data_7H6B
# 
_entry.id   7H6B 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7H6B         pdb_00007h6b 10.2210/pdb7h6b/pdb 
WWPDB D_1001407078 ?            ?                   
# 
_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       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7H6B 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Rudolph 
_pdbx_contact_author.name_first         Markus 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              markus.rudolph@roche.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0447-1101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Banner, D.W.'  1 
'Benz, J.M.'    2 
'Schlatter, D.' 3 
'Hilpert, H.'   4 
# 
_citation.id                        primary 
_citation.title                     'Crystal structures of human Chymase and Cathepsin G' 
_citation.journal_abbrev            'To be published' 
_citation.year                      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Markus, R.'    1 0000-0003-0447-1101 
primary 'Tosstorff, A.' 2 0000-0002-4969-3667 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Chymase                                                                                   25050.904 1  3.4.21.39 
C28S ? ? 
2 non-polymer syn 'methyl 4-(5-fluoro-3-methyl-1-benzothiophene-2-sulfonamido)-3-(methanesulfonyl)benzoate' 457.516   1  ?         
?    ? ? 
3 water       nat water                                                                                     18.015    65 ?         
?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Alpha-chymase,Mast cell protease I' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'methyl 4-(5-fluoro-3-methyl-1-benzothiophene-2-sulfonamido)-3-(methanesulfonyl)benzoate' A1AO9 
3 water                                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   ILE n 
1 3   GLY n 
1 4   GLY n 
1 5   THR n 
1 6   GLU n 
1 7   SER n 
1 8   LYS n 
1 9   PRO n 
1 10  HIS n 
1 11  SER n 
1 12  ARG n 
1 13  PRO n 
1 14  TYR n 
1 15  MET n 
1 16  ALA n 
1 17  TYR n 
1 18  LEU n 
1 19  GLU n 
1 20  ILE n 
1 21  VAL n 
1 22  THR n 
1 23  SER n 
1 24  ASN n 
1 25  GLY n 
1 26  PRO n 
1 27  SER n 
1 28  LYS n 
1 29  PHE n 
1 30  CYS n 
1 31  GLY n 
1 32  GLY n 
1 33  PHE n 
1 34  LEU n 
1 35  ILE n 
1 36  ARG n 
1 37  ARG n 
1 38  ASN n 
1 39  PHE n 
1 40  VAL n 
1 41  LEU n 
1 42  THR n 
1 43  ALA n 
1 44  ALA n 
1 45  HIS n 
1 46  CYS n 
1 47  ALA n 
1 48  GLY n 
1 49  ARG n 
1 50  SER n 
1 51  ILE n 
1 52  THR n 
1 53  VAL n 
1 54  THR n 
1 55  LEU n 
1 56  GLY n 
1 57  ALA n 
1 58  HIS n 
1 59  ASN n 
1 60  ILE n 
1 61  THR n 
1 62  GLU n 
1 63  GLU n 
1 64  GLU n 
1 65  ASP n 
1 66  THR n 
1 67  TRP n 
1 68  GLN n 
1 69  LYS n 
1 70  LEU n 
1 71  GLU n 
1 72  VAL n 
1 73  ILE n 
1 74  LYS n 
1 75  GLN n 
1 76  PHE n 
1 77  ARG n 
1 78  HIS n 
1 79  PRO n 
1 80  LYS n 
1 81  TYR n 
1 82  ASN n 
1 83  THR n 
1 84  SER n 
1 85  THR n 
1 86  LEU n 
1 87  HIS n 
1 88  HIS n 
1 89  ASP n 
1 90  ILE n 
1 91  MET n 
1 92  LEU n 
1 93  LEU n 
1 94  LYS n 
1 95  LEU n 
1 96  LYS n 
1 97  GLU n 
1 98  LYS n 
1 99  ALA n 
1 100 SER n 
1 101 LEU n 
1 102 THR n 
1 103 LEU n 
1 104 ALA n 
1 105 VAL n 
1 106 GLY n 
1 107 THR n 
1 108 LEU n 
1 109 PRO n 
1 110 PHE n 
1 111 PRO n 
1 112 SER n 
1 113 GLN n 
1 114 PHE n 
1 115 ASN n 
1 116 PHE n 
1 117 VAL n 
1 118 PRO n 
1 119 PRO n 
1 120 GLY n 
1 121 ARG n 
1 122 MET n 
1 123 CYS n 
1 124 ARG n 
1 125 VAL n 
1 126 ALA n 
1 127 GLY n 
1 128 TRP n 
1 129 GLY n 
1 130 ARG n 
1 131 THR n 
1 132 GLY n 
1 133 VAL n 
1 134 LEU n 
1 135 LYS n 
1 136 PRO n 
1 137 GLY n 
1 138 SER n 
1 139 ASP n 
1 140 THR n 
1 141 LEU n 
1 142 GLN n 
1 143 GLU n 
1 144 VAL n 
1 145 LYS n 
1 146 LEU n 
1 147 ARG n 
1 148 LEU n 
1 149 MET n 
1 150 ASP n 
1 151 PRO n 
1 152 GLN n 
1 153 ALA n 
1 154 CYS n 
1 155 SER n 
1 156 HIS n 
1 157 PHE n 
1 158 ARG n 
1 159 ASP n 
1 160 PHE n 
1 161 ASP n 
1 162 HIS n 
1 163 ASN n 
1 164 LEU n 
1 165 GLN n 
1 166 LEU n 
1 167 CYS n 
1 168 VAL n 
1 169 GLY n 
1 170 ASN n 
1 171 PRO n 
1 172 ARG n 
1 173 LYS n 
1 174 THR n 
1 175 LYS n 
1 176 SER n 
1 177 ALA n 
1 178 PHE n 
1 179 LYS n 
1 180 GLY n 
1 181 ASP n 
1 182 SER n 
1 183 GLY n 
1 184 GLY n 
1 185 PRO n 
1 186 LEU n 
1 187 LEU n 
1 188 CYS n 
1 189 ALA n 
1 190 GLY n 
1 191 VAL n 
1 192 ALA n 
1 193 GLN n 
1 194 GLY n 
1 195 ILE n 
1 196 VAL n 
1 197 SER n 
1 198 TYR n 
1 199 GLY n 
1 200 ARG n 
1 201 SER n 
1 202 ASP n 
1 203 ALA n 
1 204 LYS n 
1 205 PRO n 
1 206 PRO n 
1 207 ALA n 
1 208 VAL n 
1 209 PHE n 
1 210 THR n 
1 211 ARG n 
1 212 ILE n 
1 213 SER n 
1 214 HIS n 
1 215 TYR n 
1 216 ARG n 
1 217 PRO n 
1 218 TRP n 
1 219 ILE n 
1 220 ASN n 
1 221 GLN n 
1 222 ILE n 
1 223 LEU n 
1 224 GLN n 
1 225 ALA n 
1 226 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   226 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CMA1, CYH, CYM' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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 
A1AO9 non-polymer         . 'methyl 4-(5-fluoro-3-methyl-1-benzothiophene-2-sulfonamido)-3-(methanesulfonyl)benzoate' ? 
'C18 H16 F N O6 S3' 457.516 
ALA   'L-peptide linking' y ALANINE                                                                                   ? 
'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE                                                                                  ? 
'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                ? 
'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                           ? 
'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                  ? 
'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                 ? 
'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                           ? 
'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                                   ? 
'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                 ? 
'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                                     ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                ? 
'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                   ? 
'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                                    ? 
'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                                                ? 
'C5 H11 N O2 S'     149.211 
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   ILE 1   16  16  ILE ILE A . n 
A 1 2   ILE 2   17  17  ILE ILE A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   THR 5   20  20  THR THR A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   SER 7   22  22  SER SER A . n 
A 1 8   LYS 8   23  23  LYS LYS A . n 
A 1 9   PRO 9   24  24  PRO PRO A . n 
A 1 10  HIS 10  25  25  HIS HIS A . n 
A 1 11  SER 11  26  26  SER SER A . n 
A 1 12  ARG 12  27  27  ARG ARG A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  MET 15  30  30  MET MET A . n 
A 1 16  ALA 16  31  31  ALA ALA A . n 
A 1 17  TYR 17  32  32  TYR TYR A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  GLU 19  34  34  GLU GLU A . n 
A 1 20  ILE 20  35  35  ILE ILE A . n 
A 1 21  VAL 21  36  36  VAL VAL A . n 
A 1 22  THR 22  36  36  THR THR A A n 
A 1 23  SER 23  36  36  SER SER A B n 
A 1 24  ASN 24  36  ?   ?   ?   A C n 
A 1 25  GLY 25  36  ?   ?   ?   A D n 
A 1 26  PRO 26  38  38  PRO PRO A . n 
A 1 27  SER 27  39  39  SER SER A . n 
A 1 28  LYS 28  40  40  LYS LYS A . n 
A 1 29  PHE 29  41  41  PHE PHE A . n 
A 1 30  CYS 30  42  42  CYS CYS A . n 
A 1 31  GLY 31  43  43  GLY GLY A . n 
A 1 32  GLY 32  44  44  GLY GLY A . n 
A 1 33  PHE 33  45  45  PHE PHE A . n 
A 1 34  LEU 34  46  46  LEU LEU A . n 
A 1 35  ILE 35  47  47  ILE ILE A . n 
A 1 36  ARG 36  48  48  ARG ARG A . n 
A 1 37  ARG 37  49  49  ARG ARG A . n 
A 1 38  ASN 38  50  50  ASN ASN A . n 
A 1 39  PHE 39  51  51  PHE PHE A . n 
A 1 40  VAL 40  52  52  VAL VAL A . n 
A 1 41  LEU 41  53  53  LEU LEU A . n 
A 1 42  THR 42  54  54  THR THR A . n 
A 1 43  ALA 43  55  55  ALA ALA A . n 
A 1 44  ALA 44  56  56  ALA ALA A . n 
A 1 45  HIS 45  57  57  HIS HIS A . n 
A 1 46  CYS 46  58  58  CYS CYS A . n 
A 1 47  ALA 47  59  59  ALA ALA A . n 
A 1 48  GLY 48  60  60  GLY GLY A . n 
A 1 49  ARG 49  61  61  ARG ARG A . n 
A 1 50  SER 50  63  63  SER SER A . n 
A 1 51  ILE 51  64  64  ILE ILE A . n 
A 1 52  THR 52  65  65  THR THR A . n 
A 1 53  VAL 53  66  66  VAL VAL A . n 
A 1 54  THR 54  67  67  THR THR A . n 
A 1 55  LEU 55  68  68  LEU LEU A . n 
A 1 56  GLY 56  69  69  GLY GLY A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  HIS 58  71  71  HIS HIS A . n 
A 1 59  ASN 59  72  72  ASN ASN A . n 
A 1 60  ILE 60  73  73  ILE ILE A . n 
A 1 61  THR 61  74  74  THR THR A . n 
A 1 62  GLU 62  75  75  GLU GLU A . n 
A 1 63  GLU 63  76  76  GLU GLU A . n 
A 1 64  GLU 64  77  77  GLU GLU A . n 
A 1 65  ASP 65  78  78  ASP ASP A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  TRP 67  80  80  TRP TRP A . n 
A 1 68  GLN 68  81  81  GLN GLN A . n 
A 1 69  LYS 69  82  82  LYS LYS A . n 
A 1 70  LEU 70  83  83  LEU LEU A . n 
A 1 71  GLU 71  84  84  GLU GLU A . n 
A 1 72  VAL 72  85  85  VAL VAL A . n 
A 1 73  ILE 73  86  86  ILE ILE A . n 
A 1 74  LYS 74  87  87  LYS LYS A . n 
A 1 75  GLN 75  88  88  GLN GLN A . n 
A 1 76  PHE 76  89  89  PHE PHE A . n 
A 1 77  ARG 77  90  90  ARG ARG A . n 
A 1 78  HIS 78  91  91  HIS HIS A . n 
A 1 79  PRO 79  92  92  PRO PRO A . n 
A 1 80  LYS 80  93  93  LYS LYS A . n 
A 1 81  TYR 81  94  94  TYR TYR A . n 
A 1 82  ASN 82  95  95  ASN ASN A . n 
A 1 83  THR 83  96  96  THR THR A . n 
A 1 84  SER 84  97  97  SER SER A . n 
A 1 85  THR 85  98  98  THR THR A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  HIS 87  100 100 HIS HIS A . n 
A 1 88  HIS 88  101 101 HIS HIS A . n 
A 1 89  ASP 89  102 102 ASP ASP A . n 
A 1 90  ILE 90  103 103 ILE ILE A . n 
A 1 91  MET 91  104 104 MET MET A . n 
A 1 92  LEU 92  105 105 LEU LEU A . n 
A 1 93  LEU 93  106 106 LEU LEU A . n 
A 1 94  LYS 94  107 107 LYS LYS A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LYS 96  109 109 LYS LYS A . n 
A 1 97  GLU 97  110 110 GLU GLU A . n 
A 1 98  LYS 98  111 111 LYS LYS A . n 
A 1 99  ALA 99  112 112 ALA ALA A . n 
A 1 100 SER 100 113 113 SER SER A . n 
A 1 101 LEU 101 114 114 LEU LEU A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 LEU 103 116 116 LEU LEU A . n 
A 1 104 ALA 104 117 117 ALA ALA A . n 
A 1 105 VAL 105 118 118 VAL VAL A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 THR 107 120 120 THR THR A . n 
A 1 108 LEU 108 121 121 LEU LEU A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PHE 110 123 123 PHE PHE A . n 
A 1 111 PRO 111 124 124 PRO PRO A . n 
A 1 112 SER 112 125 125 SER SER A . n 
A 1 113 GLN 113 126 126 GLN GLN A . n 
A 1 114 PHE 114 127 127 PHE PHE A . n 
A 1 115 ASN 115 128 128 ASN ASN A . n 
A 1 116 PHE 116 129 129 PHE PHE A . n 
A 1 117 VAL 117 130 130 VAL VAL A . n 
A 1 118 PRO 118 131 131 PRO PRO A . n 
A 1 119 PRO 119 132 132 PRO PRO A . n 
A 1 120 GLY 120 133 133 GLY GLY A . n 
A 1 121 ARG 121 134 134 ARG ARG A . n 
A 1 122 MET 122 135 135 MET MET A . n 
A 1 123 CYS 123 136 136 CYS CYS A . n 
A 1 124 ARG 124 137 137 ARG ARG A . n 
A 1 125 VAL 125 138 138 VAL VAL A . n 
A 1 126 ALA 126 139 139 ALA ALA A . n 
A 1 127 GLY 127 140 140 GLY GLY A . n 
A 1 128 TRP 128 141 141 TRP TRP A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 ARG 130 143 143 ARG ARG A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 GLY 132 145 145 GLY GLY A . n 
A 1 133 VAL 133 146 146 VAL VAL A . n 
A 1 134 LEU 134 147 147 LEU LEU A . n 
A 1 135 LYS 135 148 148 LYS LYS A . n 
A 1 136 PRO 136 150 150 PRO PRO A . n 
A 1 137 GLY 137 151 151 GLY GLY A . n 
A 1 138 SER 138 152 152 SER SER A . n 
A 1 139 ASP 139 153 153 ASP ASP A . n 
A 1 140 THR 140 154 154 THR THR A . n 
A 1 141 LEU 141 155 155 LEU LEU A . n 
A 1 142 GLN 142 156 156 GLN GLN A . n 
A 1 143 GLU 143 157 157 GLU GLU A . n 
A 1 144 VAL 144 158 158 VAL VAL A . n 
A 1 145 LYS 145 159 159 LYS LYS A . n 
A 1 146 LEU 146 160 160 LEU LEU A . n 
A 1 147 ARG 147 161 161 ARG ARG A . n 
A 1 148 LEU 148 162 162 LEU LEU A . n 
A 1 149 MET 149 163 163 MET MET A . n 
A 1 150 ASP 150 164 164 ASP ASP A . n 
A 1 151 PRO 151 165 165 PRO PRO A . n 
A 1 152 GLN 152 166 166 GLN GLN A . n 
A 1 153 ALA 153 167 167 ALA ALA A . n 
A 1 154 CYS 154 168 168 CYS CYS A . n 
A 1 155 SER 155 169 169 SER SER A . n 
A 1 156 HIS 156 172 172 HIS HIS A . n 
A 1 157 PHE 157 173 173 PHE PHE A . n 
A 1 158 ARG 158 174 174 ARG ARG A . n 
A 1 159 ASP 159 175 175 ASP ASP A . n 
A 1 160 PHE 160 176 176 PHE PHE A . n 
A 1 161 ASP 161 177 177 ASP ASP A . n 
A 1 162 HIS 162 178 178 HIS HIS A . n 
A 1 163 ASN 163 178 178 ASN ASN A A n 
A 1 164 LEU 164 179 179 LEU LEU A . n 
A 1 165 GLN 165 180 180 GLN GLN A . n 
A 1 166 LEU 166 181 181 LEU LEU A . n 
A 1 167 CYS 167 182 182 CYS CYS A . n 
A 1 168 VAL 168 183 183 VAL VAL A . n 
A 1 169 GLY 169 184 184 GLY GLY A . n 
A 1 170 ASN 170 185 185 ASN ASN A . n 
A 1 171 PRO 171 186 186 PRO PRO A . n 
A 1 172 ARG 172 186 186 ARG ARG A A n 
A 1 173 LYS 173 186 186 LYS LYS A B n 
A 1 174 THR 174 187 187 THR THR A . n 
A 1 175 LYS 175 188 188 LYS LYS A . n 
A 1 176 SER 176 189 189 SER SER A . n 
A 1 177 ALA 177 190 190 ALA ALA A . n 
A 1 178 PHE 178 191 191 PHE PHE A . n 
A 1 179 LYS 179 192 192 LYS LYS A . n 
A 1 180 GLY 180 193 193 GLY GLY A . n 
A 1 181 ASP 181 194 194 ASP ASP A . n 
A 1 182 SER 182 195 195 SER SER A . n 
A 1 183 GLY 183 196 196 GLY GLY A . n 
A 1 184 GLY 184 197 197 GLY GLY A . n 
A 1 185 PRO 185 198 198 PRO PRO A . n 
A 1 186 LEU 186 199 199 LEU LEU A . n 
A 1 187 LEU 187 200 200 LEU LEU A . n 
A 1 188 CYS 188 201 201 CYS CYS A . n 
A 1 189 ALA 189 202 202 ALA ALA A . n 
A 1 190 GLY 190 207 207 GLY GLY A . n 
A 1 191 VAL 191 208 208 VAL VAL A . n 
A 1 192 ALA 192 209 209 ALA ALA A . n 
A 1 193 GLN 193 210 210 GLN GLN A . n 
A 1 194 GLY 194 211 211 GLY GLY A . n 
A 1 195 ILE 195 212 212 ILE ILE A . n 
A 1 196 VAL 196 213 213 VAL VAL A . n 
A 1 197 SER 197 214 214 SER SER A . n 
A 1 198 TYR 198 215 215 TYR TYR A . n 
A 1 199 GLY 199 216 216 GLY GLY A . n 
A 1 200 ARG 200 217 217 ARG ARG A . n 
A 1 201 SER 201 218 218 SER SER A . n 
A 1 202 ASP 202 219 219 ASP ASP A . n 
A 1 203 ALA 203 220 220 ALA ALA A . n 
A 1 204 LYS 204 221 221 LYS LYS A . n 
A 1 205 PRO 205 224 224 PRO PRO A . n 
A 1 206 PRO 206 225 225 PRO PRO A . n 
A 1 207 ALA 207 226 226 ALA ALA A . n 
A 1 208 VAL 208 227 227 VAL VAL A . n 
A 1 209 PHE 209 228 228 PHE PHE A . n 
A 1 210 THR 210 229 229 THR THR A . n 
A 1 211 ARG 211 230 230 ARG ARG A . n 
A 1 212 ILE 212 231 231 ILE ILE A . n 
A 1 213 SER 213 232 232 SER SER A . n 
A 1 214 HIS 214 233 233 HIS HIS A . n 
A 1 215 TYR 215 234 234 TYR TYR A . n 
A 1 216 ARG 216 235 235 ARG ARG A . n 
A 1 217 PRO 217 236 236 PRO PRO A . n 
A 1 218 TRP 218 237 237 TRP TRP A . n 
A 1 219 ILE 219 238 238 ILE ILE A . n 
A 1 220 ASN 220 239 239 ASN ASN A . n 
A 1 221 GLN 221 240 240 GLN GLN A . n 
A 1 222 ILE 222 241 241 ILE ALA A . n 
A 1 223 LEU 223 242 242 LEU ALA A . n 
A 1 224 GLN 224 243 ?   ?   ?   A . n 
A 1 225 ALA 225 244 ?   ?   ?   A . n 
A 1 226 ASN 226 245 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AO9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AO9 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AO9 1  301 301 A1AO9 021 A . 
C 3 HOH   1  401 69  HOH   HOH A . 
C 3 HOH   2  402 86  HOH   HOH A . 
C 3 HOH   3  403 57  HOH   HOH A . 
C 3 HOH   4  404 83  HOH   HOH A . 
C 3 HOH   5  405 77  HOH   HOH A . 
C 3 HOH   6  406 37  HOH   HOH A . 
C 3 HOH   7  407 38  HOH   HOH A . 
C 3 HOH   8  408 30  HOH   HOH A . 
C 3 HOH   9  409 18  HOH   HOH A . 
C 3 HOH   10 410 21  HOH   HOH A . 
C 3 HOH   11 411 39  HOH   HOH A . 
C 3 HOH   12 412 53  HOH   HOH A . 
C 3 HOH   13 413 20  HOH   HOH A . 
C 3 HOH   14 414 23  HOH   HOH A . 
C 3 HOH   15 415 43  HOH   HOH A . 
C 3 HOH   16 416 5   HOH   HOH A . 
C 3 HOH   17 417 16  HOH   HOH A . 
C 3 HOH   18 418 32  HOH   HOH A . 
C 3 HOH   19 419 6   HOH   HOH A . 
C 3 HOH   20 420 76  HOH   HOH A . 
C 3 HOH   21 421 13  HOH   HOH A . 
C 3 HOH   22 422 7   HOH   HOH A . 
C 3 HOH   23 423 52  HOH   HOH A . 
C 3 HOH   24 424 8   HOH   HOH A . 
C 3 HOH   25 425 50  HOH   HOH A . 
C 3 HOH   26 426 35  HOH   HOH A . 
C 3 HOH   27 427 46  HOH   HOH A . 
C 3 HOH   28 428 22  HOH   HOH A . 
C 3 HOH   29 429 54  HOH   HOH A . 
C 3 HOH   30 430 79  HOH   HOH A . 
C 3 HOH   31 431 51  HOH   HOH A . 
C 3 HOH   32 432 19  HOH   HOH A . 
C 3 HOH   33 433 49  HOH   HOH A . 
C 3 HOH   34 434 10  HOH   HOH A . 
C 3 HOH   35 435 82  HOH   HOH A . 
C 3 HOH   36 436 11  HOH   HOH A . 
C 3 HOH   37 437 4   HOH   HOH A . 
C 3 HOH   38 438 36  HOH   HOH A . 
C 3 HOH   39 439 48  HOH   HOH A . 
C 3 HOH   40 440 45  HOH   HOH A . 
C 3 HOH   41 441 9   HOH   HOH A . 
C 3 HOH   42 442 3   HOH   HOH A . 
C 3 HOH   43 443 14  HOH   HOH A . 
C 3 HOH   44 444 42  HOH   HOH A . 
C 3 HOH   45 445 25  HOH   HOH A . 
C 3 HOH   46 446 58  HOH   HOH A . 
C 3 HOH   47 447 73  HOH   HOH A . 
C 3 HOH   48 448 12  HOH   HOH A . 
C 3 HOH   49 449 27  HOH   HOH A . 
C 3 HOH   50 450 26  HOH   HOH A . 
C 3 HOH   51 451 17  HOH   HOH A . 
C 3 HOH   52 452 84  HOH   HOH A . 
C 3 HOH   53 453 60  HOH   HOH A . 
C 3 HOH   54 454 28  HOH   HOH A . 
C 3 HOH   55 455 24  HOH   HOH A . 
C 3 HOH   56 456 75  HOH   HOH A . 
C 3 HOH   57 457 2   HOH   HOH A . 
C 3 HOH   58 458 72  HOH   HOH A . 
C 3 HOH   59 459 31  HOH   HOH A . 
C 3 HOH   60 460 15  HOH   HOH A . 
C 3 HOH   61 461 67  HOH   HOH A . 
C 3 HOH   62 462 47  HOH   HOH A . 
C 3 HOH   63 463 85  HOH   HOH A . 
C 3 HOH   64 464 87  HOH   HOH A . 
C 3 HOH   65 465 66  HOH   HOH A . 
# 
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 241 ? CG1 ? A ILE 222 CG1 
2 1 Y 1 A ILE 241 ? CG2 ? A ILE 222 CG2 
3 1 Y 1 A ILE 241 ? CD1 ? A ILE 222 CD1 
4 1 Y 1 A LEU 242 ? CG  ? A LEU 223 CG  
5 1 Y 1 A LEU 242 ? CD1 ? A LEU 223 CD1 
6 1 Y 1 A LEU 242 ? CD2 ? A LEU 223 CD2 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       PHENIX '(1.21_5207: ???)' ? 1 ? ? ? ? 
'data scaling'   XSCALE .                  ? 2 ? ? ? ? 
'data reduction' XDS    .                  ? 3 ? ? ? ? 
phasing          PHASER .                  ? 4 ? ? ? ? 
# 
_cell.entry_id           7H6B 
_cell.length_a           46.580 
_cell.length_b           53.520 
_cell.length_c           65.260 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7H6B 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          7H6B 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.66 
_exptl_crystal.density_percent_sol   25.96 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
;Sample of human Chymase in 50 mM MES/NaOH pH 5.5, 150mM NaCl, 1mM TCEP, 10% Glycerol) at a concentration of 11mg/ml to 14mg/ml.Add [2-[(4-methylpyridin-2-yl)amino]-2-oxoethyl] 2-methylquinoline-4-carboxylate at 10x molar ratio. The compound helps to obtain crystals but is not visible in the structures. Add 0.5 mM ZnCl2. Add inhibitor, incubate for 16h on ice. Crystallize using microbatch setups with Al's oil (Hampton Research), with total drop size 1ul with 50% protein sample, using crystallization reagent of 0.1M Tris/HCl pH 8.5, 0.2M NaCl, 25% PEG 3350.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                               1 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.pdbx_collection_date   2004-11-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'BRUKER AXS MICROSTAR' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H6B 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             18.96 
_reflns.d_resolution_high            2.18 
_reflns.number_obs                   8882 
_reflns.percent_possible_obs         96.3 
_reflns.pdbx_Rmerge_I_obs            0.077 
_reflns.pdbx_netI_over_sigmaI        13.69 
_reflns.pdbx_Rrim_I_all              0.088 
_reflns.pdbx_number_measured_all     36488 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_CC_star                 ? 
_reflns.pdbx_Rpim_I_all              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.number_unique_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_Rpim_I_all 
1 1 2.18 2.31  4395 1161 0.404 82.6 3.60  0.465 ? ? ? ? ? ? ? ? 
1 2 2.31 2.47  5936 1343 0.336 99.6 4.98  0.379 ? ? ? ? ? ? ? ? 
1 3 2.47 2.66  5295 1204 0.241 99.8 6.63  0.272 ? ? ? ? ? ? ? ? 
1 4 2.66 2.91  5036 1150 0.166 99.3 8.91  0.187 ? ? ? ? ? ? ? ? 
1 5 2.91 3.24  4464 1029 0.089 99.6 14.46 0.101 ? ? ? ? ? ? ? ? 
1 6 3.24 3.72  4019 932  0.051 99.6 22.49 0.057 ? ? ? ? ? ? ? ? 
1 7 3.72 4.51  3369 797  0.044 99.3 26.23 0.05  ? ? ? ? ? ? ? ? 
1 8 4.51 6.2   2663 648  0.036 99.1 30.21 0.042 ? ? ? ? ? ? ? ? 
1 9 6.20 18.96 1311 389  0.028 87.4 33.57 0.033 ? ? ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7H6B 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     8880 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.40 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             18.96 
_refine.ls_d_res_high                            2.17 
_refine.ls_percent_reflns_obs                    98.25 
_refine.ls_R_factor_obs                          0.2019 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2000 
_refine.ls_R_factor_R_free                       0.2389 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.76 
_refine.ls_number_reflns_R_free                  423 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.00 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.60 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.30 
_refine.pdbx_overall_phase_error                 27.70 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1721 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             65 
_refine_hist.number_atoms_total               1815 
_refine_hist.d_res_high                       2.17 
_refine_hist.d_res_low                        18.96 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.002  ? ? 1796 'X-RAY DIFFRACTION' ? 
f_angle_d          0.513  ? ? 2436 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 13.898 ? ? 675  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.044  ? ? 261  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 311  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.17 2.48  2666 0.2369 95.00  0.2973 . . 138 . . . . 
'X-RAY DIFFRACTION' . 2.48 3.13  2834 0.2223 100.00 0.2516 . . 145 . . . . 
'X-RAY DIFFRACTION' . 3.13 18.96 2957 0.1781 100.00 0.2138 . . 140 . . . . 
