -0.03688 0.15274  0.07553  16  LYS C CB  
3544 C CG  . LYS C 16  ? 0.84393 0.69445 0.77849 -0.03504 0.14649  0.07152  16  LYS C CG  
3545 C CD  . LYS C 16  ? 0.79924 0.65151 0.74636 -0.03639 0.14808  0.07446  16  LYS C CD  
3546 C CE  . LYS C 16  ? 0.83684 0.69081 0.79667 -0.04059 0.16199  0.06975  16  LYS C CE  
3547 N NZ  . LYS C 16  ? 0.83800 0.69243 0.81073 -0.04374 0.16503  0.07066  16  LYS C NZ  
3548 N N   . ALA C 17  ? 0.91335 0.73914 0.76100 -0.03371 0.14530  0.09137  17  ALA C N   
3549 C CA  . ALA C 17  ? 0.99029 0.81047 0.81223 -0.03319 0.14980  0.09378  17  ALA C CA  
3550 C C   . ALA C 17  ? 0.97341 0.78011 0.78336 -0.02919 0.16078  0.10274  17  ALA C C   
3551 O O   . ALA C 17  ? 0.94653 0.74885 0.75948 -0.02504 0.16147  0.10955  17  ALA C O   
3552 C CB  . ALA C 17  ? 1.02628 0.85819 0.83098 -0.03165 0.13778  0.09414  17  ALA C CB  
3553 N N   . ALA C 18  ? 0.99791 0.79537 0.79185 -0.03032 0.17080  0.10281  18  ALA C N   
3554 C CA  . ALA C 18  ? 1.01021 0.79151 0.78533 -0.02569 0.18244  0.11208  18  ALA C CA  
3555 C C   . ALA C 18  ? 1.02899 0.81378 0.77912 -0.01561 0.17426  0.12133  18  ALA C C   
3556 O O   . ALA C 18  ? 1.04869 0.84961 0.78830 -0.01447 0.16252  0.11839  18  ALA C O   
3557 C CB  . ALA C 18  ? 0.99043 0.76166 0.75284 -0.02905 0.19496  0.10969  18  ALA C CB  
3558 N N   . VAL C 19  ? 1.01948 0.78999 0.75953 -0.00797 0.18123  0.13183  19  VAL C N   
3559 C CA  . VAL C 19  ? 1.04423 0.81933 0.76146 0.00523  0.17355  0.14176  19  VAL C CA  
3560 C C   . VAL C 19  ? 1.13070 0.88929 0.81395 0.01422  0.18506  0.15104  19  VAL C C   
3561 O O   . VAL C 19  ? 1.12046 0.85263 0.79823 0.01357  0.20301  0.15586  19  VAL C O   
3562 C CB  . VAL C 19  ? 1.04455 0.81405 0.77174 0.01055  0.17265  0.14814  19  VAL C CB  
3563 C CG1 . VAL C 19  ? 1.08564 0.87677 0.83943 0.00481  0.15736  0.13996  19  VAL C CG1 
3564 C CG2 . VAL C 19  ? 1.00293 0.74790 0.74230 0.00406  0.19072  0.14848  19  VAL C CG2 
3565 N N   . ILE C 20  ? 1.15438 0.92942 0.81429 0.02191  0.17555  0.15243  20  ILE C N   
3566 C CA  . ILE C 20  ? 1.17240 0.93472 0.79582 0.03443  0.18447  0.16276  20  ILE C CA  
3567 C C   . ILE C 20  ? 1.21111 0.96272 0.81596 0.05235  0.18658  0.17745  20  ILE C C   
3568 O O   . ILE C 20  ? 1.24199 0.96194 0.82751 0.05969  0.20429  0.18813  20  ILE C O   
3569 C CB  . ILE C 20  ? 1.16579 0.95365 0.77078 0.03621  0.17337  0.15732  20  ILE C CB  
3570 N N   . ASP C 21  ? 1.32473 1.10011 0.93495 0.05953  0.17032  0.17805  21  ASP C N   
3571 C CA  . ASP C 21  ? 1.33330 1.09817 0.92735 0.07779  0.17251  0.19202  21  ASP C CA  
3572 C C   . ASP C 21  ? 1.31976 1.10865 0.93664 0.07779  0.15604  0.18839  21  ASP C C   
3573 O O   . ASP C 21  ? 1.30852 1.12534 0.94776 0.06579  0.14162  0.17565  21  ASP C O   
3574 C CB  . ASP C 21  ? 1.36868 1.13841 0.91988 0.10021  0.17196  0.20349  21  ASP C CB  
3575 C CG  . ASP C 21  ? 1.42268 1.24084 0.96958 0.10677  0.14929  0.19740  21  ASP C CG  
3576 O OD1 . ASP C 21  ? 1.43232 1.27860 1.00743 0.09304  0.13456  0.18412  21  ASP C OD1 
3577 O OD2 . ASP C 21  ? 1.46753 1.29647 0.98049 0.12686  0.14700  0.20589  21  ASP C OD2 
3578 N N   . LEU C 22  ? 1.24937 1.02446 0.85804 0.09185  0.15989  0.20002  22  LEU C N   
3579 C CA  . LEU C 22  ? 1.26892 1.06574 0.89185 0.09704  0.14525  0.19967  22  LEU C CA  
3580 C C   . LEU C 22  ? 1.26653 1.06916 0.85624 0.12406  0.14241  0.21376  22  LEU C C   
3581 O O   . LEU C 22  ? 1.28061 1.05004 0.84209 0.13886  0.15886  0.22788  22  LEU C O   
3582 C CB  . LEU C 22  ? 1.23824 1.01292 0.88749 0.08794  0.15289  0.19923  22  LEU C CB  
3583 C CG  . LEU C 22  ? 1.21325 1.00465 0.87380 0.09566  0.14034  0.20122  22  LEU C CG  
3584 C CD1 . LEU C 22  ? 1.20530 1.03942 0.88693 0.08719  0.11871  0.18844  22  LEU C CD1 
3585 C CD2 . LEU C 22  ? 1.15958 0.92502 0.84077 0.08815  0.15077  0.20189  22  LEU C CD2 
3586 N N   . ALA C 23  ? 1.28428 1.12882 0.87695 0.13089  0.12260  0.20962  23  ALA C N   
3587 C CA  . ALA C 23  ? 1.30161 1.16242 0.86575 0.15832  0.11648  0.22121  23  ALA C CA  
3588 C C   . ALA C 23  ? 1.29508 1.17046 0.87850 0.16213  0.10623  0.22123  23  ALA C C   
3589 O O   . ALA C 23  ? 1.26399 1.16802 0.87770 0.14594  0.09205  0.20730  23  ALA C O   
3590 C CB  . ALA C 23  ? 1.36544 1.27209 0.91443 0.16409  0.10136  0.21432  23  ALA C CB  
3591 N N   . VAL C 24  ? 1.32977 1.18336 0.89378 0.18388  0.11459  0.23695  24  VAL C N   
3592 C CA  . VAL C 24  ? 1.30062 1.15875 0.88168 0.18801  0.10880  0.23875  24  VAL C CA  
3593 C C   . VAL C 24  ? 1.37097 1.23776 0.91931 0.22174  0.10681  0.25392  24  VAL C C   
3594 O O   . VAL C 24  ? 1.41305 1.24249 0.92695 0.24137  0.12416  0.27021  24  VAL C O   
3595 C CB  . VAL C 24  ? 1.28230 1.09264 0.87905 0.17618  0.12632  0.24172  24  VAL C CB  
3596 C CG1 . VAL C 24  ? 1.27949 1.09695 0.89502 0.17920  0.11928  0.24219  24  VAL C CG1 
3597 C CG2 . VAL C 24  ? 1.25745 1.05965 0.88291 0.14685  0.12989  0.22794  24  VAL C CG2 
3598 N N   . ILE C 25  ? 1.37235 1.28588 0.93106 0.22897  0.08735  0.24879  25  ILE C N   
3599 C CA  . ILE C 25  ? 1.38719 1.31647 0.91890 0.26228  0.08320  0.26186  25  ILE C CA  
3600 C C   . ILE C 25  ? 1.43919 1.38060 0.99614 0.26143  0.07474  0.25948  25  ILE C C   
3601 O O   . ILE C 25  ? 1.37409 1.35217 0.96449 0.24206  0.05863  0.24327  25  ILE C O   
3602 C CB  . ILE C 25  ? 1.39480 1.38311 0.90996 0.27670  0.06557  0.25684  25  ILE C CB  
3603 C CG1 . ILE C 25  ? 1.40066 1.38335 0.89370 0.27477  0.07152  0.25637  25  ILE C CG1 
3604 C CG2 . ILE C 25  ? 1.48145 1.48378 0.96361 0.31561  0.06360  0.27232  25  ILE C CG2 
3605 C CD1 . ILE C 25  ? 1.39601 1.44240 0.87770 0.28417  0.05303  0.24732  25  ILE C CD1 
3606 N N   . ALA C 26  ? 1.49781 1.40700 1.03656 0.28291  0.08669  0.27565  26  ALA C N   
3607 C CA  . ALA C 26  ? 1.48435 1.41286 1.03694 0.29183  0.07717  0.27621  26  ALA C CA  
3608 C C   . ALA C 26  ? 1.53243 1.52009 1.06851 0.31792  0.05909  0.27701  26  ALA C C   
3609 O O   . ALA C 26  ? 1.52008 1.52087 1.02343 0.33799  0.05905  0.28349  26  ALA C O   
3610 C CB  . ALA C 26  ? 1.49739 1.36995 1.03273 0.30721  0.09770  0.29318  26  ALA C CB  
3611 N N   . PHE C 27  ? 1.55767 1.58441 1.11680 0.31763  0.04349  0.26941  27  PHE C N   
3612 C CA  . PHE C 27  ? 1.57267 1.66396 1.12088 0.34019  0.02524  0.26692  27  PHE C CA  
3613 C C   . PHE C 27  ? 1.52521 1.63875 1.09294 0.34598  0.01595  0.26518  27  PHE C C   
3614 O O   . PHE C 27  ? 1.52773 1.60611 1.11671 0.33184  0.02329  0.26575  27  PHE C O   
3615 C CB  . PHE C 27  ? 1.50323 1.64925 1.06630 0.32049  0.00856  0.24662  27  PHE C CB  
3616 C CG  . PHE C 27  ? 1.41340 1.57202 1.02151 0.28265  0.00000  0.22644  27  PHE C CG  
3617 C CD1 . PHE C 27  ? 1.41453 1.53277 1.03985 0.25371  0.00983  0.22098  27  PHE C CD1 
3618 C CD2 . PHE C 27  ? 1.37384 1.58548 1.00558 0.27671  -0.01712 0.21257  27  PHE C CD2 
3619 C CE1 . PHE C 27  ? 1.35808 1.48610 1.02128 0.22188  0.00284  0.20353  27  PHE C CE1 
3620 C CE2 . PHE C 27  ? 1.36492 1.58398 1.03452 0.24267  -0.02309 0.19461  27  PHE C CE2 
3621 C CZ  . PHE C 27  ? 1.30807 1.48433 0.99220 0.21645  -0.01309 0.19077  27  PHE C CZ  
3622 N N   . ASP C 28  ? 1.54668 1.72180 1.10656 0.36763  -0.00027 0.26245  28  ASP C N   
3623 C CA  . ASP C 28  ? 1.54337 1.74645 1.11587 0.37999  -0.00944 0.26229  28  ASP C CA  
3624 C C   . ASP C 28  ? 1.55806 1.81914 1.17135 0.35173  -0.02902 0.23758  28  ASP C C   
3625 O O   . ASP C 28  ? 1.53774 1.85633 1.15101 0.34887  -0.04280 0.22387  28  ASP C O   
3626 C CB  . ASP C 28  ? 1.60899 1.84559 1.14460 0.42542  -0.01378 0.27541  28  ASP C CB  
3627 C CG  . ASP C 28  ? 1.58930 1.84799 1.13321 0.44327  -0.02024 0.27855  28  ASP C CG  
3628 O OD1 . ASP C 28  ? 1.61108 1.85296 1.18793 0.41992  -0.01984 0.27172  28  ASP C OD1 
3629 O OD2 . ASP C 28  ? 1.57010 1.86581 1.08752 0.48146  -0.02618 0.28736  28  ASP C OD2 
3630 N N   . PRO C 29  ? 1.59548 1.84442 1.24282 0.33020  -0.03006 0.23039  29  PRO C N   
3631 C CA  . PRO C 29  ? 1.53580 1.83472 1.21974 0.30221  -0.04624 0.20682  29  PRO C CA  
3632 C C   . PRO C 29  ? 1.61295 1.98347 1.30026 0.31857  -0.06301 0.19895  29  PRO C C   
3633 O O   . PRO C 29  ? 1.57119 1.99667 1.27708 0.29977  -0.07646 0.17777  29  PRO C O   
3634 C CB  . PRO C 29  ? 1.48623 1.74162 1.19962 0.27893  -0.03937 0.20528  29  PRO C CB  
3635 C CG  . PRO C 29  ? 1.47320 1.67765 1.16642 0.30322  -0.02450 0.22719  29  PRO C CG  
3636 C CD  . PRO C 29  ? 1.54146 1.72566 1.19483 0.32651  -0.01438 0.24205  29  PRO C CD  
3637 N N   . ASN C 30  ? 1.74231 2.11327 1.41124 0.35308  -0.06126 0.21486  30  ASN C N   
3638 C CA  . ASN C 30  ? 1.74509 2.18568 1.41803 0.37140  -0.07678 0.20804  30  ASN C CA  
3639 C C   . ASN C 30  ? 1.73675 2.24543 1.39315 0.38397  -0.08939 0.19856  30  ASN C C   
3640 O O   . ASN C 30  ? 1.72880 2.22447 1.35000 0.40734  -0.08336 0.21198  30  ASN C O   
3641 C CB  . ASN C 30  ? 1.74551 2.16359 1.39562 0.41022  -0.06925 0.23033  30  ASN C CB  
3642 C CG  . ASN C 30  ? 1.72857 2.21271 1.38809 0.42786  -0.08396 0.22375  30  ASN C CG  
3643 O OD1 . ASN C 30  ? 1.70278 2.25217 1.38704 0.40983  -0.09974 0.20135  30  ASN C OD1 
3644 N ND2 . ASN C 30  ? 1.76551 2.23175 1.40436 0.46321  -0.07736 0.24292  30  ASN C ND2 
3645 N N   . PRO C 31  ? 1.64188 2.22454 1.32184 0.36850  -0.10609 0.17461  31  PRO C N   
3646 C CA  . PRO C 31  ? 1.56990 2.22565 1.23705 0.37732  -0.11880 0.16154  31  PRO C CA  
3647 C C   . PRO C 31  ? 1.54594 2.23602 1.17611 0.42855  -0.12272 0.17736  31  PRO C C   
3648 O O   . PRO C 31  ? 1.44183 2.17887 1.05288 0.44077  -0.12980 0.17145  31  PRO C O   
3649 C CB  . PRO C 31  ? 1.50539 2.22847 1.20888 0.35020  -0.13316 0.13291  31  PRO C CB  
3650 C CG  . PRO C 31  ? 1.51760 2.18821 1.25237 0.31548  -0.12564 0.12882  31  PRO C CG  
3651 C CD  . PRO C 31  ? 1.57783 2.17497 1.29902 0.33568  -0.11197 0.15600  31  PRO C CD  
3652 N N   . THR C 36  ? 1.82803 2.29992 1.20870 0.51325  -0.05010 0.25719  36  THR C N   
3653 C CA  . THR C 36  ? 1.77948 2.28057 1.14113 0.51754  -0.05315 0.24988  36  THR C CA  
3654 C C   . THR C 36  ? 1.77215 2.20569 1.10887 0.50665  -0.03660 0.26244  36  THR C C   
3655 O O   . THR C 36  ? 1.79365 2.14957 1.11987 0.50702  -0.01777 0.28154  36  THR C O   
3656 C CB  . THR C 36  ? 1.79257 2.31538 1.13300 0.55886  -0.05053 0.25606  36  THR C CB  
3657 O OG1 . THR C 36  ? 1.82788 2.27154 1.14112 0.58398  -0.02776 0.28199  36  THR C OG1 
3658 C CG2 . THR C 36  ? 1.79159 2.38720 1.15686 0.56993  -0.06605 0.24197  36  THR C CG2 
3659 N N   . PHE C 37  ? 1.65712 2.12164 0.98497 0.49632  -0.04258 0.25031  37  PHE C N   
3660 C CA  . PHE C 37  ? 1.64635 2.05814 0.96702 0.47165  -0.02980 0.25260  37  PHE C CA  
3661 C C   . PHE C 37  ? 1.69257 2.02394 0.97190 0.49573  -0.00543 0.28089  37  PHE C C   
3662 O O   . PHE C 37  ? 1.65311 1.91566 0.94154 0.47227  0.01173  0.28575  37  PHE C O   
3663 C CB  . PHE C 37  ? 1.61523 2.08197 0.93571 0.45575  -0.04160 0.23146  37  PHE C CB  
3664 C CG  . PHE C 37  ? 1.60342 2.01778 0.92495 0.42738  -0.02781 0.22932  37  PHE C CG  
3665 C CD1 . PHE C 37  ? 1.55502 1.93095 0.91669 0.38526  -0.02194 0.21876  37  PHE C CD1 
3666 C CD2 . PHE C 37  ? 1.63892 2.04639 0.92099 0.44358  -0.02126 0.23698  37  PHE C CD2 
3667 C CE1 . PHE C 37  ? 1.56758 1.89918 0.93079 0.36047  -0.00954 0.21613  37  PHE C CE1 
3668 C CE2 . PHE C 37  ? 1.65999 2.02130 0.94357 0.41741  -0.00842 0.23431  37  PHE C CE2 
3669 C CZ  . PHE C 37  ? 1.64107 1.96514 0.96589 0.37591  -0.00262 0.22371  37  PHE C CZ  
3670 N N   . ASP C 38  ? 1.71345 2.04622 0.97010 0.53130  -0.00029 0.29015  38  ASP C N   
3671 C CA  . ASP C 38  ? 1.70737 1.96007 0.93074 0.55006  0.02556  0.31272  38  ASP C CA  
3672 C C   . ASP C 38  ? 1.74648 1.92973 0.97378 0.55058  0.04313  0.32868  38  ASP C C   
3673 O O   . ASP C 38  ? 1.73018 1.83607 0.93831 0.54923  0.06718  0.34373  38  ASP C O   
3674 C CB  . ASP C 38  ? 1.73096 2.00314 0.92789 0.58992  0.02752  0.31836  38  ASP C CB  
3675 C CG  . ASP C 38  ? 1.66102 1.98341 0.84661 0.58985  0.01664  0.30604  38  ASP C CG  
3676 O OD1 . ASP C 38  ? 1.62257 1.93411 0.80837 0.56168  0.01725  0.29986  38  ASP C OD1 
3677 O OD2 . ASP C 38  ? 1.52115 1.89377 0.69731 0.61837  0.00844  0.30228  38  ASP C OD2 
3678 N N   . GLU C 39  ? 1.79787 2.00817 1.05065 0.55120  0.03235  0.32419  39  GLU C N   
3679 C CA  . GLU C 39  ? 1.81471 1.96425 1.07551 0.54775  0.04725  0.33659  39  GLU C CA  
3680 C C   . GLU C 39  ? 1.80949 1.91152 1.08221 0.51199  0.05609  0.33778  39  GLU C C   
3681 O O   . GLU C 39  ? 1.84491 1.86976 1.10444 0.50811  0.08056  0.35146  39  GLU C O   
3682 C CB  . GLU C 39  ? 1.81199 2.00980 1.10121 0.55168  0.03071  0.32847  39  GLU C CB  
3683 C CG  . GLU C 39  ? 1.87371 2.11462 1.15366 0.58829  0.02490  0.32815  39  GLU C CG  
3684 C CD  . GLU C 39  ? 1.89665 2.19283 1.20849 0.58746  0.00719  0.31683  39  GLU C CD  
3685 O OE1 . GLU C 39  ? 1.88320 2.18878 1.22447 0.55732  -0.00261 0.30796  39  GLU C OE1 
3686 O OE2 . GLU C 39  ? 1.89137 2.22258 1.19845 0.61732  0.00365  0.31645  39  GLU C OE2 
3687 N N   . LEU C 40  ? 1.71951 1.86690 1.03581 0.47610  0.03813  0.31381  40  LEU C N   
3688 C CA  . LEU C 40  ? 1.70302 1.81160 1.06022 0.43185  0.04497  0.30251  40  LEU C CA  
3689 C C   . LEU C 40  ? 1.66116 1.71665 1.00398 0.41783  0.06333  0.30665  40  LEU C C   
3690 O O   . LEU C 40  ? 1.61491 1.61020 0.97128 0.39753  0.08054  0.30983  40  LEU C O   
3691 C CB  . LEU C 40  ? 1.61044 1.78014 1.01384 0.39872  0.02272  0.27505  40  LEU C CB  
3692 C CG  . LEU C 40  ? 1.63353 1.86062 1.05439 0.40908  0.00433  0.26809  40  LEU C CG  
3693 C CD1 . LEU C 40  ? 1.56860 1.85448 1.03077 0.37524  -0.01506 0.23985  40  LEU C CD1 
3694 C CD2 . LEU C 40  ? 1.60329 1.78802 1.03491 0.41368  0.01374  0.27976  40  LEU C CD2 
3695 N N   . VAL C 41  ? 1.67459 1.75428 0.99039 0.42819  0.05996  0.30563  41  VAL C N   
3696 C CA  . VAL C 41  ? 1.62775 1.66336 0.93125 0.41342  0.07596  0.30743  41  VAL C CA  
3697 C C   . VAL C 41  ? 1.63745 1.59373 0.90570 0.43199  0.10450  0.33158  41  VAL C C   
3698 O O   . VAL C 41  ? 1.59063 1.49337 0.86295 0.41048  0.12272  0.33234  41  VAL C O   
3699 C CB  . VAL C 41  ? 1.65378 1.73659 0.93346 0.42306  0.06539  0.30105  41  VAL C CB  
3700 C CG1 . VAL C 41  ? 1.59091 1.74589 0.90850 0.39728  0.04074  0.27393  41  VAL C CG1 
3701 C CG2 . VAL C 41  ? 1.70406 1.80702 0.93370 0.47293  0.06413  0.31888  41  VAL C CG2 
3702 N N   . SER C 42  ? 1.69214 1.63877 0.92427 0.47189  0.11031  0.35106  42  SER C N   
3703 C CA  . SER C 42  ? 1.73733 1.60286 0.94071 0.48577  0.13991  0.37186  42  SER C CA  
3704 C C   . SER C 42  ? 1.73078 1.56158 0.96272 0.47076  0.14763  0.37271  42  SER C C   
3705 O O   . SER C 42  ? 1.77807 1.54092 0.99490 0.47532  0.17329  0.38498  42  SER C O   
3706 C CB  . SER C 42  ? 1.67914 1.54575 0.85286 0.52536  0.14504  0.38027  42  SER C CB  
3707 O OG  . SER C 42  ? 1.71372 1.63262 0.89829 0.54599  0.12712  0.37690  42  SER C OG  
3708 N N   . ARG C 43  ? 1.67901 1.55525 0.95965 0.44814  0.12667  0.35479  43  ARG C N   
3709 C CA  . ARG C 43  ? 1.70551 1.54763 1.01844 0.42802  0.13430  0.35243  43  ARG C CA  
3710 C C   . ARG C 43  ? 1.69929 1.52003 1.05289 0.38246  0.13887  0.33637  43  ARG C C   
3711 O O   . ARG C 43  ? 1.70151 1.47238 1.06928 0.36690  0.15551  0.33824  43  ARG C O   
3712 C CB  . ARG C 43  ? 1.67971 1.57536 1.02139 0.43088  0.11195  0.34398  43  ARG C CB  
3713 C CG  . ARG C 43  ? 1.65668 1.51098 1.02285 0.41719  0.12265  0.34546  43  ARG C CG  
3714 C CD  . ARG C 43  ? 1.72128 1.62221 1.12322 0.41222  0.10215  0.33483  43  ARG C CD  
3715 N NE  . ARG C 43  ? 1.80847 1.74446 1.18685 0.45097  0.09257  0.34501  43  ARG C NE  
3716 C CZ  . ARG C 43  ? 1.78550 1.79695 1.18055 0.45531  0.06683  0.33282  43  ARG C CZ  
3717 N NH1 . ARG C 43  ? 1.71564 1.77200 1.14945 0.42270  0.04906  0.31017  43  ARG C NH1 
3718 N NH2 . ARG C 43  ? 1.84106 1.88301 1.21330 0.49300  0.05995  0.34298  43  ARG C NH2 
3719 N N   . GLY C 44  ? 1.59583 1.45347 0.96778 0.36101  0.12530  0.32004  44  GLY C N   
3720 C CA  . GLY C 44  ? 1.52591 1.36571 0.93450 0.32105  0.12934  0.30525  44  GLY C CA  
3721 C C   . GLY C 44  ? 1.51857 1.30248 0.90630 0.31454  0.15379  0.31218  44  GLY C C   
3722 O O   . GLY C 44  ? 1.57811 1.34342 0.92110 0.33927  0.16527  0.32659  44  GLY C O   
3723 N N   . ILE C 45  ? 1.47132 1.22969 0.89171 0.28124  0.16211  0.30133  45  ILE C N   
3724 C CA  . ILE C 45  ? 1.46767 1.17700 0.87577 0.26958  0.18524  0.30421  45  ILE C CA  
3725 C C   . ILE C 45  ? 1.42083 1.15007 0.86480 0.23617  0.17694  0.28469  45  ILE C C   
3726 O O   . ILE C 45  ? 1.39620 1.15926 0.87934 0.21762  0.15952  0.26986  45  ILE C O   
3727 C CB  . ILE C 45  ? 1.47835 1.12468 0.88511 0.26458  0.21154  0.31235  45  ILE C CB  
3728 C CG1 . ILE C 45  ? 1.48253 1.13446 0.93948 0.23711  0.20554  0.29827  45  ILE C CG1 
3729 C CG2 . ILE C 45  ? 1.53479 1.15372 0.90030 0.29947  0.22330  0.33302  45  ILE C CG2 
3730 C CD1 . ILE C 45  ? 1.43604 1.07400 0.92362 0.20335  0.21365  0.28395  45  ILE C CD1 
3731 N N   . LYS C 46  ? 1.37362 1.08020 0.80199 0.22964  0.19049  0.28512  46  LYS C N   
3732 C CA  . LYS C 46  ? 1.34968 1.07014 0.80654 0.20069  0.18571  0.26814  46  LYS C CA  
3733 C C   . LYS C 46  ? 1.32421 0.99398 0.78603 0.18302  0.21071  0.26795  46  LYS C C   
3734 O O   . LYS C 46  ? 1.33361 0.96080 0.76070 0.19547  0.23281  0.28126  46  LYS C O   
3735 C CB  . LYS C 46  ? 1.38736 1.13925 0.82364 0.20713  0.17568  0.26498  46  LYS C CB  
3736 N N   . ILE C 47  ? 1.30119 0.97680 0.80507 0.15449  0.20784  0.25232  47  ILE C N   
3737 C CA  . ILE C 47  ? 1.27000 0.90727 0.78738 0.13465  0.22934  0.24816  47  ILE C CA  
3738 C C   . ILE C 47  ? 1.27484 0.92638 0.80490 0.11674  0.22667  0.23565  47  ILE C C   
3739 O O   . ILE C 47  ? 1.26659 0.95382 0.82609 0.10338  0.20838  0.22209  47  ILE C O   
3740 C CB  . ILE C 47  ? 1.25054 0.88527 0.80725 0.11792  0.22870  0.23974  47  ILE C CB  
3741 C CG1 . ILE C 47  ? 1.31580 0.93967 0.86121 0.13579  0.22936  0.25128  47  ILE C CG1 
3742 C CG2 . ILE C 47  ? 1.20905 0.80892 0.77882 0.09793  0.25174  0.23399  47  ILE C CG2 
3743 C CD1 . ILE C 47  ? 1.25624 0.89229 0.84172 0.12193  0.22054  0.24186  47  ILE C CD1 
3744 N N   . LYS C 48  ? 1.29403 0.91575 0.80075 0.11649  0.24612  0.24011  48  LYS C N   
3745 C CA  . LYS C 48  ? 1.26333 0.89492 0.77925 0.10061  0.24613  0.22903  48  LYS C CA  
3746 C C   . LYS C 48  ? 1.26172 0.87279 0.80794 0.07683  0.26157  0.21889  48  LYS C C   
3747 O O   . LYS C 48  ? 1.28455 0.85738 0.82287 0.07565  0.28371  0.22459  48  LYS C O   
3748 C CB  . LYS C 48  ? 1.25417 0.86899 0.72653 0.11447  0.25768  0.23894  48  LYS C CB  
3749 N N   . PHE C 49  ? 1.22205 0.85874 0.80201 0.05826  0.25100  0.20329  49  PHE C N   
3750 C CA  . PHE C 49  ? 1.24665 0.87262 0.85847 0.03733  0.26308  0.19218  49  PHE C CA  
3751 C C   . PHE C 49  ? 1.24144 0.85942 0.84862 0.02740  0.27541  0.18647  49  PHE C C   
3752 O O   . PHE C 49  ? 1.20528 0.83991 0.80038 0.03065  0.26606  0.18495  49  PHE C O   
3753 C CB  . PHE C 49  ? 1.16223 0.81938 0.81751 0.02401  0.24573  0.17838  49  PHE C CB  
3754 C CG  . PHE C 49  ? 1.14632 0.81694 0.81058 0.03185  0.23093  0.18179  49  PHE C CG  
3755 C CD1 . PHE C 49  ? 1.22090 0.89913 0.85947 0.05093  0.22049  0.19275  49  PHE C CD1 
3756 C CD2 . PHE C 49  ? 1.20615 0.87901 0.90278 0.02117  0.23056  0.17469  49  PHE C CD2 
3757 C CE1 . PHE C 49  ? 1.17952 0.87090 0.82743 0.05805  0.20776  0.19539  49  PHE C CE1 
3758 C CE2 . PHE C 49  ? 1.18955 0.87225 0.89396 0.02816  0.21858  0.17804  49  PHE C CE2 
3759 C CZ  . PHE C 49  ? 1.13155 0.82281 0.81157 0.04651  0.20747  0.18855  49  PHE C CZ  
3760 N N   . ASP C 50  ? 1.41346 1.00766 1.03124 0.01423  0.29686  0.18194  50  ASP C N   
3761 C CA  . ASP C 50  ? 1.42804 1.01638 1.04838 0.00201  0.31023  0.17408  50  ASP C CA  
3762 C C   . ASP C 50  ? 1.39430 1.01791 1.04966 -0.01021 0.29434  0.15875  50  ASP C C   
3763 O O   . ASP C 50  ? 1.43061 1.06608 1.12103 -0.02213 0.29297  0.14815  50  ASP C O   
3764 C CB  . ASP C 50  ? 1.47975 1.03693 1.10527 -0.01015 0.33783  0.17136  50  ASP C CB  
3765 C CG  . ASP C 50  ? 1.54114 1.09511 1.17373 -0.02455 0.35314  0.16124  50  ASP C CG  
3766 O OD1 . ASP C 50  ? 1.53556 1.11216 1.17377 -0.02615 0.34175  0.15527  50  ASP C OD1 
3767 O OD2 . ASP C 50  ? 1.58263 1.11007 1.21415 -0.03493 0.37847  0.15865  50  ASP C OD2 
3768 N N   . LEU C 51  ? 1.27536 0.91497 0.91946 -0.00678 0.28352  0.15725  51  LEU C N   
3769 C CA  . LEU C 51  ? 1.24614 0.91403 0.91789 -0.01680 0.27056  0.14354  51  LEU C CA  
3770 C C   . LEU C 51  ? 1.26150 0.92627 0.95594 -0.03144 0.28553  0.13230  51  LEU C C   
3771 O O   . LEU C 51  ? 1.24732 0.93237 0.97436 -0.03970 0.27840  0.12091  51  LEU C O   
3772 C CB  . LEU C 51  ? 1.22237 0.90405 0.87324 -0.01115 0.25913  0.14363  51  LEU C CB  
3773 C CG  . LEU C 51  ? 1.16714 0.86824 0.80542 0.00006  0.23880  0.14831  51  LEU C CG  
3774 C CD1 . LEU C 51  ? 1.22998 0.94305 0.84414 0.00359  0.23230  0.14676  51  LEU C CD1 
3775 C CD2 . LEU C 51  ? 1.05258 0.77644 0.72265 -0.00627 0.22297  0.13950  51  LEU C CD2 
3776 N N   . LYS C 52  ? 1.31633 0.95719 0.99315 -0.03393 0.30666  0.13501  52  LYS C N   
3777 C CA  . LYS C 52  ? 1.28223 0.92390 0.98012 -0.04796 0.32162  0.12309  52  LYS C CA  
3778 C C   . LYS C 52  ? 1.28965 0.94104 1.02437 -0.05844 0.32485  0.11353  52  LYS C C   
3779 O O   . LYS C 52  ? 1.24660 0.92130 1.01204 -0.06665 0.32161  0.10038  52  LYS C O   
3780 C CB  . LYS C 52  ? 1.27890 0.88956 0.94984 -0.04946 0.34633  0.12832  52  LYS C CB  
3781 N N   . SER C 53  ? 1.27738 0.91221 1.00851 -0.05709 0.33103  0.11982  53  SER C N   
3782 C CA  . SER C 53  ? 1.24496 0.88830 1.00933 -0.06831 0.33606  0.10981  53  SER C CA  
3783 C C   . SER C 53  ? 1.28479 0.96226 1.08046 -0.06763 0.31296  0.10240  53  SER C C   
3784 O O   . SER C 53  ? 1.27848 0.97176 1.10587 -0.07705 0.31501  0.09108  53  SER C O   
3785 C CB  . SER C 53  ? 1.25839 0.87270 1.00796 -0.06638 0.34835  0.11878  53  SER C CB  
3786 O OG  . SER C 53  ? 1.30582 0.92343 1.04605 -0.05270 0.32962  0.12920  53  SER C OG  
3787 N N   . GLN C 54  ? 1.29135 0.98107 1.07804 -0.05711 0.29206  0.10768  54  GLN C N   
3788 C CA  . GLN C 54  ? 1.20171 0.91953 1.01342 -0.05596 0.27150  0.10143  54  GLN C CA  
3789 C C   . GLN C 54  ? 1.32716 1.06654 1.15827 -0.06050 0.26794  0.08936  54  GLN C C   
3790 O O   . GLN C 54  ? 1.29729 1.05805 1.15031 -0.05969 0.25418  0.08309  54  GLN C O   
3791 C CB  . GLN C 54  ? 1.11553 0.83702 0.90839 -0.04439 0.25262  0.11065  54  GLN C CB  
3792 C CG  . GLN C 54  ? 1.12691 0.82868 0.89540 -0.03540 0.25505  0.12419  54  GLN C CG  
3793 C CD  . GLN C 54  ? 1.05493 0.76833 0.80927 -0.02398 0.23525  0.13116  54  GLN C CD  
3794 O OE1 . GLN C 54  ? 1.04445 0.78023 0.81170 -0.02521 0.21929  0.12474  54  GLN C OE1 
3795 N NE2 . GLN C 54  ? 1.07383 0.77192 0.79880 -0.01222 0.23755  0.14405  54  GLN C NE2 
3796 N N   . LYS C 55  ? 1.51580 1.24874 1.33719 -0.06379 0.28035  0.08660  55  LYS C N   
3797 C CA  . LYS C 55  ? 1.49238 1.24423 1.32960 -0.06607 0.27825  0.07574  55  LYS C CA  
3798 C C   . LYS C 55  ? 1.50311 1.27784 1.37741 -0.07157 0.27932  0.06346  55  LYS C C   
3799 O O   . LYS C 55  ? 1.53055 1.30397 1.41776 -0.07955 0.29236  0.05924  55  LYS C O   
3800 C CB  . LYS C 55  ? 1.47270 1.21316 1.29484 -0.06954 0.29437  0.07428  55  LYS C CB  
3801 C CG  . LYS C 55  ? 1.50390 1.23100 1.29194 -0.06303 0.29024  0.08271  55  LYS C CG  
3802 C CD  . LYS C 55  ? 1.52047 1.26363 1.31139 -0.05894 0.27398  0.07824  55  LYS C CD  
3803 C CE  . LYS C 55  ? 1.58381 1.33837 1.38993 -0.06194 0.28027  0.06699  55  LYS C CE  
3804 N NZ  . LYS C 55  ? 1.51809 1.28066 1.32068 -0.05751 0.26768  0.06343  55  LYS C NZ  
3805 N N   . GLY C 56  ? 1.40229 1.19800 1.29223 -0.06705 0.26636  0.05722  56  GLY C N   
3806 C CA  . GLY C 56  ? 1.36438 1.18560 1.28792 -0.06899 0.26510  0.04607  56  GLY C CA  
3807 C C   . GLY C 56  ? 1.41102 1.23659 1.34809 -0.07015 0.25825  0.04750  56  GLY C C   
3808 O O   . GLY C 56  ? 1.48074 1.32790 1.44576 -0.07374 0.26006  0.03736  56  GLY C O   
3809 N N   . HIS C 57  ? 1.40121 1.20880 1.31907 -0.06686 0.25077  0.05926  57  HIS C N   
3810 C CA  . HIS C 57  ? 1.39915 1.20880 1.32689 -0.06641 0.24292  0.06202  57  HIS C CA  
3811 C C   . HIS C 57  ? 1.33130 1.13988 1.24739 -0.05768 0.22390  0.07011  57  HIS C C   
3812 O O   . HIS C 57  ? 1.27589 1.09655 1.20790 -0.05569 0.21294  0.06847  57  HIS C O   
3813 C CB  . HIS C 57  ? 1.43344 1.22021 1.34985 -0.07212 0.25782  0.06772  57  HIS C CB  
3814 C CG  . HIS C 57  ? 1.48875 1.27849 1.42089 -0.08403 0.27786  0.05695  57  HIS C CG  
3815 N ND1 . HIS C 57  ? 1.48801 1.26993 1.41064 -0.08866 0.29315  0.05427  57  HIS C ND1 
3816 C CD2 . HIS C 57  ? 1.55272 1.35452 1.50998 -0.09350 0.28578  0.04662  57  HIS C CD2 
3817 C CE1 . HIS C 57  ? 1.55458 1.34425 1.49647 -0.10090 0.30999  0.04240  57  HIS C CE1 
3818 N NE2 . HIS C 57  ? 1.61964 1.42211 1.58280 -0.10450 0.30597  0.03704  57  HIS C NE2 
3819 N N   . ARG C 58  ? 1.19937 0.99565 1.08824 -0.05311 0.22018  0.07770  58  ARG C N   
3820 C CA  . ARG C 58  ? 1.09265 0.89248 0.97061 -0.04683 0.20317  0.08208  58  ARG C CA  
3821 C C   . ARG C 58  ? 1.03550 0.83632 0.90085 -0.04585 0.20161  0.07875  58  ARG C C   
3822 O O   . ARG C 58  ? 1.13045 0.92914 0.99592 -0.04859 0.21288  0.07417  58  ARG C O   
3823 C CB  . ARG C 58  ? 1.01778 0.80488 0.87307 -0.04214 0.19964  0.09380  58  ARG C CB  
3824 C CG  . ARG C 58  ? 0.98109 0.76339 0.84682 -0.04263 0.20280  0.09721  58  ARG C CG  
3825 C CD  . ARG C 58  ? 0.95946 0.73037 0.80250 -0.03470 0.19851  0.10939  58  ARG C CD  
3826 N NE  . ARG C 58  ? 0.93180 0.71777 0.77378 -0.02948 0.17961  0.11052  58  ARG C NE  
3827 C CZ  . ARG C 58  ? 0.89923 0.69699 0.76094 -0.02969 0.16940  0.10780  58  ARG C CZ  
3828 N NH1 . ARG C 58  ? 0.89001 0.68914 0.77520 -0.03455 0.17477  0.10298  58  ARG C NH1 
3829 N NH2 . ARG C 58  ? 0.89753 0.70777 0.75569 -0.02580 0.15388  0.10858  58  ARG C NH2 
3830 N N   . LEU C 59  ? 0.97166 0.77566 0.82577 -0.04281 0.18875  0.08003  59  LEU C N   
3831 C CA  . LEU C 59  ? 0.98572 0.79077 0.83116 -0.04320 0.18719  0.07433  59  LEU C CA  
3832 C C   . LEU C 59  ? 1.04882 0.84603 0.86402 -0.04333 0.18674  0.07845  59  LEU C C   
3833 O O   . LEU C 59  ? 1.02210 0.82162 0.82464 -0.04100 0.17798  0.08405  59  LEU C O   
3834 C CB  . LEU C 59  ? 0.99880 0.81275 0.85389 -0.04167 0.17527  0.06983  59  LEU C CB  
3835 C CG  . LEU C 59  ? 1.05919 0.87067 0.90673 -0.04193 0.17500  0.06285  59  LEU C CG  
3836 C CD1 . LEU C 59  ? 1.07665 0.88891 0.93629 -0.03954 0.18547  0.05691  59  LEU C CD1 
3837 C CD2 . LEU C 59  ? 1.06674 0.88270 0.91959 -0.04088 0.16397  0.06039  59  LEU C CD2 
3838 N N   . PHE C 60  ? 1.06802 0.85849 0.87186 -0.04536 0.19611  0.07502  60  PHE C N   
3839 C CA  . PHE C 60  ? 1.10967 0.89486 0.88478 -0.04622 0.19639  0.07609  60  PHE C CA  
3840 C C   . PHE C 60  ? 1.17903 0.96586 0.95045 -0.04942 0.19332  0.06699  60  PHE C C   
3841 O O   . PHE C 60  ? 1.24778 1.03075 1.02793 -0.04983 0.20119  0.06111  60  PHE C O   
3842 C CB  . PHE C 60  ? 1.05986 0.83332 0.82288 -0.04691 0.21124  0.07818  60  PHE C CB  
3843 C CG  . PHE C 60  ? 1.08210 0.84705 0.84185 -0.04444 0.21850  0.08715  60  PHE C CG  
3844 C CD1 . PHE C 60  ? 1.11989 0.87907 0.85336 -0.03933 0.21677  0.09630  60  PHE C CD1 
3845 C CD2 . PHE C 60  ? 1.13315 0.89581 0.91466 -0.04690 0.22837  0.08581  60  PHE C CD2 
3846 C CE1 . PHE C 60  ? 1.14236 0.88772 0.86858 -0.03559 0.22626  0.10555  60  PHE C CE1 
3847 C CE2 . PHE C 60  ? 1.15823 0.90837 0.93451 -0.04627 0.23810  0.09314  60  PHE C CE2 
3848 C CZ  . PHE C 60  ? 1.12868 0.86717 0.87590 -0.04010 0.23786  0.10379  60  PHE C CZ  
3849 N N   . THR C 61  ? 1.25517 1.04743 1.01219 -0.05166 0.18353  0.06511  61  THR C N   
3850 C CA  . THR C 61  ? 1.30314 1.09357 1.05629 -0.05639 0.18212  0.05552  61  THR C CA  
3851 C C   . THR C 61  ? 1.36786 1.15326 1.09471 -0.06150 0.18724  0.05066  61  THR C C   
3852 O O   . THR C 61  ? 1.40524 1.19762 1.11382 -0.06195 0.18361  0.05369  61  THR C O   
3853 C CB  . THR C 61  ? 1.31090 1.11124 1.06747 -0.05858 0.16944  0.05337  61  THR C CB  
3854 O OG1 . THR C 61  ? 1.28194 1.08700 1.06239 -0.05365 0.16462  0.05794  61  THR C OG1 
3855 C CG2 . THR C 61  ? 1.31937 1.11241 1.07014 -0.06456 0.17127  0.04285  61  THR C CG2 
3856 N N   . LYS C 62  ? 1.36369 1.13743 1.08734 -0.06432 0.19591  0.04287  62  LYS C N   
3857 C CA  . LYS C 62  ? 1.32786 1.09491 1.02638 -0.07034 0.20234  0.03668  62  LYS C CA  
3858 C C   . LYS C 62  ? 1.36960 1.14722 1.05062 -0.07832 0.19352  0.03075  62  LYS C C   
3859 O O   . LYS C 62  ? 1.38648 1.17064 1.04637 -0.08151 0.19333  0.02942  62  LYS C O   
3860 C CB  . LYS C 62  ? 1.23564 0.98587 0.93368 -0.07105 0.21384  0.02906  62  LYS C CB  
3861 C CG  . LYS C 62  ? 1.23204 0.97414 0.93152 -0.06653 0.22646  0.03096  62  LYS C CG  
3862 C CD  . LYS C 62  ? 1.22146 0.97043 0.94637 -0.05894 0.22738  0.03790  62  LYS C CD  
3863 C CE  . LYS C 62  ? 1.27471 1.01875 0.99885 -0.05695 0.24056  0.03876  62  LYS C CE  
3864 N NZ  . LYS C 62  ? 1.38337 1.11591 1.10122 -0.05569 0.25123  0.03117  62  LYS C NZ  
3865 N N   . SER C 63  ? 1.37100 1.15248 1.06030 -0.08176 0.18647  0.02627  63  SER C N   
3866 C CA  . SER C 63  ? 1.38147 1.17626 1.05651 -0.09139 0.17898  0.01801  63  SER C CA  
3867 C C   . SER C 63  ? 1.39461 1.21390 1.06544 -0.08767 0.16702  0.02449  63  SER C C   
3868 O O   . SER C 63  ? 1.38801 1.22534 1.04356 -0.09455 0.16098  0.01715  63  SER C O   
3869 C CB  . SER C 63  ? 1.42872 1.21969 1.11441 -0.09591 0.17606  0.01198  63  SER C CB  
3870 O OG  . SER C 63  ? 1.47355 1.27183 1.18187 -0.08760 0.16750  0.02093  63  SER C OG  
3871 N N   . THR C 64  ? 1.41047 1.23139 1.09361 -0.07662 0.16433  0.03738  64  THR C N   
3872 C CA  . THR C 64  ? 1.41757 1.25654 1.09305 -0.06951 0.15553  0.04577  64  THR C CA  
3873 C C   . THR C 64  ? 1.38503 1.21839 1.04344 -0.06287 0.16274  0.05342  64  THR C C   
3874 O O   . THR C 64  ? 1.39355 1.24177 1.03518 -0.05669 0.15695  0.05843  64  THR C O   
3875 C CB  . THR C 64  ? 1.29743 1.13965 0.99444 -0.06163 0.14858  0.05518  64  THR C CB  
3876 O OG1 . THR C 64  ? 1.26566 1.08979 0.98044 -0.05789 0.15733  0.06031  64  THR C OG1 
3877 C CG2 . THR C 64  ? 1.27226 1.12448 0.98194 -0.06731 0.13946  0.04829  64  THR C CG2 
3878 N N   . ILE C 65  ? 1.36586 1.17896 1.02695 -0.06287 0.17563  0.05455  65  ILE C N   
3879 C CA  . ILE C 65  ? 1.42842 1.23443 1.07041 -0.05842 0.18425  0.06023  65  ILE C CA  
3880 C C   . ILE C 65  ? 1.57336 1.38699 1.18909 -0.06472 0.18465  0.05119  65  ILE C C   
3881 O O   . ILE C 65  ? 1.55369 1.37484 1.14667 -0.05932 0.18414  0.05568  65  ILE C O   
3882 C CB  . ILE C 65  ? 1.38742 1.17246 1.04128 -0.05779 0.19867  0.06235  65  ILE C CB  
3883 C CG1 . ILE C 65  ? 1.28846 1.06939 0.96693 -0.05240 0.19940  0.07017  65  ILE C CG1 
3884 C CG2 . ILE C 65  ? 1.36405 1.14002 0.99566 -0.05499 0.20920  0.06672  65  ILE C CG2 
3885 C CD1 . ILE C 65  ? 1.18185 0.94966 0.87694 -0.05344 0.21254  0.06842  65  ILE C CD1 
3886 N N   . GLU C 66  ? 1.68022 1.49058 1.29674 -0.07586 0.18693  0.03807  66  GLU C N   
3887 C CA  . GLU C 66  ? 1.69943 1.51733 1.29119 -0.08438 0.18833  0.02707  66  GLU C CA  
3888 C C   . GLU C 66  ? 1.71172 1.56055 1.29188 -0.08549 0.17444  0.02333  66  GLU C C   
3889 O O   . GLU C 66  ? 1.72925 1.59310 1.28558 -0.08734 0.17328  0.01832  66  GLU C O   
3890 C CB  . GLU C 66  ? 1.70278 1.50561 1.29635 -0.09650 0.19643  0.01347  66  GLU C CB  
3891 C CG  . GLU C 66  ? 1.78954 1.59373 1.35653 -0.10688 0.20249  0.00104  66  GLU C CG  
3892 C CD  . GLU C 66  ? 1.86937 1.65001 1.43506 -0.11727 0.21483  -0.01098 66  GLU C CD  
3893 O OE1 . GLU C 66  ? 1.96216 1.72769 1.54679 -0.11511 0.21741  -0.00949 66  GLU C OE1 
3894 O OE2 . GLU C 66  ? 1.76877 1.54483 1.31303 -0.12643 0.22283  -0.02160 66  GLU C OE2 
3895 N N   . TRP C 67  ? 1.59004 1.45144 1.18669 -0.08364 0.16371  0.02531  67  TRP C N   
3896 C CA  . TRP C 67  ? 1.60232 1.49743 1.19020 -0.08198 0.14984  0.02294  67  TRP C CA  
3897 C C   . TRP C 67  ? 1.59352 1.50057 1.16197 -0.06691 0.14686  0.03477  67  TRP C C   
3898 O O   . TRP C 67  ? 1.63468 1.56863 1.18182 -0.06649 0.14082  0.02897  67  TRP C O   
3899 C CB  . TRP C 67  ? 1.54180 1.44540 1.15199 -0.07919 0.13986  0.02654  67  TRP C CB  
3900 C CG  . TRP C 67  ? 1.55358 1.49525 1.15609 -0.07742 0.12565  0.02264  67  TRP C CG  
3901 C CD1 . TRP C 67  ? 1.57963 1.54515 1.18015 -0.09126 0.11987  0.00583  67  TRP C CD1 
3902 C CD2 . TRP C 67  ? 1.59042 1.55239 1.18287 -0.06035 0.11691  0.03474  67  TRP C CD2 
3903 N NE1 . TRP C 67  ? 1.57370 1.57776 1.16746 -0.08388 0.10650  0.00614  67  TRP C NE1 
3904 C CE2 . TRP C 67  ? 1.61180 1.61378 1.19929 -0.06336 0.10425  0.02458  67  TRP C CE2 
3905 C CE3 . TRP C 67  ? 1.52911 1.47798 1.11537 -0.04250 0.11992  0.05299  67  TRP C CE3 
3906 C CZ2 . TRP C 67  ? 1.64196 1.67349 1.21849 -0.04646 0.09325  0.03297  67  TRP C CZ2 
3907 C CZ3 . TRP C 67  ? 1.52190 1.49417 1.09471 -0.02603 0.11063  0.06212  67  TRP C CZ3 
3908 C CH2 . TRP C 67  ? 1.60087 1.61523 1.16897 -0.02678 0.09676  0.05258  67  TRP C CH2 
3909 N N   . TRP C 68  ? 1.55849 1.44647 1.13297 -0.05396 0.15164  0.05106  68  TRP C N   
3910 C CA  . TRP C 68  ? 1.57559 1.46873 1.12857 -0.03776 0.15112  0.06411  68  TRP C CA  
3911 C C   . TRP C 68  ? 1.62018 1.51351 1.14524 -0.03865 0.15798  0.06041  68  TRP C C   
3912 O O   . TRP C 68  ? 1.62774 1.53797 1.12767 -0.02664 0.15386  0.06588  68  TRP C O   
3913 C CB  . TRP C 68  ? 1.50012 1.36567 1.06279 -0.02698 0.15980  0.08045  68  TRP C CB  
3914 C CG  . TRP C 68  ? 1.42428 1.29194 1.00768 -0.02098 0.15262  0.08779  68  TRP C CG  
3915 C CD1 . TRP C 68  ? 1.39344 1.24751 1.00649 -0.02708 0.15455  0.08686  68  TRP C CD1 
3916 C CD2 . TRP C 68  ? 1.37946 1.26407 0.95413 -0.00643 0.14290  0.09725  68  TRP C CD2 
3917 N NE1 . TRP C 68  ? 1.32640 1.18703 0.95024 -0.01897 0.14678  0.09456  68  TRP C NE1 
3918 C CE2 . TRP C 68  ? 1.32907 1.20733 0.92974 -0.00603 0.13989  0.10131  68  TRP C CE2 
3919 C CE3 . TRP C 68  ? 1.39691 1.30260 0.94322 0.00789  0.13656  0.10274  68  TRP C CE3 
3920 C CZ2 . TRP C 68  ? 1.29304 1.18286 0.89251 0.00724  0.13148  0.11066  68  TRP C CZ2 
3921 C CZ3 . TRP C 68  ? 1.38747 1.30601 0.93206 0.02287  0.12793  0.11247  68  TRP C CZ3 
3922 C CH2 . TRP C 68  ? 1.32452 1.23383 0.89572 0.02199  0.12581  0.11638  68  TRP C CH2 
3923 N N   . LYS C 69  ? 1.63195 1.50729 1.15951 -0.05145 0.16855  0.05119  69  LYS C N   
3924 C CA  . LYS C 69  ? 1.67811 1.54993 1.17977 -0.05275 0.17678  0.04788  69  LYS C CA  
3925 C C   . LYS C 69  ? 1.69672 1.60377 1.17610 -0.05657 0.16711  0.03581  69  LYS C C   
3926 O O   . LYS C 69  ? 1.69389 1.60586 1.14672 -0.05294 0.17085  0.03541  69  LYS C O   
3927 C CB  . LYS C 69  ? 1.66313 1.50901 1.17336 -0.06568 0.19019  0.03939  69  LYS C CB  
3928 C CG  . LYS C 69  ? 1.61255 1.42916 1.14433 -0.06168 0.20056  0.04937  69  LYS C CG  
3929 C CD  . LYS C 69  ? 1.55396 1.34817 1.08628 -0.06954 0.21522  0.04295  69  LYS C CD  
3930 C CE  . LYS C 69  ? 1.59726 1.38983 1.13929 -0.08265 0.21525  0.02815  69  LYS C CE  
3931 N NZ  . LYS C 69  ? 1.63462 1.40372 1.17645 -0.08718 0.23054  0.02337  69  LYS C NZ  
3932 N N   . ASN C 70  ? 1.67439 1.60801 1.16384 -0.06400 0.15512  0.02522  70  ASN C N   
3933 C CA  . ASN C 70  ? 1.70828 1.68122 1.17978 -0.07051 0.14603  0.01011  70  ASN C CA  
3934 C C   . ASN C 70  ? 1.77324 1.78033 1.22681 -0.05136 0.13380  0.01896  70  ASN C C   
3935 O O   . ASN C 70  ? 1.82707 1.87398 1.26405 -0.05415 0.12529  0.00638  70  ASN C O   
3936 C CB  . ASN C 70  ? 1.65497 1.64364 1.14438 -0.08795 0.13983  -0.00674 70  ASN C CB  
3937 C CG  . ASN C 70  ? 1.70835 1.66441 1.20915 -0.10587 0.15277  -0.01715 70  ASN C CG  
3938 O OD1 . ASN C 70  ? 1.77450 1.71104 1.26247 -0.11103 0.16463  -0.02079 70  ASN C OD1 
3939 N ND2 . ASN C 70  ? 1.67910 1.62834 1.20231 -0.11430 0.15121  -0.02183 70  ASN C ND2 
3940 N N   . GLN C 71  ? 1.79024 1.78357 1.24522 -0.03169 0.13360  0.03944  71  GLN C N   
3941 C CA  . GLN C 71  ? 1.83795 1.86236 1.28276 -0.01246 0.12070  0.04832  71  GLN C CA  
3942 C C   . GLN C 71  ? 1.91332 1.94335 1.32243 0.00818  0.12272  0.05997  71  GLN C C   
3943 O O   . GLN C 71  ? 1.88428 1.88365 1.27971 0.01014  0.13622  0.06675  71  GLN C O   
3944 C CB  . GLN C 71  ? 1.74860 1.75388 1.21506 -0.00269 0.11964  0.06343  71  GLN C CB  
3945 C CG  . GLN C 71  ? 1.66112 1.65858 1.16105 -0.02105 0.11838  0.05332  71  GLN C CG  
3946 C CD  . GLN C 71  ? 1.69654 1.73425 1.20140 -0.03478 0.10650  0.03367  71  GLN C CD  
3947 O OE1 . GLN C 71  ? 1.75893 1.83803 1.25051 -0.02592 0.09452  0.03091  71  GLN C OE1 
3948 N NE2 . GLN C 71  ? 1.67132 1.69741 1.19482 -0.05607 0.11067  0.01952  71  GLN C NE2 
3949 N N   . SER C 72  ? 2.14813 2.21870 1.54149 0.02494  0.10938  0.06241  72  SER C N   
3950 C CA  . SER C 72  ? 2.14107 2.22188 1.49676 0.04863  0.10979  0.07402  72  SER C CA  
3951 C C   . SER C 72  ? 2.12236 2.15199 1.46904 0.06512  0.12467  0.09798  72  SER C C   
3952 O O   . SER C 72  ? 2.14231 2.14568 1.51059 0.06644  0.12806  0.10794  72  SER C O   
3953 C CB  . SER C 72  ? 2.12079 2.25309 1.46421 0.06818  0.09269  0.07521  72  SER C CB  
3954 O OG  . SER C 72  ? 2.16050 2.30007 1.46440 0.09571  0.09380  0.08911  72  SER C OG  
3955 N N   . PRO C 73  ? 1.90393 1.91760 1.21879 0.07660  0.13501  0.10668  73  PRO C N   
3956 C CA  . PRO C 73  ? 1.89490 1.85835 1.19885 0.09129  0.15161  0.12870  73  PRO C CA  
3957 C C   . PRO C 73  ? 1.88310 1.84435 1.17981 0.11602  0.14823  0.14687  73  PRO C C   
3958 O O   . PRO C 73  ? 1.86708 1.78343 1.16684 0.12179  0.16237  0.16229  73  PRO C O   
3959 C CB  . PRO C 73  ? 1.89893 1.85609 1.16371 0.10107  0.16084  0.13276  73  PRO C CB  
3960 C CG  . PRO C 73  ? 1.83264 1.82103 1.10184 0.07975  0.15395  0.10933  73  PRO C CG  
3961 C CD  . PRO C 73  ? 1.85718 1.89258 1.14681 0.07237  0.13481  0.09490  73  PRO C CD  
3962 N N   . GLU C 74  ? 1.88023 1.88913 1.16750 0.13047  0.13085  0.14468  74  GLU C N   
3963 C CA  . GLU C 74  ? 1.87331 1.88151 1.15980 0.15199  0.12659  0.16004  74  GLU C CA  
3964 C C   . GLU C 74  ? 1.85873 1.84213 1.18688 0.13558  0.12880  0.15925  74  GLU C C   
3965 O O   . GLU C 74  ? 1.89556 1.84887 1.22443 0.14856  0.13619  0.17562  74  GLU C O   
3966 C CB  . GLU C 74  ? 1.86626 1.93846 1.14374 0.16604  0.10539  0.15305  74  GLU C CB  
3967 N N   . ALA C 75  ? 1.87915 1.87370 1.24058 0.10736  0.12344  0.14006  75  ALA C N   
3968 C CA  . ALA C 75  ? 1.75714 1.72933 1.15750 0.09179  0.12555  0.13836  75  ALA C CA  
3969 C C   . ALA C 75  ? 1.72770 1.64443 1.13506 0.08575  0.14576  0.14771  75  ALA C C   
3970 O O   . ALA C 75  ? 1.69128 1.58376 1.12095 0.08350  0.15060  0.15408  75  ALA C O   
3971 C CB  . ALA C 75  ? 1.71967 1.71656 1.14875 0.06515  0.11608  0.11570  75  ALA C CB  
3972 N N   . ARG C 76  ? 1.74997 1.64821 1.13901 0.08265  0.15800  0.14768  76  ARG C N   
3973 C CA  . ARG C 76  ? 1.71900 1.56994 1.11715 0.07372  0.17759  0.15290  76  ARG C CA  
3974 C C   . ARG C 76  ? 1.66093 1.47536 1.03733 0.09296  0.19284  0.17366  76  ARG C C   
3975 O O   . ARG C 76  ? 1.57001 1.34534 0.95576 0.08542  0.21046  0.17805  76  ARG C O   
3976 C CB  . ARG C 76  ? 1.79052 1.63775 1.17804 0.06177  0.18498  0.14317  76  ARG C CB  
3977 C CG  . ARG C 76  ? 1.76513 1.57268 1.16705 0.04806  0.20362  0.14288  76  ARG C CG  
3978 C CD  . ARG C 76  ? 1.79607 1.61222 1.19235 0.03424  0.20510  0.12863  76  ARG C CD  
3979 N NE  . ARG C 76  ? 1.81623 1.66342 1.23340 0.01942  0.19007  0.11126  76  ARG C NE  
3980 C CZ  . ARG C 76  ? 1.83036 1.71468 1.23272 0.01875  0.17721  0.10064  76  ARG C CZ  
3981 N NH1 . ARG C 76  ? 1.86036 1.76017 1.22701 0.03378  0.17531  0.10557  76  ARG C NH1 
3982 N NH2 . ARG C 76  ? 1.76215 1.66931 1.18501 0.00268  0.16674  0.08407  76  ARG C NH2 
3983 N N   . LYS C 77  ? 1.69279 1.51919 1.03954 0.11782  0.18761  0.18592  77  LYS C N   
3984 C CA  . LYS C 77  ? 1.72697 1.51453 1.05241 0.13703  0.20326  0.20629  77  LYS C CA  
3985 C C   . LYS C 77  ? 1.65003 1.42259 1.00480 0.13352  0.20397  0.21009  77  LYS C C   
3986 O O   . LYS C 77  ? 1.59385 1.32877 0.93488 0.14560  0.21965  0.22543  77  LYS C O   
3987 C CB  . LYS C 77  ? 1.79842 1.60270 1.07900 0.16840  0.19813  0.21929  77  LYS C CB  
3988 N N   . ASN C 78  ? 1.65529 1.45476 1.04802 0.11734  0.18858  0.19634  78  ASN C N   
3989 C CA  . ASN C 78  ? 1.59147 1.37506 1.01575 0.11024  0.19043  0.19784  78  ASN C CA  
3990 C C   . ASN C 78  ? 1.50367 1.25408 0.95283 0.08945  0.20664  0.19274  78  ASN C C   
3991 O O   . ASN C 78  ? 1.49502 1.20791 0.94251 0.09145  0.22433  0.20229  78  ASN C O   
3992 C CB  . ASN C 78  ? 1.61158 1.43503 1.06621 0.10113  0.16891  0.18519  78  ASN C CB  
3993 C CG  . ASN C 78  ? 1.65436 1.51672 1.08973 0.12065  0.15215  0.18822  78  ASN C CG  
3994 O OD1 . ASN C 78  ? 1.69321 1.54752 1.09597 0.14547  0.15667  0.20387  78  ASN C OD1 
3995 N ND2 . ASN C 78  ? 1.60843 1.51311 1.06402 0.11009  0.13352  0.17307  78  ASN C ND2 
3996 N N   . ILE C 79  ? 1.50762 1.27203 0.97870 0.06954  0.20192  0.17692  79  ILE C N   
3997 C CA  . ILE C 79  ? 1.49679 1.23876 0.99623 0.05056  0.21423  0.16990  79  ILE C CA  
3998 C C   . ILE C 79  ? 1.50608 1.21103 0.98596 0.05212  0.23748  0.17766  79  ILE C C   
3999 O O   . ILE C 79  ? 1.47086 1.15378 0.97186 0.03956  0.25141  0.17455  79  ILE C O   
4000 C CB  . ILE C 79  ? 1.46715 1.23126 0.98721 0.03263  0.20504  0.15227  79  ILE C CB  
4001 C CG1 . ILE C 79  ? 1.46284 1.22994 0.95640 0.03246  0.20903  0.14886  79  ILE C CG1 
4002 C CG2 . ILE C 79  ? 1.36227 1.16270 0.89403 0.03134  0.18373  0.14420  79  ILE C CG2 
4003 C CD1 . ILE C 79  ? 1.49223 1.27027 1.00367 0.01420  0.20601  0.13225  79  ILE C CD1 
4004 N N   . ALA C 80  ? 1.54909 1.24851 0.98842 0.06749  0.24234  0.18705  80  ALA C N   
4005 C CA  . ALA C 80  ? 1.46097 1.12260 0.87617 0.07067  0.26585  0.19572  80  ALA C CA  
4006 C C   . ALA C 80  ? 1.51247 1.13754 0.92803 0.07499  0.28300  0.20702  80  ALA C C   
4007 O O   . ALA C 80  ? 1.49649 1.12060 0.89965 0.09128  0.27838  0.21780  80  ALA C O   
4008 C CB  . ALA C 80  ? 1.49787 1.16304 0.86580 0.09034  0.26570  0.20510  80  ALA C CB  
4009 N N   . PRO C 81  ? 1.49583 1.09100 0.92425 0.06083  0.30385  0.20421  81  PRO C N   
4010 C CA  . PRO C 81  ? 1.43981 1.00118 0.87278 0.06015  0.32171  0.21128  81  PRO C CA  
4011 C C   . PRO C 81  ? 1.46504 0.99556 0.85168 0.08340  0.33441  0.23063  81  PRO C C   
4012 O O   . PRO C 81  ? 1.57075 1.10301 0.91867 0.10116  0.33238  0.23963  81  PRO C O   
4013 C CB  . PRO C 81  ? 1.36520 0.90492 0.81371 0.04058  0.34324  0.20271  81  PRO C CB  
4014 C CG  . PRO C 81  ? 1.43465 1.00613 0.90564 0.02807  0.32954  0.18797  81  PRO C CG  
4015 C CD  . PRO C 81  ? 1.48398 1.07981 0.92908 0.04240  0.31103  0.19151  81  PRO C CD  
4016 N N   . SER C 82  ? 1.44446 0.94578 0.83426 0.08382  0.34856  0.23684  82  SER C N   
4017 C CA  . SER C 82  ? 1.52709 0.99475 0.87443 0.10707  0.36179  0.25590  82  SER C CA  
4018 C C   . SER C 82  ? 1.63052 1.05279 0.98401 0.09601  0.38943  0.25736  82  SER C C   
4019 O O   . SER C 82  ? 1.63242 1.06405 1.02884 0.07620  0.38735  0.24490  82  SER C O   
4020 C CB  . SER C 82  ? 1.46367 0.95939 0.80755 0.12641  0.33854  0.26255  82  SER C CB  
4021 O OG  . SER C 82  ? 1.54291 1.00410 0.85093 0.14887  0.35233  0.28064  82  SER C OG  
4022 N N   . ASP C 83  ? 1.73104 1.10387 1.04041 0.10847  0.41649  0.27183  83  ASP C N   
4023 C CA  . ASP C 83  ? 1.74421 1.07042 1.05448 0.09863  0.44500  0.27343  83  ASP C CA  
4024 C C   . ASP C 83  ? 1.76383 1.09344 1.08677 0.10551  0.43588  0.27713  83  ASP C C   
4025 O O   . ASP C 83  ? 1.75815 1.06561 1.10152 0.08939  0.45186  0.27110  83  ASP C O   
4026 C CB  . ASP C 83  ? 1.85047 1.11847 1.10410 0.11346  0.47708  0.28992  83  ASP C CB  
4027 C CG  . ASP C 83  ? 1.95188 1.21331 1.19341 0.10481  0.48884  0.28565  83  ASP C CG  
4028 O OD1 . ASP C 83  ? 1.93463 1.22718 1.21750 0.08119  0.47986  0.26758  83  ASP C OD1 
4029 O OD2 . ASP C 83  ? 1.99305 1.21998 1.18619 0.12246  0.50578  0.29893  83  ASP C OD2 
4030 N N   . GLU C 84  ? 1.67184 1.03216 0.98447 0.12814  0.41021  0.28536  84  GLU C N   
4031 C CA  . GLU C 84  ? 1.65819 1.02950 0.98302 0.13706  0.39723  0.28888  84  GLU C CA  
4032 C C   . GLU C 84  ? 1.53786 0.95941 0.91987 0.11750  0.37064  0.27095  84  GLU C C   
4033 O O   . GLU C 84  ? 1.39172 0.84268 0.78266 0.12868  0.34847  0.27290  84  GLU C O   
4034 C CB  . GLU C 84  ? 1.66998 1.05189 0.95362 0.17270  0.38380  0.30635  84  GLU C CB  
4035 N N   . ASP C 85  ? 1.48958 0.92326 0.90822 0.09035  0.37208  0.25377  85  ASP C N   
4036 C CA  . ASP C 85  ? 1.41286 0.88535 0.88444 0.07118  0.35257  0.23696  85  ASP C CA  
4037 C C   . ASP C 85  ? 1.43169 0.88524 0.92824 0.05742  0.36554  0.23174  85  ASP C C   
4038 O O   . ASP C 85  ? 1.47746 0.88549 0.95465 0.05606  0.39360  0.23745  85  ASP C O   
4039 C CB  . ASP C 85  ? 1.40424 0.89778 0.90252 0.05057  0.34969  0.22107  85  ASP C CB  
4040 C CG  . ASP C 85  ? 1.39789 0.91788 0.88002 0.05996  0.33315  0.22203  85  ASP C CG  
4041 O OD1 . ASP C 85  ? 1.38631 0.92601 0.85162 0.07865  0.31502  0.22994  85  ASP C OD1 
4042 O OD2 . ASP C 85  ? 1.37789 0.90092 0.86515 0.04804  0.33853  0.21369  85  ASP C OD2 
4043 N N   . VAL C 86  ? 1.40419 0.89283 0.94336 0.04648  0.34564  0.21995  86  VAL C N   
4044 C CA  . VAL C 86  ? 1.29001 0.77107 0.85908 0.03177  0.35341  0.21189  86  VAL C CA  
4045 C C   . VAL C 86  ? 1.28203 0.80474 0.90128 0.01244  0.33614  0.19318  86  VAL C C   
4046 O O   . VAL C 86  ? 1.27538 0.83391 0.90540 0.01544  0.31252  0.18953  86  VAL C O   
4047 C CB  . VAL C 86  ? 1.33208 0.80695 0.89148 0.04784  0.34679  0.22269  86  VAL C CB  
4048 C CG1 . VAL C 86  ? 1.31854 0.75075 0.82433 0.07108  0.36458  0.24271  86  VAL C CG1 
4049 C CG2 . VAL C 86  ? 1.28338 0.80524 0.85808 0.05694  0.31333  0.22149  86  VAL C CG2 
4050 N N   . SER C 87  ? 1.29744 0.81530 0.94612 -0.00727 0.34915  0.18067  87  SER C N   
4051 C CA  . SER C 87  ? 1.22414 0.78090 0.91940 -0.02307 0.33414  0.16342  87  SER C CA  
4052 C C   . SER C 87  ? 1.20974 0.79316 0.92063 -0.01505 0.30868  0.16472  87  SER C C   
4053 O O   . SER C 87  ? 1.25822 0.82794 0.94983 -0.00095 0.30670  0.17676  87  SER C O   
4054 C CB  . SER C 87  ? 1.19038 0.73966 0.91254 -0.04403 0.35355  0.14948  87  SER C CB  
4055 O OG  . SER C 87  ? 1.21515 0.74543 0.93602 -0.04305 0.36091  0.15316  87  SER C OG  
4056 N N   . THR C 88  ? 1.18908 0.81002 0.93392 -0.02321 0.28997  0.15237  88  THR C N   
4057 C CA  . THR C 88  ? 1.11453 0.76063 0.87427 -0.01680 0.26642  0.15272  88  THR C CA  
4058 C C   . THR C 88  ? 1.13430 0.76711 0.90129 -0.01724 0.27224  0.15474  88  THR C C   
4059 O O   . THR C 88  ? 1.17648 0.81089 0.93347 -0.00415 0.26080  0.16388  88  THR C O   
4060 C CB  . THR C 88  ? 1.04928 0.73111 0.84385 -0.02656 0.25022  0.13856  88  THR C CB  
4061 O OG1 . THR C 88  ? 1.14552 0.83011 0.96854 -0.04225 0.26222  0.12560  88  THR C OG1 
4062 C CG2 . THR C 88  ? 1.00392 0.69805 0.78952 -0.02518 0.24346  0.13670  88  THR C CG2 
4063 N N   . ILE C 89  ? 1.14044 0.75999 0.92336 -0.03239 0.29135  0.14573  89  ILE C N   
4064 C CA  . ILE C 89  ? 1.17439 0.77816 0.96294 -0.03494 0.30000  0.14620  89  ILE C CA  
4065 C C   . ILE C 89  ? 1.23840 0.80410 0.98581 -0.01833 0.31125  0.16427  89  ILE C C   
4066 O O   . ILE C 89  ? 1.23473 0.79762 0.97827 -0.00820 0.30390  0.17136  89  ILE C O   
4067 C CB  . ILE C 89  ? 1.15440 0.75055 0.96454 -0.05622 0.32189  0.13132  89  ILE C CB  
4068 C CG1 . ILE C 89  ? 1.19281 0.83162 1.04532 -0.06916 0.30896  0.11343  89  ILE C CG1 
4069 C CG2 . ILE C 89  ? 1.16861 0.74585 0.98093 -0.05908 0.33193  0.13174  89  ILE C CG2 
4070 C CD1 . ILE C 89  ? 1.14067 0.80620 1.01786 -0.06643 0.28752  0.11010  89  ILE C CD1 
4071 N N   . ASP C 90  ? 1.37020 0.90499 1.08488 -0.01411 0.33033  0.17227  90  ASP C N   
4072 C CA  . ASP C 90  ? 1.41874 0.91434 1.08953 0.00489  0.34303  0.19078  90  ASP C CA  
4073 C C   . ASP C 90  ? 1.43933 0.95512 1.09521 0.02813  0.31806  0.20321  90  ASP C C   
4074 O O   . ASP C 90  ? 1.45379 0.95304 1.09010 0.04401  0.31925  0.21516  90  ASP C O   
4075 C CB  . ASP C 90  ? 1.44756 0.90935 1.08298 0.00787  0.36562  0.19799  90  ASP C CB  
4076 C CG  . ASP C 90  ? 1.47568 0.90559 1.11544 -0.01279 0.39736  0.18852  90  ASP C CG  
4077 O OD1 . ASP C 90  ? 1.45720 0.87842 1.11469 -0.02443 0.40688  0.18109  90  ASP C OD1 
4078 O OD2 . ASP C 90  ? 1.50761 0.92103 1.13173 -0.01772 0.41373  0.18802  90  ASP C OD2 
4079 N N   . GLY C 91  ? 1.31589 0.86795 0.98019 0.03014  0.29636  0.19971  91  GLY C N   
4080 C CA  . GLY C 91  ? 1.29472 0.87116 0.94597 0.04966  0.27310  0.20858  91  GLY C CA  
4081 C C   . GLY C 91  ? 1.26286 0.85859 0.93552 0.05205  0.25696  0.20695  91  GLY C C   
4082 O O   . GLY C 91  ? 1.26934 0.87052 0.92338 0.07151  0.24673  0.21794  91  GLY C O   
4083 N N   . ILE C 92  ? 1.25676 0.86555 0.96854 0.03327  0.25414  0.19290  92  ILE C N   
4084 C CA  . ILE C 92  ? 1.21863 0.84587 0.95136 0.03482  0.23887  0.19077  92  ILE C CA  
4085 C C   . ILE C 92  ? 1.26880 0.86164 0.98894 0.04019  0.25587  0.19860  92  ILE C C   
4086 O O   . ILE C 92  ? 1.27538 0.87049 0.98554 0.05572  0.24701  0.20766  92  ILE C O   
4087 C CB  . ILE C 92  ? 1.17366 0.83026 0.95048 0.01549  0.22786  0.17335  92  ILE C CB  
4088 C CG1 . ILE C 92  ? 1.12967 0.81213 0.92515 0.01947  0.20690  0.17175  92  ILE C CG1 
4089 C CG2 . ILE C 92  ? 1.18714 0.82776 0.98349 -0.00281 0.24745  0.16279  92  ILE C CG2 
4090 C CD1 . ILE C 92  ? 1.06427 0.77286 0.84861 0.03220  0.18590  0.17650  92  ILE C CD1 
4091 N N   . ALA C 93  ? 1.30768 0.86657 1.02494 0.02809  0.28223  0.19536  93  ALA C N   
4092 C CA  . ALA C 93  ? 1.31402 0.83189 1.01292 0.03248  0.30355  0.20293  93  ALA C CA  
4093 C C   . ALA C 93  ? 1.38953 0.88137 1.04083 0.06030  0.30856  0.22385  93  ALA C C   
4094 O O   . ALA C 93  ? 1.44294 0.90619 1.07693 0.07074  0.31989  0.23291  93  ALA C O   
4095 C CB  . ALA C 93  ? 1.32615 0.81062 1.02564 0.01300  0.33412  0.19462  93  ALA C CB  
4096 N N   . LYS C 94  ? 1.38817 0.88801 1.01600 0.07324  0.30207  0.23158  94  LYS C N   
4097 C CA  . LYS C 94  ? 1.40712 0.89641 0.99217 0.10338  0.30001  0.25070  94  LYS C CA  
4098 C C   . LYS C 94  ? 1.39721 0.93201 0.99344 0.11679  0.26920  0.25214  94  LYS C C   
4099 O O   . LYS C 94  ? 1.43047 0.96022 1.00059 0.14123  0.26654  0.26599  94  LYS C O   
4100 C CB  . LYS C 94  ? 1.42329 0.90464 0.97729 0.11190  0.30625  0.25746  94  LYS C CB  
4101 C CG  . LYS C 94  ? 1.52471 0.95626 1.05984 0.10132  0.33985  0.25811  94  LYS C CG  
4102 C CD  . LYS C 94  ? 1.66735 1.04238 1.15798 0.11964  0.36671  0.27517  94  LYS C CD  
4103 C CE  . LYS C 94  ? 1.66618 1.01195 1.17390 0.10276  0.38574  0.26800  94  LYS C CE  
4104 N NZ  . LYS C 94  ? 1.78687 1.07276 1.24835 0.12081  0.41408  0.28470  94  LYS C NZ  
4105 N N   . PHE C 95  ? 1.35346 0.93242 0.98691 0.10174  0.24693  0.23780  95  PHE C N   
4106 C CA  . PHE C 95  ? 1.31163 0.93294 0.95806 0.11071  0.21968  0.23680  95  PHE C CA  
4107 C C   . PHE C 95  ? 1.40180 1.01633 1.05915 0.11394  0.21945  0.23880  95  PHE C C   
4108 O O   . PHE C 95  ? 1.43941 1.07165 1.08767 0.13237  0.20589  0.24624  95  PHE C O   
4109 C CB  . PHE C 95  ? 1.24593 0.90804 0.92847 0.09188  0.20019  0.22038  95  PHE C CB  
4110 C CG  . PHE C 95  ? 1.21903 0.92256 0.91779 0.09664  0.17456  0.21679  95  PHE C CG  
4111 C CD1 . PHE C 95  ? 1.20497 0.93556 0.88389 0.11365  0.15968  0.22225  95  PHE C CD1 
4112 C CD2 . PHE C 95  ? 1.15096 0.86761 0.88412 0.08405  0.16608  0.20722  95  PHE C CD2 
4113 C CE1 . PHE C 95  ? 1.14950 0.91946 0.84402 0.11613  0.13765  0.21721  95  PHE C CE1 
4114 C CE2 . PHE C 95  ? 1.09656 0.84871 0.84306 0.08787  0.14444  0.20387  95  PHE C CE2 
4115 C CZ  . PHE C 95  ? 1.06469 0.84340 0.79235 0.10307  0.13069  0.20842  95  PHE C CZ  
4116 N N   . ASN C 96  ? 1.38653 0.97819 1.06405 0.09586  0.23437  0.23112  96  ASN C N   
4117 C CA  . ASN C 96  ? 1.38498 0.96730 1.07205 0.09759  0.23621  0.23225  96  ASN C CA  
4118 C C   . ASN C 96  ? 1.54362 1.08759 1.18826 0.12210  0.25258  0.25067  96  ASN C C   
4119 O O   . ASN C 96  ? 1.57308 1.12564 1.21202 0.13888  0.24296  0.25810  96  ASN C O   
4120 C CB  . ASN C 96  ? 1.36295 0.92984 1.07878 0.07197  0.25072  0.21848  96  ASN C CB  
4121 C CG  . ASN C 96  ? 1.35279 0.95649 1.10805 0.05082  0.23602  0.20108  96  ASN C CG  
4122 O OD1 . ASN C 96  ? 1.30439 0.94662 1.07323 0.05347  0.21192  0.19788  96  ASN C OD1 
4123 N ND2 . ASN C 96  ? 1.31972 0.91196 1.09329 0.02970  0.25159  0.18895  96  ASN C ND2 
4124 N N   . ASP C 97  ? 1.69019 1.19065 1.30273 0.12568  0.27828  0.25857  97  ASP C N   
4125 C CA  . ASP C 97  ? 1.74992 1.20753 1.31551 0.15159  0.29709  0.27770  97  ASP C CA  
4126 C C   . ASP C 97  ? 1.78011 1.26638 1.32230 0.18306  0.27677  0.29114  97  ASP C C   
4127 O O   . ASP C 97  ? 1.80683 1.27786 1.32510 0.20650  0.28066  0.30436  97  ASP C O   
4128 C CB  . ASP C 97  ? 1.73589 1.14640 1.26771 0.15134  0.32604  0.28405  97  ASP C CB  
4129 C CG  . ASP C 97  ? 1.75260 1.13483 1.30549 0.12008  0.34928  0.26971  97  ASP C CG  
4130 O OD1 . ASP C 97  ? 1.77580 1.16362 1.36042 0.10364  0.34816  0.25842  97  ASP C OD1 
4131 O OD2 . ASP C 97  ? 1.76638 1.12193 1.30356 0.11200  0.36936  0.26912  97  ASP C OD2 
4132 N N   . TYR C 98  ? 1.63868 1.16774 1.18668 0.18419  0.25577  0.28717  98  TYR C N   
4133 C CA  . TYR C 98  ? 1.63351 1.20076 1.16497 0.21068  0.23404  0.29568  98  TYR C CA  
4134 C C   . TYR C 98  ? 1.59976 1.20014 1.15755 0.21248  0.21418  0.29123  98  TYR C C   
4135 O O   . TYR C 98  ? 1.63653 1.24953 1.17389 0.23933  0.20640  0.30234  98  TYR C O   
4136 C CB  . TYR C 98  ? 1.53465 1.14424 1.07349 0.20505  0.21556  0.28770  98  TYR C CB  
4137 C CG  . TYR C 98  ? 1.54664 1.19878 1.06613 0.23127  0.19487  0.29448  98  TYR C CG  
4138 C CD1 . TYR C 98  ? 1.54332 1.18343 1.01558 0.25918  0.20285  0.30995  98  TYR C CD1 
4139 C CD2 . TYR C 98  ? 1.49853 1.20369 1.04581 0.22886  0.16831  0.28501  98  TYR C CD2 
4140 C CE1 . TYR C 98  ? 1.54683 1.23183 1.00162 0.28392  0.18354  0.31468  98  TYR C CE1 
4141 C CE2 . TYR C 98  ? 1.50952 1.25859 1.04038 0.25151  0.14996  0.28888  98  TYR C CE2 
4142 C CZ  . TYR C 98  ? 1.53654 1.27757 1.02156 0.27937  0.15711  0.30340  98  TYR C CZ  
4143 O OH  . TYR C 98  ? 1.54617 1.33614 1.01428 0.30311  0.13869  0.30615  98  TYR C OH  
4144 N N   . ILE C 99  ? 1.57301 1.19026 1.17565 0.18524  0.20539  0.27486  99  ILE C N   
4145 C CA  . ILE C 99  ? 1.55077 1.20139 1.17994 0.18499  0.18578  0.26938  99  ILE C CA  
4146 C C   . ILE C 99  ? 1.59555 1.21318 1.21161 0.19842  0.19948  0.27962  99  ILE C C   
4147 O O   . ILE C 99  ? 1.61060 1.25012 1.22415 0.21607  0.18652  0.28484  99  ILE C O   
4148 C CB  . ILE C 99  ? 1.48830 1.16208 1.16525 0.15387  0.17457  0.24998  99  ILE C CB  
4149 C CG1 . ILE C 99  ? 1.33802 1.04616 1.02429 0.14426  0.15981  0.24079  99  ILE C CG1 
4150 C CG2 . ILE C 99  ? 1.43989 1.14126 1.14369 0.15215  0.15761  0.24438  99  ILE C CG2 
4151 C CD1 . ILE C 99  ? 1.25537 1.01121 0.93643 0.15870  0.13626  0.24130  99  ILE C CD1 
4152 N N   . ASN C 100 ? 1.60440 1.16872 1.21050 0.19036  0.22711  0.28215  100 ASN C N   
4153 C CA  . ASN C 100 ? 1.63835 1.16487 1.22845 0.20225  0.24376  0.29160  100 ASN C CA  
4154 C C   . ASN C 100 ? 1.71687 1.23086 1.25899 0.24075  0.24802  0.31247  100 ASN C C   
4155 O O   . ASN C 100 ? 1.78543 1.28999 1.31694 0.25830  0.25004  0.32097  100 ASN C O   
4156 C CB  . ASN C 100 ? 1.67444 1.14366 1.25877 0.18469  0.27609  0.28905  100 ASN C CB  
4157 C CG  . ASN C 100 ? 1.71218 1.19585 1.34005 0.14874  0.27378  0.26836  100 ASN C CG  
4158 O OD1 . ASN C 100 ? 1.73716 1.20333 1.36153 0.13501  0.28813  0.26386  100 ASN C OD1 
4159 N ND2 . ASN C 100 ? 1.61433 1.13187 1.28264 0.13456  0.25551  0.25568  100 ASN C ND2 
4160 N N   . ALA C 101 ? 1.79630 1.31075 1.30800 0.25568  0.24964  0.32104  101 ALA C N   
4161 C CA  . ALA C 101 ? 1.82444 1.31791 1.28338 0.29401  0.25953  0.34223  101 ALA C CA  
4162 C C   . ALA C 101 ? 1.83203 1.38424 1.28552 0.32047  0.23123  0.34694  101 ALA C C   
4163 O O   . ALA C 101 ? 1.86973 1.41417 1.27878 0.35577  0.23621  0.36430  101 ALA C O   
4164 C CB  . ALA C 101 ? 1.79101 1.25011 1.21474 0.29819  0.27923  0.34991  101 ALA C CB  
4165 N N   . HIS C 102 ? 1.70900 1.32019 1.20464 0.30528  0.20271  0.33169  102 HIS C N   
4166 C CA  . HIS C 102 ? 1.67573 1.34701 1.16652 0.32686  0.17687  0.33310  102 HIS C CA  
4167 C C   . HIS C 102 ? 1.69425 1.40925 1.22016 0.32167  0.15518  0.32344  102 HIS C C   
4168 O O   . HIS C 102 ? 1.68888 1.46390 1.23236 0.32004  0.13016  0.31367  102 HIS C O   
4169 C CB  . HIS C 102 ? 1.65465 1.36389 1.15275 0.31566  0.16235  0.32325  102 HIS C CB  
4170 C CG  . HIS C 102 ? 1.63154 1.31164 1.08648 0.33145  0.17863  0.33552  102 HIS C CG  
4171 N ND1 . HIS C 102 ? 1.61484 1.24087 1.06200 0.31544  0.20320  0.33665  102 HIS C ND1 
4172 C CD2 . HIS C 102 ? 1.63324 1.33301 1.05042 0.36163  0.17385  0.34636  102 HIS C CD2 
4173 C CE1 . HIS C 102 ? 1.69607 1.30577 1.10130 0.33504  0.21377  0.34860  102 HIS C CE1 
4174 N NE2 . HIS C 102 ? 1.71846 1.37248 1.10428 0.36394  0.19590  0.35498  102 HIS C NE2 
4175 N N   . ASN C 103 ? 1.69518 1.38049 1.23062 0.31837  0.16551  0.32529  103 ASN C N   
4176 C CA  . ASN C 103 ? 1.71294 1.43296 1.27411 0.31961  0.14823  0.31974  103 ASN C CA  
4177 C C   . ASN C 103 ? 1.66956 1.43425 1.28055 0.28749  0.12650  0.29854  103 ASN C C   
4178 O O   . ASN C 103 ? 1.70529 1.51938 1.33446 0.29050  0.10519  0.29197  103 ASN C O   
4179 C CB  . ASN C 103 ? 1.77008 1.53064 1.30735 0.35612  0.13400  0.32979  103 ASN C CB  
4180 C CG  . ASN C 103 ? 1.79139 1.50715 1.27899 0.39275  0.15527  0.35221  103 ASN C CG  
4181 O OD1 . ASN C 103 ? 1.84152 1.50001 1.32066 0.39075  0.17799  0.35886  103 ASN C OD1 
4182 N ND2 . ASN C 103 ? 1.85124 1.59371 1.30441 0.42733  0.14852  0.36354  103 ASN C ND2 
4183 N N   . ILE C 104 ? 1.69314 1.44154 1.32563 0.25734  0.13233  0.28744  104 ILE C N   
4184 C CA  . ILE C 104 ? 1.69085 1.47687 1.36677 0.22888  0.11378  0.26840  104 ILE C CA  
4185 C C   . ILE C 104 ? 1.76752 1.54471 1.47357 0.21404  0.11413  0.26154  104 ILE C C   
4186 O O   . ILE C 104 ? 1.73056 1.46187 1.43270 0.21013  0.13399  0.26560  104 ILE C O   
4187 C CB  . ILE C 104 ? 1.54190 1.31813 1.22664 0.20593  0.11900  0.25962  104 ILE C CB  
4188 C CG1 . ILE C 104 ? 1.55733 1.34046 1.20945 0.22188  0.11965  0.26709  104 ILE C CG1 
4189 C CG2 . ILE C 104 ? 1.48409 1.29857 1.20841 0.18043  0.10034  0.24124  104 ILE C CG2 
4190 C CD1 . ILE C 104 ? 1.54236 1.38458 1.19334 0.23365  0.09594  0.26339  104 ILE C CD1 
4191 N N   . ASP C 105 ? 2.05679 1.87805 1.79195 0.20536  0.09300  0.25037  105 ASP C N   
4192 C CA  . ASP C 105 ? 2.04008 1.85877 1.80404 0.19234  0.09076  0.24333  105 ASP C CA  
4193 C C   . ASP C 105 ? 2.02112 1.84753 1.82004 0.16122  0.08546  0.22682  105 ASP C C   
4194 O O   . ASP C 105 ? 2.00190 1.86605 1.81561 0.15191  0.06878  0.21678  105 ASP C O   
4195 C CB  . ASP C 105 ? 2.03335 1.89339 1.80445 0.20515  0.07259  0.24265  105 ASP C CB  
4196 C CG  . ASP C 105 ? 2.01417 1.87026 1.81199 0.19425  0.07083  0.23671  105 ASP C CG  
4197 O OD1 . ASP C 105 ? 2.01422 1.84254 1.82921 0.17433  0.08078  0.23061  105 ASP C OD1 
4198 O OD2 . ASP C 105 ? 1.99874 1.88144 1.79977 0.20661  0.05970  0.23789  105 ASP C OD2 
4199 N N   . PRO C 106 ? 1.66938 1.46241 1.48155 0.14502  0.09965  0.22282  106 PRO C N   
4200 C CA  . PRO C 106 ? 1.49382 1.29639 1.33794 0.11832  0.09474  0.20739  106 PRO C CA  
4201 C C   . PRO C 106 ? 1.41230 1.25462 1.28340 0.10995  0.07385  0.19673  106 PRO C C   
4202 O O   . PRO C 106 ? 1.32840 1.18982 1.21579 0.09491  0.06503  0.18602  106 PRO C O   
4203 C CB  . PRO C 106 ? 1.42076 1.18624 1.27382 0.10691  0.11294  0.20521  106 PRO C CB  
4204 C CG  . PRO C 106 ? 1.41855 1.14448 1.23674 0.12417  0.13322  0.21986  106 PRO C CG  
4205 C CD  . PRO C 106 ? 1.61412 1.35881 1.41021 0.15060  0.12262  0.23158  106 PRO C CD  
4206 N N   . TRP C 107 ? 1.41742 1.27120 1.29196 0.11969  0.06684  0.19944  107 TRP C N   
4207 C CA  . TRP C 107 ? 1.28901 1.17629 1.18930 0.11008  0.04952  0.18878  107 TRP C CA  
4208 C C   . TRP C 107 ? 1.31705 1.24516 1.21060 0.12044  0.03329  0.18835  107 TRP C C   
4209 O O   . TRP C 107 ? 1.22390 1.18036 1.13518 0.10763  0.02046  0.17688  107 TRP C O   
4210 C CB  . TRP C 107 ? 1.16464 1.04175 1.07776 0.11035  0.05172  0.18902  107 TRP C CB  
4211 C CG  . TRP C 107 ? 1.11816 0.96421 1.04457 0.09488  0.06555  0.18418  107 TRP C CG  
4212 C CD1 . TRP C 107 ? 1.13762 0.94458 1.04994 0.09752  0.08566  0.19058  107 TRP C CD1 
4213 C CD2 . TRP C 107 ? 1.02868 0.88203 0.98425 0.07468  0.06113  0.17092  107 TRP C CD2 
4214 N NE1 . TRP C 107 ? 1.08191 0.87544 1.01518 0.07829  0.09352  0.18036  107 TRP C NE1 
4215 C CE2 . TRP C 107 ? 0.98902 0.81196 0.94876 0.06562  0.07791  0.16878  107 TRP C CE2 
4216 C CE3 . TRP C 107 ? 0.99427 0.87627 0.97097 0.06395  0.04582  0.16041  107 TRP C CE3 
4217 C CZ2 . TRP C 107 ? 0.90631 0.73241 0.89182 0.04777  0.07787  0.15626  107 TRP C CZ2 
4218 C CZ3 . TRP C 107 ? 1.00250 0.88242 1.00205 0.04797  0.04665  0.14988  107 TRP C CZ3 
4219 C CH2 . TRP C 107 ? 0.97402 0.82891 0.97852 0.04072  0.06164  0.14775  107 TRP C CH2 
4220 N N   . LYS C 108 ? 1.42502 1.35775 1.29215 0.14328  0.03438  0.19972  108 LYS C N   
4221 C CA  . LYS C 108 ? 1.45203 1.43079 1.31462 0.15355  0.01836  0.19738  108 LYS C CA  
4222 C C   . LYS C 108 ? 1.46459 1.46043 1.30828 0.15847  0.01549  0.19763  108 LYS C C   
4223 O O   . LYS C 108 ? 1.40802 1.44723 1.25531 0.15703  0.00127  0.18910  108 LYS C O   
4224 C CB  . LYS C 108 ? 1.53194 1.51745 1.37961 0.17912  0.01770  0.20839  108 LYS C CB  
4225 N N   . SER C 109 ? 1.53365 1.49733 1.35693 0.16337  0.02935  0.20617  109 SER C N   
4226 C CA  . SER C 109 ? 1.49849 1.47727 1.30130 0.16955  0.02726  0.20717  109 SER C CA  
4227 C C   . SER C 109 ? 1.38037 1.37745 1.20175 0.14502  0.01948  0.19158  109 SER C C   
4228 O O   . SER C 109 ? 1.37539 1.35696 1.21968 0.12429  0.02207  0.18348  109 SER C O   
4229 C CB  . SER C 109 ? 1.56059 1.49603 1.33576 0.18026  0.04605  0.22040  109 SER C CB  
4230 O OG  . SER C 109 ? 1.63385 1.55176 1.38363 0.20699  0.05462  0.23615  109 SER C OG  
4231 N N   . GLN C 110 ? 1.32578 1.35650 1.13546 0.14854  0.01053  0.18719  110 GLN C N   
4232 C CA  . GLN C 110 ? 1.30420 1.35497 1.12736 0.12676  0.00341  0.17176  110 GLN C CA  
4233 C C   . GLN C 110 ? 1.24595 1.28236 1.04986 0.12655  0.01134  0.17442  110 GLN C C   
4234 O O   . GLN C 110 ? 1.27145 1.31948 1.04881 0.14512  0.01120  0.18191  110 GLN C O   
4235 C CB  . GLN C 110 ? 1.29450 1.39942 1.12142 0.12667  -0.01279 0.16065  110 GLN C CB  
4236 C CG  . GLN C 110 ? 1.34348 1.46532 1.19259 0.12221  -0.02092 0.15483  110 GLN C CG  
4237 C CD  . GLN C 110 ? 1.38263 1.56041 1.23532 0.12043  -0.03534 0.14197  110 GLN C CD  
4238 O OE1 . GLN C 110 ? 1.33254 1.53944 1.16951 0.12525  -0.03982 0.13807  110 GLN C OE1 
4239 N NE2 . GLN C 110 ? 1.37974 1.57428 1.25336 0.11221  -0.04213 0.13394  110 GLN C NE2 
4240 N N   . GLY C 111 ? 1.23540 1.24838 1.05186 0.10685  0.01815  0.16823  111 GLY C N   
4241 C CA  . GLY C 111 ? 1.20107 1.20522 1.00246 0.10328  0.02436  0.16775  111 GLY C CA  
4242 C C   . GLY C 111 ? 1.20495 1.24637 1.00817 0.09205  0.01313  0.15348  111 GLY C C   
4243 O O   . GLY C 111 ? 1.22757 1.28648 1.05152 0.07627  0.00525  0.14065  111 GLY C O   
4244 N N   . TRP C 112 ? 1.19254 1.24421 0.97210 0.09989  0.01388  0.15537  112 TRP C N   
4245 C CA  . TRP C 112 ? 1.19562 1.28530 0.97203 0.09083  0.00429  0.14148  112 TRP C CA  
4246 C C   . TRP C 112 ? 1.19362 1.26567 0.95920 0.08194  0.01270  0.13920  112 TRP C C   
4247 O O   . TRP C 112 ? 1.19533 1.23501 0.94641 0.09096  0.02447  0.15131  112 TRP C O   
4248 C CB  . TRP C 112 ? 1.23113 1.36244 0.98708 0.11151  -0.00538 0.14416  112 TRP C CB  
4249 C CG  . TRP C 112 ? 1.19223 1.35047 0.96051 0.11788  -0.01538 0.14251  112 TRP C CG  
4250 C CD1 . TRP C 112 ? 1.24444 1.39034 1.00949 0.13719  -0.01339 0.15645  112 TRP C CD1 
4251 C CD2 . TRP C 112 ? 1.20193 1.40434 0.98675 0.10471  -0.02787 0.12528  112 TRP C CD2 
4252 N NE1 . TRP C 112 ? 1.28760 1.46844 1.06779 0.13744  -0.02493 0.14934  112 TRP C NE1 
4253 C CE2 . TRP C 112 ? 1.25057 1.46716 1.04339 0.11713  -0.03384 0.12989  112 TRP C CE2 
4254 C CE3 . TRP C 112 ? 1.20017 1.42938 0.99305 0.08254  -0.03291 0.10570  112 TRP C CE3 
4255 C CZ2 . TRP C 112 ? 1.24968 1.50830 1.05955 0.10782  -0.04513 0.11539  112 TRP C CZ2 
4256 C CZ3 . TRP C 112 ? 1.24079 1.50964 1.04935 0.07234  -0.04289 0.09085  112 TRP C CZ3 
4257 C CH2 . TRP C 112 ? 1.25907 1.54331 1.07668 0.08484  -0.04917 0.09568  112 TRP C CH2 
4258 N N   . CYS C 113 ? 1.16399 1.25572 0.93569 0.06364  0.00807  0.12317  113 CYS C N   
4259 C CA  . CYS C 113 ? 1.23707 1.31890 0.99571 0.05614  0.01476  0.11951  113 CYS C CA  
4260 C C   . CYS C 113 ? 1.24410 1.35628 1.00703 0.03742  0.00807  0.10000  113 CYS C C   
4261 O O   . CYS C 113 ? 1.16565 1.28934 0.94777 0.02360  0.00298  0.08881  113 CYS C O   
4262 C CB  . CYS C 113 ? 1.17633 1.21238 0.94500 0.04647  0.02800  0.12329  113 CYS C CB  
4263 S SG  . CYS C 113 ? 1.19133 1.21701 0.99109 0.02270  0.02796  0.10993  113 CYS C SG  
4264 N N   . ARG C 114 ? 1.34477 1.46851 1.08818 0.03655  0.00938  0.09547  114 ARG C N   
4265 C CA  . ARG C 114 ? 1.35613 1.50351 1.10183 0.01615  0.00617  0.07555  114 ARG C CA  
4266 C C   . ARG C 114 ? 1.36403 1.47427 1.12215 -0.00312 0.01659  0.06996  114 ARG C C   
4267 O O   . ARG C 114 ? 1.35442 1.43571 1.10417 -0.00153 0.02632  0.07662  114 ARG C O   
4268 C CB  . ARG C 114 ? 1.35856 1.53383 1.07885 0.02123  0.00389  0.07103  114 ARG C CB  
4269 C CG  . ARG C 114 ? 1.37766 1.58306 1.10024 -0.00118 0.00054  0.04782  114 ARG C CG  
4270 C CD  . ARG C 114 ? 1.48764 1.72206 1.18543 0.00154  -0.00125 0.04105  114 ARG C CD  
4271 N NE  . ARG C 114 ? 1.53175 1.80833 1.21389 0.02487  -0.01193 0.04698  114 ARG C NE  
4272 C CZ  . ARG C 114 ? 1.52291 1.85056 1.21079 0.02521  -0.02385 0.03572  114 ARG C CZ  
4273 N NH1 . ARG C 114 ? 1.47373 1.81203 1.18382 0.00334  -0.02586 0.01954  114 ARG C NH1 
4274 N NH2 . ARG C 114 ? 1.43892 1.80830 1.10895 0.04896  -0.03328 0.04079  114 ARG C NH2 
4275 N N   . GLY C 115 ? 1.29905 1.41048 1.07562 -0.02040 0.01529  0.05761  115 GLY C N   
4276 C CA  . GLY C 115 ? 1.20771 1.28273 0.99695 -0.03434 0.02490  0.05440  115 GLY C CA  
4277 C C   . GLY C 115 ? 1.13289 1.17802 0.93959 -0.02762 0.02820  0.06664  115 GLY C C   
4278 O O   . GLY C 115 ? 1.06156 1.07697 0.86842 -0.02451 0.03716  0.07461  115 GLY C O   
4279 N N   . MET C 116 ? 1.15075 1.20564 0.97264 -0.02619 0.02138  0.06692  116 MET C N   
4280 C CA  . MET C 116 ? 1.10985 1.14158 0.94876 -0.01976 0.02330  0.07732  116 MET C CA  
4281 C C   . MET C 116 ? 1.03950 1.03787 0.88928 -0.02800 0.03307  0.07646  116 MET C C   
4282 O O   . MET C 116 ? 0.99619 0.97484 0.85738 -0.02189 0.03684  0.08533  116 MET C O   
4283 C CB  . MET C 116 ? 1.10802 1.15578 0.96239 -0.02207 0.01504  0.07325  116 MET C CB  
4284 C CG  . MET C 116 ? 1.11732 1.14896 0.98643 -0.01192 0.01497  0.08502  116 MET C CG  
4285 S SD  . MET C 116 ? 1.03055 1.07291 0.92055 -0.01658 0.00738  0.08001  116 MET C SD  
4286 C CE  . MET C 116 ? 1.08752 1.17595 0.96828 -0.01302 -0.00385 0.07401  116 MET C CE  
4287 N N   . SER C 117 ? 1.03958 1.03250 0.88580 -0.04150 0.03775  0.06514  117 SER C N   
4288 C CA  . SER C 117 ? 0.98192 0.94574 0.83586 -0.04690 0.04725  0.06398  117 SER C CA  
4289 C C   . SER C 117 ? 0.96298 0.90966 0.80962 -0.04111 0.05574  0.07136  117 SER C C   
4290 O O   . SER C 117 ? 0.93056 0.85605 0.78658 -0.04205 0.06334  0.07244  117 SER C O   
4291 C CB  . SER C 117 ? 0.96963 0.93042 0.81789 -0.06190 0.05136  0.04970  117 SER C CB  
4292 O OG  . SER C 117 ? 0.94486 0.87817 0.79606 -0.06428 0.06143  0.04901  117 SER C OG  
4293 N N   . PHE C 118 ? 0.95765 0.91431 0.78709 -0.03464 0.05509  0.07597  118 PHE C N   
4294 C CA  . PHE C 118 ? 0.98439 0.92435 0.80323 -0.03095 0.06461  0.08147  118 PHE C CA  
4295 C C   . PHE C 118 ? 0.92885 0.85772 0.74870 -0.01797 0.06802  0.09549  118 PHE C C   