# 
_struct.entry_id                  7H6B 
_struct.title                     
;THE 2.17 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH methyl 4-[(5-fluoro-3-methyl-1-benzothiophen-2-yl)sulfonylamino]-3-methylsulfonylbenzoate (TOA EIYO INHIBITOR)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H6B 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'HUMAN CHYMASE, SERINE PROTEINASE, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CMA1_HUMAN 
_struct_ref.pdbx_db_accession          P23946 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7H6B 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 226 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P23946 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       245 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             7H6B 
_struct_ref_seq_dif.mon_id                       SER 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      7 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P23946 
_struct_ref_seq_dif.db_mon_id                    CYS 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          28 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            22 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 43  ? ALA A 47  ? ALA A 55  ALA A 59  5 ? 5 
HELX_P HELX_P2 AA2 ASP A 150 ? SER A 155 ? ASP A 164 SER A 169 5 ? 6 
HELX_P HELX_P3 AA3 TYR A 215 ? ASN A 220 ? TYR A 234 ASN A 239 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 30  SG ? ? ? 1_555 A CYS 46  SG ? ? A CYS 42  A CYS 58  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2 disulf ? ? A CYS 123 SG ? ? ? 1_555 A CYS 188 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? A CYS 154 SG ? ? ? 1_555 A CYS 167 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 30  ? CYS A 46  ? CYS A 42  ? 1_555 CYS A 58  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 123 ? CYS A 188 ? CYS A 136 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 154 ? CYS A 167 ? CYS A 168 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           205 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            224 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    206 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     225 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       4.10 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 5   ? GLU A 6   ? THR A 20  GLU A 21  
AA1 2 GLN A 142 ? ARG A 147 ? GLN A 156 ARG A 161 
AA1 3 MET A 122 ? GLY A 127 ? MET A 135 GLY A 140 
AA1 4 PRO A 185 ? CYS A 188 ? PRO A 198 CYS A 201 
AA1 5 VAL A 191 ? TYR A 198 ? VAL A 208 TYR A 215 
AA1 6 ALA A 207 ? ARG A 211 ? ALA A 226 ARG A 230 
AA1 7 GLN A 165 ? VAL A 168 ? GLN A 180 VAL A 183 
AA2 1 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
AA2 2 SER A 27  ? ARG A 36  ? SER A 39  ARG A 48  
AA2 3 PHE A 39  ? THR A 42  ? PHE A 51  THR A 54  
AA2 4 MET A 91  ? LEU A 95  ? MET A 104 LEU A 108 
AA2 5 GLN A 68  ? ARG A 77  ? GLN A 81  ARG A 90  
AA2 6 SER A 50  ? LEU A 55  ? SER A 63  LEU A 68  
AA2 7 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 5   ? N THR A 20  O GLU A 143 ? O GLU A 157 
AA1 2 3 O LEU A 146 ? O LEU A 160 N CYS A 123 ? N CYS A 136 
AA1 3 4 N ARG A 124 ? N ARG A 137 O LEU A 187 ? O LEU A 200 
AA1 4 5 N LEU A 186 ? N LEU A 199 O GLY A 194 ? O GLY A 211 
AA1 5 6 N TYR A 198 ? N TYR A 215 O VAL A 208 ? O VAL A 227 
AA1 6 7 O ALA A 207 ? O ALA A 226 N VAL A 168 ? N VAL A 183 
AA2 1 2 N ALA A 16  ? N ALA A 31  O GLY A 32  ? O GLY A 44  
AA2 2 3 N PHE A 33  ? N PHE A 45  O LEU A 41  ? O LEU A 53  
AA2 3 4 N THR A 42  ? N THR A 54  O MET A 91  ? O MET A 104 
AA2 4 5 O LEU A 92  ? O LEU A 105 N PHE A 76  ? N PHE A 89  
AA2 5 6 O LEU A 70  ? O LEU A 83  N VAL A 53  ? N VAL A 66  
AA2 6 7 O SER A 50  ? O SER A 63  N VAL A 21  ? N VAL A 36  
# 
_pdbx_entry_details.entry_id                   7H6B 
_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   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 THR A 115 ? ? -128.58 -169.52 
2 1 LEU A 147 ? ? 67.55   -1.32   
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 33.8902 -2.5175 24.9256 0.2347 0.2044 0.1857 -0.0169 0.0161  -0.0327 1.6069 3.1161 0.1646 1.2388  
0.3065  0.5808  -0.0325 0.3626  -0.1783 -0.2149 0.2992  -0.6234 -0.0514 0.0937  -0.0163 
'X-RAY DIFFRACTION' 2 ? refined 17.2349 -1.1868 23.2697 0.3048 0.1452 0.1085 0.0458  0.0198  -0.0447 2.4167 0.4138 0.5341 0.7449  
0.3275  0.4005  -0.0798 0.3932  0.2366  -0.1057 -0.2128 0.0977  -0.1252 -0.0724 -0.3221 
'X-RAY DIFFRACTION' 3 ? refined 15.9417 -3.6174 25.2769 0.2125 0.1250 0.1223 -0.0151 0.0073  -0.0123 1.7037 1.2680 0.9305 -0.3851 
-0.4345 0.4676  -0.0831 0.1146  0.0114  0.0209  0.0275  0.1548  0.2203  -0.2380 0.0464  
'X-RAY DIFFRACTION' 4 ? refined 25.4240 -4.3106 29.7912 0.3009 0.1516 0.1726 0.0093  -0.0392 0.0346  0.7885 0.4393 0.3323 -0.1245 
-0.4818 -0.0499 -0.0658 -0.2345 -0.1565 0.2103  -0.0262 -0.1220 0.2017  0.1385  -0.0947 
'X-RAY DIFFRACTION' 5 ? refined 25.1628 7.8846  42.7239 0.3133 0.3631 0.2107 -0.0194 -0.0563 -0.0215 1.6012 1.0535 1.4684 -0.9194 
-0.6389 -0.4311 -0.0065 -0.5264 -0.2793 0.2122  0.0858  0.0824  0.0485  0.1656  -0.0015 
'X-RAY DIFFRACTION' 6 ? refined 23.6961 2.2179  37.1409 0.2113 0.1672 0.1357 0.0148  0.0083  0.0170  1.6792 2.2707 1.7058 0.3603  
-0.1219 0.0177  -0.0291 -0.3929 -0.0475 0.1001  -0.1146 -0.1940 -0.0954 0.3050  0.0191  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 16 through 29 )
;
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 30 through 48 )
;
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 49 through 103 )
;
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 104 through 155 )
;
'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 156 through 179 )
;
'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 180 through 242 )
;
# 
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 ASN 36  C A ASN 24  
2 1 Y 1 A GLY 36  D A GLY 25  
3 1 Y 1 A GLN 243 ? A GLN 224 
4 1 Y 1 A ALA 244 ? A ALA 225 
5 1 Y 1 A ASN 245 ? A ASN 226 
# 
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 
A1AO9 C14  C N N 1   
A1AO9 C17  C Y N 2   
A1AO9 C21  C N N 3   
A1AO9 C10  C Y N 4   
A1AO9 C11  C Y N 5   
A1AO9 C12  C Y N 6   
A1AO9 C16  C Y N 7   
A1AO9 C22  C Y N 8   
A1AO9 C23  C Y N 9   
A1AO9 C24  C N N 10  
A1AO9 C27  C N N 11  
A1AO9 C28  C Y N 12  
A1AO9 C29  C Y N 13  
A1AO9 C4   C Y N 14  
A1AO9 C5   C Y N 15  
A1AO9 C6   C Y N 16  
A1AO9 C7   C Y N 17  
A1AO9 C9   C Y N 18  
A1AO9 F13  F N N 19  
A1AO9 N15  N N N 20  
A1AO9 O19  O N N 21  
A1AO9 O2   O N N 22  
A1AO9 O20  O N N 23  
A1AO9 O25  O N N 24  
A1AO9 O26  O N N 25  
A1AO9 O3   O N N 26  
A1AO9 S1   S N N 27  
A1AO9 S18  S N N 28  
A1AO9 S8   S Y N 29  
A1AO9 H1   H N N 30  
A1AO9 H2   H N N 31  
A1AO9 H3   H N N 32  
A1AO9 H4   H N N 33  
A1AO9 H5   H N N 34  
A1AO9 H6   H N N 35  
A1AO9 H7   H N N 36  
A1AO9 H8   H N N 37  
A1AO9 H9   H N N 38  
A1AO9 H10  H N N 39  
A1AO9 H11  H N N 40  
A1AO9 H12  H N N 41  
A1AO9 H13  H N N 42  
A1AO9 H14  H N N 43  
A1AO9 H15  H N N 44  
A1AO9 H16  H N N 45  
ALA   N    N N N 46  
ALA   CA   C N S 47  
ALA   C    C N N 48  
ALA   O    O N N 49  
ALA   CB   C N N 50  
ALA   OXT  O N N 51  
ALA   H    H N N 52  
ALA   H2   H N N 53  
ALA   HA   H N N 54  
ALA   HB1  H N N 55  
ALA   HB2  H N N 56  
ALA   HB3  H N N 57  
ALA   HXT  H N N 58  
ARG   N    N N N 59  
ARG   CA   C N S 60  
ARG   C    C N N 61  
ARG   O    O N N 62  
ARG   CB   C N N 63  
ARG   CG   C N N 64  
ARG   CD   C N N 65  
ARG   NE   N N N 66  
ARG   CZ   C N N 67  
ARG   NH1  N N N 68  
ARG   NH2  N N N 69  
ARG   OXT  O N N 70  
ARG   H    H N N 71  
ARG   H2   H N N 72  
ARG   HA   H N N 73  
ARG   HB2  H N N 74  
ARG   HB3  H N N 75  
ARG   HG2  H N N 76  
ARG   HG3  H N N 77  
ARG   HD2  H N N 78  
ARG   HD3  H N N 79  
ARG   HE   H N N 80  
ARG   HH11 H N N 81  
ARG   HH12 H N N 82  
ARG   HH21 H N N 83  
ARG   HH22 H N N 84  
ARG   HXT  H N N 85  
ASN   N    N N N 86  
ASN   CA   C N S 87  
ASN   C    C N N 88  
ASN   O    O N N 89  
ASN   CB   C N N 90  
ASN   CG   C N N 91  
ASN   OD1  O N N 92  
ASN   ND2  N N N 93  
ASN   OXT  O N N 94  
ASN   H    H N N 95  
ASN   H2   H N N 96  
ASN   HA   H N N 97  
ASN   HB2  H N N 98  
ASN   HB3  H N N 99  
ASN   HD21 H N N 100 
ASN   HD22 H N N 101 
ASN   HXT  H N N 102 
ASP   N    N N N 103 
ASP   CA   C N S 104 
ASP   C    C N N 105 
ASP   O    O N N 106 
ASP   CB   C N N 107 
ASP   CG   C N N 108 
ASP   OD1  O N N 109 
ASP   OD2  O N N 110 
ASP   OXT  O N N 111 
ASP   H    H N N 112 
ASP   H2   H N N 113 
ASP   HA   H N N 114 
ASP   HB2  H N N 115 
ASP   HB3  H N N 116 
ASP   HD2  H N N 117 
ASP   HXT  H N N 118 
CYS   N    N N N 119 
CYS   CA   C N R 120 
CYS   C    C N N 121 
CYS   O    O N N 122 
CYS   CB   C N N 123 
CYS   SG   S N N 124 
CYS   OXT  O N N 125 
CYS   H    H N N 126 
CYS   H2   H N N 127 
CYS   HA   H N N 128 
CYS   HB2  H N N 129 
CYS   HB3  H N N 130 
CYS   HG   H N N 131 
CYS   HXT  H N N 132 
GLN   N    N N N 133 
GLN   CA   C N S 134 
GLN   C    C N N 135 
GLN   O    O N N 136 
GLN   CB   C N N 137 
GLN   CG   C N N 138 
GLN   CD   C N N 139 
GLN   OE1  O N N 140 
GLN   NE2  N N N 141 
GLN   OXT  O N N 142 
GLN   H    H N N 143 
GLN   H2   H N N 144 
GLN   HA   H N N 145 
GLN   HB2  H N N 146 
GLN   HB3  H N N 147 
GLN   HG2  H N N 148 
GLN   HG3  H N N 149 
GLN   HE21 H N N 150 
GLN   HE22 H N N 151 
GLN   HXT  H N N 152 
GLU   N    N N N 153 
GLU   CA   C N S 154 
GLU   C    C N N 155 
GLU   O    O N N 156 
GLU   CB   C N N 157 
GLU   CG   C N N 158 
GLU   CD   C N N 159 
GLU   OE1  O N N 160 
GLU   OE2  O N N 161 
GLU   OXT  O N N 162 
GLU   H    H N N 163 
GLU   H2   H N N 164 
GLU   HA   H N N 165 
GLU   HB2  H N N 166 
GLU   HB3  H N N 167 
GLU   HG2  H N N 168 
GLU   HG3  H N N 169 
GLU   HE2  H N N 170 
GLU   HXT  H N N 171 
GLY   N    N N N 172 
GLY   CA   C N N 173 
GLY   C    C N N 174 
GLY   O    O N N 175 
GLY   OXT  O N N 176 
GLY   H    H N N 177 
GLY   H2   H N N 178 
GLY   HA2  H N N 179 
GLY   HA3  H N N 180 
GLY   HXT  H N N 181 
HIS   N    N N N 182 
HIS   CA   C N S 183 
HIS   C    C N N 184 
HIS   O    O N N 185 
HIS   CB   C N N 186 
HIS   CG   C Y N 187 
HIS   ND1  N Y N 188 
HIS   CD2  C Y N 189 
HIS   CE1  C Y N 190 
HIS   NE2  N Y N 191 
HIS   OXT  O N N 192 
HIS   H    H N N 193 
HIS   H2   H N N 194 
HIS   HA   H N N 195 
HIS   HB2  H N N 196 
HIS   HB3  H N N 197 
HIS   HD1  H N N 198 
HIS   HD2  H N N 199 
HIS   HE1  H N N 200 
HIS   HE2  H N N 201 
HIS   HXT  H N N 202 
HOH   O    O N N 203 
HOH   H1   H N N 204 
HOH   H2   H N N 205 
ILE   N    N N N 206 
ILE   CA   C N S 207 
ILE   C    C N N 208 
ILE   O    O N N 209 
ILE   CB   C N S 210 
ILE   CG1  C N N 211 
ILE   CG2  C N N 212 
ILE   CD1  C N N 213 
ILE   OXT  O N N 214 
ILE   H    H N N 215 
ILE   H2   H N N 216 
ILE   HA   H N N 217 
ILE   HB   H N N 218 
ILE   HG12 H N N 219 
ILE   HG13 H N N 220 
ILE   HG21 H N N 221 
ILE   HG22 H N N 222 
ILE   HG23 H N N 223 
ILE   HD11 H N N 224 
ILE   HD12 H N N 225 
ILE   HD13 H N N 226 
ILE   HXT  H N N 227 
LEU   N    N N N 228 
LEU   CA   C N S 229 
LEU   C    C N N 230 
LEU   O    O N N 231 
LEU   CB   C N N 232 
LEU   CG   C N N 233 
LEU   CD1  C N N 234 
LEU   CD2  C N N 235 
LEU   OXT  O N N 236 
LEU   H    H N N 237 
LEU   H2   H N N 238 
LEU   HA   H N N 239 
LEU   HB2  H N N 240 
LEU   HB3  H N N 241 
LEU   HG   H N N 242 
LEU   HD11 H N N 243 
LEU   HD12 H N N 244 
LEU   HD13 H N N 245 
LEU   HD21 H N N 246 
LEU   HD22 H N N 247 
LEU   HD23 H N N 248 
LEU   HXT  H N N 249 
LYS   N    N N N 250 
LYS   CA   C N S 251 
LYS   C    C N N 252 
LYS   O    O N N 253 
LYS   CB   C N N 254 
LYS   CG   C N N 255 
LYS   CD   C N N 256 
LYS   CE   C N N 257 
LYS   NZ   N N N 258 
LYS   OXT  O N N 259 
LYS   H    H N N 260 
LYS   H2   H N N 261 
LYS   HA   H N N 262 
LYS   HB2  H N N 263 
LYS   HB3  H N N 264 
LYS   HG2  H N N 265 
LYS   HG3  H N N 266 
LYS   HD2  H N N 267 
LYS   HD3  H N N 268 
LYS   HE2  H N N 269 
LYS   HE3  H N N 270 
LYS   HZ1  H N N 271 
LYS   HZ2  H N N 272 
LYS   HZ3  H N N 273 
LYS   HXT  H N N 274 
MET   N    N N N 275 
MET   CA   C N S 276 
MET   C    C N N 277 
MET   O    O N N 278 
MET   CB   C N N 279 
MET   CG   C N N 280 
MET   SD   S N N 281 
MET   CE   C N N 282 
MET   OXT  O N N 283 
MET   H    H N N 284 
MET   H2   H N N 285 
MET   HA   H N N 286 
MET   HB2  H N N 287 
MET   HB3  H N N 288 
MET   HG2  H N N 289 
MET   HG3  H N N 290 
MET   HE1  H N N 291 
MET   HE2  H N N 292 
MET   HE3  H N N 293 
MET   HXT  H N N 294 
PHE   N    N N N 295 
PHE   CA   C N S 296 
PHE   C    C N N 297 
PHE   O    O N N 298 
PHE   CB   C N N 299 
PHE   CG   C Y N 300 
PHE   CD1  C Y N 301 
PHE   CD2  C Y N 302 
PHE   CE1  C Y N 303 
PHE   CE2  C Y N 304 
PHE   CZ   C Y N 305 
PHE   OXT  O N N 306 
PHE   H    H N N 307 
PHE   H2   H N N 308 
PHE   HA   H N N 309 
PHE   HB2  H N N 310 
PHE   HB3  H N N 311 
PHE   HD1  H N N 312 
PHE   HD2  H N N 313 
PHE   HE1  H N N 314 
PHE   HE2  H N N 315 
PHE   HZ   H N N 316 
PHE   HXT  H N N 317 
PRO   N    N N N 318 
PRO   CA   C N S 319 
PRO   C    C N N 320 
PRO   O    O N N 321 
PRO   CB   C N N 322 
PRO   CG   C N N 323 
PRO   CD   C N N 324 
PRO   OXT  O N N 325 
PRO   H    H N N 326 
PRO   HA   H N N 327 
PRO   HB2  H N N 328 
PRO   HB3  H N N 329 
PRO   HG2  H N N 330 
PRO   HG3  H N N 331 
PRO   HD2  H N N 332 
PRO   HD3  H N N 333 
PRO   HXT  H N N 334 
SER   N    N N N 335 
SER   CA   C N S 336 
SER   C    C N N 337 
SER   O    O N N 338 
SER   CB   C N N 339 
SER   OG   O N N 340 
SER   OXT  O N N 341 
SER   H    H N N 342 
SER   H2   H N N 343 
SER   HA   H N N 344 
SER   HB2  H N N 345 
SER   HB3  H N N 346 
SER   HG   H N N 347 
SER   HXT  H N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TRP   N    N N N 366 
TRP   CA   C N S 367 
TRP   C    C N N 368 
TRP   O    O N N 369 
TRP   CB   C N N 370 
TRP   CG   C Y N 371 
TRP   CD1  C Y N 372 
TRP   CD2  C Y N 373 
TRP   NE1  N Y N 374 
TRP   CE2  C Y N 375 
TRP   CE3  C Y N 376 
TRP   CZ2  C Y N 377 
TRP   CZ3  C Y N 378 
TRP   CH2  C Y N 379 
TRP   OXT  O N N 380 
TRP   H    H N N 381 
TRP   H2   H N N 382 
TRP   HA   H N N 383 
TRP   HB2  H N N 384 
TRP   HB3  H N N 385 
TRP   HD1  H N N 386 
TRP   HE1  H N N 387 
TRP   HE3  H N N 388 
TRP   HZ2  H N N 389 
TRP   HZ3  H N N 390 
TRP   HH2  H N N 391 
TRP   HXT  H N N 392 
TYR   N    N N N 393 
TYR   CA   C N S 394 
TYR   C    C N N 395 
TYR   O    O N N 396 
TYR   CB   C N N 397 
TYR   CG   C Y N 398 
TYR   CD1  C Y N 399 
TYR   CD2  C Y N 400 
TYR   CE1  C Y N 401 
TYR   CE2  C Y N 402 
TYR   CZ   C Y N 403 
TYR   OH   O N N 404 
TYR   OXT  O N N 405 
TYR   H    H N N 406 
TYR   H2   H N N 407 
TYR   HA   H N N 408 
TYR   HB2  H N N 409 
TYR   HB3  H N N 410 
TYR   HD1  H N N 411 
TYR   HD2  H N N 412 
TYR   HE1  H N N 413 
TYR   HE2  H N N 414 
TYR   HH   H N N 415 
TYR   HXT  H N N 416 
VAL   N    N N N 417 
VAL   CA   C N S 418 
VAL   C    C N N 419 
VAL   O    O N N 420 
VAL   CB   C N N 421 
VAL   CG1  C N N 422 
VAL   CG2  C N N 423 
VAL   OXT  O N N 424 
VAL   H    H N N 425 
VAL   H2   H N N 426 
VAL   HA   H N N 427 
VAL   HB   H N N 428 
VAL   HG11 H N N 429 
VAL   HG12 H N N 430 
VAL   HG13 H N N 431 
VAL   HG21 H N N 432 
VAL   HG22 H N N 433 
VAL   HG23 H N N 434 
VAL   HXT  H N N 435 
# 
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 
A1AO9 O2  S1   doub N N 1   
A1AO9 S1  O3   doub N N 2   
A1AO9 S1  N15  sing N N 3   
A1AO9 S1  C4   sing N N 4   
A1AO9 O19 S18  doub N N 5   
A1AO9 C14 C5   sing N N 6   
A1AO9 N15 C16  sing N N 7   
A1AO9 C4  C5   doub Y N 8   
A1AO9 C4  S8   sing Y N 9   
A1AO9 C5  C6   sing Y N 10  
A1AO9 C21 S18  sing N N 11  
A1AO9 S8  C7   sing Y N 12  
A1AO9 C6  C12  doub Y N 13  
A1AO9 C6  C7   sing Y N 14  
A1AO9 S18 O20  doub N N 15  
A1AO9 S18 C17  sing N N 16  
A1AO9 C12 C11  sing Y N 17  
A1AO9 C7  C9   doub Y N 18  
A1AO9 C16 C17  doub Y N 19  
A1AO9 C16 C29  sing Y N 20  
A1AO9 C11 F13  sing N N 21  
A1AO9 C11 C10  doub Y N 22  
A1AO9 C9  C10  sing Y N 23  
A1AO9 C17 C22  sing Y N 24  
A1AO9 C29 C28  doub Y N 25  
A1AO9 C22 C23  doub Y N 26  
A1AO9 C28 C23  sing Y N 27  
A1AO9 C23 C24  sing N N 28  
A1AO9 C24 O26  sing N N 29  
A1AO9 C24 O25  doub N N 30  
A1AO9 O26 C27  sing N N 31  
A1AO9 C14 H1   sing N N 32  
A1AO9 C14 H2   sing N N 33  
A1AO9 C14 H3   sing N N 34  
A1AO9 C21 H4   sing N N 35  
A1AO9 C21 H5   sing N N 36  
A1AO9 C21 H6   sing N N 37  
A1AO9 C10 H7   sing N N 38  
A1AO9 C12 H8   sing N N 39  
A1AO9 C22 H9   sing N N 40  
A1AO9 C27 H10  sing N N 41  
A1AO9 C27 H11  sing N N 42  
A1AO9 C27 H12  sing N N 43  
A1AO9 C28 H13  sing N N 44  
A1AO9 C29 H14  sing N N 45  
A1AO9 C9  H15  sing N N 46  
A1AO9 N15 H16  sing N N 47  
ALA   N   CA   sing N N 48  
ALA   N   H    sing N N 49  
ALA   N   H2   sing N N 50  
ALA   CA  C    sing N N 51  
ALA   CA  CB   sing N N 52  
ALA   CA  HA   sing N N 53  
ALA   C   O    doub N N 54  
ALA   C   OXT  sing N N 55  
ALA   CB  HB1  sing N N 56  
ALA   CB  HB2  sing N N 57  
ALA   CB  HB3  sing N N 58  
ALA   OXT HXT  sing N N 59  
ARG   N   CA   sing N N 60  
ARG   N   H    sing N N 61  
ARG   N   H2   sing N N 62  
ARG   CA  C    sing N N 63  
ARG   CA  CB   sing N N 64  
ARG   CA  HA   sing N N 65  
ARG   C   O    doub N N 66  
ARG   C   OXT  sing N N 67  
ARG   CB  CG   sing N N 68  
ARG   CB  HB2  sing N N 69  
ARG   CB  HB3  sing N N 70  
ARG   CG  CD   sing N N 71  
ARG   CG  HG2  sing N N 72  
ARG   CG  HG3  sing N N 73  
ARG   CD  NE   sing N N 74  
ARG   CD  HD2  sing N N 75  
ARG   CD  HD3  sing N N 76  
ARG   NE  CZ   sing N N 77  
ARG   NE  HE   sing N N 78  
ARG   CZ  NH1  sing N N 79  
ARG   CZ  NH2  doub N N 80  
ARG   NH1 HH11 sing N N 81  
ARG   NH1 HH12 sing N N 82  
ARG   NH2 HH21 sing N N 83  
ARG   NH2 HH22 sing N N 84  
ARG   OXT HXT  sing N N 85  
ASN   N   CA   sing N N 86  
ASN   N   H    sing N N 87  
ASN   N   H2   sing N N 88  
ASN   CA  C    sing N N 89  
ASN   CA  CB   sing N N 90  
ASN   CA  HA   sing N N 91  
ASN   C   O    doub N N 92  
ASN   C   OXT  sing N N 93  
ASN   CB  CG   sing N N 94  
ASN   CB  HB2  sing N N 95  
ASN   CB  HB3  sing N N 96  
ASN   CG  OD1  doub N N 97  
ASN   CG  ND2  sing N N 98  
ASN   ND2 HD21 sing N N 99  
ASN   ND2 HD22 sing N N 100 
ASN   OXT HXT  sing N N 101 
ASP   N   CA   sing N N 102 
ASP   N   H    sing N N 103 
ASP   N   H2   sing N N 104 
ASP   CA  C    sing N N 105 
ASP   CA  CB   sing N N 106 
ASP   CA  HA   sing N N 107 
ASP   C   O    doub N N 108 
ASP   C   OXT  sing N N 109 
ASP   CB  CG   sing N N 110 
ASP   CB  HB2  sing N N 111 
ASP   CB  HB3  sing N N 112 
ASP   CG  OD1  doub N N 113 
ASP   CG  OD2  sing N N 114 
ASP   OD2 HD2  sing N N 115 
ASP   OXT HXT  sing N N 116 
CYS   N   CA   sing N N 117 
CYS   N   H    sing N N 118 
CYS   N   H2   sing N N 119 
CYS   CA  C    sing N N 120 
CYS   CA  CB   sing N N 121 
CYS   CA  HA   sing N N 122 
CYS   C   O    doub N N 123 
CYS   C   OXT  sing N N 124 
CYS   CB  SG   sing N N 125 
CYS   CB  HB2  sing N N 126 
CYS   CB  HB3  sing N N 127 
CYS   SG  HG   sing N N 128 
CYS   OXT HXT  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002292 
_pdbx_deposit_group.group_description   'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_title         'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_type          undefined 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'apo structure' 
# 
_atom_sites.entry_id                    7H6B 
_atom_sites.fract_transf_matrix[1][1]   0.021468 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018685 
_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]   0.015323 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE   A 1 1   ? 28.727 6.850   26.550 1.00 14.77 ? 16  ILE   A N   1 
ATOM   2    C CA  . ILE   A 1 1   ? 29.881 6.696   27.426 1.00 17.50 ? 16  ILE   A CA  1 
ATOM   3    C C   . ILE   A 1 1   ? 30.838 7.865   27.230 1.00 18.57 ? 16  ILE   A C   1 
ATOM   4    O O   . ILE   A 1 1   ? 31.352 8.082   26.132 1.00 19.17 ? 16  ILE   A O   1 
ATOM   5    C CB  . ILE   A 1 1   ? 30.590 5.355   27.181 1.00 16.77 ? 16  ILE   A CB  1 
ATOM   6    C CG1 . ILE   A 1 1   ? 29.634 4.188   27.445 1.00 15.92 ? 16  ILE   A CG1 1 
ATOM   7    C CG2 . ILE   A 1 1   ? 31.829 5.244   28.054 1.00 18.72 ? 16  ILE   A CG2 1 
ATOM   8    C CD1 . ILE   A 1 1   ? 29.167 4.089   28.882 1.00 18.19 ? 16  ILE   A CD1 1 
ATOM   9    N N   . ILE   A 1 2   ? 31.078 8.612   28.303 1.00 18.91 ? 17  ILE   A N   1 
ATOM   10   C CA  . ILE   A 1 2   ? 31.899 9.816   28.270 1.00 21.81 ? 17  ILE   A CA  1 
ATOM   11   C C   . ILE   A 1 2   ? 33.237 9.518   28.933 1.00 21.27 ? 17  ILE   A C   1 
ATOM   12   O O   . ILE   A 1 2   ? 33.281 8.952   30.032 1.00 21.56 ? 17  ILE   A O   1 
ATOM   13   C CB  . ILE   A 1 2   ? 31.194 10.994  28.963 1.00 20.77 ? 17  ILE   A CB  1 
ATOM   14   C CG1 . ILE   A 1 2   ? 29.840 11.263  28.307 1.00 20.03 ? 17  ILE   A CG1 1 
ATOM   15   C CG2 . ILE   A 1 2   ? 32.064 12.240  28.916 1.00 23.44 ? 17  ILE   A CG2 1 
ATOM   16   C CD1 . ILE   A 1 2   ? 29.087 12.405  28.934 1.00 16.38 ? 17  ILE   A CD1 1 
ATOM   17   N N   . GLY   A 1 3   ? 34.324 9.896   28.262 1.00 20.65 ? 18  GLY   A N   1 
ATOM   18   C CA  . GLY   A 1 3   ? 35.647 9.741   28.832 1.00 20.46 ? 18  GLY   A CA  1 
ATOM   19   C C   . GLY   A 1 3   ? 36.165 8.324   28.879 1.00 22.64 ? 18  GLY   A C   1 
ATOM   20   O O   . GLY   A 1 3   ? 37.095 8.041   29.637 1.00 24.91 ? 18  GLY   A O   1 
ATOM   21   N N   . GLY   A 1 4   ? 35.591 7.419   28.088 1.00 20.58 ? 19  GLY   A N   1 
ATOM   22   C CA  . GLY   A 1 4   ? 36.009 6.036   28.065 1.00 20.94 ? 19  GLY   A CA  1 
ATOM   23   C C   . GLY   A 1 4   ? 36.945 5.729   26.909 1.00 25.12 ? 19  GLY   A C   1 
ATOM   24   O O   . GLY   A 1 4   ? 37.388 6.609   26.168 1.00 28.80 ? 19  GLY   A O   1 
ATOM   25   N N   . THR   A 1 5   ? 37.249 4.443   26.766 1.00 24.42 ? 20  THR   A N   1 
ATOM   26   C CA  . THR   A 1 5   ? 38.090 3.946   25.689 1.00 26.33 ? 20  THR   A CA  1 
ATOM   27   C C   . THR   A 1 5   ? 37.337 2.863   24.933 1.00 23.72 ? 20  THR   A C   1 
ATOM   28   O O   . THR   A 1 5   ? 36.391 2.262   25.447 1.00 22.62 ? 20  THR   A O   1 
ATOM   29   C CB  . THR   A 1 5   ? 39.421 3.381   26.208 1.00 26.88 ? 20  THR   A CB  1 
ATOM   30   O OG1 . THR   A 1 5   ? 39.172 2.199   26.980 1.00 37.17 ? 20  THR   A OG1 1 
ATOM   31   C CG2 . THR   A 1 5   ? 40.137 4.405   27.076 1.00 32.39 ? 20  THR   A CG2 1 
ATOM   32   N N   . GLU   A 1 6   ? 37.765 2.626   23.695 1.00 26.95 ? 21  GLU   A N   1 
ATOM   33   C CA  . GLU   A 1 6   ? 37.165 1.568   22.895 1.00 28.50 ? 21  GLU   A CA  1 
ATOM   34   C C   . GLU   A 1 6   ? 37.399 0.213   23.547 1.00 26.52 ? 21  GLU   A C   1 
ATOM   35   O O   . GLU   A 1 6   ? 38.520 -0.113  23.948 1.00 25.93 ? 21  GLU   A O   1 
ATOM   36   C CB  . GLU   A 1 6   ? 37.747 1.573   21.481 1.00 32.26 ? 21  GLU   A CB  1 
ATOM   37   C CG  . GLU   A 1 6   ? 36.758 1.971   20.404 1.00 35.45 ? 21  GLU   A CG  1 
ATOM   38   C CD  . GLU   A 1 6   ? 36.959 1.199   19.113 1.00 40.70 ? 21  GLU   A CD  1 
ATOM   39   O OE1 . GLU   A 1 6   ? 37.282 -0.005  19.183 1.00 41.70 ? 21  GLU   A OE1 1 
ATOM   40   O OE2 . GLU   A 1 6   ? 36.799 1.797   18.029 1.00 44.32 ? 21  GLU   A OE2 1 
ATOM   41   N N   . SER   A 1 7   ? 36.335 -0.575  23.652 1.00 24.29 ? 22  SER   A N   1 
ATOM   42   C CA  . SER   A 1 7   ? 36.472 -1.939  24.131 1.00 26.79 ? 22  SER   A CA  1 
ATOM   43   C C   . SER   A 1 7   ? 37.154 -2.797  23.072 1.00 27.42 ? 22  SER   A C   1 
ATOM   44   O O   . SER   A 1 7   ? 37.147 -2.483  21.879 1.00 32.67 ? 22  SER   A O   1 
ATOM   45   C CB  . SER   A 1 7   ? 35.105 -2.532  24.477 1.00 26.68 ? 22  SER   A CB  1 
ATOM   46   O OG  . SER   A 1 7   ? 34.402 -1.713  25.395 1.00 28.99 ? 22  SER   A OG  1 
ATOM   47   N N   . LYS   A 1 8   ? 37.763 -3.884  23.521 1.00 28.92 ? 23  LYS   A N   1 
ATOM   48   C CA  . LYS   A 1 8   ? 38.219 -4.893  22.581 1.00 28.72 ? 23  LYS   A CA  1 
ATOM   49   C C   . LYS   A 1 8   ? 37.001 -5.471  21.870 1.00 30.62 ? 23  LYS   A C   1 
ATOM   50   O O   . LYS   A 1 8   ? 35.995 -5.774  22.528 1.00 30.24 ? 23  LYS   A O   1 
ATOM   51   C CB  . LYS   A 1 8   ? 38.997 -5.994  23.300 1.00 37.50 ? 23  LYS   A CB  1 
ATOM   52   C CG  . LYS   A 1 8   ? 40.175 -5.481  24.116 1.00 46.99 ? 23  LYS   A CG  1 
ATOM   53   C CD  . LYS   A 1 8   ? 40.982 -6.621  24.717 1.00 47.00 ? 23  LYS   A CD  1 
ATOM   54   C CE  . LYS   A 1 8   ? 42.150 -6.093  25.536 1.00 55.34 ? 23  LYS   A CE  1 
ATOM   55   N NZ  . LYS   A 1 8   ? 43.013 -7.192  26.049 1.00 61.20 ? 23  LYS   A NZ  1 
ATOM   56   N N   . PRO   A 1 9   ? 37.028 -5.605  20.545 1.00 32.39 ? 24  PRO   A N   1 
ATOM   57   C CA  . PRO   A 1 9   ? 35.825 -6.051  19.830 1.00 30.27 ? 24  PRO   A CA  1 
ATOM   58   C C   . PRO   A 1 9   ? 35.363 -7.418  20.315 1.00 29.83 ? 24  PRO   A C   1 
ATOM   59   O O   . PRO   A 1 9   ? 36.157 -8.353  20.445 1.00 28.13 ? 24  PRO   A O   1 
ATOM   60   C CB  . PRO   A 1 9   ? 36.274 -6.084  18.363 1.00 30.06 ? 24  PRO   A CB  1 
ATOM   61   C CG  . PRO   A 1 9   ? 37.766 -6.136  18.411 1.00 33.10 ? 24  PRO   A CG  1 
ATOM   62   C CD  . PRO   A 1 9   ? 38.161 -5.372  19.635 1.00 28.89 ? 24  PRO   A CD  1 
ATOM   63   N N   . HIS   A 1 10  ? 34.065 -7.511  20.606 1.00 27.87 ? 25  HIS   A N   1 
ATOM   64   C CA  . HIS   A 1 10  ? 33.410 -8.728  21.081 1.00 28.28 ? 25  HIS   A CA  1 
ATOM   65   C C   . HIS   A 1 10  ? 33.948 -9.199  22.430 1.00 25.69 ? 25  HIS   A C   1 
ATOM   66   O O   . HIS   A 1 10  ? 33.786 -10.370 22.792 1.00 28.23 ? 25  HIS   A O   1 
ATOM   67   C CB  . HIS   A 1 10  ? 33.511 -9.847  20.038 1.00 30.12 ? 25  HIS   A CB  1 
ATOM   68   C CG  . HIS   A 1 10  ? 33.236 -9.382  18.642 1.00 29.43 ? 25  HIS   A CG  1 
ATOM   69   N ND1 . HIS   A 1 10  ? 32.021 -8.854  18.260 1.00 28.04 ? 25  HIS   A ND1 1 
ATOM   70   C CD2 . HIS   A 1 10  ? 34.025 -9.346  17.542 1.00 30.06 ? 25  HIS   A CD2 1 
ATOM   71   C CE1 . HIS   A 1 10  ? 32.070 -8.522  16.982 1.00 30.95 ? 25  HIS   A CE1 1 
ATOM   72   N NE2 . HIS   A 1 10  ? 33.275 -8.810  16.523 1.00 38.07 ? 25  HIS   A NE2 1 
ATOM   73   N N   . SER   A 1 11  ? 34.585 -8.307  23.190 1.00 25.25 ? 26  SER   A N   1 
ATOM   74   C CA  . SER   A 1 11  ? 34.967 -8.616  24.562 1.00 28.65 ? 26  SER   A CA  1 
ATOM   75   C C   . SER   A 1 11  ? 33.813 -8.441  25.537 1.00 26.75 ? 26  SER   A C   1 
ATOM   76   O O   . SER   A 1 11  ? 33.967 -8.758  26.720 1.00 28.39 ? 26  SER   A O   1 
ATOM   77   C CB  . SER   A 1 11  ? 36.144 -7.743  25.000 1.00 28.44 ? 26  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 11  ? 35.777 -6.374  25.032 1.00 26.55 ? 26  SER   A OG  1 
ATOM   79   N N   . ARG   A 1 12  ? 32.676 -7.931  25.071 1.00 26.43 ? 27  ARG   A N   1 
ATOM   80   C CA  . ARG   A 1 12  ? 31.453 -7.822  25.864 1.00 23.43 ? 27  ARG   A CA  1 
ATOM   81   C C   . ARG   A 1 12  ? 30.312 -8.408  25.040 1.00 20.91 ? 27  ARG   A C   1 
ATOM   82   O O   . ARG   A 1 12  ? 29.415 -7.685  24.590 1.00 17.79 ? 27  ARG   A O   1 
ATOM   83   C CB  . ARG   A 1 12  ? 31.170 -6.369  26.247 1.00 21.26 ? 27  ARG   A CB  1 
ATOM   84   C CG  . ARG   A 1 12  ? 32.355 -5.619  26.844 1.00 23.33 ? 27  ARG   A CG  1 
ATOM   85   C CD  . ARG   A 1 12  ? 32.584 -6.002  28.294 1.00 26.66 ? 27  ARG   A CD  1 
ATOM   86   N NE  . ARG   A 1 12  ? 33.607 -5.177  28.928 1.00 38.36 ? 27  ARG   A NE  1 
ATOM   87   C CZ  . ARG   A 1 12  ? 34.861 -5.557  29.130 1.00 38.61 ? 27  ARG   A CZ  1 
ATOM   88   N NH1 . ARG   A 1 12  ? 35.290 -6.753  28.760 1.00 36.58 ? 27  ARG   A NH1 1 
ATOM   89   N NH2 . ARG   A 1 12  ? 35.706 -4.718  29.722 1.00 43.78 ? 27  ARG   A NH2 1 
ATOM   90   N N   . PRO   A 1 13  ? 30.320 -9.728  24.822 1.00 21.50 ? 28  PRO   A N   1 
ATOM   91   C CA  . PRO   A 1 13  ? 29.367 -10.329 23.873 1.00 20.94 ? 28  PRO   A CA  1 
ATOM   92   C C   . PRO   A 1 13  ? 27.920 -10.276 24.332 1.00 20.18 ? 28  PRO   A C   1 
ATOM   93   O O   . PRO   A 1 13  ? 27.024 -10.552 23.524 1.00 17.25 ? 28  PRO   A O   1 
ATOM   94   C CB  . PRO   A 1 13  ? 29.857 -11.778 23.760 1.00 22.59 ? 28  PRO   A CB  1 
ATOM   95   C CG  . PRO   A 1 13  ? 30.513 -12.042 25.072 1.00 23.41 ? 28  PRO   A CG  1 
ATOM   96   C CD  . PRO   A 1 13  ? 31.155 -10.745 25.485 1.00 21.98 ? 28  PRO   A CD  1 
ATOM   97   N N   . TYR   A 1 14  ? 27.665 -9.939  25.593 1.00 18.91 ? 29  TYR   A N   1 
ATOM   98   C CA  . TYR   A 1 14  ? 26.312 -9.823  26.111 1.00 18.76 ? 29  TYR   A CA  1 
ATOM   99   C C   . TYR   A 1 14  ? 25.677 -8.466  25.836 1.00 17.69 ? 29  TYR   A C   1 
ATOM   100  O O   . TYR   A 1 14  ? 24.458 -8.333  25.992 1.00 15.27 ? 29  TYR   A O   1 
ATOM   101  C CB  . TYR   A 1 14  ? 26.313 -10.088 27.620 1.00 19.93 ? 29  TYR   A CB  1 
ATOM   102  C CG  . TYR   A 1 14  ? 27.505 -9.479  28.317 1.00 20.91 ? 29  TYR   A CG  1 
ATOM   103  C CD1 . TYR   A 1 14  ? 27.514 -8.137  28.672 1.00 17.28 ? 29  TYR   A CD1 1 
ATOM   104  C CD2 . TYR   A 1 14  ? 28.628 -10.242 28.605 1.00 22.97 ? 29  TYR   A CD2 1 
ATOM   105  C CE1 . TYR   A 1 14  ? 28.607 -7.574  29.301 1.00 23.64 ? 29  TYR   A CE1 1 
ATOM   106  C CE2 . TYR   A 1 14  ? 29.724 -9.689  29.232 1.00 22.38 ? 29  TYR   A CE2 1 
ATOM   107  C CZ  . TYR   A 1 14  ? 29.708 -8.356  29.578 1.00 21.57 ? 29  TYR   A CZ  1 
ATOM   108  O OH  . TYR   A 1 14  ? 30.800 -7.807  30.203 1.00 24.20 ? 29  TYR   A OH  1 
ATOM   109  N N   . MET   A 1 15  ? 26.460 -7.471  25.421 1.00 16.48 ? 30  MET   A N   1 
ATOM   110  C CA  . MET   A 1 15  ? 25.929 -6.124  25.243 1.00 17.83 ? 30  MET   A CA  1 
ATOM   111  C C   . MET   A 1 15  ? 24.859 -6.093  24.158 1.00 16.90 ? 30  MET   A C   1 
ATOM   112  O O   . MET   A 1 15  ? 25.002 -6.710  23.099 1.00 17.05 ? 30  MET   A O   1 
ATOM   113  C CB  . MET   A 1 15  ? 27.055 -5.149  24.893 1.00 12.97 ? 30  MET   A CB  1 
ATOM   114  C CG  . MET   A 1 15  ? 27.974 -4.823  26.054 1.00 16.18 ? 30  MET   A CG  1 
ATOM   115  S SD  . MET   A 1 15  ? 27.083 -4.188  27.486 1.00 15.91 ? 30  MET   A SD  1 
ATOM   116  C CE  . MET   A 1 15  ? 26.278 -2.752  26.781 1.00 15.32 ? 30  MET   A CE  1 
ATOM   117  N N   . ALA   A 1 16  ? 23.785 -5.358  24.431 1.00 12.90 ? 31  ALA   A N   1 
ATOM   118  C CA  . ALA   A 1 16  ? 22.661 -5.221  23.519 1.00 14.03 ? 31  ALA   A CA  1 
ATOM   119  C C   . ALA   A 1 16  ? 22.425 -3.751  23.205 1.00 14.80 ? 31  ALA   A C   1 
ATOM   120  O O   . ALA   A 1 16  ? 22.509 -2.896  24.091 1.00 13.39 ? 31  ALA   A O   1 
ATOM   121  C CB  . ALA   A 1 16  ? 21.389 -5.836  24.109 1.00 13.41 ? 31  ALA   A CB  1 
ATOM   122  N N   . TYR   A 1 17  ? 22.125 -3.466  21.941 1.00 16.88 ? 32  TYR   A N   1 
ATOM   123  C CA  . TYR   A 1 17  ? 21.804 -2.122  21.478 1.00 14.83 ? 32  TYR   A CA  1 
ATOM   124  C C   . TYR   A 1 17  ? 20.323 -2.083  21.126 1.00 15.58 ? 32  TYR   A C   1 
ATOM   125  O O   . TYR   A 1 17  ? 19.855 -2.887  20.312 1.00 18.87 ? 32  TYR   A O   1 
ATOM   126  C CB  . TYR   A 1 17  ? 22.664 -1.744  20.272 1.00 15.64 ? 32  TYR   A CB  1 
ATOM   127  C CG  . TYR   A 1 17  ? 22.493 -0.316  19.807 1.00 19.75 ? 32  TYR   A CG  1 
ATOM   128  C CD1 . TYR   A 1 17  ? 23.083 0.733   20.499 1.00 21.81 ? 32  TYR   A CD1 1 
ATOM   129  C CD2 . TYR   A 1 17  ? 21.755 -0.018  18.669 1.00 20.13 ? 32  TYR   A CD2 1 
ATOM   130  C CE1 . TYR   A 1 17  ? 22.936 2.040   20.076 1.00 19.53 ? 32  TYR   A CE1 1 
ATOM   131  C CE2 . TYR   A 1 17  ? 21.603 1.286   18.238 1.00 18.35 ? 32  TYR   A CE2 1 
ATOM   132  C CZ  . TYR   A 1 17  ? 22.196 2.310   18.946 1.00 18.97 ? 32  TYR   A CZ  1 
ATOM   133  O OH  . TYR   A 1 17  ? 22.050 3.612   18.524 1.00 30.15 ? 32  TYR   A OH  1 
ATOM   134  N N   . LEU   A 1 18  ? 19.590 -1.154  21.733 1.00 15.16 ? 33  LEU   A N   1 
ATOM   135  C CA  . LEU   A 1 18  ? 18.140 -1.093  21.600 1.00 15.43 ? 33  LEU   A CA  1 
ATOM   136  C C   . LEU   A 1 18  ? 17.741 0.098   20.741 1.00 16.41 ? 33  LEU   A C   1 
ATOM   137  O O   . LEU   A 1 18  ? 18.122 1.237   21.033 1.00 16.67 ? 33  LEU   A O   1 
ATOM   138  C CB  . LEU   A 1 18  ? 17.460 -0.996  22.969 1.00 14.87 ? 33  LEU   A CB  1 
ATOM   139  C CG  . LEU   A 1 18  ? 17.801 -2.051  24.025 1.00 20.41 ? 33  LEU   A CG  1 
ATOM   140  C CD1 . LEU   A 1 18  ? 16.810 -2.000  25.183 1.00 14.77 ? 33  LEU   A CD1 1 
ATOM   141  C CD2 . LEU   A 1 18  ? 17.848 -3.441  23.418 1.00 17.93 ? 33  LEU   A CD2 1 
ATOM   142  N N   . GLU   A 1 19  ? 16.974 -0.171  19.689 1.00 17.06 ? 34  GLU   A N   1 
ATOM   143  C CA  . GLU   A 1 19  ? 16.347 0.859   18.869 1.00 18.14 ? 34  GLU   A CA  1 
ATOM   144  C C   . GLU   A 1 19  ? 14.862 0.844   19.207 1.00 20.61 ? 34  GLU   A C   1 
ATOM   145  O O   . GLU   A 1 19  ? 14.153 -0.111  18.873 1.00 21.62 ? 34  GLU   A O   1 
ATOM   146  C CB  . GLU   A 1 19  ? 16.588 0.604   17.382 1.00 21.64 ? 34  GLU   A CB  1 
ATOM   147  C CG  . GLU   A 1 19  ? 16.756 1.861   16.530 0.10 24.37 ? 34  GLU   A CG  1 
ATOM   148  C CD  . GLU   A 1 19  ? 15.449 2.588   16.263 0.10 26.04 ? 34  GLU   A CD  1 
ATOM   149  O OE1 . GLU   A 1 19  ? 14.829 3.095   17.221 0.10 26.08 ? 34  GLU   A OE1 1 
ATOM   150  O OE2 . GLU   A 1 19  ? 15.041 2.653   15.084 0.10 26.39 ? 34  GLU   A OE2 1 
ATOM   151  N N   . ILE   A 1 20  ? 14.397 1.899   19.871 1.00 19.49 ? 35  ILE   A N   1 
ATOM   152  C CA  . ILE   A 1 20  ? 13.056 1.956   20.440 1.00 25.63 ? 35  ILE   A CA  1 
ATOM   153  C C   . ILE   A 1 20  ? 12.221 2.933   19.628 1.00 27.69 ? 35  ILE   A C   1 
ATOM   154  O O   . ILE   A 1 20  ? 12.661 4.055   19.354 1.00 27.31 ? 35  ILE   A O   1 
ATOM   155  C CB  . ILE   A 1 20  ? 13.099 2.368   21.921 1.00 24.06 ? 35  ILE   A CB  1 
ATOM   156  C CG1 . ILE   A 1 20  ? 13.963 1.384   22.713 1.00 18.93 ? 35  ILE   A CG1 1 
ATOM   157  C CG2 . ILE   A 1 20  ? 11.693 2.448   22.497 1.00 19.23 ? 35  ILE   A CG2 1 
ATOM   158  C CD1 . ILE   A 1 20  ? 14.870 2.051   23.718 1.00 19.25 ? 35  ILE   A CD1 1 
ATOM   159  N N   . VAL   A 1 21  ? 11.022 2.508   19.241 1.00 27.50 ? 36  VAL   A N   1 
ATOM   160  C CA  . VAL   A 1 21  ? 10.086 3.340   18.494 1.00 30.13 ? 36  VAL   A CA  1 
ATOM   161  C C   . VAL   A 1 21  ? 8.894  3.643   19.388 1.00 32.63 ? 36  VAL   A C   1 
ATOM   162  O O   . VAL   A 1 21  ? 8.282  2.727   19.949 1.00 30.52 ? 36  VAL   A O   1 
ATOM   163  C CB  . VAL   A 1 21  ? 9.634  2.656   17.193 1.00 33.92 ? 36  VAL   A CB  1 
ATOM   164  C CG1 . VAL   A 1 21  ? 8.514  3.450   16.544 1.00 33.38 ? 36  VAL   A CG1 1 
ATOM   165  C CG2 . VAL   A 1 21  ? 10.807 2.505   16.240 1.00 32.89 ? 36  VAL   A CG2 1 
ATOM   166  N N   . THR   A 1 22  A 8.572  4.923   19.528 1.00 36.05 ? 36  THR   A N   1 
ATOM   167  C CA  . THR   A 1 22  A 7.407  5.324   20.297 1.00 39.37 ? 36  THR   A CA  1 
ATOM   168  C C   . THR   A 1 22  A 6.210  5.521   19.370 1.00 43.59 ? 36  THR   A C   1 
ATOM   169  O O   . THR   A 1 22  A 6.319  5.446   18.144 1.00 41.15 ? 36  THR   A O   1 
ATOM   170  C CB  . THR   A 1 22  A 7.695  6.601   21.084 1.00 43.42 ? 36  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 22  A 7.862  7.696   20.174 1.00 43.96 ? 36  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 22  A 8.962  6.441   21.906 1.00 38.83 ? 36  THR   A CG2 1 
ATOM   173  N N   . SER   A 1 23  B 5.052  5.771   19.971 1.00 46.01 ? 36  SER   A N   1 
ATOM   174  C CA  . SER   A 1 23  B 3.825  5.972   19.207 1.00 52.34 ? 36  SER   A CA  1 
ATOM   175  C C   . SER   A 1 23  B 3.729  7.391   18.650 1.00 47.57 ? 36  SER   A C   1 
ATOM   176  O O   . SER   A 1 23  B 4.719  8.121   18.598 1.00 46.76 ? 36  SER   A O   1 
ATOM   177  C CB  . SER   A 1 23  B 2.601  5.671   20.074 1.00 53.55 ? 36  SER   A CB  1 
ATOM   178  O OG  . SER   A 1 23  B 2.647  4.348   20.580 1.00 57.21 ? 36  SER   A OG  1 
ATOM   179  N N   . PRO   A 1 26  ? 8.900  9.442   17.107 1.00 37.53 ? 38  PRO   A N   1 
ATOM   180  C CA  . PRO   A 1 26  ? 10.168 9.666   17.809 1.00 41.38 ? 38  PRO   A CA  1 
ATOM   181  C C   . PRO   A 1 26  ? 10.797 8.365   18.298 1.00 43.23 ? 38  PRO   A C   1 
ATOM   182  O O   . PRO   A 1 26  ? 10.092 7.484   18.790 1.00 40.67 ? 38  PRO   A O   1 
ATOM   183  C CB  . PRO   A 1 26  ? 9.761  10.557  18.984 1.00 44.17 ? 38  PRO   A CB  1 
ATOM   184  C CG  . PRO   A 1 26  ? 8.577  11.303  18.478 1.00 50.28 ? 38  PRO   A CG  1 
ATOM   185  C CD  . PRO   A 1 26  ? 7.834  10.331  17.602 1.00 40.62 ? 38  PRO   A CD  1 
ATOM   186  N N   . SER   A 1 27  ? 12.115 8.251   18.166 1.00 34.24 ? 39  SER   A N   1 
ATOM   187  C CA  . SER   A 1 27  ? 12.826 7.025   18.489 1.00 32.16 ? 39  SER   A CA  1 
ATOM   188  C C   . SER   A 1 27  ? 13.795 7.249   19.644 1.00 32.22 ? 39  SER   A C   1 
ATOM   189  O O   . SER   A 1 27  ? 14.345 8.341   19.816 1.00 35.35 ? 39  SER   A O   1 
ATOM   190  C CB  . SER   A 1 27  ? 13.582 6.487   17.267 1.00 31.16 ? 39  SER   A CB  1 
ATOM   191  O OG  . SER   A 1 27  ? 14.297 7.520   16.612 1.00 44.95 ? 39  SER   A OG  1 
ATOM   192  N N   . LYS   A 1 28  ? 13.992 6.199   20.436 1.00 26.98 ? 40  LYS   A N   1 
ATOM   193  C CA  . LYS   A 1 28  ? 14.922 6.206   21.553 1.00 26.43 ? 40  LYS   A CA  1 
ATOM   194  C C   . LYS   A 1 28  ? 15.989 5.141   21.340 1.00 24.91 ? 40  LYS   A C   1 
ATOM   195  O O   . LYS   A 1 28  ? 15.787 4.163   20.614 1.00 23.86 ? 40  LYS   A O   1 
ATOM   196  C CB  . LYS   A 1 28  ? 14.207 5.956   22.889 1.00 21.95 ? 40  LYS   A CB  1 
ATOM   197  C CG  . LYS   A 1 28  ? 13.218 7.034   23.285 1.00 32.64 ? 40  LYS   A CG  1 
ATOM   198  C CD  . LYS   A 1 28  ? 12.757 6.858   24.725 1.00 34.37 ? 40  LYS   A CD  1 
ATOM   199  C CE  . LYS   A 1 28  ? 12.090 5.509   24.937 1.00 21.90 ? 40  LYS   A CE  1 
ATOM   200  N NZ  . LYS   A 1 28  ? 11.540 5.381   26.317 1.00 26.18 ? 40  LYS   A NZ  1 
ATOM   201  N N   . PHE   A 1 29  ? 17.135 5.345   21.984 1.00 18.58 ? 41  PHE   A N   1 
ATOM   202  C CA  . PHE   A 1 29  ? 18.252 4.414   21.910 1.00 17.80 ? 41  PHE   A CA  1 
ATOM   203  C C   . PHE   A 1 29  ? 18.729 4.109   23.321 1.00 21.42 ? 41  PHE   A C   1 
ATOM   204  O O   . PHE   A 1 29  ? 18.987 5.028   24.105 1.00 21.41 ? 41  PHE   A O   1 
ATOM   205  C CB  . PHE   A 1 29  ? 19.390 4.987   21.060 1.00 21.08 ? 41  PHE   A CB  1 
ATOM   206  C CG  . PHE   A 1 29  ? 18.981 5.323   19.652 1.00 23.95 ? 41  PHE   A CG  1 
ATOM   207  C CD1 . PHE   A 1 29  ? 19.082 4.379   18.644 1.00 25.62 ? 41  PHE   A CD1 1 
ATOM   208  C CD2 . PHE   A 1 29  ? 18.485 6.579   19.338 1.00 23.67 ? 41  PHE   A CD2 1 
ATOM   209  C CE1 . PHE   A 1 29  ? 18.705 4.681   17.348 1.00 26.40 ? 41  PHE   A CE1 1 
ATOM   210  C CE2 . PHE   A 1 29  ? 18.104 6.887   18.043 1.00 28.08 ? 41  PHE   A CE2 1 
ATOM   211  C CZ  . PHE   A 1 29  ? 18.214 5.936   17.047 1.00 26.75 ? 41  PHE   A CZ  1 
ATOM   212  N N   . CYS   A 1 30  ? 18.843 2.822   23.640 1.00 17.50 ? 42  CYS   A N   1 
ATOM   213  C CA  . CYS   A 1 30  ? 19.195 2.381   24.980 1.00 17.26 ? 42  CYS   A CA  1 
ATOM   214  C C   . CYS   A 1 30  ? 20.194 1.239   24.897 1.00 16.60 ? 42  CYS   A C   1 
ATOM   215  O O   . CYS   A 1 30  ? 20.460 0.686   23.826 1.00 15.56 ? 42  CYS   A O   1 
ATOM   216  C CB  . CYS   A 1 30  ? 17.963 1.926   25.771 1.00 15.97 ? 42  CYS   A CB  1 
ATOM   217  S SG  . CYS   A 1 30  ? 17.046 3.224   26.607 1.00 24.15 ? 42  CYS   A SG  1 
ATOM   218  N N   . GLY   A 1 31  ? 20.748 0.891   26.056 1.00 13.97 ? 43  GLY   A N   1 
ATOM   219  C CA  . GLY   A 1 31  ? 21.582 -0.280  26.191 1.00 13.77 ? 43  GLY   A CA  1 
ATOM   220  C C   . GLY   A 1 31  ? 20.844 -1.419  26.878 1.00 14.35 ? 43  GLY   A C   1 
ATOM   221  O O   . GLY   A 1 31  ? 19.713 -1.286  27.337 1.00 13.11 ? 43  GLY   A O   1 
ATOM   222  N N   . GLY   A 1 32  ? 21.519 -2.557  26.936 1.00 13.95 ? 44  GLY   A N   1 
ATOM   223  C CA  . GLY   A 1 32  ? 20.964 -3.735  27.576 1.00 12.27 ? 44  GLY   A CA  1 
ATOM   224  C C   . GLY   A 1 32  ? 21.978 -4.851  27.493 1.00 14.75 ? 44  GLY   A C   1 
ATOM   225  O O   . GLY   A 1 32  ? 23.017 -4.730  26.834 1.00 13.62 ? 44  GLY   A O   1 
ATOM   226  N N   . PHE   A 1 33  ? 21.666 -5.948  28.173 1.00 13.96 ? 45  PHE   A N   1 
ATOM   227  C CA  . PHE   A 1 33  ? 22.577 -7.080  28.178 1.00 18.83 ? 45  PHE   A CA  1 
ATOM   228  C C   . PHE   A 1 33  ? 21.803 -8.385  28.134 1.00 15.63 ? 45  PHE   A C   1 
ATOM   229  O O   . PHE   A 1 33  ? 20.782 -8.545  28.809 1.00 11.92 ? 45  PHE   A O   1 
ATOM   230  C CB  . PHE   A 1 33  ? 23.528 -7.052  29.390 1.00 15.71 ? 45  PHE   A CB  1 
ATOM   231  C CG  . PHE   A 1 33  ? 22.859 -6.737  30.700 1.00 19.37 ? 45  PHE   A CG  1 
ATOM   232  C CD1 . PHE   A 1 33  ? 22.469 -5.443  31.006 1.00 20.54 ? 45  PHE   A CD1 1 
ATOM   233  C CD2 . PHE   A 1 33  ? 22.662 -7.729  31.645 1.00 20.98 ? 45  PHE   A CD2 1 
ATOM   234  C CE1 . PHE   A 1 33  ? 21.869 -5.149  32.212 1.00 22.22 ? 45  PHE   A CE1 1 
ATOM   235  C CE2 . PHE   A 1 33  ? 22.064 -7.442  32.856 1.00 22.26 ? 45  PHE   A CE2 1 
ATOM   236  C CZ  . PHE   A 1 33  ? 21.669 -6.150  33.140 1.00 22.02 ? 45  PHE   A CZ  1 
ATOM   237  N N   . LEU   A 1 34  ? 22.309 -9.313  27.329 1.00 14.33 ? 46  LEU   A N   1 
ATOM   238  C CA  . LEU   A 1 34  ? 21.706 -10.629 27.173 1.00 18.75 ? 46  LEU   A CA  1 
ATOM   239  C C   . LEU   A 1 34  ? 22.003 -11.478 28.405 1.00 18.58 ? 46  LEU   A C   1 
ATOM   240  O O   . LEU   A 1 34  ? 23.168 -11.763 28.705 1.00 20.44 ? 46  LEU   A O   1 
ATOM   241  C CB  . LEU   A 1 34  ? 22.251 -11.294 25.910 1.00 18.45 ? 46  LEU   A CB  1 
ATOM   242  C CG  . LEU   A 1 34  ? 21.516 -12.478 25.285 1.00 19.87 ? 46  LEU   A CG  1 
ATOM   243  C CD1 . LEU   A 1 34  ? 20.253 -12.020 24.574 1.00 19.20 ? 46  LEU   A CD1 1 
ATOM   244  C CD2 . LEU   A 1 34  ? 22.436 -13.217 24.326 1.00 22.38 ? 46  LEU   A CD2 1 
ATOM   245  N N   . ILE   A 1 35  ? 20.950 -11.888 29.111 1.00 18.64 ? 47  ILE   A N   1 
ATOM   246  C CA  . ILE   A 1 35  ? 21.094 -12.746 30.281 1.00 22.35 ? 47  ILE   A CA  1 
ATOM   247  C C   . ILE   A 1 35  ? 20.807 -14.193 29.892 1.00 25.39 ? 47  ILE   A C   1 
ATOM   248  O O   . ILE   A 1 35  ? 21.386 -15.122 30.464 1.00 33.32 ? 47  ILE   A O   1 
ATOM   249  C CB  . ILE   A 1 35  ? 20.179 -12.287 31.433 1.00 24.22 ? 47  ILE   A CB  1 
ATOM   250  C CG1 . ILE   A 1 35  ? 18.718 -12.263 30.984 1.00 21.99 ? 47  ILE   A CG1 1 