4296 O O   . PHE C 118 ? 0.83510 0.74296 0.66568 -0.01797 0.07667  0.09908  118 PHE C O   
4297 C CB  . PHE C 118 ? 1.02787 0.98352 0.82310 -0.03234 0.06363  0.07696  118 PHE C CB  
4298 C CG  . PHE C 118 ? 1.00465 0.94349 0.78634 -0.03009 0.07392  0.08100  118 PHE C CG  
4299 C CD1 . PHE C 118 ? 1.02746 0.94968 0.81044 -0.04008 0.08263  0.07368  118 PHE C CD1 
4300 C CD2 . PHE C 118 ? 1.01723 0.95548 0.78293 -0.01701 0.07597  0.09238  118 PHE C CD2 
4301 C CE1 . PHE C 118 ? 1.08484 0.99266 0.85582 -0.03837 0.09245  0.07680  118 PHE C CE1 
4302 C CE2 . PHE C 118 ? 1.09023 1.01204 0.84221 -0.01549 0.08647  0.09586  118 PHE C CE2 
4303 C CZ  . PHE C 118 ? 1.14460 1.05236 0.90043 -0.02687 0.09440  0.08765  118 PHE C CZ  
4304 N N   . ASP C 119 ? 0.97917 0.92278 0.78759 -0.00672 0.06201  0.10272  119 ASP C N   
4305 C CA  . ASP C 119 ? 0.93950 0.86835 0.74035 0.00685  0.06818  0.11669  119 ASP C CA  
4306 C C   . ASP C 119 ? 0.91255 0.82466 0.73494 0.00690  0.07169  0.12073  119 ASP C C   
4307 O O   . ASP C 119 ? 0.91949 0.80841 0.74525 0.00717  0.08330  0.12543  119 ASP C O   
4308 C CB  . ASP C 119 ? 0.99855 0.94816 0.78102 0.02154  0.06048  0.12356  119 ASP C CB  
4309 C CG  . ASP C 119 ? 1.07787 1.04345 0.83507 0.02481  0.05914  0.12147  119 ASP C CG  
4310 O OD1 . ASP C 119 ? 1.11042 1.05886 0.85852 0.02109  0.06879  0.12154  119 ASP C OD1 
4311 O OD2 . ASP C 119 ? 1.13190 1.12953 0.87871 0.03096  0.04843  0.11887  119 ASP C OD2 
4312 N N   . PHE C 120 ? 0.92501 0.84992 0.76262 0.00544  0.06236  0.11763  120 PHE C N   
4313 C CA  . PHE C 120 ? 0.89332 0.80481 0.74976 0.00669  0.06507  0.12162  120 PHE C CA  
4314 C C   . PHE C 120 ? 0.87764 0.77233 0.75180 -0.00301 0.07334  0.11637  120 PHE C C   
4315 O O   . PHE C 120 ? 0.91595 0.79441 0.79819 -0.00124 0.08194  0.12099  120 PHE C O   
4316 C CB  . PHE C 120 ? 0.90241 0.83210 0.77068 0.00721  0.05321  0.11899  120 PHE C CB  
4317 C CG  . PHE C 120 ? 0.94266 0.88589 0.79701 0.02129  0.04750  0.12732  120 PHE C CG  
4318 C CD1 . PHE C 120 ? 0.96111 0.88811 0.81283 0.03267  0.05345  0.13879  120 PHE C CD1 
4319 C CD2 . PHE C 120 ? 1.00109 0.97401 0.84414 0.02357  0.03715  0.12301  120 PHE C CD2 
4320 C CE1 . PHE C 120 ? 1.00952 0.94733 0.84590 0.04873  0.04912  0.14759  120 PHE C CE1 
4321 C CE2 . PHE C 120 ? 1.02433 1.01421 0.85430 0.03932  0.03133  0.13063  120 PHE C CE2 
4322 C CZ  . PHE C 120 ? 1.04789 1.01896 0.87358 0.05326  0.03734  0.14386  120 PHE C CZ  
4323 N N   . PRO C 121 ? 0.86700 0.76468 0.74693 -0.01267 0.07246  0.10653  121 PRO C N   
4324 C CA  . PRO C 121 ? 0.86337 0.74692 0.75710 -0.01818 0.08148  0.10260  121 PRO C CA  
4325 C C   . PRO C 121 ? 0.88666 0.75459 0.77242 -0.01620 0.09432  0.10759  121 PRO C C   
4326 O O   . PRO C 121 ? 0.90249 0.76085 0.80302 -0.01817 0.10243  0.10700  121 PRO C O   
4327 C CB  . PRO C 121 ? 0.80662 0.69421 0.69840 -0.02589 0.07963  0.09273  121 PRO C CB  
4328 C CG  . PRO C 121 ? 0.81500 0.71822 0.70384 -0.02745 0.06874  0.08951  121 PRO C CG  
4329 C CD  . PRO C 121 ? 0.87023 0.78388 0.74716 -0.01922 0.06398  0.09748  121 PRO C CD  
4330 N N   . ILE C 122 ? 0.84977 0.71598 0.71245 -0.01269 0.09711  0.11172  122 ILE C N   
4331 C CA  . ILE C 122 ? 0.88592 0.73423 0.73931 -0.01081 0.11102  0.11697  122 ILE C CA  
4332 C C   . ILE C 122 ? 0.88897 0.72447 0.74315 -0.00448 0.11731  0.12588  122 ILE C C   
4333 O O   . ILE C 122 ? 0.88478 0.70466 0.74699 -0.00806 0.13019  0.12590  122 ILE C O   
4334 C CB  . ILE C 122 ? 0.93515 0.78404 0.76091 -0.00718 0.11271  0.11988  122 ILE C CB  
4335 C CG1 . ILE C 122 ? 0.93147 0.78772 0.75690 -0.01587 0.11053  0.10952  122 ILE C CG1 
4336 C CG2 . ILE C 122 ? 0.93976 0.76714 0.75223 -0.00368 0.12823  0.12715  122 ILE C CG2 
4337 C CD1 . ILE C 122 ? 0.94070 0.80437 0.74026 -0.01384 0.10881  0.10963  122 ILE C CD1 
4338 N N   . LEU C 123 ? 0.89589 0.73817 0.74162 0.00460  0.10935  0.13261  123 LEU C N   
4339 C CA  . LEU C 123 ? 0.85658 0.68274 0.69739 0.01262  0.11688  0.14232  123 LEU C CA  
4340 C C   . LEU C 123 ? 0.86520 0.68516 0.73274 0.00526  0.12082  0.13778  123 LEU C C   
4341 O O   . LEU C 123 ? 0.89625 0.69549 0.76378 0.00443  0.13516  0.14103  123 LEU C O   
4342 C CB  . LEU C 123 ? 0.84398 0.68250 0.67046 0.02575  0.10629  0.14990  123 LEU C CB  
4343 C CG  . LEU C 123 ? 0.88619 0.70554 0.70387 0.03679  0.11455  0.16118  123 LEU C CG  
4344 C CD1 . LEU C 123 ? 0.89824 0.68765 0.69389 0.04163  0.13330  0.16959  123 LEU C CD1 
4345 C CD2 . LEU C 123 ? 0.94611 0.78280 0.74963 0.05213  0.10266  0.16826  123 LEU C CD2 
4346 N N   . VAL C 124 ? 0.88062 0.71800 0.76994 -0.00049 0.10932  0.12958  124 VAL C N   
4347 C CA  . VAL C 124 ? 0.85695 0.69305 0.77214 -0.00694 0.11172  0.12397  124 VAL C CA  
4348 C C   . VAL C 124 ? 0.84541 0.67481 0.77228 -0.01599 0.12393  0.11673  124 VAL C C   
4349 O O   . VAL C 124 ? 0.85361 0.67687 0.79544 -0.02093 0.13286  0.11343  124 VAL C O   
4350 C CB  . VAL C 124 ? 0.84006 0.69594 0.77224 -0.00923 0.09672  0.11746  124 VAL C CB  
4351 C CG1 . VAL C 124 ? 0.80818 0.66604 0.76669 -0.01493 0.09844  0.11073  124 VAL C CG1 
4352 C CG2 . VAL C 124 ? 0.80894 0.67382 0.73216 -0.00117 0.08585  0.12347  124 VAL C CG2 
4353 N N   . ASP C 125 ? 0.83675 0.66911 0.75746 -0.01875 0.12503  0.11298  125 ASP C N   
4354 C CA  . ASP C 125 ? 0.83610 0.66523 0.76792 -0.02623 0.13662  0.10567  125 ASP C CA  
4355 C C   . ASP C 125 ? 0.92511 0.73343 0.84539 -0.02760 0.15433  0.11025  125 ASP C C   
4356 O O   . ASP C 125 ? 0.95751 0.76353 0.89226 -0.03552 0.16634  0.10323  125 ASP C O   
4357 C CB  . ASP C 125 ? 0.79846 0.63444 0.72499 -0.02790 0.13388  0.10072  125 ASP C CB  
4358 C CG  . ASP C 125 ? 0.83710 0.67466 0.77790 -0.03398 0.14434  0.09219  125 ASP C CG  
4359 O OD1 . ASP C 125 ? 0.89786 0.74855 0.86096 -0.03592 0.14125  0.08434  125 ASP C OD1 
4360 O OD2 . ASP C 125 ? 0.87407 0.70125 0.80399 -0.03614 0.15614  0.09307  125 ASP C OD2 
4361 N N   . LEU C 126 ? 0.88893 0.68265 0.78212 -0.01972 0.15719  0.12136  126 LEU C N   
4362 C CA  . LEU C 126 ? 0.95163 0.71953 0.83030 -0.01963 0.17609  0.12724  126 LEU C CA  
4363 C C   . LEU C 126 ? 0.96384 0.72105 0.85287 -0.02146 0.18299  0.12800  126 LEU C C   
4364 O O   . LEU C 126 ? 1.00155 0.74175 0.89366 -0.02932 0.20135  0.12495  126 LEU C O   
4365 C CB  . LEU C 126 ? 0.95204 0.70692 0.79533 -0.00744 0.17738  0.13994  126 LEU C CB  
4366 C CG  . LEU C 126 ? 0.90646 0.66883 0.73715 -0.00751 0.17448  0.13815  126 LEU C CG  
4367 C CD1 . LEU C 126 ? 0.95178 0.70778 0.74802 0.00604  0.17307  0.14987  126 LEU C CD1 
4368 C CD2 . LEU C 126 ? 0.89989 0.65142 0.73572 -0.01761 0.19087  0.13184  126 LEU C CD2 
4369 N N   . ILE C 127 ? 0.89670 0.66358 0.79130 -0.01555 0.16968  0.13087  127 ILE C N   
4370 C CA  . ILE C 127 ? 0.95322 0.71141 0.85958 -0.01812 0.17550  0.13018  127 ILE C CA  
4371 C C   . ILE C 127 ? 0.95661 0.72928 0.89605 -0.03207 0.17794  0.11526  127 ILE C C   
4372 O O   . ILE C 127 ? 0.98114 0.74267 0.92966 -0.04009 0.19202  0.11062  127 ILE C O   
4373 C CB  . ILE C 127 ? 0.96662 0.73417 0.87146 -0.00792 0.15987  0.13643  127 ILE C CB  
4374 C CG1 . ILE C 127 ? 0.95508 0.71277 0.82702 0.00782  0.15807  0.15054  127 ILE C CG1 
4375 C CG2 . ILE C 127 ? 1.00568 0.76383 0.92296 -0.01108 0.16620  0.13497  127 ILE C CG2 
4376 C CD1 . ILE C 127 ? 0.94247 0.71807 0.81407 0.01803  0.14026  0.15486  127 ILE C CD1 
4377 N N   . ARG C 128 ? 0.98954 0.78768 0.94640 -0.03469 0.16507  0.10696  128 ARG C N   
4378 C CA  . ARG C 128 ? 0.97120 0.78648 0.95724 -0.04493 0.16762  0.09288  128 ARG C CA  
4379 C C   . ARG C 128 ? 0.99797 0.80489 0.98604 -0.05488 0.18737  0.08620  128 ARG C C   
4380 O O   . ARG C 128 ? 0.99467 0.81482 1.00643 -0.06459 0.19391  0.07370  128 ARG C O   
4381 C CB  . ARG C 128 ? 0.93438 0.77478 0.93321 -0.04269 0.15186  0.08675  128 ARG C CB  
4382 C CG  . ARG C 128 ? 0.93184 0.78308 0.93262 -0.03557 0.13319  0.09016  128 ARG C CG  
4383 C CD  . ARG C 128 ? 0.95984 0.83044 0.97130 -0.03409 0.12165  0.08321  128 ARG C CD  
4384 N NE  . ARG C 128 ? 1.01214 0.88844 1.01865 -0.02863 0.10656  0.08667  128 ARG C NE  
4385 C CZ  . ARG C 128 ? 1.06780 0.95298 1.08693 -0.02700 0.09762  0.08520  128 ARG C CZ  
4386 N NH1 . ARG C 128 ? 1.00554 0.89542 1.04278 -0.02982 0.10107  0.08086  128 ARG C NH1 
4387 N NH2 . ARG C 128 ? 1.02938 0.91917 1.04238 -0.02344 0.08569  0.08724  128 ARG C NH2 
4388 N N   . ASP C 129 ? 0.98774 0.77513 0.95162 -0.05294 0.19741  0.09327  129 ASP C N   
4389 C CA  . ASP C 129 ? 1.01051 0.78753 0.97473 -0.06331 0.21822  0.08690  129 ASP C CA  
4390 C C   . ASP C 129 ? 1.02502 0.78126 0.98952 -0.07184 0.23730  0.08504  129 ASP C C   
4391 O O   . ASP C 129 ? 1.01656 0.77499 0.99486 -0.08541 0.25363  0.07297  129 ASP C O   
4392 C CB  . ASP C 129 ? 1.10419 0.86191 1.03922 -0.05861 0.22564  0.09586  129 ASP C CB  
4393 C CG  . ASP C 129 ? 1.10177 0.87845 1.03999 -0.05696 0.21607  0.09175  129 ASP C CG  
4394 O OD1 . ASP C 129 ? 1.06390 0.86625 1.02796 -0.06105 0.20934  0.08026  129 ASP C OD1 
4395 O OD2 . ASP C 129 ? 1.10899 0.87350 1.02198 -0.05111 0.21717  0.09985  129 ASP C OD2 
4396 N N   . ILE C 130 ? 1.03242 0.76740 0.97986 -0.06421 0.23730  0.09643  130 ILE C N   
4397 C CA  . ILE C 130 ? 0.98539 0.69859 0.93297 -0.07198 0.25517  0.09431  130 ILE C CA  
4398 C C   . ILE C 130 ? 0.99207 0.73224 0.97649 -0.08639 0.25528  0.07595  130 ILE C C   
4399 O O   . ILE C 130 ? 0.99622 0.73058 0.99006 -0.10177 0.27552  0.06430  130 ILE C O   
4400 C CB  . ILE C 130 ? 0.97917 0.67509 0.90885 -0.05867 0.24873  0.10827  130 ILE C CB  
4401 C CG1 . ILE C 130 ? 1.05304 0.72630 0.94488 -0.04232 0.24889  0.12600  130 ILE C CG1 
4402 C CG2 . ILE C 130 ? 1.10328 0.77533 1.03332 -0.06711 0.26787  0.10513  130 ILE C CG2 
4403 C CD1 . ILE C 130 ? 1.06968 0.74111 0.94813 -0.02576 0.23487  0.13868  130 ILE C CD1 
4404 N N   . GLN C 131 ? 0.96061 0.73195 0.96561 -0.08162 0.23311  0.07234  131 GLN C N   
4405 C CA  . GLN C 131 ? 0.91460 0.71534 0.95321 -0.09181 0.23037  0.05578  131 GLN C CA  
4406 C C   . GLN C 131 ? 0.89862 0.72581 0.95742 -0.10112 0.23518  0.04060  131 GLN C C   
4407 O O   . GLN C 131 ? 0.90482 0.74709 0.98524 -0.11505 0.24670  0.02454  131 GLN C O   
4408 C CB  . GLN C 131 ? 0.94985 0.77305 1.00012 -0.08175 0.20602  0.05802  131 GLN C CB  
4409 C CG  . GLN C 131 ? 1.00958 0.81133 1.04447 -0.07396 0.20245  0.07032  131 GLN C CG  
4410 C CD  . GLN C 131 ? 0.98985 0.81308 1.03730 -0.06609 0.18055  0.07118  131 GLN C CD  
4411 O OE1 . GLN C 131 ? 1.02709 0.87847 1.09181 -0.06507 0.16779  0.06391  131 GLN C OE1 
4412 N NE2 . GLN C 131 ? 1.02653 0.83519 1.06393 -0.05967 0.17720  0.08026  131 GLN C NE2 
4413 N N   . ARG C 132 ? 0.93487 0.76994 0.98715 -0.09377 0.22702  0.04434  132 ARG C N   
4414 C CA  . ARG C 132 ? 0.90161 0.75875 0.96950 -0.10105 0.23387  0.03114  132 ARG C CA  
4415 C C   . ARG C 132 ? 0.89933 0.73881 0.96352 -0.11635 0.26065  0.02423  132 ARG C C   
4416 O O   . ARG C 132 ? 0.82189 0.68567 0.90976 -0.12893 0.27060  0.00660  132 ARG C O   
4417 C CB  . ARG C 132 ? 0.82514 0.68473 0.88020 -0.09034 0.22355  0.03837  132 ARG C CB  
4418 C CG  . ARG C 132 ? 0.91852 0.80354 0.98522 -0.07946 0.20112  0.03792  132 ARG C CG  
4419 C CD  . ARG C 132 ? 0.91182 0.80199 0.96922 -0.07109 0.19340  0.04095  132 ARG C CD  
4420 N NE  . ARG C 132 ? 0.97186 0.83747 1.00026 -0.06384 0.18809  0.05586  132 ARG C NE  
4421 C CZ  . ARG C 132 ? 0.93577 0.80239 0.95647 -0.05474 0.17147  0.06291  132 ARG C CZ  
4422 N NH1 . ARG C 132 ? 0.95624 0.84289 0.99368 -0.05074 0.15887  0.05784  132 ARG C NH1 
4423 N NH2 . ARG C 132 ? 0.93092 0.77922 0.92569 -0.04944 0.16803  0.07463  132 ARG C NH2 
4424 N N   . LEU C 133 ? 0.95333 0.75096 0.98732 -0.11530 0.27352  0.03734  133 LEU C N   
4425 C CA  . LEU C 133 ? 0.97983 0.75179 1.00496 -0.12992 0.30215  0.03222  133 LEU C CA  
4426 C C   . LEU C 133 ? 0.99713 0.77487 1.04282 -0.14588 0.31482  0.01729  133 LEU C C   
4427 O O   . LEU C 133 ? 0.98897 0.76153 1.04028 -0.16362 0.33872  0.00411  133 LEU C O   
4428 C CB  . LEU C 133 ? 1.04724 0.77001 1.03122 -0.12117 0.31238  0.05184  133 LEU C CB  
4429 C CG  . LEU C 133 ? 1.04142 0.72284 1.00341 -0.13209 0.34435  0.05239  133 LEU C CG  
4430 C CD1 . LEU C 133 ? 0.95971 0.64878 0.92660 -0.14314 0.35834  0.04207  133 LEU C CD1 
4431 C CD2 . LEU C 133 ? 1.04814 0.68558 0.96700 -0.11551 0.34760  0.07522  133 LEU C CD2 
4432 N N   . ASN C 134 ? 0.95061 0.73872 1.00706 -0.14110 0.30041  0.01816  134 ASN C N   
4433 C CA  . ASN C 134 ? 0.88949 0.69054 0.96900 -0.15621 0.30930  0.00183  134 ASN C CA  
4434 C C   . ASN C 134 ? 0.88572 0.74234 1.00398 -0.16346 0.30039  -0.01927 134 ASN C C   
4435 O O   . ASN C 134 ? 0.92589 0.80010 1.06579 -0.17850 0.30959  -0.03672 134 ASN C O   
4436 C CB  . ASN C 134 ? 0.92852 0.71825 1.00292 -0.14744 0.29781  0.01135  134 ASN C CB  
4437 C CG  . ASN C 134 ? 1.02100 0.75806 1.06403 -0.14751 0.31690  0.02368  134 ASN C CG  
4438 O OD1 . ASN C 134 ? 1.05040 0.76596 1.09012 -0.16432 0.34383  0.01436  134 ASN C OD1 
4439 N ND2 . ASN C 134 ? 1.06846 0.78328 1.08601 -0.12836 0.30486  0.04454  134 ASN C ND2 
4440 N N   . GLY C 135 ? 0.90991 0.79491 1.03636 -0.15284 0.28388  -0.01883 135 GLY C N   
4441 C CA  . GLY C 135 ? 0.85958 0.79777 1.01988 -0.15566 0.27544  -0.03756 135 GLY C CA  
4442 C C   . GLY C 135 ? 0.84881 0.81404 1.02287 -0.14211 0.25022  -0.03599 135 GLY C C   
4443 O O   . GLY C 135 ? 0.87338 0.88372 1.07532 -0.14324 0.24359  -0.05209 135 GLY C O   
4444 N N   . VAL C 136 ? 0.83862 0.77930 0.99344 -0.12871 0.23634  -0.01756 136 VAL C N   
4445 C CA  . VAL C 136 ? 0.90351 0.86694 1.06916 -0.11591 0.21330  -0.01551 136 VAL C CA  
4446 C C   . VAL C 136 ? 0.91228 0.90479 1.08564 -0.10401 0.19984  -0.01766 136 VAL C C   
4447 O O   . VAL C 136 ? 0.90999 0.89242 1.07012 -0.10066 0.20304  -0.01220 136 VAL C O   
4448 C CB  . VAL C 136 ? 0.92785 0.85874 1.07005 -0.10510 0.20294  0.00416  136 VAL C CB  
4449 C CG1 . VAL C 136 ? 0.88896 0.84072 1.04083 -0.09302 0.18079  0.00614  136 VAL C CG1 
4450 C CG2 . VAL C 136 ? 0.86533 0.76583 0.99791 -0.11441 0.21766  0.00681  136 VAL C CG2 
4451 N N   . SER C 137 ? 0.93387 0.96206 1.12755 -0.09704 0.18604  -0.02606 137 SER C N   
4452 C CA  . SER C 137 ? 0.92753 0.97940 1.12490 -0.08206 0.17283  -0.02626 137 SER C CA  
4453 C C   . SER C 137 ? 0.96429 0.98975 1.13791 -0.06828 0.15885  -0.00769 137 SER C C   
4454 O O   . SER C 137 ? 0.99458 1.00058 1.15880 -0.06698 0.15251  0.00185  137 SER C O   
4455 C CB  . SER C 137 ? 0.90998 1.00585 1.13286 -0.07675 0.16320  -0.03992 137 SER C CB  
4456 O OG  . SER C 137 ? 0.94126 1.05773 1.16495 -0.05946 0.15160  -0.03938 137 SER C OG  
4457 N N   . GLU C 138 ? 0.96325 0.98947 1.12737 -0.05842 0.15476  -0.00376 138 GLU C N   
4458 C CA  . GLU C 138 ? 0.96277 0.96257 1.10223 -0.04882 0.14505  0.01181  138 GLU C CA  
4459 C C   . GLU C 138 ? 0.95188 0.95276 1.09047 -0.03945 0.12911  0.01716  138 GLU C C   
4460 O O   . GLU C 138 ? 0.92193 0.89920 1.04210 -0.03678 0.12263  0.02916  138 GLU C O   
4461 C CB  . GLU C 138 ? 0.94684 0.95011 1.07831 -0.04071 0.14507  0.01196  138 GLU C CB  
4462 C CG  . GLU C 138 ? 0.90017 0.87654 1.00515 -0.03385 0.13793  0.02542  138 GLU C CG  
4463 C CD  . GLU C 138 ? 0.94443 0.89140 1.02942 -0.04151 0.14455  0.03520  138 GLU C CD  
4464 O OE1 . GLU C 138 ? 0.96486 0.90778 1.05301 -0.05124 0.15798  0.03200  138 GLU C OE1 
4465 O OE2 . GLU C 138 ? 0.97731 0.90584 1.04229 -0.03753 0.13725  0.04551  138 GLU C OE2 
4466 N N   . ASN C 139 ? 0.93242 0.96218 1.08991 -0.03379 0.12280  0.00794  139 ASN C N   
4467 C CA  . ASN C 139 ? 0.89343 0.92512 1.05140 -0.02566 0.10933  0.01175  139 ASN C CA  
4468 C C   . ASN C 139 ? 0.89899 0.92768 1.06532 -0.03449 0.10945  0.01113  139 ASN C C   
4469 O O   . ASN C 139 ? 0.88300 0.91799 1.05383 -0.02897 0.09920  0.01192  139 ASN C O   
4470 C CB  . ASN C 139 ? 0.89812 0.96172 1.06975 -0.01315 0.10307  0.00277  139 ASN C CB  
4471 C CG  . ASN C 139 ? 0.88951 0.98952 1.08729 -0.01895 0.10975  -0.01365 139 ASN C CG  
4472 O OD1 . ASN C 139 ? 0.91360 1.01164 1.11939 -0.03458 0.12033  -0.01887 139 ASN C OD1 
4473 N ND2 . ASN C 139 ? 0.76607 0.89989 0.97605 -0.00614 0.10468  -0.02252 139 ASN C ND2 
4474 N N   . GLU C 140 ? 0.89758 0.91536 1.06499 -0.04780 0.12221  0.00938  140 GLU C N   
4475 C CA  . GLU C 140 ? 0.90425 0.91321 1.07599 -0.05628 0.12523  0.00939  140 GLU C CA  
4476 C C   . GLU C 140 ? 0.88821 0.86008 1.03843 -0.06125 0.13287  0.02179  140 GLU C C   
4477 O O   . GLU C 140 ? 0.92058 0.87979 1.07125 -0.06895 0.14038  0.02187  140 GLU C O   
4478 C CB  . GLU C 140 ? 0.90055 0.93363 1.09568 -0.06839 0.13656  -0.00779 140 GLU C CB  
4479 C CG  . GLU C 140 ? 0.91777 0.99227 1.13517 -0.06204 0.12740  -0.02060 140 GLU C CG  
4480 C CD  . GLU C 140 ? 1.01442 1.11929 1.25628 -0.07554 0.13903  -0.04046 140 GLU C CD  
4481 O OE1 . GLU C 140 ? 1.05204 1.14360 1.29298 -0.09094 0.15634  -0.04483 140 GLU C OE1 
4482 O OE2 . GLU C 140 ? 1.08479 1.22722 1.34593 -0.07102 0.13167  -0.05239 140 GLU C OE2 
4483 N N   . LEU C 141 ? 0.90607 0.86031 1.03607 -0.05616 0.13179  0.03204  141 LEU C N   
4484 C CA  . LEU C 141 ? 0.89764 0.81999 1.00415 -0.05630 0.13572  0.04540  141 LEU C CA  
4485 C C   . LEU C 141 ? 0.98099 0.89617 1.08148 -0.04982 0.12344  0.05412  141 LEU C C   
4486 O O   . LEU C 141 ? 1.01089 0.93632 1.11219 -0.04202 0.10909  0.05589  141 LEU C O   
4487 C CB  . LEU C 141 ? 0.90803 0.81971 0.99521 -0.05136 0.13494  0.05275  141 LEU C CB  
4488 C CG  . LEU C 141 ? 0.93591 0.83973 1.01707 -0.05768 0.15040  0.05024  141 LEU C CG  
4489 C CD1 . LEU C 141 ? 0.92797 0.85710 1.03237 -0.06407 0.15760  0.03474  141 LEU C CD1 
4490 C CD2 . LEU C 141 ? 0.95773 0.85667 1.02183 -0.05026 0.14368  0.05693  141 LEU C CD2 
4491 N N   . ASP C 142 ? 0.94895 0.84479 1.04180 -0.05276 0.13042  0.05959  142 ASP C N   
4492 C CA  . ASP C 142 ? 0.96746 0.85509 1.05194 -0.04565 0.12006  0.06907  142 ASP C CA  
4493 C C   . ASP C 142 ? 0.96239 0.82106 1.02238 -0.04293 0.12892  0.08130  142 ASP C C   
4494 O O   . ASP C 142 ? 1.01269 0.85412 1.07005 -0.04857 0.14393  0.08088  142 ASP C O   
4495 C CB  . ASP C 142 ? 1.02746 0.92544 1.13050 -0.04900 0.11792  0.06220  142 ASP C CB  
4496 C CG  . ASP C 142 ? 1.07378 0.96494 1.16908 -0.04128 0.10708  0.07156  142 ASP C CG  
4497 O OD1 . ASP C 142 ? 1.09146 0.99407 1.18640 -0.03432 0.09215  0.07401  142 ASP C OD1 
4498 O OD2 . ASP C 142 ? 1.12393 0.99719 1.21248 -0.04223 0.11481  0.07614  142 ASP C OD2 
4499 N N   . THR C 143 ? 0.98841 0.84178 1.02910 -0.03393 0.12065  0.09165  143 THR C N   
4500 C CA  . THR C 143 ? 1.04234 0.87187 1.05648 -0.02804 0.12834  0.10375  143 THR C CA  
4501 C C   . THR C 143 ? 1.10208 0.92886 1.10471 -0.01729 0.11824  0.11385  143 THR C C   
4502 O O   . THR C 143 ? 1.08909 0.90401 1.06762 -0.00795 0.11927  0.12479  143 THR C O   
4503 C CB  . THR C 143 ? 1.02680 0.85543 1.02545 -0.02563 0.12827  0.10686  143 THR C CB  
4504 O OG1 . THR C 143 ? 1.02539 0.87015 1.02113 -0.01969 0.11114  0.10862  143 THR C OG1 
4505 C CG2 . THR C 143 ? 0.95069 0.78767 0.96388 -0.03524 0.13584  0.09569  143 THR C CG2 
4506 N N   . PHE C 144 ? 1.07558 0.91524 1.09475 -0.01758 0.10848  0.11005  144 PHE C N   
4507 C CA  . PHE C 144 ? 1.05172 0.89341 1.06277 -0.00768 0.09774  0.11818  144 PHE C CA  
4508 C C   . PHE C 144 ? 1.08400 0.90104 1.07359 0.00060  0.10872  0.12949  144 PHE C C   
4509 O O   . PHE C 144 ? 1.08599 0.90190 1.05505 0.01268  0.10365  0.13968  144 PHE C O   
4510 C CB  . PHE C 144 ? 1.05910 0.91489 1.09202 -0.01072 0.08909  0.11148  144 PHE C CB  
4511 C CG  . PHE C 144 ? 1.07085 0.93157 1.09819 -0.00148 0.07782  0.11839  144 PHE C CG  
4512 C CD1 . PHE C 144 ? 1.03662 0.91298 1.05743 0.00362  0.06408  0.12065  144 PHE C CD1 
4513 C CD2 . PHE C 144 ? 1.06716 0.91807 1.09658 0.00101  0.08181  0.12110  144 PHE C CD2 
4514 C CE1 . PHE C 144 ? 1.03089 0.91566 1.04809 0.01118  0.05429  0.12534  144 PHE C CE1 
4515 C CE2 . PHE C 144 ? 1.02741 0.88486 1.05247 0.01015  0.07165  0.12706  144 PHE C CE2 
4516 C CZ  . PHE C 144 ? 1.03682 0.91279 1.05649 0.01524  0.05761  0.12897  144 PHE C CZ  
4517 N N   . LYS C 145 ? 1.07931 0.87637 1.07160 -0.00524 0.12502  0.12739  145 LYS C N   
4518 C CA  . LYS C 145 ? 1.08049 0.84838 1.04865 0.00415  0.13789  0.13901  145 LYS C CA  
4519 C C   . LYS C 145 ? 1.16456 0.91439 1.10538 0.01061  0.14804  0.14785  145 LYS C C   
4520 O O   . LYS C 145 ? 1.26286 0.99427 1.17666 0.02536  0.15312  0.16102  145 LYS C O   
4521 C CB  . LYS C 145 ? 1.08137 0.82850 1.05732 -0.00559 0.15557  0.13332  145 LYS C CB  
4522 C CG  . LYS C 145 ? 1.13411 0.87490 1.11954 -0.02165 0.17148  0.12225  145 LYS C CG  
4523 C CD  . LYS C 145 ? 1.21273 0.93064 1.20209 -0.03266 0.19217  0.11573  145 LYS C CD  
4524 C CE  . LYS C 145 ? 1.21996 0.93199 1.21641 -0.04957 0.21067  0.10386  145 LYS C CE  
4525 N NZ  . LYS C 145 ? 1.26826 0.95288 1.26333 -0.06206 0.23531  0.09702  145 LYS C NZ  
4526 N N   . LEU C 146 ? 1.14903 0.90451 1.09478 0.00160  0.15096  0.14133  146 LEU C N   
4527 C CA  . LEU C 146 ? 1.13577 0.87196 1.05529 0.00653  0.16265  0.14904  146 LEU C CA  
4528 C C   . LEU C 146 ? 1.10390 0.85434 1.00482 0.02045  0.14814  0.15787  146 LEU C C   
4529 O O   . LEU C 146 ? 1.15961 0.89284 1.03225 0.03038  0.15665  0.16789  146 LEU C O   
4530 C CB  . LEU C 146 ? 1.08982 0.82700 1.02153 -0.00871 0.17264  0.13805  146 LEU C CB  
4531 C CG  . LEU C 146 ? 1.08855 0.80620 1.02929 -0.02329 0.19484  0.12937  146 LEU C CG  
4532 C CD1 . LEU C 146 ? 1.12100 0.85629 1.09279 -0.03389 0.19025  0.11676  146 LEU C CD1 
4533 C CD2 . LEU C 146 ? 1.07260 0.79123 1.01719 -0.03433 0.20531  0.12141  146 LEU C CD2 
4534 N N   . GLU C 147 ? 1.05816 0.83935 0.97289 0.02102  0.12774  0.15367  147 GLU C N   
4535 C CA  . GLU C 147 ? 1.04653 0.84524 0.94570 0.03074  0.11474  0.15854  147 GLU C CA  
4536 C C   . GLU C 147 ? 1.09849 0.89157 0.97288 0.04960  0.11362  0.17189  147 GLU C C   
4537 O O   . GLU C 147 ? 1.15170 0.93977 1.03012 0.05442  0.11366  0.17494  147 GLU C O   
4538 C CB  . GLU C 147 ? 1.10101 0.93114 1.02100 0.02481  0.09581  0.14930  147 GLU C CB  
4539 C CG  . GLU C 147 ? 1.03397 0.87099 0.97525 0.01006  0.09621  0.13704  147 GLU C CG  
4540 C CD  . GLU C 147 ? 1.12726 0.98649 1.09030 0.00475  0.08178  0.12838  147 GLU C CD  
4541 O OE1 . GLU C 147 ? 1.10566 0.97553 1.06978 0.01023  0.07146  0.13080  147 GLU C OE1 
4542 O OE2 . GLU C 147 ? 1.13329 0.99856 1.11194 -0.00419 0.08186  0.11912  147 GLU C OE2 
4543 N N   . PRO C 148 ? 1.16903 0.96411 1.01672 0.06184  0.11271  0.17994  148 PRO C N   
4544 C CA  . PRO C 148 ? 1.18278 0.97611 1.00462 0.08353  0.11137  0.19316  148 PRO C CA  
4545 C C   . PRO C 148 ? 1.15218 0.97897 0.98386 0.08970  0.09193  0.19129  148 PRO C C   
4546 O O   . PRO C 148 ? 1.18226 1.01020 0.99669 0.10826  0.09052  0.20136  148 PRO C O   
4547 C CB  . PRO C 148 ? 1.12316 0.91746 0.91630 0.09374  0.11338  0.19957  148 PRO C CB  
4548 C CG  . PRO C 148 ? 1.09020 0.90195 0.89928 0.07701  0.10665  0.18740  148 PRO C CG  
4549 C CD  . PRO C 148 ? 1.12943 0.92970 0.96780 0.05801  0.11308  0.17740  148 PRO C CD  
4550 N N   . CYS C 149 ? 1.12284 0.97626 0.97966 0.07576  0.07800  0.17890  149 CYS C N   
4551 C CA  . CYS C 149 ? 1.13376 1.01588 1.00245 0.07848  0.06198  0.17554  149 CYS C CA  
4552 C C   . CYS C 149 ? 1.12542 1.01620 1.02523 0.05974  0.05577  0.16251  149 CYS C C   
4553 O O   . CYS C 149 ? 1.14491 1.02955 1.05447 0.04661  0.05983  0.15531  149 CYS C O   
4554 C CB  . CYS C 149 ? 1.13198 1.04809 0.98698 0.08692  0.04854  0.17495  149 CYS C CB  
4555 S SG  . CYS C 149 ? 1.12243 1.06150 0.98681 0.06902  0.03981  0.16045  149 CYS C SG  
4556 N N   . LYS C 150 ? 1.15824 1.06298 1.07232 0.06013  0.04653  0.15998  150 LYS C N   
4557 C CA  . LYS C 150 ? 1.10168 1.01593 1.04216 0.04517  0.03980  0.14851  150 LYS C CA  
4558 C C   . LYS C 150 ? 1.08119 1.01711 1.02358 0.03652  0.03052  0.13939  150 LYS C C   
4559 O O   . LYS C 150 ? 1.10826 1.06531 1.03781 0.04208  0.02291  0.13967  150 LYS C O   
4560 C CB  . LYS C 150 ? 1.01738 0.94216 0.96918 0.04888  0.03211  0.14853  150 LYS C CB  
4561 C CG  . LYS C 150 ? 0.99538 0.89676 0.94351 0.05725  0.04246  0.15704  150 LYS C CG  
4562 C CD  . LYS C 150 ? 0.96166 0.83973 0.92226 0.04544  0.05457  0.15269  150 LYS C CD  
4563 C CE  . LYS C 150 ? 1.03018 0.88147 0.98508 0.05114  0.06810  0.15955  150 LYS C CE  
4564 N NZ  . LYS C 150 ? 1.02823 0.85946 0.99472 0.03786  0.08185  0.15325  150 LYS C NZ  
4565 N N   . PHE C 151 ? 1.00449 0.93624 0.96226 0.02316  0.03173  0.13049  151 PHE C N   
4566 C CA  . PHE C 151 ? 0.99715 0.94205 0.95264 0.01491  0.02674  0.12224  151 PHE C CA  
4567 C C   . PHE C 151 ? 1.05047 1.02107 1.00695 0.01349  0.01469  0.11675  151 PHE C C   
4568 O O   . PHE C 151 ? 1.02994 1.01370 0.97933 0.00725  0.01126  0.10980  151 PHE C O   
4569 C CB  . PHE C 151 ? 0.92355 0.85847 0.89406 0.00372  0.03072  0.11437  151 PHE C CB  
4570 C CG  . PHE C 151 ? 0.98910 0.92810 0.97814 -0.00056 0.02552  0.10905  151 PHE C CG  
4571 C CD1 . PHE C 151 ? 1.00923 0.93875 1.01225 0.00083  0.02912  0.11091  151 PHE C CD1 
4572 C CD2 . PHE C 151 ? 1.00510 0.95665 0.99639 -0.00660 0.01815  0.10144  151 PHE C CD2 
4573 C CE1 . PHE C 151 ? 0.94366 0.87816 0.96286 -0.00218 0.02391  0.10598  151 PHE C CE1 
4574 C CE2 . PHE C 151 ? 0.95053 0.90366 0.95650 -0.00950 0.01425  0.09723  151 PHE C CE2 
4575 C CZ  . PHE C 151 ? 0.88108 0.82659 0.90111 -0.00651 0.01642  0.09987  151 PHE C CZ  
4576 N N   . TRP C 152 ? 1.06246 1.04062 1.02760 0.01796  0.00925  0.11859  152 TRP C N   
4577 C CA  . TRP C 152 ? 1.04789 1.05328 1.01334 0.01714  -0.00131 0.11322  152 TRP C CA  
4578 C C   . TRP C 152 ? 1.10759 1.13351 1.05566 0.03002  -0.00563 0.11876  152 TRP C C   
4579 O O   . TRP C 152 ? 1.13879 1.19406 1.08566 0.02846  -0.01431 0.11212  152 TRP C O   
4580 C CB  . TRP C 152 ? 1.03494 1.04239 1.01732 0.01641  -0.00565 0.11190  152 TRP C CB  
4581 C CG  . TRP C 152 ? 0.98478 0.98285 0.96881 0.02870  -0.00333 0.12207  152 TRP C CG  
4582 C CD1 . TRP C 152 ? 0.99699 1.00909 0.97267 0.04219  -0.00747 0.12863  152 TRP C CD1 
4583 C CD2 . TRP C 152 ? 0.92622 0.89948 0.92043 0.02844  0.00455  0.12565  152 TRP C CD2 
4584 N NE1 . TRP C 152 ? 0.92827 0.92055 0.90613 0.05064  -0.00127 0.13718  152 TRP C NE1 
4585 C CE2 . TRP C 152 ? 0.90845 0.87731 0.89826 0.04096  0.00631  0.13463  152 TRP C CE2 
4586 C CE3 . TRP C 152 ? 0.90348 0.85963 0.90950 0.01924  0.01088  0.12137  152 TRP C CE3 
4587 C CZ2 . TRP C 152 ? 0.91721 0.86270 0.91382 0.04201  0.01526  0.13848  152 TRP C CZ2 
4588 C CZ3 . TRP C 152 ? 0.87192 0.81043 0.88651 0.02046  0.01839  0.12437  152 TRP C CZ3 
4589 C CH2 . TRP C 152 ? 0.90791 0.83994 0.91772 0.03052  0.02107  0.13240  152 TRP C CH2 
4590 N N   . ASN C 153 ? 1.25230 1.26446 1.18572 0.04296  0.00098  0.13008  153 ASN C N   
4591 C CA  . ASN C 153 ? 1.27263 1.30370 1.18517 0.05878  -0.00234 0.13660  153 ASN C CA  
4592 C C   . ASN C 153 ? 1.28714 1.32651 1.18259 0.05735  -0.00141 0.13406  153 ASN C C   
4593 O O   . ASN C 153 ? 1.31559 1.37861 1.19350 0.06998  -0.00618 0.13699  153 ASN C O   
4594 C CB  . ASN C 153 ? 1.27840 1.28707 1.17841 0.07683  0.00608  0.15180  153 ASN C CB  
4595 C CG  . ASN C 153 ? 1.28628 1.29182 1.19829 0.08193  0.00450  0.15505  153 ASN C CG  
4596 O OD1 . ASN C 153 ? 1.29286 1.26864 1.21191 0.08042  0.01383  0.15933  153 ASN C OD1 
4597 N ND2 . ASN C 153 ? 1.29099 1.32907 1.20606 0.08697  -0.00693 0.15170  153 ASN C ND2 
4598 N N   . GLN C 154 ? 1.18155 1.20373 1.08075 0.04374  0.00463  0.12870  154 GLN C N   
4599 C CA  . GLN C 154 ? 1.13436 1.16439 1.01781 0.04078  0.00569  0.12496  154 GLN C CA  
4600 C C   . GLN C 154 ? 1.17148 1.24023 1.05351 0.03444  -0.00514 0.11278  154 GLN C C   
4601 O O   . GLN C 154 ? 1.22931 1.30942 1.12709 0.02361  -0.01045 0.10334  154 GLN C O   
4602 C CB  . GLN C 154 ? 1.05509 1.06145 0.94575 0.02622  0.01375  0.11962  154 GLN C CB  
4603 C CG  . GLN C 154 ? 1.04654 1.01913 0.94106 0.02882  0.02536  0.12797  154 GLN C CG  
4604 C CD  . GLN C 154 ? 0.99310 0.94988 0.89749 0.01499  0.03168  0.12073  154 GLN C CD  
4605 O OE1 . GLN C 154 ? 0.94486 0.91201 0.85019 0.00482  0.02820  0.11085  154 GLN C OE1 
4606 N NE2 . GLN C 154 ? 1.00253 0.93485 0.91454 0.01434  0.04176  0.12461  154 GLN C NE2 
4607 N N   . ARG C 155 ? 1.14022 1.23007 1.00263 0.04065  -0.00764 0.11208  155 ARG C N   
4608 C CA  . ARG C 155 ? 1.15282 1.28450 1.01311 0.03363  -0.01719 0.09834  155 ARG C CA  
4609 C C   . ARG C 155 ? 1.18352 1.32192 1.02776 0.02723  -0.01463 0.09175  155 ARG C C   
4610 O O   . ARG C 155 ? 1.20674 1.32350 1.03692 0.03476  -0.00727 0.10099  155 ARG C O   
4611 C CB  . ARG C 155 ? 1.21374 1.38213 1.06680 0.05137  -0.02676 0.10201  155 ARG C CB  
4612 C CG  . ARG C 155 ? 1.29956 1.46743 1.16950 0.05531  -0.03036 0.10530  155 ARG C CG  
4613 C CD  . ARG C 155 ? 1.29233 1.46949 1.18302 0.03317  -0.03368 0.08937  155 ARG C CD  
4614 N NE  . ARG C 155 ? 1.31769 1.50147 1.22353 0.03698  -0.03843 0.09093  155 ARG C NE  
4615 C CZ  . ARG C 155 ? 1.32764 1.47901 1.24638 0.03742  -0.03387 0.09843  155 ARG C CZ  
4616 N NH1 . ARG C 155 ? 1.27829 1.39028 1.19694 0.03605  -0.02444 0.10573  155 ARG C NH1 
4617 N NH2 . ARG C 155 ? 1.33867 1.49978 1.27104 0.03901  -0.03872 0.09762  155 ARG C NH2 
4618 N N   . ASP C 156 ? 1.19816 1.36587 1.04428 0.01190  -0.01956 0.07467  156 ASP C N   
4619 C CA  . ASP C 156 ? 1.19684 1.37028 1.03027 0.00039  -0.01624 0.06436  156 ASP C CA  
4620 C C   . ASP C 156 ? 1.26196 1.48340 1.07847 0.00937  -0.02476 0.05934  156 ASP C C   
4621 O O   . ASP C 156 ? 1.27719 1.53815 1.09931 0.01010  -0.03399 0.05139  156 ASP C O   
4622 C CB  . ASP C 156 ? 1.23202 1.40150 1.07716 -0.02499 -0.01302 0.04690  156 ASP C CB  
4623 C CG  . ASP C 156 ? 1.23192 1.39646 1.06411 -0.03826 -0.00638 0.03681  156 ASP C CG  
4624 O OD1 . ASP C 156 ? 1.22175 1.35023 1.05093 -0.03809 0.00250  0.04386  156 ASP C OD1 
4625 O OD2 . ASP C 156 ? 1.26073 1.45843 1.08606 -0.04961 -0.00942 0.02078  156 ASP C OD2 
4626 N N   . ILE C 157 ? 1.27918 1.49951 1.07485 0.01696  -0.02167 0.06361  157 ILE C N   
4627 C CA  . ILE C 157 ? 1.22469 1.49279 1.00171 0.02835  -0.02997 0.05944  157 ILE C CA  
4628 C C   . ILE C 157 ? 1.24960 1.55862 1.03099 0.00643  -0.03474 0.03485  157 ILE C C   
4629 O O   . ILE C 157 ? 1.23825 1.59890 1.01947 0.01063  -0.04505 0.02580  157 ILE C O   
4630 C CB  . ILE C 157 ? 1.27874 1.53281 1.03067 0.04115  -0.02430 0.06973  157 ILE C CB  
4631 C CG1 . ILE C 157 ? 1.27223 1.49001 1.01618 0.06438  -0.01837 0.09346  157 ILE C CG1 
4632 C CG2 . ILE C 157 ? 1.31561 1.62292 1.04752 0.05067  -0.03310 0.06226  157 ILE C CG2 
4633 C CD1 . ILE C 157 ? 1.22792 1.46922 0.96618 0.08865  -0.02607 0.10362  157 ILE C CD1 
4634 N N   . ARG C 158 ? 1.26484 1.55227 1.04947 -0.01735 -0.02627 0.02276  158 ARG C N   
4635 C CA  . ARG C 158 ? 1.30419 1.62801 1.08864 -0.03946 -0.02794 -0.00186 158 ARG C CA  
4636 C C   . ARG C 158 ? 1.34130 1.67232 1.14654 -0.05778 -0.02855 -0.01541 158 ARG C C   
4637 O O   . ARG C 158 ? 1.38250 1.74582 1.18834 -0.07766 -0.02880 -0.03755 158 ARG C O   
4638 C CB  . ARG C 158 ? 1.34447 1.64454 1.11833 -0.05713 -0.01711 -0.01096 158 ARG C CB  
4639 C CG  . ARG C 158 ? 1.37017 1.61791 1.15526 -0.07419 -0.00490 -0.01207 158 ARG C CG  
4640 C CD  . ARG C 158 ? 1.39152 1.62289 1.16308 -0.09112 0.00581  -0.02351 158 ARG C CD  
4641 N NE  . ARG C 158 ? 1.39015 1.60293 1.14616 -0.07738 0.00925  -0.01019 158 ARG C NE  
4642 C CZ  . ARG C 158 ? 1.38751 1.55202 1.14580 -0.07364 0.01841  0.00258  158 ARG C CZ  
4643 N NH1 . ARG C 158 ? 1.39331 1.52422 1.16799 -0.08108 0.02437  0.00413  158 ARG C NH1 
4644 N NH2 . ARG C 158 ? 1.35795 1.50932 1.10127 -0.06178 0.02199  0.01350  158 ARG C NH2 
4645 N N   . THR C 159 ? 1.33084 1.63272 1.15222 -0.05261 -0.02776 -0.00376 159 THR C N   
4646 C CA  . THR C 159 ? 1.34515 1.66053 1.18467 -0.06470 -0.03032 -0.01437 159 THR C CA  
4647 C C   . THR C 159 ? 1.34863 1.71462 1.19155 -0.04859 -0.04344 -0.01320 159 THR C C   
4648 O O   . THR C 159 ? 1.36963 1.77720 1.21988 -0.06118 -0.04786 -0.03124 159 THR C O   
4649 C CB  . THR C 159 ? 1.36495 1.63000 1.21974 -0.06565 -0.02415 -0.00328 159 THR C CB  
4650 O OG1 . THR C 159 ? 1.39066 1.61527 1.24309 -0.08227 -0.01184 -0.00827 159 THR C OG1 
4651 C CG2 . THR C 159 ? 1.33271 1.61181 1.20507 -0.07336 -0.02772 -0.01084 159 THR C CG2 
4652 N N   . ARG C 160 ? 1.32711 1.68939 1.16388 -0.02059 -0.04849 0.00753  160 ARG C N   
4653 C CA  . ARG C 160 ? 1.31011 1.71883 1.14602 -0.00011 -0.06032 0.01117  160 ARG C CA  
4654 C C   . ARG C 160 ? 1.37509 1.84894 1.20184 -0.00396 -0.06813 -0.00761 160 ARG C C   
4655 O O   . ARG C 160 ? 1.40221 1.92421 1.23899 -0.00687 -0.07601 -0.02039 160 ARG C O   
4656 C CB  . ARG C 160 ? 1.29300 1.68288 1.11413 0.03127  -0.06097 0.03610  160 ARG C CB  
4657 C CG  . ARG C 160 ? 1.26049 1.69270 1.07561 0.05787  -0.07164 0.04324  160 ARG C CG  
4658 C CD  . ARG C 160 ? 1.27363 1.69628 1.10776 0.06124  -0.07350 0.04887  160 ARG C CD  
4659 N NE  . ARG C 160 ? 1.24320 1.69553 1.06872 0.09157  -0.08152 0.06044  160 ARG C NE  
4660 C CZ  . ARG C 160 ? 1.24616 1.69105 1.08360 0.10161  -0.08327 0.06900  160 ARG C CZ  
4661 N NH1 . ARG C 160 ? 1.26684 1.67607 1.12529 0.08424  -0.07813 0.06782  160 ARG C NH1 
4662 N NH2 . ARG C 160 ? 1.17305 1.64561 0.99937 0.13139  -0.08976 0.07967  160 ARG C NH2 
4663 N N   . ILE C 161 ? 1.45114 1.92977 1.25915 -0.00450 -0.06584 -0.01062 161 ILE C N   
4664 C CA  . ILE C 161 ? 1.46793 2.01277 1.26453 -0.00426 -0.07410 -0.02740 161 ILE C CA  
4665 C C   . ILE C 161 ? 1.48199 2.05752 1.29187 -0.03810 -0.07232 -0.05743 161 ILE C C   
4666 O O   . ILE C 161 ? 1.48072 2.12020 1.29539 -0.03999 -0.08128 -0.07390 161 ILE C O   
4667 C CB  . ILE C 161 ? 1.45627 1.99443 1.22810 0.00355  -0.07109 -0.02252 161 ILE C CB  
4668 C CG1 . ILE C 161 ? 1.42732 1.93876 1.18347 0.03836  -0.07172 0.00657  161 ILE C CG1 
4669 C CG2 . ILE C 161 ? 1.50726 2.11602 1.26754 0.00064  -0.07921 -0.04297 161 ILE C CG2 
4670 C CD1 . ILE C 161 ? 1.41970 1.97465 1.17221 0.06702  -0.08341 0.01463  161 ILE C CD1 
4671 N N   . GLU C 162 ? 1.42133 1.95190 1.23621 -0.06501 -0.05956 -0.06556 162 GLU C N   