ATOM   251  C CG2 . ILE   A 1 35  ? 20.598 -10.913 31.939 1.00 25.35 ? 47  ILE   A CG2 1 
ATOM   252  C CD1 . ILE   A 1 35  ? 17.756 -11.857 32.075 1.00 32.55 ? 47  ILE   A CD1 1 
ATOM   253  N N   . ARG   A 1 36  ? 19.916 -14.397 28.924 1.00 25.89 ? 48  ARG   A N   1 
ATOM   254  C CA  . ARG   A 1 36  ? 19.680 -15.716 28.355 1.00 22.96 ? 48  ARG   A CA  1 
ATOM   255  C C   . ARG   A 1 36  ? 19.395 -15.546 26.870 1.00 25.06 ? 48  ARG   A C   1 
ATOM   256  O O   . ARG   A 1 36  ? 19.248 -14.428 26.375 1.00 22.28 ? 48  ARG   A O   1 
ATOM   257  C CB  . ARG   A 1 36  ? 18.539 -16.451 29.067 1.00 29.94 ? 48  ARG   A CB  1 
ATOM   258  C CG  . ARG   A 1 36  ? 18.943 -17.060 30.397 1.00 34.82 ? 48  ARG   A CG  1 
ATOM   259  C CD  . ARG   A 1 36  ? 17.814 -17.864 30.999 1.00 43.16 ? 48  ARG   A CD  1 
ATOM   260  N NE  . ARG   A 1 36  ? 18.258 -19.189 31.413 1.00 51.11 ? 48  ARG   A NE  1 
ATOM   261  C CZ  . ARG   A 1 36  ? 18.122 -20.285 30.680 1.00 53.33 ? 48  ARG   A CZ  1 
ATOM   262  N NH1 . ARG   A 1 36  ? 17.540 -20.254 29.492 1.00 59.50 ? 48  ARG   A NH1 1 
ATOM   263  N NH2 . ARG   A 1 36  ? 18.584 -21.440 31.149 1.00 59.45 ? 48  ARG   A NH2 1 
ATOM   264  N N   . ARG   A 1 37  ? 19.312 -16.677 26.161 1.00 22.24 ? 49  ARG   A N   1 
ATOM   265  C CA  . ARG   A 1 37  ? 19.288 -16.640 24.698 1.00 26.56 ? 49  ARG   A CA  1 
ATOM   266  C C   . ARG   A 1 37  ? 18.182 -15.747 24.150 1.00 24.76 ? 49  ARG   A C   1 
ATOM   267  O O   . ARG   A 1 37  ? 18.355 -15.118 23.100 1.00 23.34 ? 49  ARG   A O   1 
ATOM   268  C CB  . ARG   A 1 37  ? 19.131 -18.048 24.127 1.00 33.98 ? 49  ARG   A CB  1 
ATOM   269  C CG  . ARG   A 1 37  ? 20.401 -18.879 24.112 1.00 35.26 ? 49  ARG   A CG  1 
ATOM   270  C CD  . ARG   A 1 37  ? 20.594 -19.513 22.748 1.00 34.50 ? 49  ARG   A CD  1 
ATOM   271  N NE  . ARG   A 1 37  ? 21.584 -20.582 22.755 1.00 42.74 ? 49  ARG   A NE  1 
ATOM   272  C CZ  . ARG   A 1 37  ? 22.072 -21.150 21.660 1.00 41.40 ? 49  ARG   A CZ  1 
ATOM   273  N NH1 . ARG   A 1 37  ? 21.706 -20.750 20.453 1.00 40.27 ? 49  ARG   A NH1 1 
ATOM   274  N NH2 . ARG   A 1 37  ? 22.950 -22.142 21.779 1.00 31.32 ? 49  ARG   A NH2 1 
ATOM   275  N N   . ASN   A 1 38  ? 17.043 -15.671 24.838 1.00 26.59 ? 50  ASN   A N   1 
ATOM   276  C CA  . ASN   A 1 38  ? 15.894 -14.926 24.337 1.00 26.06 ? 50  ASN   A CA  1 
ATOM   277  C C   . ASN   A 1 38  ? 15.428 -13.845 25.306 1.00 21.60 ? 50  ASN   A C   1 
ATOM   278  O O   . ASN   A 1 38  ? 14.302 -13.352 25.182 1.00 20.42 ? 50  ASN   A O   1 
ATOM   279  C CB  . ASN   A 1 38  ? 14.749 -15.885 24.015 1.00 25.55 ? 50  ASN   A CB  1 
ATOM   280  C CG  . ASN   A 1 38  ? 14.706 -17.068 24.957 1.00 38.07 ? 50  ASN   A CG  1 
ATOM   281  O OD1 . ASN   A 1 38  ? 15.097 -16.964 26.120 1.00 34.68 ? 50  ASN   A OD1 1 
ATOM   282  N ND2 . ASN   A 1 38  ? 14.247 -18.207 24.455 1.00 39.62 ? 50  ASN   A ND2 1 
ATOM   283  N N   . PHE   A 1 39  ? 16.267 -13.458 26.264 1.00 20.23 ? 51  PHE   A N   1 
ATOM   284  C CA  . PHE   A 1 39  ? 15.899 -12.453 27.252 1.00 19.66 ? 51  PHE   A CA  1 
ATOM   285  C C   . PHE   A 1 39  ? 17.017 -11.432 27.400 1.00 18.39 ? 51  PHE   A C   1 
ATOM   286  O O   . PHE   A 1 39  ? 18.185 -11.799 27.562 1.00 15.16 ? 51  PHE   A O   1 
ATOM   287  C CB  . PHE   A 1 39  ? 15.579 -13.097 28.603 1.00 19.83 ? 51  PHE   A CB  1 
ATOM   288  C CG  . PHE   A 1 39  ? 14.210 -13.709 28.664 1.00 26.21 ? 51  PHE   A CG  1 
ATOM   289  C CD1 . PHE   A 1 39  ? 13.098 -12.919 28.905 1.00 26.01 ? 51  PHE   A CD1 1 
ATOM   290  C CD2 . PHE   A 1 39  ? 14.032 -15.068 28.471 1.00 29.12 ? 51  PHE   A CD2 1 
ATOM   291  C CE1 . PHE   A 1 39  ? 11.834 -13.472 28.958 1.00 27.81 ? 51  PHE   A CE1 1 
ATOM   292  C CE2 . PHE   A 1 39  ? 12.769 -15.629 28.523 1.00 36.48 ? 51  PHE   A CE2 1 
ATOM   293  C CZ  . PHE   A 1 39  ? 11.669 -14.829 28.767 1.00 31.97 ? 51  PHE   A CZ  1 
ATOM   294  N N   . VAL   A 1 40  ? 16.646 -10.156 27.346 1.00 16.52 ? 52  VAL   A N   1 
ATOM   295  C CA  . VAL   A 1 40  ? 17.562 -9.037  27.516 1.00 14.25 ? 52  VAL   A CA  1 
ATOM   296  C C   . VAL   A 1 40  ? 17.099 -8.219  28.713 1.00 17.20 ? 52  VAL   A C   1 
ATOM   297  O O   . VAL   A 1 40  ? 15.903 -7.944  28.864 1.00 17.29 ? 52  VAL   A O   1 
ATOM   298  C CB  . VAL   A 1 40  ? 17.629 -8.162  26.245 1.00 15.95 ? 52  VAL   A CB  1 
ATOM   299  C CG1 . VAL   A 1 40  ? 18.317 -6.837  26.536 1.00 13.03 ? 52  VAL   A CG1 1 
ATOM   300  C CG2 . VAL   A 1 40  ? 18.348 -8.904  25.131 1.00 15.78 ? 52  VAL   A CG2 1 
ATOM   301  N N   . LEU   A 1 41  ? 18.042 -7.845  29.572 1.00 12.83 ? 53  LEU   A N   1 
ATOM   302  C CA  . LEU   A 1 41  ? 17.754 -7.021  30.737 1.00 14.80 ? 53  LEU   A CA  1 
ATOM   303  C C   . LEU   A 1 41  ? 18.134 -5.577  30.438 1.00 15.14 ? 53  LEU   A C   1 
ATOM   304  O O   . LEU   A 1 41  ? 19.260 -5.301  30.012 1.00 16.51 ? 53  LEU   A O   1 
ATOM   305  C CB  . LEU   A 1 41  ? 18.510 -7.529  31.966 1.00 17.33 ? 53  LEU   A CB  1 
ATOM   306  C CG  . LEU   A 1 41  ? 18.086 -6.914  33.299 1.00 24.80 ? 53  LEU   A CG  1 
ATOM   307  C CD1 . LEU   A 1 41  ? 16.586 -7.059  33.485 1.00 20.27 ? 53  LEU   A CD1 1 
ATOM   308  C CD2 . LEU   A 1 41  ? 18.828 -7.566  34.452 1.00 30.08 ? 53  LEU   A CD2 1 
ATOM   309  N N   . THR   A 1 42  ? 17.191 -4.663  30.655 1.00 14.37 ? 54  THR   A N   1 
ATOM   310  C CA  . THR   A 1 42  ? 17.403 -3.252  30.371 1.00 11.77 ? 54  THR   A CA  1 
ATOM   311  C C   . THR   A 1 42  ? 16.627 -2.427  31.391 1.00 16.41 ? 54  THR   A C   1 
ATOM   312  O O   . THR   A 1 42  ? 16.026 -2.963  32.327 1.00 17.85 ? 54  THR   A O   1 
ATOM   313  C CB  . THR   A 1 42  ? 16.980 -2.909  28.940 1.00 15.11 ? 54  THR   A CB  1 
ATOM   314  O OG1 . THR   A 1 42  ? 17.309 -1.544  28.654 1.00 15.63 ? 54  THR   A OG1 1 
ATOM   315  C CG2 . THR   A 1 42  ? 15.482 -3.108  28.770 1.00 17.84 ? 54  THR   A CG2 1 
ATOM   316  N N   . ALA   A 1 43  ? 16.647 -1.111  31.203 1.00 12.72 ? 55  ALA   A N   1 
ATOM   317  C CA  . ALA   A 1 43  ? 15.935 -0.193  32.080 1.00 14.12 ? 55  ALA   A CA  1 
ATOM   318  C C   . ALA   A 1 43  ? 14.481 -0.058  31.646 1.00 14.90 ? 55  ALA   A C   1 
ATOM   319  O O   . ALA   A 1 43  ? 14.157 -0.125  30.458 1.00 13.24 ? 55  ALA   A O   1 
ATOM   320  C CB  . ALA   A 1 43  ? 16.607 1.181   32.087 1.00 13.16 ? 55  ALA   A CB  1 
ATOM   321  N N   . ALA   A 1 44  ? 13.603 0.141   32.633 1.00 15.66 ? 56  ALA   A N   1 
ATOM   322  C CA  . ALA   A 1 44  ? 12.170 0.201   32.361 1.00 15.96 ? 56  ALA   A CA  1 
ATOM   323  C C   . ALA   A 1 44  ? 11.785 1.449   31.576 1.00 18.54 ? 56  ALA   A C   1 
ATOM   324  O O   . ALA   A 1 44  ? 10.817 1.418   30.806 1.00 18.31 ? 56  ALA   A O   1 
ATOM   325  C CB  . ALA   A 1 44  ? 11.386 0.138   33.671 1.00 15.51 ? 56  ALA   A CB  1 
ATOM   326  N N   . HIS   A 1 45  ? 12.517 2.552   31.751 1.00 13.31 ? 57  HIS   A N   1 
ATOM   327  C CA  . HIS   A 1 45  ? 12.191 3.776   31.028 1.00 16.18 ? 57  HIS   A CA  1 
ATOM   328  C C   . HIS   A 1 45  ? 12.494 3.681   29.539 1.00 17.57 ? 57  HIS   A C   1 
ATOM   329  O O   . HIS   A 1 45  ? 12.072 4.562   28.783 1.00 18.03 ? 57  HIS   A O   1 
ATOM   330  C CB  . HIS   A 1 45  ? 12.944 4.965   31.628 1.00 16.67 ? 57  HIS   A CB  1 
ATOM   331  C CG  . HIS   A 1 45  ? 14.409 4.964   31.330 1.00 17.20 ? 57  HIS   A CG  1 
ATOM   332  N ND1 . HIS   A 1 45  ? 15.356 4.569   32.251 1.00 15.12 ? 57  HIS   A ND1 1 
ATOM   333  C CD2 . HIS   A 1 45  ? 15.091 5.308   30.213 1.00 17.14 ? 57  HIS   A CD2 1 
ATOM   334  C CE1 . HIS   A 1 45  ? 16.558 4.671   31.714 1.00 15.06 ? 57  HIS   A CE1 1 
ATOM   335  N NE2 . HIS   A 1 45  ? 16.425 5.120   30.479 1.00 20.90 ? 57  HIS   A NE2 1 
ATOM   336  N N   . CYS   A 1 46  ? 13.214 2.649   29.103 1.00 15.37 ? 58  CYS   A N   1 
ATOM   337  C CA  . CYS   A 1 46  ? 13.476 2.436   27.687 1.00 20.54 ? 58  CYS   A CA  1 
ATOM   338  C C   . CYS   A 1 46  ? 12.289 1.830   26.956 1.00 19.13 ? 58  CYS   A C   1 
ATOM   339  O O   . CYS   A 1 46  ? 12.362 1.640   25.738 1.00 21.90 ? 58  CYS   A O   1 
ATOM   340  C CB  . CYS   A 1 46  ? 14.701 1.538   27.507 1.00 15.90 ? 58  CYS   A CB  1 
ATOM   341  S SG  . CYS   A 1 46  ? 16.221 2.236   28.177 1.00 26.52 ? 58  CYS   A SG  1 
ATOM   342  N N   . ALA   A 1 47  ? 11.212 1.514   27.670 1.00 17.52 ? 59  ALA   A N   1 
ATOM   343  C CA  . ALA   A 1 47  ? 10.041 0.925   27.042 1.00 19.10 ? 59  ALA   A CA  1 
ATOM   344  C C   . ALA   A 1 47  ? 9.421  1.892   26.041 1.00 24.58 ? 59  ALA   A C   1 
ATOM   345  O O   . ALA   A 1 47  ? 9.395  3.107   26.252 1.00 21.22 ? 59  ALA   A O   1 
ATOM   346  C CB  . ALA   A 1 47  ? 9.014  0.532   28.102 1.00 25.96 ? 59  ALA   A CB  1 
ATOM   347  N N   . GLY   A 1 48  ? 8.934  1.342   24.944 1.00 29.77 ? 60  GLY   A N   1 
ATOM   348  C CA  . GLY   A 1 48  ? 8.240  2.111   23.926 1.00 30.64 ? 60  GLY   A CA  1 
ATOM   349  C C   . GLY   A 1 48  ? 7.218  1.229   23.259 1.00 31.88 ? 60  GLY   A C   1 
ATOM   350  O O   . GLY   A 1 48  ? 6.716  0.274   23.860 1.00 37.53 ? 60  GLY   A O   1 
ATOM   351  N N   . ARG   A 1 49  ? 6.899  1.548   22.007 1.00 33.00 ? 61  ARG   A N   1 
ATOM   352  C CA  . ARG   A 1 49  ? 6.002  0.688   21.246 1.00 31.81 ? 61  ARG   A CA  1 
ATOM   353  C C   . ARG   A 1 49  ? 6.775  -0.466  20.614 1.00 32.56 ? 61  ARG   A C   1 
ATOM   354  O O   . ARG   A 1 49  ? 6.518  -1.635  20.914 1.00 30.92 ? 61  ARG   A O   1 
ATOM   355  C CB  . ARG   A 1 49  ? 5.257  1.513   20.190 1.00 39.47 ? 61  ARG   A CB  1 
ATOM   356  C CG  . ARG   A 1 49  ? 4.038  0.820   19.596 1.00 43.73 ? 61  ARG   A CG  1 
ATOM   357  C CD  . ARG   A 1 49  ? 2.949  0.571   20.629 1.00 42.26 ? 61  ARG   A CD  1 
ATOM   358  N NE  . ARG   A 1 49  ? 2.124  1.752   20.853 1.00 55.73 ? 61  ARG   A NE  1 
ATOM   359  C CZ  . ARG   A 1 49  ? 0.984  1.752   21.532 1.00 57.44 ? 61  ARG   A CZ  1 
ATOM   360  N NH1 . ARG   A 1 49  ? 0.499  0.644   22.068 1.00 51.91 ? 61  ARG   A NH1 1 
ATOM   361  N NH2 . ARG   A 1 49  ? 0.312  2.891   21.673 1.00 54.27 ? 61  ARG   A NH2 1 
ATOM   362  N N   . SER   A 1 50  ? 7.753  -0.154  19.768 1.00 32.64 ? 63  SER   A N   1 
ATOM   363  C CA  . SER   A 1 50  ? 8.572  -1.156  19.102 1.00 27.28 ? 63  SER   A CA  1 
ATOM   364  C C   . SER   A 1 50  ? 10.010 -1.056  19.588 1.00 25.04 ? 63  SER   A C   1 
ATOM   365  O O   . SER   A 1 50  ? 10.557 0.044   19.702 1.00 24.94 ? 63  SER   A O   1 
ATOM   366  C CB  . SER   A 1 50  ? 8.532  -0.986  17.582 1.00 32.01 ? 63  SER   A CB  1 
ATOM   367  O OG  . SER   A 1 50  ? 9.491  -1.816  16.953 1.00 28.92 ? 63  SER   A OG  1 
ATOM   368  N N   . ILE   A 1 51  ? 10.617 -2.208  19.876 1.00 22.68 ? 64  ILE   A N   1 
ATOM   369  C CA  . ILE   A 1 51  ? 12.018 -2.285  20.275 1.00 23.96 ? 64  ILE   A CA  1 
ATOM   370  C C   . ILE   A 1 51  ? 12.707 -3.340  19.420 1.00 22.96 ? 64  ILE   A C   1 
ATOM   371  O O   . ILE   A 1 51  ? 12.223 -4.473  19.314 1.00 23.62 ? 64  ILE   A O   1 
ATOM   372  C CB  . ILE   A 1 51  ? 12.178 -2.619  21.771 1.00 24.15 ? 64  ILE   A CB  1 
ATOM   373  C CG1 . ILE   A 1 51  ? 11.479 -1.566  22.635 1.00 23.12 ? 64  ILE   A CG1 1 
ATOM   374  C CG2 . ILE   A 1 51  ? 13.651 -2.714  22.139 1.00 20.83 ? 64  ILE   A CG2 1 
ATOM   375  C CD1 . ILE   A 1 51  ? 11.603 -1.813  24.123 1.00 22.59 ? 64  ILE   A CD1 1 
ATOM   376  N N   . THR   A 1 52  ? 13.832 -2.969  18.814 1.00 19.76 ? 65  THR   A N   1 
ATOM   377  C CA  . THR   A 1 52  ? 14.664 -3.886  18.046 1.00 19.03 ? 65  THR   A CA  1 
ATOM   378  C C   . THR   A 1 52  ? 16.013 -4.015  18.736 1.00 18.50 ? 65  THR   A C   1 
ATOM   379  O O   . THR   A 1 52  ? 16.657 -3.005  19.040 1.00 18.88 ? 65  THR   A O   1 
ATOM   380  C CB  . THR   A 1 52  ? 14.852 -3.399  16.607 1.00 22.38 ? 65  THR   A CB  1 
ATOM   381  O OG1 . THR   A 1 52  ? 13.575 -3.273  15.972 1.00 32.57 ? 65  THR   A OG1 1 
ATOM   382  C CG2 . THR   A 1 52  ? 15.708 -4.381  15.822 1.00 22.71 ? 65  THR   A CG2 1 
ATOM   383  N N   . VAL   A 1 53  ? 16.440 -5.252  18.974 1.00 18.23 ? 66  VAL   A N   1 
ATOM   384  C CA  . VAL   A 1 53  ? 17.668 -5.541  19.706 1.00 16.86 ? 66  VAL   A CA  1 
ATOM   385  C C   . VAL   A 1 53  ? 18.750 -5.940  18.716 1.00 18.23 ? 66  VAL   A C   1 
ATOM   386  O O   . VAL   A 1 53  ? 18.539 -6.823  17.877 1.00 20.09 ? 66  VAL   A O   1 
ATOM   387  C CB  . VAL   A 1 53  ? 17.449 -6.655  20.743 1.00 19.52 ? 66  VAL   A CB  1 
ATOM   388  C CG1 . VAL   A 1 53  ? 18.753 -6.979  21.452 1.00 21.10 ? 66  VAL   A CG1 1 
ATOM   389  C CG2 . VAL   A 1 53  ? 16.377 -6.251  21.738 1.00 24.40 ? 66  VAL   A CG2 1 
ATOM   390  N N   . THR   A 1 54  ? 19.909 -5.296  18.815 1.00 15.53 ? 67  THR   A N   1 
ATOM   391  C CA  . THR   A 1 54  ? 21.081 -5.653  18.027 1.00 17.06 ? 67  THR   A CA  1 
ATOM   392  C C   . THR   A 1 54  ? 22.117 -6.274  18.955 1.00 16.65 ? 67  THR   A C   1 
ATOM   393  O O   . THR   A 1 54  ? 22.547 -5.638  19.923 1.00 15.81 ? 67  THR   A O   1 
ATOM   394  C CB  . THR   A 1 54  ? 21.663 -4.434  17.310 1.00 19.69 ? 67  THR   A CB  1 
ATOM   395  O OG1 . THR   A 1 54  ? 20.687 -3.896  16.411 1.00 20.35 ? 67  THR   A OG1 1 
ATOM   396  C CG2 . THR   A 1 54  ? 22.905 -4.825  16.524 1.00 18.52 ? 67  THR   A CG2 1 
ATOM   397  N N   . LEU   A 1 55  ? 22.508 -7.509  18.658 1.00 15.38 ? 68  LEU   A N   1 
ATOM   398  C CA  . LEU   A 1 55  ? 23.501 -8.243  19.424 1.00 13.83 ? 68  LEU   A CA  1 
ATOM   399  C C   . LEU   A 1 55  ? 24.736 -8.502  18.570 1.00 14.51 ? 68  LEU   A C   1 
ATOM   400  O O   . LEU   A 1 55  ? 24.697 -8.416  17.339 1.00 14.16 ? 68  LEU   A O   1 
ATOM   401  C CB  . LEU   A 1 55  ? 22.931 -9.576  19.929 1.00 13.33 ? 68  LEU   A CB  1 
ATOM   402  C CG  . LEU   A 1 55  ? 21.673 -9.532  20.797 1.00 12.90 ? 68  LEU   A CG  1 
ATOM   403  C CD1 . LEU   A 1 55  ? 21.143 -10.937 21.039 1.00 15.80 ? 68  LEU   A CD1 1 
ATOM   404  C CD2 . LEU   A 1 55  ? 21.959 -8.839  22.117 1.00 13.96 ? 68  LEU   A CD2 1 
ATOM   405  N N   . GLY   A 1 56  ? 25.838 -8.823  19.244 1.00 14.72 ? 69  GLY   A N   1 
ATOM   406  C CA  . GLY   A 1 56  ? 27.068 -9.173  18.558 1.00 16.36 ? 69  GLY   A CA  1 
ATOM   407  C C   . GLY   A 1 56  ? 27.676 -8.052  17.749 1.00 20.75 ? 69  GLY   A C   1 
ATOM   408  O O   . GLY   A 1 56  ? 28.342 -8.312  16.741 1.00 21.35 ? 69  GLY   A O   1 
ATOM   409  N N   . ALA   A 1 57  ? 27.474 -6.810  18.167 1.00 16.65 ? 70  ALA   A N   1 
ATOM   410  C CA  . ALA   A 1 57  ? 27.964 -5.651  17.441 1.00 20.03 ? 70  ALA   A CA  1 
ATOM   411  C C   . ALA   A 1 57  ? 29.107 -4.991  18.200 1.00 22.01 ? 70  ALA   A C   1 
ATOM   412  O O   . ALA   A 1 57  ? 29.053 -4.849  19.426 1.00 24.28 ? 70  ALA   A O   1 
ATOM   413  C CB  . ALA   A 1 57  ? 26.841 -4.637  17.212 1.00 18.68 ? 70  ALA   A CB  1 
ATOM   414  N N   . HIS   A 1 58  ? 30.149 -4.604  17.466 1.00 16.75 ? 71  HIS   A N   1 
ATOM   415  C CA  . HIS   A 1 58  ? 31.139 -3.659  17.962 1.00 19.72 ? 71  HIS   A CA  1 
ATOM   416  C C   . HIS   A 1 58  ? 30.954 -2.297  17.306 1.00 19.07 ? 71  HIS   A C   1 
ATOM   417  O O   . HIS   A 1 58  ? 30.787 -1.289  17.998 1.00 16.11 ? 71  HIS   A O   1 
ATOM   418  C CB  . HIS   A 1 58  ? 32.562 -4.182  17.726 1.00 25.65 ? 71  HIS   A CB  1 
ATOM   419  C CG  . HIS   A 1 58  ? 33.624 -3.313  18.324 1.00 24.39 ? 71  HIS   A CG  1 
ATOM   420  N ND1 . HIS   A 1 58  ? 33.843 -3.235  19.683 1.00 25.56 ? 71  HIS   A ND1 1 
ATOM   421  C CD2 . HIS   A 1 58  ? 34.518 -2.473  17.750 1.00 25.72 ? 71  HIS   A CD2 1 
ATOM   422  C CE1 . HIS   A 1 58  ? 34.829 -2.390  19.920 1.00 25.48 ? 71  HIS   A CE1 1 
ATOM   423  N NE2 . HIS   A 1 58  ? 35.257 -1.914  18.765 1.00 28.80 ? 71  HIS   A NE2 1 
ATOM   424  N N   . ASN   A 1 59  ? 30.964 -2.249  15.977 1.00 19.15 ? 72  ASN   A N   1 
ATOM   425  C CA  . ASN   A 1 59  ? 30.570 -1.050  15.251 1.00 24.63 ? 72  ASN   A CA  1 
ATOM   426  C C   . ASN   A 1 59  ? 29.056 -1.070  15.083 1.00 24.61 ? 72  ASN   A C   1 
ATOM   427  O O   . ASN   A 1 59  ? 28.494 -2.049  14.576 1.00 24.88 ? 72  ASN   A O   1 
ATOM   428  C CB  . ASN   A 1 59  ? 31.278 -0.988  13.897 1.00 22.19 ? 72  ASN   A CB  1 
ATOM   429  C CG  . ASN   A 1 59  ? 31.093 0.347   13.191 1.00 32.95 ? 72  ASN   A CG  1 
ATOM   430  O OD1 . ASN   A 1 59  ? 30.063 1.007   13.333 1.00 33.05 ? 72  ASN   A OD1 1 
ATOM   431  N ND2 . ASN   A 1 59  ? 32.096 0.746   12.417 1.00 32.66 ? 72  ASN   A ND2 1 
ATOM   432  N N   . ILE   A 1 60  ? 28.393 0.002   15.521 1.00 23.01 ? 73  ILE   A N   1 
ATOM   433  C CA  . ILE   A 1 60  ? 26.937 0.081   15.455 1.00 26.33 ? 73  ILE   A CA  1 
ATOM   434  C C   . ILE   A 1 60  ? 26.447 0.838   14.227 1.00 28.62 ? 73  ILE   A C   1 
ATOM   435  O O   . ILE   A 1 60  ? 25.243 0.792   13.925 1.00 25.59 ? 73  ILE   A O   1 
ATOM   436  C CB  . ILE   A 1 60  ? 26.363 0.720   16.739 1.00 20.67 ? 73  ILE   A CB  1 
ATOM   437  C CG1 . ILE   A 1 60  ? 24.918 0.271   16.971 1.00 24.33 ? 73  ILE   A CG1 1 
ATOM   438  C CG2 . ILE   A 1 60  ? 26.455 2.237   16.674 1.00 21.04 ? 73  ILE   A CG2 1 
ATOM   439  C CD1 . ILE   A 1 60  ? 24.768 -1.226  17.143 1.00 25.70 ? 73  ILE   A CD1 1 
ATOM   440  N N   . THR   A 1 61  ? 27.336 1.512   13.496 1.00 29.07 ? 74  THR   A N   1 
ATOM   441  C CA  . THR   A 1 61  ? 26.925 2.358   12.382 1.00 31.60 ? 74  THR   A CA  1 
ATOM   442  C C   . THR   A 1 61  ? 26.817 1.606   11.063 1.00 36.94 ? 74  THR   A C   1 
ATOM   443  O O   . THR   A 1 61  ? 25.975 1.958   10.228 1.00 36.23 ? 74  THR   A O   1 
ATOM   444  C CB  . THR   A 1 61  ? 27.904 3.525   12.220 1.00 38.66 ? 74  THR   A CB  1 
ATOM   445  O OG1 . THR   A 1 61  ? 29.189 3.023   11.832 1.00 33.46 ? 74  THR   A OG1 1 
ATOM   446  C CG2 . THR   A 1 61  ? 28.041 4.285   13.533 1.00 33.59 ? 74  THR   A CG2 1 
ATOM   447  N N   . GLU   A 1 62  ? 27.644 0.586   10.848 1.00 29.02 ? 75  GLU   A N   1 
ATOM   448  C CA  . GLU   A 1 62  ? 27.589 -0.219  9.637  1.00 32.58 ? 75  GLU   A CA  1 
ATOM   449  C C   . GLU   A 1 62  ? 27.418 -1.682  10.009 1.00 29.06 ? 75  GLU   A C   1 
ATOM   450  O O   . GLU   A 1 62  ? 28.038 -2.167  10.959 1.00 28.87 ? 75  GLU   A O   1 
ATOM   451  C CB  . GLU   A 1 62  ? 28.846 -0.035  8.776  1.00 36.45 ? 75  GLU   A CB  1 
ATOM   452  C CG  . GLU   A 1 62  ? 28.689 0.984   7.655  0.10 33.97 ? 75  GLU   A CG  1 
ATOM   453  C CD  . GLU   A 1 62  ? 27.847 0.469   6.499  0.10 33.54 ? 75  GLU   A CD  1 
ATOM   454  O OE1 . GLU   A 1 62  ? 27.443 -0.714  6.526  0.10 34.21 ? 75  GLU   A OE1 1 
ATOM   455  O OE2 . GLU   A 1 62  ? 27.597 1.246   5.554  0.10 33.13 ? 75  GLU   A OE2 1 
ATOM   456  N N   . GLU   A 1 63  ? 26.575 -2.379  9.250  1.00 32.65 ? 76  GLU   A N   1 
ATOM   457  C CA  . GLU   A 1 63  ? 26.231 -3.756  9.574  1.00 33.27 ? 76  GLU   A CA  1 
ATOM   458  C C   . GLU   A 1 63  ? 27.453 -4.663  9.488  1.00 29.57 ? 76  GLU   A C   1 
ATOM   459  O O   . GLU   A 1 63  ? 28.238 -4.586  8.539  1.00 32.26 ? 76  GLU   A O   1 
ATOM   460  C CB  . GLU   A 1 63  ? 25.123 -4.247  8.642  1.00 35.66 ? 76  GLU   A CB  1 
ATOM   461  C CG  . GLU   A 1 63  ? 25.184 -3.675  7.234  1.00 53.62 ? 76  GLU   A CG  1 
ATOM   462  C CD  . GLU   A 1 63  ? 23.838 -3.715  6.532  1.00 73.59 ? 76  GLU   A CD  1 
ATOM   463  O OE1 . GLU   A 1 63  ? 22.806 -3.514  7.208  1.00 60.14 ? 76  GLU   A OE1 1 
ATOM   464  O OE2 . GLU   A 1 63  ? 23.810 -3.952  5.306  1.00 75.77 ? 76  GLU   A OE2 1 
ATOM   465  N N   . GLU   A 1 64  ? 27.610 -5.519  10.493 1.00 20.73 ? 77  GLU   A N   1 
ATOM   466  C CA  . GLU   A 1 64  ? 28.704 -6.473  10.577 1.00 25.79 ? 77  GLU   A CA  1 
ATOM   467  C C   . GLU   A 1 64  ? 28.175 -7.888  10.385 1.00 24.18 ? 77  GLU   A C   1 
ATOM   468  O O   . GLU   A 1 64  ? 26.982 -8.158  10.542 1.00 23.40 ? 77  GLU   A O   1 
ATOM   469  C CB  . GLU   A 1 64  ? 29.426 -6.371  11.926 1.00 25.16 ? 77  GLU   A CB  1 
ATOM   470  C CG  . GLU   A 1 64  ? 30.015 -5.004  12.242 1.00 29.22 ? 77  GLU   A CG  1 
ATOM   471  C CD  . GLU   A 1 64  ? 30.495 -4.895  13.682 1.00 29.39 ? 77  GLU   A CD  1 
ATOM   472  O OE1 . GLU   A 1 64  ? 29.894 -5.543  14.565 1.00 24.11 ? 77  GLU   A OE1 1 
ATOM   473  O OE2 . GLU   A 1 64  ? 31.478 -4.166  13.931 1.00 30.81 ? 77  GLU   A OE2 1 
ATOM   474  N N   . ASP   A 1 65  ? 29.090 -8.798  10.043 1.00 22.11 ? 78  ASP   A N   1 
ATOM   475  C CA  . ASP   A 1 65  ? 28.724 -10.201 9.888  1.00 24.20 ? 78  ASP   A CA  1 
ATOM   476  C C   . ASP   A 1 65  ? 28.366 -10.853 11.217 1.00 24.48 ? 78  ASP   A C   1 
ATOM   477  O O   . ASP   A 1 65  ? 27.700 -11.894 11.226 1.00 21.28 ? 78  ASP   A O   1 
ATOM   478  C CB  . ASP   A 1 65  ? 29.867 -10.961 9.214  1.00 27.05 ? 78  ASP   A CB  1 
ATOM   479  C CG  . ASP   A 1 65  ? 29.512 -12.401 8.908  1.00 37.05 ? 78  ASP   A CG  1 
ATOM   480  O OD1 . ASP   A 1 65  ? 28.552 -12.628 8.142  1.00 35.01 ? 78  ASP   A OD1 1 
ATOM   481  O OD2 . ASP   A 1 65  ? 30.198 -13.306 9.428  1.00 43.85 ? 78  ASP   A OD2 1 
ATOM   482  N N   . THR   A 1 66  ? 28.783 -10.264 12.335 1.00 28.06 ? 79  THR   A N   1 
ATOM   483  C CA  . THR   A 1 66  ? 28.484 -10.793 13.658 1.00 25.12 ? 79  THR   A CA  1 
ATOM   484  C C   . THR   A 1 66  ? 27.172 -10.267 14.227 1.00 23.71 ? 79  THR   A C   1 