4672 C CA  . GLU C 162 ? 1.43387 1.98392 1.25768 -0.09882 -0.05386 -0.09411 162 GLU C CA  
4673 C C   . GLU C 162 ? 1.44001 2.01334 1.28440 -0.10432 -0.05816 -0.10162 162 GLU C C   
4674 O O   . GLU C 162 ? 1.42881 2.04680 1.27963 -0.12585 -0.05809 -0.12734 162 GLU C O   
4675 C CB  . GLU C 162 ? 1.46429 1.95098 1.28663 -0.12149 -0.03750 -0.09672 162 GLU C CB  
4676 C CG  . GLU C 162 ? 1.48323 1.97522 1.30945 -0.15754 -0.02669 -0.12508 162 GLU C CG  
4677 C CD  . GLU C 162 ? 1.49092 1.91827 1.30971 -0.17501 -0.00954 -0.12556 162 GLU C CD  
4678 O OE1 . GLU C 162 ? 1.50306 1.88718 1.31549 -0.15953 -0.00730 -0.10501 162 GLU C OE1 
4679 O OE2 . GLU C 162 ? 1.51777 1.93680 1.33608 -0.20418 0.00294  -0.14694 162 GLU C OE2 
4680 N N   . ALA C 163 ? 1.41622 1.96096 1.27097 -0.08604 -0.06114 -0.08059 163 ALA C N   
4681 C CA  . ALA C 163 ? 1.36158 1.93281 1.23463 -0.08616 -0.06695 -0.08529 163 ALA C CA  
4682 C C   . ALA C 163 ? 1.37442 2.01884 1.24527 -0.06532 -0.08202 -0.08803 163 ALA C C   
4683 O O   . ALA C 163 ? 1.37634 2.07106 1.25966 -0.07559 -0.08667 -0.10641 163 ALA C O   
4684 C CB  . ALA C 163 ? 1.32574 1.84435 1.20929 -0.07238 -0.06529 -0.06219 163 ALA C CB  
4685 N N   . LEU C 164 ? 1.39914 2.05079 1.25298 -0.03513 -0.08897 -0.07007 164 LEU C N   
4686 C CA  . LEU C 164 ? 1.35567 2.07404 1.20365 -0.00882 -0.10316 -0.06902 164 LEU C CA  
4687 C C   . LEU C 164 ? 1.36854 2.16215 1.21491 -0.02488 -0.10839 -0.09891 164 LEU C C   
4688 O O   . LEU C 164 ? 1.37132 2.23278 1.22348 -0.01491 -0.11949 -0.10883 164 LEU C O   
4689 C CB  . LEU C 164 ? 1.32284 2.02527 1.14747 0.02646  -0.10631 -0.04326 164 LEU C CB  
4690 C CG  . LEU C 164 ? 1.35091 1.99116 1.17677 0.04674  -0.10218 -0.01429 164 LEU C CG  
4691 C CD1 . LEU C 164 ? 1.38368 2.00002 1.18350 0.07674  -0.10094 0.00919  164 LEU C CD1 
4692 C CD2 . LEU C 164 ? 1.32986 1.99353 1.16965 0.06114  -0.10964 -0.00988 164 LEU C CD2 
4693 N N   . LEU C 165 ? 1.38419 2.16938 1.22253 -0.04949 -0.10022 -0.11444 165 LEU C N   
4694 C CA  . LEU C 165 ? 1.37739 2.23332 1.21219 -0.06635 -0.10383 -0.14428 165 LEU C CA  
4695 C C   . LEU C 165 ? 1.36227 2.22746 1.21466 -0.10865 -0.09428 -0.17469 165 LEU C C   
4696 O O   . LEU C 165 ? 1.36684 2.29403 1.21933 -0.12779 -0.09559 -0.20381 165 LEU C O   
4697 C CB  . LEU C 165 ? 1.34488 2.19153 1.15650 -0.06620 -0.10038 -0.14413 165 LEU C CB  
4698 C CG  . LEU C 165 ? 1.33725 2.17235 1.12921 -0.02310 -0.10814 -0.11318 165 LEU C CG  
4699 C CD1 . LEU C 165 ? 1.40545 2.22358 1.17332 -0.02073 -0.10377 -0.10961 165 LEU C CD1 
4700 C CD2 . LEU C 165 ? 1.27242 2.17977 1.06093 0.00873  -0.12440 -0.11037 165 LEU C CD2 
4701 N N   . LEU C 166 ? 1.35156 2.15783 1.21773 -0.12333 -0.08400 -0.16923 166 LEU C N   
4702 C CA  . LEU C 166 ? 1.34930 2.15490 1.22958 -0.16201 -0.07235 -0.19568 166 LEU C CA  
4703 C C   . LEU C 166 ? 1.35559 2.16758 1.22462 -0.19426 -0.06073 -0.22213 166 LEU C C   
4704 O O   . LEU C 166 ? 1.34950 2.20681 1.22499 -0.22292 -0.05608 -0.25357 166 LEU C O   
4705 C CB  . LEU C 166 ? 1.34594 2.22149 1.24388 -0.16385 -0.08126 -0.21228 166 LEU C CB  
4706 C CG  . LEU C 166 ? 1.36591 2.23153 1.28123 -0.14756 -0.08681 -0.19645 166 LEU C CG  
4707 C CD1 . LEU C 166 ? 1.39563 2.18516 1.31990 -0.16732 -0.07187 -0.19140 166 LEU C CD1 
4708 C CD2 . LEU C 166 ? 1.33701 2.19867 1.24614 -0.10226 -0.10039 -0.16396 166 LEU C CD2 
4709 N N   . VAL C 167 ? 1.37175 2.13868 1.22333 -0.19018 -0.05507 -0.21023 167 VAL C N   
4710 C CA  . VAL C 167 ? 1.37118 2.13522 1.20918 -0.21825 -0.04295 -0.23217 167 VAL C CA  
4711 C C   . VAL C 167 ? 1.42667 2.10125 1.25528 -0.22310 -0.02828 -0.21618 167 VAL C C   
4712 O O   . VAL C 167 ? 1.45765 2.09160 1.28283 -0.19608 -0.03265 -0.18661 167 VAL C O   
4713 C CB  . VAL C 167 ? 1.38669 2.20964 1.20865 -0.20430 -0.05411 -0.23759 167 VAL C CB  
4714 C CG1 . VAL C 167 ? 1.37666 2.19111 1.18355 -0.23404 -0.04038 -0.25982 167 VAL C CG1 
4715 C CG2 . VAL C 167 ? 1.34648 2.26481 1.17746 -0.19737 -0.06927 -0.25458 167 VAL C CG2 
4716 N N   . ARG C 168 ? 1.46436 2.10873 1.28790 -0.25741 -0.00979 -0.23644 168 ARG C N   
4717 C CA  . ARG C 168 ? 1.48979 2.05305 1.30241 -0.26234 0.00528  -0.22386 168 ARG C CA  
4718 C C   . ARG C 168 ? 1.49740 2.05325 1.29269 -0.24330 0.00064  -0.20941 168 ARG C C   
4719 O O   . ARG C 168 ? 1.47757 2.08805 1.26318 -0.24152 -0.00693 -0.22122 168 ARG C O   
4720 C CB  . ARG C 168 ? 1.46964 2.00747 1.27547 -0.30236 0.02737  -0.25100 168 ARG C CB  
4721 C CG  . ARG C 168 ? 1.46423 1.92049 1.25577 -0.30824 0.04492  -0.24094 168 ARG C CG  
4722 C CD  . ARG C 168 ? 1.47083 1.86486 1.27138 -0.29223 0.04703  -0.21474 168 ARG C CD  
4723 N NE  . ARG C 168 ? 1.51398 1.83703 1.30104 -0.29287 0.06173  -0.20377 168 ARG C NE  
4724 C CZ  . ARG C 168 ? 1.51653 1.78690 1.29579 -0.31351 0.08247  -0.21240 168 ARG C CZ  
4725 N NH1 . ARG C 168 ? 1.58079 1.85543 1.36374 -0.33725 0.09275  -0.23202 168 ARG C NH1 
4726 N NH2 . ARG C 168 ? 1.46158 1.67242 1.22794 -0.30908 0.09408  -0.20062 168 ARG C NH2 
4727 N N   . ASP C 169 ? 1.54679 2.03757 1.33890 -0.22713 0.00450  -0.18311 169 ASP C N   
4728 C CA  . ASP C 169 ? 1.53127 1.99714 1.30880 -0.20683 0.00260  -0.16350 169 ASP C CA  
4729 C C   . ASP C 169 ? 1.55403 2.07948 1.32265 -0.18444 -0.01364 -0.15981 169 ASP C C   
4730 O O   . ASP C 169 ? 1.57146 2.09797 1.32229 -0.17988 -0.01270 -0.15863 169 ASP C O   
4731 C CB  . ASP C 169 ? 1.48944 1.91322 1.25097 -0.22748 0.01999  -0.17322 169 ASP C CB  
4732 C CG  . ASP C 169 ? 1.53999 2.00994 1.28837 -0.24943 0.02321  -0.20204 169 ASP C CG  
4733 O OD1 . ASP C 169 ? 1.55931 2.09847 1.31182 -0.25151 0.01235  -0.21777 169 ASP C OD1 
4734 O OD2 . ASP C 169 ? 1.57500 2.01291 1.30804 -0.26412 0.03698  -0.20937 169 ASP C OD2 
4735 N N   . MET C 170 ? 1.60636 2.17924 1.38567 -0.16762 -0.02828 -0.15615 170 MET C N   
4736 C CA  . MET C 170 ? 1.62831 2.25946 1.39720 -0.14170 -0.04394 -0.15108 170 MET C CA  
4737 C C   . MET C 170 ? 1.67485 2.26911 1.43825 -0.10639 -0.04905 -0.11645 170 MET C C   
4738 O O   . MET C 170 ? 1.65975 2.26046 1.43242 -0.08479 -0.05778 -0.10094 170 MET C O   
4739 C CB  . MET C 170 ? 1.59741 2.30180 1.37880 -0.14022 -0.05623 -0.16593 170 MET C CB  
4740 C CG  . MET C 170 ? 1.57127 2.34729 1.33978 -0.11440 -0.07229 -0.16575 170 MET C CG  
4741 S SD  . MET C 170 ? 1.61802 2.44445 1.36735 -0.13290 -0.07069 -0.19404 170 MET C SD  
4742 C CE  . MET C 170 ? 1.54922 2.42670 1.27694 -0.08638 -0.08874 -0.17548 170 MET C CE  
4743 N N   . THR C 171 ? 1.66145 2.21427 1.40897 -0.10173 -0.04187 -0.10495 171 THR C N   
4744 C CA  . THR C 171 ? 1.66440 2.17963 1.40433 -0.07120 -0.04369 -0.07405 171 THR C CA  
4745 C C   . THR C 171 ? 1.65577 2.21276 1.37448 -0.04246 -0.05436 -0.06516 171 THR C C   
4746 O O   . THR C 171 ? 1.65016 2.20080 1.36488 -0.01244 -0.06015 -0.04235 171 THR C O   
4747 C CB  . THR C 171 ? 1.65155 2.09796 1.38630 -0.07972 -0.02930 -0.06498 171 THR C CB  
4748 O OG1 . THR C 171 ? 1.69609 2.15256 1.41328 -0.09290 -0.02402 -0.07930 171 THR C OG1 
4749 C CG2 . THR C 171 ? 1.57532 1.97953 1.32869 -0.10283 -0.01889 -0.07116 171 THR C CG2 
4750 N N   . THR C 172 ? 1.61036 2.20949 1.31363 -0.05032 -0.05625 -0.08285 172 THR C N   
4751 C CA  . THR C 172 ? 1.59521 2.23980 1.27596 -0.02164 -0.06691 -0.07581 172 THR C CA  
4752 C C   . THR C 172 ? 1.58082 2.29077 1.26828 -0.00408 -0.08201 -0.07901 172 THR C C   
4753 O O   . THR C 172 ? 1.55573 2.29343 1.26438 -0.02288 -0.08451 -0.09696 172 THR C O   
4754 C CB  . THR C 172 ? 1.52937 2.20678 1.19286 -0.03677 -0.06524 -0.09688 172 THR C CB  
4755 O OG1 . THR C 172 ? 1.50683 2.12146 1.16326 -0.05081 -0.05068 -0.09243 172 THR C OG1 
4756 C CG2 . THR C 172 ? 1.47963 2.20575 1.11715 -0.00504 -0.07644 -0.08942 172 THR C CG2 
4757 N N   . CYS C 173 ? 1.55094 2.28357 1.21888 0.03346  -0.09105 -0.06077 173 CYS C N   
4758 C CA  . CYS C 173 ? 1.50346 2.29437 1.17495 0.05692  -0.10510 -0.05943 173 CYS C CA  
4759 C C   . CYS C 173 ? 1.47318 2.30217 1.11389 0.09672  -0.11429 -0.04595 173 CYS C C   
4760 O O   . CYS C 173 ? 1.48806 2.39648 1.12226 0.10382  -0.12621 -0.06272 173 CYS C O   
4761 C CB  . CYS C 173 ? 1.46618 2.21328 1.15454 0.06745  -0.10325 -0.03942 173 CYS C CB  
4762 S SG  . CYS C 173 ? 1.48089 2.29194 1.17668 0.09502  -0.11874 -0.03708 173 CYS C SG  
4763 N N   . THR C 179 ? 1.52126 2.43561 0.94265 0.41045  -0.13313 0.09320  179 THR C N   
4764 C CA  . THR C 179 ? 1.58580 2.43319 0.97831 0.44857  -0.11979 0.12772  179 THR C CA  
4765 C C   . THR C 179 ? 1.64024 2.42666 0.99622 0.45490  -0.10585 0.14515  179 THR C C   
4766 O O   . THR C 179 ? 1.64854 2.42532 0.97708 0.48815  -0.09948 0.15927  179 THR C O   
4767 C CB  . THR C 179 ? 1.48659 2.28005 0.88938 0.44495  -0.11375 0.14342  179 THR C CB  
4768 O OG1 . THR C 179 ? 1.42594 2.27136 0.85840 0.44778  -0.12475 0.13168  179 THR C OG1 
4769 C CG2 . THR C 179 ? 1.53127 2.24444 0.90300 0.47823  -0.09576 0.17782  179 THR C CG2 
4770 N N   . LEU C 180 ? 1.59525 2.34314 0.95114 0.42238  -0.10049 0.14272  180 LEU C N   
4771 C CA  . LEU C 180 ? 1.62558 2.29862 0.94966 0.42471  -0.08323 0.16284  180 LEU C CA  
4772 C C   . LEU C 180 ? 1.73246 2.42798 1.03336 0.43476  -0.08321 0.15772  180 LEU C C   
4773 O O   . LEU C 180 ? 1.73039 2.46575 1.03826 0.40780  -0.09049 0.13427  180 LEU C O   
4774 C CB  . LEU C 180 ? 1.60750 2.23545 0.96293 0.37652  -0.07531 0.15119  180 LEU C CB  
4775 C CG  . LEU C 180 ? 1.58921 2.16755 0.97903 0.35852  -0.06872 0.15628  180 LEU C CG  
4776 C CD1 . LEU C 180 ? 1.64507 2.28649 1.06829 0.34693  -0.08530 0.13640  180 LEU C CD1 
4777 C CD2 . LEU C 180 ? 1.56010 2.08065 0.97341 0.31750  -0.05638 0.14932  180 LEU C CD2 
4778 N N   . ASP C 181 ? 1.71208 2.37994 0.98438 0.47294  -0.07373 0.17910  181 ASP C N   
4779 C CA  . ASP C 181 ? 1.66951 2.33591 0.91330 0.48280  -0.06891 0.18054  181 ASP C CA  
4780 C C   . ASP C 181 ? 1.64408 2.22017 0.86151 0.47742  -0.04792 0.20146  181 ASP C C   
4781 O O   . ASP C 181 ? 1.66860 2.17743 0.87804 0.48880  -0.03311 0.22430  181 ASP C O   
4782 C CB  . ASP C 181 ? 1.63653 2.32470 0.86127 0.52759  -0.06893 0.19085  181 ASP C CB  
4783 C CG  . ASP C 181 ? 1.69430 2.47566 0.94543 0.53487  -0.08805 0.16976  181 ASP C CG  
4784 O OD1 . ASP C 181 ? 1.76051 2.59221 1.04410 0.50134  -0.10144 0.14421  181 ASP C OD1 
4785 O OD2 . ASP C 181 ? 1.56869 2.37425 0.80732 0.57344  -0.08842 0.17733  181 ASP C OD2 
4786 N N   . GLY C 182 ? 1.61505 2.19033 0.82040 0.45832  -0.04551 0.19211  182 GLY C N   
4787 C CA  . GLY C 182 ? 1.59368 2.08919 0.77421 0.45189  -0.02477 0.20931  182 GLY C CA  
4788 C C   . GLY C 182 ? 1.73306 2.17744 0.94366 0.41555  -0.01581 0.20736  182 GLY C C   
4789 O O   . GLY C 182 ? 1.79117 2.16006 0.99786 0.41939  0.00245  0.22784  182 GLY C O   
4790 N N   . PHE C 183 ? 1.71245 2.19255 0.96447 0.37565  -0.02686 0.17930  183 PHE C N   
4791 C CA  . PHE C 183 ? 1.69887 2.12701 0.99021 0.33544  -0.01732 0.17256  183 PHE C CA  
4792 C C   . PHE C 183 ? 1.74713 2.12855 1.02857 0.31727  -0.00241 0.17266  183 PHE C C   
4793 O O   . PHE C 183 ? 1.78201 2.19364 1.04131 0.31941  -0.00569 0.16421  183 PHE C O   
4794 C CB  . PHE C 183 ? 1.73246 2.21206 1.06775 0.30091  -0.03250 0.14313  183 PHE C CB  
4795 C CG  . PHE C 183 ? 1.70878 2.13779 1.08325 0.26228  -0.02340 0.13627  183 PHE C CG  
4796 C CD1 . PHE C 183 ? 1.63171 2.01980 1.02638 0.26270  -0.01791 0.14869  183 PHE C CD1 
4797 C CD2 . PHE C 183 ? 1.66971 2.09216 1.05899 0.22697  -0.01979 0.11747  183 PHE C CD2 
4798 C CE1 . PHE C 183 ? 1.62707 1.97237 1.05596 0.22975  -0.01010 0.14240  183 PHE C CE1 
4799 C CE2 . PHE C 183 ? 1.56532 1.94218 0.98771 0.19515  -0.01115 0.11212  183 PHE C CE2 
4800 C CZ  . PHE C 183 ? 1.62505 1.96507 1.06730 0.19704  -0.00683 0.12454  183 PHE C CZ  
4801 N N   . VAL C 184 ? 1.76133 2.07076 1.05934 0.29964  0.01418  0.18168  184 VAL C N   
4802 C CA  . VAL C 184 ? 1.77171 2.03190 1.06394 0.28173  0.03013  0.18260  184 VAL C CA  
4803 C C   . VAL C 184 ? 1.76900 2.01665 1.10631 0.23810  0.03065  0.16320  184 VAL C C   
4804 O O   . VAL C 184 ? 1.77253 2.00949 1.14208 0.22602  0.02869  0.16143  184 VAL C O   
4805 C CB  . VAL C 184 ? 1.80460 1.98916 1.07308 0.30030  0.05229  0.21012  184 VAL C CB  
4806 C CG1 . VAL C 184 ? 1.84842 1.98473 1.11471 0.27940  0.06912  0.20917  184 VAL C CG1 
4807 C CG2 . VAL C 184 ? 1.85147 2.04447 1.07000 0.34571  0.05373  0.23021  184 VAL C CG2 
4808 N N   . ALA C 185 ? 1.61656 1.86325 0.95385 0.21596  0.03431  0.14943  185 ALA C N   
4809 C CA  . ALA C 185 ? 1.60898 1.85980 0.98319 0.17661  0.03199  0.12664  185 ALA C CA  
4810 C C   . ALA C 185 ? 1.66883 1.86695 1.07616 0.15902  0.04173  0.13153  185 ALA C C   
4811 O O   . ALA C 185 ? 1.55210 1.76443 0.98915 0.14814  0.03346  0.12384  185 ALA C O   
4812 C CB  . ALA C 185 ? 1.46248 1.70585 0.82448 0.16036  0.03935  0.11627  185 ALA C CB  
4813 N N   . HIS C 186 ? 1.65549 1.79439 1.05671 0.15771  0.05961  0.14455  186 HIS C N   
4814 C CA  . HIS C 186 ? 1.61248 1.70184 1.04322 0.14152  0.07044  0.14870  186 HIS C CA  
4815 C C   . HIS C 186 ? 1.58080 1.63117 1.00063 0.16432  0.08068  0.17213  186 HIS C C   
4816 O O   . HIS C 186 ? 1.56634 1.56428 0.99022 0.15912  0.09752  0.18152  186 HIS C O   
4817 C CB  . HIS C 186 ? 1.66813 1.72195 1.10428 0.12008  0.08415  0.14308  186 HIS C CB  
4818 N N   . ASP C 187 ? 1.58654 1.66291 0.98991 0.19063  0.07182  0.18134  187 ASP C N   
4819 C CA  . ASP C 187 ? 1.63346 1.67479 1.02765 0.21231  0.08094  0.20235  187 ASP C CA  
4820 C C   . ASP C 187 ? 1.57714 1.62281 1.00994 0.19972  0.07347  0.19678  187 ASP C C   
4821 O O   . ASP C 187 ? 1.53560 1.62943 0.97807 0.20356  0.05641  0.18861  187 ASP C O   
4822 C CB  . ASP C 187 ? 1.66948 1.73499 1.02339 0.25020  0.07614  0.21620  187 ASP C CB  
4823 C CG  . ASP C 187 ? 1.68616 1.70214 1.01906 0.27515  0.09188  0.24064  187 ASP C CG  
4824 O OD1 . ASP C 187 ? 1.65305 1.61760 1.00406 0.26064  0.10669  0.24531  187 ASP C OD1 
4825 O OD2 . ASP C 187 ? 1.73577 1.76483 1.03302 0.30973  0.09014  0.25463  187 ASP C OD2 
4826 N N   . SER C 188 ? 1.52931 1.52695 0.98437 0.18436  0.08643  0.20023  188 SER C N   
4827 C CA  . SER C 188 ? 1.50572 1.50574 0.99866 0.16983  0.08000  0.19358  188 SER C CA  
4828 C C   . SER C 188 ? 1.50285 1.51101 0.98948 0.19350  0.07498  0.20566  188 SER C C   
4829 O O   . SER C 188 ? 1.45002 1.48099 0.96368 0.18589  0.06331  0.19778  188 SER C O   
4830 C CB  . SER C 188 ? 1.50622 1.45566 1.02177 0.15047  0.09557  0.19461  188 SER C CB  
4831 O OG  . SER C 188 ? 1.54835 1.49474 1.07251 0.12880  0.09879  0.18208  188 SER C OG  
4832 N N   . ILE C 189 ? 1.55467 1.54182 1.00462 0.22280  0.08491  0.22512  189 ILE C N   
4833 C CA  . ILE C 189 ? 1.49936 1.49664 0.93838 0.24921  0.08017  0.23715  189 ILE C CA  
4834 C C   . ILE C 189 ? 1.50415 1.57178 0.93741 0.26176  0.05818  0.22805  189 ILE C C   
4835 O O   . ILE C 189 ? 1.46904 1.56588 0.91578 0.26877  0.04626  0.22614  189 ILE C O   
4836 C CB  . ILE C 189 ? 1.49518 1.44524 0.89209 0.27873  0.09966  0.26127  189 ILE C CB  
4837 C CG1 . ILE C 189 ? 1.43322 1.31587 0.83814 0.26267  0.12305  0.26732  189 ILE C CG1 
4838 C CG2 . ILE C 189 ? 1.46493 1.42334 0.84730 0.30879  0.09596  0.27464  189 ILE C CG2 
4839 C CD1 . ILE C 189 ? 1.47389 1.34287 0.91858 0.24374  0.12289  0.26177  189 ILE C CD1 
4840 N N   . HIS C 190 ? 1.53758 1.63587 0.95102 0.26428  0.05273  0.22117  190 HIS C N   
4841 C CA  . HIS C 190 ? 1.54904 1.72093 0.95964 0.27225  0.03175  0.20832  190 HIS C CA  
4842 C C   . HIS C 190 ? 1.50754 1.71552 0.96150 0.24014  0.01770  0.18432  190 HIS C C   
4843 O O   . HIS C 190 ? 1.49286 1.75742 0.95517 0.24488  0.00116  0.17414  190 HIS C O   
4844 C CB  . HIS C 190 ? 1.59108 1.78689 0.97084 0.27977  0.03029  0.20465  190 HIS C CB  
4845 C CG  . HIS C 190 ? 1.68797 1.86603 1.01855 0.31913  0.03974  0.22759  190 HIS C CG  
4846 N ND1 . HIS C 190 ? 1.74156 1.93239 1.03740 0.33154  0.04136  0.22894  190 HIS C ND1 
4847 C CD2 . HIS C 190 ? 1.66662 1.81250 0.97433 0.34979  0.04943  0.25046  190 HIS C CD2 
4848 C CE1 . HIS C 190 ? 1.74264 1.90978 0.99539 0.36931  0.05153  0.25233  190 HIS C CE1 
4849 N NE2 . HIS C 190 ? 1.73031 1.86848 0.98879 0.38099  0.05726  0.26581  190 HIS C NE2 
4850 N N   . ASP C 191 ? 1.50769 1.68403 0.98812 0.20816  0.02496  0.17485  191 ASP C N   
4851 C CA  . ASP C 191 ? 1.47266 1.67400 0.99127 0.17790  0.01483  0.15336  191 ASP C CA  
4852 C C   . ASP C 191 ? 1.39384 1.59492 0.93691 0.17929  0.00986  0.15623  191 ASP C C   
4853 O O   . ASP C 191 ? 1.36114 1.60833 0.92267 0.17104  -0.00426 0.14152  191 ASP C O   
4854 C CB  . ASP C 191 ? 1.49629 1.65893 1.03211 0.14835  0.02581  0.14539  191 ASP C CB  
4855 C CG  . ASP C 191 ? 1.45998 1.63333 0.97574 0.14244  0.02803  0.13723  191 ASP C CG  
4856 O OD1 . ASP C 191 ? 1.42784 1.65550 0.93240 0.14656  0.01556  0.12572  191 ASP C OD1 
4857 O OD2 . ASP C 191 ? 1.43990 1.57029 0.95036 0.13468  0.04224  0.14194  191 ASP C OD2 
4858 N N   . CYS C 192 ? 1.38450 1.53470 0.92758 0.18883  0.02214  0.17405  192 CYS C N   
4859 C CA  . CYS C 192 ? 1.38822 1.53741 0.95135 0.19268  0.01802  0.17794  192 CYS C CA  
4860 C C   . CYS C 192 ? 1.38029 1.57940 0.92856 0.21951  0.00460  0.18098  192 CYS C C   
4861 O O   . CYS C 192 ? 1.38564 1.62407 0.95620 0.21254  -0.00869 0.16912  192 CYS C O   
4862 C CB  . CYS C 192 ? 1.39501 1.48120 0.95524 0.20043  0.03542  0.19670  192 CYS C CB  
4863 S SG  . CYS C 192 ? 1.28890 1.31949 0.87612 0.16921  0.05072  0.19252  192 CYS C SG  
4864 N N   . ALA C 193 ? 1.41350 1.61309 0.92287 0.25130  0.00832  0.19653  193 ALA C N   
4865 C CA  . ALA C 193 ? 1.42617 1.67146 0.91807 0.28253  -0.00323 0.20214  193 ALA C CA  
4866 C C   . ALA C 193 ? 1.39093 1.71446 0.89525 0.27316  -0.02351 0.17917  193 ALA C C   
4867 O O   . ALA C 193 ? 1.38326 1.75216 0.89570 0.28422  -0.03630 0.17496  193 ALA C O   
4868 C CB  . ALA C 193 ? 1.51241 1.74321 0.95558 0.31947  0.00562  0.22274  193 ALA C CB  
4869 N N   . LYS C 194 ? 1.38086 1.72207 0.88631 0.25233  -0.02576 0.16311  194 LYS C N   
4870 C CA  . LYS C 194 ? 1.35137 1.76360 0.87194 0.23652  -0.04247 0.13757  194 LYS C CA  
4871 C C   . LYS C 194 ? 1.38040 1.80029 0.94233 0.20994  -0.04812 0.12304  194 LYS C C   
4872 O O   . LYS C 194 ? 1.38252 1.85937 0.95607 0.21152  -0.06187 0.11072  194 LYS C O   
4873 C CB  . LYS C 194 ? 1.30946 1.72878 0.82447 0.21503  -0.04048 0.12248  194 LYS C CB  
4874 C CG  . LYS C 194 ? 1.23100 1.72020 0.76034 0.19453  -0.05474 0.09358  194 LYS C CG  
4875 C CD  . LYS C 194 ? 1.23609 1.72525 0.75710 0.17368  -0.05029 0.07968  194 LYS C CD  
4876 C CE  . LYS C 194 ? 1.41050 1.83458 0.95156 0.14433  -0.03624 0.07911  194 LYS C CE  
4877 N NZ  . LYS C 194 ? 1.40365 1.82786 0.98265 0.11548  -0.03869 0.06376  194 LYS C NZ  
4878 N N   . ASP C 195 ? 1.34885 1.71264 0.93279 0.18654  -0.03720 0.12441  195 ASP C N   
4879 C CA  . ASP C 195 ? 1.35568 1.72182 0.97629 0.16322  -0.04133 0.11235  195 ASP C CA  
4880 C C   . ASP C 195 ? 1.36929 1.73968 0.99606 0.18371  -0.04574 0.12420  195 ASP C C   
4881 O O   . ASP C 195 ? 1.34895 1.75400 0.99888 0.17320  -0.05561 0.11102  195 ASP C O   
4882 C CB  . ASP C 195 ? 1.38324 1.68994 1.02375 0.13678  -0.02866 0.11185  195 ASP C CB  
4883 C CG  . ASP C 195 ? 1.40352 1.71442 1.04763 0.10904  -0.02632 0.09330  195 ASP C CG  
4884 O OD1 . ASP C 195 ? 1.40752 1.77168 1.04775 0.10238  -0.03583 0.07560  195 ASP C OD1 
4885 O OD2 . ASP C 195 ? 1.35204 1.61486 1.00386 0.09303  -0.01464 0.09495  195 ASP C OD2 
4886 N N   . ILE C 196 ? 1.40592 1.74035 1.01134 0.21237  -0.03733 0.14836  196 ILE C N   
4887 C CA  . ILE C 196 ? 1.36547 1.70366 0.97308 0.23413  -0.04055 0.15999  196 ILE C CA  
4888 C C   . ILE C 196 ? 1.40020 1.81466 1.00207 0.25096  -0.05757 0.15081  196 ILE C C   
4889 O O   . ILE C 196 ? 1.42259 1.86657 1.04554 0.24874  -0.06667 0.14362  196 ILE C O   
4890 C CB  . ILE C 196 ? 1.41284 1.69863 0.99107 0.26417  -0.02612 0.18734  196 ILE C CB  
4891 C CG1 . ILE C 196 ? 1.42726 1.64077 1.01223 0.24688  -0.00817 0.19496  196 ILE C CG1 
4892 C CG2 . ILE C 196 ? 1.37491 1.66336 0.95377 0.28712  -0.02842 0.19896  196 ILE C CG2 
4893 C CD1 . ILE C 196 ? 1.41155 1.57250 0.96326 0.27345  0.00915  0.21951  196 ILE C CD1 
4894 N N   . LEU C 197 ? 1.44505 1.89498 1.01807 0.26846  -0.06205 0.15029  197 LEU C N   
4895 C CA  . LEU C 197 ? 1.42230 1.95135 0.98713 0.28778  -0.07846 0.14118  197 LEU C CA  
4896 C C   . LEU C 197 ? 1.41006 1.99587 1.00774 0.25502  -0.09106 0.11072  197 LEU C C   
4897 O O   . LEU C 197 ? 1.43178 2.06768 1.04335 0.26029  -0.10255 0.10209  197 LEU C O   
4898 C CB  . LEU C 197 ? 1.45831 2.01205 0.98413 0.31210  -0.07977 0.14613  197 LEU C CB  
4899 C CG  . LEU C 197 ? 1.50363 2.00901 0.98922 0.35100  -0.06708 0.17673  197 LEU C CG  
4900 C CD1 . LEU C 197 ? 1.49556 2.02133 0.94456 0.36809  -0.06733 0.17873  197 LEU C CD1 
4901 C CD2 . LEU C 197 ? 1.53517 2.05615 1.00913 0.38820  -0.07106 0.19195  197 LEU C CD2 
4902 N N   . MET C 198 ? 1.37974 1.95601 0.98945 0.22051  -0.08746 0.09388  198 MET C N   
4903 C CA  . MET C 198 ? 1.37718 2.00403 1.01275 0.18785  -0.09627 0.06349  198 MET C CA  
4904 C C   . MET C 198 ? 1.43692 2.06346 1.10562 0.17298  -0.09902 0.05707  198 MET C C   
4905 O O   . MET C 198 ? 1.43146 2.11804 1.11663 0.16130  -0.10946 0.03592  198 MET C O   
4906 C CB  . MET C 198 ? 1.34966 1.94703 0.99081 0.15391  -0.08742 0.05051  198 MET C CB  
4907 C CG  . MET C 198 ? 1.28044 1.88898 0.89269 0.16110  -0.08594 0.04971  198 MET C CG  
4908 S SD  . MET C 198 ? 1.33509 1.88255 0.95355 0.12599  -0.07078 0.04339  198 MET C SD  
4909 C CE  . MET C 198 ? 1.37920 1.96986 1.02447 0.08346  -0.07533 0.00698  198 MET C CE  
4910 N N   . MET C 199 ? 1.39075 1.95123 1.06980 0.17175  -0.08908 0.07370  199 MET C N   
4911 C CA  . MET C 199 ? 1.38202 1.93859 1.09015 0.16083  -0.09124 0.07008  199 MET C CA  
4912 C C   . MET C 199 ? 1.45031 2.05837 1.15584 0.18834  -0.10279 0.07345  199 MET C C   
4913 O O   . MET C 199 ? 1.44199 2.09225 1.17008 0.17566  -0.11109 0.05679  199 MET C O   
4914 C CB  . MET C 199 ? 1.31171 1.79042 1.02704 0.15953  -0.07846 0.08904  199 MET C CB  
4915 C CG  . MET C 199 ? 1.29548 1.72827 1.02432 0.12754  -0.06827 0.08170  199 MET C CG  
4916 S SD  . MET C 199 ? 1.31938 1.66804 1.04940 0.13335  -0.05299 0.10570  199 MET C SD  
4917 C CE  . MET C 199 ? 1.30277 1.65197 1.05550 0.13852  -0.05741 0.10996  199 MET C CE  
4918 N N   . LYS C 200 ? 1.50281 2.10727 1.17924 0.22707  -0.10237 0.09503  200 LYS C N   
4919 C CA  . LYS C 200 ? 1.52110 2.17065 1.19093 0.25884  -0.11214 0.10134  200 LYS C CA  
4920 C C   . LYS C 200 ? 1.49673 2.23974 1.16915 0.25770  -0.12793 0.07742  200 LYS C C   
4921 O O   . LYS C 200 ? 1.49320 2.28683 1.17877 0.26536  -0.13809 0.06968  200 LYS C O   
4922 C CB  . LYS C 200 ? 1.54800 2.16767 1.17986 0.30173  -0.10546 0.13023  200 LYS C CB  
4923 C CG  . LYS C 200 ? 1.55870 2.19792 1.18131 0.33831  -0.11008 0.14439  200 LYS C CG  
4924 C CD  . LYS C 200 ? 1.53447 2.12863 1.18244 0.32729  -0.10398 0.15058  200 LYS C CD  
4925 C CE  . LYS C 200 ? 1.53236 2.03532 1.17366 0.32193  -0.08538 0.16931  200 LYS C CE  
4926 N NZ  . LYS C 200 ? 1.58870 2.05528 1.18987 0.36169  -0.07451 0.19648  200 LYS C NZ  
4927 N N   . TYR C 201 ? 1.58791 2.35720 1.24809 0.24774  -0.12982 0.06434  201 TYR C N   
4928 C CA  . TYR C 201 ? 1.57382 2.43445 1.23844 0.24110  -0.14379 0.03740  201 TYR C CA  
4929 C C   . TYR C 201 ? 1.58594 2.46533 1.28689 0.19514  -0.14485 0.00803  201 TYR C C   
4930 O O   . TYR C 201 ? 1.60400 2.55600 1.31966 0.18910  -0.15570 -0.01337 201 TYR C O   
4931 C CB  . TYR C 201 ? 1.60257 2.48566 1.23952 0.24672  -0.14481 0.03291  201 TYR C CB  
4932 N N   . ALA C 202 ? 1.44300 2.25874 1.15754 0.16284  -0.13279 0.00598  202 ALA C N   
4933 C CA  . ALA C 202 ? 1.41660 2.23913 1.16268 0.12178  -0.13104 -0.01871 202 ALA C CA  
4934 C C   . ALA C 202 ? 1.40260 2.22267 1.17140 0.12427  -0.13358 -0.01482 202 ALA C C   
4935 O O   . ALA C 202 ? 1.39023 2.24013 1.18313 0.09742  -0.13558 -0.03747 202 ALA C O   
4936 C CB  . ALA C 202 ? 1.41150 2.16392 1.16356 0.09116  -0.11684 -0.01960 202 ALA C CB  
4937 N N   . LEU C 203 ? 1.38553 2.16814 1.14608 0.15502  -0.13203 0.01300  203 LEU C N   
4938 C CA  . LEU C 203 ? 1.39390 2.17301 1.17453 0.15932  -0.13418 0.01774  203 LEU C CA  
4939 C C   . LEU C 203 ? 1.42561 2.28946 1.20861 0.17758  -0.14842 0.00706  203 LEU C C   
4940 O O   . LEU C 203 ? 1.38426 2.28174 1.19267 0.15899  -0.15261 -0.01104 203 LEU C O   
4941 C CB  . LEU C 203 ? 1.38699 2.09861 1.15671 0.18549  -0.12642 0.04957  203 LEU C CB  
4942 C CG  . LEU C 203 ? 1.27901 1.98054 1.06841 0.19021  -0.12741 0.05581  203 LEU C CG  
4943 C CD1 . LEU C 203 ? 1.28288 1.96365 1.10273 0.15017  -0.12305 0.03929  203 LEU C CD1 
4944 C CD2 . LEU C 203 ? 1.24119 1.87803 1.01734 0.21623  -0.11842 0.08587  203 LEU C CD2 
4945 N N   . ARG C 204 ? 1.44646 2.34638 1.20207 0.21522  -0.15544 0.01811  204 ARG C N   
4946 C CA  . ARG C 204 ? 1.41478 2.40010 1.17031 0.23797  -0.16962 0.00917  204 ARG C CA  
4947 C C   . ARG C 204 ? 1.41184 2.47455 1.18737 0.20608  -0.17755 -0.02810 204 ARG C C   
4948 O O   . ARG C 204 ? 1.45796 2.58370 1.25039 0.20731  -0.18672 -0.04279 204 ARG C O   
4949 C CB  . ARG C 204 ? 1.42744 2.43755 1.14528 0.28459  -0.17480 0.02692  204 ARG C CB  
4950 N N   . TYR C 205 ? 1.39011 2.44753 1.16431 0.17592  -0.17274 -0.04462 205 TYR C N   
4951 C CA  . TYR C 205 ? 1.36372 2.49526 1.15179 0.14535  -0.17819 -0.08157 205 TYR C CA  
4952 C C   . TYR C 205 ? 1.37474 2.52681 1.19686 0.11608  -0.17791 -0.10242 205 TYR C C   
4953 O O   . TYR C 205 ? 1.41180 2.64633 1.24663 0.11011  -0.18632 -0.12728 205 TYR C O   
4954 C CB  . TYR C 205 ? 1.31730 2.41814 1.09925 0.11356  -0.16865 -0.09358 205 TYR C CB  
4955 N N   . ALA C 206 ? 1.36762 2.44540 1.20539 0.09772  -0.16708 -0.09313 206 ALA C N   
4956 C CA  . ALA C 206 ? 1.31063 2.40219 1.17826 0.07294  -0.16584 -0.11006 206 ALA C CA  
4957 C C   . ALA C 206 ? 1.32477 2.35340 1.20076 0.08702  -0.16186 -0.08435 206 ALA C C   
4958 O O   . ALA C 206 ? 1.33076 2.35569 1.19411 0.12641  -0.16731 -0.06014 206 ALA C O   
4959 C CB  . ALA C 206 ? 1.26118 2.33391 1.14305 0.02245  -0.15416 -0.13621 206 ALA C CB  
4960 N N   . MET D 1   ? 1.94219 1.78732 1.58317 -0.48051 0.29156  -0.30683 1   MET D N   
4961 C CA  . MET D 1   ? 1.93995 1.81449 1.59670 -0.45067 0.26465  -0.28488 1   MET D CA  
4962 C C   . MET D 1   ? 1.88660 1.80472 1.57548 -0.42659 0.23554  -0.26617 1   MET D C   
4963 O O   . MET D 1   ? 1.86437 1.83352 1.56968 -0.43884 0.22680  -0.27966 1   MET D O   
4964 C CB  . MET D 1   ? 1.92308 1.84841 1.57817 -0.46586 0.25905  -0.30362 1   MET D CB  
4965 C CG  . MET D 1   ? 1.86890 1.81634 1.53297 -0.43784 0.23661  -0.28302 1   MET D CG  
4966 S SD  . MET D 1   ? 1.86211 1.89947 1.56002 -0.41938 0.19914  -0.27480 1   MET D SD  
4967 C CE  . MET D 1   ? 1.67067 1.70065 1.36971 -0.38550 0.18297  -0.24645 1   MET D CE  
4968 N N   . PHE D 2   ? 1.89040 1.78891 1.58800 -0.39283 0.22155  -0.23612 2   PHE D N   
4969 C CA  . PHE D 2   ? 1.87400 1.78792 1.59584 -0.37052 0.20236  -0.21676 2   PHE D CA  
4970 C C   . PHE D 2   ? 1.78713 1.72511 1.52659 -0.33912 0.17703  -0.19233 2   PHE D C   
4971 O O   . PHE D 2   ? 1.74114 1.67234 1.47254 -0.33105 0.17590  -0.18637 2   PHE D O   
4972 C CB  . PHE D 2   ? 1.88419 1.73297 1.59625 -0.36176 0.21733  -0.20432 2   PHE D CB  
4973 C CG  . PHE D 2   ? 1.92988 1.75004 1.62403 -0.39014 0.24311  -0.22559 2   PHE D CG  
4974 C CD1 . PHE D 2   ? 1.87602 1.72285 1.58419 -0.40093 0.23976  -0.23445 2   PHE D CD1 
4975 C CD2 . PHE D 2   ? 2.00455 1.77037 1.66640 -0.40717 0.27243  -0.23784 2   PHE D CD2 
4976 C CE1 . PHE D 2   ? 1.87841 1.69728 1.56902 -0.42889 0.26565  -0.25514 2   PHE D CE1 
4977 C CE2 . PHE D 2   ? 2.00279 1.73744 1.64503 -0.43492 0.29946  -0.25835 2   PHE D CE2 
4978 C CZ  . PHE D 2   ? 1.94542 1.70676 1.60227 -0.44643 0.29628  -0.26729 2   PHE D CZ  
4979 N N   . ASP D 3   ? 1.75449 1.71868 1.51730 -0.32201 0.15810  -0.17854 3   ASP D N   
4980 C CA  . ASP D 3   ? 1.69159 1.66237 1.47020 -0.29062 0.13832  -0.15230 3   ASP D CA  
4981 C C   . ASP D 3   ? 1.67430 1.58624 1.44922 -0.27370 0.14622  -0.13375 3   ASP D C   
4982 O O   . ASP D 3   ? 1.70005 1.56556 1.45755 -0.28415 0.16685  -0.14009 3   ASP D O   
4983 C CB  . ASP D 3   ? 1.62960 1.65430 1.43300 -0.28066 0.11627  -0.14729 3   ASP D CB  
4984 C CG  . ASP D 3   ? 1.61909 1.70860 1.42651 -0.29019 0.10519  -0.16249 3   ASP D CG  
4985 O OD1 . ASP D 3   ? 1.61869 1.71512 1.41367 -0.29483 0.10765  -0.16863 3   ASP D OD1 
4986 O OD2 . ASP D 3   ? 1.58966 1.72505 1.41241 -0.29175 0.09376  -0.16825 3   ASP D OD2 
4987 N N   . PHE D 4   ? 1.53653 1.45009 1.32637 -0.24689 0.13083  -0.11111 4   PHE D N   
4988 C CA  . PHE D 4   ? 1.46422 1.33634 1.25663 -0.22936 0.13398  -0.09435 4   PHE D CA  
4989 C C   . PHE D 4   ? 1.36961 1.26794 1.18701 -0.20669 0.11240  -0.07582 4   PHE D C   
4990 O O   . PHE D 4   ? 1.35453 1.29573 1.18356 -0.20242 0.09696  -0.07398 4   PHE D O   
4991 C CB  . PHE D 4   ? 1.44017 1.26424 1.21488 -0.22101 0.14771  -0.08731 4   PHE D CB  
4992 C CG  . PHE D 4   ? 1.40394 1.24099 1.18412 -0.20622 0.13727  -0.07604 4   PHE D CG  
4993 C CD1 . PHE D 4   ? 1.48013 1.33130 1.24904 -0.21740 0.14002  -0.08630 4   PHE D CD1 
4994 C CD2 . PHE D 4   ? 1.31899 1.15292 1.11442 -0.18204 0.12623  -0.05617 4   PHE D CD2 
4995 C CE1 . PHE D 4   ? 1.41108 1.27152 1.18323 -0.20360 0.13175  -0.07554 4   PHE D CE1 
4996 C CE2 . PHE D 4   ? 1.33507 1.17851 1.13459 -0.16985 0.11888  -0.04658 4   PHE D CE2 
4997 C CZ  . PHE D 4   ? 1.34637 1.20190 1.13376 -0.18007 0.12171  -0.05557 4   PHE D CZ  
4998 N N   . ILE D 5   ? 1.35509 1.22694 1.17910 -0.19195 0.11242  -0.06262 5   ILE D N   
4999 C CA  . ILE D 5   ? 1.27637 1.16501 1.12255 -0.17062 0.09503  -0.04505 5   ILE D CA  
5000 C C   . ILE D 5   ? 1.27061 1.12066 1.11602 -0.15288 0.09992  -0.03098 5   ILE D C   
5001 O O   . ILE D 5   ? 1.31447 1.12572 1.14365 -0.15549 0.11563  -0.03404 5   ILE D O   
5002 C CB  . ILE D 5   ? 1.21170 1.12600 1.07358 -0.17250 0.08546  -0.04648 5   ILE D CB  
5003 C CG1 . ILE D 5   ? 1.17710 1.11400 1.06044 -0.15224 0.06742  -0.03002 5   ILE D CG1 
5004 C CG2 . ILE D 5   ? 1.35659 1.23677 1.21293 -0.17488 0.09676  -0.04760 5   ILE D CG2 
5005 C CD1 . ILE D 5   ? 1.20006 1.16869 1.09823 -0.15349 0.05678  -0.03184 5   ILE D CD1 
5006 N N   . ILE D 6   ? 1.16693 1.02804 1.02858 -0.13425 0.08743  -0.01599 6   ILE D N   
5007 C CA  . ILE D 6   ? 1.10852 0.94287 0.97293 -0.11669 0.09008  -0.00380 6   ILE D CA  
5008 C C   . ILE D 6   ? 1.11938 0.97180 1.00719 -0.10221 0.07562  0.00815  6   ILE D C   
5009 O O   . ILE D 6   ? 1.09361 0.97745 0.99425 -0.10271 0.06339  0.00977  6   ILE D O   
5010 C CB  . ILE D 6   ? 1.14347 0.96808 1.00142 -0.10984 0.09393  0.00049  6   ILE D CB  
5011 C CG1 . ILE D 6   ? 1.14069 0.99708 1.01265 -0.10412 0.08032  0.00723  6   ILE D CG1 
5012 C CG2 . ILE D 6   ? 1.19311 1.00043 1.02695 -0.12495 0.10862  -0.01197 6   ILE D CG2 
5013 C CD1 . ILE D 6   ? 1.13993 0.98676 1.00742 -0.09647 0.08421  0.01241  6   ILE D CD1 
5014 N N   . ASP D 7   ? 1.10287 0.93507 0.99479 -0.08851 0.07792  0.01606  7   ASP D N   
5015 C CA  . ASP D 7   ? 1.02424 0.87050 0.93782 -0.07442 0.06619  0.02676  7   ASP D CA  
5016 C C   . ASP D 7   ? 1.02448 0.85112 0.93874 -0.05911 0.07104  0.03348  7   ASP D C   
5017 O O   . ASP D 7   ? 1.04620 0.84684 0.94742 -0.05573 0.08112  0.03174  7   ASP D O   
5018 C CB  . ASP D 7   ? 1.07389 0.92708 0.99579 -0.07636 0.06117  0.02588  7   ASP D CB  
5019 C CG  . ASP D 7   ? 1.15284 1.02573 1.09748 -0.06474 0.04820  0.03547  7   ASP D CG  
5020 O OD1 . ASP D 7   ? 1.18746 1.06743 1.14066 -0.05634 0.04431  0.04214  7   ASP D OD1 
5021 O OD2 . ASP D 7   ? 1.12421 1.00440 1.07745 -0.06481 0.04310  0.03575  7   ASP D OD2 
5022 N N   . PHE D 8   ? 1.00090 0.83992 0.92853 -0.04962 0.06519  0.04051  8   PHE D N   
5023 C CA  . PHE D 8   ? 0.94078 0.77145 0.87438 -0.03462 0.06764  0.04581  8   PHE D CA  
5024 C C   . PHE D 8   ? 0.91590 0.76209 0.87055 -0.02637 0.05786  0.05112  8   PHE D C   
5025 O O   . PHE D 8   ? 0.94113 0.80634 0.90811 -0.03035 0.04884  0.05325  8   PHE D O   
5026 C CB  . PHE D 8   ? 0.91592 0.75200 0.85269 -0.03067 0.06893  0.04847  8   PHE D CB  
5027 C CG  . PHE D 8   ? 0.91433 0.73359 0.83069 -0.03609 0.07959  0.04373  8   PHE D CG  
5028 C CD1 . PHE D 8   ? 0.93436 0.73050 0.83773 -0.02784 0.09060  0.04271  8   PHE D CD1 
5029 C CD2 . PHE D 8   ? 0.93987 0.76721 0.84891 -0.04806 0.07892  0.04035  8   PHE D CD2 
5030 C CE1 . PHE D 8   ? 0.96824 0.74615 0.85123 -0.03296 0.10188  0.03810  8   PHE D CE1 
5031 C CE2 . PHE D 8   ? 0.93559 0.74769 0.82526 -0.05415 0.08927  0.03493  8   PHE D CE2 
5032 C CZ  . PHE D 8   ? 0.93503 0.72105 0.81177 -0.04730 0.10118  0.03374  8   PHE D CZ  
5033 N N   . GLU D 9   ? 0.86916 0.70780 0.82677 -0.01380 0.06012  0.05309  9   GLU D N   
5034 C CA  . GLU D 9   ? 0.86471 0.72103 0.84396 -0.00474 0.05190  0.05714  9   GLU D CA  
5035 C C   . GLU D 9   ? 0.83784 0.70026 0.82456 0.00504  0.05455  0.05831  9   GLU D C   
5036 O O   . GLU D 9   ? 0.79468 0.64313 0.76836 0.01161  0.06304  0.05691  9   GLU D O   
5037 C CB  . GLU D 9   ? 0.86910 0.71928 0.84819 0.00243  0.05099  0.05735  9   GLU D CB  
5038 C CG  . GLU D 9   ? 0.91959 0.76902 0.89592 -0.00854 0.04750  0.05566  9   GLU D CG  
5039 C CD  . GLU D 9   ? 1.03018 0.87016 1.00351 -0.00209 0.04814  0.05582  9   GLU D CD  
5040 O OE1 . GLU D 9   ? 1.02404 0.85450 0.99239 0.01194  0.05255  0.05729  9   GLU D OE1 
5041 O OE2 . GLU D 9   ? 1.09039 0.93379 1.06579 -0.00997 0.04430  0.05450  9   GLU D OE2 
5042 N N   . THR D 10  ? 0.79342 0.67595 0.79984 0.00522  0.04871  0.06027  10  THR D N   
5043 C CA  . THR D 10  ? 0.78517 0.67630 0.79960 0.01024  0.05226  0.05972  10  THR D CA  
5044 C C   . THR D 10  ? 0.76686 0.67819 0.80338 0.01728  0.04807  0.05882  10  THR D C   
5045 O O   . THR D 10  ? 0.72511 0.64363 0.77136 0.01693  0.04167  0.05957  10  THR D O   
5046 C CB  . THR D 10  ? 0.77535 0.66936 0.78918 0.00085  0.05329  0.06124  10  THR D CB  
5047 O OG1 . THR D 10  ? 0.76649 0.67069 0.79066 -0.00482 0.04651  0.06430  10  THR D OG1 