ATOM   485  O O   . THR   A 1 66  ? 26.788 -10.671 15.330 1.00 20.63 ? 79  THR   A O   1 
ATOM   486  C CB  . THR   A 1 66  ? 29.628 -10.468 14.624 1.00 22.74 ? 79  THR   A CB  1 
ATOM   487  O OG1 . THR   A 1 66  ? 29.821 -9.049  14.678 1.00 20.39 ? 79  THR   A OG1 1 
ATOM   488  C CG2 . THR   A 1 66  ? 30.916 -11.134 14.167 1.00 23.36 ? 79  THR   A CG2 1 
ATOM   489  N N   . TRP   A 1 67  ? 26.481 -9.384  13.509 1.00 20.05 ? 80  TRP   A N   1 
ATOM   490  C CA  . TRP   A 1 67  ? 25.240 -8.807  14.007 1.00 19.74 ? 80  TRP   A CA  1 
ATOM   491  C C   . TRP   A 1 67  ? 24.141 -9.856  14.122 1.00 21.78 ? 80  TRP   A C   1 
ATOM   492  O O   . TRP   A 1 67  ? 24.050 -10.793 13.323 1.00 18.32 ? 80  TRP   A O   1 
ATOM   493  C CB  . TRP   A 1 67  ? 24.758 -7.681  13.090 1.00 20.44 ? 80  TRP   A CB  1 
ATOM   494  C CG  . TRP   A 1 67  ? 25.441 -6.367  13.306 1.00 23.52 ? 80  TRP   A CG  1 
ATOM   495  C CD1 . TRP   A 1 67  ? 26.637 -6.153  13.925 1.00 26.53 ? 80  TRP   A CD1 1 
ATOM   496  C CD2 . TRP   A 1 67  ? 24.957 -5.078  12.910 1.00 27.49 ? 80  TRP   A CD2 1 
ATOM   497  N NE1 . TRP   A 1 67  ? 26.933 -4.811  13.930 1.00 24.39 ? 80  TRP   A NE1 1 
ATOM   498  C CE2 . TRP   A 1 67  ? 25.917 -4.129  13.315 1.00 22.87 ? 80  TRP   A CE2 1 
ATOM   499  C CE3 . TRP   A 1 67  ? 23.808 -4.635  12.248 1.00 27.00 ? 80  TRP   A CE3 1 
ATOM   500  C CZ2 . TRP   A 1 67  ? 25.761 -2.764  13.082 1.00 21.52 ? 80  TRP   A CZ2 1 
ATOM   501  C CZ3 . TRP   A 1 67  ? 23.655 -3.280  12.017 1.00 26.73 ? 80  TRP   A CZ3 1 
ATOM   502  C CH2 . TRP   A 1 67  ? 24.627 -2.360  12.433 1.00 26.51 ? 80  TRP   A CH2 1 
ATOM   503  N N   . GLN   A 1 68  ? 23.297 -9.683  15.137 1.00 19.00 ? 81  GLN   A N   1 
ATOM   504  C CA  . GLN   A 1 68  ? 22.067 -10.455 15.283 1.00 18.78 ? 81  GLN   A CA  1 
ATOM   505  C C   . GLN   A 1 68  ? 20.971 -9.492  15.716 1.00 18.76 ? 81  GLN   A C   1 
ATOM   506  O O   . GLN   A 1 68  ? 20.989 -9.002  16.850 1.00 16.34 ? 81  GLN   A O   1 
ATOM   507  C CB  . GLN   A 1 68  ? 22.228 -11.593 16.292 1.00 16.29 ? 81  GLN   A CB  1 
ATOM   508  C CG  . GLN   A 1 68  ? 23.206 -12.676 15.866 1.00 22.81 ? 81  GLN   A CG  1 
ATOM   509  C CD  . GLN   A 1 68  ? 23.189 -13.873 16.797 1.00 24.14 ? 81  GLN   A CD  1 
ATOM   510  O OE1 . GLN   A 1 68  ? 22.190 -14.141 17.464 1.00 24.92 ? 81  GLN   A OE1 1 
ATOM   511  N NE2 . GLN   A 1 68  ? 24.300 -14.598 16.850 1.00 21.71 ? 81  GLN   A NE2 1 
ATOM   512  N N   . LYS   A 1 69  ? 20.028 -9.213  14.819 1.00 20.26 ? 82  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 69  ? 18.909 -8.324  15.106 1.00 22.12 ? 82  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 69  ? 17.664 -9.148  15.406 1.00 22.31 ? 82  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 69  ? 17.299 -10.036 14.629 1.00 24.93 ? 82  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 69  ? 18.638 -7.374  13.938 1.00 23.30 ? 82  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 69  ? 19.560 -6.167  13.873 1.00 26.21 ? 82  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 69  ? 18.888 -5.012  13.139 1.00 26.82 ? 82  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 69  ? 19.878 -3.909  12.799 1.00 36.89 ? 82  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 69  ? 20.557 -3.360  14.005 1.00 37.46 ? 82  LYS   A NZ  1 
ATOM   521  N N   . LEU   A 1 70  ? 17.016 -8.844  16.530 1.00 21.57 ? 83  LEU   A N   1 
ATOM   522  C CA  . LEU   A 1 70  ? 15.846 -9.576  16.993 1.00 20.59 ? 83  LEU   A CA  1 
ATOM   523  C C   . LEU   A 1 70  ? 14.773 -8.594  17.438 1.00 24.09 ? 83  LEU   A C   1 
ATOM   524  O O   . LEU   A 1 70  ? 15.079 -7.541  18.007 1.00 16.52 ? 83  LEU   A O   1 
ATOM   525  C CB  . LEU   A 1 70  ? 16.195 -10.523 18.154 1.00 25.63 ? 83  LEU   A CB  1 
ATOM   526  C CG  . LEU   A 1 70  ? 17.331 -11.533 17.956 1.00 26.24 ? 83  LEU   A CG  1 
ATOM   527  C CD1 . LEU   A 1 70  ? 18.687 -10.918 18.275 1.00 26.71 ? 83  LEU   A CD1 1 
ATOM   528  C CD2 . LEU   A 1 70  ? 17.097 -12.773 18.799 1.00 29.75 ? 83  LEU   A CD2 1 
ATOM   529  N N   . GLU   A 1 71  ? 13.517 -8.946  17.182 1.00 26.91 ? 84  GLU   A N   1 
ATOM   530  C CA  . GLU   A 1 71  ? 12.389 -8.121  17.582 1.00 24.17 ? 84  GLU   A CA  1 
ATOM   531  C C   . GLU   A 1 71  ? 11.923 -8.507  18.979 1.00 24.82 ? 84  GLU   A C   1 
ATOM   532  O O   . GLU   A 1 71  ? 11.864 -9.691  19.324 1.00 21.85 ? 84  GLU   A O   1 
ATOM   533  C CB  . GLU   A 1 71  ? 11.232 -8.263  16.591 1.00 26.56 ? 84  GLU   A CB  1 
ATOM   534  C CG  . GLU   A 1 71  ? 11.651 -8.175  15.134 1.00 36.90 ? 84  GLU   A CG  1 
ATOM   535  C CD  . GLU   A 1 71  ? 11.626 -9.523  14.435 1.00 35.74 ? 84  GLU   A CD  1 
ATOM   536  O OE1 . GLU   A 1 71  ? 10.593 -10.220 14.522 1.00 42.91 ? 84  GLU   A OE1 1 
ATOM   537  O OE2 . GLU   A 1 71  ? 12.640 -9.889  13.805 1.00 38.72 ? 84  GLU   A OE2 1 
ATOM   538  N N   . VAL   A 1 72  ? 11.598 -7.498  19.781 1.00 22.73 ? 85  VAL   A N   1 
ATOM   539  C CA  . VAL   A 1 72  ? 11.055 -7.728  21.115 1.00 23.59 ? 85  VAL   A CA  1 
ATOM   540  C C   . VAL   A 1 72  ? 9.567  -8.027  20.993 1.00 26.00 ? 85  VAL   A C   1 
ATOM   541  O O   . VAL   A 1 72  ? 8.818  -7.276  20.356 1.00 26.62 ? 85  VAL   A O   1 
ATOM   542  C CB  . VAL   A 1 72  ? 11.307 -6.515  22.024 1.00 23.72 ? 85  VAL   A CB  1 
ATOM   543  C CG1 . VAL   A 1 72  ? 10.638 -6.717  23.378 1.00 20.19 ? 85  VAL   A CG1 1 
ATOM   544  C CG2 . VAL   A 1 72  ? 12.796 -6.286  22.193 1.00 18.93 ? 85  VAL   A CG2 1 
ATOM   545  N N   . ILE   A 1 73  ? 9.134  -9.133  21.600 1.00 22.19 ? 86  ILE   A N   1 
ATOM   546  C CA  . ILE   A 1 73  ? 7.732  -9.532  21.544 1.00 28.05 ? 86  ILE   A CA  1 
ATOM   547  C C   . ILE   A 1 73  ? 6.990  -9.237  22.840 1.00 30.84 ? 86  ILE   A C   1 
ATOM   548  O O   . ILE   A 1 73  ? 5.748  -9.254  22.845 1.00 30.41 ? 86  ILE   A O   1 
ATOM   549  C CB  . ILE   A 1 73  ? 7.598  -11.027 21.175 1.00 25.52 ? 86  ILE   A CB  1 
ATOM   550  C CG1 . ILE   A 1 73  ? 6.413  -11.244 20.236 1.00 38.32 ? 86  ILE   A CG1 1 
ATOM   551  C CG2 . ILE   A 1 73  ? 7.448  -11.883 22.423 1.00 32.94 ? 86  ILE   A CG2 1 
ATOM   552  C CD1 . ILE   A 1 73  ? 6.257  -12.681 19.788 1.00 48.48 ? 86  ILE   A CD1 1 
ATOM   553  N N   . LYS   A 1 74  ? 7.700  -8.956  23.930 1.00 24.66 ? 87  LYS   A N   1 
ATOM   554  C CA  . LYS   A 1 74  ? 7.062  -8.650  25.201 1.00 28.08 ? 87  LYS   A CA  1 
ATOM   555  C C   . LYS   A 1 74  ? 8.008  -7.806  26.042 1.00 22.35 ? 87  LYS   A C   1 
ATOM   556  O O   . LYS   A 1 74  ? 9.204  -8.095  26.119 1.00 22.22 ? 87  LYS   A O   1 
ATOM   557  C CB  . LYS   A 1 74  ? 6.674  -9.928  25.956 1.00 28.43 ? 87  LYS   A CB  1 
ATOM   558  C CG  . LYS   A 1 74  ? 5.934  -9.668  27.256 1.00 29.91 ? 87  LYS   A CG  1 
ATOM   559  C CD  . LYS   A 1 74  ? 4.707  -8.803  27.016 1.00 36.13 ? 87  LYS   A CD  1 
ATOM   560  C CE  . LYS   A 1 74  ? 3.942  -8.551  28.304 1.00 35.42 ? 87  LYS   A CE  1 
ATOM   561  N NZ  . LYS   A 1 74  ? 2.760  -7.673  28.081 1.00 36.41 ? 87  LYS   A NZ  1 
ATOM   562  N N   . GLN   A 1 75  ? 7.461  -6.764  26.665 1.00 23.08 ? 88  GLN   A N   1 
ATOM   563  C CA  . GLN   A 1 75  ? 8.209  -5.874  27.547 1.00 19.99 ? 88  GLN   A CA  1 
ATOM   564  C C   . GLN   A 1 75  ? 7.649  -6.032  28.956 1.00 21.04 ? 88  GLN   A C   1 
ATOM   565  O O   . GLN   A 1 75  ? 6.545  -5.560  29.248 1.00 22.95 ? 88  GLN   A O   1 
ATOM   566  C CB  . GLN   A 1 75  ? 8.113  -4.426  27.070 1.00 20.91 ? 88  GLN   A CB  1 
ATOM   567  C CG  . GLN   A 1 75  ? 8.541  -4.219  25.625 1.00 23.49 ? 88  GLN   A CG  1 
ATOM   568  C CD  . GLN   A 1 75  ? 8.385  -2.781  25.167 1.00 31.87 ? 88  GLN   A CD  1 
ATOM   569  O OE1 . GLN   A 1 75  ? 8.716  -1.846  25.895 1.00 25.84 ? 88  GLN   A OE1 1 
ATOM   570  N NE2 . GLN   A 1 75  ? 7.873  -2.597  23.955 1.00 35.43 ? 88  GLN   A NE2 1 
ATOM   571  N N   . PHE   A 1 76  ? 8.409  -6.694  29.824 1.00 18.60 ? 89  PHE   A N   1 
ATOM   572  C CA  . PHE   A 1 76  ? 7.978  -6.980  31.192 1.00 20.80 ? 89  PHE   A CA  1 
ATOM   573  C C   . PHE   A 1 76  ? 8.656  -5.974  32.117 1.00 18.65 ? 89  PHE   A C   1 
ATOM   574  O O   . PHE   A 1 76  ? 9.748  -6.213  32.632 1.00 16.24 ? 89  PHE   A O   1 
ATOM   575  C CB  . PHE   A 1 76  ? 8.312  -8.419  31.574 1.00 20.37 ? 89  PHE   A CB  1 
ATOM   576  C CG  . PHE   A 1 76  ? 7.637  -8.894  32.835 1.00 27.17 ? 89  PHE   A CG  1 
ATOM   577  C CD1 . PHE   A 1 76  ? 6.720  -8.096  33.503 1.00 29.87 ? 89  PHE   A CD1 1 
ATOM   578  C CD2 . PHE   A 1 76  ? 7.926  -10.146 33.354 1.00 35.06 ? 89  PHE   A CD2 1 
ATOM   579  C CE1 . PHE   A 1 76  ? 6.104  -8.537  34.662 1.00 30.86 ? 89  PHE   A CE1 1 
ATOM   580  C CE2 . PHE   A 1 76  ? 7.314  -10.594 34.510 1.00 38.99 ? 89  PHE   A CE2 1 
ATOM   581  C CZ  . PHE   A 1 76  ? 6.402  -9.788  35.166 1.00 32.48 ? 89  PHE   A CZ  1 
ATOM   582  N N   . ARG   A 1 77  ? 7.998  -4.836  32.321 1.00 19.51 ? 90  ARG   A N   1 
ATOM   583  C CA  . ARG   A 1 77  ? 8.457  -3.870  33.306 1.00 21.60 ? 90  ARG   A CA  1 
ATOM   584  C C   . ARG   A 1 77  ? 8.245  -4.410  34.714 1.00 20.18 ? 90  ARG   A C   1 
ATOM   585  O O   . ARG   A 1 77  ? 7.364  -5.237  34.962 1.00 20.35 ? 90  ARG   A O   1 
ATOM   586  C CB  . ARG   A 1 77  ? 7.719  -2.539  33.148 1.00 18.59 ? 90  ARG   A CB  1 
ATOM   587  C CG  . ARG   A 1 77  ? 8.446  -1.523  32.287 1.00 27.98 ? 90  ARG   A CG  1 
ATOM   588  C CD  . ARG   A 1 77  ? 7.618  -1.114  31.080 1.00 32.09 ? 90  ARG   A CD  1 
ATOM   589  N NE  . ARG   A 1 77  ? 6.458  -0.306  31.439 1.00 36.83 ? 90  ARG   A NE  1 
ATOM   590  C CZ  . ARG   A 1 77  ? 6.442  1.020   31.455 1.00 45.87 ? 90  ARG   A CZ  1 
ATOM   591  N NH1 . ARG   A 1 77  ? 7.519  1.728   31.154 1.00 40.48 ? 90  ARG   A NH1 1 
ATOM   592  N NH2 . ARG   A 1 77  ? 5.318  1.652   31.779 1.00 43.28 ? 90  ARG   A NH2 1 
ATOM   593  N N   . HIS   A 1 78  ? 9.075  -3.940  35.639 1.00 17.27 ? 91  HIS   A N   1 
ATOM   594  C CA  . HIS   A 1 78  ? 8.875  -4.285  37.036 1.00 20.50 ? 91  HIS   A CA  1 
ATOM   595  C C   . HIS   A 1 78  ? 7.526  -3.738  37.495 1.00 21.59 ? 91  HIS   A C   1 
ATOM   596  O O   . HIS   A 1 78  ? 7.184  -2.591  37.182 1.00 20.25 ? 91  HIS   A O   1 
ATOM   597  C CB  . HIS   A 1 78  ? 10.004 -3.716  37.896 1.00 22.76 ? 91  HIS   A CB  1 
ATOM   598  C CG  . HIS   A 1 78  ? 10.028 -4.252  39.293 1.00 21.66 ? 91  HIS   A CG  1 
ATOM   599  N ND1 . HIS   A 1 78  ? 9.220  -3.760  40.295 1.00 22.48 ? 91  HIS   A ND1 1 
ATOM   600  C CD2 . HIS   A 1 78  ? 10.765 -5.240  39.854 1.00 24.45 ? 91  HIS   A CD2 1 
ATOM   601  C CE1 . HIS   A 1 78  ? 9.457  -4.422  41.414 1.00 25.34 ? 91  HIS   A CE1 1 
ATOM   602  N NE2 . HIS   A 1 78  ? 10.390 -5.326  41.174 1.00 27.34 ? 91  HIS   A NE2 1 
ATOM   603  N N   . PRO   A 1 79  ? 6.730  -4.528  38.221 1.00 21.56 ? 92  PRO   A N   1 
ATOM   604  C CA  . PRO   A 1 79  ? 5.353  -4.102  38.527 1.00 21.95 ? 92  PRO   A CA  1 
ATOM   605  C C   . PRO   A 1 79  ? 5.261  -2.827  39.349 1.00 21.53 ? 92  PRO   A C   1 
ATOM   606  O O   . PRO   A 1 79  ? 4.218  -2.162  39.315 1.00 25.29 ? 92  PRO   A O   1 
ATOM   607  C CB  . PRO   A 1 79  ? 4.775  -5.303  39.290 1.00 28.99 ? 92  PRO   A CB  1 
ATOM   608  C CG  . PRO   A 1 79  ? 5.972  -6.049  39.803 1.00 24.24 ? 92  PRO   A CG  1 
ATOM   609  C CD  . PRO   A 1 79  ? 7.036  -5.860  38.767 1.00 21.00 ? 92  PRO   A CD  1 
ATOM   610  N N   . LYS   A 1 80  ? 6.308  -2.455  40.083 1.00 22.10 ? 93  LYS   A N   1 
ATOM   611  C CA  . LYS   A 1 80  ? 6.290  -1.246  40.894 1.00 21.36 ? 93  LYS   A CA  1 
ATOM   612  C C   . LYS   A 1 80  ? 7.093  -0.109  40.272 1.00 19.50 ? 93  LYS   A C   1 
ATOM   613  O O   . LYS   A 1 80  ? 7.446  0.845   40.973 1.00 18.83 ? 93  LYS   A O   1 
ATOM   614  C CB  . LYS   A 1 80  ? 6.796  -1.552  42.303 1.00 21.08 ? 93  LYS   A CB  1 
ATOM   615  C CG  . LYS   A 1 80  ? 5.776  -2.289  43.151 1.00 28.17 ? 93  LYS   A CG  1 
ATOM   616  C CD  . LYS   A 1 80  ? 6.417  -3.015  44.319 1.00 38.26 ? 93  LYS   A CD  1 
ATOM   617  C CE  . LYS   A 1 80  ? 5.369  -3.778  45.117 1.00 43.58 ? 93  LYS   A CE  1 
ATOM   618  N NZ  . LYS   A 1 80  ? 5.977  -4.668  46.144 1.00 45.10 ? 93  LYS   A NZ  1 
ATOM   619  N N   . TYR   A 1 81  ? 7.386  -0.190  38.977 1.00 18.01 ? 94  TYR   A N   1 
ATOM   620  C CA  . TYR   A 1 81  ? 8.134  0.868   38.314 1.00 17.59 ? 94  TYR   A CA  1 
ATOM   621  C C   . TYR   A 1 81  ? 7.347  2.175   38.316 1.00 20.82 ? 94  TYR   A C   1 
ATOM   622  O O   . TYR   A 1 81  ? 6.139  2.197   38.064 1.00 17.94 ? 94  TYR   A O   1 
ATOM   623  C CB  . TYR   A 1 81  ? 8.471  0.452   36.882 1.00 21.88 ? 94  TYR   A CB  1 
ATOM   624  C CG  . TYR   A 1 81  ? 9.027  1.569   36.031 1.00 20.04 ? 94  TYR   A CG  1 
ATOM   625  C CD1 . TYR   A 1 81  ? 10.247 2.159   36.334 1.00 16.76 ? 94  TYR   A CD1 1 
ATOM   626  C CD2 . TYR   A 1 81  ? 8.335  2.027   34.918 1.00 20.36 ? 94  TYR   A CD2 1 
ATOM   627  C CE1 . TYR   A 1 81  ? 10.757 3.180   35.557 1.00 17.79 ? 94  TYR   A CE1 1 
ATOM   628  C CE2 . TYR   A 1 81  ? 8.839  3.045   34.134 1.00 20.71 ? 94  TYR   A CE2 1 
ATOM   629  C CZ  . TYR   A 1 81  ? 10.049 3.617   34.458 1.00 21.49 ? 94  TYR   A CZ  1 
ATOM   630  O OH  . TYR   A 1 81  ? 10.550 4.629   33.678 1.00 23.42 ? 94  TYR   A OH  1 
ATOM   631  N N   . ASN   A 1 82  ? 8.045  3.270   38.610 1.00 17.20 ? 95  ASN   A N   1 
ATOM   632  C CA  . ASN   A 1 82  ? 7.469  4.609   38.624 1.00 19.15 ? 95  ASN   A CA  1 
ATOM   633  C C   . ASN   A 1 82  ? 7.980  5.357   37.400 1.00 17.81 ? 95  ASN   A C   1 
ATOM   634  O O   . ASN   A 1 82  ? 9.194  5.479   37.206 1.00 15.95 ? 95  ASN   A O   1 
ATOM   635  C CB  . ASN   A 1 82  ? 7.833  5.349   39.911 1.00 18.69 ? 95  ASN   A CB  1 
ATOM   636  C CG  . ASN   A 1 82  ? 7.076  6.655   40.071 1.00 18.29 ? 95  ASN   A CG  1 
ATOM   637  O OD1 . ASN   A 1 82  ? 7.356  7.636   39.381 1.00 17.91 ? 95  ASN   A OD1 1 
ATOM   638  N ND2 . ASN   A 1 82  ? 6.118  6.675   40.991 1.00 19.23 ? 95  ASN   A ND2 1 
ATOM   639  N N   . THR   A 1 83  ? 7.053  5.865   36.586 1.00 18.76 ? 96  THR   A N   1 
ATOM   640  C CA  . THR   A 1 83  ? 7.414  6.415   35.283 1.00 21.28 ? 96  THR   A CA  1 
ATOM   641  C C   . THR   A 1 83  ? 8.160  7.742   35.372 1.00 21.96 ? 96  THR   A C   1 
ATOM   642  O O   . THR   A 1 83  ? 8.806  8.133   34.394 1.00 24.57 ? 96  THR   A O   1 
ATOM   643  C CB  . THR   A 1 83  ? 6.163  6.584   34.422 1.00 22.69 ? 96  THR   A CB  1 
ATOM   644  O OG1 . THR   A 1 83  ? 5.109  7.150   35.212 1.00 25.91 ? 96  THR   A OG1 1 
ATOM   645  C CG2 . THR   A 1 83  ? 5.714  5.240   33.868 1.00 22.54 ? 96  THR   A CG2 1 
ATOM   646  N N   . SER   A 1 84  ? 8.090  8.446   36.500 1.00 20.82 ? 97  SER   A N   1 
ATOM   647  C CA  . SER   A 1 84  ? 8.774  9.726   36.643 1.00 17.57 ? 97  SER   A CA  1 
ATOM   648  C C   . SER   A 1 84  ? 9.966  9.665   37.587 1.00 21.64 ? 97  SER   A C   1 
ATOM   649  O O   . SER   A 1 84  ? 11.039 10.176  37.256 1.00 24.27 ? 97  SER   A O   1 
ATOM   650  C CB  . SER   A 1 84  ? 7.788  10.809  37.109 1.00 20.22 ? 97  SER   A CB  1 
ATOM   651  O OG  . SER   A 1 84  ? 6.667  10.242  37.761 1.00 24.68 ? 97  SER   A OG  1 
ATOM   652  N N   . THR   A 1 85  ? 9.812  9.051   38.761 1.00 19.17 ? 98  THR   A N   1 
ATOM   653  C CA  . THR   A 1 85  ? 10.917 8.947   39.705 1.00 20.63 ? 98  THR   A CA  1 
ATOM   654  C C   . THR   A 1 85  ? 11.901 7.841   39.347 1.00 19.84 ? 98  THR   A C   1 
ATOM   655  O O   . THR   A 1 85  ? 12.987 7.785   39.937 1.00 18.97 ? 98  THR   A O   1 
ATOM   656  C CB  . THR   A 1 85  ? 10.386 8.715   41.122 1.00 20.29 ? 98  THR   A CB  1 
ATOM   657  O OG1 . THR   A 1 85  ? 9.870  7.384   41.228 1.00 19.49 ? 98  THR   A OG1 1 
ATOM   658  C CG2 . THR   A 1 85  ? 9.276  9.703   41.436 1.00 21.14 ? 98  THR   A CG2 1 
ATOM   659  N N   . LEU   A 1 86  ? 11.542 6.962   38.410 1.00 17.85 ? 99  LEU   A N   1 
ATOM   660  C CA  . LEU   A 1 86  ? 12.399 5.886   37.916 1.00 16.68 ? 99  LEU   A CA  1 
ATOM   661  C C   . LEU   A 1 86  ? 12.804 4.904   39.010 1.00 17.71 ? 99  LEU   A C   1 
ATOM   662  O O   . LEU   A 1 86  ? 13.839 4.239   38.897 1.00 14.88 ? 99  LEU   A O   1 
ATOM   663  C CB  . LEU   A 1 86  ? 13.648 6.433   37.215 1.00 19.49 ? 99  LEU   A CB  1 
ATOM   664  C CG  . LEU   A 1 86  ? 13.450 7.281   35.955 1.00 23.09 ? 99  LEU   A CG  1 
ATOM   665  C CD1 . LEU   A 1 86  ? 14.672 7.190   35.053 1.00 17.43 ? 99  LEU   A CD1 1 
ATOM   666  C CD2 . LEU   A 1 86  ? 12.195 6.881   35.197 1.00 22.73 ? 99  LEU   A CD2 1 
ATOM   667  N N   . HIS   A 1 87  ? 12.016 4.797   40.077 1.00 17.84 ? 100 HIS   A N   1 
ATOM   668  C CA  . HIS   A 1 87  ? 12.243 3.742   41.053 1.00 17.12 ? 100 HIS   A CA  1 
ATOM   669  C C   . HIS   A 1 87  ? 11.889 2.392   40.444 1.00 18.58 ? 100 HIS   A C   1 
ATOM   670  O O   . HIS   A 1 87  ? 10.891 2.258   39.731 1.00 20.33 ? 100 HIS   A O   1 
ATOM   671  C CB  . HIS   A 1 87  ? 11.421 3.993   42.317 1.00 18.89 ? 100 HIS   A CB  1 
ATOM   672  C CG  . HIS   A 1 87  ? 11.939 5.120   43.155 1.00 23.72 ? 100 HIS   A CG  1 
ATOM   673  N ND1 . HIS   A 1 87  ? 11.476 5.377   44.427 1.00 24.69 ? 100 HIS   A ND1 1 
ATOM   674  C CD2 . HIS   A 1 87  ? 12.888 6.053   42.904 1.00 25.41 ? 100 HIS   A CD2 1 
ATOM   675  C CE1 . HIS   A 1 87  ? 12.114 6.423   44.922 1.00 31.67 ? 100 HIS   A CE1 1 
ATOM   676  N NE2 . HIS   A 1 87  ? 12.975 6.852   44.018 1.00 27.79 ? 100 HIS   A NE2 1 
ATOM   677  N N   . HIS   A 1 88  ? 12.721 1.389   40.729 1.00 16.35 ? 101 HIS   A N   1 
ATOM   678  C CA  . HIS   A 1 88  ? 12.597 0.060   40.128 1.00 20.41 ? 101 HIS   A CA  1 
ATOM   679  C C   . HIS   A 1 88  ? 12.652 0.150   38.603 1.00 16.79 ? 101 HIS   A C   1 
ATOM   680  O O   . HIS   A 1 88  ? 11.782 -0.355  37.890 1.00 15.61 ? 101 HIS   A O   1 
ATOM   681  C CB  . HIS   A 1 88  ? 11.321 -0.642  40.602 1.00 19.10 ? 101 HIS   A CB  1 
ATOM   682  C CG  . HIS   A 1 88  ? 11.057 -0.478  42.066 1.00 21.09 ? 101 HIS   A CG  1 
ATOM   683  N ND1 . HIS   A 1 88  ? 11.846 -1.060  43.034 1.00 19.05 ? 101 HIS   A ND1 1 
ATOM   684  C CD2 . HIS   A 1 88  ? 10.095 0.209   42.727 1.00 20.86 ? 101 HIS   A CD2 1 
ATOM   685  C CE1 . HIS   A 1 88  ? 11.380 -0.742  44.228 1.00 21.31 ? 101 HIS   A CE1 1 
ATOM   686  N NE2 . HIS   A 1 88  ? 10.318 0.027   44.070 1.00 27.70 ? 101 HIS   A NE2 1 
ATOM   687  N N   . ASP   A 1 89  ? 13.698 0.811   38.107 1.00 16.17 ? 102 ASP   A N   1 
ATOM   688  C CA  . ASP   A 1 89  ? 13.890 1.033   36.674 1.00 16.76 ? 102 ASP   A CA  1 
ATOM   689  C C   . ASP   A 1 89  ? 14.601 -0.184  36.086 1.00 17.75 ? 102 ASP   A C   1 
ATOM   690  O O   . ASP   A 1 89  ? 15.803 -0.177  35.812 1.00 15.97 ? 102 ASP   A O   1 
ATOM   691  C CB  . ASP   A 1 89  ? 14.672 2.319   36.439 1.00 15.80 ? 102 ASP   A CB  1 
ATOM   692  C CG  . ASP   A 1 89  ? 14.732 2.711   34.978 1.00 18.76 ? 102 ASP   A CG  1 
ATOM   693  O OD1 . ASP   A 1 89  ? 13.968 2.137   34.174 1.00 15.27 ? 102 ASP   A OD1 1 
ATOM   694  O OD2 . ASP   A 1 89  ? 15.547 3.592   34.632 1.00 16.81 ? 102 ASP   A OD2 1 
ATOM   695  N N   . ILE   A 1 90  ? 13.830 -1.252  35.893 1.00 14.74 ? 103 ILE   A N   1 
ATOM   696  C CA  . ILE   A 1 90  ? 14.352 -2.508  35.364 1.00 15.39 ? 103 ILE   A CA  1 
ATOM   697  C C   . ILE   A 1 90  ? 13.249 -3.184  34.559 1.00 15.49 ? 103 ILE   A C   1 
ATOM   698  O O   . ILE   A 1 90  ? 12.076 -3.159  34.945 1.00 14.77 ? 103 ILE   A O   1 
ATOM   699  C CB  . ILE   A 1 90  ? 14.881 -3.414  36.499 1.00 16.12 ? 103 ILE   A CB  1 
ATOM   700  C CG1 . ILE   A 1 90  ? 15.524 -4.681  35.934 1.00 16.69 ? 103 ILE   A CG1 1 
ATOM   701  C CG2 . ILE   A 1 90  ? 13.771 -3.760  37.485 1.00 20.78 ? 103 ILE   A CG2 1 
ATOM   702  C CD1 . ILE   A 1 90  ? 16.202 -5.538  36.982 1.00 17.63 ? 103 ILE   A CD1 1 
ATOM   703  N N   . MET   A 1 91  ? 13.627 -3.780  33.429 1.00 15.59 ? 104 MET   A N   1 
ATOM   704  C CA  . MET   A 1 91  ? 12.658 -4.382  32.523 1.00 15.46 ? 104 MET   A CA  1 
ATOM   705  C C   . MET   A 1 91  ? 13.271 -5.598  31.845 1.00 15.61 ? 104 MET   A C   1 
ATOM   706  O O   . MET   A 1 91  ? 14.444 -5.580  31.464 1.00 15.60 ? 104 MET   A O   1 
ATOM   707  C CB  . MET   A 1 91  ? 12.187 -3.370  31.470 1.00 16.39 ? 104 MET   A CB  1 
ATOM   708  C CG  . MET   A 1 91  ? 11.243 -3.938  30.422 1.00 17.13 ? 104 MET   A CG  1 
ATOM   709  S SD  . MET   A 1 91  ? 10.523 -2.665  29.367 1.00 21.13 ? 104 MET   A SD  1 
ATOM   710  C CE  . MET   A 1 91  ? 11.995 -1.908  28.686 1.00 18.38 ? 104 MET   A CE  1 
ATOM   711  N N   . LEU   A 1 92  ? 12.467 -6.648  31.695 1.00 15.89 ? 105 LEU   A N   1 
ATOM   712  C CA  . LEU   A 1 92  ? 12.854 -7.850  30.966 1.00 18.44 ? 105 LEU   A CA  1 
ATOM   713  C C   . LEU   A 1 92  ? 12.242 -7.815  29.572 1.00 20.95 ? 105 LEU   A C   1 
ATOM   714  O O   . LEU   A 1 92  ? 11.046 -7.542  29.421 1.00 20.84 ? 105 LEU   A O   1 
ATOM   715  C CB  . LEU   A 1 92  ? 12.401 -9.110  31.706 1.00 19.75 ? 105 LEU   A CB  1 
ATOM   716  C CG  . LEU   A 1 92  ? 13.151 -9.487  32.983 1.00 24.86 ? 105 LEU   A CG  1 
ATOM   717  C CD1 . LEU   A 1 92  ? 12.401 -10.567 33.747 1.00 24.92 ? 105 LEU   A CD1 1 
ATOM   718  C CD2 . LEU   A 1 92  ? 14.558 -9.953  32.647 1.00 27.59 ? 105 LEU   A CD2 1 
ATOM   719  N N   . LEU   A 1 93  ? 13.059 -8.093  28.561 1.00 16.38 ? 106 LEU   A N   1 
ATOM   720  C CA  . LEU   A 1 93  ? 12.618 -8.114  27.173 1.00 17.72 ? 106 LEU   A CA  1 
ATOM   721  C C   . LEU   A 1 93  ? 12.679 -9.539  26.646 1.00 19.44 ? 106 LEU   A C   1 
ATOM   722  O O   . LEU   A 1 93  ? 13.720 -10.196 26.744 1.00 20.77 ? 106 LEU   A O   1 
ATOM   723  C CB  . LEU   A 1 93  ? 13.486 -7.200  26.304 1.00 15.34 ? 106 LEU   A CB  1 
ATOM   724  C CG  . LEU   A 1 93  ? 13.557 -5.721  26.681 1.00 16.20 ? 106 LEU   A CG  1 
ATOM   725  C CD1 . LEU   A 1 93  ? 14.491 -4.983  25.736 1.00 16.14 ? 106 LEU   A CD1 1 
ATOM   726  C CD2 . LEU   A 1 93  ? 12.172 -5.095  26.668 1.00 19.19 ? 106 LEU   A CD2 1 
ATOM   727  N N   . LYS   A 1 94  ? 11.570 -10.011 26.085 1.00 19.89 ? 107 LYS   A N   1 
ATOM   728  C CA  . LYS   A 1 94  ? 11.501 -11.337 25.484 1.00 20.16 ? 107 LYS   A CA  1 
ATOM   729  C C   . LYS   A 1 94  ? 11.674 -11.195 23.977 1.00 20.22 ? 107 LYS   A C   1 
ATOM   730  O O   . LYS   A 1 94  ? 10.872 -10.527 23.315 1.00 19.14 ? 107 LYS   A O   1 
ATOM   731  C CB  . LYS   A 1 94  ? 10.179 -12.027 25.823 1.00 22.44 ? 107 LYS   A CB  1 
ATOM   732  C CG  . LYS   A 1 94  ? 10.173 -13.536 25.581 1.00 27.42 ? 107 LYS   A CG  1 
ATOM   733  C CD  . LYS   A 1 94  ? 9.774  -13.880 24.155 1.00 32.49 ? 107 LYS   A CD  1 
ATOM   734  C CE  . LYS   A 1 94  ? 9.967  -15.354 23.846 1.00 32.95 ? 107 LYS   A CE  1 
ATOM   735  N NZ  . LYS   A 1 94  ? 9.132  -16.218 24.719 1.00 40.54 ? 107 LYS   A NZ  1 
ATOM   736  N N   . LEU   A 1 95  ? 12.718 -11.820 23.443 1.00 22.69 ? 108 LEU   A N   1 
ATOM   737  C CA  . LEU   A 1 95  ? 13.003 -11.739 22.019 1.00 20.97 ? 108 LEU   A CA  1 
ATOM   738  C C   . LEU   A 1 95  ? 12.124 -12.712 21.243 1.00 25.40 ? 108 LEU   A C   1 
ATOM   739  O O   . LEU   A 1 95  ? 11.784 -13.796 21.726 1.00 24.45 ? 108 LEU   A O   1 
ATOM   740  C CB  . LEU   A 1 95  ? 14.480 -12.034 21.754 1.00 20.75 ? 108 LEU   A CB  1 
ATOM   741  C CG  . LEU   A 1 95  ? 15.467 -11.242 22.616 1.00 20.94 ? 108 LEU   A CG  1 
ATOM   742  C CD1 . LEU   A 1 95  ? 16.899 -11.671 22.340 1.00 21.47 ? 108 LEU   A CD1 1 
ATOM   743  C CD2 . LEU   A 1 95  ? 15.299 -9.748  22.396 1.00 15.98 ? 108 LEU   A CD2 1 
ATOM   744  N N   . LYS   A 1 96  ? 11.762 -12.312 20.021 1.00 24.36 ? 109 LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 96  ? 10.902 -13.147 19.188 1.00 27.22 ? 109 LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 96  ? 11.536 -14.507 18.924 1.00 26.62 ? 109 LYS   A C   1 
ATOM   747  O O   . LYS   A 1 96  ? 10.861 -15.541 19.004 1.00 31.29 ? 109 LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 96  ? 10.599 -12.430 17.870 1.00 30.86 ? 109 LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 96  ? 10.016 -13.327 16.789 1.00 32.95 ? 109 LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 96  ? 8.523  -13.528 16.969 1.00 37.00 ? 109 LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 96  ? 7.741  -12.344 16.425 1.00 33.96 ? 109 LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 96  ? 7.936  -12.182 14.956 1.00 40.36 ? 109 LYS   A NZ  1 
ATOM   753  N N   . GLU   A 1 97  ? 12.828 -14.531 18.617 1.00 26.54 ? 110 GLU   A N   1 
ATOM   754  C CA  . GLU   A 1 97  ? 13.559 -15.769 18.401 1.00 31.82 ? 110 GLU   A CA  1 
ATOM   755  C C   . GLU   A 1 97  ? 14.755 -15.834 19.344 1.00 29.29 ? 110 GLU   A C   1 
ATOM   756  O O   . GLU   A 1 97  ? 15.055 -14.888 20.076 1.00 27.31 ? 110 GLU   A O   1 
ATOM   757  C CB  . GLU   A 1 97  ? 14.018 -15.897 16.941 1.00 28.07 ? 110 GLU   A CB  1 
ATOM   758  C CG  . GLU   A 1 97  ? 15.047 -14.863 16.500 1.00 26.16 ? 110 GLU   A CG  1 
ATOM   759  C CD  . GLU   A 1 97  ? 14.427 -13.535 16.101 0.50 32.15 ? 110 GLU   A CD  1 
ATOM   760  O OE1 . GLU   A 1 97  ? 13.191 -13.396 16.201 0.50 33.09 ? 110 GLU   A OE1 1 
ATOM   761  O OE2 . GLU   A 1 97  ? 15.179 -12.629 15.683 0.50 31.11 ? 110 GLU   A OE2 1 
ATOM   762  N N   . LYS   A 1 98  ? 15.431 -16.979 19.330 1.00 29.51 ? 111 LYS   A N   1 
ATOM   763  C CA  . LYS   A 1 98  ? 16.619 -17.187 20.145 1.00 28.86 ? 111 LYS   A CA  1 
ATOM   764  C C   . LYS   A 1 98  ? 17.856 -16.709 19.400 1.00 28.68 ? 111 LYS   A C   1 
ATOM   765  O O   . LYS   A 1 98  ? 18.026 -16.990 18.210 1.00 32.77 ? 111 LYS   A O   1 
ATOM   766  C CB  . LYS   A 1 98  ? 16.780 -18.662 20.513 1.00 31.95 ? 111 LYS   A CB  1 
ATOM   767  C CG  . LYS   A 1 98  ? 15.881 -19.141 21.639 1.00 37.38 ? 111 LYS   A CG  1 
ATOM   768  C CD  . LYS   A 1 98  ? 15.933 -20.656 21.765 1.00 43.09 ? 111 LYS   A CD  1 
ATOM   769  C CE  . LYS   A 1 98  ? 15.292 -21.139 23.057 1.00 48.35 ? 111 LYS   A CE  1 
ATOM   770  N NZ  . LYS   A 1 98  ? 16.125 -20.815 24.248 1.00 56.88 ? 111 LYS   A NZ  1 
ATOM   771  N N   . ALA   A 1 99  ? 18.718 -15.985 20.108 1.00 23.84 ? 112 ALA   A N   1 
ATOM   772  C CA  . ALA   A 1 99  ? 19.996 -15.590 19.542 1.00 24.63 ? 112 ALA   A CA  1 
ATOM   773  C C   . ALA   A 1 99  ? 20.914 -16.801 19.409 1.00 26.51 ? 112 ALA   A C   1 
ATOM   774  O O   . ALA   A 1 99  ? 20.719 -17.841 20.045 1.00 28.45 ? 112 ALA   A O   1 
ATOM   775  C CB  . ALA   A 1 99  ? 20.660 -14.518 20.405 1.00 25.73 ? 112 ALA   A CB  1 
ATOM   776  N N   . SER   A 1 100 ? 21.923 -16.660 18.558 1.00 28.19 ? 113 SER   A N   1 
ATOM   777  C CA  . SER   A 1 100 ? 22.902 -17.712 18.325 1.00 26.89 ? 113 SER   A CA  1 
ATOM   778  C C   . SER   A 1 100 ? 24.151 -17.410 19.143 1.00 26.22 ? 113 SER   A C   1 
ATOM   779  O O   . SER   A 1 100 ? 24.737 -16.330 19.009 1.00 27.25 ? 113 SER   A O   1 
ATOM   780  C CB  . SER   A 1 100 ? 23.240 -17.823 16.839 1.00 26.14 ? 113 SER   A CB  1 
ATOM   781  O OG  . SER   A 1 100 ? 22.082 -18.124 16.077 1.00 27.28 ? 113 SER   A OG  1 
ATOM   782  N N   . LEU   A 1 101 ? 24.551 -18.358 19.987 1.00 28.16 ? 114 LEU   A N   1 
ATOM   783  C CA  . LEU   A 1 101 ? 25.740 -18.187 20.815 1.00 27.02 ? 114 LEU   A CA  1 
ATOM   784  C C   . LEU   A 1 101 ? 26.980 -18.335 19.945 1.00 29.13 ? 114 LEU   A C   1 
ATOM   785  O O   . LEU   A 1 101 ? 27.297 -19.436 19.481 1.00 32.53 ? 114 LEU   A O   1 
ATOM   786  C CB  . LEU   A 1 101 ? 25.748 -19.201 21.955 1.00 30.03 ? 114 LEU   A CB  1 
ATOM   787  C CG  . LEU   A 1 101 ? 24.647 -19.053 23.005 1.00 33.59 ? 114 LEU   A CG  1 
ATOM   788  C CD1 . LEU   A 1 101 ? 24.825 -20.073 24.120 1.00 37.18 ? 114 LEU   A CD1 1 
ATOM   789  C CD2 . LEU   A 1 101 ? 24.628 -17.639 23.565 1.00 32.22 ? 114 LEU   A CD2 1 
ATOM   790  N N   . THR   A 1 102 ? 27.681 -17.226 19.719 1.00 25.93 ? 115 THR   A N   1 
ATOM   791  C CA  . THR   A 1 102 ? 28.864 -17.221 18.870 1.00 28.60 ? 115 THR   A CA  1 
ATOM   792  C C   . THR   A 1 102 ? 30.037 -16.570 19.591 1.00 29.44 ? 115 THR   A C   1 
ATOM   793  O O   . THR   A 1 102 ? 29.975 -16.321 20.799 1.00 26.50 ? 115 THR   A O   1 
ATOM   794  C CB  . THR   A 1 102 ? 28.593 -16.481 17.556 1.00 30.94 ? 115 THR   A CB  1 
ATOM   795  O OG1 . THR   A 1 102 ? 28.341 -15.097 17.829 1.00 22.78 ? 115 THR   A OG1 1 
ATOM   796  C CG2 . THR   A 1 102 ? 27.393 -17.078 16.833 1.00 27.18 ? 115 THR   A CG2 1 
ATOM   797  N N   . LEU   A 1 103 ? 31.116 -16.307 18.851 1.00 28.65 ? 116 LEU   A N   1 
ATOM   798  C CA  . LEU   A 1 103 ? 32.225 -15.530 19.393 1.00 27.91 ? 116 LEU   A CA  1 
ATOM   799  C C   . LEU   A 1 103 ? 31.778 -14.137 19.815 1.00 29.74 ? 116 LEU   A C   1 
ATOM   800  O O   . LEU   A 1 103 ? 32.352 -13.554 20.742 1.00 27.08 ? 116 LEU   A O   1 
ATOM   801  C CB  . LEU   A 1 103 ? 33.347 -15.428 18.359 1.00 32.03 ? 116 LEU   A CB  1 
ATOM   802  C CG  . LEU   A 1 103 ? 32.947 -14.869 16.988 1.00 42.10 ? 116 LEU   A CG  1 
ATOM   803  C CD1 . LEU   A 1 103 ? 34.058 -14.009 16.404 1.00 47.29 ? 116 LEU   A CD1 1 
ATOM   804  C CD2 . LEU   A 1 103 ? 32.580 -15.989 16.022 1.00 35.14 ? 116 LEU   A CD2 1 
ATOM   805  N N   . ALA   A 1 104 ? 30.759 -13.590 19.151 1.00 28.76 ? 117 ALA   A N   1 
ATOM   806  C CA  . ALA   A 1 104 ? 30.328 -12.220 19.386 1.00 24.01 ? 117 ALA   A CA  1 
ATOM   807  C C   . ALA   A 1 104 ? 29.062 -12.110 20.223 1.00 25.46 ? 117 ALA   A C   1 
ATOM   808  O O   . ALA   A 1 104 ? 28.765 -11.019 20.721 1.00 24.22 ? 117 ALA   A O   1 
ATOM   809  C CB  . ALA   A 1 104 ? 30.104 -11.504 18.050 1.00 26.40 ? 117 ALA   A CB  1 
ATOM   810  N N   . VAL   A 1 105 ? 28.310 -13.196 20.386 1.00 25.40 ? 118 VAL   A N   1 
ATOM   811  C CA  . VAL   A 1 105 ? 27.063 -13.186 21.143 1.00 24.13 ? 118 VAL   A CA  1 
ATOM   812  C C   . VAL   A 1 105 ? 27.187 -14.193 22.276 1.00 24.92 ? 118 VAL   A C   1 
ATOM   813  O O   . VAL   A 1 105 ? 27.347 -15.396 22.031 1.00 19.71 ? 118 VAL   A O   1 
ATOM   814  C CB  . VAL   A 1 105 ? 25.850 -13.510 20.258 1.00 22.93 ? 118 VAL   A CB  1 
ATOM   815  C CG1 . VAL   A 1 105 ? 24.570 -13.456 21.078 1.00 25.80 ? 118 VAL   A CG1 1 
ATOM   816  C CG2 . VAL   A 1 105 ? 25.779 -12.553 19.081 1.00 17.93 ? 118 VAL   A CG2 1 
ATOM   817  N N   . GLY   A 1 106 ? 27.097 -13.703 23.514 1.00 18.51 ? 119 GLY   A N   1 
ATOM   818  C CA  . GLY   A 1 106 ? 27.193 -14.557 24.677 1.00 19.32 ? 119 GLY   A CA  1 
ATOM   819  C C   . GLY   A 1 106 ? 26.299 -14.047 25.789 1.00 21.92 ? 119 GLY   A C   1 
ATOM   820  O O   . GLY   A 1 106 ? 25.794 -12.924 25.743 1.00 20.55 ? 119 GLY   A O   1 
ATOM   821  N N   . THR   A 1 107 ? 26.116 -14.896 26.792 1.00 24.10 ? 120 THR   A N   1 
ATOM   822  C CA  . THR   A 1 107 ? 25.244 -14.599 27.917 1.00 24.55 ? 120 THR   A CA  1 
ATOM   823  C C   . THR   A 1 107 ? 26.063 -14.088 29.097 1.00 24.98 ? 120 THR   A C   1 
ATOM   824  O O   . THR   A 1 107 ? 27.185 -14.545 29.335 1.00 27.95 ? 120 THR   A O   1 
ATOM   825  C CB  . THR   A 1 107 ? 24.436 -15.844 28.306 1.00 29.54 ? 120 THR   A CB  1 
ATOM   826  O OG1 . THR   A 1 107 ? 23.072 -15.676 27.900 1.00 32.01 ? 120 THR   A OG1 1 
ATOM   827  C CG2 . THR   A 1 107 ? 24.492 -16.116 29.805 1.00 31.88 ? 120 THR   A CG2 1 
ATOM   828  N N   . LEU   A 1 108 ? 25.505 -13.114 29.817 1.00 25.99 ? 121 LEU   A N   1 
ATOM   829  C CA  . LEU   A 1 108 ? 26.138 -12.599 31.022 1.00 30.69 ? 121 LEU   A CA  1 
ATOM   830  C C   . LEU   A 1 108 ? 25.682 -13.440 32.206 1.00 33.81 ? 121 LEU   A C   1 
ATOM   831  O O   . LEU   A 1 108 ? 24.487 -13.423 32.539 1.00 32.82 ? 121 LEU   A O   1 
ATOM   832  C CB  . LEU   A 1 108 ? 25.777 -11.136 31.235 1.00 31.40 ? 121 LEU   A CB  1 
ATOM   833  C CG  . LEU   A 1 108 ? 26.344 -10.475 32.492 1.00 31.41 ? 121 LEU   A CG  1 
ATOM   834  C CD1 . LEU   A 1 108 ? 27.860 -10.577 32.517 1.00 29.67 ? 121 LEU   A CD1 1 
ATOM   835  C CD2 . LEU   A 1 108 ? 25.901 -9.025  32.573 1.00 32.11 ? 121 LEU   A CD2 1 
ATOM   836  N N   . PRO   A 1 109 ? 26.571 -14.182 32.861 1.00 37.45 ? 122 PRO   A N   1 
ATOM   837  C CA  . PRO   A 1 109 ? 26.141 -15.053 33.959 1.00 46.83 ? 122 PRO   A CA  1 
ATOM   838  C C   . PRO   A 1 109 ? 25.907 -14.276 35.246 1.00 43.24 ? 122 PRO   A C   1 
ATOM   839  O O   . PRO   A 1 109 ? 26.597 -13.297 35.545 1.00 42.25 ? 122 PRO   A O   1 
ATOM   840  C CB  . PRO   A 1 109 ? 27.314 -16.029 34.105 1.00 42.03 ? 122 PRO   A CB  1 
ATOM   841  C CG  . PRO   A 1 109 ? 28.498 -15.229 33.678 1.00 43.28 ? 122 PRO   A CG  1 
ATOM   842  C CD  . PRO   A 1 109 ? 28.012 -14.311 32.582 1.00 39.78 ? 122 PRO   A CD  1 
ATOM   843  N N   . PHE   A 1 110 ? 24.917 -14.728 36.012 1.00 41.65 ? 123 PHE   A N   1 
ATOM   844  C CA  . PHE   A 1 110 ? 24.583 -14.129 37.293 1.00 43.75 ? 123 PHE   A CA  1 
ATOM   845  C C   . PHE   A 1 110 ? 24.981 -15.060 38.427 1.00 44.15 ? 123 PHE   A C   1 
ATOM   846  O O   . PHE   A 1 110 ? 24.554 -16.223 38.446 1.00 46.94 ? 123 PHE   A O   1 
ATOM   847  C CB  . PHE   A 1 110 ? 23.083 -13.816 37.370 1.00 48.43 ? 123 PHE   A CB  1 
ATOM   848  C CG  . PHE   A 1 110 ? 22.710 -12.491 36.760 1.00 45.62 ? 123 PHE   A CG  1 
ATOM   849  C CD1 . PHE   A 1 110 ? 22.981 -12.224 35.428 1.00 44.46 ? 123 PHE   A CD1 1 
ATOM   850  C CD2 . PHE   A 1 110 ? 22.087 -11.514 37.520 1.00 46.18 ? 123 PHE   A CD2 1 
ATOM   851  C CE1 . PHE   A 1 110 ? 22.641 -11.006 34.865 1.00 40.16 ? 123 PHE   A CE1 1 
ATOM   852  C CE2 . PHE   A 1 110 ? 21.744 -10.293 36.963 1.00 44.04 ? 123 PHE   A CE2 1 
ATOM   853  C CZ  . PHE   A 1 110 ? 22.021 -10.040 35.634 1.00 37.70 ? 123 PHE   A CZ  1 
ATOM   854  N N   . PRO   A 1 111 ? 25.793 -14.597 39.375 1.00 44.31 ? 124 PRO   A N   1 
ATOM   855  C CA  . PRO   A 1 111 ? 26.249 -15.474 40.458 1.00 46.59 ? 124 PRO   A CA  1 
ATOM   856  C C   . PRO   A 1 111 ? 25.115 -15.837 41.406 1.00 53.56 ? 124 PRO   A C   1 
ATOM   857  O O   . PRO   A 1 111 ? 24.021 -15.272 41.376 1.00 54.13 ? 124 PRO   A O   1 
ATOM   858  C CB  . PRO   A 1 111 ? 27.319 -14.635 41.163 1.00 45.47 ? 124 PRO   A CB  1 
ATOM   859  C CG  . PRO   A 1 111 ? 26.928 -13.229 40.876 1.00 44.07 ? 124 PRO   A CG  1 
ATOM   860  C CD  . PRO   A 1 111 ? 26.375 -13.249 39.477 1.00 45.48 ? 124 PRO   A CD  1 
ATOM   861  N N   . SER   A 1 112 ? 25.403 -16.819 42.262 1.00 58.14 ? 125 SER   A N   1 
ATOM   862  C CA  . SER   A 1 112 ? 24.425 -17.276 43.241 1.00 64.07 ? 125 SER   A CA  1 
ATOM   863  C C   . SER   A 1 112 ? 24.195 -16.266 44.358 1.00 65.30 ? 125 SER   A C   1 
ATOM   864  O O   . SER   A 1 112 ? 23.156 -16.326 45.024 1.00 87.16 ? 125 SER   A O   1 
ATOM   865  C CB  . SER   A 1 112 ? 24.868 -18.614 43.832 1.00 73.41 ? 125 SER   A CB  1 
ATOM   866  O OG  . SER   A 1 112 ? 26.150 -18.503 44.425 1.00 63.51 ? 125 SER   A OG  1 
ATOM   867  N N   . GLN   A 1 113 ? 25.133 -15.348 44.583 1.00 62.43 ? 126 GLN   A N   1 
ATOM   868  C CA  . GLN   A 1 113 ? 25.029 -14.361 45.650 1.00 57.50 ? 126 GLN   A CA  1 
ATOM   869  C C   . GLN   A 1 113 ? 25.149 -12.960 45.072 1.00 53.86 ? 126 GLN   A C   1 
ATOM   870  O O   . GLN   A 1 113 ? 26.033 -12.696 44.250 1.00 57.94 ? 126 GLN   A O   1 
ATOM   871  C CB  . GLN   A 1 113 ? 26.107 -14.572 46.714 1.00 61.63 ? 126 GLN   A CB  1 
ATOM   872  C CG  . GLN   A 1 113 ? 25.991 -15.874 47.475 1.00 52.82 ? 126 GLN   A CG  1 
ATOM   873  C CD  . GLN   A 1 113 ? 26.781 -15.853 48.765 1.00 48.55 ? 126 GLN   A CD  1 
ATOM   874  O OE1 . GLN   A 1 113 ? 27.842 -16.468 48.868 1.00 53.96 ? 126 GLN   A OE1 1 
ATOM   875  N NE2 . GLN   A 1 113 ? 26.267 -15.140 49.760 1.00 54.77 ? 126 GLN   A NE2 1 
ATOM   876  N N   . PHE   A 1 114 ? 24.262 -12.071 45.508 1.00 52.49 ? 127 PHE   A N   1 
ATOM   877  C CA  . PHE   A 1 114 ? 24.298 -10.657 45.144 1.00 52.93 ? 127 PHE   A CA  1 
ATOM   878  C C   . PHE   A 1 114 ? 24.347 -9.844  46.432 1.00 54.12 ? 127 PHE   A C   1 
ATOM   879  O O   . PHE   A 1 114 ? 23.327 -9.662  47.104 1.00 52.71 ? 127 PHE   A O   1 
ATOM   880  C CB  . PHE   A 1 114 ? 23.095 -10.276 44.289 1.00 46.70 ? 127 PHE   A CB  1 
ATOM   881  C CG  . PHE   A 1 114 ? 23.395 -10.203 42.822 1.00 45.43 ? 127 PHE   A CG  1 
ATOM   882  C CD1 . PHE   A 1 114 ? 23.498 -8.978  42.185 1.00 43.78 ? 127 PHE   A CD1 1 
ATOM   883  C CD2 . PHE   A 1 114 ? 23.578 -11.357 42.079 1.00 46.80 ? 127 PHE   A CD2 1 
ATOM   884  C CE1 . PHE   A 1 114 ? 23.769 -8.905  40.833 1.00 40.45 ? 127 PHE   A CE1 1 
ATOM   885  C CE2 . PHE   A 1 114 ? 23.847 -11.289 40.725 1.00 46.52 ? 127 PHE   A CE2 1 
ATOM   886  C CZ  . PHE   A 1 114 ? 23.946 -10.062 40.102 1.00 42.23 ? 127 PHE   A CZ  1 
ATOM   887  N N   . ASN   A 1 115 ? 25.535 -9.357  46.770 1.00 59.34 ? 128 ASN   A N   1 
ATOM   888  C CA  . ASN   A 1 115 ? 25.711 -8.542  47.961 1.00 59.09 ? 128 ASN   A CA  1 
ATOM   889  C C   . ASN   A 1 115 ? 25.233 -7.118  47.707 1.00 57.17 ? 128 ASN   A C   1 
ATOM   890  O O   . ASN   A 1 115 ? 25.403 -6.576  46.611 1.00 57.60 ? 128 ASN   A O   1 
ATOM   891  C CB  . ASN   A 1 115 ? 27.183 -8.552  48.385 1.00 58.41 ? 128 ASN   A CB  1 
ATOM   892  C CG  . ASN   A 1 115 ? 27.562 -7.354  49.239 1.00 63.72 ? 128 ASN   A CG  1 
ATOM   893  O OD1 . ASN   A 1 115 ? 27.342 -7.340  50.451 1.00 67.50 ? 128 ASN   A OD1 1 
ATOM   894  N ND2 . ASN   A 1 115 ? 28.158 -6.348  48.608 1.00 58.20 ? 128 ASN   A ND2 1 
ATOM   895  N N   . PHE   A 1 116 ? 24.611 -6.524  48.725 1.00 54.03 ? 129 PHE   A N   1 
ATOM   896  C CA  . PHE   A 1 116 ? 24.330 -5.092  48.718 1.00 52.23 ? 129 PHE   A CA  1 
ATOM   897  C C   . PHE   A 1 116 ? 25.656 -4.345  48.696 1.00 50.48 ? 129 PHE   A C   1 
ATOM   898  O O   . PHE   A 1 116 ? 26.352 -4.269  49.713 1.00 43.09 ? 129 PHE   A O   1 
ATOM   899  C CB  . PHE   A 1 116 ? 23.509 -4.698  49.943 1.00 50.56 ? 129 PHE   A CB  1 
ATOM   900  C CG  . PHE   A 1 116 ? 23.171 -3.231  50.003 1.00 45.89 ? 129 PHE   A CG  1 
ATOM   901  C CD1 . PHE   A 1 116 ? 24.007 -2.330  50.647 1.00 48.18 ? 129 PHE   A CD1 1 
ATOM   902  C CD2 . PHE   A 1 116 ? 22.015 -2.754  49.409 1.00 45.51 ? 129 PHE   A CD2 1 
ATOM   903  C CE1 . PHE   A 1 116 ? 23.694 -0.981  50.695 1.00 45.81 ? 129 PHE   A CE1 1 
ATOM   904  C CE2 . PHE   A 1 116 ? 21.697 -1.409  49.456 1.00 41.77 ? 129 PHE   A CE2 1 
ATOM   905  C CZ  . PHE   A 1 116 ? 22.537 -0.523  50.099 1.00 37.59 ? 129 PHE   A CZ  1 
ATOM   906  N N   . VAL   A 1 117 ? 26.003 -3.786  47.542 1.00 46.74 ? 130 VAL   A N   1 
ATOM   907  C CA  . VAL   A 1 117 ? 27.332 -3.221  47.330 1.00 47.80 ? 130 VAL   A CA  1 
ATOM   908  C C   . VAL   A 1 117 ? 27.381 -1.805  47.887 1.00 42.31 ? 130 VAL   A C   1 
ATOM   909  O O   . VAL   A 1 117 ? 26.667 -0.921  47.393 1.00 40.77 ? 130 VAL   A O   1 
ATOM   910  C CB  . VAL   A 1 117 ? 27.711 -3.231  45.842 1.00 44.63 ? 130 VAL   A CB  1 
ATOM   911  C CG1 . VAL   A 1 117 ? 29.098 -2.644  45.660 1.00 46.62 ? 130 VAL   A CG1 1 
ATOM   912  C CG2 . VAL   A 1 117 ? 27.650 -4.645  45.287 1.00 45.71 ? 130 VAL   A CG2 1 
ATOM   913  N N   . PRO   A 1 118 ? 28.213 -1.547  48.891 1.00 44.42 ? 131 PRO   A N   1 
ATOM   914  C CA  . PRO   A 1 118 ? 28.341 -0.193  49.437 1.00 42.98 ? 131 PRO   A CA  1 
ATOM   915  C C   . PRO   A 1 118 ? 29.259 0.652   48.572 1.00 37.55 ? 131 PRO   A C   1 
ATOM   916  O O   . PRO   A 1 118 ? 29.953 0.119   47.692 1.00 35.57 ? 131 PRO   A O   1 
ATOM   917  C CB  . PRO   A 1 118 ? 28.945 -0.440  50.826 1.00 40.79 ? 131 PRO   A CB  1 
ATOM   918  C CG  . PRO   A 1 118 ? 29.735 -1.692  50.657 1.00 41.99 ? 131 PRO   A CG  1 
ATOM   919  C CD  . PRO   A 1 118 ? 28.997 -2.532  49.656 1.00 43.58 ? 131 PRO   A CD  1 
ATOM   920  N N   . PRO   A 1 119 ? 29.296 1.967   48.786 1.00 31.01 ? 132 PRO   A N   1 
ATOM   921  C CA  . PRO   A 1 119 ? 30.137 2.830   47.948 1.00 32.31 ? 132 PRO   A CA  1 
ATOM   922  C C   . PRO   A 1 119 ? 31.618 2.534   48.135 1.00 33.48 ? 132 PRO   A C   1 
ATOM   923  O O   . PRO   A 1 119 ? 32.042 1.830   49.054 1.00 34.73 ? 132 PRO   A O   1 
ATOM   924  C CB  . PRO   A 1 119 ? 29.787 4.244   48.424 1.00 37.53 ? 132 PRO   A CB  1 
ATOM   925  C CG  . PRO   A 1 119 ? 29.208 4.061   49.787 1.00 37.20 ? 132 PRO   A CG  1 
ATOM   926  C CD  . PRO   A 1 119 ? 28.483 2.753   49.730 1.00 36.97 ? 132 PRO   A CD  1 
ATOM   927  N N   . GLY   A 1 120 ? 32.413 3.097   47.224 1.00 33.33 ? 133 GLY   A N   1 
ATOM   928  C CA  . GLY   A 1 120 ? 33.848 2.919   47.211 1.00 33.48 ? 133 GLY   A CA  1 
ATOM   929  C C   . GLY   A 1 120 ? 34.356 1.945   46.169 1.00 36.28 ? 133 GLY   A C   1 
ATOM   930  O O   . GLY   A 1 120 ? 35.562 1.933   45.893 1.00 48.90 ? 133 GLY   A O   1 
ATOM   931  N N   . ARG   A 1 121 ? 33.477 1.142   45.580 1.00 34.00 ? 134 ARG   A N   1 
ATOM   932  C CA  . ARG   A 1 121 ? 33.883 0.148   44.599 1.00 37.89 ? 134 ARG   A CA  1 
ATOM   933  C C   . ARG   A 1 121 ? 34.154 0.792   43.243 1.00 37.95 ? 134 ARG   A C   1 
ATOM   934  O O   . ARG   A 1 121 ? 33.550 1.804   42.876 1.00 34.59 ? 134 ARG   A O   1 
ATOM   935  C CB  . ARG   A 1 121 ? 32.808 -0.932  44.457 1.00 37.90 ? 134 ARG   A CB  1 
ATOM   936  C CG  . ARG   A 1 121 ? 33.008 -2.162  45.341 1.00 43.24 ? 134 ARG   A CG  1 
ATOM   937  C CD  . ARG   A 1 121 ? 33.376 -1.788  46.768 0.50 38.52 ? 134 ARG   A CD  1 
ATOM   938  N NE  . ARG   A 1 121 ? 32.500 -2.414  47.751 0.50 39.23 ? 134 ARG   A NE  1 
ATOM   939  C CZ  . ARG   A 1 121 ? 32.669 -3.638  48.231 0.50 42.14 ? 134 ARG   A CZ  1 
ATOM   940  N NH1 . ARG   A 1 121 ? 33.664 -4.409  47.824 0.50 41.19 ? 134 ARG   A NH1 1 
ATOM   941  N NH2 . ARG   A 1 121 ? 31.819 -4.100  49.143 0.50 44.55 ? 134 ARG   A NH2 1 
ATOM   942  N N   . MET   A 1 122 ? 35.074 0.187   42.498 1.00 35.77 ? 135 MET   A N   1 
ATOM   943  C CA  . MET   A 1 122 ? 35.376 0.589   41.130 1.00 35.97 ? 135 MET   A CA  1 
ATOM   944  C C   . MET   A 1 122 ? 34.738 -0.404  40.168 1.00 33.41 ? 135 MET   A C   1 
ATOM   945  O O   . MET   A 1 122 ? 34.930 -1.617  40.303 1.00 35.81 ? 135 MET   A O   1 
ATOM   946  C CB  . MET   A 1 122 ? 36.886 0.657   40.898 1.00 38.58 ? 135 MET   A CB  1 
ATOM   947  C CG  . MET   A 1 122 ? 37.528 1.960   41.342 1.00 42.12 ? 135 MET   A CG  1 
ATOM   948  S SD  . MET   A 1 122 ? 37.042 3.342   40.292 1.00 50.48 ? 135 MET   A SD  1 
ATOM   949  C CE  . MET   A 1 122 ? 37.918 4.696   41.072 1.00 44.44 ? 135 MET   A CE  1 
ATOM   950  N N   . CYS   A 1 123 ? 33.977 0.110   39.202 1.00 27.96 ? 136 CYS   A N   1 
ATOM   951  C CA  . CYS   A 1 123 ? 33.233 -0.738  38.283 1.00 27.90 ? 136 CYS   A CA  1 