5048 C CG2 . THR D 10  ? 0.80307 0.68103 0.79501 -0.00649 0.05769  0.06017  10  THR D CG2 
5049 N N   . MET D 11  ? 0.75901 0.68063 0.80301 0.02339  0.05249  0.05597  11  MET D N   
5050 C CA  . MET D 11  ? 0.73022 0.67601 0.79688 0.02686  0.05066  0.05222  11  MET D CA  
5051 C C   . MET D 11  ? 0.75043 0.70378 0.82670 0.01770  0.05450  0.05135  11  MET D C   
5052 O O   . MET D 11  ? 0.72554 0.69882 0.82003 0.01829  0.05626  0.04600  11  MET D O   
5053 C CB  . MET D 11  ? 0.71535 0.67266 0.78447 0.04197  0.05346  0.04765  11  MET D CB  
5054 C CG  . MET D 11  ? 0.78001 0.73400 0.84317 0.05313  0.04963  0.04846  11  MET D CG  
5055 S SD  . MET D 11  ? 0.87100 0.84601 0.95645 0.04987  0.04051  0.04634  11  MET D SD  
5056 C CE  . MET D 11  ? 0.76795 0.77983 0.87567 0.05838  0.04180  0.03686  11  MET D CE  
5057 N N   . GLY D 12  ? 0.76530 0.70373 0.82870 0.00917  0.05682  0.05567  12  GLY D N   
5058 C CA  . GLY D 12  ? 0.75857 0.69934 0.82616 0.00174  0.06216  0.05608  12  GLY D CA  
5059 C C   . GLY D 12  ? 0.80551 0.73299 0.86006 -0.00619 0.06054  0.06260  12  GLY D C   
5060 O O   . GLY D 12  ? 0.78645 0.70637 0.83053 -0.00709 0.05500  0.06536  12  GLY D O   
5061 N N   . SER D 13  ? 1.10044 1.02605 1.15442 -0.01150 0.06634  0.06449  13  SER D N   
5062 C CA  . SER D 13  ? 1.10416 1.02038 1.14583 -0.01634 0.06552  0.07131  13  SER D CA  
5063 C C   . SER D 13  ? 1.11254 1.01906 1.13472 -0.01843 0.06896  0.07323  13  SER D C   
5064 O O   . SER D 13  ? 1.15388 1.05644 1.16201 -0.02023 0.06422  0.07669  13  SER D O   
5065 C CB  . SER D 13  ? 1.11343 1.02979 1.16330 -0.01969 0.07159  0.07322  13  SER D CB  
5066 O OG  . SER D 13  ? 1.12463 1.04133 1.17744 -0.02211 0.08205  0.06953  13  SER D OG  
5067 N N   . GLY D 14  ? 0.88947 0.79451 0.91067 -0.01845 0.07716  0.07013  14  GLY D N   
5068 C CA  . GLY D 14  ? 0.91823 0.81384 0.92115 -0.02121 0.08189  0.07222  14  GLY D CA  
5069 C C   . GLY D 14  ? 0.90482 0.79394 0.89312 -0.02096 0.08075  0.06932  14  GLY D C   
5070 O O   . GLY D 14  ? 0.90268 0.79120 0.89041 -0.01944 0.07549  0.06732  14  GLY D O   
5071 N N   . GLU D 15  ? 0.90575 0.78767 0.88035 -0.02311 0.08729  0.06873  15  GLU D N   
5072 C CA  . GLU D 15  ? 0.88699 0.75972 0.84691 -0.02356 0.08935  0.06453  15  GLU D CA  
5073 C C   . GLU D 15  ? 0.83974 0.71125 0.80663 -0.01638 0.09500  0.05990  15  GLU D C   
5074 O O   . GLU D 15  ? 0.86408 0.72382 0.81727 -0.01488 0.09899  0.05670  15  GLU D O   
5075 C CB  . GLU D 15  ? 0.88297 0.74843 0.82322 -0.02875 0.09421  0.06483  15  GLU D CB  
5076 C CG  . GLU D 15  ? 0.90756 0.76998 0.84765 -0.02740 0.10429  0.06419  15  GLU D CG  
5077 C CD  . GLU D 15  ? 0.93140 0.78721 0.85073 -0.03248 0.10844  0.06539  15  GLU D CD  
5078 O OE1 . GLU D 15  ? 0.92543 0.78210 0.83055 -0.03687 0.10305  0.06607  15  GLU D OE1 
5079 O OE2 . GLU D 15  ? 0.98692 0.83911 0.90436 -0.03201 0.11722  0.06499  15  GLU D OE2 
5080 N N   . LYS D 16  ? 0.82551 0.70949 0.81209 -0.01164 0.09644  0.05881  16  LYS D N   
5081 C CA  . LYS D 16  ? 0.80923 0.69950 0.80468 -0.00203 0.10007  0.05393  16  LYS D CA  
5082 C C   . LYS D 16  ? 0.78898 0.68916 0.79788 0.00442  0.09313  0.05289  16  LYS D C   
5083 O O   . LYS D 16  ? 0.76847 0.67970 0.78704 0.01469  0.09475  0.04882  16  LYS D O   
5084 C CB  . LYS D 16  ? 0.77651 0.67997 0.78551 -0.00127 0.10750  0.05060  16  LYS D CB  
5085 C CG  . LYS D 16  ? 0.73894 0.63234 0.73433 -0.00636 0.11577  0.05136  16  LYS D CG  
5086 C CD  . LYS D 16  ? 0.82095 0.69769 0.79502 -0.00339 0.11923  0.05057  16  LYS D CD  
5087 C CE  . LYS D 16  ? 0.85628 0.73635 0.83287 0.00937  0.12391  0.04592  16  LYS D CE  
5088 N NZ  . LYS D 16  ? 0.90873 0.76592 0.86016 0.01093  0.13007  0.04551  16  LYS D NZ  
5089 N N   . ALA D 17  ? 0.80668 0.70475 0.81556 -0.00033 0.08538  0.05629  17  ALA D N   
5090 C CA  . ALA D 17  ? 0.75486 0.66074 0.77486 0.00489  0.07856  0.05570  17  ALA D CA  
5091 C C   . ALA D 17  ? 0.76414 0.66187 0.77465 0.01545  0.08009  0.05358  17  ALA D C   
5092 O O   . ALA D 17  ? 0.74023 0.61832 0.72998 0.01424  0.08416  0.05394  17  ALA D O   
5093 C CB  . ALA D 17  ? 0.79358 0.69494 0.80988 -0.00243 0.07112  0.05991  17  ALA D CB  
5094 N N   . ALA D 18  ? 0.77698 0.68933 0.80115 0.02619  0.07780  0.05096  18  ALA D N   
5095 C CA  . ALA D 18  ? 0.76557 0.66861 0.77846 0.03920  0.07907  0.05050  18  ALA D CA  
5096 C C   . ALA D 18  ? 0.75479 0.63913 0.75418 0.03397  0.07549  0.05355  18  ALA D C   
5097 O O   . ALA D 18  ? 0.74942 0.64007 0.75796 0.02562  0.06816  0.05523  18  ALA D O   
5098 C CB  . ALA D 18  ? 0.73845 0.66555 0.76891 0.05266  0.07570  0.04709  18  ALA D CB  
5099 N N   . VAL D 19  ? 0.75693 0.61711 0.73338 0.03838  0.08211  0.05375  19  VAL D N   
5100 C CA  . VAL D 19  ? 0.79006 0.63014 0.75094 0.03116  0.08181  0.05465  19  VAL D CA  
5101 C C   . VAL D 19  ? 0.84328 0.67661 0.79931 0.04498  0.08230  0.05547  19  VAL D C   
5102 O O   . VAL D 19  ? 0.84215 0.66917 0.78920 0.06127  0.08894  0.05550  19  VAL D O   
5103 C CB  . VAL D 19  ? 0.84067 0.65449 0.77605 0.02272  0.09151  0.05274  19  VAL D CB  
5104 C CG1 . VAL D 19  ? 0.84086 0.66289 0.77953 0.00721  0.08826  0.05220  19  VAL D CG1 
5105 C CG2 . VAL D 19  ? 0.83887 0.64137 0.76221 0.03482  0.10224  0.05189  19  VAL D CG2 
5106 N N   . ILE D 20  ? 0.83284 0.66850 0.79417 0.04001  0.07540  0.05646  20  ILE D N   
5107 C CA  . ILE D 20  ? 0.86683 0.69347 0.82107 0.05169  0.07600  0.05765  20  ILE D CA  
5108 C C   . ILE D 20  ? 0.89045 0.68116 0.81526 0.04758  0.08657  0.05702  20  ILE D C   
5109 O O   . ILE D 20  ? 0.91924 0.68868 0.82460 0.06205  0.09593  0.05825  20  ILE D O   
5110 C CB  . ILE D 20  ? 0.86585 0.71154 0.83974 0.04771  0.06444  0.05849  20  ILE D CB  
5111 C CG1 . ILE D 20  ? 0.80462 0.68284 0.80617 0.04944  0.05660  0.05763  20  ILE D CG1 
5112 C CG2 . ILE D 20  ? 0.89564 0.73304 0.86179 0.06084  0.06512  0.05983  20  ILE D CG2 
5113 C CD1 . ILE D 20  ? 0.81173 0.70432 0.83039 0.04053  0.04701  0.05833  20  ILE D CD1 
5114 N N   . ASP D 21  ? 0.90347 0.68745 0.82355 0.02815  0.08624  0.05450  21  ASP D N   
5115 C CA  . ASP D 21  ? 0.97393 0.72535 0.86640 0.01910  0.09826  0.05090  21  ASP D CA  
5116 C C   . ASP D 21  ? 0.95566 0.71125 0.84670 -0.00226 0.09750  0.04599  21  ASP D C   
5117 O O   . ASP D 21  ? 0.93920 0.72163 0.84972 -0.00912 0.08639  0.04691  21  ASP D O   
5118 C CB  . ASP D 21  ? 0.95457 0.69192 0.83867 0.01876  0.09987  0.05070  21  ASP D CB  
5119 C CG  . ASP D 21  ? 1.02821 0.78903 0.93204 0.00574  0.08712  0.04975  21  ASP D CG  
5120 O OD1 . ASP D 21  ? 1.04717 0.83548 0.97187 0.00041  0.07629  0.05071  21  ASP D OD1 
5121 O OD2 . ASP D 21  ? 1.15275 0.90282 1.04947 0.00089  0.08908  0.04804  21  ASP D OD2 
5122 N N   . LEU D 22  ? 1.02831 0.75608 0.89391 -0.01211 0.11064  0.04033  22  LEU D N   
5123 C CA  . LEU D 22  ? 1.07464 0.80473 0.93363 -0.03327 0.11238  0.03292  22  LEU D CA  
5124 C C   . LEU D 22  ? 1.12319 0.83328 0.96473 -0.04690 0.12129  0.02548  22  LEU D C   
5125 O O   . LEU D 22  ? 1.10077 0.77652 0.92031 -0.04138 0.13554  0.02474  22  LEU D O   
5126 C CB  . LEU D 22  ? 1.02073 0.73689 0.86415 -0.03522 0.12270  0.03007  22  LEU D CB  
5127 C CG  . LEU D 22  ? 0.98724 0.70289 0.81855 -0.05700 0.12736  0.02038  22  LEU D CG  
5128 C CD1 . LEU D 22  ? 1.03410 0.78775 0.88632 -0.06639 0.11142  0.02025  22  LEU D CD1 
5129 C CD2 . LEU D 22  ? 1.00159 0.70365 0.81880 -0.05612 0.13713  0.01869  22  LEU D CD2 
5130 N N   . ALA D 23  ? 1.11047 0.84197 0.96044 -0.06426 0.11405  0.01959  23  ALA D N   
5131 C CA  . ALA D 23  ? 1.15607 0.87581 0.99276 -0.08092 0.12209  0.00993  23  ALA D CA  
5132 C C   . ALA D 23  ? 1.20125 0.93187 1.03049 -0.10255 0.12523  -0.00188 23  ALA D C   
5133 O O   . ALA D 23  ? 1.19923 0.96640 1.04530 -0.10962 0.11173  -0.00344 23  ALA D O   
5134 C CB  . ALA D 23  ? 1.20397 0.94564 1.05955 -0.08111 0.10983  0.01213  23  ALA D CB  
5135 N N   . VAL D 24  ? 1.26838 0.96763 1.07100 -0.11259 0.14369  -0.01068 24  VAL D N   
5136 C CA  . VAL D 24  ? 1.35814 1.06661 1.15090 -0.13542 0.14913  -0.02489 24  VAL D CA  
5137 C C   . VAL D 24  ? 1.51497 1.21177 1.29431 -0.15592 0.16118  -0.03887 24  VAL D C   
5138 O O   . VAL D 24  ? 1.55241 1.20686 1.31062 -0.15505 0.17865  -0.04020 24  VAL D O   
5139 C CB  . VAL D 24  ? 1.35596 1.03895 1.12804 -0.13568 0.16278  -0.02743 24  VAL D CB  
5140 C CG1 . VAL D 24  ? 1.39337 1.02295 1.13837 -0.12799 0.18392  -0.02623 24  VAL D CG1 
5141 C CG2 . VAL D 24  ? 1.35417 1.04939 1.11603 -0.16037 0.16831  -0.04368 24  VAL D CG2 
5142 N N   . ILE D 25  ? 1.61724 1.35209 1.40788 -0.17369 0.15268  -0.04957 25  ILE D N   
5143 C CA  . ILE D 25  ? 1.63141 1.36465 1.41257 -0.19692 0.16351  -0.06614 25  ILE D CA  
5144 C C   . ILE D 25  ? 1.62870 1.39110 1.40652 -0.22003 0.16461  -0.08363 25  ILE D C   
5145 O O   . ILE D 25  ? 1.60134 1.41323 1.39902 -0.22002 0.14614  -0.08369 25  ILE D O   
5146 C CB  . ILE D 25  ? 1.56938 1.32887 1.37137 -0.19500 0.15053  -0.06342 25  ILE D CB  
5147 C CG1 . ILE D 25  ? 1.52965 1.25811 1.33121 -0.17488 0.15225  -0.04909 25  ILE D CG1 
5148 C CG2 . ILE D 25  ? 1.59281 1.36189 1.38871 -0.22169 0.16006  -0.08307 25  ILE D CG2 
5149 C CD1 . ILE D 25  ? 1.51097 1.26602 1.33421 -0.17118 0.13825  -0.04512 25  ILE D CD1 
5150 N N   . ALA D 26  ? 1.66093 1.39277 1.41217 -0.23911 0.18699  -0.09880 26  ALA D N   
5151 C CA  . ALA D 26  ? 1.65747 1.41808 1.40397 -0.26515 0.19056  -0.11967 26  ALA D CA  
5152 C C   . ALA D 26  ? 1.67725 1.47464 1.43586 -0.28371 0.18638  -0.13420 26  ALA D C   
5153 O O   . ALA D 26  ? 1.69323 1.47423 1.45278 -0.28346 0.19117  -0.13260 26  ALA D O   
5154 C CB  . ALA D 26  ? 1.63263 1.34657 1.34590 -0.28271 0.21858  -0.13373 26  ALA D CB  
5155 N N   . PHE D 27  ? 1.68907 1.53915 1.45704 -0.29880 0.17704  -0.14859 27  PHE D N   
5156 C CA  . PHE D 27  ? 1.69525 1.58737 1.47565 -0.31667 0.17288  -0.16451 27  PHE D CA  
5157 C C   . PHE D 27  ? 1.77515 1.71587 1.55503 -0.33877 0.17137  -0.18679 27  PHE D C   
5158 O O   . PHE D 27  ? 1.76614 1.71838 1.54224 -0.33421 0.16610  -0.18504 27  PHE D O   
5159 C CB  . PHE D 27  ? 1.64139 1.56972 1.45025 -0.29616 0.14862  -0.14881 27  PHE D CB  
5160 C CG  . PHE D 27  ? 1.62880 1.60321 1.45461 -0.27931 0.12535  -0.13837 27  PHE D CG  
5161 C CD1 . PHE D 27  ? 1.61188 1.56647 1.43857 -0.25577 0.11834  -0.11781 27  PHE D CD1 
5162 C CD2 . PHE D 27  ? 1.60754 1.64573 1.44810 -0.28543 0.11084  -0.14867 27  PHE D CD2 
5163 C CE1 . PHE D 27  ? 1.57424 1.56671 1.41395 -0.24044 0.09925  -0.10785 27  PHE D CE1 
5164 C CE2 . PHE D 27  ? 1.59969 1.67662 1.45212 -0.26732 0.09083  -0.13759 27  PHE D CE2 
5165 C CZ  . PHE D 27  ? 1.56033 1.61188 1.41154 -0.24535 0.08579  -0.11693 27  PHE D CZ  
5166 N N   . ASP D 28  ? 1.81050 1.78243 1.59441 -0.36325 0.17626  -0.20895 28  ASP D N   
5167 C CA  . ASP D 28  ? 1.82526 1.84085 1.60505 -0.39010 0.18034  -0.23612 28  ASP D CA  
5168 C C   . ASP D 28  ? 1.77756 1.87117 1.58101 -0.37895 0.15242  -0.23479 28  ASP D C   
5169 O O   . ASP D 28  ? 1.71826 1.84622 1.54278 -0.36848 0.13674  -0.22865 28  ASP D O   
5170 C CB  . ASP D 28  ? 1.83613 1.85200 1.60881 -0.42347 0.20040  -0.26329 28  ASP D CB  
5171 C CG  . ASP D 28  ? 1.82543 1.87951 1.58999 -0.45530 0.20973  -0.29494 28  ASP D CG  
5172 O OD1 . ASP D 28  ? 1.86065 1.87737 1.60111 -0.46769 0.22833  -0.30302 28  ASP D OD1 
5173 O OD2 . ASP D 28  ? 1.81509 1.93835 1.59716 -0.46762 0.19867  -0.31243 28  ASP D OD2 
5174 N N   . PRO D 29  ? 1.75777 1.87946 1.55626 -0.38012 0.14670  -0.24046 29  PRO D N   
5175 C CA  . PRO D 29  ? 1.71587 1.90809 1.53264 -0.36447 0.12046  -0.23617 29  PRO D CA  
5176 C C   . PRO D 29  ? 1.68716 1.95063 1.51636 -0.38295 0.11454  -0.26095 29  PRO D C   
5177 O O   . PRO D 29  ? 1.68378 1.99876 1.53235 -0.36471 0.09280  -0.25267 29  PRO D O   
5178 C CB  . PRO D 29  ? 1.77962 1.97198 1.58215 -0.36205 0.12038  -0.23611 29  PRO D CB  
5179 C CG  . PRO D 29  ? 1.78505 1.93001 1.56315 -0.39034 0.14873  -0.25494 29  PRO D CG  
5180 C CD  . PRO D 29  ? 1.77681 1.86207 1.55071 -0.39215 0.16427  -0.24821 29  PRO D CD  
5181 N N   . ASN D 30  ? 1.68782 1.95627 1.50607 -0.41825 0.13404  -0.29152 30  ASN D N   
5182 C CA  . ASN D 30  ? 1.64189 1.98119 1.47269 -0.43937 0.13063  -0.31901 30  ASN D CA  
5183 C C   . ASN D 30  ? 1.68346 2.03217 1.53368 -0.43205 0.12376  -0.31218 30  ASN D C   
5184 O O   . ASN D 30  ? 1.68206 1.97300 1.52593 -0.43942 0.14047  -0.30870 30  ASN D O   
5185 C CB  . ASN D 30  ? 1.57197 1.89762 1.38422 -0.48161 0.15880  -0.35292 30  ASN D CB  
5186 C CG  . ASN D 30  ? 1.50051 1.90708 1.32439 -0.50796 0.15692  -0.38697 30  ASN D CG  
5187 O OD1 . ASN D 30  ? 1.47909 1.95306 1.32535 -0.49363 0.13446  -0.38510 30  ASN D OD1 
5188 N ND2 . ASN D 30  ? 1.42427 1.82569 1.23212 -0.54692 0.18156  -0.41945 30  ASN D ND2 
5189 N N   . PRO D 31  ? 1.66402 2.08323 1.53633 -0.41627 0.10012  -0.30967 31  PRO D N   
5190 C CA  . PRO D 31  ? 1.64790 2.06479 1.53838 -0.39609 0.08870  -0.29095 31  PRO D CA  
5191 C C   . PRO D 31  ? 1.67850 2.09554 1.57602 -0.41900 0.10168  -0.30824 31  PRO D C   
5192 O O   . PRO D 31  ? 1.70714 2.07641 1.60698 -0.40962 0.10568  -0.29175 31  PRO D O   
5193 C CB  . PRO D 31  ? 1.62600 2.11896 1.53384 -0.37110 0.06080  -0.28374 31  PRO D CB  
5194 C CG  . PRO D 31  ? 1.62579 2.17966 1.52869 -0.39056 0.06103  -0.31181 31  PRO D CG  
5195 C CD  . PRO D 31  ? 1.63768 2.13834 1.51706 -0.41088 0.08190  -0.32016 31  PRO D CD  
5196 N N   . GLU D 32  ? 1.65532 2.12660 1.55629 -0.44883 0.10855  -0.34164 32  GLU D N   
5197 C CA  . GLU D 32  ? 1.60898 2.10321 1.52319 -0.46656 0.11478  -0.35833 32  GLU D CA  
5198 C C   . GLU D 32  ? 1.58755 2.00045 1.48996 -0.47812 0.13805  -0.35344 32  GLU D C   
5199 O O   . GLU D 32  ? 1.52484 1.92254 1.43864 -0.46164 0.13153  -0.33621 32  GLU D O   
5200 C CB  . GLU D 32  ? 1.60807 2.16729 1.52429 -0.50318 0.12407  -0.39965 32  GLU D CB  
5201 C CG  . GLU D 32  ? 1.69167 2.20653 1.58269 -0.54050 0.15472  -0.42363 32  GLU D CG  
5202 C CD  . GLU D 32  ? 1.76693 2.35167 1.66172 -0.57550 0.16412  -0.46469 32  GLU D CD  
5203 O OE1 . GLU D 32  ? 1.77882 2.44815 1.69660 -0.56422 0.14579  -0.47030 32  GLU D OE1 
5204 O OE2 . GLU D 32  ? 1.78560 2.33376 1.66098 -0.60095 0.19358  -0.48046 32  GLU D OE2 
5205 N N   . THR D 36  ? 1.86864 1.83368 1.76729 -0.33560 0.16210  -0.17363 36  THR D N   
5206 C CA  . THR D 36  ? 1.78603 1.79711 1.70721 -0.31445 0.13465  -0.16092 36  THR D CA  
5207 C C   . THR D 36  ? 1.78402 1.76264 1.69389 -0.29643 0.13174  -0.14439 36  THR D C   
5208 O O   . THR D 36  ? 1.75038 1.75375 1.66144 -0.29937 0.12603  -0.14919 36  THR D O   
5209 C CB  . THR D 36  ? 1.75784 1.79302 1.70309 -0.29186 0.11412  -0.14470 36  THR D CB  
5210 O OG1 . THR D 36  ? 1.74730 1.81602 1.70975 -0.26933 0.09053  -0.13005 36  THR D OG1 
5211 C CG2 . THR D 36  ? 1.75345 1.73218 1.68836 -0.27755 0.12135  -0.12849 36  THR D CG2 
5212 N N   . PHE D 37  ? 1.81729 1.74229 1.71536 -0.27835 0.13654  -0.12631 37  PHE D N   
5213 C CA  . PHE D 37  ? 1.76909 1.66871 1.66175 -0.25616 0.13042  -0.10788 37  PHE D CA  
5214 C C   . PHE D 37  ? 1.77694 1.61593 1.63749 -0.26128 0.15378  -0.10946 37  PHE D C   
5215 O O   . PHE D 37  ? 1.74876 1.57848 1.60275 -0.25382 0.15237  -0.10392 37  PHE D O   
5216 C CB  . PHE D 37  ? 1.78707 1.67893 1.69298 -0.22834 0.11598  -0.08582 37  PHE D CB  
5217 C CG  . PHE D 37  ? 1.77402 1.64170 1.67650 -0.20508 0.11004  -0.06745 37  PHE D CG  
5218 C CD1 . PHE D 37  ? 1.67112 1.56749 1.58582 -0.19633 0.09516  -0.06177 37  PHE D CD1 
5219 C CD2 . PHE D 37  ? 1.80579 1.62471 1.69338 -0.19035 0.11891  -0.05561 37  PHE D CD2 
5220 C CE1 . PHE D 37  ? 1.64658 1.52282 1.55955 -0.17626 0.09051  -0.04615 37  PHE D CE1 
5221 C CE2 . PHE D 37  ? 1.77116 1.57408 1.65787 -0.16872 0.11292  -0.04016 37  PHE D CE2 
5222 C CZ  . PHE D 37  ? 1.70219 1.53383 1.60239 -0.16288 0.09907  -0.03601 37  PHE D CZ  
5223 N N   . ASP D 38  ? 1.85834 1.65458 1.69692 -0.27387 0.17670  -0.11725 38  ASP D N   
5224 C CA  . ASP D 38  ? 1.85175 1.57960 1.65779 -0.26728 0.19797  -0.11072 38  ASP D CA  
5225 C C   . ASP D 38  ? 1.84072 1.54720 1.62424 -0.28265 0.21500  -0.12238 38  ASP D C   
5226 O O   . ASP D 38  ? 1.86568 1.51799 1.62280 -0.27220 0.23016  -0.11430 38  ASP D O   
5227 C CB  . ASP D 38  ? 1.90239 1.58789 1.68797 -0.27574 0.21958  -0.11549 38  ASP D CB  
5228 N N   . GLU D 39  ? 1.76470 1.51250 1.55667 -0.30620 0.21346  -0.14141 39  GLU D N   
5229 C CA  . GLU D 39  ? 1.74316 1.46337 1.50874 -0.32681 0.23595  -0.15694 39  GLU D CA  
5230 C C   . GLU D 39  ? 1.75217 1.46772 1.51513 -0.31067 0.22794  -0.14560 39  GLU D C   
5231 O O   . GLU D 39  ? 1.79893 1.46191 1.53266 -0.31082 0.24819  -0.14516 39  GLU D O   
5232 C CB  . GLU D 39  ? 1.68173 1.44731 1.45456 -0.36144 0.24077  -0.18535 39  GLU D CB  
5233 C CG  . GLU D 39  ? 1.65426 1.49244 1.45417 -0.36246 0.21626  -0.19041 39  GLU D CG  
5234 C CD  . GLU D 39  ? 1.60534 1.49820 1.43945 -0.34431 0.18710  -0.17868 39  GLU D CD  
5235 O OE1 . GLU D 39  ? 1.67814 1.55031 1.51782 -0.32144 0.17956  -0.15878 39  GLU D OE1 
5236 O OE2 . GLU D 39  ? 1.49443 1.45192 1.34886 -0.35291 0.17254  -0.19028 39  GLU D OE2 
5237 N N   . LEU D 40  ? 1.71164 1.47822 1.50284 -0.29554 0.20006  -0.13573 40  LEU D N   
5238 C CA  . LEU D 40  ? 1.73360 1.49663 1.52293 -0.28046 0.19271  -0.12497 40  LEU D CA  
5239 C C   . LEU D 40  ? 1.71405 1.43672 1.49776 -0.25012 0.19065  -0.10143 40  LEU D C   
5240 O O   . LEU D 40  ? 1.65924 1.36069 1.43230 -0.23882 0.19327  -0.09372 40  LEU D O   
5241 C CB  . LEU D 40  ? 1.62719 1.45517 1.44543 -0.27423 0.16582  -0.12226 40  LEU D CB  
5242 C CG  . LEU D 40  ? 1.56150 1.43978 1.38609 -0.29968 0.16415  -0.14485 40  LEU D CG  
5243 C CD1 . LEU D 40  ? 1.45359 1.39198 1.30554 -0.28511 0.13626  -0.13664 40  LEU D CD1 
5244 C CD2 . LEU D 40  ? 1.59796 1.45577 1.39906 -0.31720 0.18188  -0.15881 40  LEU D CD2 
5245 N N   . VAL D 41  ? 1.71006 1.42573 1.50169 -0.23666 0.18550  -0.09076 41  VAL D N   
5246 C CA  . VAL D 41  ? 1.68671 1.37067 1.47471 -0.20745 0.18256  -0.06992 41  VAL D CA  
5247 C C   . VAL D 41  ? 1.70946 1.32872 1.46044 -0.20494 0.20871  -0.06945 41  VAL D C   
5248 O O   . VAL D 41  ? 1.67569 1.27055 1.41915 -0.18109 0.20820  -0.05454 41  VAL D O   
5249 C CB  . VAL D 41  ? 1.72615 1.41718 1.52795 -0.19763 0.17395  -0.06227 41  VAL D CB  
5250 C CG1 . VAL D 41  ? 1.69511 1.36468 1.49751 -0.16671 0.16742  -0.04178 41  VAL D CG1 
5251 C CG2 . VAL D 41  ? 1.71926 1.47169 1.55370 -0.20293 0.15188  -0.06536 41  VAL D CG2 
5252 N N   . SER D 42  ? 1.75330 1.34340 1.47962 -0.22899 0.23316  -0.08612 42  SER D N   
5253 C CA  . SER D 42  ? 1.78267 1.30670 1.46912 -0.22815 0.26157  -0.08692 42  SER D CA  
5254 C C   . SER D 42  ? 1.75994 1.27927 1.43691 -0.23098 0.26582  -0.09022 42  SER D C   
5255 O O   . SER D 42  ? 1.79410 1.26585 1.44504 -0.21614 0.28044  -0.08208 42  SER D O   
5256 C CB  . SER D 42  ? 1.84230 1.33517 1.50416 -0.25629 0.28892  -0.10568 42  SER D CB  
5257 O OG  . SER D 42  ? 1.82910 1.35920 1.50032 -0.28863 0.28986  -0.12814 42  SER D OG  
5258 N N   . ARG D 43  ? 1.75048 1.31993 1.44768 -0.24793 0.25284  -0.10153 43  ARG D N   
5259 C CA  . ARG D 43  ? 1.77209 1.33398 1.45450 -0.26064 0.26331  -0.11174 43  ARG D CA  
5260 C C   . ARG D 43  ? 1.81718 1.36730 1.49860 -0.23365 0.25572  -0.09411 43  ARG D C   
5261 O O   . ARG D 43  ? 1.84122 1.35036 1.49521 -0.23420 0.27472  -0.09630 43  ARG D O   
5262 C CB  . ARG D 43  ? 1.72977 1.35378 1.43431 -0.28396 0.24995  -0.12852 43  ARG D CB  
5263 C CG  . ARG D 43  ? 1.75787 1.39440 1.46242 -0.31172 0.25981  -0.14829 43  ARG D CG  
5264 C CD  . ARG D 43  ? 1.81273 1.50642 1.53131 -0.33918 0.25363  -0.17060 43  ARG D CD  
5265 N NE  . ARG D 43  ? 1.84811 1.55158 1.56605 -0.36567 0.26549  -0.19041 43  ARG D NE  
5266 C CZ  . ARG D 43  ? 1.84195 1.59021 1.56696 -0.39555 0.26747  -0.21577 43  ARG D CZ  
5267 N NH1 . ARG D 43  ? 1.84317 1.62782 1.57307 -0.40386 0.25995  -0.22541 43  ARG D NH1 
5268 N NH2 . ARG D 43  ? 1.83496 1.59273 1.56138 -0.41796 0.27807  -0.23290 43  ARG D NH2 
5269 N N   . GLY D 44  ? 1.78950 1.37336 1.49955 -0.21014 0.22974  -0.07714 44  GLY D N   
5270 C CA  . GLY D 44  ? 1.74510 1.33119 1.46075 -0.18802 0.21968  -0.06307 44  GLY D CA  
5271 C C   . GLY D 44  ? 1.73348 1.28286 1.43902 -0.15815 0.22341  -0.04529 44  GLY D C   
5272 O O   . GLY D 44  ? 1.74359 1.26446 1.43690 -0.15193 0.23288  -0.04196 44  GLY D O   
5273 N N   . ILE D 45  ? 1.56978 1.12280 1.28053 -0.13888 0.21570  -0.03420 45  ILE D N   
5274 C CA  . ILE D 45  ? 1.49397 1.01867 1.19540 -0.10907 0.21888  -0.01873 45  ILE D CA  
5275 C C   . ILE D 45  ? 1.38970 0.95663 1.12419 -0.08952 0.19362  -0.00580 45  ILE D C   
5276 O O   . ILE D 45  ? 1.35630 0.96641 1.11599 -0.09852 0.17652  -0.00793 45  ILE D O   
5277 C CB  . ILE D 45  ? 1.46003 0.93765 1.12778 -0.10410 0.24134  -0.01972 45  ILE D CB  
5278 C CG1 . ILE D 45  ? 1.53294 1.03243 1.20957 -0.10809 0.23462  -0.02190 45  ILE D CG1 
5279 C CG2 . ILE D 45  ? 1.52327 0.95884 1.15799 -0.12744 0.26814  -0.03465 45  ILE D CG2 
5280 C CD1 . ILE D 45  ? 1.45931 0.96749 1.14696 -0.07970 0.22424  -0.00709 45  ILE D CD1 
5281 N N   . LYS D 46  ? 1.36605 0.92044 1.09917 -0.06210 0.19231  0.00723  46  LYS D N   
5282 C CA  . LYS D 46  ? 1.25879 0.85094 1.02233 -0.04383 0.17096  0.01813  46  LYS D CA  
5283 C C   . LYS D 46  ? 1.26034 0.83463 1.01315 -0.01830 0.17682  0.02703  46  LYS D C   
5284 O O   . LYS D 46  ? 1.24531 0.79056 0.97942 -0.00037 0.18697  0.03255  46  LYS D O   
5285 C CB  . LYS D 46  ? 1.08434 0.69740 0.86816 -0.03663 0.15710  0.02365  46  LYS D CB  
5286 N N   . ILE D 47  ? 1.25284 0.84621 1.01708 -0.01538 0.17047  0.02851  47  ILE D N   
5287 C CA  . ILE D 47  ? 1.17599 0.76221 0.93540 0.00873  0.17375  0.03603  47  ILE D CA  
5288 C C   . ILE D 47  ? 1.08564 0.70893 0.87525 0.02636  0.15520  0.04423  47  ILE D C   
5289 O O   . ILE D 47  ? 1.05372 0.71217 0.87109 0.01680  0.13880  0.04389  47  ILE D O   
5290 C CB  . ILE D 47  ? 1.15757 0.74798 0.91578 0.00235  0.17641  0.03278  47  ILE D CB  
5291 C CG1 . ILE D 47  ? 1.21898 0.77873 0.95014 -0.01962 0.19363  0.02204  47  ILE D CG1 
5292 C CG2 . ILE D 47  ? 1.18423 0.76505 0.93474 0.02768  0.18226  0.03954  47  ILE D CG2 
5293 C CD1 . ILE D 47  ? 1.19787 0.78666 0.94422 -0.04627 0.18382  0.01317  47  ILE D CD1 
5294 N N   . LYS D 48  ? 1.10162 0.71832 0.88529 0.05246  0.15830  0.05099  48  LYS D N   
5295 C CA  . LYS D 48  ? 1.08115 0.73551 0.89319 0.06866  0.14199  0.05649  48  LYS D CA  
5296 C C   . LYS D 48  ? 1.08664 0.75109 0.90110 0.08817  0.14339  0.05941  48  LYS D C   
5297 O O   . LYS D 48  ? 1.12108 0.75458 0.90783 0.10148  0.15884  0.06086  48  LYS D O   
5298 C CB  . LYS D 48  ? 1.01644 0.66319 0.82280 0.08286  0.14154  0.06065  48  LYS D CB  
5299 C CG  . LYS D 48  ? 1.02801 0.71680 0.86487 0.09668  0.12427  0.06421  48  LYS D CG  
5300 C CD  . LYS D 48  ? 1.09121 0.77514 0.92447 0.10487  0.12202  0.06704  48  LYS D CD  
5301 C CE  . LYS D 48  ? 1.02225 0.74989 0.88649 0.11613  0.10499  0.06874  48  LYS D CE  
5302 N NZ  . LYS D 48  ? 1.05780 0.79805 0.92038 0.14353  0.10605  0.07136  48  LYS D NZ  
5303 N N   . PHE D 49  ? 1.02198 0.72895 0.86870 0.08951  0.12857  0.05971  49  PHE D N   
5304 C CA  . PHE D 49  ? 1.05056 0.77410 0.90498 0.10136  0.12908  0.05995  49  PHE D CA  
5305 C C   . PHE D 49  ? 1.04640 0.79995 0.91709 0.12526  0.12165  0.06231  49  PHE D C   
5306 O O   . PHE D 49  ? 1.07510 0.85380 0.96679 0.12479  0.10955  0.06239  49  PHE D O   
5307 C CB  . PHE D 49  ? 0.97390 0.72335 0.85153 0.08296  0.12052  0.05680  49  PHE D CB  
5308 C CG  . PHE D 49  ? 0.96701 0.69584 0.83085 0.06058  0.12613  0.05337  49  PHE D CG  
5309 C CD1 . PHE D 49  ? 0.98869 0.69010 0.82826 0.05966  0.14032  0.05130  49  PHE D CD1 
5310 C CD2 . PHE D 49  ? 0.94936 0.68865 0.82442 0.04091  0.11725  0.05149  49  PHE D CD2 
5311 C CE1 . PHE D 49  ? 1.02151 0.70767 0.84874 0.03804  0.14538  0.04629  49  PHE D CE1 
5312 C CE2 . PHE D 49  ? 0.94956 0.67622 0.81254 0.02106  0.12160  0.04689  49  PHE D CE2 
5313 C CZ  . PHE D 49  ? 0.96589 0.66663 0.80514 0.01884  0.13564  0.04370  49  PHE D CZ  
5314 N N   . ASP D 50  ? 1.05138 0.80527 0.91312 0.14589  0.12889  0.06327  50  ASP D N   
5315 C CA  . ASP D 50  ? 1.05508 0.84610 0.93427 0.16896  0.12182  0.06323  50  ASP D CA  
5316 C C   . ASP D 50  ? 1.04377 0.88099 0.96142 0.15663  0.10895  0.05802  50  ASP D C   
5317 O O   . ASP D 50  ? 1.08430 0.92994 1.00849 0.15123  0.11171  0.05530  50  ASP D O   
5318 C CB  . ASP D 50  ? 1.08946 0.86821 0.94666 0.19416  0.13434  0.06517  50  ASP D CB  
5319 C CG  . ASP D 50  ? 1.12949 0.95443 1.00602 0.21884  0.12734  0.06308  50  ASP D CG  
5320 O OD1 . ASP D 50  ? 1.16439 1.03291 1.07386 0.21359  0.11337  0.05853  50  ASP D OD1 
5321 O OD2 . ASP D 50  ? 1.17708 0.99576 1.03495 0.24430  0.13677  0.06522  50  ASP D OD2 
5322 N N   . LEU D 51  ? 1.05726 0.92300 0.99910 0.15255  0.09632  0.05634  51  LEU D N   
5323 C CA  . LEU D 51  ? 1.04503 0.95119 1.02141 0.14065  0.08659  0.05083  51  LEU D CA  
5324 C C   . LEU D 51  ? 1.05111 0.99050 1.04072 0.15606  0.08782  0.04570  51  LEU D C   
5325 O O   . LEU D 51  ? 1.04433 1.00429 1.05318 0.14419  0.08684  0.04092  51  LEU D O   
5326 C CB  . LEU D 51  ? 0.96672 0.89626 0.96460 0.13580  0.07467  0.04919  51  LEU D CB  
5327 C CG  . LEU D 51  ? 0.88541 0.79796 0.88364 0.11503  0.07002  0.05194  51  LEU D CG  
5328 C CD1 . LEU D 51  ? 0.86963 0.81127 0.89274 0.11208  0.05896  0.04916  51  LEU D CD1 
5329 C CD2 . LEU D 51  ? 0.92663 0.83207 0.92819 0.09401  0.07157  0.05165  51  LEU D CD2 
5330 N N   . LYS D 52  ? 1.17194 1.11990 1.15214 0.18310  0.08993  0.04613  52  LYS D N   
5331 C CA  . LYS D 52  ? 1.13874 1.12871 1.13543 0.19932  0.08929  0.03943  52  LYS D CA  
5332 C C   . LYS D 52  ? 1.15632 1.13504 1.14305 0.20020  0.09968  0.03919  52  LYS D C   
5333 O O   . LYS D 52  ? 1.13890 1.15210 1.14773 0.19759  0.09890  0.03180  52  LYS D O   
5334 C CB  . LYS D 52  ? 1.17065 1.17472 1.15716 0.23132  0.08850  0.04043  52  LYS D CB  
5335 C CG  . LYS D 52  ? 1.19351 1.22787 1.19996 0.23133  0.07633  0.03679  52  LYS D CG  
5336 C CD  . LYS D 52  ? 1.19699 1.19236 1.18582 0.22364  0.07531  0.04463  52  LYS D CD  
5337 C CE  . LYS D 52  ? 1.22850 1.25483 1.23662 0.22523  0.06338  0.04088  52  LYS D CE  
5338 N NZ  . LYS D 52  ? 1.17403 1.23467 1.21902 0.20104  0.05470  0.03211  52  LYS D NZ  
5339 N N   . SER D 53  ? 1.11568 1.04566 1.06902 0.20224  0.11061  0.04629  53  SER D N   
5340 C CA  . SER D 53  ? 1.13246 1.04833 1.07410 0.20232  0.12140  0.04602  53  SER D CA  
5341 C C   . SER D 53  ? 1.08281 1.00848 1.04480 0.17444  0.11868  0.04184  53  SER D C   
5342 O O   . SER D 53  ? 1.13818 1.07565 1.10569 0.17464  0.12381  0.03819  53  SER D O   
5343 C CB  . SER D 53  ? 1.10108 0.95906 1.00161 0.20601  0.13507  0.05319  53  SER D CB  
5344 O OG  . SER D 53  ? 1.04301 0.87036 0.93612 0.17966  0.13498  0.05504  53  SER D OG  
5345 N N   . GLN D 54  ? 1.04059 0.96277 1.01341 0.15198  0.11100  0.04246  54  GLN D N   
5346 C CA  . GLN D 54  ? 1.01694 0.94378 1.00444 0.12719  0.10898  0.04021  54  GLN D CA  
5347 C C   . GLN D 54  ? 1.08070 1.05305 1.10203 0.12288  0.10338  0.03267  54  GLN D C   
5348 O O   . GLN D 54  ? 1.05149 1.02710 1.08408 0.10370  0.10341  0.03102  54  GLN D O   
5349 C CB  . GLN D 54  ? 0.90591 0.81370 0.89088 0.10769  0.10322  0.04391  54  GLN D CB  
5350 C CG  . GLN D 54  ? 0.92380 0.79036 0.87844 0.10816  0.10868  0.04897  54  GLN D CG  
5351 C CD  . GLN D 54  ? 0.93435 0.79026 0.89037 0.08780  0.10229  0.05081  54  GLN D CD  
5352 O OE1 . GLN D 54  ? 0.92858 0.80235 0.90390 0.07345  0.09548  0.04964  54  GLN D OE1 
5353 N NE2 . GLN D 54  ? 0.95666 0.78512 0.89266 0.08788  0.10482  0.05349  54  GLN D NE2 
5354 N N   . LYS D 55  ? 1.24629 1.25385 1.28314 0.13951  0.09931  0.02744  55  LYS D N   
5355 C CA  . LYS D 55  ? 1.22992 1.28293 1.29922 0.13351  0.09617  0.01742  55  LYS D CA  
5356 C C   . LYS D 55  ? 1.24763 1.30772 1.32023 0.12989  0.10502  0.01321  55  LYS D C   
5357 O O   . LYS D 55  ? 1.26835 1.31793 1.32353 0.14530  0.11232  0.01508  55  LYS D O   
5358 C CB  . LYS D 55  ? 1.21375 1.30792 1.29736 0.15415  0.09090  0.01062  55  LYS D CB  
5359 C CG  . LYS D 55  ? 1.20697 1.30427 1.29508 0.15456  0.08127  0.01218  55  LYS D CG  
5360 C CD  . LYS D 55  ? 1.24337 1.38512 1.34402 0.17717  0.07613  0.00464  55  LYS D CD  
5361 C CE  . LYS D 55  ? 1.21949 1.36888 1.32804 0.17522  0.06636  0.00458  55  LYS D CE  
5362 N NZ  . LYS D 55  ? 1.20410 1.30689 1.28342 0.18050  0.06620  0.01709  55  LYS D NZ  
5363 N N   . GLY D 56  ? 1.08810 1.16358 1.18146 0.10958  0.10566  0.00768  56  GLY D N   
5364 C CA  . GLY D 56  ? 1.08472 1.16431 1.18146 0.10222  0.11480  0.00378  56  GLY D CA  
5365 C C   . GLY D 56  ? 1.07921 1.11556 1.15354 0.08881  0.11980  0.01246  56  GLY D C   
5366 O O   . GLY D 56  ? 1.08162 1.11581 1.16154 0.07219  0.12454  0.01106  56  GLY D O   
5367 N N   . HIS D 57  ? 1.07376 1.07543 1.12145 0.09561  0.11950  0.02087  57  HIS D N   
5368 C CA  . HIS D 57  ? 1.01486 0.97830 1.03938 0.08404  0.12446  0.02729  57  HIS D CA  
5369 C C   . HIS D 57  ? 0.97801 0.92760 1.00317 0.06428  0.11831  0.03166  57  HIS D C   
5370 O O   . HIS D 57  ? 0.97326 0.90870 0.99136 0.05016  0.12165  0.03386  57  HIS D O   
5371 C CB  . HIS D 57  ? 1.11155 1.04375 1.10666 0.09789  0.12883  0.03237  57  HIS D CB  
5372 C CG  . HIS D 57  ? 1.21136 1.15393 1.20152 0.12111  0.13573  0.02962  57  HIS D CG  
5373 N ND1 . HIS D 57  ? 1.20477 1.16779 1.20023 0.14263  0.13219  0.02810  57  HIS D ND1 
5374 C CD2 . HIS D 57  ? 1.24695 1.18423 1.22690 0.12781  0.14598  0.02814  57  HIS D CD2 
5375 C CE1 . HIS D 57  ? 1.28794 1.25845 1.27599 0.16300  0.13988  0.02614  57  HIS D CE1 
5376 N NE2 . HIS D 57  ? 1.31866 1.27310 1.29761 0.15407  0.14856  0.02608  57  HIS D NE2 
5377 N N   . ARG D 58  ? 0.98837 0.94224 1.02051 0.06433  0.10947  0.03320  58  ARG D N   
5378 C CA  . ARG D 58  ? 0.88079 0.82199 0.91205 0.04841  0.10336  0.03778  58  ARG D CA  
5379 C C   . ARG D 58  ? 0.80341 0.76976 0.85983 0.04403  0.09649  0.03475  58  ARG D C   
5380 O O   . ARG D 58  ? 0.83438 0.82743 0.90736 0.05391  0.09475  0.02877  58  ARG D O   
5381 C CB  . ARG D 58  ? 0.80195 0.71544 0.81143 0.04979  0.10077  0.04309  58  ARG D CB  
5382 C CG  . ARG D 58  ? 0.80587 0.69225 0.78963 0.04983  0.10956  0.04458  58  ARG D CG  
5383 C CD  . ARG D 58  ? 0.76687 0.62431 0.72779 0.04673  0.10998  0.04760  58  ARG D CD  
5384 N NE  . ARG D 58  ? 0.79982 0.65576 0.76316 0.03032  0.10290  0.04973  58  ARG D NE  
5385 C CZ  . ARG D 58  ? 0.80986 0.65954 0.76583 0.01688  0.10407  0.05039  58  ARG D CZ  
5386 N NH1 . ARG D 58  ? 0.79399 0.63761 0.74097 0.01584  0.11206  0.04896  58  ARG D NH1 
5387 N NH2 . ARG D 58  ? 0.84626 0.69750 0.80350 0.00539  0.09693  0.05254  58  ARG D NH2 
5388 N N   . LEU D 59  ? 0.80055 0.75876 0.85855 0.02944  0.09320  0.03848  59  LEU D N   
5389 C CA  . LEU D 59  ? 0.76422 0.73989 0.84330 0.02051  0.09115  0.03573  59  LEU D CA  
5390 C C   . LEU D 59  ? 0.74050 0.72017 0.82651 0.02192  0.08188  0.03708  59  LEU D C   
5391 O O   . LEU D 59  ? 0.71595 0.67660 0.78908 0.01830  0.07696  0.04364  59  LEU D O   
5392 C CB  . LEU D 59  ? 0.78774 0.74772 0.85954 0.00641  0.09460  0.04066  59  LEU D CB  
5393 C CG  . LEU D 59  ? 0.85088 0.81631 0.93593 -0.00379 0.09466  0.04072  59  LEU D CG  
5394 C CD1 . LEU D 59  ? 0.88136 0.86816 0.98611 -0.00758 0.10328  0.03142  59  LEU D CD1 
5395 C CD2 . LEU D 59  ? 0.82676 0.76995 0.89523 -0.01244 0.09565  0.04936  59  LEU D CD2 
5396 N N   . PHE D 60  ? 0.80938 0.81615 0.91641 0.02616  0.07970  0.02988  60  PHE D N   
5397 C CA  . PHE D 60  ? 0.80104 0.81401 0.91628 0.02738  0.07118  0.03020  60  PHE D CA  
5398 C C   . PHE D 60  ? 0.80637 0.82517 0.93661 0.01311  0.07239  0.02832  60  PHE D C   
5399 O O   . PHE D 60  ? 0.78928 0.83281 0.93975 0.01014  0.07545  0.01900  60  PHE D O   
5400 C CB  . PHE D 60  ? 0.71349 0.75295 0.84027 0.04210  0.06734  0.02328  60  PHE D CB  
5401 C CG  . PHE D 60  ? 0.77765 0.81095 0.88781 0.06019  0.06820  0.02519  60  PHE D CG  
5402 C CD1 . PHE D 60  ? 0.80722 0.82052 0.89920 0.06201  0.07494  0.02880  60  PHE D CD1 
5403 C CD2 . PHE D 60  ? 0.83465 0.87757 0.94376 0.07602  0.06285  0.02436  60  PHE D CD2 
5404 C CE1 . PHE D 60  ? 0.82638 0.82976 0.90049 0.07940  0.07777  0.03073  60  PHE D CE1 
5405 C CE2 . PHE D 60  ? 0.89144 0.92356 0.98107 0.09470  0.06558  0.02729  60  PHE D CE2 
5406 C CZ  . PHE D 60  ? 0.86490 0.87591 0.93675 0.09610  0.07358  0.03050  60  PHE D CZ  
5407 N N   . THR D 61  ? 0.90057 0.89675 1.01977 0.00451  0.07090  0.03659  61  THR D N   
5408 C CA  . THR D 61  ? 0.87670 0.87186 1.00495 -0.00656 0.07306  0.03691  61  THR D CA  
5409 C C   . THR D 61  ? 0.86943 0.87942 1.01276 -0.00491 0.06669  0.03283  61  THR D C   
5410 O O   . THR D 61  ? 0.86131 0.86687 0.99879 0.00172  0.05792  0.03679  61  THR D O   
5411 C CB  . THR D 61  ? 0.86510 0.83448 0.97497 -0.01172 0.07178  0.04772  61  THR D CB  
5412 O OG1 . THR D 61  ? 0.86774 0.82579 0.96531 -0.01510 0.07933  0.05030  61  THR D OG1 
5413 C CG2 . THR D 61  ? 0.87120 0.83585 0.98638 -0.01872 0.07250  0.05030  61  THR D CG2 
5414 N N   . LYS D 62  ? 0.83662 0.86369 0.99876 -0.01210 0.07220  0.02405  62  LYS D N   
5415 C CA  . LYS D 62  ? 0.81269 0.85722 0.99017 -0.01100 0.06668  0.01816  62  LYS D CA  
5416 C C   . LYS D 62  ? 0.79599 0.82151 0.96783 -0.01573 0.06280  0.02604  62  LYS D C   
5417 O O   . LYS D 62  ? 0.79095 0.82420 0.96863 -0.01163 0.05505  0.02497  62  LYS D O   
5418 C CB  . LYS D 62  ? 0.80594 0.87752 1.00597 -0.01902 0.07469  0.00369  62  LYS D CB  
5419 C CG  . LYS D 62  ? 0.86092 0.91769 1.06201 -0.03474 0.08697  0.00305  62  LYS D CG  
5420 C CD  . LYS D 62  ? 0.89817 0.98252 1.12240 -0.04524 0.09601  -0.01387 62  LYS D CD  
5421 C CE  . LYS D 62  ? 0.99328 1.08749 1.22885 -0.04734 0.09097  -0.01859 62  LYS D CE  
5422 N NZ  . LYS D 62  ? 1.01860 1.07799 1.24165 -0.05427 0.09425  -0.00797 62  LYS D NZ  
5423 N N   . SER D 63  ? 0.74279 0.74452 0.90248 -0.02281 0.06809  0.03408  63  SER D N   