ATOM   952  C C   . CYS   A 1 123 ? 33.343 -0.181  36.871 1.00 26.00 ? 136 CYS   A C   1 
ATOM   953  O O   . CYS   A 1 123 ? 33.905 0.893   36.642 1.00 28.45 ? 136 CYS   A O   1 
ATOM   954  C CB  . CYS   A 1 123 ? 31.763 -0.866  38.700 1.00 28.52 ? 136 CYS   A CB  1 
ATOM   955  S SG  . CYS   A 1 123 ? 31.520 -1.302  40.437 1.00 44.75 ? 136 CYS   A SG  1 
ATOM   956  N N   . ARG   A 1 124 ? 32.802 -0.937  35.919 1.00 22.08 ? 137 ARG   A N   1 
ATOM   957  C CA  . ARG   A 1 124 ? 32.853 -0.594  34.507 1.00 21.94 ? 137 ARG   A CA  1 
ATOM   958  C C   . ARG   A 1 124 ? 31.446 -0.546  33.930 1.00 21.74 ? 137 ARG   A C   1 
ATOM   959  O O   . ARG   A 1 124 ? 30.563 -1.304  34.343 1.00 20.61 ? 137 ARG   A O   1 
ATOM   960  C CB  . ARG   A 1 124 ? 33.689 -1.606  33.718 1.00 25.42 ? 137 ARG   A CB  1 
ATOM   961  C CG  . ARG   A 1 124 ? 35.139 -1.693  34.148 1.00 32.81 ? 137 ARG   A CG  1 
ATOM   962  C CD  . ARG   A 1 124 ? 35.896 -2.690  33.289 1.00 32.75 ? 137 ARG   A CD  1 
ATOM   963  N NE  . ARG   A 1 124 ? 37.336 -2.591  33.487 1.00 45.63 ? 137 ARG   A NE  1 
ATOM   964  C CZ  . ARG   A 1 124 ? 38.116 -1.714  32.870 1.00 44.29 ? 137 ARG   A CZ  1 
ATOM   965  N NH1 . ARG   A 1 124 ? 37.624 -0.840  32.007 1.00 40.38 ? 137 ARG   A NH1 1 
ATOM   966  N NH2 . ARG   A 1 124 ? 39.420 -1.711  33.128 1.00 44.68 ? 137 ARG   A NH2 1 
ATOM   967  N N   . VAL   A 1 125 ? 31.247 0.351   32.969 1.00 18.68 ? 138 VAL   A N   1 
ATOM   968  C CA  . VAL   A 1 125 ? 29.999 0.439   32.219 1.00 18.89 ? 138 VAL   A CA  1 
ATOM   969  C C   . VAL   A 1 125 ? 30.345 0.610   30.746 1.00 21.68 ? 138 VAL   A C   1 
ATOM   970  O O   . VAL   A 1 125 ? 31.313 1.296   30.398 1.00 18.34 ? 138 VAL   A O   1 
ATOM   971  C CB  . VAL   A 1 125 ? 29.102 1.591   32.727 1.00 19.22 ? 138 VAL   A CB  1 
ATOM   972  C CG1 . VAL   A 1 125 ? 29.800 2.932   32.577 1.00 24.53 ? 138 VAL   A CG1 1 
ATOM   973  C CG2 . VAL   A 1 125 ? 27.765 1.592   31.998 1.00 16.45 ? 138 VAL   A CG2 1 
ATOM   974  N N   . ALA   A 1 126 ? 29.570 -0.038  29.880 1.00 20.27 ? 139 ALA   A N   1 
ATOM   975  C CA  . ALA   A 1 126 ? 29.818 -0.013  28.448 1.00 19.06 ? 139 ALA   A CA  1 
ATOM   976  C C   . ALA   A 1 126 ? 28.531 0.313   27.705 1.00 18.69 ? 139 ALA   A C   1 
ATOM   977  O O   . ALA   A 1 126 ? 27.429 0.041   28.189 1.00 19.12 ? 139 ALA   A O   1 
ATOM   978  C CB  . ALA   A 1 126 ? 30.387 -1.351  27.952 1.00 17.54 ? 139 ALA   A CB  1 
ATOM   979  N N   . GLY   A 1 127 ? 28.683 0.903   26.526 1.00 15.16 ? 140 GLY   A N   1 
ATOM   980  C CA  . GLY   A 1 127 ? 27.535 1.237   25.705 1.00 15.01 ? 140 GLY   A CA  1 
ATOM   981  C C   . GLY   A 1 127 ? 27.954 2.012   24.478 1.00 14.64 ? 140 GLY   A C   1 
ATOM   982  O O   . GLY   A 1 127 ? 29.121 2.379   24.304 1.00 17.04 ? 140 GLY   A O   1 
ATOM   983  N N   . TRP   A 1 128 ? 26.964 2.254   23.617 1.00 14.41 ? 141 TRP   A N   1 
ATOM   984  C CA  . TRP   A 1 128 ? 27.142 3.026   22.394 1.00 16.73 ? 141 TRP   A CA  1 
ATOM   985  C C   . TRP   A 1 128 ? 26.531 4.419   22.498 1.00 20.22 ? 141 TRP   A C   1 
ATOM   986  O O   . TRP   A 1 128 ? 26.280 5.060   21.473 1.00 20.99 ? 141 TRP   A O   1 
ATOM   987  C CB  . TRP   A 1 128 ? 26.539 2.287   21.199 1.00 16.61 ? 141 TRP   A CB  1 
ATOM   988  C CG  . TRP   A 1 128 ? 27.194 0.981   20.874 1.00 16.47 ? 141 TRP   A CG  1 
ATOM   989  C CD1 . TRP   A 1 128 ? 28.251 0.781   20.035 1.00 19.73 ? 141 TRP   A CD1 1 
ATOM   990  C CD2 . TRP   A 1 128 ? 26.823 -0.311  21.366 1.00 17.36 ? 141 TRP   A CD2 1 
ATOM   991  N NE1 . TRP   A 1 128 ? 28.566 -0.555  19.979 1.00 17.86 ? 141 TRP   A NE1 1 
ATOM   992  C CE2 . TRP   A 1 128 ? 27.703 -1.247  20.788 1.00 16.38 ? 141 TRP   A CE2 1 
ATOM   993  C CE3 . TRP   A 1 128 ? 25.833 -0.768  22.243 1.00 16.17 ? 141 TRP   A CE3 1 
ATOM   994  C CZ2 . TRP   A 1 128 ? 27.625 -2.612  21.059 1.00 16.76 ? 141 TRP   A CZ2 1 
ATOM   995  C CZ3 . TRP   A 1 128 ? 25.757 -2.124  22.509 1.00 17.42 ? 141 TRP   A CZ3 1 
ATOM   996  C CH2 . TRP   A 1 128 ? 26.647 -3.029  21.920 1.00 17.20 ? 141 TRP   A CH2 1 
ATOM   997  N N   . GLY   A 1 129 ? 26.287 4.899   23.712 1.00 15.89 ? 142 GLY   A N   1 
ATOM   998  C CA  . GLY   A 1 129 ? 25.626 6.171   23.900 1.00 17.68 ? 142 GLY   A CA  1 
ATOM   999  C C   . GLY   A 1 129 ? 26.500 7.347   23.505 1.00 17.76 ? 142 GLY   A C   1 
ATOM   1000 O O   . GLY   A 1 129 ? 27.622 7.207   23.016 1.00 16.73 ? 142 GLY   A O   1 
ATOM   1001 N N   . ARG   A 1 130 ? 25.951 8.540   23.720 1.00 17.00 ? 143 ARG   A N   1 
ATOM   1002 C CA  . ARG   A 1 130 ? 26.668 9.767   23.403 1.00 14.70 ? 143 ARG   A CA  1 
ATOM   1003 C C   . ARG   A 1 130 ? 27.987 9.832   24.163 1.00 14.88 ? 143 ARG   A C   1 
ATOM   1004 O O   . ARG   A 1 130 ? 28.065 9.474   25.342 1.00 16.51 ? 143 ARG   A O   1 
ATOM   1005 C CB  . ARG   A 1 130 ? 25.808 10.985  23.743 1.00 14.33 ? 143 ARG   A CB  1 
ATOM   1006 C CG  . ARG   A 1 130 ? 24.499 11.069  22.973 1.00 18.60 ? 143 ARG   A CG  1 
ATOM   1007 C CD  . ARG   A 1 130 ? 23.703 12.297  23.393 1.00 17.92 ? 143 ARG   A CD  1 
ATOM   1008 N NE  . ARG   A 1 130 ? 22.551 12.544  22.533 1.00 19.75 ? 143 ARG   A NE  1 
ATOM   1009 C CZ  . ARG   A 1 130 ? 22.547 13.389  21.510 1.00 23.83 ? 143 ARG   A CZ  1 
ATOM   1010 N NH1 . ARG   A 1 130 ? 23.627 14.080  21.179 1.00 19.59 ? 143 ARG   A NH1 1 
ATOM   1011 N NH2 . ARG   A 1 130 ? 21.432 13.547  20.803 1.00 27.13 ? 143 ARG   A NH2 1 
ATOM   1012 N N   . THR   A 1 131 ? 29.029 10.288  23.474 1.00 17.85 ? 144 THR   A N   1 
ATOM   1013 C CA  . THR   A 1 131 ? 30.352 10.443  24.062 1.00 18.99 ? 144 THR   A CA  1 
ATOM   1014 C C   . THR   A 1 131 ? 30.514 11.770  24.790 1.00 18.35 ? 144 THR   A C   1 
ATOM   1015 O O   . THR   A 1 131 ? 31.612 12.069  25.270 1.00 18.30 ? 144 THR   A O   1 
ATOM   1016 C CB  . THR   A 1 131 ? 31.428 10.311  22.979 1.00 18.73 ? 144 THR   A CB  1 
ATOM   1017 O OG1 . THR   A 1 131 ? 31.152 11.229  21.914 1.00 20.05 ? 144 THR   A OG1 1 
ATOM   1018 C CG2 . THR   A 1 131 ? 31.450 8.895   22.422 1.00 24.64 ? 144 THR   A CG2 1 
ATOM   1019 N N   . GLY   A 1 132 ? 29.455 12.565  24.870 1.00 16.31 ? 145 GLY   A N   1 
ATOM   1020 C CA  . GLY   A 1 132 ? 29.489 13.830  25.575 1.00 14.59 ? 145 GLY   A CA  1 
ATOM   1021 C C   . GLY   A 1 132 ? 28.192 14.571  25.348 1.00 15.78 ? 145 GLY   A C   1 
ATOM   1022 O O   . GLY   A 1 132 ? 27.320 14.133  24.591 1.00 13.80 ? 145 GLY   A O   1 
ATOM   1023 N N   . VAL   A 1 133 ? 28.072 15.716  26.027 1.00 19.79 ? 146 VAL   A N   1 
ATOM   1024 C CA  . VAL   A 1 133 ? 26.899 16.561  25.838 1.00 18.68 ? 146 VAL   A CA  1 
ATOM   1025 C C   . VAL   A 1 133 ? 26.842 17.021  24.391 1.00 15.93 ? 146 VAL   A C   1 
ATOM   1026 O O   . VAL   A 1 133 ? 27.836 17.507  23.836 1.00 19.69 ? 146 VAL   A O   1 
ATOM   1027 C CB  . VAL   A 1 133 ? 26.927 17.758  26.800 1.00 20.85 ? 146 VAL   A CB  1 
ATOM   1028 C CG1 . VAL   A 1 133 ? 25.717 18.653  26.566 1.00 22.24 ? 146 VAL   A CG1 1 
ATOM   1029 C CG2 . VAL   A 1 133 ? 26.948 17.285  28.229 1.00 22.78 ? 146 VAL   A CG2 1 
ATOM   1030 N N   . LEU   A 1 134 ? 25.677 16.849  23.766 1.00 16.59 ? 147 LEU   A N   1 
ATOM   1031 C CA  . LEU   A 1 134 ? 25.388 17.218  22.382 1.00 21.96 ? 147 LEU   A CA  1 
ATOM   1032 C C   . LEU   A 1 134 ? 26.155 16.377  21.369 1.00 19.65 ? 147 LEU   A C   1 
ATOM   1033 O O   . LEU   A 1 134 ? 25.983 16.581  20.165 1.00 18.11 ? 147 LEU   A O   1 
ATOM   1034 C CB  . LEU   A 1 134 ? 25.660 18.705  22.106 1.00 17.73 ? 147 LEU   A CB  1 
ATOM   1035 C CG  . LEU   A 1 134 ? 25.071 19.678  23.130 1.00 21.94 ? 147 LEU   A CG  1 
ATOM   1036 C CD1 . LEU   A 1 134 ? 25.522 21.105  22.856 1.00 26.62 ? 147 LEU   A CD1 1 
ATOM   1037 C CD2 . LEU   A 1 134 ? 23.552 19.581  23.149 1.00 23.76 ? 147 LEU   A CD2 1 
ATOM   1038 N N   . LYS   A 1 135 ? 27.002 15.443  21.811 1.00 17.88 ? 148 LYS   A N   1 
ATOM   1039 C CA  . LYS   A 1 135 ? 27.737 14.595  20.884 1.00 18.30 ? 148 LYS   A CA  1 
ATOM   1040 C C   . LYS   A 1 135 ? 26.836 13.487  20.342 1.00 20.26 ? 148 LYS   A C   1 
ATOM   1041 O O   . LYS   A 1 135 ? 25.860 13.099  20.988 1.00 20.07 ? 148 LYS   A O   1 
ATOM   1042 C CB  . LYS   A 1 135 ? 28.949 13.976  21.574 1.00 21.51 ? 148 LYS   A CB  1 
ATOM   1043 C CG  . LYS   A 1 135 ? 29.960 14.981  22.099 1.00 23.19 ? 148 LYS   A CG  1 
ATOM   1044 C CD  . LYS   A 1 135 ? 30.501 15.856  20.982 1.00 24.98 ? 148 LYS   A CD  1 
ATOM   1045 C CE  . LYS   A 1 135 ? 30.100 17.310  21.179 0.50 26.83 ? 148 LYS   A CE  1 
ATOM   1046 N NZ  . LYS   A 1 135 ? 30.662 18.182  20.114 0.50 26.27 ? 148 LYS   A NZ  1 
ATOM   1047 N N   . PRO   A 1 136 ? 27.136 12.966  19.157 1.00 23.58 ? 150 PRO   A N   1 
ATOM   1048 C CA  . PRO   A 1 136 ? 26.386 11.812  18.654 1.00 21.18 ? 150 PRO   A CA  1 
ATOM   1049 C C   . PRO   A 1 136 ? 26.770 10.546  19.404 1.00 19.85 ? 150 PRO   A C   1 
ATOM   1050 O O   . PRO   A 1 136 ? 27.757 10.491  20.141 1.00 18.67 ? 150 PRO   A O   1 
ATOM   1051 C CB  . PRO   A 1 136 ? 26.794 11.734  17.180 1.00 21.05 ? 150 PRO   A CB  1 
ATOM   1052 C CG  . PRO   A 1 136 ? 28.143 12.346  17.145 1.00 24.72 ? 150 PRO   A CG  1 
ATOM   1053 C CD  . PRO   A 1 136 ? 28.135 13.438  18.180 1.00 21.32 ? 150 PRO   A CD  1 
ATOM   1054 N N   . GLY   A 1 137 ? 25.952 9.514   19.210 1.00 20.78 ? 151 GLY   A N   1 
ATOM   1055 C CA  . GLY   A 1 137 ? 26.276 8.219   19.772 1.00 17.74 ? 151 GLY   A CA  1 
ATOM   1056 C C   . GLY   A 1 137 ? 27.575 7.677   19.208 1.00 19.22 ? 151 GLY   A C   1 
ATOM   1057 O O   . GLY   A 1 137 ? 27.953 7.956   18.068 1.00 21.54 ? 151 GLY   A O   1 
ATOM   1058 N N   . SER   A 1 138 ? 28.271 6.898   20.029 1.00 18.03 ? 152 SER   A N   1 
ATOM   1059 C CA  . SER   A 1 138 ? 29.570 6.380   19.628 1.00 19.19 ? 152 SER   A CA  1 
ATOM   1060 C C   . SER   A 1 138 ? 29.419 5.364   18.503 1.00 22.67 ? 152 SER   A C   1 
ATOM   1061 O O   . SER   A 1 138 ? 28.477 4.566   18.484 1.00 24.17 ? 152 SER   A O   1 
ATOM   1062 C CB  . SER   A 1 138 ? 30.281 5.745   20.821 1.00 19.62 ? 152 SER   A CB  1 
ATOM   1063 O OG  . SER   A 1 138 ? 31.644 5.503   20.521 1.00 29.82 ? 152 SER   A OG  1 
ATOM   1064 N N   . ASP   A 1 139 ? 30.357 5.407   17.555 1.00 21.84 ? 153 ASP   A N   1 
ATOM   1065 C CA  . ASP   A 1 139 ? 30.343 4.452   16.452 1.00 25.51 ? 153 ASP   A CA  1 
ATOM   1066 C C   . ASP   A 1 139 ? 30.637 3.040   16.942 1.00 25.04 ? 153 ASP   A C   1 
ATOM   1067 O O   . ASP   A 1 139 ? 30.079 2.067   16.422 1.00 27.74 ? 153 ASP   A O   1 
ATOM   1068 C CB  . ASP   A 1 139 ? 31.359 4.866   15.387 1.00 28.62 ? 153 ASP   A CB  1 
ATOM   1069 C CG  . ASP   A 1 139 ? 31.225 6.322   14.986 0.50 31.83 ? 153 ASP   A CG  1 
ATOM   1070 O OD1 . ASP   A 1 139 ? 30.347 7.018   15.539 0.50 30.91 ? 153 ASP   A OD1 1 
ATOM   1071 O OD2 . ASP   A 1 139 ? 32.002 6.773   14.118 0.50 33.41 ? 153 ASP   A OD2 1 
ATOM   1072 N N   . THR   A 1 140 ? 31.507 2.911   17.939 1.00 20.58 ? 154 THR   A N   1 
ATOM   1073 C CA  . THR   A 1 140 ? 31.949 1.626   18.455 1.00 20.49 ? 154 THR   A CA  1 
ATOM   1074 C C   . THR   A 1 140 ? 31.682 1.543   19.952 1.00 19.40 ? 154 THR   A C   1 
ATOM   1075 O O   . THR   A 1 140 ? 31.485 2.556   20.630 1.00 15.83 ? 154 THR   A O   1 
ATOM   1076 C CB  . THR   A 1 140 ? 33.441 1.402   18.183 1.00 26.10 ? 154 THR   A CB  1 
ATOM   1077 O OG1 . THR   A 1 140 ? 34.186 2.517   18.685 1.00 26.18 ? 154 THR   A OG1 1 
ATOM   1078 C CG2 . THR   A 1 140 ? 33.698 1.259   16.689 1.00 30.53 ? 154 THR   A CG2 1 
ATOM   1079 N N   . LEU   A 1 141 ? 31.681 0.314   20.463 1.00 18.62 ? 155 LEU   A N   1 
ATOM   1080 C CA  . LEU   A 1 141 ? 31.395 0.076   21.872 1.00 20.15 ? 155 LEU   A CA  1 
ATOM   1081 C C   . LEU   A 1 141 ? 32.495 0.678   22.740 1.00 19.03 ? 155 LEU   A C   1 
ATOM   1082 O O   . LEU   A 1 141 ? 33.669 0.313   22.614 1.00 24.43 ? 155 LEU   A O   1 
ATOM   1083 C CB  . LEU   A 1 141 ? 31.260 -1.420  22.137 1.00 19.92 ? 155 LEU   A CB  1 
ATOM   1084 C CG  . LEU   A 1 141 ? 30.886 -1.823  23.564 1.00 19.21 ? 155 LEU   A CG  1 
ATOM   1085 C CD1 . LEU   A 1 141 ? 29.500 -1.307  23.918 1.00 18.02 ? 155 LEU   A CD1 1 
ATOM   1086 C CD2 . LEU   A 1 141 ? 30.961 -3.334  23.743 1.00 24.70 ? 155 LEU   A CD2 1 
ATOM   1087 N N   . GLN   A 1 142 ? 32.113 1.593   23.626 1.00 21.35 ? 156 GLN   A N   1 
ATOM   1088 C CA  . GLN   A 1 142 ? 33.028 2.242   24.552 1.00 20.97 ? 156 GLN   A CA  1 
ATOM   1089 C C   . GLN   A 1 142 ? 32.789 1.719   25.962 1.00 21.22 ? 156 GLN   A C   1 
ATOM   1090 O O   . GLN   A 1 142 ? 31.676 1.316   26.309 1.00 21.36 ? 156 GLN   A O   1 
ATOM   1091 C CB  . GLN   A 1 142 ? 32.841 3.762   24.534 1.00 21.94 ? 156 GLN   A CB  1 
ATOM   1092 C CG  . GLN   A 1 142 ? 33.066 4.410   23.178 1.00 27.07 ? 156 GLN   A CG  1 
ATOM   1093 C CD  . GLN   A 1 142 ? 34.502 4.848   22.972 1.00 27.54 ? 156 GLN   A CD  1 
ATOM   1094 O OE1 . GLN   A 1 142 ? 35.090 5.510   23.827 1.00 27.91 ? 156 GLN   A OE1 1 
ATOM   1095 N NE2 . GLN   A 1 142 ? 35.074 4.481   21.832 1.00 33.07 ? 156 GLN   A NE2 1 
ATOM   1096 N N   . GLU   A 1 143 ? 33.842 1.729   26.776 1.00 21.39 ? 157 GLU   A N   1 
ATOM   1097 C CA  . GLU   A 1 143 ? 33.721 1.375   28.183 1.00 21.68 ? 157 GLU   A CA  1 
ATOM   1098 C C   . GLU   A 1 143 ? 34.547 2.339   29.021 1.00 21.54 ? 157 GLU   A C   1 
ATOM   1099 O O   . GLU   A 1 143 ? 35.619 2.782   28.600 1.00 23.05 ? 157 GLU   A O   1 
ATOM   1100 C CB  . GLU   A 1 143 ? 34.162 -0.072  28.447 1.00 22.69 ? 157 GLU   A CB  1 
ATOM   1101 C CG  . GLU   A 1 143 ? 35.599 -0.377  28.064 1.00 26.13 ? 157 GLU   A CG  1 
ATOM   1102 C CD  . GLU   A 1 143 ? 35.990 -1.806  28.387 1.00 38.87 ? 157 GLU   A CD  1 
ATOM   1103 O OE1 . GLU   A 1 143 ? 35.295 -2.442  29.207 1.00 40.04 ? 157 GLU   A OE1 1 
ATOM   1104 O OE2 . GLU   A 1 143 ? 36.990 -2.295  27.818 1.00 41.16 ? 157 GLU   A OE2 1 
ATOM   1105 N N   . VAL   A 1 144 ? 34.039 2.659   30.209 1.00 21.34 ? 158 VAL   A N   1 
ATOM   1106 C CA  . VAL   A 1 144 ? 34.702 3.586   31.115 1.00 21.26 ? 158 VAL   A CA  1 
ATOM   1107 C C   . VAL   A 1 144 ? 34.669 3.003   32.522 1.00 23.52 ? 158 VAL   A C   1 
ATOM   1108 O O   . VAL   A 1 144 ? 33.747 2.270   32.893 1.00 23.29 ? 158 VAL   A O   1 
ATOM   1109 C CB  . VAL   A 1 144 ? 34.053 4.992   31.071 1.00 20.67 ? 158 VAL   A CB  1 
ATOM   1110 C CG1 . VAL   A 1 144 ? 32.644 4.961   31.640 1.00 20.29 ? 158 VAL   A CG1 1 
ATOM   1111 C CG2 . VAL   A 1 144 ? 34.919 6.014   31.799 1.00 22.07 ? 158 VAL   A CG2 1 
ATOM   1112 N N   . LYS   A 1 145 ? 35.700 3.319   33.300 1.00 22.35 ? 159 LYS   A N   1 
ATOM   1113 C CA  . LYS   A 1 145 ? 35.803 2.879   34.684 1.00 24.30 ? 159 LYS   A CA  1 
ATOM   1114 C C   . LYS   A 1 145 ? 35.246 3.965   35.593 1.00 22.85 ? 159 LYS   A C   1 
ATOM   1115 O O   . LYS   A 1 145 ? 35.678 5.120   35.524 1.00 23.64 ? 159 LYS   A O   1 
ATOM   1116 C CB  . LYS   A 1 145 ? 37.256 2.574   35.043 1.00 26.32 ? 159 LYS   A CB  1 
ATOM   1117 C CG  . LYS   A 1 145 ? 37.430 1.645   36.229 1.00 30.62 ? 159 LYS   A CG  1 
ATOM   1118 C CD  . LYS   A 1 145 ? 38.896 1.506   36.600 0.10 30.99 ? 159 LYS   A CD  1 
ATOM   1119 C CE  . LYS   A 1 145 ? 39.115 0.353   37.561 0.10 32.19 ? 159 LYS   A CE  1 
ATOM   1120 N NZ  . LYS   A 1 145 ? 38.928 -0.965  36.895 0.10 32.80 ? 159 LYS   A NZ  1 
ATOM   1121 N N   . LEU   A 1 146 ? 34.291 3.594   36.444 1.00 23.77 ? 160 LEU   A N   1 
ATOM   1122 C CA  . LEU   A 1 146 ? 33.592 4.550   37.290 1.00 23.66 ? 160 LEU   A CA  1 
ATOM   1123 C C   . LEU   A 1 146 ? 33.654 4.103   38.744 1.00 27.74 ? 160 LEU   A C   1 
ATOM   1124 O O   . LEU   A 1 146 ? 33.809 2.917   39.051 1.00 24.82 ? 160 LEU   A O   1 
ATOM   1125 C CB  . LEU   A 1 146 ? 32.130 4.719   36.855 1.00 22.21 ? 160 LEU   A CB  1 
ATOM   1126 C CG  . LEU   A 1 146 ? 31.898 5.232   35.433 1.00 22.25 ? 160 LEU   A CG  1 
ATOM   1127 C CD1 . LEU   A 1 146 ? 30.413 5.416   35.169 1.00 23.99 ? 160 LEU   A CD1 1 
ATOM   1128 C CD2 . LEU   A 1 146 ? 32.651 6.532   35.201 1.00 24.11 ? 160 LEU   A CD2 1 
ATOM   1129 N N   . ARG   A 1 147 ? 33.524 5.077   39.639 1.00 24.00 ? 161 ARG   A N   1 
ATOM   1130 C CA  . ARG   A 1 147 ? 33.605 4.849   41.075 1.00 28.32 ? 161 ARG   A CA  1 
ATOM   1131 C C   . ARG   A 1 147 ? 32.213 4.908   41.687 1.00 24.96 ? 161 ARG   A C   1 
ATOM   1132 O O   . ARG   A 1 147 ? 31.436 5.821   41.388 1.00 24.22 ? 161 ARG   A O   1 
ATOM   1133 C CB  . ARG   A 1 147 ? 34.511 5.889   41.739 1.00 31.78 ? 161 ARG   A CB  1 
ATOM   1134 C CG  . ARG   A 1 147 ? 34.745 5.659   43.225 1.00 32.92 ? 161 ARG   A CG  1 
ATOM   1135 C CD  . ARG   A 1 147 ? 35.427 6.858   43.867 1.00 35.38 ? 161 ARG   A CD  1 
ATOM   1136 N NE  . ARG   A 1 147 ? 35.987 6.538   45.175 1.00 38.42 ? 161 ARG   A NE  1 
ATOM   1137 C CZ  . ARG   A 1 147 ? 35.309 6.579   46.314 1.00 38.61 ? 161 ARG   A CZ  1 
ATOM   1138 N NH1 . ARG   A 1 147 ? 34.029 6.912   46.345 1.00 37.34 ? 161 ARG   A NH1 1 
ATOM   1139 N NH2 . ARG   A 1 147 ? 35.931 6.276   47.450 1.00 34.45 ? 161 ARG   A NH2 1 
ATOM   1140 N N   . LEU   A 1 148 ? 31.901 3.933   42.538 1.00 25.83 ? 162 LEU   A N   1 
ATOM   1141 C CA  . LEU   A 1 148 ? 30.665 3.970   43.312 1.00 26.04 ? 162 LEU   A CA  1 
ATOM   1142 C C   . LEU   A 1 148 ? 30.801 5.021   44.405 1.00 26.51 ? 162 LEU   A C   1 
ATOM   1143 O O   . LEU   A 1 148 ? 31.594 4.862   45.338 1.00 27.56 ? 162 LEU   A O   1 
ATOM   1144 C CB  . LEU   A 1 148 ? 30.362 2.597   43.902 1.00 28.91 ? 162 LEU   A CB  1 
ATOM   1145 C CG  . LEU   A 1 148 ? 29.336 1.764   43.133 1.00 33.96 ? 162 LEU   A CG  1 
ATOM   1146 C CD1 . LEU   A 1 148 ? 29.778 1.556   41.694 1.00 29.26 ? 162 LEU   A CD1 1 
ATOM   1147 C CD2 . LEU   A 1 148 ? 29.102 0.434   43.823 1.00 31.63 ? 162 LEU   A CD2 1 
ATOM   1148 N N   . MET   A 1 149 ? 30.030 6.095   44.291 1.00 25.86 ? 163 MET   A N   1 
ATOM   1149 C CA  . MET   A 1 149 ? 30.183 7.250   45.159 1.00 27.97 ? 163 MET   A CA  1 
ATOM   1150 C C   . MET   A 1 149 ? 29.337 7.115   46.419 1.00 28.93 ? 163 MET   A C   1 
ATOM   1151 O O   . MET   A 1 149 ? 28.384 6.334   46.486 1.00 27.19 ? 163 MET   A O   1 
ATOM   1152 C CB  . MET   A 1 149 ? 29.801 8.531   44.419 1.00 25.30 ? 163 MET   A CB  1 
ATOM   1153 C CG  . MET   A 1 149 ? 30.741 8.890   43.288 1.00 28.72 ? 163 MET   A CG  1 
ATOM   1154 S SD  . MET   A 1 149 ? 32.426 9.145   43.872 1.00 35.24 ? 163 MET   A SD  1 
ATOM   1155 C CE  . MET   A 1 149 ? 32.164 10.420  45.102 1.00 29.18 ? 163 MET   A CE  1 
ATOM   1156 N N   . ASP   A 1 150 ? 29.704 7.903   47.426 1.00 28.67 ? 164 ASP   A N   1 
ATOM   1157 C CA  . ASP   A 1 150 ? 28.886 8.026   48.617 1.00 32.42 ? 164 ASP   A CA  1 
ATOM   1158 C C   . ASP   A 1 150 ? 27.518 8.589   48.229 1.00 30.94 ? 164 ASP   A C   1 
ATOM   1159 O O   . ASP   A 1 150 ? 27.414 9.395   47.300 1.00 30.13 ? 164 ASP   A O   1 
ATOM   1160 C CB  . ASP   A 1 150 ? 29.572 8.937   49.634 1.00 34.55 ? 164 ASP   A CB  1 
ATOM   1161 C CG  . ASP   A 1 150 ? 29.122 8.673   51.056 1.00 44.49 ? 164 ASP   A CG  1 
ATOM   1162 O OD1 . ASP   A 1 150 ? 29.277 7.526   51.525 1.00 50.17 ? 164 ASP   A OD1 1 
ATOM   1163 O OD2 . ASP   A 1 150 ? 28.610 9.608   51.705 1.00 54.32 ? 164 ASP   A OD2 1 
ATOM   1164 N N   . PRO   A 1 151 ? 26.450 8.168   48.913 1.00 35.42 ? 165 PRO   A N   1 
ATOM   1165 C CA  . PRO   A 1 151 ? 25.107 8.635   48.528 1.00 33.76 ? 165 PRO   A CA  1 
ATOM   1166 C C   . PRO   A 1 151 ? 24.960 10.143  48.556 1.00 32.21 ? 165 PRO   A C   1 
ATOM   1167 O O   . PRO   A 1 151 ? 24.137 10.694  47.814 1.00 28.25 ? 165 PRO   A O   1 
ATOM   1168 C CB  . PRO   A 1 151 ? 24.194 7.972   49.567 1.00 30.47 ? 165 PRO   A CB  1 
ATOM   1169 C CG  . PRO   A 1 151 ? 24.974 6.832   50.097 1.00 37.80 ? 165 PRO   A CG  1 
ATOM   1170 C CD  . PRO   A 1 151 ? 26.408 7.210   50.029 1.00 34.87 ? 165 PRO   A CD  1 
ATOM   1171 N N   . GLN   A 1 152 ? 25.737 10.828  49.396 1.00 31.66 ? 166 GLN   A N   1 
ATOM   1172 C CA  . GLN   A 1 152 ? 25.639 12.276  49.513 1.00 35.95 ? 166 GLN   A CA  1 
ATOM   1173 C C   . GLN   A 1 152 ? 26.029 12.992  48.225 1.00 34.51 ? 166 GLN   A C   1 
ATOM   1174 O O   . GLN   A 1 152 ? 25.662 14.158  48.041 1.00 30.49 ? 166 GLN   A O   1 
ATOM   1175 C CB  . GLN   A 1 152 ? 26.508 12.741  50.679 1.00 42.15 ? 166 GLN   A CB  1 
ATOM   1176 C CG  . GLN   A 1 152 ? 26.247 11.952  51.957 1.00 50.92 ? 166 GLN   A CG  1 
ATOM   1177 C CD  . GLN   A 1 152 ? 27.335 12.123  52.999 1.00 58.68 ? 166 GLN   A CD  1 
ATOM   1178 O OE1 . GLN   A 1 152 ? 28.145 13.046  52.922 1.00 64.52 ? 166 GLN   A OE1 1 
ATOM   1179 N NE2 . GLN   A 1 152 ? 27.361 11.225  53.978 1.00 53.27 ? 166 GLN   A NE2 1 
ATOM   1180 N N   . ALA   A 1 153 ? 26.759 12.323  47.329 1.00 31.63 ? 167 ALA   A N   1 
ATOM   1181 C CA  . ALA   A 1 153 ? 27.110 12.932  46.051 1.00 26.69 ? 167 ALA   A CA  1 
ATOM   1182 C C   . ALA   A 1 153 ? 25.918 13.024  45.107 1.00 29.50 ? 167 ALA   A C   1 
ATOM   1183 O O   . ALA   A 1 153 ? 25.945 13.836  44.176 1.00 30.84 ? 167 ALA   A O   1 
ATOM   1184 C CB  . ALA   A 1 153 ? 28.244 12.150  45.387 1.00 25.84 ? 167 ALA   A CB  1 
ATOM   1185 N N   . CYS   A 1 154 ? 24.880 12.215  45.320 1.00 28.68 ? 168 CYS   A N   1 