5424 C CA  . SER D 63  ? 0.71756 0.70360 0.87014 -0.02363 0.06315  0.04231  63  SER D CA  
5425 C C   . SER D 63  ? 0.72835 0.70676 0.86734 -0.01532 0.05202  0.05004  63  SER D C   
5426 O O   . SER D 63  ? 0.75749 0.72711 0.89143 -0.01493 0.04650  0.05606  63  SER D O   
5427 C CB  . SER D 63  ? 0.78597 0.74936 0.92656 -0.03023 0.07186  0.04968  63  SER D CB  
5428 O OG  . SER D 63  ? 0.90743 0.85720 1.02905 -0.02690 0.07059  0.05807  63  SER D OG  
5429 N N   . THR D 64  ? 0.76367 0.74387 0.89540 -0.00931 0.05011  0.04963  64  THR D N   
5430 C CA  . THR D 64  ? 0.77924 0.75335 0.89951 -0.00225 0.04176  0.05364  64  THR D CA  
5431 C C   . THR D 64  ? 0.72346 0.71311 0.85343 0.00631  0.03677  0.04785  64  THR D C   
5432 O O   . THR D 64  ? 0.65965 0.64436 0.78442 0.01025  0.03010  0.05074  64  THR D O   
5433 C CB  . THR D 64  ? 0.72355 0.68649 0.82697 -0.00027 0.04443  0.05623  64  THR D CB  
5434 O OG1 . THR D 64  ? 0.79358 0.74419 0.88694 -0.00720 0.04827  0.06170  64  THR D OG1 
5435 C CG2 . THR D 64  ? 0.71391 0.66618 0.80275 0.00428  0.03882  0.05931  64  THR D CG2 
5436 N N   . ILE D 65  ? 0.66706 0.67722 0.81071 0.00963  0.04022  0.03925  65  ILE D N   
5437 C CA  . ILE D 65  ? 0.70164 0.73173 0.85531 0.01931  0.03520  0.03310  65  ILE D CA  
5438 C C   . ILE D 65  ? 0.72773 0.76357 0.89282 0.01471  0.03073  0.03171  65  ILE D C   
5439 O O   . ILE D 65  ? 0.70691 0.74616 0.87117 0.02226  0.02390  0.03209  65  ILE D O   
5440 C CB  . ILE D 65  ? 0.69774 0.75573 0.86590 0.02343  0.03979  0.02238  65  ILE D CB  
5441 C CG1 . ILE D 65  ? 0.71016 0.76139 0.86595 0.02943  0.04451  0.02420  65  ILE D CG1 
5442 C CG2 . ILE D 65  ? 0.60426 0.68753 0.78192 0.03575  0.03381  0.01564  65  ILE D CG2 
5443 C CD1 . ILE D 65  ? 0.66255 0.74348 0.83308 0.03327  0.04961  0.01334  65  ILE D CD1 
5444 N N   . GLU D 66  ? 0.73825 0.77377 0.91290 0.00270  0.03588  0.02983  66  GLU D N   
5445 C CA  . GLU D 66  ? 0.64549 0.68192 0.82861 -0.00220 0.03324  0.02914  66  GLU D CA  
5446 C C   . GLU D 66  ? 0.73052 0.74719 0.89958 0.00050  0.02591  0.03958  66  GLU D C   
5447 O O   . GLU D 66  ? 0.74624 0.76727 0.91928 0.00357  0.01969  0.03908  66  GLU D O   
5448 C CB  . GLU D 66  ? 0.57527 0.60583 0.76493 -0.01530 0.04317  0.02706  66  GLU D CB  
5449 N N   . TRP D 67  ? 0.69711 0.69432 0.84977 -0.00083 0.02666  0.04807  67  TRP D N   
5450 C CA  . TRP D 67  ? 0.67914 0.66214 0.81911 0.00049  0.02020  0.05600  67  TRP D CA  
5451 C C   . TRP D 67  ? 0.74807 0.73356 0.88383 0.00900  0.01389  0.05495  67  TRP D C   
5452 O O   . TRP D 67  ? 0.77449 0.75877 0.91087 0.01004  0.00841  0.05658  67  TRP D O   
5453 C CB  . TRP D 67  ? 0.63256 0.60051 0.75588 -0.00209 0.02236  0.06246  67  TRP D CB  
5454 C CG  . TRP D 67  ? 0.64698 0.60531 0.75860 -0.00292 0.01698  0.06872  67  TRP D CG  
5455 C CD1 . TRP D 67  ? 0.68281 0.63700 0.79250 -0.00577 0.01568  0.07407  67  TRP D CD1 
5456 C CD2 . TRP D 67  ? 0.69574 0.64824 0.79498 -0.00082 0.01307  0.06950  67  TRP D CD2 
5457 N NE1 . TRP D 67  ? 0.71974 0.67081 0.81835 -0.00563 0.00991  0.07745  67  TRP D NE1 
5458 C CE2 . TRP D 67  ? 0.68189 0.63103 0.77429 -0.00418 0.00884  0.07404  67  TRP D CE2 
5459 C CE3 . TRP D 67  ? 0.70761 0.65628 0.79924 0.00384  0.01418  0.06652  67  TRP D CE3 
5460 C CZ2 . TRP D 67  ? 0.66471 0.60921 0.74515 -0.00576 0.00592  0.07386  67  TRP D CZ2 
5461 C CZ3 . TRP D 67  ? 0.74194 0.68010 0.81907 0.00268  0.01264  0.06749  67  TRP D CZ3 
5462 C CH2 . TRP D 67  ? 0.73455 0.67178 0.80715 -0.00348 0.00864  0.07028  67  TRP D CH2 
5463 N N   . TRP D 68  ? 0.74112 0.72771 0.87035 0.01597  0.01573  0.05273  68  TRP D N   
5464 C CA  . TRP D 68  ? 0.74345 0.72722 0.86407 0.02595  0.01230  0.05264  68  TRP D CA  
5465 C C   . TRP D 68  ? 0.78777 0.78875 0.92181 0.03178  0.00772  0.04792  68  TRP D C   
5466 O O   . TRP D 68  ? 0.78779 0.78297 0.91475 0.03751  0.00379  0.04977  68  TRP D O   
5467 C CB  . TRP D 68  ? 0.74521 0.72680 0.85553 0.03524  0.01693  0.05102  68  TRP D CB  
5468 C CG  . TRP D 68  ? 0.80887 0.76866 0.90012 0.03099  0.02102  0.05557  68  TRP D CG  
5469 C CD1 . TRP D 68  ? 0.77748 0.73359 0.86509 0.02602  0.02631  0.05597  68  TRP D CD1 
5470 C CD2 . TRP D 68  ? 0.83201 0.77117 0.90480 0.02956  0.02097  0.05918  68  TRP D CD2 
5471 N NE1 . TRP D 68  ? 0.76516 0.70091 0.83315 0.02206  0.02880  0.05938  68  TRP D NE1 
5472 C CE2 . TRP D 68  ? 0.79003 0.71549 0.84903 0.02324  0.02605  0.06073  68  TRP D CE2 
5473 C CE3 . TRP D 68  ? 0.78492 0.71602 0.85111 0.03208  0.01811  0.06032  68  TRP D CE3 
5474 C CZ2 . TRP D 68  ? 0.79715 0.70322 0.83709 0.01813  0.02851  0.06197  68  TRP D CZ2 
5475 C CZ3 . TRP D 68  ? 0.81927 0.72955 0.86648 0.02685  0.02125  0.06200  68  TRP D CZ3 
5476 C CH2 . TRP D 68  ? 0.81124 0.71000 0.84583 0.01934  0.02654  0.06215  68  TRP D CH2 
5477 N N   . LYS D 69  ? 0.74249 0.76493 0.89521 0.02968  0.00907  0.04087  69  LYS D N   
5478 C CA  . LYS D 69  ? 0.80145 0.84459 0.96727 0.03508  0.00484  0.03435  69  LYS D CA  
5479 C C   . LYS D 69  ? 0.81574 0.85231 0.98513 0.02869  0.00060  0.03714  69  LYS D C   
5480 O O   . LYS D 69  ? 0.81088 0.85892 0.98603 0.03410  -0.00407 0.03367  69  LYS D O   
5481 C CB  . LYS D 69  ? 0.78399 0.85541 0.96957 0.03247  0.00867  0.02325  69  LYS D CB  
5482 C CG  . LYS D 69  ? 0.98082 1.07982 1.18004 0.03891  0.00396  0.01424  69  LYS D CG  
5483 C CD  . LYS D 69  ? 0.97921 1.08258 1.16589 0.05851  -0.00072 0.01590  69  LYS D CD  
5484 C CE  . LYS D 69  ? 0.91886 1.04865 1.11555 0.06699  -0.00652 0.00836  69  LYS D CE  
5485 N NZ  . LYS D 69  ? 0.90680 1.01973 1.10160 0.06005  -0.01040 0.01343  69  LYS D NZ  
5486 N N   . ASN D 70  ? 0.80846 0.82738 0.97297 0.01892  0.00206  0.04362  70  ASN D N   
5487 C CA  . ASN D 70  ? 0.83666 0.84740 1.00146 0.01455  -0.00169 0.04776  70  ASN D CA  
5488 C C   . ASN D 70  ? 0.86749 0.86115 1.01532 0.01664  -0.00540 0.05500  70  ASN D C   
5489 O O   . ASN D 70  ? 0.90975 0.89423 1.05378 0.01119  -0.00693 0.06016  70  ASN D O   
5490 C CB  . ASN D 70  ? 0.81626 0.82056 0.98566 0.00449  0.00311  0.05002  70  ASN D CB  
5491 C CG  . ASN D 70  ? 0.84834 0.86705 1.03456 -0.00084 0.00920  0.04105  70  ASN D CG  
5492 O OD1 . ASN D 70  ? 0.82174 0.85924 1.02029 0.00148  0.00715  0.03255  70  ASN D OD1 
5493 N ND2 . ASN D 70  ? 0.91181 0.92219 1.09772 -0.00850 0.01764  0.04209  70  ASN D ND2 
5494 N N   . GLN D 71  ? 0.83685 0.82626 0.97336 0.02462  -0.00573 0.05486  71  GLN D N   
5495 C CA  . GLN D 71  ? 0.84836 0.82031 0.96775 0.02479  -0.00670 0.05945  71  GLN D CA  
5496 C C   . GLN D 71  ? 0.82880 0.80042 0.94408 0.03401  -0.00914 0.05807  71  GLN D C   
5497 O O   . GLN D 71  ? 0.79276 0.77819 0.91466 0.04346  -0.00995 0.05384  71  GLN D O   
5498 C CB  . GLN D 71  ? 0.85576 0.81424 0.95881 0.02519  -0.00143 0.06097  71  GLN D CB  
5499 C CG  . GLN D 71  ? 0.81823 0.77545 0.92159 0.01702  0.00128  0.06278  71  GLN D CG  
5500 C CD  . GLN D 71  ? 0.82398 0.77896 0.92744 0.00832  -0.00169 0.06672  71  GLN D CD  
5501 O OE1 . GLN D 71  ? 0.78722 0.74861 0.90072 0.00496  -0.00186 0.06810  71  GLN D OE1 
5502 N NE2 . GLN D 71  ? 0.81944 0.76542 0.91058 0.00500  -0.00293 0.06806  71  GLN D NE2 
5503 N N   . SER D 72  ? 0.86621 0.82277 0.96896 0.03157  -0.00953 0.06111  72  SER D N   
5504 C CA  . SER D 72  ? 0.91108 0.86307 1.00716 0.03955  -0.01060 0.06069  72  SER D CA  
5505 C C   . SER D 72  ? 0.92961 0.87693 1.01327 0.05376  -0.00618 0.05969  72  SER D C   
5506 O O   . SER D 72  ? 0.92905 0.87037 1.00498 0.05518  -0.00123 0.05995  72  SER D O   
5507 C CB  . SER D 72  ? 0.97793 0.91213 1.06025 0.03260  -0.00904 0.06306  72  SER D CB  
5508 O OG  . SER D 72  ? 1.00806 0.92271 1.07056 0.03084  -0.00163 0.06362  72  SER D OG  
5509 N N   . PRO D 73  ? 0.92927 0.88045 1.01025 0.06605  -0.00776 0.05867  73  PRO D N   
5510 C CA  . PRO D 73  ? 0.94555 0.89176 1.01098 0.08356  -0.00305 0.05880  73  PRO D CA  
5511 C C   . PRO D 73  ? 0.98469 0.89828 1.02312 0.08398  0.00684  0.06269  73  PRO D C   
5512 O O   . PRO D 73  ? 1.01406 0.92275 1.04134 0.09491  0.01238  0.06308  73  PRO D O   
5513 C CB  . PRO D 73  ? 0.90536 0.85668 0.96818 0.09560  -0.00631 0.05838  73  PRO D CB  
5514 C CG  . PRO D 73  ? 0.82876 0.80085 0.91569 0.08499  -0.01437 0.05508  73  PRO D CG  
5515 C CD  . PRO D 73  ? 0.83823 0.80072 0.93014 0.06638  -0.01389 0.05724  73  PRO D CD  
5516 N N   . GLU D 74  ? 1.04738 0.93935 1.07480 0.07195  0.01016  0.06456  74  GLU D N   
5517 C CA  . GLU D 74  ? 1.07152 0.93133 1.07233 0.06954  0.02169  0.06610  74  GLU D CA  
5518 C C   . GLU D 74  ? 1.06677 0.92676 1.06842 0.06274  0.02455  0.06522  74  GLU D C   
5519 O O   . GLU D 74  ? 1.08792 0.92926 1.07027 0.07009  0.03387  0.06605  74  GLU D O   
5520 C CB  . GLU D 74  ? 1.11275 0.95581 1.10533 0.05449  0.02468  0.06547  74  GLU D CB  
5521 N N   . ALA D 75  ? 1.06202 0.94146 1.08414 0.05000  0.01749  0.06394  75  ALA D N   
5522 C CA  . ALA D 75  ? 1.09140 0.97193 1.11422 0.04365  0.02001  0.06335  75  ALA D CA  
5523 C C   . ALA D 75  ? 1.03943 0.92957 1.06511 0.05764  0.02154  0.06285  75  ALA D C   
5524 O O   . ALA D 75  ? 0.98515 0.86276 0.99769 0.05958  0.02889  0.06297  75  ALA D O   
5525 C CB  . ALA D 75  ? 1.05660 0.95566 1.09896 0.03031  0.01260  0.06315  75  ALA D CB  
5526 N N   . ARG D 76  ? 0.99107 0.90545 1.03409 0.06722  0.01507  0.06120  76  ARG D N   
5527 C CA  . ARG D 76  ? 0.95311 0.88414 1.00143 0.08097  0.01595  0.05872  76  ARG D CA  
5528 C C   . ARG D 76  ? 1.03974 0.95519 1.06464 0.10077  0.02285  0.06068  76  ARG D C   
5529 O O   . ARG D 76  ? 0.99957 0.92535 1.02339 0.11400  0.02551  0.05916  76  ARG D O   
5530 C CB  . ARG D 76  ? 0.78007 0.74542 0.85465 0.08324  0.00763  0.05389  76  ARG D CB  
5531 N N   . LYS D 77  ? 1.05997 0.95049 1.06494 0.10409  0.02679  0.06403  77  LYS D N   
5532 C CA  . LYS D 77  ? 1.02922 0.89576 1.00531 0.12336  0.03658  0.06733  77  LYS D CA  
5533 C C   . LYS D 77  ? 1.07089 0.90391 1.02316 0.11814  0.04919  0.06910  77  LYS D C   
5534 O O   . LYS D 77  ? 1.07476 0.89424 1.00765 0.13495  0.05794  0.07109  77  LYS D O   
5535 C CB  . LYS D 77  ? 1.03425 0.88361 0.99592 0.12848  0.03814  0.07006  77  LYS D CB  
5536 N N   . ASN D 78  ? 1.18637 1.00737 1.13931 0.09563  0.05053  0.06783  78  ASN D N   
5537 C CA  . ASN D 78  ? 1.20693 1.00269 1.14168 0.08675  0.06138  0.06722  78  ASN D CA  
5538 C C   . ASN D 78  ? 1.22608 1.03983 1.17320 0.08714  0.05940  0.06584  78  ASN D C   
5539 O O   . ASN D 78  ? 1.25118 1.04575 1.18327 0.08151  0.06843  0.06513  78  ASN D O   
5540 C CB  . ASN D 78  ? 1.20064 0.98682 1.13508 0.06239  0.06182  0.06448  78  ASN D CB  
5541 N N   . ILE D 79  ? 1.11426 0.96371 1.08795 0.09198  0.04897  0.06445  79  ILE D N   
5542 C CA  . ILE D 79  ? 1.05498 0.92206 1.04030 0.09303  0.04855  0.06239  79  ILE D CA  
5543 C C   . ILE D 79  ? 1.00237 0.87948 0.98317 0.11718  0.05156  0.06214  79  ILE D C   
5544 O O   . ILE D 79  ? 1.05095 0.95434 1.04844 0.12051  0.04889  0.05874  79  ILE D O   
5545 C CB  . ILE D 79  ? 0.90505 0.80399 0.92146 0.08067  0.03807  0.05955  79  ILE D CB  
5546 N N   . ALA D 80  ? 0.99980 0.85738 0.95756 0.13482  0.05769  0.06543  80  ALA D N   
5547 C CA  . ALA D 80  ? 0.98306 0.85706 0.93749 0.16186  0.05837  0.06543  80  ALA D CA  
5548 C C   . ALA D 80  ? 1.03865 0.88069 0.96081 0.17731  0.07291  0.06928  80  ALA D C   
5549 O O   . ALA D 80  ? 1.10163 0.90136 0.99832 0.16858  0.08394  0.07226  80  ALA D O   
5550 C CB  . ALA D 80  ? 1.04032 0.91967 0.99129 0.17624  0.05399  0.06710  80  ALA D CB  
5551 N N   . PRO D 81  ? 1.03387 0.89525 0.95540 0.20037  0.07431  0.06851  81  PRO D N   
5552 C CA  . PRO D 81  ? 1.02845 0.85807 0.91820 0.21629  0.08929  0.07257  81  PRO D CA  
5553 C C   . PRO D 81  ? 1.12629 0.90775 0.97709 0.22787  0.10192  0.07945  81  PRO D C   
5554 O O   . PRO D 81  ? 1.17608 0.95903 1.02399 0.23598  0.09796  0.08160  81  PRO D O   
5555 C CB  . PRO D 81  ? 0.92724 0.79605 0.82647 0.24333  0.08581  0.07012  81  PRO D CB  
5556 C CG  . PRO D 81  ? 0.95755 0.87843 0.89884 0.23033  0.07067  0.06199  81  PRO D CG  
5557 C CD  . PRO D 81  ? 1.01452 0.92984 0.96527 0.21138  0.06319  0.06246  81  PRO D CD  
5558 N N   . SER D 82  ? 1.15062 0.88674 0.97015 0.22697  0.11858  0.08240  82  SER D N   
5559 C CA  . SER D 82  ? 1.29160 0.97634 1.06788 0.24193  0.13552  0.08885  82  SER D CA  
5560 C C   . SER D 82  ? 1.37875 1.03483 1.12527 0.25947  0.15219  0.09195  82  SER D C   
5561 O O   . SER D 82  ? 1.37612 1.05628 1.13797 0.26040  0.14895  0.08889  82  SER D O   
5562 C CB  . SER D 82  ? 1.28563 0.93100 1.04846 0.21480  0.14299  0.08791  82  SER D CB  
5563 O OG  . SER D 82  ? 1.32667 0.94652 1.08033 0.19322  0.15310  0.08434  82  SER D OG  
5564 N N   . ASP D 83  ? 1.54831 1.15100 1.25052 0.27429  0.17145  0.09812  83  ASP D N   
5565 C CA  . ASP D 83  ? 1.59163 1.15888 1.25988 0.29205  0.19036  0.10179  83  ASP D CA  
5566 C C   . ASP D 83  ? 1.64141 1.16580 1.29370 0.26339  0.20522  0.09773  83  ASP D C   
5567 O O   . ASP D 83  ? 1.70874 1.20562 1.33663 0.27320  0.22061  0.09918  83  ASP D O   
5568 C CB  . ASP D 83  ? 1.65627 1.18387 1.27987 0.32631  0.20644  0.11114  83  ASP D CB  
5569 C CG  . ASP D 83  ? 1.73931 1.31463 1.37505 0.36207  0.19310  0.11469  83  ASP D CG  
5570 O OD1 . ASP D 83  ? 1.71554 1.34608 1.38493 0.36644  0.17835  0.10989  83  ASP D OD1 
5571 O OD2 . ASP D 83  ? 1.86633 1.42576 1.47802 0.38533  0.19769  0.12140  83  ASP D OD2 
5572 N N   . GLU D 84  ? 1.50185 1.02286 1.16763 0.22886  0.20088  0.09195  84  GLU D N   
5573 C CA  . GLU D 84  ? 1.53583 1.02867 1.19301 0.19858  0.21160  0.08547  84  GLU D CA  
5574 C C   . GLU D 84  ? 1.42037 0.95813 1.11662 0.17810  0.19525  0.07922  84  GLU D C   
5575 O O   . GLU D 84  ? 1.40199 0.92812 1.09835 0.14997  0.19921  0.07275  84  GLU D O   
5576 C CB  . GLU D 84  ? 1.55853 1.02124 1.20389 0.17348  0.21866  0.08159  84  GLU D CB  
5577 C CG  . GLU D 84  ? 1.60007 1.10569 1.28353 0.15659  0.19693  0.07861  84  GLU D CG  
5578 C CD  . GLU D 84  ? 1.68604 1.16230 1.35549 0.13575  0.20528  0.07487  84  GLU D CD  
5579 O OE1 . GLU D 84  ? 1.67486 1.09584 1.30394 0.13419  0.22923  0.07414  84  GLU D OE1 
5580 O OE2 . GLU D 84  ? 1.68384 1.19135 1.38171 0.12093  0.18922  0.07220  84  GLU D OE2 
5581 N N   . ASP D 85  ? 1.32738 0.91619 1.05534 0.19161  0.17805  0.08036  85  ASP D N   
5582 C CA  . ASP D 85  ? 1.24668 0.87056 1.00434 0.17737  0.16747  0.07549  85  ASP D CA  
5583 C C   . ASP D 85  ? 1.25309 0.85026 0.98772 0.18186  0.18326  0.07507  85  ASP D C   
5584 O O   . ASP D 85  ? 1.32159 0.88583 1.02319 0.20543  0.19914  0.07979  85  ASP D O   
5585 C CB  . ASP D 85  ? 1.24490 0.92562 1.03752 0.19249  0.14973  0.07562  85  ASP D CB  
5586 C CG  . ASP D 85  ? 1.17744 0.88734 0.99528 0.18668  0.13369  0.07506  85  ASP D CG  
5587 O OD1 . ASP D 85  ? 1.11758 0.81475 0.93683 0.16421  0.13177  0.07354  85  ASP D OD1 
5588 O OD2 . ASP D 85  ? 1.15851 0.90709 0.99569 0.20456  0.12302  0.07515  85  ASP D OD2 
5589 N N   . VAL D 86  ? 1.27742 0.88668 1.02732 0.15958  0.17981  0.06965  86  VAL D N   
5590 C CA  . VAL D 86  ? 1.24758 0.83849 0.98119 0.16099  0.19255  0.06815  86  VAL D CA  
5591 C C   . VAL D 86  ? 1.10416 0.74007 0.87232 0.15172  0.17886  0.06462  86  VAL D C   
5592 O O   . VAL D 86  ? 1.09572 0.76576 0.89493 0.13616  0.16272  0.06234  86  VAL D O   
5593 C CB  . VAL D 86  ? 1.26735 0.81134 0.97256 0.13735  0.20894  0.06337  86  VAL D CB  
5594 C CG1 . VAL D 86  ? 1.31118 0.80743 0.98171 0.14172  0.22468  0.06542  86  VAL D CG1 
5595 C CG2 . VAL D 86  ? 1.25465 0.82116 0.98417 0.10438  0.19672  0.05673  86  VAL D CG2 
5596 N N   . SER D 87  ? 1.14292 0.77632 0.90379 0.16143  0.18685  0.06426  87  SER D N   
5597 C CA  . SER D 87  ? 1.15965 0.82825 0.94853 0.14937  0.17741  0.06031  87  SER D CA  
5598 C C   . SER D 87  ? 1.13791 0.80040 0.93113 0.11634  0.17472  0.05565  87  SER D C   
5599 O O   . SER D 87  ? 1.15754 0.78599 0.92866 0.10214  0.18333  0.05370  87  SER D O   
5600 C CB  . SER D 87  ? 1.18600 0.84835 0.96284 0.16371  0.18865  0.06016  87  SER D CB  
5601 O OG  . SER D 87  ? 1.18613 0.87315 0.96955 0.19435  0.18675  0.06289  87  SER D OG  
5602 N N   . THR D 88  ? 1.10381 0.80168 0.92563 0.10453  0.16312  0.05326  88  THR D N   
5603 C CA  . THR D 88  ? 1.13094 0.82904 0.95724 0.07685  0.15965  0.04941  88  THR D CA  
5604 C C   . THR D 88  ? 1.16851 0.83212 0.96615 0.06730  0.17512  0.04573  88  THR D C   
5605 O O   . THR D 88  ? 1.11814 0.77065 0.90791 0.04505  0.17616  0.04128  88  THR D O   
5606 C CB  . THR D 88  ? 1.01782 0.75662 0.87606 0.07099  0.14716  0.04883  88  THR D CB  
5607 O OG1 . THR D 88  ? 1.04077 0.79193 0.90360 0.08790  0.15145  0.04894  88  THR D OG1 
5608 C CG2 . THR D 88  ? 0.97434 0.74289 0.85926 0.07147  0.13253  0.05049  88  THR D CG2 
5609 N N   . ILE D 89  ? 1.21704 0.86552 0.99884 0.08395  0.18740  0.04668  89  ILE D N   
5610 C CA  . ILE D 89  ? 1.25082 0.85860 0.99968 0.07759  0.20557  0.04308  89  ILE D CA  
5611 C C   . ILE D 89  ? 1.27989 0.84524 0.99891 0.07272  0.21801  0.04155  89  ILE D C   
5612 O O   . ILE D 89  ? 1.27133 0.81604 0.97519 0.04951  0.22503  0.03472  89  ILE D O   
5613 C CB  . ILE D 89  ? 1.25739 0.85585 0.99375 0.10085  0.21721  0.04545  89  ILE D CB  
5614 C CG1 . ILE D 89  ? 1.29412 0.92751 1.05446 0.09906  0.20980  0.04415  89  ILE D CG1 
5615 C CG2 . ILE D 89  ? 1.29318 0.83906 0.98871 0.09841  0.23937  0.04266  89  ILE D CG2 
5616 C CD1 . ILE D 89  ? 1.29311 0.92817 1.04774 0.12477  0.21865  0.04622  89  ILE D CD1 
5617 N N   . ASP D 90  ? 1.23585 0.78717 0.94401 0.09507  0.22254  0.04710  90  ASP D N   
5618 C CA  . ASP D 90  ? 1.27945 0.78604 0.95646 0.09180  0.23694  0.04612  90  ASP D CA  
5619 C C   . ASP D 90  ? 1.31203 0.82740 1.00030 0.06380  0.22809  0.04056  90  ASP D C   
5620 O O   . ASP D 90  ? 1.35137 0.83455 1.01655 0.04440  0.24109  0.03348  90  ASP D O   
5621 C CB  . ASP D 90  ? 1.33114 0.82873 0.99888 0.12123  0.23937  0.05422  90  ASP D CB  
5622 C CG  . ASP D 90  ? 1.40910 0.88900 1.05533 0.15292  0.25280  0.05976  90  ASP D CG  
5623 O OD1 . ASP D 90  ? 1.42846 0.88680 1.05706 0.15053  0.26619  0.05699  90  ASP D OD1 
5624 O OD2 . ASP D 90  ? 1.35027 0.83681 0.99484 0.18145  0.25074  0.06680  90  ASP D OD2 
5625 N N   . GLY D 91  ? 1.30447 0.86438 1.02805 0.06125  0.20678  0.04279  91  GLY D N   
5626 C CA  . GLY D 91  ? 1.29402 0.86594 1.02955 0.03820  0.19730  0.03844  91  GLY D CA  
5627 C C   . GLY D 91  ? 1.30231 0.87626 1.03584 0.01064  0.19845  0.02960  91  GLY D C   
5628 O O   . GLY D 91  ? 1.32287 0.88394 1.04558 -0.00949 0.20314  0.02230  91  GLY D O   
5629 N N   . ILE D 92  ? 1.27225 0.86511 1.01645 0.00926  0.19419  0.02936  92  ILE D N   
5630 C CA  . ILE D 92  ? 1.28454 0.88173 1.02529 -0.01499 0.19494  0.02104  92  ILE D CA  
5631 C C   . ILE D 92  ? 1.35937 0.91185 1.06341 -0.02452 0.21737  0.01291  92  ILE D C   
5632 O O   . ILE D 92  ? 1.39375 0.94200 1.08833 -0.04861 0.22138  0.00263  92  ILE D O   
5633 C CB  . ILE D 92  ? 1.26084 0.88734 1.02020 -0.01327 0.18578  0.02341  92  ILE D CB  
5634 C CG1 . ILE D 92  ? 1.20855 0.85341 0.97232 -0.03699 0.17928  0.01667  92  ILE D CG1 
5635 C CG2 . ILE D 92  ? 1.29865 0.90278 1.03980 -0.00208 0.20037  0.02360  92  ILE D CG2 
5636 C CD1 . ILE D 92  ? 1.15563 0.83026 0.94088 -0.04553 0.16280  0.01757  92  ILE D CD1 
5637 N N   . ALA D 93  ? 1.36888 0.88781 1.05071 -0.00566 0.23323  0.01659  93  ALA D N   
5638 C CA  . ALA D 93  ? 1.42049 0.88872 1.06318 -0.01331 0.25796  0.00930  93  ALA D CA  
5639 C C   . ALA D 93  ? 1.50116 0.94613 1.12886 -0.02750 0.26606  0.00335  93  ALA D C   
5640 O O   . ALA D 93  ? 1.56845 0.99447 1.17778 -0.05234 0.27837  -0.00905 93  ALA D O   
5641 C CB  . ALA D 93  ? 1.34782 0.78336 0.96836 0.01482  0.27346  0.01659  93  ALA D CB  
5642 N N   . LYS D 94  ? 1.44569 0.89400 1.08159 -0.01308 0.25952  0.01094  94  LYS D N   
5643 C CA  . LYS D 94  ? 1.47626 0.90894 1.10292 -0.02740 0.26464  0.00555  94  LYS D CA  
5644 C C   . LYS D 94  ? 1.51461 0.98196 1.16124 -0.05732 0.25180  -0.00482 94  LYS D C   
5645 O O   . LYS D 94  ? 1.54585 0.99675 1.17826 -0.07860 0.26206  -0.01557 94  LYS D O   
5646 C CB  . LYS D 94  ? 1.46325 0.90333 1.10115 -0.00586 0.25540  0.01630  94  LYS D CB  
5647 C CG  . LYS D 94  ? 1.54526 0.94403 1.15476 0.02372  0.27182  0.02521  94  LYS D CG  
5648 C CD  . LYS D 94  ? 1.53558 0.94721 1.15739 0.04218  0.26086  0.03420  94  LYS D CD  
5649 C CE  . LYS D 94  ? 1.53723 0.90628 1.12608 0.07288  0.27820  0.04305  94  LYS D CE  
5650 N NZ  . LYS D 94  ? 1.49025 0.79756 1.03604 0.06207  0.30561  0.03761  94  LYS D NZ  
5651 N N   . PHE D 95  ? 1.51055 1.02660 1.18940 -0.05855 0.23006  -0.00196 95  PHE D N   
5652 C CA  . PHE D 95  ? 1.48062 1.03214 1.17681 -0.08300 0.21735  -0.01064 95  PHE D CA  
5653 C C   . PHE D 95  ? 1.54354 1.08241 1.21903 -0.10735 0.23092  -0.02541 95  PHE D C   
5654 O O   . PHE D 95  ? 1.55401 1.10486 1.22922 -0.13090 0.23073  -0.03754 95  PHE D O   
5655 C CB  . PHE D 95  ? 1.36054 0.96065 1.09037 -0.07651 0.19417  -0.00324 95  PHE D CB  
5656 C CG  . PHE D 95  ? 1.29013 0.92543 1.03284 -0.09800 0.18260  -0.01127 95  PHE D CG  
5657 C CD1 . PHE D 95  ? 1.25228 0.90818 1.00730 -0.10831 0.17314  -0.01456 95  PHE D CD1 
5658 C CD2 . PHE D 95  ? 1.31995 0.96809 1.06046 -0.10693 0.18193  -0.01591 95  PHE D CD2 
5659 C CE1 . PHE D 95  ? 1.24799 0.93907 1.01330 -0.12548 0.16266  -0.02212 95  PHE D CE1 
5660 C CE2 . PHE D 95  ? 1.25478 0.93711 1.00443 -0.12407 0.17144  -0.02323 95  PHE D CE2 
5661 C CZ  . PHE D 95  ? 1.25879 0.96354 1.02076 -0.13271 0.16170  -0.02638 95  PHE D CZ  
5662 N N   . ASN D 96  ? 1.52874 1.04740 1.18797 -0.10245 0.24233  -0.02563 96  ASN D N   
5663 C CA  . ASN D 96  ? 1.60583 1.11161 1.24403 -0.12605 0.25635  -0.04073 96  ASN D CA  
5664 C C   . ASN D 96  ? 1.69610 1.15323 1.30087 -0.13974 0.28185  -0.05183 96  ASN D C   
5665 O O   . ASN D 96  ? 1.73233 1.19278 1.32864 -0.16788 0.28872  -0.06846 96  ASN D O   
5666 C CB  . ASN D 96  ? 1.60367 1.10007 1.23322 -0.11679 0.26218  -0.03781 96  ASN D CB  
5667 C CG  . ASN D 96  ? 1.59345 1.13701 1.25409 -0.10754 0.23940  -0.02900 96  ASN D CG  
5668 O OD1 . ASN D 96  ? 1.50342 1.04672 1.17069 -0.08610 0.23696  -0.01816 96  ASN D OD1 
5669 N ND2 . ASN D 96  ? 1.56505 1.14978 1.24434 -0.12297 0.22335  -0.03379 96  ASN D ND2 
5670 N N   . ASP D 97  ? 1.71800 1.13059 1.30269 -0.11998 0.29679  -0.04343 97  ASP D N   
5671 C CA  . ASP D 97  ? 1.76388 1.12168 1.31163 -0.13133 0.32483  -0.05291 97  ASP D CA  
5672 C C   . ASP D 97  ? 1.73566 1.10576 1.29024 -0.15277 0.32230  -0.06265 97  ASP D C   
5673 O O   . ASP D 97  ? 1.80149 1.13795 1.32953 -0.17484 0.34468  -0.07728 97  ASP D O   
5674 C CB  . ASP D 97  ? 1.75008 1.05918 1.27402 -0.10096 0.34013  -0.03947 97  ASP D CB  
5675 C CG  . ASP D 97  ? 1.79468 1.08275 1.30341 -0.08167 0.34957  -0.03303 97  ASP D CG  
5676 O OD1 . ASP D 97  ? 1.75092 1.04745 1.25827 -0.09698 0.35154  -0.04184 97  ASP D OD1 
5677 O OD2 . ASP D 97  ? 1.77888 1.04140 1.27499 -0.05070 0.35618  -0.01976 97  ASP D OD2 
5678 N N   . TYR D 98  ? 1.74202 1.15891 1.33117 -0.14711 0.29675  -0.05546 98  TYR D N   
5679 C CA  . TYR D 98  ? 1.79469 1.23473 1.39534 -0.16939 0.29101  -0.06612 98  TYR D CA  
5680 C C   . TYR D 98  ? 1.81460 1.29279 1.42463 -0.19814 0.28490  -0.08292 98  TYR D C   
5681 O O   . TYR D 98  ? 1.84843 1.32112 1.44568 -0.22592 0.29800  -0.10129 98  TYR D O   
5682 C CB  . TYR D 98  ? 1.66796 1.14600 1.30194 -0.15289 0.26582  -0.05278 98  TYR D CB  
5683 C CG  . TYR D 98  ? 1.65125 1.15792 1.30038 -0.17227 0.25741  -0.06192 98  TYR D CG  
5684 C CD1 . TYR D 98  ? 1.72875 1.20595 1.36324 -0.17699 0.27091  -0.06521 98  TYR D CD1 
5685 C CD2 . TYR D 98  ? 1.68163 1.24492 1.35830 -0.18490 0.23671  -0.06725 98  TYR D CD2 
5686 C CE1 . TYR D 98  ? 1.76831 1.27423 1.41799 -0.19485 0.26326  -0.07419 98  TYR D CE1 
5687 C CE2 . TYR D 98  ? 1.67139 1.26454 1.36252 -0.20079 0.22857  -0.07572 98  TYR D CE2 
5688 C CZ  . TYR D 98  ? 1.72662 1.29200 1.40529 -0.20655 0.24176  -0.07970 98  TYR D CZ  
5689 O OH  . TYR D 98  ? 1.73274 1.32958 1.42665 -0.22260 0.23404  -0.08881 98  TYR D OH  
5690 N N   . ILE D 99  ? 1.82317 1.34069 1.45416 -0.19176 0.26610  -0.07765 99  ILE D N   
5691 C CA  . ILE D 99  ? 1.83120 1.39581 1.47556 -0.21395 0.25468  -0.09085 99  ILE D CA  
5692 C C   . ILE D 99  ? 1.88486 1.42768 1.50117 -0.23795 0.27621  -0.10980 99  ILE D C   
5693 O O   . ILE D 99  ? 1.91496 1.48783 1.53345 -0.26403 0.27508  -0.12787 99  ILE D O   
5694 C CB  . ILE D 99  ? 1.71574 1.32472 1.38778 -0.19800 0.22970  -0.07814 99  ILE D CB  
5695 C CG1 . ILE D 99  ? 1.69760 1.36332 1.38897 -0.21424 0.21222  -0.08739 99  ILE D CG1 
5696 C CG2 . ILE D 99  ? 1.71051 1.30344 1.37021 -0.19049 0.23661  -0.07511 99  ILE D CG2 
5697 C CD1 . ILE D 99  ? 1.68453 1.37487 1.39509 -0.21533 0.20005  -0.08618 99  ILE D CD1 
5698 N N   . ASN D 100 ? 1.88969 1.38217 1.47901 -0.22953 0.29640  -0.10695 100 ASN D N   
5699 C CA  . ASN D 100 ? 1.91826 1.37936 1.47598 -0.25351 0.32186  -0.12600 100 ASN D CA  
5700 C C   . ASN D 100 ? 1.96361 1.39786 1.50209 -0.27754 0.34257  -0.14264 100 ASN D C   
5701 O O   . ASN D 100 ? 1.99040 1.43686 1.52084 -0.30922 0.35192  -0.16537 100 ASN D O   
5702 C CB  . ASN D 100 ? 1.92884 1.33566 1.45929 -0.23607 0.34112  -0.11770 100 ASN D CB  
5703 C CG  . ASN D 100 ? 1.90928 1.34113 1.45331 -0.22134 0.32653  -0.10817 100 ASN D CG  
5704 O OD1 . ASN D 100 ? 1.90937 1.38323 1.46605 -0.23591 0.31439  -0.11678 100 ASN D OD1 
5705 N ND2 . ASN D 100 ? 1.86017 1.26736 1.40068 -0.19173 0.32827  -0.09074 100 ASN D ND2 
5706 N N   . ALA D 101 ? 1.99461 1.39405 1.52556 -0.26312 0.35023  -0.13233 101 ALA D N   
5707 C CA  . ALA D 101 ? 1.96269 1.32256 1.46917 -0.28224 0.37494  -0.14555 101 ALA D CA  
5708 C C   . ALA D 101 ? 1.95182 1.35718 1.48226 -0.30079 0.36130  -0.15557 101 ALA D C   
5709 O O   . ALA D 101 ? 1.98249 1.35882 1.49962 -0.30890 0.37660  -0.16046 101 ALA D O   
5710 C CB  . ALA D 101 ? 1.90647 1.20601 1.39046 -0.25540 0.39038  -0.12875 101 ALA D CB  
5711 N N   . HIS D 102 ? 1.90059 1.37521 1.46447 -0.30634 0.33385  -0.15827 102 HIS D N   
5712 C CA  . HIS D 102 ? 1.97415 1.49570 1.56023 -0.32376 0.32124  -0.16910 102 HIS D CA  
5713 C C   . HIS D 102 ? 2.06240 1.64565 1.66417 -0.34593 0.30818  -0.18667 102 HIS D C   
5714 O O   . HIS D 102 ? 2.02822 1.67142 1.66004 -0.34539 0.28361  -0.18604 102 HIS D O   
5715 C CB  . HIS D 102 ? 1.93881 1.48535 1.55412 -0.29779 0.29644  -0.14821 102 HIS D CB  
5716 C CG  . HIS D 102 ? 1.94768 1.44264 1.54769 -0.28390 0.31045  -0.13770 102 HIS D CG  
5717 N ND1 . HIS D 102 ? 1.94943 1.39923 1.53468 -0.25516 0.31728  -0.11900 102 HIS D ND1 
5718 C CD2 . HIS D 102 ? 1.92360 1.40535 1.51895 -0.29436 0.31988  -0.14387 102 HIS D CD2 
5719 C CE1 . HIS D 102 ? 1.92837 1.33963 1.49954 -0.24702 0.32968  -0.11338 102 HIS D CE1 
5720 N NE2 . HIS D 102 ? 1.95811 1.38593 1.53479 -0.27095 0.33188  -0.12796 102 HIS D NE2 
5721 N N   . ASN D 103 ? 2.32605 1.89486 1.90586 -0.36450 0.32521  -0.20259 103 ASN D N   
5722 C CA  . ASN D 103 ? 2.31686 1.93640 1.90197 -0.39337 0.32168  -0.22687 103 ASN D CA  
5723 C C   . ASN D 103 ? 2.27566 1.96954 1.89555 -0.38032 0.28645  -0.21826 103 ASN D C   
5724 O O   . ASN D 103 ? 2.25414 2.00313 1.89510 -0.39023 0.27132  -0.22729 103 ASN D O   
5725 C CB  . ASN D 103 ? 2.27500 1.90062 1.85379 -0.42736 0.33763  -0.25300 103 ASN D CB  
5726 N N   . ILE D 104 ? 2.01562 1.70815 1.63978 -0.35631 0.27472  -0.19991 104 ILE D N   
5727 C CA  . ILE D 104 ? 1.91685 1.66965 1.56822 -0.34144 0.24477  -0.18960 104 ILE D CA  
5728 C C   . ILE D 104 ? 1.88349 1.63966 1.52385 -0.34172 0.24599  -0.19196 104 ILE D C   
5729 O O   . ILE D 104 ? 1.88402 1.59460 1.50975 -0.32813 0.25652  -0.18064 104 ILE D O   
5730 C CB  . ILE D 104 ? 1.89897 1.65079 1.57171 -0.30824 0.22607  -0.16140 104 ILE D CB  
5731 C CG1 . ILE D 104 ? 1.87464 1.64663 1.56509 -0.30961 0.21734  -0.16123 104 ILE D CG1 
5732 C CG2 . ILE D 104 ? 1.80379 1.59338 1.49411 -0.28887 0.20315  -0.14702 104 ILE D CG2 
5733 C CD1 . ILE D 104 ? 1.76278 1.52888 1.47174 -0.28018 0.20250  -0.13626 104 ILE D CD1 
5734 N N   . ASP D 105 ? 1.79762 1.60976 1.44420 -0.35670 0.23548  -0.20736 105 ASP D N   
5735 C CA  . ASP D 105 ? 1.72124 1.54213 1.35696 -0.35846 0.23584  -0.21133 105 ASP D CA  
5736 C C   . ASP D 105 ? 1.70580 1.53956 1.35725 -0.32669 0.21484  -0.18529 105 ASP D C   
5737 O O   . ASP D 105 ? 1.66523 1.53776 1.34041 -0.31163 0.19266  -0.17329 105 ASP D O   
5738 C CB  . ASP D 105 ? 1.70272 1.58452 1.34015 -0.38229 0.22983  -0.23589 105 ASP D CB  
5739 C CG  . ASP D 105 ? 1.73069 1.61727 1.35215 -0.38771 0.23399  -0.24336 105 ASP D CG  
5740 O OD1 . ASP D 105 ? 1.79933 1.64469 1.39515 -0.40717 0.25931  -0.25862 105 ASP D OD1 
5741 O OD2 . ASP D 105 ? 1.66679 1.59455 1.29929 -0.37186 0.21341  -0.23344 105 ASP D OD2 
5742 N N   . PRO D 106 ? 1.66977 1.47157 1.30773 -0.31673 0.22255  -0.17701 106 PRO D N   
5743 C CA  . PRO D 106 ? 1.59542 1.40788 1.24798 -0.28823 0.20484  -0.15343 106 PRO D CA  
5744 C C   . PRO D 106 ? 1.55851 1.43470 1.22638 -0.28454 0.18197  -0.15292 106 PRO D C   
5745 O O   . PRO D 106 ? 1.46273 1.35602 1.14915 -0.26166 0.16413  -0.13325 106 PRO D O   
5746 C CB  . PRO D 106 ? 1.60327 1.37620 1.23461 -0.28590 0.22053  -0.15220 106 PRO D CB  
5747 C CG  . PRO D 106 ? 1.64946 1.37303 1.25568 -0.30513 0.24819  -0.16775 106 PRO D CG  
5748 C CD  . PRO D 106 ? 1.67499 1.42840 1.28308 -0.33119 0.24910  -0.18917 106 PRO D CD  
5749 N N   . TRP D 107 ? 1.58099 1.49324 1.24030 -0.30618 0.18288  -0.17470 107 TRP D N   
5750 C CA  . TRP D 107 ? 1.55239 1.52625 1.22128 -0.30050 0.16226  -0.17478 107 TRP D CA  
5751 C C   . TRP D 107 ? 1.53249 1.55551 1.21950 -0.30374 0.14760  -0.18050 107 TRP D C   
5752 O O   . TRP D 107 ? 1.51591 1.56289 1.22102 -0.28204 0.12876  -0.16290 107 TRP D O   
5753 C CB  . TRP D 107 ? 1.49673 1.48956 1.14602 -0.31986 0.16980  -0.19565 107 TRP D CB  
5754 C CG  . TRP D 107 ? 1.46887 1.41567 1.09870 -0.31777 0.18494  -0.19174 107 TRP D CG  
5755 C CD1 . TRP D 107 ? 1.53413 1.42868 1.14361 -0.33374 0.21007  -0.20274 107 TRP D CD1 
5756 C CD2 . TRP D 107 ? 1.47979 1.42885 1.10663 -0.29938 0.17751  -0.17709 107 TRP D CD2 
5757 N NE1 . TRP D 107 ? 1.50619 1.37160 1.10164 -0.32536 0.21785  -0.19541 107 TRP D NE1 
5758 C CE2 . TRP D 107 ? 1.50970 1.40849 1.11614 -0.30520 0.19813  -0.18013 107 TRP D CE2 
5759 C CE3 . TRP D 107 ? 1.42189 1.40759 1.05946 -0.27813 0.15709  -0.16145 107 TRP D CE3 
5760 C CZ2 . TRP D 107 ? 1.40348 1.29089 1.00239 -0.29130 0.19792  -0.16869 107 TRP D CZ2 
5761 C CZ3 . TRP D 107 ? 1.39655 1.36783 1.02511 -0.26501 0.15808  -0.14996 107 TRP D CZ3 
5762 C CH2 . TRP D 107 ? 1.37817 1.30237 0.98876 -0.27217 0.17788  -0.15404 107 TRP D CH2 
5763 N N   . LYS D 108 ? 1.57346 1.60913 1.25546 -0.33096 0.15772  -0.20527 108 LYS D N   
5764 C CA  . LYS D 108 ? 1.56184 1.65503 1.26012 -0.33669 0.14383  -0.21522 108 LYS D CA  
5765 C C   . LYS D 108 ? 1.56659 1.64918 1.28430 -0.32281 0.13641  -0.19961 108 LYS D C   
5766 O O   . LYS D 108 ? 1.55137 1.68317 1.28536 -0.32055 0.12145  -0.20237 108 LYS D O   
5767 C CB  . LYS D 108 ? 1.64818 1.75914 1.33600 -0.37292 0.15895  -0.24907 108 LYS D CB  
5768 C CG  . LYS D 108 ? 1.65656 1.79829 1.32796 -0.39079 0.16332  -0.27080 108 LYS D CG  
5769 C CD  . LYS D 108 ? 1.70401 1.86736 1.36871 -0.42905 0.17872  -0.30655 108 LYS D CD  
5770 C CE  . LYS D 108 ? 1.70654 1.90395 1.35497 -0.45094 0.18465  -0.33258 108 LYS D CE  
5771 N NZ  . LYS D 108 ? 1.61675 1.83594 1.25975 -0.49086 0.20144  -0.36970 108 LYS D NZ  
5772 N N   . SER D 109 ? 1.58381 1.60638 1.29987 -0.31281 0.14634  -0.18401 109 SER D N   
5773 C CA  . SER D 109 ? 1.57813 1.58890 1.31078 -0.30182 0.14119  -0.17145 109 SER D CA  
5774 C C   . SER D 109 ? 1.50141 1.52988 1.25334 -0.27121 0.11944  -0.14594 109 SER D C   
5775 O O   . SER D 109 ? 1.46189 1.48758 1.21137 -0.25538 0.11369  -0.13279 109 SER D O   
5776 C CB  . SER D 109 ? 1.63590 1.57728 1.35740 -0.30166 0.16075  -0.16536 109 SER D CB  
5777 O OG  . SER D 109 ? 1.70062 1.61732 1.40200 -0.32990 0.18409  -0.18822 109 SER D OG  
5778 N N   . GLN D 110 ? 1.47851 1.52168 1.24867 -0.26358 0.10919  -0.13922 110 GLN D N   
5779 C CA  . GLN D 110 ? 1.48084 1.53682 1.26902 -0.23612 0.09082  -0.11599 110 GLN D CA  
5780 C C   . GLN D 110 ? 1.43632 1.45281 1.23446 -0.22528 0.09367  -0.10168 110 GLN D C   
5781 O O   . GLN D 110 ? 1.46443 1.46750 1.26266 -0.23793 0.10235  -0.11077 110 GLN D O   
5782 C CB  . GLN D 110 ? 1.47897 1.59700 1.28071 -0.23262 0.07294  -0.11952 110 GLN D CB  
5783 C CG  . GLN D 110 ? 1.45246 1.61777 1.24529 -0.23653 0.06621  -0.13049 110 GLN D CG  
5784 C CD  . GLN D 110 ? 1.45463 1.68137 1.26013 -0.22543 0.04709  -0.12963 110 GLN D CD  
5785 O OE1 . GLN D 110 ? 1.44768 1.68018 1.26917 -0.21600 0.03940  -0.12115 110 GLN D OE1 
5786 N NE2 . GLN D 110 ? 1.43436 1.70806 1.23166 -0.22516 0.03952  -0.13838 110 GLN D NE2 
5787 N N   . GLY D 111 ? 1.40986 1.40937 1.21591 -0.20217 0.08680  -0.08008 111 GLY D N   
5788 C CA  . GLY D 111 ? 1.34510 1.31350 1.16217 -0.18901 0.08721  -0.06569 111 GLY D CA  
5789 C C   . GLY D 111 ? 1.27779 1.27384 1.11572 -0.17150 0.06927  -0.05163 111 GLY D C   
5790 O O   . GLY D 111 ? 1.23210 1.25116 1.07396 -0.15884 0.05829  -0.04258 111 GLY D O   
5791 N N   . TRP D 112 ? 1.27342 1.26356 1.12251 -0.17045 0.06794  -0.04959 112 TRP D N   
5792 C CA  . TRP D 112 ? 1.23654 1.25166 1.10468 -0.15621 0.05263  -0.03848 112 TRP D CA  
5793 C C   . TRP D 112 ? 1.22258 1.20786 1.10149 -0.13881 0.05152  -0.02108 112 TRP D C   
5794 O O   . TRP D 112 ? 1.18685 1.13449 1.05931 -0.13767 0.06231  -0.01860 112 TRP D O   
5795 C CB  . TRP D 112 ? 1.21157 1.25082 1.08598 -0.16866 0.05048  -0.05079 112 TRP D CB  
5796 C CG  . TRP D 112 ? 1.22577 1.31293 1.09658 -0.17868 0.04459  -0.06462 112 TRP D CG  
5797 C CD1 . TRP D 112 ? 1.26425 1.36042 1.12022 -0.19973 0.05407  -0.08434 112 TRP D CD1 
5798 C CD2 . TRP D 112 ? 1.22168 1.35703 1.10289 -0.16727 0.02819  -0.06068 112 TRP D CD2 
5799 N NE1 . TRP D 112 ? 1.27312 1.42494 1.13110 -0.20208 0.04321  -0.09361 112 TRP D NE1 
5800 C CE2 . TRP D 112 ? 1.25574 1.43221 1.12838 -0.18093 0.02715  -0.07863 112 TRP D CE2 
5801 C CE3 . TRP D 112 ? 1.17654 1.32398 1.07202 -0.14608 0.01513  -0.04394 112 TRP D CE3 
5802 C CZ2 . TRP D 112 ? 1.21021 1.44198 1.08800 -0.17160 0.01239  -0.07955 112 TRP D CZ2 
5803 C CZ3 . TRP D 112 ? 1.20292 1.39987 1.10189 -0.13692 0.00195  -0.04398 112 TRP D CZ3 
5804 C CH2 . TRP D 112 ? 1.19302 1.43291 1.08314 -0.14850 0.00014  -0.06132 112 TRP D CH2 
5805 N N   . CYS D 113 ? 1.30690 1.31141 1.20153 -0.12427 0.03857  -0.00934 113 CYS D N   
5806 C CA  . CYS D 113 ? 1.28212 1.26662 1.18785 -0.10712 0.03601  0.00695  113 CYS D CA  
5807 C C   . CYS D 113 ? 1.28933 1.29731 1.21047 -0.09438 0.02307  0.01692  113 CYS D C   
5808 O O   . CYS D 113 ? 1.31150 1.35111 1.23101 -0.09223 0.01523  0.01613  113 CYS D O   
5809 C CB  . CYS D 113 ? 1.26475 1.23637 1.16266 -0.10086 0.03991  0.01298  113 CYS D CB  
5810 S SG  . CYS D 113 ? 1.33382 1.28491 1.24425 -0.08304 0.03914  0.02937  113 CYS D SG  
5811 N N   . ARG D 114 ? 1.25872 1.25280 1.19346 -0.08492 0.02101  0.02608  114 ARG D N   
5812 C CA  . ARG D 114 ? 1.25973 1.26898 1.20745 -0.07125 0.01104  0.03725  114 ARG D CA  
5813 C C   . ARG D 114 ? 1.26515 1.25788 1.21558 -0.05921 0.01287  0.04922  114 ARG D C   
5814 O O   . ARG D 114 ? 1.30991 1.27849 1.26469 -0.05746 0.01873  0.05149  114 ARG D O   
5815 C CB  . ARG D 114 ? 1.26819 1.27525 1.22996 -0.06902 0.00765  0.03906  114 ARG D CB  
5816 C CG  . ARG D 114 ? 1.25665 1.28562 1.21982 -0.07872 0.00422  0.02890  114 ARG D CG  
5817 C CD  . ARG D 114 ? 1.25269 1.27990 1.23062 -0.07352 -0.00002 0.03323  114 ARG D CD  
5818 N NE  . ARG D 114 ? 1.20711 1.25206 1.19510 -0.05980 -0.00946 0.04340  114 ARG D NE  
5819 C CZ  . ARG D 114 ? 1.18816 1.26408 1.17929 -0.05838 -0.01702 0.04104  114 ARG D CZ  
5820 N NH1 . ARG D 114 ? 1.18239 1.27935 1.16993 -0.07158 -0.01697 0.02741  114 ARG D NH1 
5821 N NH2 . ARG D 114 ? 1.11105 1.19722 1.10848 -0.04340 -0.02371 0.05192  114 ARG D NH2 
5822 N N   . GLY D 115 ? 1.27223 1.27873 1.21959 -0.05018 0.00854  0.05660  115 GLY D N   
5823 C CA  . GLY D 115 ? 1.24639 1.23672 1.19301 -0.04151 0.01289  0.06607  115 GLY D CA  
5824 C C   . GLY D 115 ? 1.23315 1.21217 1.16701 -0.04780 0.02056  0.06136  115 GLY D C   
5825 O O   . GLY D 115 ? 1.22031 1.17733 1.15725 -0.04833 0.02763  0.06173  115 GLY D O   
5826 N N   . MET D 116 ? 1.16075 1.15702 1.07997 -0.05191 0.01917  0.05633  116 MET D N   
5827 C CA  . MET D 116 ? 1.08922 1.07673 0.99424 -0.05885 0.02653  0.05073  116 MET D CA  
5828 C C   . MET D 116 ? 1.01222 0.98123 0.91594 -0.05060 0.03244  0.06003  116 MET D C   
5829 O O   . MET D 116 ? 0.99265 0.94743 0.88809 -0.05553 0.04028  0.05620  116 MET D O   
5830 C CB  . MET D 116 ? 1.10855 1.12458 0.99912 -0.06316 0.02224  0.04382  116 MET D CB  
5831 C CG  . MET D 116 ? 1.03761 1.04944 0.91151 -0.07041 0.02899  0.03738  116 MET D CG  
5832 S SD  . MET D 116 ? 1.17924 1.23511 1.03890 -0.07455 0.02127  0.02763  116 MET D SD  
5833 C CE  . MET D 116 ? 1.13198 1.17995 0.97156 -0.07712 0.02884  0.02550  116 MET D CE  
5834 N N   . SER D 117 ? 0.98951 0.95753 0.90060 -0.03879 0.03016  0.07145  117 SER D N   
5835 C CA  . SER D 117 ? 0.96014 0.90933 0.87321 -0.03248 0.03749  0.07936  117 SER D CA  
5836 C C   . SER D 117 ? 1.00517 0.93530 0.93020 -0.03586 0.04376  0.07630  117 SER D C   
5837 O O   . SER D 117 ? 0.97752 0.89457 0.90351 -0.03366 0.05130  0.07894  117 SER D O   
5838 C CB  . SER D 117 ? 0.98718 0.93562 0.90763 -0.02147 0.03577  0.09028  117 SER D CB  
5839 O OG  . SER D 117 ? 1.05202 1.01903 0.96239 -0.01429 0.02908  0.09459  117 SER D OG  
5840 N N   . PHE D 118 ? 1.01793 0.94753 0.95170 -0.03995 0.04107  0.07091  118 PHE D N   
5841 C CA  . PHE D 118 ? 0.97937 0.89511 0.92662 -0.03829 0.04472  0.07014  118 PHE D CA  
5842 C C   . PHE D 118 ? 0.95974 0.86275 0.89945 -0.04424 0.05062  0.06186  118 PHE D C   
5843 O O   . PHE D 118 ? 0.92566 0.81562 0.86653 -0.04123 0.05777  0.06146  118 PHE D O   
5844 C CB  . PHE D 118 ? 0.98924 0.91158 0.95113 -0.03521 0.03779  0.07229  118 PHE D CB  
5845 C CG  . PHE D 118 ? 0.97182 0.88420 0.94702 -0.03219 0.04024  0.07106  118 PHE D CG  
5846 C CD1 . PHE D 118 ? 0.96199 0.87158 0.94989 -0.02634 0.04343  0.07483  118 PHE D CD1 
5847 C CD2 . PHE D 118 ? 0.95871 0.86468 0.93197 -0.03517 0.04070  0.06523  118 PHE D CD2 
5848 C CE1 . PHE D 118 ? 0.93337 0.83954 0.93356 -0.02244 0.04505  0.07243  118 PHE D CE1 
5849 C CE2 . PHE D 118 ? 0.98135 0.87937 0.96421 -0.02951 0.04293  0.06466  118 PHE D CE2 
5850 C CZ  . PHE D 118 ? 0.98964 0.89049 0.98683 -0.02259 0.04418  0.06805  118 PHE D CZ  
5851 N N   . ASP D 119 ? 0.98180 0.88780 0.91277 -0.05251 0.04909  0.05467  119 ASP D N   
5852 C CA  . ASP D 119 ? 0.95939 0.84732 0.88057 -0.05812 0.05722  0.04690  119 ASP D CA  
5853 C C   . ASP D 119 ? 0.94681 0.82516 0.85129 -0.06293 0.06573  0.04261  119 ASP D C   
5854 O O   . ASP D 119 ? 0.95571 0.81587 0.85711 -0.05879 0.07410  0.04258  119 ASP D O   
5855 C CB  . ASP D 119 ? 1.06715 0.95912 0.98337 -0.06776 0.05542  0.03920  119 ASP D CB  
5856 C CG  . ASP D 119 ? 1.08004 0.97372 1.01114 -0.06264 0.04989  0.04247  119 ASP D CG  
5857 O OD1 . ASP D 119 ? 1.05651 0.93873 0.99668 -0.05313 0.05165  0.04720  119 ASP D OD1 
5858 O OD2 . ASP D 119 ? 1.12098 1.03013 1.05510 -0.06773 0.04357  0.03980  119 ASP D OD2 
5859 N N   . PHE D 120 ? 0.96227 0.85445 0.85538 -0.07069 0.06376  0.03864  120 PHE D N   
5860 C CA  . PHE D 120 ? 0.92424 0.80757 0.80040 -0.07619 0.07216  0.03363  120 PHE D CA  
5861 C C   . PHE D 120 ? 0.87542 0.74879 0.75413 -0.06709 0.07689  0.04069  120 PHE D C   
5862 O O   . PHE D 120 ? 0.87614 0.73188 0.74401 -0.06889 0.08688  0.03672  120 PHE D O   
5863 C CB  . PHE D 120 ? 0.91857 0.82437 0.78292 -0.08470 0.06787  0.02806  120 PHE D CB  
5864 C CG  . PHE D 120 ? 1.02057 0.93031 0.87471 -0.09977 0.07043  0.01442  120 PHE D CG  
5865 C CD1 . PHE D 120 ? 1.06290 0.94977 0.90128 -0.10986 0.08339  0.00466  120 PHE D CD1 
5866 C CD2 . PHE D 120 ? 1.07051 1.00631 0.92956 -0.10449 0.06152  0.01033  120 PHE D CD2 
5867 C CE1 . PHE D 120 ? 1.09938 0.98667 0.92677 -0.12622 0.08873  -0.00959 120 PHE D CE1 
5868 C CE2 . PHE D 120 ? 1.11691 1.05799 0.96697 -0.12091 0.06559  -0.00456 120 PHE D CE2 
5869 C CZ  . PHE D 120 ? 1.14089 1.05656 0.97481 -0.13276 0.07986  -0.01490 120 PHE D CZ  
5870 N N   . PRO D 121 ? 0.90073 0.78308 0.79190 -0.05802 0.07197  0.05017  121 PRO D N   
5871 C CA  . PRO D 121 ? 0.87693 0.74917 0.77203 -0.05117 0.07866  0.05485  121 PRO D CA  
5872 C C   . PRO D 121 ? 0.90755 0.76439 0.80977 -0.04632 0.08506  0.05303  121 PRO D C   
5873 O O   . PRO D 121 ? 0.87640 0.72326 0.77468 -0.04355 0.09341  0.05226  121 PRO D O   
5874 C CB  . PRO D 121 ? 0.85164 0.73464 0.76005 -0.04404 0.07329  0.06399  121 PRO D CB  
5875 C CG  . PRO D 121 ? 0.87018 0.76944 0.77261 -0.04633 0.06468  0.06493  121 PRO D CG  
5876 C CD  . PRO D 121 ? 0.89597 0.79749 0.79488 -0.05419 0.06206  0.05638  121 PRO D CD  
5877 N N   . ILE D 122 ? 0.85715 0.71303 0.76888 -0.04385 0.08145  0.05246  122 ILE D N   
5878 C CA  . ILE D 122 ? 0.84747 0.69019 0.76325 -0.03641 0.08708  0.05101  122 ILE D CA  
5879 C C   . ILE D 122 ? 0.84548 0.66726 0.74039 -0.04076 0.09649  0.04411  122 ILE D C   
5880 O O   . ILE D 122 ? 0.85160 0.65867 0.74197 -0.03298 0.10504  0.04326  122 ILE D O   
5881 C CB  . ILE D 122 ? 0.87653 0.72532 0.80787 -0.03113 0.08021  0.05323  122 ILE D CB  
5882 C CG1 . ILE D 122 ? 0.83150 0.69698 0.78308 -0.02653 0.07399  0.05905  122 ILE D CG1 
5883 C CG2 . ILE D 122 ? 0.85087 0.68763 0.78301 -0.02132 0.08567  0.05180  122 ILE D CG2 
5884 C CD1 . ILE D 122 ? 0.83802 0.71068 0.80324 -0.02341 0.06668  0.06058  122 ILE D CD1 
5885 N N   . LEU D 123 ? 0.86271 0.68297 0.74391 -0.05294 0.09620  0.03834  123 LEU D N   
5886 C CA  . LEU D 123 ? 0.86084 0.65806 0.71982 -0.05993 0.10790  0.03015  123 LEU D CA  
5887 C C   . LEU D 123 ? 0.92659 0.71454 0.77347 -0.06006 0.11670  0.02861  123 LEU D C   
5888 O O   . LEU D 123 ? 0.97731 0.74227 0.81273 -0.05475 0.12821  0.02680  123 LEU D O   
5889 C CB  . LEU D 123 ? 0.91434 0.71729 0.76258 -0.07612 0.10636  0.02167  123 LEU D CB  
5890 C CG  . LEU D 123 ? 0.98656 0.76437 0.81031 -0.08793 0.12050  0.01045  123 LEU D CG  
5891 C CD1 . LEU D 123 ? 0.95036 0.69903 0.76772 -0.08068 0.12991  0.01091  123 LEU D CD1 
5892 C CD2 . LEU D 123 ? 0.97908 0.77260 0.79608 -0.10633 0.11778  -0.00016 123 LEU D CD2 
5893 N N   . VAL D 124 ? 0.94024 0.74546 0.78865 -0.06420 0.11181  0.03015  124 VAL D N   
5894 C CA  . VAL D 124 ? 0.90765 0.70543 0.74328 -0.06583 0.11994  0.02822  124 VAL D CA  
5895 C C   . VAL D 124 ? 0.94403 0.73441 0.78858 -0.05213 0.12520  0.03372  124 VAL D C   
5896 O O   . VAL D 124 ? 0.95878 0.73261 0.79055 -0.05036 0.13620  0.03082  124 VAL D O   
5897 C CB  . VAL D 124 ? 0.94199 0.76127 0.77591 -0.07177 0.11292  0.02943  124 VAL D CB  
5898 C CG1 . VAL D 124 ? 0.98363 0.79614 0.80493 -0.07249 0.12105  0.02842  124 VAL D CG1 
5899 C CG2 . VAL D 124 ? 0.91761 0.74836 0.74134 -0.08505 0.10869  0.02128  124 VAL D CG2 
5900 N N   . ASP D 125 ? 0.85977 0.66351 0.72628 -0.04254 0.11825  0.04057  125 ASP D N   
5901 C CA  . ASP D 125 ? 0.88612 0.68890 0.76300 -0.03056 0.12338  0.04340  125 ASP D CA  
5902 C C   . ASP D 125 ? 0.96134 0.74496 0.83004 -0.02146 0.13213  0.04055  125 ASP D C   
5903 O O   . ASP D 125 ? 0.93745 0.71576 0.80476 -0.01236 0.14020  0.04028  125 ASP D O   
5904 C CB  . ASP D 125 ? 0.84515 0.66753 0.74727 -0.02416 0.11529  0.04887  125 ASP D CB  
5905 C CG  . ASP D 125 ? 0.89414 0.72302 0.80889 -0.01493 0.12080  0.04959  125 ASP D CG  
5906 O OD1 . ASP D 125 ? 0.94963 0.78165 0.86317 -0.01807 0.12484  0.05045  125 ASP D OD1 
5907 O OD2 . ASP D 125 ? 0.84834 0.68055 0.77346 -0.00420 0.12169  0.04867  125 ASP D OD2 
5908 N N   . LEU D 126 ? 0.97771 0.75070 0.84014 -0.02245 0.13134  0.03870  126 LEU D N   
5909 C CA  . LEU D 126 ? 0.98393 0.73307 0.83268 -0.01265 0.14155  0.03684  126 LEU D CA  
5910 C C   . LEU D 126 ? 1.04588 0.76823 0.86683 -0.01925 0.15549  0.03098  126 LEU D C   
5911 O O   . LEU D 126 ? 1.07668 0.78042 0.88580 -0.00773 0.16694  0.03078  126 LEU D O   
5912 C CB  . LEU D 126 ? 0.97235 0.71526 0.82033 -0.01304 0.13801  0.03667  126 LEU D CB  
5913 C CG  . LEU D 126 ? 0.91004 0.67584 0.78344 -0.00497 0.12570  0.04186  126 LEU D CG  
5914 C CD1 . LEU D 126 ? 0.86693 0.62676 0.73747 -0.00971 0.12194  0.04092  126 LEU D CD1 
5915 C CD2 . LEU D 126 ? 0.87048 0.64116 0.75352 0.01483  0.12791  0.04479  126 LEU D CD2 
5916 N N   . ILE D 127 ? 1.02542 0.74689 0.83507 -0.03726 0.15509  0.02552  127 ILE D N   
5917 C CA  . ILE D 127 ? 1.06626 0.76583 0.85035 -0.04650 0.16828  0.01824  127 ILE D CA  
5918 C C   . ILE D 127 ? 1.06203 0.76457 0.84703 -0.03986 0.17261  0.02051  127 ILE D C   
5919 O O   . ILE D 127 ? 1.09916 0.77777 0.86589 -0.03577 0.18652  0.01762  127 ILE D O   
5920 C CB  . ILE D 127 ? 1.07103 0.77974 0.84687 -0.06758 0.16452  0.01058  127 ILE D CB  
5921 C CG1 . ILE D 127 ? 1.04451 0.74826 0.81792 -0.07501 0.16302  0.00647  127 ILE D CG1 
5922 C CG2 . ILE D 127 ? 1.03254 0.72451 0.78393 -0.07889 0.17720  0.00179  127 ILE D CG2 
5923 C CD1 . ILE D 127 ? 1.06644 0.79172 0.83931 -0.09386 0.15534  -0.00099 127 ILE D CD1 
5924 N N   . ARG D 128 ? 1.07405 0.80398 0.87903 -0.03847 0.16221  0.02568  128 ARG D N   
5925 C CA  . ARG D 128 ? 1.11791 0.85236 0.92655 -0.03177 0.16671  0.02799  128 ARG D CA  
5926 C C   . ARG D 128 ? 1.13558 0.86314 0.94937 -0.01324 0.17375  0.03033  128 ARG D C   
5927 O O   . ARG D 128 ? 1.15904 0.88425 0.96991 -0.00741 0.18162  0.02996  128 ARG D O   
5928 C CB  . ARG D 128 ? 1.09228 0.85466 0.92165 -0.03298 0.15589  0.03349  128 ARG D CB  
5929 C CG  . ARG D 128 ? 1.11202 0.88367 0.93314 -0.04679 0.15076  0.03240  128 ARG D CG  
5930 C CD  . ARG D 128 ? 1.08234 0.87613 0.92240 -0.04444 0.14148  0.03958  128 ARG D CD  
5931 N NE  . ARG D 128 ? 1.10335 0.90875 0.93575 -0.05353 0.13469  0.04044  128 ARG D NE  
5932 C CZ  . ARG D 128 ? 1.10473 0.92648 0.94928 -0.05197 0.12541  0.04678  128 ARG D CZ  
5933 N NH1 . ARG D 128 ? 1.01934 0.84710 0.88497 -0.04456 0.12189  0.05152  128 ARG D NH1 
5934 N NH2 . ARG D 128 ? 1.12771 0.96064 0.96193 -0.05735 0.11981  0.04788  128 ARG D NH2 
5935 N N   . ASP D 129 ? 1.18567 0.91290 1.00742 -0.00263 0.17078  0.03265  129 ASP D N   
5936 C CA  . ASP D 129 ? 1.18079 0.90699 1.00709 0.01765  0.17654  0.03463  129 ASP D CA  
5937 C C   . ASP D 129 ? 1.20404 0.89552 1.00123 0.02433  0.19265  0.03177  129 ASP D C   
5938 O O   . ASP D 129 ? 1.23904 0.92834 1.03485 0.04229  0.20007  0.03304  129 ASP D O   
5939 C CB  . ASP D 129 ? 1.18838 0.92796 1.03167 0.02866  0.16793  0.03803  129 ASP D CB  
5940 C CG  . ASP D 129 ? 1.18520 0.95946 1.05901 0.02525  0.15449  0.04057  129 ASP D CG  
5941 O OD1 . ASP D 129 ? 1.16911 0.95990 1.05491 0.02380  0.15465  0.04043  129 ASP D OD1 
5942 O OD2 . ASP D 129 ? 1.15020 0.93285 1.03450 0.02308  0.14499  0.04242  129 ASP D OD2 
5943 N N   . ILE D 130 ? 1.17564 0.84068 0.94898 0.01012  0.19915  0.02715  130 ILE D N   
5944 C CA  . ILE D 130 ? 1.17948 0.80591 0.92095 0.01265  0.21765  0.02310  130 ILE D CA  
5945 C C   . ILE D 130 ? 1.21055 0.83638 0.94641 0.01295  0.22521  0.02130  130 ILE D C   
5946 O O   . ILE D 130 ? 1.18420 0.78895 0.90407 0.02717  0.23901  0.02140  130 ILE D O   
5947 C CB  . ILE D 130 ? 1.11254 0.71445 0.83150 -0.00773 0.22360  0.01578  130 ILE D CB  
5948 C CG1 . ILE D 130 ? 1.14666 0.74129 0.86620 -0.00478 0.22065  0.01748  130 ILE D CG1 
5949 C CG2 . ILE D 130 ? 1.19243 0.75388 0.87771 -0.00953 0.24438  0.00993  130 ILE D CG2 
5950 C CD1 . ILE D 130 ? 1.22874 0.81074 0.93420 -0.02775 0.22318  0.00913  130 ILE D CD1 
5951 N N   . GLN D 131 ? 1.22770 0.87613 0.97529 -0.00146 0.21681  0.02007  131 GLN D N   
5952 C CA  . GLN D 131 ? 1.16546 0.81617 0.90908 -0.00316 0.22280  0.01848  131 GLN D CA  
5953 C C   . GLN D 131 ? 1.16743 0.84227 0.93392 0.01333  0.21990  0.02342  131 GLN D C   
5954 O O   . GLN D 131 ? 1.18536 0.85557 0.94556 0.01938  0.22953  0.02220  131 GLN D O   
5955 C CB  . GLN D 131 ? 1.20681 0.87242 0.95178 -0.02348 0.21518  0.01578  131 GLN D CB  
5956 C CG  . GLN D 131 ? 1.26323 0.91210 0.98574 -0.04247 0.21867  0.00769  131 GLN D CG  
5957 C CD  . GLN D 131 ? 1.35146 1.01643 1.07065 -0.05862 0.21378  0.00417  131 GLN D CD  
5958 O OE1 . GLN D 131 ? 1.36045 1.04460 1.09251 -0.05490 0.20867  0.00914  131 GLN D OE1 
5959 N NE2 . GLN D 131 ? 1.34980 1.00733 1.05035 -0.07641 0.21651  -0.00514 131 GLN D NE2 
5960 N N   . ARG D 132 ? 1.17499 0.87737 0.96852 0.01920  0.20734  0.02777  132 ARG D N   
5961 C CA  . ARG D 132 ? 1.18009 0.90745 0.99608 0.03482  0.20602  0.02996  132 ARG D CA  
5962 C C   . ARG D 132 ? 1.16614 0.88212 0.97327 0.05738  0.21578  0.03010  132 ARG D C   
5963 O O   . ARG D 132 ? 1.16793 0.90239 0.98730 0.07127  0.21887  0.02966  132 ARG D O   
5964 C CB  . ARG D 132 ? 1.15098 0.90910 0.99640 0.03447  0.19156  0.03292  132 ARG D CB  
5965 C CG  . ARG D 132 ? 1.19393 0.97108 1.05365 0.02005  0.18494  0.03385  132 ARG D CG  
5966 C CD  . ARG D 132 ? 1.14017 0.94534 1.02843 0.02130  0.17379  0.03609  132 ARG D CD  
5967 N NE  . ARG D 132 ? 1.14061 0.94149 1.02786 0.01532  0.16429  0.03844  132 ARG D NE  
5968 C CZ  . ARG D 132 ? 1.13094 0.93406 1.01792 0.00127  0.15716  0.04060  132 ARG D CZ  
5969 N NH1 . ARG D 132 ? 1.10277 0.91189 0.99041 -0.00724 0.15814  0.04174  132 ARG D NH1 
5970 N NH2 . ARG D 132 ? 1.08849 0.88798 0.97335 -0.00315 0.14940  0.04181  132 ARG D NH2 
5971 N N   . LEU D 133 ? 1.16447 0.85096 0.94977 0.06194  0.22140  0.03050  133 LEU D N   
5972 C CA  . LEU D 133 ? 1.19451 0.86048 0.96190 0.08484  0.23399  0.03161  133 LEU D CA  
5973 C C   . LEU D 133 ? 1.22223 0.86253 0.96520 0.08629  0.25051  0.02868  133 LEU D C   
5974 O O   . LEU D 133 ? 1.14354 0.77431 0.87547 0.10866  0.26141  0.02997  133 LEU D O   
5975 C CB  . LEU D 133 ? 1.16116 0.79709 0.90852 0.08654  0.23729  0.03302  133 LEU D CB  
5976 C CG  . LEU D 133 ? 1.17924 0.78844 0.90359 0.11259  0.25074  0.03600  133 LEU D CG  
5977 C CD1 . LEU D 133 ? 1.12032 0.76686 0.86907 0.13770  0.24230  0.03971  133 LEU D CD1 
5978 C CD2 . LEU D 133 ? 1.18345 0.75645 0.88421 0.10735  0.25630  0.03640  133 LEU D CD2 
5979 N N   . ASN D 134 ? 1.22183 0.85295 0.95609 0.06408  0.25238  0.02470  134 ASN D N   
5980 C CA  . ASN D 134 ? 1.19483 0.80119 0.90529 0.06141  0.26768  0.02085  134 ASN D CA  
5981 C C   . ASN D 134 ? 1.23770 0.87171 0.96593 0.06284  0.26609  0.02045  134 ASN D C   
5982 O O   . ASN D 134 ? 1.30918 0.92676 1.02023 0.05953  0.27781  0.01716  134 ASN D O   
5983 C CB  . ASN D 134 ? 1.23634 0.81933 0.92599 0.03531  0.27075  0.01506  134 ASN D CB  
5984 C CG  . ASN D 134 ? 1.29154 0.83135 0.94462 0.03358  0.29156  0.00968  134 ASN D CG  
5985 O OD1 . ASN D 134 ? 1.30335 0.82555 0.94355 0.05397  0.30475  0.01162  134 ASN D OD1 
5986 N ND2 . ASN D 134 ? 1.28032 0.80375 0.91564 0.00936  0.29519  0.00213  134 ASN D ND2 
5987 N N   . GLY D 135 ? 1.23586 0.91032 0.99727 0.06660  0.25322  0.02290  135 GLY D N   
5988 C CA  . GLY D 135 ? 1.27019 0.97130 1.04957 0.06621  0.25301  0.02163  135 GLY D CA  
5989 C C   . GLY D 135 ? 1.28994 0.99692 1.07207 0.04303  0.24809  0.02059  135 GLY D C   
5990 O O   . GLY D 135 ? 1.26372 0.98839 1.05750 0.04100  0.24985  0.01962  135 GLY D O   
5991 N N   . VAL D 136 ? 1.29411 0.98755 1.06474 0.02638  0.24265  0.02048  136 VAL D N   
5992 C CA  . VAL D 136 ? 1.28835 0.98956 1.05942 0.00691  0.23665  0.02018  136 VAL D CA  
5993 C C   . VAL D 136 ? 1.28204 1.01628 1.08323 0.00602  0.22514  0.02419  136 VAL D C   
5994 O O   . VAL D 136 ? 1.29361 1.04210 1.11293 0.01224  0.21662  0.02657  136 VAL D O   
5995 C CB  . VAL D 136 ? 1.28377 0.96902 1.03774 -0.00810 0.23247  0.01805  136 VAL D CB  
5996 C CG1 . VAL D 136 ? 1.30591 1.00335 1.05909 -0.02517 0.22508  0.01799  136 VAL D CG1 
5997 C CG2 . VAL D 136 ? 1.30065 0.94989 1.02330 -0.00941 0.24688  0.01225  136 VAL D CG2 
5998 N N   . SER D 137 ? 1.30966 1.05415 1.11453 -0.00211 0.22609  0.02471  137 SER D N   
5999 C CA  . SER D 137 ? 1.25408 1.02456 1.08385 -0.00437 0.21918  0.02796  137 SER D CA  
6000 C C   . SER D 137 ? 1.26476 1.03937 1.09628 -0.01523 0.20693  0.03199  137 SER D C   
6001 O O   . SER D 137 ? 1.28625 1.04749 1.09907 -0.02348 0.20386  0.03143  137 SER D O   
6002 C CB  . SER D 137 ? 1.29129 1.06604 1.12008 -0.00889 0.22733  0.02736  137 SER D CB  
6003 O OG  . SER D 137 ? 1.36610 1.14120 1.19600 0.00203  0.23852  0.02325  137 SER D OG  
6004 N N   . GLU D 138 ? 1.23037 1.02505 1.08472 -0.01527 0.20071  0.03517  138 GLU D N   
6005 C CA  . GLU D 138 ? 1.20412 1.00368 1.06122 -0.02307 0.18969  0.03987  138 GLU D CA  
6006 C C   . GLU D 138 ? 1.21161 1.00256 1.04734 -0.03350 0.18933  0.04213  138 GLU D C   
6007 O O   . GLU D 138 ? 1.14674 0.93663 0.97357 -0.03909 0.18070  0.04376  138 GLU D O   
6008 C CB  . GLU D 138 ? 1.21032 1.02904 1.09241 -0.02223 0.18727  0.04233  138 GLU D CB  
6009 C CG  . GLU D 138 ? 1.20374 1.03707 1.10820 -0.01343 0.18298  0.04006  138 GLU D CG  
6010 C CD  . GLU D 138 ? 1.26979 1.10025 1.17322 -0.01388 0.17156  0.04267  138 GLU D CD  
6011 O OE1 . GLU D 138 ? 1.29394 1.12052 1.18935 -0.02213 0.16541  0.04693  138 GLU D OE1 
6012 O OE2 . GLU D 138 ? 1.30290 1.13539 1.21229 -0.00498 0.16909  0.04052  138 GLU D OE2 
6013 N N   . ASN D 139 ? 1.21757 1.00522 1.04529 -0.03561 0.19849  0.04199  139 ASN D N   
6014 C CA  . ASN D 139 ? 1.23844 1.01897 1.04319 -0.04353 0.19912  0.04379  139 ASN D CA  
6015 C C   . ASN D 139 ? 1.23713 1.00359 1.01832 -0.04784 0.20186  0.03776  139 ASN D C   
6016 O O   . ASN D 139 ? 1.22225 0.98744 0.98421 -0.05534 0.19891  0.03741  139 ASN D O   
6017 C CB  . ASN D 139 ? 1.23620 1.01652 1.03975 -0.04404 0.20935  0.04577  139 ASN D CB  
6018 C CG  . ASN D 139 ? 1.26765 1.04445 1.07495 -0.03940 0.22105  0.04014  139 ASN D CG  
6019 O OD1 . ASN D 139 ? 1.33823 1.10925 1.14377 -0.03476 0.22228  0.03539  139 ASN D OD1 
6020 N ND2 . ASN D 139 ? 1.32208 1.10170 1.13386 -0.03984 0.23084  0.04064  139 ASN D ND2 
6021 N N   . GLU D 140 ? 1.24921 1.00533 1.03011 -0.04284 0.20833  0.03249  140 GLU D N   
6022 C CA  . GLU D 140 ? 1.28174 1.01960 1.03880 -0.04785 0.21362  0.02577  140 GLU D CA  
6023 C C   . GLU D 140 ? 1.27913 1.01278 1.03175 -0.05223 0.20648  0.02291  140 GLU D C   
6024 O O   . GLU D 140 ? 1.29433 1.01270 1.02553 -0.06001 0.21151  0.01583  140 GLU D O   
6025 C CB  . GLU D 140 ? 1.32547 1.04908 1.07964 -0.03891 0.22652  0.02189  140 GLU D CB  
6026 C CG  . GLU D 140 ? 1.40556 1.13034 1.15863 -0.03666 0.23631  0.02201  140 GLU D CG  
6027 C CD  . GLU D 140 ? 1.48324 1.19610 1.23381 -0.02536 0.24883  0.01812  140 GLU D CD  
6028 O OE1 . GLU D 140 ? 1.41492 1.11840 1.16514 -0.01719 0.24966  0.01662  140 GLU D OE1 
6029 O OE2 . GLU D 140 ? 1.52786 1.24017 1.27542 -0.02356 0.25846  0.01690  140 GLU D OE2 
6030 N N   . LEU D 141 ? 1.27229 1.01826 1.04382 -0.04859 0.19625  0.02718  141 LEU D N   
6031 C CA  . LEU D 141 ? 1.29556 1.03722 1.06328 -0.05286 0.19044  0.02417  141 LEU D CA  
6032 C C   . LEU D 141 ? 1.39672 1.14250 1.14697 -0.06708 0.18567  0.01984  141 LEU D C   
6033 O O   . LEU D 141 ? 1.41233 1.17244 1.16040 -0.07049 0.18071  0.02302  141 LEU D O   
6034 C CB  . LEU D 141 ? 1.25148 1.00837 1.04313 -0.04683 0.17945  0.02991  141 LEU D CB  
6035 C CG  . LEU D 141 ? 1.21574 0.97386 1.02610 -0.03285 0.18146  0.03207  141 LEU D CG  
6036 C CD1 . LEU D 141 ? 1.14382 0.92076 0.97735 -0.02996 0.16983  0.03718  141 LEU D CD1 
6037 C CD2 . LEU D 141 ? 1.20638 0.94334 1.00405 -0.02837 0.18821  0.02761  141 LEU D CD2 
6038 N N   . ASP D 142 ? 1.52233 1.25558 1.25851 -0.07506 0.18840  0.01181  142 ASP D N   
6039 C CA  . ASP D 142 ? 1.53728 1.28115 1.26096 -0.08948 0.18234  0.00525  142 ASP D CA  
6040 C C   . ASP D 142 ? 1.53800 1.26791 1.25521 -0.09618 0.18544  -0.00254 142 ASP D C   
6041 O O   . ASP D 142 ? 1.55956 1.26258 1.25992 -0.09914 0.19934  -0.00962 142 ASP D O   
6042 C CB  . ASP D 142 ? 1.56508 1.30734 1.26636 -0.09927 0.18881  -0.00177 142 ASP D CB  
6043 C CG  . ASP D 142 ? 1.60118 1.36368 1.29166 -0.11312 0.18087  -0.00946 142 ASP D CG  
6044 O OD1 . ASP D 142 ? 1.60415 1.39241 1.30227 -0.11009 0.16853  -0.00309 142 ASP D OD1 
6045 O OD2 . ASP D 142 ? 1.64969 1.40294 1.32376 -0.12668 0.18760  -0.02236 142 ASP D OD2 
6046 N N   . THR D 143 ? 1.42918 1.17514 1.15779 -0.09864 0.17401  -0.00137 143 THR D N   
6047 C CA  . THR D 143 ? 1.34245 1.07490 1.06679 -0.10447 0.17725  -0.00791 143 THR D CA  
6048 C C   . THR D 143 ? 1.33382 1.08368 1.04984 -0.12185 0.17176  -0.01824 143 THR D C   
6049 O O   . THR D 143 ? 1.33995 1.08817 1.05831 -0.12730 0.17035  -0.02246 143 THR D O   
6050 C CB  . THR D 143 ? 1.27021 1.00491 1.01645 -0.09141 0.17019  0.00128  143 THR D CB  
6051 O OG1 . THR D 143 ? 1.25398 1.01880 1.01825 -0.08982 0.15442  0.00785  143 THR D OG1 
6052 C CG2 . THR D 143 ? 1.24702 0.97060 1.00212 -0.07449 0.17581  0.00907  143 THR D CG2 
6053 N N   . PHE D 144 ? 1.37140 1.13967 1.07721 -0.13038 0.16907  -0.02313 144 PHE D N   
6054 C CA  . PHE D 144 ? 1.38349 1.17508 1.08068 -0.14693 0.16391  -0.03530 144 PHE D CA  
6055 C C   . PHE D 144 ? 1.40193 1.17163 1.08464 -0.16274 0.17676  -0.05018 144 PHE D C   
6056 O O   . PHE D 144 ? 1.36198 1.14423 1.04874 -0.17209 0.17226  -0.05695 144 PHE D O   
6057 C CB  . PHE D 144 ? 1.42768 1.23623 1.11019 -0.15261 0.16350  -0.04005 144 PHE D CB  
6058 C CG  . PHE D 144 ? 1.39127 1.23046 1.06347 -0.16938 0.15832  -0.05480 144 PHE D CG  
6059 C CD1 . PHE D 144 ? 1.37177 1.25009 1.05497 -0.16581 0.14155  -0.05136 144 PHE D CD1 
6060 C CD2 . PHE D 144 ? 1.40342 1.23390 1.05412 -0.18843 0.17098  -0.07297 144 PHE D CD2 
6061 C CE1 . PHE D 144 ? 1.36900 1.28212 1.04349 -0.17984 0.13609  -0.06606 144 PHE D CE1 
6062 C CE2 . PHE D 144 ? 1.42706 1.29147 1.06948 -0.20517 0.16634  -0.08906 144 PHE D CE2 
6063 C CZ  . PHE D 144 ? 1.39727 1.30566 1.05234 -0.20029 0.14814  -0.08571 144 PHE D CZ  
6064 N N   . LYS D 145 ? 1.48615 1.22033 1.15107 -0.16525 0.19440  -0.05514 145 LYS D N   
6065 C CA  . LYS D 145 ? 1.46439 1.16927 1.10912 -0.18091 0.21152  -0.06988 145 LYS D CA  
6066 C C   . LYS D 145 ? 1.45476 1.13276 1.10423 -0.17359 0.21692  -0.06525 145 LYS D C   
6067 O O   . LYS D 145 ? 1.49372 1.14673 1.12617 -0.18716 0.23133  -0.07721 145 LYS D O   
6068 C CB  . LYS D 145 ? 1.50782 1.18175 1.12929 -0.18381 0.22963  -0.07549 145 LYS D CB  
6069 C CG  . LYS D 145 ? 1.51527 1.16971 1.14282 -0.16110 0.23265  -0.06014 145 LYS D CG  
6070 C CD  . LYS D 145 ? 1.67368 1.30696 1.27936 -0.16439 0.24780  -0.06586 145 LYS D CD  
6071 C CE  . LYS D 145 ? 1.61380 1.23626 1.22762 -0.14225 0.24956  -0.05169 145 LYS D CE  
6072 N NZ  . LYS D 145 ? 1.56060 1.16460 1.15313 -0.14596 0.26395  -0.05765 145 LYS D NZ  
6073 N N   . LEU D 146 ? 1.37018 1.05239 1.04087 -0.15331 0.20680  -0.04916 146 LEU D N   
6074 C CA  . LEU D 146 ? 1.29088 0.94875 0.96503 -0.14369 0.21160  -0.04403 146 LEU D CA  
6075 C C   . LEU D 146 ? 1.31635 0.99834 1.00892 -0.14589 0.19744  -0.04228 146 LEU D C   
6076 O O   . LEU D 146 ? 1.36094 1.02577 1.05765 -0.13713 0.19975  -0.03730 146 LEU D O   
6077 C CB  . LEU D 146 ? 1.19762 0.84444 0.88268 -0.11907 0.21129  -0.02907 146 LEU D CB  
6078 C CG  . LEU D 146 ? 1.19463 0.81727 0.86407 -0.11207 0.22539  -0.02868 146 LEU D CG  
6079 C CD1 . LEU D 146 ? 1.16100 0.78493 0.84734 -0.08765 0.22178  -0.01480 146 LEU D CD1 
6080 C CD2 . LEU D 146 ? 1.24081 0.81869 0.87946 -0.11887 0.24805  -0.03850 146 LEU D CD2 
6081 N N   . GLU D 147 ? 1.27518 0.99936 0.97793 -0.15696 0.18238  -0.04667 147 GLU D N   
6082 C CA  . GLU D 147 ? 1.27853 1.02720 1.00247 -0.15309 0.16724  -0.04109 147 GLU D CA  
6083 C C   . GLU D 147 ? 1.30431 1.05928 1.02164 -0.17278 0.16997  -0.05583 147 GLU D C   
6084 O O   . GLU D 147 ? 1.29277 1.05371 0.99425 -0.19207 0.17692  -0.07158 147 GLU D O   
6085 C CB  . GLU D 147 ? 1.26613 1.05570 1.00753 -0.14628 0.14862  -0.03280 147 GLU D CB  
6086 C CG  . GLU D 147 ? 1.28434 1.07017 1.03494 -0.12808 0.14600  -0.01847 147 GLU D CG  
6087 C CD  . GLU D 147 ? 1.29673 1.11630 1.06353 -0.11953 0.12973  -0.00831 147 GLU D CD  
6088 O OE1 . GLU D 147 ? 1.27541 1.12317 1.04772 -0.12429 0.11858  -0.01042 147 GLU D OE1 
6089 O OE2 . GLU D 147 ? 1.21226 1.02911 0.98467 -0.10773 0.12954  0.00150  147 GLU D OE2 
6090 N N   . PRO D 148 ? 1.35386 1.11019 1.08383 -0.16913 0.16469  -0.05205 148 PRO D N   
6091 C CA  . PRO D 148 ? 1.33028 1.09235 1.05479 -0.18858 0.16855  -0.06675 148 PRO D CA  
6092 C C   . PRO D 148 ? 1.33342 1.14323 1.06245 -0.20336 0.15731  -0.07793 148 PRO D C   
6093 O O   . PRO D 148 ? 1.36093 1.17687 1.07938 -0.22517 0.16505  -0.09613 148 PRO D O   
6094 C CB  . PRO D 148 ? 1.35097 1.11109 1.09256 -0.17680 0.16115  -0.05655 148 PRO D CB  
6095 C CG  . PRO D 148 ? 1.26550 1.03974 1.02742 -0.15452 0.14653  -0.03845 148 PRO D CG  
6096 C CD  . PRO D 148 ? 1.28555 1.04232 1.03642 -0.14822 0.15452  -0.03534 148 PRO D CD  
6097 N N   . CYS D 149 ? 1.40262 1.24740 1.14631 -0.19171 0.13996  -0.06808 149 CYS D N   
6098 C CA  . CYS D 149 ? 1.39942 1.29058 1.14342 -0.20145 0.12958  -0.07753 149 CYS D CA  
6099 C C   . CYS D 149 ? 1.38350 1.28796 1.12837 -0.18752 0.12141  -0.06639 149 CYS D C   
6100 O O   . CYS D 149 ? 1.38057 1.26935 1.13476 -0.16905 0.11844  -0.04947 149 CYS D O   
6101 C CB  . CYS D 149 ? 1.42212 1.35124 1.18428 -0.19993 0.11410  -0.07667 149 CYS D CB  
6102 S SG  . CYS D 149 ? 1.37646 1.31424 1.16203 -0.17179 0.09690  -0.05156 149 CYS D SG  
6103 N N   . LYS D 150 ? 1.37244 1.30691 1.10696 -0.19678 0.11850  -0.07678 150 LYS D N   
6104 C CA  . LYS D 150 ? 1.38968 1.33981 1.12356 -0.18261 0.11000  -0.06566 150 LYS D CA  
6105 C C   . LYS D 150 ? 1.36069 1.33836 1.11290 -0.16476 0.09243  -0.05058 150 LYS D C   
6106 O O   . LYS D 150 ? 1.35220 1.35176 1.11530 -0.16698 0.08444  -0.05355 150 LYS D O   
6107 C CB  . LYS D 150 ? 1.37025 1.34868 1.08685 -0.19558 0.11063  -0.08076 150 LYS D CB  
6108 C CG  . LYS D 150 ? 1.34555 1.29580 1.04231 -0.21550 0.12973  -0.09763 150 LYS D CG  
6109 C CD  . LYS D 150 ? 1.39642 1.29972 1.08715 -0.20538 0.14136  -0.08638 150 LYS D CD  
6110 C CE  . LYS D 150 ? 1.44077 1.31369 1.10834 -0.22341 0.16170  -0.10246 150 LYS D CE  
6111 N NZ  . LYS D 150 ? 1.46529 1.31111 1.12746 -0.23848 0.17559  -0.11426 150 LYS D NZ  
6112 N N   . PHE D 151 ? 1.34056 1.31511 1.09513 -0.14716 0.08788  -0.03451 151 PHE D N   
6113 C CA  . PHE D 151 ? 1.29270 1.28083 1.06330 -0.12908 0.07524  -0.01828 151 PHE D CA  
6114 C C   . PHE D 151 ? 1.27916 1.31369 1.05030 -0.12731 0.06175  -0.02154 151 PHE D C   
6115 O O   . PHE D 151 ? 1.24547 1.29154 1.03005 -0.11488 0.05204  -0.01095 151 PHE D O   
6116 C CB  . PHE D 151 ? 1.27173 1.24671 1.04141 -0.11294 0.07580  -0.00245 151 PHE D CB  
6117 C CG  . PHE D 151 ? 1.29870 1.29214 1.05037 -0.11145 0.07461  -0.00400 151 PHE D CG  
6118 C CD1 . PHE D 151 ? 1.31369 1.28992 1.05012 -0.11915 0.08566  -0.01042 151 PHE D CD1 
6119 C CD2 . PHE D 151 ? 1.31791 1.34528 1.06620 -0.10051 0.06289  0.00162  151 PHE D CD2 
6120 C CE1 . PHE D 151 ? 1.35109 1.34427 1.06990 -0.11725 0.08467  -0.01171 151 PHE D CE1 
6121 C CE2 . PHE D 151 ? 1.34939 1.39423 1.07880 -0.09684 0.06179  0.00091  151 PHE D CE2 
6122 C CZ  . PHE D 151 ? 1.36118 1.38925 1.07604 -0.10583 0.07251  -0.00598 151 PHE D CZ  
6123 N N   . TRP D 152 ? 1.31943 1.38250 1.07585 -0.13850 0.06109  -0.03622 152 TRP D N   
6124 C CA  . TRP D 152 ? 1.31794 1.43151 1.07500 -0.13694 0.04815  -0.04208 152 TRP D CA  
6125 C C   . TRP D 152 ? 1.28792 1.41700 1.05494 -0.15274 0.04732  -0.05706 152 TRP D C   
6126 O O   . TRP D 152 ? 1.27485 1.44873 1.04602 -0.15099 0.03610  -0.06239 152 TRP D O   
6127 C CB  . TRP D 152 ? 1.32876 1.47351 1.06618 -0.14125 0.04678  -0.05267 152 TRP D CB  
6128 C CG  . TRP D 152 ? 1.29368 1.42612 1.01761 -0.16455 0.06014  -0.07205 152 TRP D CG  
6129 C CD1 . TRP D 152 ? 1.30805 1.45703 1.02964 -0.18813 0.06498  -0.09507 152 TRP D CD1 
6130 C CD2 . TRP D 152 ? 1.29603 1.39765 1.00520 -0.16700 0.07162  -0.07105 152 TRP D CD2 
6131 N NE1 . TRP D 152 ? 1.34403 1.47083 1.04933 -0.20544 0.07977  -0.10837 152 TRP D NE1 
6132 C CE2 . TRP D 152 ? 1.33334 1.43181 1.03093 -0.19203 0.08341  -0.09359 152 TRP D CE2 
6133 C CE3 . TRP D 152 ? 1.34426 1.42016 1.04863 -0.15126 0.07426  -0.05409 152 TRP D CE3 
6134 C CZ2 . TRP D 152 ? 1.37491 1.44458 1.05576 -0.20032 0.09721  -0.09876 152 TRP D CZ2 
6135 C CZ3 . TRP D 152 ? 1.34167 1.39155 1.03085 -0.15958 0.08728  -0.05944 152 TRP D CZ3 
6136 C CH2 . TRP D 152 ? 1.33419 1.38081 1.01160 -0.18313 0.09827  -0.08110 152 TRP D CH2 
6137 N N   . ASN D 153 ? 1.32551 1.41862 1.09551 -0.16674 0.05952  -0.06355 153 ASN D N   
6138 C CA  . ASN D 153 ? 1.39545 1.49590 1.17417 -0.18134 0.06102  -0.07623 153 ASN D CA  
6139 C C   . ASN D 153 ? 1.35176 1.43686 1.14965 -0.16870 0.05587  -0.06166 153 ASN D C   
6140 O O   . ASN D 153 ? 1.29137 1.39078 1.09848 -0.17681 0.05359  -0.06964 153 ASN D O   
6141 C CB  . ASN D 153 ? 1.40287 1.47002 1.16964 -0.20429 0.07972  -0.09268 153 ASN D CB  
6142 C CG  . ASN D 153 ? 1.33004 1.41775 1.07846 -0.22265 0.08591  -0.11280 153 ASN D CG  
6143 O OD1 . ASN D 153 ? 1.22930 1.36902 0.97711 -0.22616 0.07579  -0.12302 153 ASN D OD1 
6144 N ND2 . ASN D 153 ? 1.35706 1.40517 1.08980 -0.23424 0.10309  -0.11947 153 ASN D ND2 
6145 N N   . GLN D 154 ? 1.26095 1.31862 1.06505 -0.15031 0.05471  -0.04193 154 GLN D N   
6146 C CA  . GLN D 154 ? 1.21668 1.26287 1.03896 -0.13793 0.04938  -0.02855 154 GLN D CA  
6147 C C   . GLN D 154 ? 1.26377 1.35224 1.09554 -0.12883 0.03442  -0.02531 154 GLN D C   
6148 O O   . GLN D 154 ? 1.28501 1.40384 1.10967 -0.12056 0.02664  -0.02317 154 GLN D O   
6149 C CB  . GLN D 154 ? 1.19186 1.20874 1.01851 -0.12076 0.05082  -0.01014 154 GLN D CB  
6150 C CG  . GLN D 154 ? 1.21340 1.19161 1.03089 -0.12537 0.06485  -0.01146 154 GLN D CG  
6151 C CD  . GLN D 154 ? 1.12030 1.08028 0.94188 -0.10902 0.06552  0.00464  154 GLN D CD  
6152 O OE1 . GLN D 154 ? 1.02865 1.00127 0.85854 -0.09540 0.05690  0.01669  154 GLN D OE1 
6153 N NE2 . GLN D 154 ? 1.13317 1.06344 0.94757 -0.11068 0.07709  0.00405  154 GLN D NE2 
6154 N N   . ARG D 155 ? 1.29837 1.38874 1.14471 -0.12893 0.03078  -0.02466 155 ARG D N   
6155 C CA  . ARG D 155 ? 1.26309 1.39247 1.11909 -0.11978 0.01737  -0.02189 155 ARG D CA  
6156 C C   . ARG D 155 ? 1.24008 1.35070 1.11307 -0.10753 0.01397  -0.00772 155 ARG D C   
6157 O O   . ARG D 155 ? 1.25550 1.32921 1.13357 -0.11021 0.02179  -0.00466 155 ARG D O   
6158 C CB  . ARG D 155 ? 1.27021 1.43566 1.12627 -0.13762 0.01593  -0.04242 155 ARG D CB  
6159 C CG  . ARG D 155 ? 1.38014 1.57176 1.21989 -0.15163 0.01888  -0.05959 155 ARG D CG  
6160 C CD  . ARG D 155 ? 1.36095 1.59222 1.19321 -0.13494 0.00704  -0.05348 155 ARG D CD  
6161 N NE  . ARG D 155 ? 1.38681 1.64895 1.20400 -0.14907 0.00903  -0.07206 155 ARG D NE  
6162 C CZ  . ARG D 155 ? 1.38711 1.63392 1.18845 -0.15147 0.01567  -0.07270 155 ARG D CZ  
6163 N NH1 . ARG D 155 ? 1.36664 1.56912 1.16511 -0.14003 0.02090  -0.05556 155 ARG D NH1 
6164 N NH2 . ARG D 155 ? 1.41332 1.69241 1.20170 -0.16621 0.01732  -0.09207 155 ARG D NH2 
6165 N N   . ASP D 156 ? 1.24263 1.37987 1.12316 -0.09292 0.00253  0.00076  156 ASP D N   
6166 C CA  . ASP D 156 ? 1.25435 1.37673 1.15009 -0.07995 -0.00117 0.01468  156 ASP D CA  
6167 C C   . ASP D 156 ? 1.30241 1.45115 1.20948 -0.08355 -0.00787 0.00792  156 ASP D C   
6168 O O   . ASP D 156 ? 1.31627 1.50764 1.22059 -0.08299 -0.01552 0.00077  156 ASP D O   
6169 C CB  . ASP D 156 ? 1.26854 1.39165 1.16196 -0.05817 -0.00620 0.03228  156 ASP D CB  
6170 C CG  . ASP D 156 ? 1.26383 1.36608 1.17200 -0.04655 -0.00734 0.04589  156 ASP D CG  
6171 O OD1 . ASP D 156 ? 1.22912 1.29775 1.14418 -0.04973 -0.00030 0.04894  156 ASP D OD1 
6172 O OD2 . ASP D 156 ? 1.23728 1.35723 1.14910 -0.03315 -0.01480 0.05356  156 ASP D OD2 
6173 N N   . ILE D 157 ? 1.30397 1.42912 1.22347 -0.08671 -0.00483 0.00969  157 ILE D N   
6174 C CA  . ILE D 157 ? 1.28820 1.43296 1.21902 -0.09135 -0.00948 0.00324  157 ILE D CA  
6175 C C   . ILE D 157 ? 1.27096 1.43930 1.21006 -0.07224 -0.02088 0.01498  157 ILE D C   
6176 O O   . ILE D 157 ? 1.29004 1.49603 1.23324 -0.07283 -0.02798 0.00789  157 ILE D O   
6177 C CB  . ILE D 157 ? 1.29363 1.40261 1.23253 -0.09859 -0.00192 0.00286  157 ILE D CB  
6178 C CG1 . ILE D 157 ? 1.27114 1.35938 1.19836 -0.11822 0.01097  -0.01124 157 ILE D CG1 
6179 C CG2 . ILE D 157 ? 1.26887 1.39399 1.22117 -0.09863 -0.00750 0.00092  157 ILE D CG2 
6180 C CD1 . ILE D 157 ? 1.23363 1.28028 1.16327 -0.12029 0.02003  -0.00848 157 ILE D CD1 
6181 N N   . ARG D 158 ? 1.25111 1.39735 1.19264 -0.05534 -0.02160 0.03231  158 ARG D N   
6182 C CA  . ARG D 158 ? 1.26699 1.42875 1.21401 -0.03688 -0.02979 0.04397  158 ARG D CA  
6183 C C   . ARG D 158 ? 1.33277 1.53515 1.26774 -0.02685 -0.03708 0.04318  158 ARG D C   
6184 O O   . ARG D 158 ? 1.33509 1.56724 1.27343 -0.01588 -0.04511 0.04513  158 ARG D O   
6185 C CB  . ARG D 158 ? 1.23563 1.36342 1.18506 -0.02283 -0.02630 0.06107  158 ARG D CB  
6186 C CG  . ARG D 158 ? 1.15874 1.25030 1.11948 -0.03014 -0.01956 0.06196  158 ARG D CG  
6187 C CD  . ARG D 158 ? 1.16313 1.23043 1.12928 -0.01670 -0.01705 0.07666  158 ARG D CD  
6188 N NE  . ARG D 158 ? 1.21249 1.24927 1.18750 -0.02277 -0.01025 0.07648  158 ARG D NE  
6189 C CZ  . ARG D 158 ? 1.21933 1.23515 1.19030 -0.02297 -0.00308 0.07933  158 ARG D CZ  
6190 N NH1 . ARG D 158 ? 1.27424 1.29108 1.23257 -0.01720 -0.00087 0.08435  158 ARG D NH1 
6191 N NH2 . ARG D 158 ? 1.20366 1.19797 1.18290 -0.02776 0.00224  0.07729  158 ARG D NH2 
6192 N N   . THR D 159 ? 1.47121 1.67640 1.39113 -0.02907 -0.03435 0.04041  159 THR D N   
6193 C CA  . THR D 159 ? 1.46810 1.71458 1.37411 -0.01911 -0.04126 0.03849  159 THR D CA  
6194 C C   . THR D 159 ? 1.44423 1.73884 1.35434 -0.03150 -0.04735 0.01940  159 THR D C   
6195 O O   . THR D 159 ? 1.45494 1.79209 1.36330 -0.01828 -0.05670 0.01940  159 THR D O   
6196 C CB  . THR D 159 ? 1.47748 1.71458 1.36643 -0.02135 -0.03601 0.03801  159 THR D CB  
6197 O OG1 . THR D 159 ? 1.46993 1.66286 1.35652 -0.01186 -0.02900 0.05415  159 THR D OG1 
6198 C CG2 . THR D 159 ? 1.46034 1.74045 1.33241 -0.00752 -0.04346 0.03771  159 THR D CG2 
6199 N N   . ARG D 160 ? 1.30114 1.58968 1.21592 -0.05658 -0.04103 0.00254  160 ARG D N   
6200 C CA  . ARG D 160 ? 1.27828 1.61218 1.19569 -0.07284 -0.04394 -0.01896 160 ARG D CA  
6201 C C   . ARG D 160 ? 1.25231 1.61329 1.18455 -0.06686 -0.05167 -0.01948 160 ARG D C   
6202 O O   . ARG D 160 ? 1.24296 1.65852 1.17575 -0.06439 -0.05995 -0.02960 160 ARG D O   
6203 C CB  . ARG D 160 ? 1.20784 1.51795 1.12518 -0.10129 -0.03178 -0.03557 160 ARG D CB  
6204 C CG  . ARG D 160 ? 1.18026 1.53355 1.09756 -0.12266 -0.03110 -0.06072 160 ARG D CG  
6205 C CD  . ARG D 160 ? 1.22138 1.61223 1.12434 -0.12133 -0.03508 -0.06854 160 ARG D CD  
6206 N NE  . ARG D 160 ? 1.22882 1.66788 1.13143 -0.14339 -0.03420 -0.09559 160 ARG D NE  
6207 C CZ  . ARG D 160 ? 1.22150 1.64700 1.11768 -0.17170 -0.02099 -0.11503 160 ARG D CZ  
6208 N NH1 . ARG D 160 ? 1.20113 1.56532 1.09132 -0.18016 -0.00779 -0.10978 160 ARG D NH1 
6209 N NH2 . ARG D 160 ? 1.23630 1.71150 1.13131 -0.19184 -0.02010 -0.14109 160 ARG D NH2 
6210 N N   . ILE D 161 ? 1.25938 1.58571 1.20380 -0.06366 -0.04933 -0.00911 161 ILE D N   
6211 C CA  . ILE D 161 ? 1.29715 1.64655 1.25560 -0.05851 -0.05585 -0.00962 161 ILE D CA  
6212 C C   . ILE D 161 ? 1.28968 1.66837 1.24456 -0.03024 -0.06655 0.00391  161 ILE D C   
6213 O O   . ILE D 161 ? 1.27243 1.70117 1.23121 -0.02538 -0.07476 -0.00383 161 ILE D O   
6214 C CB  . ILE D 161 ? 1.28683 1.59145 1.25801 -0.06201 -0.05035 -0.00226 161 ILE D CB  
6215 C CG1 . ILE D 161 ? 1.26503 1.55152 1.23818 -0.08922 -0.03992 -0.01884 161 ILE D CG1 
6216 C CG2 . ILE D 161 ? 1.24665 1.56961 1.23093 -0.05057 -0.05764 0.00264  161 ILE D CG2 
6217 C CD1 . ILE D 161 ? 1.29859 1.54315 1.28175 -0.09163 -0.03436 -0.01241 161 ILE D CD1 
6218 N N   . GLU D 162 ? 1.29557 1.64451 1.24138 -0.01070 -0.06554 0.02370  162 GLU D N   
6219 C CA  . GLU D 162 ? 1.30253 1.67502 1.24061 0.01768  -0.07336 0.03717  162 GLU D CA  
6220 C C   . GLU D 162 ? 1.28502 1.71021 1.20868 0.02428  -0.08022 0.02876  162 GLU D C   
6221 O O   . GLU D 162 ? 1.28361 1.73949 1.19894 0.04913  -0.08771 0.03716  162 GLU D O   
6222 C CB  . GLU D 162 ? 1.29080 1.61824 1.21917 0.03689  -0.06828 0.05963  162 GLU D CB  
6223 C CG  . GLU D 162 ? 1.32959 1.65063 1.23818 0.04148  -0.06500 0.06341  162 GLU D CG  
6224 C CD  . GLU D 162 ? 1.34556 1.62901 1.24140 0.06306  -0.05934 0.08527  162 GLU D CD  
6225 O OE1 . GLU D 162 ? 1.34623 1.60362 1.24956 0.07208  -0.05667 0.09692  162 GLU D OE1 
6226 O OE2 . GLU D 162 ? 1.35749 1.63829 1.23438 0.07093  -0.05675 0.09019  162 GLU D OE2 
6227 N N   . ALA D 163 ? 1.26764 1.70339 1.18655 0.00376  -0.07720 0.01251  163 ALA D N   
6228 C CA  . ALA D 163 ? 1.24615 1.73894 1.15346 0.00584  -0.08398 -0.00012 163 ALA D CA  
6229 C C   . ALA D 163 ? 1.23904 1.78446 1.16012 -0.01213 -0.08854 -0.02393 163 ALA D C   
6230 O O   . ALA D 163 ? 1.23060 1.83293 1.15163 0.00223  -0.09879 -0.02805 163 ALA D O   
6231 C CB  . ALA D 163 ? 1.27410 1.75175 1.16728 -0.00690 -0.07744 -0.00593 163 ALA D CB  
6232 N N   . LEU D 164 ? 1.24396 1.77073 1.17602 -0.04275 -0.08000 -0.03980 164 LEU D N   
6233 C CA  . LEU D 164 ? 1.23495 1.80818 1.17947 -0.06313 -0.08145 -0.06411 164 LEU D CA  
6234 C C   . LEU D 164 ? 1.22817 1.83119 1.18553 -0.04601 -0.09067 -0.05859 164 LEU D C   
6235 O O   . LEU D 164 ? 1.17900 1.84802 1.13832 -0.03955 -0.10000 -0.06993 164 LEU D O   
6236 C CB  . LEU D 164 ? 1.21817 1.75148 1.17039 -0.09523 -0.06790 -0.07712 164 LEU D CB  
6237 N N   . LEU D 165 ? 1.23841 1.79494 1.20351 -0.03578 -0.08852 -0.04024 165 LEU D N   
6238 C CA  . LEU D 165 ? 1.21240 1.78677 1.18865 -0.01783 -0.09582 -0.03192 165 LEU D CA  
6239 C C   . LEU D 165 ? 1.19771 1.79938 1.16200 0.01817  -0.10578 -0.01550 165 LEU D C   
6240 O O   . LEU D 165 ? 1.19225 1.81410 1.16355 0.03559  -0.11193 -0.00912 165 LEU D O   
6241 C CB  . LEU D 165 ? 1.26251 1.77601 1.24846 -0.01717 -0.08969 -0.01681 165 LEU D CB  
6242 C CG  . LEU D 165 ? 1.25535 1.74958 1.25764 -0.04114 -0.08292 -0.02793 165 LEU D CG  
6243 C CD1 . LEU D 165 ? 1.25031 1.71598 1.24921 -0.07046 -0.07130 -0.04188 165 LEU D CD1 
6244 C CD2 . LEU D 165 ? 1.23364 1.68070 1.24341 -0.02845 -0.08122 -0.00845 165 LEU D CD2 
6245 N N   . LEU D 166 ? 1.20075 1.79883 1.14553 0.03097  -0.10622 -0.00725 166 LEU D N   
6246 C CA  . LEU D 166 ? 1.16647 1.79018 1.09440 0.06672  -0.11409 0.00816  166 LEU D CA  
6247 C C   . LEU D 166 ? 1.14290 1.73959 1.07250 0.09230  -0.11448 0.03024  166 LEU D C   
6248 O O   . LEU D 166 ? 1.09871 1.73215 1.02222 0.11937  -0.12212 0.03698  166 LEU D O   
6249 C CB  . LEU D 166 ? 1.10840 1.81636 1.03476 0.07182  -0.12514 -0.00952 166 LEU D CB  
6250 C CG  . LEU D 166 ? 1.17060 1.90607 1.08657 0.05539  -0.12487 -0.02699 166 LEU D CG  
6251 C CD1 . LEU D 166 ? 1.10569 1.93208 1.02255 0.05611  -0.13569 -0.04932 166 LEU D CD1 
6252 C CD2 . LEU D 166 ? 1.12054 1.82197 1.01166 0.07548  -0.12212 -0.00728 166 LEU D CD2 
6253 N N   . VAL D 167 ? 1.15780 1.69082 1.09520 0.08411  -0.10567 0.04092  167 VAL D N   
6254 C CA  . VAL D 167 ? 1.20347 1.70105 1.14007 0.10627  -0.10327 0.06231  167 VAL D CA  
6255 C C   . VAL D 167 ? 1.27980 1.70846 1.21022 0.10338  -0.09227 0.07673  167 VAL D C   
6256 O O   . VAL D 167 ? 1.29356 1.69318 1.23425 0.07809  -0.08639 0.06882  167 VAL D O   
6257 C CB  . VAL D 167 ? 1.19915 1.69862 1.15807 0.09792  -0.10460 0.05734  167 VAL D CB  
6258 C CG1 . VAL D 167 ? 1.18203 1.64368 1.13831 0.12088  -0.10111 0.07909  167 VAL D CG1 
6259 C CG2 . VAL D 167 ? 1.12580 1.69690 1.09287 0.09837  -0.11472 0.04071  167 VAL D CG2 
6260 N N   . ARG D 168 ? 1.34762 1.75026 1.26033 0.12959  -0.08840 0.09737  168 ARG D N   
6261 C CA  . ARG D 168 ? 1.38482 1.72743 1.28987 0.12748  -0.07712 0.10986  168 ARG D CA  
6262 C C   . ARG D 168 ? 1.39915 1.69785 1.32372 0.11346  -0.07078 0.11200  168 ARG D C   
6263 O O   . ARG D 168 ? 1.36243 1.66749 1.29979 0.11639  -0.07368 0.11216  168 ARG D O   
6264 C CB  . ARG D 168 ? 1.37514 1.69971 1.25423 0.15891  -0.07226 0.13078  168 ARG D CB  
6265 C CG  . ARG D 168 ? 1.40378 1.67172 1.27109 0.15729  -0.05937 0.14242  168 ARG D CG  
6266 C CD  . ARG D 168 ? 1.47446 1.72837 1.31145 0.18912  -0.05334 0.16185  168 ARG D CD  
6267 N NE  . ARG D 168 ? 1.47299 1.67492 1.29651 0.18791  -0.03957 0.17235  168 ARG D NE  
6268 C CZ  . ARG D 168 ? 1.48113 1.63052 1.30536 0.18895  -0.02671 0.18367  168 ARG D CZ  
6269 N NH1 . ARG D 168 ? 1.48050 1.61913 1.31783 0.19123  -0.02581 0.18666  168 ARG D NH1 
6270 N NH2 . ARG D 168 ? 1.51609 1.62385 1.32763 0.18680  -0.01377 0.19111  168 ARG D NH2 
6271 N N   . ASP D 169 ? 1.38858 1.64540 1.31539 0.09824  -0.06229 0.11272  169 ASP D N   
6272 C CA  . ASP D 169 ? 1.34881 1.56314 1.29200 0.08575  -0.05553 0.11478  169 ASP D CA  
6273 C C   . ASP D 169 ? 1.33021 1.55780 1.29443 0.06397  -0.05962 0.09908  169 ASP D C   
6274 O O   . ASP D 169 ? 1.30659 1.50262 1.28404 0.05211  -0.05470 0.09854  169 ASP D O   
6275 C CB  . ASP D 169 ? 1.29731 1.48812 1.23949 0.10418  -0.05142 0.13004  169 ASP D CB  
6276 N N   . MET D 170 ? 1.31296 1.58723 1.27939 0.05812  -0.06761 0.08540  170 MET D N   
6277 C CA  . MET D 170 ? 1.25925 1.54623 1.24318 0.03704  -0.06959 0.06964  170 MET D CA  
6278 C C   . MET D 170 ? 1.23234 1.50749 1.21549 0.01371  -0.06432 0.05723  170 MET D C   
6279 O O   . MET D 170 ? 1.23232 1.53819 1.20887 0.00470  -0.06647 0.04449  170 MET D O   
6280 C CB  . MET D 170 ? 1.28390 1.62710 1.27145 0.04029  -0.07879 0.05922  170 MET D CB  
6281 C CG  . MET D 170 ? 1.31537 1.66750 1.30643 0.06228  -0.08313 0.07054  170 MET D CG  
6282 S SD  . MET D 170 ? 1.40339 1.71631 1.41354 0.05521  -0.07867 0.07482  170 MET D SD  
6283 C CE  . MET D 170 ? 1.28347 1.54565 1.28352 0.07560  -0.07130 0.09784  170 MET D CE  
6284 N N   . THR D 171 ? 1.27591 1.50654 1.26530 0.00448  -0.05681 0.06058  171 THR D N   
6285 C CA  . THR D 171 ? 1.28774 1.49696 1.27483 -0.01431 -0.04972 0.05197  171 THR D CA  
6286 C C   . THR D 171 ? 1.31035 1.51908 1.30715 -0.03510 -0.04685 0.03715  171 THR D C   
6287 O O   . THR D 171 ? 1.29151 1.48201 1.28383 -0.05077 -0.03953 0.02888  171 THR D O   
6288 C CB  . THR D 171 ? 1.25905 1.42185 1.24622 -0.00997 -0.04256 0.06423  171 THR D CB  
6289 O OG1 . THR D 171 ? 1.23796 1.38134 1.23907 -0.00747 -0.04189 0.06967  171 THR D OG1 
6290 C CG2 . THR D 171 ? 1.26117 1.42010 1.23616 0.00881  -0.04245 0.07819  171 THR D CG2 
6291 N N   . THR D 172 ? 1.43172 1.65753 1.43992 -0.03500 -0.05112 0.03396  172 THR D N   
6292 C CA  . THR D 172 ? 1.42775 1.64809 1.44445 -0.05319 -0.04690 0.02165  172 THR D CA  
6293 C C   . THR D 172 ? 1.41827 1.68591 1.43994 -0.05964 -0.05214 0.00792  172 THR D C   
6294 O O   . THR D 172 ? 1.38529 1.68427 1.41064 -0.04409 -0.06084 0.01289  172 THR D O   
6295 C CB  . THR D 172 ? 1.37153 1.56071 1.39942 -0.04796 -0.04532 0.03113  172 THR D CB  
6296 O OG1 . THR D 172 ? 1.34162 1.54648 1.37579 -0.02973 -0.05286 0.04156  172 THR D OG1 
6297 C CG2 . THR D 172 ? 1.35321 1.49903 1.37825 -0.04498 -0.03908 0.04086  172 THR D CG2 
6298 N N   . CYS D 173 ? 1.38851 1.66002 1.40971 -0.08239 -0.04554 -0.00968 173 CYS D N   
6299 C CA  . CYS D 173 ? 1.37306 1.69064 1.39867 -0.09494 -0.04762 -0.02778 173 CYS D CA  
6300 C C   . CYS D 173 ? 1.44546 1.75288 1.48180 -0.10578 -0.04311 -0.03381 173 CYS D C   
6301 O O   . CYS D 173 ? 1.44850 1.70946 1.48401 -0.11066 -0.03499 -0.02911 173 CYS D O   
6302 C CB  . CYS D 173 ? 1.32490 1.65376 1.33942 -0.11656 -0.04035 -0.04637 173 CYS D CB  
6303 S SG  . CYS D 173 ? 1.25366 1.64217 1.27307 -0.13789 -0.04009 -0.07390 173 CYS D SG  
6304 N N   . PRO D 174 ? 1.44028 1.79140 1.48636 -0.10798 -0.04828 -0.04371 174 PRO D N   
6305 C CA  . PRO D 174 ? 1.42995 1.77449 1.48446 -0.12272 -0.04193 -0.05334 174 PRO D CA  
6306 C C   . PRO D 174 ? 1.45267 1.80340 1.50083 -0.15279 -0.02967 -0.07717 174 PRO D C   
6307 O O   . PRO D 174 ? 1.46378 1.84532 1.50560 -0.16265 -0.02935 -0.09052 174 PRO D O   
6308 C CB  . PRO D 174 ? 1.40174 1.79524 1.46955 -0.11011 -0.05314 -0.05349 174 PRO D CB  
6309 C CG  . PRO D 174 ? 1.39398 1.83497 1.45722 -0.09975 -0.06232 -0.05575 174 PRO D CG  
6310 C CD  . PRO D 174 ? 1.39694 1.80339 1.44692 -0.09136 -0.06097 -0.04270 174 PRO D CD  
6311 N N   . LEU D 175 ? 1.49687 1.81758 1.54554 -0.16760 -0.01846 -0.08307 175 LEU D N   
6312 C CA  . LEU D 175 ? 1.52167 1.83312 1.56062 -0.19723 -0.00214 -0.10450 175 LEU D CA  
6313 C C   . LEU D 175 ? 1.50481 1.84721 1.55368 -0.21332 0.00174  -0.12200 175 LEU D C   
6314 O O   . LEU D 175 ? 1.48995 1.84833 1.55285 -0.20032 -0.00708 -0.11456 175 LEU D O   
6315 C CB  . LEU D 175 ? 1.49100 1.73267 1.51611 -0.20195 0.01217  -0.09729 175 LEU D CB  
6316 N N   . PRO D 176 ? 1.50526 1.85821 1.54699 -0.24284 0.01592  -0.14681 176 PRO D N   
6317 C CA  . PRO D 176 ? 1.48113 1.85627 1.53067 -0.26238 0.02380  -0.16550 176 PRO D CA  
6318 C C   . PRO D 176 ? 1.48053 1.79644 1.52373 -0.26722 0.03743  -0.15949 176 PRO D C   
6319 O O   . PRO D 176 ? 1.50025 1.75694 1.52609 -0.26881 0.04907  -0.15199 176 PRO D O   
6320 C CB  . PRO D 176 ? 1.45713 1.85435 1.49744 -0.29411 0.03761  -0.19424 176 PRO D CB  
6321 C CG  . PRO D 176 ? 1.46891 1.82335 1.49029 -0.29437 0.04430  -0.18790 176 PRO D CG  
6322 C CD  . PRO D 176 ? 1.50121 1.85113 1.52761 -0.26036 0.02552  -0.16044 176 PRO D CD  
6323 N N   . VAL D 184 ? 1.56498 1.35185 1.48958 -0.08342 0.07623  0.01486  184 VAL D N   
6324 C CA  . VAL D 184 ? 1.55520 1.34042 1.48682 -0.06111 0.06817  0.02697  184 VAL D CA  
6325 C C   . VAL D 184 ? 1.51313 1.32810 1.46410 -0.05880 0.05500  0.03020  184 VAL D C   
6326 O O   . VAL D 184 ? 1.54994 1.36699 1.49520 -0.06827 0.05851  0.02541  184 VAL D O   
6327 C CB  . VAL D 184 ? 1.55203 1.29664 1.45692 -0.04989 0.08291  0.03015  184 VAL D CB  
6328 N N   . ALA D 185 ? 1.45003 1.28647 1.42252 -0.04652 0.04106  0.03792  185 ALA D N   
6329 C CA  . ALA D 185 ? 1.49300 1.35714 1.48367 -0.04559 0.02959  0.04094  185 ALA D CA  
6330 C C   . ALA D 185 ? 1.50908 1.36433 1.49456 -0.03800 0.03236  0.04427  185 ALA D C   
6331 O O   . ALA D 185 ? 1.51475 1.38177 1.50279 -0.04351 0.03018  0.04317  185 ALA D O   
6332 C CB  . ALA D 185 ? 1.48325 1.36864 1.49637 -0.03620 0.01679  0.04723  185 ALA D CB  
6333 N N   . HIS D 186 ? 1.50767 1.34428 1.48560 -0.02414 0.03702  0.04833  186 HIS D N   
6334 C CA  . HIS D 186 ? 1.48740 1.32181 1.46515 -0.01380 0.03777  0.05197  186 HIS D CA  
6335 C C   . HIS D 186 ? 1.51026 1.31646 1.46279 -0.01575 0.05196  0.04885  186 HIS D C   
6336 O O   . HIS D 186 ? 1.51765 1.31422 1.46403 -0.00302 0.05588  0.05206  186 HIS D O   
6337 C CB  . HIS D 186 ? 1.44500 1.28308 1.43143 0.00415  0.03346  0.05721  186 HIS D CB  
6338 C CG  . HIS D 186 ? 1.43548 1.29731 1.44441 0.00473  0.02166  0.05912  186 HIS D CG  
6339 N ND1 . HIS D 186 ? 1.41396 1.29946 1.44297 0.00205  0.01274  0.06079  186 HIS D ND1 
6340 C CD2 . HIS D 186 ? 1.44170 1.30461 1.45413 0.00706  0.01874  0.05951  186 HIS D CD2 
6341 C CE1 . HIS D 186 ? 1.43790 1.33721 1.48173 0.00308  0.00522  0.06207  186 HIS D CE1 
6342 N NE2 . HIS D 186 ? 1.44542 1.33294 1.48055 0.00592  0.00798  0.06115  186 HIS D NE2 
6343 N N   . ASP D 187 ? 1.48635 1.27981 1.42387 -0.03164 0.06059  0.04172  187 ASP D N   
6344 C CA  . ASP D 187 ? 1.49988 1.26640 1.41278 -0.03816 0.07555  0.03671  187 ASP D CA  
6345 C C   . ASP D 187 ? 1.47859 1.26389 1.39707 -0.05209 0.07214  0.03183  187 ASP D C   
6346 O O   . ASP D 187 ? 1.48998 1.30030 1.42065 -0.06408 0.06431  0.02780  187 ASP D O   
6347 C CB  . ASP D 187 ? 1.55326 1.29141 1.44356 -0.04901 0.09025  0.02975  187 ASP D CB  
6348 C CG  . ASP D 187 ? 1.58145 1.28543 1.44281 -0.05589 0.10896  0.02398  187 ASP D CG  
6349 O OD1 . ASP D 187 ? 1.55598 1.26099 1.41606 -0.05227 0.10914  0.02545  187 ASP D OD1 
6350 O OD2 . ASP D 187 ? 1.57289 1.24717 1.41169 -0.06548 0.12485  0.01757  187 ASP D OD2 
6351 N N   . SER D 188 ? 1.46727 1.24147 1.37578 -0.04905 0.07816  0.03227  188 SER D N   
6352 C CA  . SER D 188 ? 1.40343 1.19377 1.31461 -0.06038 0.07569  0.02812  188 SER D CA  
6353 C C   . SER D 188 ? 1.47366 1.25585 1.36784 -0.08144 0.08618  0.01584  188 SER D C   
6354 O O   . SER D 188 ? 1.42153 1.22728 1.32102 -0.09321 0.08116  0.01050  188 SER D O   
6355 C CB  . SER D 188 ? 1.26400 1.04370 1.16907 -0.05039 0.07997  0.03201  188 SER D CB  
6356 O OG  . SER D 188 ? 1.26743 1.05853 1.18933 -0.03275 0.07117  0.04094  188 SER D OG  
6357 N N   . ILE D 189 ? 1.49804 1.24690 1.37019 -0.08624 0.10192  0.01063  189 ILE D N   
6358 C CA  . ILE D 189 ? 1.50154 1.24265 1.35782 -0.10941 0.11404  -0.00364 189 ILE D CA  
6359 C C   . ILE D 189 ? 1.52901 1.30123 1.40144 -0.12148 0.10474  -0.00946 189 ILE D C   
6360 O O   . ILE D 189 ? 1.51684 1.31051 1.39010 -0.14048 0.10492  -0.02145 189 ILE D O   
6361 C CB  . ILE D 189 ? 1.49289 1.18337 1.31778 -0.11087 0.13675  -0.00734 189 ILE D CB  
6362 C CG1 . ILE D 189 ? 1.50161 1.16248 1.30898 -0.09712 0.14651  -0.00161 189 ILE D CG1 
6363 C CG2 . ILE D 189 ? 1.52199 1.20419 1.33063 -0.13816 0.15149  -0.02449 189 ILE D CG2 
6364 C CD1 . ILE D 189 ? 1.49173 1.16009 1.29466 -0.10925 0.14918  -0.00871 189 ILE D CD1 
6365 N N   . HIS D 190 ? 1.63250 1.40997 1.51792 -0.11027 0.09655  -0.00183 190 HIS D N   
6366 C CA  . HIS D 190 ? 1.66256 1.47278 1.56581 -0.11877 0.08601  -0.00582 190 HIS D CA  
6367 C C   . HIS D 190 ? 1.64163 1.49513 1.56598 -0.11811 0.06903  -0.00378 190 HIS D C   
6368 O O   . HIS D 190 ? 1.63508 1.51965 1.56765 -0.13044 0.06355  -0.01201 190 HIS D O   
6369 C CB  . HIS D 190 ? 1.67903 1.48514 1.59176 -0.10526 0.08049  0.00283  190 HIS D CB  
6370 C CG  . HIS D 190 ? 1.72241 1.48989 1.61326 -0.10765 0.09726  -0.00041 190 HIS D CG  
6371 N ND1 . HIS D 190 ? 1.68959 1.44791 1.58345 -0.09537 0.09513  0.00661  190 HIS D ND1 
6372 C CD2 . HIS D 190 ? 1.75824 1.49115 1.62143 -0.12056 0.11798  -0.00988 190 HIS D CD2 
6373 C CE1 . HIS D 190 ? 1.73542 1.45486 1.60358 -0.09946 0.11363  0.00249  190 HIS D CE1 
6374 N NE2 . HIS D 190 ? 1.77115 1.47277 1.61983 -0.11501 0.12859  -0.00755 190 HIS D NE2 
6375 N N   . ASP D 191 ? 1.54586 1.40233 1.47803 -0.10305 0.06141  0.00688  191 ASP D N   
6376 C CA  . ASP D 191 ? 1.45749 1.34867 1.40538 -0.10062 0.04774  0.01024  191 ASP D CA  
6377 C C   . ASP D 191 ? 1.41047 1.31653 1.34894 -0.11671 0.05117  -0.00114 191 ASP D C   
6378 O O   . ASP D 191 ? 1.39257 1.33425 1.34063 -0.12186 0.04185  -0.00496 191 ASP D O   
6379 C CB  . ASP D 191 ? 1.44103 1.32629 1.39525 -0.08393 0.04331  0.02198  191 ASP D CB  
6380 C CG  . ASP D 191 ? 1.49943 1.41539 1.46958 -0.07840 0.03017  0.02803  191 ASP D CG  
6381 O OD1 . ASP D 191 ? 1.58361 1.51656 1.56920 -0.07255 0.02060  0.03294  191 ASP D OD1 
6382 O OD2 . ASP D 191 ? 1.38841 1.30902 1.35403 -0.07896 0.03045  0.02841  191 ASP D OD2 
6383 N N   . CYS D 192 ? 1.42991 1.30985 1.34833 -0.12432 0.06512  -0.00737 192 CYS D N   
6384 C CA  . CYS D 192 ? 1.39874 1.29269 1.30719 -0.14049 0.06926  -0.01952 192 CYS D CA  
6385 C C   . CYS D 192 ? 1.41643 1.33112 1.32387 -0.16021 0.07193  -0.03505 192 CYS D C   
6386 O O   . CYS D 192 ? 1.39007 1.34352 1.30333 -0.16836 0.06437  -0.04270 192 CYS D O   
6387 C CB  . CYS D 192 ? 1.40178 1.25875 1.28718 -0.14515 0.08593  -0.02366 192 CYS D CB  
6388 S SG  . CYS D 192 ? 1.39984 1.24408 1.28609 -0.12583 0.08296  -0.00971 192 CYS D SG  
6389 N N   . ALA D 193 ? 1.44809 1.33873 1.34733 -0.16771 0.08329  -0.04048 193 ALA D N   
6390 C CA  . ALA D 193 ? 1.37304 1.28130 1.27013 -0.18945 0.08902  -0.05775 193 ALA D CA  
6391 C C   . ALA D 193 ? 1.30394 1.26241 1.22466 -0.18640 0.07101  -0.05700 193 ALA D C   
6392 O O   . ALA D 193 ? 1.28433 1.28091 1.20864 -0.20107 0.06838  -0.07104 193 ALA D O   
6393 C CB  . ALA D 193 ? 1.49391 1.36125 1.37594 -0.19621 0.10622  -0.06185 193 ALA D CB  
6394 N N   . LYS D 194 ? 1.33362 1.29465 1.27021 -0.16684 0.05874  -0.04133 194 LYS D N   
6395 C CA  . LYS D 194 ? 1.26785 1.27384 1.22519 -0.16067 0.04200  -0.03857 194 LYS D CA  
6396 C C   . LYS D 194 ? 1.34664 1.38840 1.30851 -0.15656 0.03106  -0.03774 194 LYS D C   
6397 O O   . LYS D 194 ? 1.32339 1.40916 1.29509 -0.15826 0.02133  -0.04304 194 LYS D O   
6398 C CB  . LYS D 194 ? 1.16628 1.16318 1.13760 -0.14055 0.03283  -0.02185 194 LYS D CB  
6399 N N   . ASP D 195 ? 1.30589 1.33032 1.25985 -0.14954 0.03262  -0.03076 195 ASP D N   
6400 C CA  . ASP D 195 ? 1.25157 1.30568 1.20446 -0.14789 0.02540  -0.03179 195 ASP D CA  
6401 C C   . ASP D 195 ? 1.27040 1.34462 1.21185 -0.17014 0.03277  -0.05232 195 ASP D C   
6402 O O   . ASP D 195 ? 1.28672 1.40749 1.23344 -0.17264 0.02374  -0.05948 195 ASP D O   
6403 C CB  . ASP D 195 ? 1.24004 1.26876 1.18667 -0.13626 0.02692  -0.02017 195 ASP D CB  
6404 C CG  . ASP D 195 ? 1.22871 1.25653 1.18922 -0.11438 0.01614  -0.00170 195 ASP D CG  
6405 O OD1 . ASP D 195 ? 1.18748 1.24386 1.16010 -0.10638 0.00496  0.00275  195 ASP D OD1 
6406 O OD2 . ASP D 195 ? 1.18446 1.18340 1.14302 -0.10541 0.01990  0.00753  195 ASP D OD2 
6407 N N   . ILE D 196 ? 1.26635 1.30682 1.19099 -0.18617 0.05000  -0.06276 196 ILE D N   
6408 C CA  . ILE D 196 ? 1.29398 1.35076 1.20627 -0.20994 0.05950  -0.08425 196 ILE D CA  
6409 C C   . ILE D 196 ? 1.35356 1.45298 1.27579 -0.22362 0.05606  -0.09947 196 ILE D C   
6410 O O   . ILE D 196 ? 1.37452 1.51301 1.29453 -0.23907 0.05596  -0.11701 196 ILE D O   
6411 C CB  . ILE D 196 ? 1.32211 1.32791 1.21216 -0.22524 0.08197  -0.09294 196 ILE D CB  
6412 C CG1 . ILE D 196 ? 1.34221 1.30919 1.22251 -0.21056 0.08554  -0.07866 196 ILE D CG1 
6413 C CG2 . ILE D 196 ? 1.31765 1.33995 1.19431 -0.25200 0.09333  -0.11688 196 ILE D CG2 
6414 C CD1 . ILE D 196 ? 1.42211 1.33410 1.27941 -0.21961 0.10780  -0.08356 196 ILE D CD1 
6415 N N   . LEU D 197 ? 1.28726 1.38259 1.22082 -0.21846 0.05335  -0.09417 197 LEU D N   
6416 C CA  . LEU D 197 ? 1.32605 1.46320 1.27056 -0.23055 0.05010  -0.10843 197 LEU D CA  
6417 C C   . LEU D 197 ? 1.37147 1.56430 1.33366 -0.21403 0.02902  -0.10189 197 LEU D C   
6418 O O   . LEU D 197 ? 1.45228 1.69699 1.41895 -0.22417 0.02441  -0.11762 197 LEU D O   
6419 C CB  . LEU D 197 ? 1.33554 1.44570 1.28343 -0.23251 0.05700  -0.10643 197 LEU D CB  
6420 C CG  . LEU D 197 ? 1.36084 1.41890 1.28834 -0.25091 0.08077  -0.11620 197 LEU D CG  
6421 C CD1 . LEU D 197 ? 1.37915 1.41629 1.31069 -0.24921 0.08513  -0.11240 197 LEU D CD1 
6422 C CD2 . LEU D 197 ? 1.32019 1.39184 1.23484 -0.28153 0.09584  -0.14281 197 LEU D CD2 
6423 N N   . MET D 198 ? 1.35494 1.53875 1.32630 -0.18827 0.01698  -0.07954 198 MET D N   
6424 C CA  . MET D 198 ? 1.32998 1.56065 1.31455 -0.17049 -0.00078 -0.07190 198 MET D CA  
6425 C C   . MET D 198 ? 1.40647 1.67841 1.38465 -0.17246 -0.00608 -0.08054 198 MET D C   
6426 O O   . MET D 198 ? 1.46057 1.78671 1.44619 -0.16889 -0.01648 -0.08703 198 MET D O   
6427 C CB  . MET D 198 ? 1.29682 1.50503 1.28760 -0.14426 -0.00948 -0.04733 198 MET D CB  
6428 C CG  . MET D 198 ? 1.28153 1.46305 1.28213 -0.13742 -0.00897 -0.03765 198 MET D CG  
6429 S SD  . MET D 198 ? 1.42113 1.59601 1.43142 -0.10768 -0.02131 -0.01285 198 MET D SD  
6430 C CE  . MET D 198 ? 1.34892 1.48405 1.34705 -0.10363 -0.01484 -0.00396 198 MET D CE  
6431 N N   . MET D 199 ? 1.39241 1.64131 1.35611 -0.17707 0.00094  -0.08102 199 MET D N   
6432 C CA  . MET D 199 ? 1.41797 1.70500 1.37368 -0.17949 -0.00341 -0.08991 199 MET D CA  
6433 C C   . MET D 199 ? 1.43123 1.75510 1.38434 -0.20655 0.00324  -0.11798 199 MET D C   
6434 O O   . MET D 199 ? 1.42798 1.81141 1.38487 -0.20571 -0.00658 -0.12817 199 MET D O   
6435 C CB  . MET D 199 ? 1.40952 1.65984 1.35029 -0.17770 0.00328  -0.08307 199 MET D CB  
6436 N N   . LYS D 200 ? 1.45389 1.74360 1.39943 -0.23052 0.02091  -0.13147 200 LYS D N   
6437 C CA  . LYS D 200 ? 1.47719 1.79761 1.41932 -0.26016 0.03078  -0.16054 200 LYS D CA  
6438 C C   . LYS D 200 ? 1.49444 1.86941 1.45425 -0.26158 0.02151  -0.17004 200 LYS D C   
6439 O O   . LYS D 200 ? 1.48377 1.91175 1.44563 -0.27941 0.02194  -0.19377 200 LYS D O   
6440 C CB  . LYS D 200 ? 1.42397 1.68800 1.35204 -0.28377 0.05427  -0.17091 200 LYS D CB  
6441 N N   . TYR D 201 ? 1.67149 2.03625 1.64440 -0.24336 0.01347  -0.15292 201 TYR D N   
6442 C CA  . TYR D 201 ? 1.64931 2.06596 1.63982 -0.23920 0.00275  -0.15819 201 TYR D CA  
6443 C C   . TYR D 201 ? 1.63724 2.10922 1.63452 -0.21422 -0.01741 -0.14943 201 TYR D C   
6444 O O   . TYR D 201 ? 1.62108 2.15642 1.62849 -0.21508 -0.02581 -0.16248 201 TYR D O   
6445 C CB  . TYR D 201 ? 1.65006 2.03167 1.65028 -0.22882 0.00282  -0.14296 201 TYR D CB  
6446 N N   . ALA D 202 ? 1.51349 1.96223 1.50441 -0.19065 -0.02455 -0.12718 202 ALA D N   
6447 C CA  . ALA D 202 ? 1.40306 1.89769 1.39429 -0.16615 -0.04085 -0.11820 202 ALA D CA  
6448 C C   . ALA D 202 ? 1.39777 1.94212 1.38026 -0.17866 -0.04163 -0.13875 202 ALA D C   
6449 O O   . ALA D 202 ? 1.40704 2.01586 1.39361 -0.16772 -0.05401 -0.14459 202 ALA D O   
6450 C CB  . ALA D 202 ? 1.30972 1.76178 1.29381 -0.14122 -0.04473 -0.09101 202 ALA D CB  
6451 N N   . LEU D 203 ? 1.39760 1.91423 1.36722 -0.20104 -0.02811 -0.15057 203 LEU D N   
6452 C CA  . LEU D 203 ? 1.38960 1.95161 1.35001 -0.21589 -0.02729 -0.17223 203 LEU D CA  
6453 C C   . LEU D 203 ? 1.44925 2.07565 1.42030 -0.23623 -0.02738 -0.20070 203 LEU D C   
6454 O O   . LEU D 203 ? 1.42733 2.12222 1.39866 -0.23355 -0.03726 -0.21391 203 LEU D O   
6455 C CB  . LEU D 203 ? 1.34023 1.85315 1.28436 -0.23844 -0.00979 -0.18046 203 LEU D CB  
6456 N N   . ARG D 204 ? 1.49213 2.09944 1.47149 -0.25662 -0.01596 -0.21127 204 ARG D N   
6457 C CA  . ARG D 204 ? 1.45327 2.12186 1.44465 -0.27706 -0.01488 -0.23901 204 ARG D CA  
6458 C C   . ARG D 204 ? 1.44039 2.17328 1.44729 -0.25011 -0.03546 -0.23183 204 ARG D C   
6459 O O   . ARG D 204 ? 1.40859 2.21883 1.42158 -0.25466 -0.04291 -0.25237 204 ARG D O   
6460 C CB  . ARG D 204 ? 1.43822 2.06488 1.43333 -0.30202 0.00297  -0.24859 204 ARG D CB  
6461 N N   . TYR D 205 ? 1.43897 2.14223 1.45162 -0.22114 -0.04438 -0.20328 205 TYR D N   
6462 C CA  . TYR D 205 ? 1.39891 2.15608 1.42276 -0.19177 -0.06274 -0.19342 205 TYR D CA  
6463 C C   . TYR D 205 ? 1.41526 2.21754 1.42883 -0.16889 -0.07635 -0.18831 205 TYR D C   
6464 O O   . TYR D 205 ? 1.39083 2.26744 1.41035 -0.15643 -0.08884 -0.19693 205 TYR D O   
6465 C CB  . TYR D 205 ? 1.35791 2.06584 1.38725 -0.16694 -0.06686 -0.16384 205 TYR D CB  
6466 N N   . ALA D 206 ? 1.51338 2.27302 1.51046 -0.16219 -0.07377 -0.17459 206 ALA D N   
6467 C CA  . ALA D 206 ? 1.50268 2.29935 1.48666 -0.14004 -0.08520 -0.16861 206 ALA D CA  
6468 C C   . ALA D 206 ? 1.48576 2.35322 1.46726 -0.15996 -0.08593 -0.20001 206 ALA D C   
6469 O O   . ALA D 206 ? 1.46114 2.38854 1.43670 -0.13921 -0.09921 -0.20055 206 ALA D O   
6470 C CB  . ALA D 206 ? 1.47533 2.20756 1.44240 -0.13149 -0.08024 -0.14838 206 ALA D CB  
6471 N N   . MET D 207 ? 1.43304 2.29460 1.41728 -0.19951 -0.07093 -0.22665 207 MET D N   
6472 C CA  . MET D 207 ? 1.40871 2.34161 1.39333 -0.22340 -0.06974 -0.26106 207 MET D CA  
6473 C C   . MET D 207 ? 1.46627 2.46600 1.47091 -0.23430 -0.07308 -0.28336 207 MET D C   
6474 O O   . MET D 207 ? 1.40391 2.47852 1.41173 -0.25046 -0.07497 -0.31304 207 MET D O   
6475 C CB  . MET D 207 ? 1.36117 2.25318 1.33536 -0.26268 -0.04902 -0.28094 207 MET D CB  
6476 N N   . GLY D 208 ? 1.61886 2.59614 1.63738 -0.22610 -0.07377 -0.27082 208 GLY D N   
6477 C CA  . GLY D 208 ? 1.56690 2.60977 1.60506 -0.22716 -0.08021 -0.28597 208 GLY D CA  
6478 C C   . GLY D 208 ? 1.58061 2.61179 1.63131 -0.26545 -0.06320 -0.30947 208 GLY D C   
6479 O O   . GLY D 208 ? 1.57045 2.65366 1.63879 -0.26637 -0.06789 -0.32135 208 GLY D O   
6480 N N   . LEU D 209 ? 1.43540 2.39941 1.47620 -0.29604 -0.04265 -0.31638 209 LEU D N   
6481 C CA  . LEU D 209 ? 1.36720 2.31239 1.41551 -0.33221 -0.02351 -0.33788 209 LEU D CA  
6482 C C   . LEU D 209 ? 1.32604 2.21799 1.38276 -0.31972 -0.02219 -0.31559 209 LEU D C   
6483 O O   . LEU D 209 ? 1.27254 2.18065 1.34246 -0.33657 -0.01535 -0.33067 209 LEU D O   
6484 C CB  . LEU D 209 ? 1.32827 2.21661 1.35871 -0.36737 0.00009  -0.35255 209 LEU D CB  
6485 N N   . GLU D 210 ? 1.36312 2.19428 1.41274 -0.29120 -0.02822 -0.28117 210 GLU D N   
6486 C CA  . GLU D 210 ? 1.39637 2.16915 1.45151 -0.28268 -0.02453 -0.26126 210 GLU D CA  
6487 C C   . GLU D 210 ? 1.40461 2.22453 1.47827 -0.25850 -0.04060 -0.25296 210 GLU D C   
6488 O O   . GLU D 210 ? 1.33984 2.21056 1.41648 -0.23022 -0.05869 -0.24411 210 GLU D O   
6489 C CB  . GLU D 210 ? 1.40739 2.10382 1.44968 -0.26138 -0.02523 -0.22942 210 GLU D CB  
6490 N N   . ASP D 211 ? 1.48649 2.28881 1.57078 -0.26935 -0.03279 -0.25621 211 ASP D N   
6491 C CA  . ASP D 211 ? 1.47693 2.30948 1.57792 -0.24630 -0.04574 -0.24545 211 ASP D CA  
6492 C C   . ASP D 211 ? 1.49857 2.27288 1.59578 -0.21334 -0.05362 -0.20874 211 ASP D C   
6493 O O   . ASP D 211 ? 1.53878 2.24325 1.62321 -0.21409 -0.04588 -0.19415 211 ASP D O   
6494 C CB  . ASP D 211 ? 1.48400 2.31718 1.59699 -0.27160 -0.03314 -0.26324 211 ASP D CB  
6495 N N   . ALA D 212 ? 1.45122 2.25641 1.55943 -0.18425 -0.06839 -0.19478 212 ALA D N   
6496 C CA  . ALA D 212 ? 1.45444 2.20798 1.56047 -0.15449 -0.07462 -0.16221 212 ALA D CA  
6497 C C   . ALA D 212 ? 1.49889 2.19737 1.61067 -0.16625 -0.06369 -0.15780 212 ALA D C   
6498 O O   . ALA D 212 ? 1.52385 2.24872 1.64829 -0.17931 -0.06024 -0.17262 212 ALA D O   
6499 C CB  . ALA D 212 ? 1.40201 2.20403 1.51501 -0.11924 -0.09185 -0.14919 212 ALA D CB  
6500 N N   . PRO D 213 ? 1.50911 2.13358 1.61161 -0.16221 -0.05769 -0.13881 213 PRO D N   
6501 C CA  . PRO D 213 ? 1.53879 2.11264 1.64552 -0.16842 -0.04890 -0.13234 213 PRO D CA  
6502 C C   . PRO D 213 ? 1.53981 2.13487 1.66105 -0.14713 -0.05926 -0.12163 213 PRO D C   
6503 O O   . PRO D 213 ? 1.51057 2.15030 1.63643 -0.12338 -0.07303 -0.11483 213 PRO D O   
6504 C CB  . PRO D 213 ? 1.53568 2.03843 1.62985 -0.15941 -0.04511 -0.11121 213 PRO D CB  
6505 C CG  . PRO D 213 ? 1.57043 2.08068 1.65192 -0.16357 -0.04480 -0.11592 213 PRO D CG  
6506 C CD  . PRO D 213 ? 1.53097 2.11665 1.61818 -0.15366 -0.05758 -0.12461 213 PRO D CD  
6507 N N   . SER D 214 ? 1.56259 2.12290 1.68909 -0.15460 -0.05164 -0.11961 214 SER D N   
6508 C CA  . SER D 214 ? 1.48757 2.06649 1.62810 -0.13866 -0.05911 -0.11245 214 SER D CA  
6509 C C   . SER D 214 ? 1.43835 2.00678 1.57809 -0.10311 -0.07196 -0.08569 214 SER D C   
6510 O O   . SER D 214 ? 1.40501 1.94002 1.53361 -0.09252 -0.07325 -0.07107 214 SER D O   
6511 C CB  . SER D 214 ? 1.46176 1.99576 1.60472 -0.15296 -0.04736 -0.11334 214 SER D CB  
6512 O OG  . SER D 214 ? 1.50414 1.96881 1.63617 -0.14826 -0.04224 -0.09600 214 SER D OG  
6513 N N   . GLU D 215 ? 1.38187 1.97963 1.53286 -0.08508 -0.08022 -0.08021 215 GLU D N   
6514 C CA  . GLU D 215 ? 1.26595 1.85699 1.41509 -0.05108 -0.09045 -0.05647 215 GLU D CA  
6515 C C   . GLU D 215 ? 1.22394 1.74312 1.36827 -0.04463 -0.08594 -0.03652 215 GLU D C   
6516 O O   . GLU D 215 ? 1.22471 1.70409 1.35856 -0.04948 -0.08145 -0.03069 215 GLU D O   
6517 C CB  . GLU D 215 ? 1.05620 1.69236 1.21781 -0.03493 -0.09793 -0.05681 215 GLU D CB  
6518 N N   . ASP D 219 ? 1.43229 1.57116 1.43503 -0.24035 0.05613  -0.11414 219 ASP D N   
6519 C CA  . ASP D 219 ? 1.43546 1.54763 1.44392 -0.22269 0.05193  -0.09711 219 ASP D CA  
6520 C C   . ASP D 219 ? 1.47707 1.61916 1.50522 -0.19692 0.02972  -0.08007 219 ASP D C   
6521 O O   . ASP D 219 ? 1.49353 1.61197 1.52045 -0.17856 0.02377  -0.06287 219 ASP D O   
6522 C CB  . ASP D 219 ? 1.31152 1.35872 1.30093 -0.21568 0.06336  -0.08532 219 ASP D CB  
6523 N N   . PRO D 220 ? 1.56241 1.75431 1.60799 -0.19521 0.01901  -0.08496 220 PRO D N   
6524 C CA  . PRO D 220 ? 1.52177 1.74571 1.58276 -0.17119 -0.00037 -0.07061 220 PRO D CA  
6525 C C   . PRO D 220 ? 1.50232 1.69407 1.56780 -0.14816 -0.00718 -0.04831 220 PRO D C   
6526 O O   . PRO D 220 ? 1.50986 1.72418 1.58814 -0.13003 -0.02024 -0.03764 220 PRO D O   
6527 C CB  . PRO D 220 ? 1.51600 1.79256 1.59205 -0.17525 -0.00635 -0.08183 220 PRO D CB  
6528 C CG  . PRO D 220 ? 1.53976 1.82998 1.60878 -0.20492 0.00757  -0.10681 220 PRO D CG  
6529 C CD  . PRO D 220 ? 1.57660 1.80255 1.62655 -0.21707 0.02571  -0.10675 220 PRO D CD  
6530 N N   . LEU D 221 ? 1.42595 1.56603 1.48036 -0.14851 0.00249  -0.04204 221 LEU D N   
6531 C CA  . LEU D 221 ? 1.45269 1.56477 1.50976 -0.12769 -0.00362 -0.02268 221 LEU D CA  
6532 C C   . LEU D 221 ? 1.52554 1.65043 1.58528 -0.11368 -0.01367 -0.01271 221 LEU D C   
6533 O O   . LEU D 221 ? 1.51312 1.62932 1.57998 -0.09583 -0.02116 0.00214  221 LEU D O   
6534 C CB  . LEU D 221 ? 1.43086 1.49104 1.47225 -0.13054 0.00915  -0.02006 221 LEU D CB  
6535 N N   . SER D 222 ? 1.52429 1.66903 1.57744 -0.12215 -0.01285 -0.02131 222 SER D N   
6536 C CA  . SER D 222 ? 1.50454 1.65735 1.55583 -0.11049 -0.01986 -0.01283 222 SER D CA  
6537 C C   . SER D 222 ? 1.48567 1.67403 1.54882 -0.09317 -0.03352 -0.00443 222 SER D C   
6538 O O   . SER D 222 ? 1.48979 1.72161 1.55602 -0.09560 -0.03869 -0.01313 222 SER D O   
6539 C CB  . SER D 222 ? 1.48139 1.64770 1.52100 -0.12588 -0.01435 -0.02647 222 SER D CB  
6540 O OG  . SER D 222 ? 1.44715 1.66024 1.49137 -0.13694 -0.01683 -0.04185 222 SER D OG  
6541 N N   . LEU D 223 ? 1.48179 1.65246 1.55038 -0.07507 -0.03854 0.01199  223 LEU D N   
6542 C CA  . LEU D 223 ? 1.48948 1.68485 1.56627 -0.05701 -0.04875 0.02158  223 LEU D CA  
6543 C C   . LEU D 223 ? 1.49009 1.66415 1.56420 -0.04075 -0.05067 0.03738  223 LEU D C   
6544 O O   . LEU D 223 ? 1.47799 1.61668 1.54984 -0.04199 -0.04531 0.04211  223 LEU D O   
6545 C CB  . LEU D 223 ? 1.51715 1.71423 1.60585 -0.05280 -0.05109 0.02369  223 LEU D CB  
6546 N N   . PRO D 224 ? 1.49406 1.68901 1.56746 -0.02444 -0.05734 0.04569  224 PRO D N   
6547 C CA  . PRO D 224 ? 1.49548 1.67261 1.56458 -0.00792 -0.05777 0.06075  224 PRO D CA  
6548 C C   . PRO D 224 ? 1.46161 1.60615 1.53883 -0.00194 -0.05507 0.07017  224 PRO D C   
6549 O O   . PRO D 224 ? 1.43202 1.55767 1.50637 0.00881  -0.05298 0.08106  224 PRO D O   
6550 C CB  . PRO D 224 ? 1.40236 1.61352 1.46818 0.00866  -0.06467 0.06556  224 PRO D CB  
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