ATOM   1186 C CA  . CYS   A 1 154 ? 23.670 12.248  44.510 1.00 26.81 ? 168 CYS   A CA  1 
ATOM   1187 C C   . CYS   A 1 154 ? 22.511 12.939  45.222 1.00 29.92 ? 168 CYS   A C   1 
ATOM   1188 O O   . CYS   A 1 154 ? 21.349 12.718  44.861 1.00 27.71 ? 168 CYS   A O   1 
ATOM   1189 C CB  . CYS   A 1 154 ? 23.264 10.830  44.101 1.00 27.54 ? 168 CYS   A CB  1 
ATOM   1190 S SG  . CYS   A 1 154 ? 24.263 10.093  42.783 1.00 22.76 ? 168 CYS   A SG  1 
ATOM   1191 N N   . SER   A 1 155 ? 22.803 13.771  46.226 1.00 28.04 ? 169 SER   A N   1 
ATOM   1192 C CA  . SER   A 1 155 ? 21.750 14.439  46.983 1.00 32.38 ? 169 SER   A CA  1 
ATOM   1193 C C   . SER   A 1 155 ? 20.978 15.450  46.148 1.00 30.25 ? 169 SER   A C   1 
ATOM   1194 O O   . SER   A 1 155 ? 19.853 15.805  46.515 1.00 37.28 ? 169 SER   A O   1 
ATOM   1195 C CB  . SER   A 1 155 ? 22.342 15.133  48.211 1.00 37.95 ? 169 SER   A CB  1 
ATOM   1196 O OG  . SER   A 1 155 ? 22.936 14.198  49.091 1.00 43.71 ? 169 SER   A OG  1 
ATOM   1197 N N   . HIS   A 1 156 ? 21.554 15.927  45.043 1.00 29.53 ? 172 HIS   A N   1 
ATOM   1198 C CA  . HIS   A 1 156 ? 20.864 16.905  44.212 1.00 29.15 ? 172 HIS   A CA  1 
ATOM   1199 C C   . HIS   A 1 156 ? 19.718 16.291  43.417 1.00 26.20 ? 172 HIS   A C   1 
ATOM   1200 O O   . HIS   A 1 156 ? 18.819 17.022  42.989 1.00 33.34 ? 172 HIS   A O   1 
ATOM   1201 C CB  . HIS   A 1 156 ? 21.857 17.591  43.270 1.00 27.20 ? 172 HIS   A CB  1 
ATOM   1202 C CG  . HIS   A 1 156 ? 22.669 16.640  42.445 1.00 24.29 ? 172 HIS   A CG  1 
ATOM   1203 N ND1 . HIS   A 1 156 ? 23.667 15.854  42.980 1.00 22.45 ? 172 HIS   A ND1 1 
ATOM   1204 C CD2 . HIS   A 1 156 ? 22.640 16.361  41.121 1.00 24.77 ? 172 HIS   A CD2 1 
ATOM   1205 C CE1 . HIS   A 1 156 ? 24.212 15.125  42.023 1.00 23.07 ? 172 HIS   A CE1 1 
ATOM   1206 N NE2 . HIS   A 1 156 ? 23.608 15.415  40.884 1.00 26.13 ? 172 HIS   A NE2 1 
ATOM   1207 N N   . PHE   A 1 157 ? 19.724 14.976  43.209 1.00 25.30 ? 173 PHE   A N   1 
ATOM   1208 C CA  . PHE   A 1 157 ? 18.620 14.315  42.528 1.00 27.34 ? 173 PHE   A CA  1 
ATOM   1209 C C   . PHE   A 1 157 ? 17.448 14.162  43.491 1.00 28.86 ? 173 PHE   A C   1 
ATOM   1210 O O   . PHE   A 1 157 ? 17.601 13.622  44.591 1.00 28.26 ? 173 PHE   A O   1 
ATOM   1211 C CB  . PHE   A 1 157 ? 19.056 12.957  41.979 1.00 28.15 ? 173 PHE   A CB  1 
ATOM   1212 C CG  . PHE   A 1 157 ? 20.047 13.052  40.851 1.00 22.87 ? 173 PHE   A CG  1 
ATOM   1213 C CD1 . PHE   A 1 157 ? 19.695 13.650  39.653 1.00 20.32 ? 173 PHE   A CD1 1 
ATOM   1214 C CD2 . PHE   A 1 157 ? 21.326 12.539  40.990 1.00 21.12 ? 173 PHE   A CD2 1 
ATOM   1215 C CE1 . PHE   A 1 157 ? 20.602 13.740  38.616 1.00 21.64 ? 173 PHE   A CE1 1 
ATOM   1216 C CE2 . PHE   A 1 157 ? 22.236 12.625  39.956 1.00 20.50 ? 173 PHE   A CE2 1 
ATOM   1217 C CZ  . PHE   A 1 157 ? 21.874 13.226  38.768 1.00 20.71 ? 173 PHE   A CZ  1 
ATOM   1218 N N   . ARG   A 1 158 ? 16.276 14.645  43.069 1.00 22.97 ? 174 ARG   A N   1 
ATOM   1219 C CA  . ARG   A 1 158 ? 15.140 14.769  43.979 1.00 29.45 ? 174 ARG   A CA  1 
ATOM   1220 C C   . ARG   A 1 158 ? 14.652 13.411  44.470 1.00 31.45 ? 174 ARG   A C   1 
ATOM   1221 O O   . ARG   A 1 158 ? 14.375 13.238  45.663 1.00 31.11 ? 174 ARG   A O   1 
ATOM   1222 C CB  . ARG   A 1 158 ? 14.013 15.537  43.287 1.00 34.83 ? 174 ARG   A CB  1 
ATOM   1223 C CG  . ARG   A 1 158 ? 12.774 15.760  44.137 1.00 34.58 ? 174 ARG   A CG  1 
ATOM   1224 C CD  . ARG   A 1 158 ? 12.062 17.041  43.725 1.00 31.19 ? 174 ARG   A CD  1 
ATOM   1225 N NE  . ARG   A 1 158 ? 12.805 18.226  44.138 0.10 30.32 ? 174 ARG   A NE  1 
ATOM   1226 C CZ  . ARG   A 1 158 ? 12.402 19.076  45.073 0.10 29.87 ? 174 ARG   A CZ  1 
ATOM   1227 N NH1 . ARG   A 1 158 ? 11.241 18.927  45.688 0.10 29.71 ? 174 ARG   A NH1 1 
ATOM   1228 N NH2 . ARG   A 1 158 ? 13.182 20.105  45.394 0.10 29.37 ? 174 ARG   A NH2 1 
ATOM   1229 N N   . ASP   A 1 159 ? 14.540 12.433  43.573 1.00 30.65 ? 175 ASP   A N   1 
ATOM   1230 C CA  . ASP   A 1 159 ? 13.959 11.140  43.909 1.00 33.66 ? 175 ASP   A CA  1 
ATOM   1231 C C   . ASP   A 1 159 ? 15.001 10.047  44.107 1.00 28.56 ? 175 ASP   A C   1 
ATOM   1232 O O   . ASP   A 1 159 ? 14.641 8.867   44.157 1.00 27.40 ? 175 ASP   A O   1 
ATOM   1233 C CB  . ASP   A 1 159 ? 12.959 10.718  42.831 1.00 31.39 ? 175 ASP   A CB  1 
ATOM   1234 C CG  . ASP   A 1 159 ? 11.926 11.791  42.544 1.00 33.71 ? 175 ASP   A CG  1 
ATOM   1235 O OD1 . ASP   A 1 159 ? 12.066 12.495  41.521 1.00 37.40 ? 175 ASP   A OD1 1 
ATOM   1236 O OD2 . ASP   A 1 159 ? 10.981 11.938  43.347 1.00 38.19 ? 175 ASP   A OD2 1 
ATOM   1237 N N   . PHE   A 1 160 ? 16.278 10.404  44.217 1.00 26.24 ? 176 PHE   A N   1 
ATOM   1238 C CA  . PHE   A 1 160 ? 17.310 9.401   44.436 1.00 24.66 ? 176 PHE   A CA  1 
ATOM   1239 C C   . PHE   A 1 160 ? 17.151 8.767   45.812 1.00 28.71 ? 176 PHE   A C   1 
ATOM   1240 O O   . PHE   A 1 160 ? 16.946 9.463   46.812 1.00 33.09 ? 176 PHE   A O   1 
ATOM   1241 C CB  . PHE   A 1 160 ? 18.698 10.022  44.298 1.00 25.12 ? 176 PHE   A CB  1 
ATOM   1242 C CG  . PHE   A 1 160 ? 19.818 9.107   44.720 1.00 28.67 ? 176 PHE   A CG  1 
ATOM   1243 C CD1 . PHE   A 1 160 ? 20.238 8.077   43.894 1.00 26.42 ? 176 PHE   A CD1 1 
ATOM   1244 C CD2 . PHE   A 1 160 ? 20.451 9.281   45.940 1.00 31.78 ? 176 PHE   A CD2 1 
ATOM   1245 C CE1 . PHE   A 1 160 ? 21.267 7.234   44.281 1.00 25.22 ? 176 PHE   A CE1 1 
ATOM   1246 C CE2 . PHE   A 1 160 ? 21.480 8.443   46.332 1.00 30.52 ? 176 PHE   A CE2 1 
ATOM   1247 C CZ  . PHE   A 1 160 ? 21.889 7.418   45.501 1.00 26.16 ? 176 PHE   A CZ  1 
ATOM   1248 N N   . ASP   A 1 161 ? 17.244 7.440   45.859 1.00 26.27 ? 177 ASP   A N   1 
ATOM   1249 C CA  . ASP   A 1 161 ? 17.254 6.691   47.109 1.00 27.53 ? 177 ASP   A CA  1 
ATOM   1250 C C   . ASP   A 1 161 ? 18.512 5.838   47.131 1.00 28.16 ? 177 ASP   A C   1 
ATOM   1251 O O   . ASP   A 1 161 ? 18.692 4.975   46.266 1.00 27.43 ? 177 ASP   A O   1 
ATOM   1252 C CB  . ASP   A 1 161 ? 16.002 5.819   47.250 1.00 28.37 ? 177 ASP   A CB  1 
ATOM   1253 C CG  . ASP   A 1 161 ? 15.857 5.219   48.637 0.50 29.81 ? 177 ASP   A CG  1 
ATOM   1254 O OD1 . ASP   A 1 161 ? 16.607 5.628   49.549 0.50 30.18 ? 177 ASP   A OD1 1 
ATOM   1255 O OD2 . ASP   A 1 161 ? 14.995 4.334   48.815 0.50 30.71 ? 177 ASP   A OD2 1 
ATOM   1256 N N   . HIS   A 1 162 ? 19.381 6.086   48.114 1.00 28.29 ? 178 HIS   A N   1 
ATOM   1257 C CA  . HIS   A 1 162 ? 20.621 5.324   48.224 1.00 28.54 ? 178 HIS   A CA  1 
ATOM   1258 C C   . HIS   A 1 162 ? 20.356 3.834   48.358 1.00 30.90 ? 178 HIS   A C   1 
ATOM   1259 O O   . HIS   A 1 162 ? 21.132 3.015   47.853 1.00 29.36 ? 178 HIS   A O   1 
ATOM   1260 C CB  . HIS   A 1 162 ? 21.430 5.815   49.422 1.00 32.32 ? 178 HIS   A CB  1 
ATOM   1261 C CG  . HIS   A 1 162 ? 22.407 4.808   49.948 1.00 37.46 ? 178 HIS   A CG  1 
ATOM   1262 N ND1 . HIS   A 1 162 ? 23.372 4.220   49.157 1.00 39.22 ? 178 HIS   A ND1 1 
ATOM   1263 C CD2 . HIS   A 1 162 ? 22.579 4.298   51.191 1.00 36.16 ? 178 HIS   A CD2 1 
ATOM   1264 C CE1 . HIS   A 1 162 ? 24.091 3.388   49.889 1.00 37.24 ? 178 HIS   A CE1 1 
ATOM   1265 N NE2 . HIS   A 1 162 ? 23.630 3.416   51.126 1.00 39.49 ? 178 HIS   A NE2 1 
ATOM   1266 N N   . ASN   A 1 163 A 19.275 3.463   49.034 1.00 32.99 ? 178 ASN   A N   1 
ATOM   1267 C CA  . ASN   A 1 163 A 19.028 2.061   49.328 1.00 32.92 ? 178 ASN   A CA  1 
ATOM   1268 C C   . ASN   A 1 163 A 18.418 1.307   48.154 1.00 31.14 ? 178 ASN   A C   1 
ATOM   1269 O O   . ASN   A 1 163 A 18.401 0.071   48.168 1.00 34.40 ? 178 ASN   A O   1 
ATOM   1270 C CB  . ASN   A 1 163 A 18.131 1.969   50.557 1.00 34.83 ? 178 ASN   A CB  1 
ATOM   1271 C CG  . ASN   A 1 163 A 18.645 2.811   51.701 0.50 33.25 ? 178 ASN   A CG  1 
ATOM   1272 O OD1 . ASN   A 1 163 A 19.808 2.707   52.093 0.50 33.52 ? 178 ASN   A OD1 1 
ATOM   1273 N ND2 . ASN   A 1 163 A 17.785 3.669   52.234 0.50 33.43 ? 178 ASN   A ND2 1 
ATOM   1274 N N   . LEU   A 1 164 ? 17.920 2.020   47.143 1.00 30.00 ? 179 LEU   A N   1 
ATOM   1275 C CA  . LEU   A 1 164 ? 17.392 1.402   45.936 1.00 29.70 ? 179 LEU   A CA  1 
ATOM   1276 C C   . LEU   A 1 164 ? 18.259 1.630   44.709 1.00 28.47 ? 179 LEU   A C   1 
ATOM   1277 O O   . LEU   A 1 164 ? 18.097 0.910   43.719 1.00 28.42 ? 179 LEU   A O   1 
ATOM   1278 C CB  . LEU   A 1 164 ? 15.980 1.929   45.638 1.00 29.99 ? 179 LEU   A CB  1 
ATOM   1279 C CG  . LEU   A 1 164 ? 14.837 1.515   46.564 1.00 34.31 ? 179 LEU   A CG  1 
ATOM   1280 C CD1 . LEU   A 1 164 ? 13.539 2.185   46.133 1.00 31.00 ? 179 LEU   A CD1 1 
ATOM   1281 C CD2 . LEU   A 1 164 ? 14.679 0.002   46.586 1.00 32.20 ? 179 LEU   A CD2 1 
ATOM   1282 N N   . GLN   A 1 165 ? 19.167 2.601   44.749 1.00 26.84 ? 180 GLN   A N   1 
ATOM   1283 C CA  . GLN   A 1 165 ? 19.917 3.009   43.571 1.00 24.33 ? 180 GLN   A CA  1 
ATOM   1284 C C   . GLN   A 1 165 ? 21.375 3.240   43.939 1.00 22.01 ? 180 GLN   A C   1 
ATOM   1285 O O   . GLN   A 1 165 ? 21.718 3.483   45.099 1.00 22.76 ? 180 GLN   A O   1 
ATOM   1286 C CB  . GLN   A 1 165 ? 19.322 4.277   42.944 1.00 20.30 ? 180 GLN   A CB  1 
ATOM   1287 C CG  . GLN   A 1 165 ? 17.930 4.086   42.367 1.00 21.14 ? 180 GLN   A CG  1 
ATOM   1288 C CD  . GLN   A 1 165 ? 17.158 5.385   42.268 1.00 22.14 ? 180 GLN   A CD  1 
ATOM   1289 O OE1 . GLN   A 1 165 ? 17.353 6.300   43.069 1.00 23.07 ? 180 GLN   A OE1 1 
ATOM   1290 N NE2 . GLN   A 1 165 ? 16.274 5.473   41.280 1.00 17.34 ? 180 GLN   A NE2 1 
ATOM   1291 N N   . LEU   A 1 166 ? 22.230 3.159   42.925 1.00 19.73 ? 181 LEU   A N   1 
ATOM   1292 C CA  . LEU   A 1 166 ? 23.658 3.393   43.068 1.00 20.99 ? 181 LEU   A CA  1 
ATOM   1293 C C   . LEU   A 1 166 ? 24.006 4.794   42.583 1.00 21.50 ? 181 LEU   A C   1 
ATOM   1294 O O   . LEU   A 1 166 ? 23.461 5.269   41.583 1.00 21.66 ? 181 LEU   A O   1 
ATOM   1295 C CB  . LEU   A 1 166 ? 24.463 2.362   42.273 1.00 22.73 ? 181 LEU   A CB  1 
ATOM   1296 C CG  . LEU   A 1 166 ? 24.345 0.897   42.692 1.00 23.61 ? 181 LEU   A CG  1 
ATOM   1297 C CD1 . LEU   A 1 166 ? 24.944 -0.006  41.629 1.00 19.75 ? 181 LEU   A CD1 1 
ATOM   1298 C CD2 . LEU   A 1 166 ? 25.031 0.676   44.026 1.00 25.44 ? 181 LEU   A CD2 1 
ATOM   1299 N N   . CYS   A 1 167 ? 24.913 5.450   43.300 1.00 21.76 ? 182 CYS   A N   1 
ATOM   1300 C CA  . CYS   A 1 167 ? 25.443 6.751   42.906 1.00 18.82 ? 182 CYS   A CA  1 
ATOM   1301 C C   . CYS   A 1 167 ? 26.811 6.514   42.274 1.00 22.28 ? 182 CYS   A C   1 
ATOM   1302 O O   . CYS   A 1 167 ? 27.775 6.186   42.973 1.00 22.92 ? 182 CYS   A O   1 
ATOM   1303 C CB  . CYS   A 1 167 ? 25.536 7.682   44.114 1.00 21.06 ? 182 CYS   A CB  1 
ATOM   1304 S SG  . CYS   A 1 167 ? 25.924 9.403   43.727 1.00 26.95 ? 182 CYS   A SG  1 
ATOM   1305 N N   . VAL   A 1 168 ? 26.895 6.674   40.955 1.00 18.18 ? 183 VAL   A N   1 
ATOM   1306 C CA  . VAL   A 1 168 ? 28.053 6.238   40.180 1.00 19.56 ? 183 VAL   A CA  1 
ATOM   1307 C C   . VAL   A 1 168 ? 28.635 7.435   39.439 1.00 20.60 ? 183 VAL   A C   1 
ATOM   1308 O O   . VAL   A 1 168 ? 27.926 8.108   38.681 1.00 19.77 ? 183 VAL   A O   1 
ATOM   1309 C CB  . VAL   A 1 168 ? 27.684 5.119   39.194 1.00 17.94 ? 183 VAL   A CB  1 
ATOM   1310 C CG1 . VAL   A 1 168 ? 28.916 4.640   38.453 1.00 20.03 ? 183 VAL   A CG1 1 
ATOM   1311 C CG2 . VAL   A 1 168 ? 27.013 3.964   39.923 1.00 17.05 ? 183 VAL   A CG2 1 
ATOM   1312 N N   . GLY   A 1 169 ? 29.929 7.682   39.641 1.00 21.22 ? 184 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 169 ? 30.626 8.725   38.912 1.00 23.55 ? 184 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 169 ? 31.254 9.793   39.783 1.00 22.75 ? 184 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 169 ? 30.562 10.459  40.558 1.00 25.44 ? 184 GLY   A O   1 
ATOM   1316 N N   . ASN   A 1 170 ? 32.562 9.974   39.652 1.00 25.94 ? 185 ASN   A N   1 
ATOM   1317 C CA  . ASN   A 1 170 ? 33.273 11.009  40.400 1.00 28.80 ? 185 ASN   A CA  1 
ATOM   1318 C C   . ASN   A 1 170 ? 32.818 12.387  39.936 1.00 26.50 ? 185 ASN   A C   1 
ATOM   1319 O O   . ASN   A 1 170 ? 32.964 12.709  38.749 1.00 25.50 ? 185 ASN   A O   1 
ATOM   1320 C CB  . ASN   A 1 170 ? 34.780 10.844  40.200 1.00 30.62 ? 185 ASN   A CB  1 
ATOM   1321 C CG  . ASN   A 1 170 ? 35.601 11.745  41.106 1.00 33.81 ? 185 ASN   A CG  1 
ATOM   1322 O OD1 . ASN   A 1 170 ? 35.075 12.636  41.770 1.00 38.08 ? 185 ASN   A OD1 1 
ATOM   1323 N ND2 . ASN   A 1 170 ? 36.907 11.519  41.126 1.00 31.08 ? 185 ASN   A ND2 1 
ATOM   1324 N N   . PRO   A 1 171 ? 32.281 13.232  40.824 1.00 27.95 ? 186 PRO   A N   1 
ATOM   1325 C CA  . PRO   A 1 171 ? 31.766 14.539  40.380 1.00 29.14 ? 186 PRO   A CA  1 
ATOM   1326 C C   . PRO   A 1 171 ? 32.833 15.490  39.858 1.00 36.13 ? 186 PRO   A C   1 
ATOM   1327 O O   . PRO   A 1 171 ? 32.480 16.461  39.178 1.00 38.47 ? 186 PRO   A O   1 
ATOM   1328 C CB  . PRO   A 1 171 ? 31.092 15.099  41.641 1.00 33.43 ? 186 PRO   A CB  1 
ATOM   1329 C CG  . PRO   A 1 171 ? 31.732 14.369  42.775 1.00 30.26 ? 186 PRO   A CG  1 
ATOM   1330 C CD  . PRO   A 1 171 ? 32.012 12.991  42.251 1.00 33.53 ? 186 PRO   A CD  1 
ATOM   1331 N N   . ARG   A 1 172 A 34.113 15.256  40.145 1.00 41.35 ? 186 ARG   A N   1 
ATOM   1332 C CA  . ARG   A 1 172 A 35.179 16.146  39.698 1.00 45.02 ? 186 ARG   A CA  1 
ATOM   1333 C C   . ARG   A 1 172 A 35.770 15.731  38.357 1.00 43.35 ? 186 ARG   A C   1 
ATOM   1334 O O   . ARG   A 1 172 A 36.798 16.282  37.948 1.00 41.82 ? 186 ARG   A O   1 
ATOM   1335 C CB  . ARG   A 1 172 A 36.294 16.224  40.740 1.00 45.28 ? 186 ARG   A CB  1 
ATOM   1336 C CG  . ARG   A 1 172 A 35.929 15.681  42.100 1.00 48.21 ? 186 ARG   A CG  1 
ATOM   1337 C CD  . ARG   A 1 172 A 37.176 15.481  42.940 1.00 51.84 ? 186 ARG   A CD  1 
ATOM   1338 N NE  . ARG   A 1 172 A 37.041 14.335  43.830 1.00 59.43 ? 186 ARG   A NE  1 
ATOM   1339 C CZ  . ARG   A 1 172 A 36.563 14.400  45.064 1.00 64.91 ? 186 ARG   A CZ  1 
ATOM   1340 N NH1 . ARG   A 1 172 A 36.173 15.547  45.593 1.00 68.33 ? 186 ARG   A NH1 1 
ATOM   1341 N NH2 . ARG   A 1 172 A 36.473 13.285  45.784 1.00 60.62 ? 186 ARG   A NH2 1 
ATOM   1342 N N   . LYS   A 1 173 B 35.160 14.770  37.673 1.00 29.70 ? 186 LYS   A N   1 
ATOM   1343 C CA  . LYS   A 1 173 B 35.610 14.341  36.359 1.00 28.78 ? 186 LYS   A CA  1 
ATOM   1344 C C   . LYS   A 1 173 B 34.432 14.381  35.394 1.00 31.01 ? 186 LYS   A C   1 
ATOM   1345 O O   . LYS   A 1 173 B 33.305 14.719  35.767 1.00 33.22 ? 186 LYS   A O   1 
ATOM   1346 C CB  . LYS   A 1 173 B 36.232 12.940  36.412 1.00 31.88 ? 186 LYS   A CB  1 
ATOM   1347 C CG  . LYS   A 1 173 B 37.549 12.870  37.170 1.00 28.71 ? 186 LYS   A CG  1 
ATOM   1348 C CD  . LYS   A 1 173 B 38.404 11.718  36.666 1.00 32.76 ? 186 LYS   A CD  1 
ATOM   1349 C CE  . LYS   A 1 173 B 39.740 11.663  37.384 0.50 32.95 ? 186 LYS   A CE  1 
ATOM   1350 N NZ  . LYS   A 1 173 B 40.650 10.657  36.772 0.50 32.21 ? 186 LYS   A NZ  1 
ATOM   1351 N N   . THR   A 1 174 ? 34.704 14.049  34.134 1.00 26.55 ? 187 THR   A N   1 
ATOM   1352 C CA  . THR   A 1 174 ? 33.660 13.931  33.127 1.00 28.27 ? 187 THR   A CA  1 
ATOM   1353 C C   . THR   A 1 174 ? 33.280 12.487  32.833 1.00 25.84 ? 187 THR   A C   1 
ATOM   1354 O O   . THR   A 1 174 ? 32.266 12.258  32.165 1.00 26.66 ? 187 THR   A O   1 
ATOM   1355 C CB  . THR   A 1 174 ? 34.090 14.611  31.821 1.00 32.26 ? 187 THR   A CB  1 
ATOM   1356 O OG1 . THR   A 1 174 ? 35.308 14.022  31.347 1.00 29.10 ? 187 THR   A OG1 1 
ATOM   1357 C CG2 . THR   A 1 174 ? 34.296 16.099  32.037 1.00 25.39 ? 187 THR   A CG2 1 
ATOM   1358 N N   . LYS   A 1 175 ? 34.063 11.518  33.306 1.00 27.19 ? 188 LYS   A N   1 
ATOM   1359 C CA  . LYS   A 1 175 ? 33.765 10.117  33.042 1.00 24.80 ? 188 LYS   A CA  1 
ATOM   1360 C C   . LYS   A 1 175 ? 32.420 9.740   33.646 1.00 24.03 ? 188 LYS   A C   1 
ATOM   1361 O O   . LYS   A 1 175 ? 32.184 9.940   34.841 1.00 23.97 ? 188 LYS   A O   1 
ATOM   1362 C CB  . LYS   A 1 175 ? 34.870 9.225   33.607 1.00 26.98 ? 188 LYS   A CB  1 
ATOM   1363 C CG  . LYS   A 1 175 ? 36.261 9.556   33.093 1.00 27.14 ? 188 LYS   A CG  1 
ATOM   1364 C CD  . LYS   A 1 175 ? 37.231 8.407   33.331 1.00 31.80 ? 188 LYS   A CD  1 
ATOM   1365 C CE  . LYS   A 1 175 ? 37.249 7.978   34.789 1.00 38.54 ? 188 LYS   A CE  1 
ATOM   1366 N NZ  . LYS   A 1 175 ? 38.152 6.812   35.005 1.00 37.60 ? 188 LYS   A NZ  1 
ATOM   1367 N N   . SER   A 1 176 ? 31.541 9.186   32.815 1.00 22.33 ? 189 SER   A N   1 
ATOM   1368 C CA  . SER   A 1 176 ? 30.188 8.843   33.228 1.00 21.96 ? 189 SER   A CA  1 
ATOM   1369 C C   . SER   A 1 176 ? 29.488 8.144   32.073 1.00 22.50 ? 189 SER   A C   1 
ATOM   1370 O O   . SER   A 1 176 ? 29.914 8.236   30.918 1.00 21.58 ? 189 SER   A O   1 
ATOM   1371 C CB  . SER   A 1 176 ? 29.389 10.085  33.644 1.00 27.18 ? 189 SER   A CB  1 
ATOM   1372 O OG  . SER   A 1 176 ? 28.009 9.792   33.763 1.00 29.83 ? 189 SER   A OG  1 
ATOM   1373 N N   . ALA   A 1 177 ? 28.415 7.431   32.403 1.00 19.45 ? 190 ALA   A N   1 
ATOM   1374 C CA  . ALA   A 1 177 ? 27.449 7.058   31.387 1.00 20.57 ? 190 ALA   A CA  1 
ATOM   1375 C C   . ALA   A 1 177 ? 26.610 8.280   31.022 1.00 19.70 ? 190 ALA   A C   1 
ATOM   1376 O O   . ALA   A 1 177 ? 26.616 9.299   31.719 1.00 17.46 ? 190 ALA   A O   1 
ATOM   1377 C CB  . ALA   A 1 177 ? 26.566 5.912   31.877 1.00 17.86 ? 190 ALA   A CB  1 
ATOM   1378 N N   . PHE   A 1 178 ? 25.889 8.184   29.912 1.00 17.01 ? 191 PHE   A N   1 
ATOM   1379 C CA  . PHE   A 1 178 ? 25.108 9.320   29.436 1.00 17.06 ? 191 PHE   A CA  1 
ATOM   1380 C C   . PHE   A 1 178 ? 23.980 8.798   28.551 1.00 15.24 ? 191 PHE   A C   1 
ATOM   1381 O O   . PHE   A 1 178 ? 23.681 7.599   28.540 1.00 13.69 ? 191 PHE   A O   1 
ATOM   1382 C CB  . PHE   A 1 178 ? 26.013 10.328  28.715 1.00 15.21 ? 191 PHE   A CB  1 
ATOM   1383 C CG  . PHE   A 1 178 ? 25.376 11.671  28.503 1.00 17.51 ? 191 PHE   A CG  1 
ATOM   1384 C CD1 . PHE   A 1 178 ? 24.679 12.290  29.528 1.00 17.91 ? 191 PHE   A CD1 1 
ATOM   1385 C CD2 . PHE   A 1 178 ? 25.470 12.313  27.280 1.00 16.16 ? 191 PHE   A CD2 1 
ATOM   1386 C CE1 . PHE   A 1 178 ? 24.085 13.523  29.336 1.00 17.87 ? 191 PHE   A CE1 1 
ATOM   1387 C CE2 . PHE   A 1 178 ? 24.882 13.547  27.082 1.00 16.68 ? 191 PHE   A CE2 1 
ATOM   1388 C CZ  . PHE   A 1 178 ? 24.190 14.154  28.112 1.00 17.09 ? 191 PHE   A CZ  1 
ATOM   1389 N N   . LYS   A 1 179 ? 23.343 9.712   27.817 1.00 15.22 ? 192 LYS   A N   1 
ATOM   1390 C CA  . LYS   A 1 179 ? 22.232 9.359   26.944 1.00 15.06 ? 192 LYS   A CA  1 
ATOM   1391 C C   . LYS   A 1 179 ? 22.653 8.297   25.937 1.00 14.69 ? 192 LYS   A C   1 
ATOM   1392 O O   . LYS   A 1 179 ? 23.734 8.368   25.346 1.00 13.93 ? 192 LYS   A O   1 
ATOM   1393 C CB  . LYS   A 1 179 ? 21.723 10.601  26.207 1.00 15.16 ? 192 LYS   A CB  1 
ATOM   1394 C CG  . LYS   A 1 179 ? 21.214 11.719  27.107 1.00 16.84 ? 192 LYS   A CG  1 
ATOM   1395 C CD  . LYS   A 1 179 ? 20.649 12.863  26.272 1.00 20.93 ? 192 LYS   A CD  1 
ATOM   1396 C CE  . LYS   A 1 179 ? 19.992 13.930  27.134 0.50 23.45 ? 192 LYS   A CE  1 
ATOM   1397 N NZ  . LYS   A 1 179 ? 20.975 14.667  27.972 0.50 22.56 ? 192 LYS   A NZ  1 
ATOM   1398 N N   . GLY   A 1 180 ? 21.785 7.306   25.743 1.00 18.64 ? 193 GLY   A N   1 
ATOM   1399 C CA  . GLY   A 1 180 ? 22.072 6.178   24.893 1.00 16.53 ? 193 GLY   A CA  1 
ATOM   1400 C C   . GLY   A 1 180 ? 22.701 4.997   25.601 1.00 15.35 ? 193 GLY   A C   1 
ATOM   1401 O O   . GLY   A 1 180 ? 22.697 3.889   25.053 1.00 16.54 ? 193 GLY   A O   1 
ATOM   1402 N N   . ASP   A 1 181 ? 23.241 5.201   26.799 1.00 14.07 ? 194 ASP   A N   1 
ATOM   1403 C CA  . ASP   A 1 181 ? 23.796 4.121   27.602 1.00 14.67 ? 194 ASP   A CA  1 
ATOM   1404 C C   . ASP   A 1 181 ? 22.796 3.559   28.602 1.00 14.44 ? 194 ASP   A C   1 
ATOM   1405 O O   . ASP   A 1 181 ? 23.135 2.626   29.337 1.00 17.71 ? 194 ASP   A O   1 
ATOM   1406 C CB  . ASP   A 1 181 ? 25.044 4.604   28.349 1.00 14.82 ? 194 ASP   A CB  1 
ATOM   1407 C CG  . ASP   A 1 181 ? 26.136 5.073   27.412 1.00 15.15 ? 194 ASP   A CG  1 
ATOM   1408 O OD1 . ASP   A 1 181 ? 26.416 4.365   26.423 1.00 16.73 ? 194 ASP   A OD1 1 
ATOM   1409 O OD2 . ASP   A 1 181 ? 26.713 6.151   27.664 1.00 17.98 ? 194 ASP   A OD2 1 
ATOM   1410 N N   . SER   A 1 182 ? 21.581 4.103   28.646 1.00 15.01 ? 195 SER   A N   1 
ATOM   1411 C CA  . SER   A 1 182 ? 20.582 3.642   29.600 1.00 17.33 ? 195 SER   A CA  1 
ATOM   1412 C C   . SER   A 1 182 ? 20.229 2.183   29.349 1.00 15.95 ? 195 SER   A C   1 
ATOM   1413 O O   . SER   A 1 182 ? 20.096 1.744   28.204 1.00 18.06 ? 195 SER   A O   1 
ATOM   1414 C CB  . SER   A 1 182 ? 19.326 4.505   29.503 1.00 18.58 ? 195 SER   A CB  1 
ATOM   1415 O OG  . SER   A 1 182 ? 19.616 5.867   29.748 1.00 23.40 ? 195 SER   A OG  1 
ATOM   1416 N N   . GLY   A 1 183 ? 20.071 1.432   30.435 1.00 13.21 ? 196 GLY   A N   1 
ATOM   1417 C CA  . GLY   A 1 183 ? 19.807 0.015   30.351 1.00 12.97 ? 196 GLY   A CA  1 
ATOM   1418 C C   . GLY   A 1 183 ? 21.042 -0.853  30.310 1.00 15.09 ? 196 GLY   A C   1 
ATOM   1419 O O   . GLY   A 1 183 ? 20.930 -2.072  30.495 1.00 17.89 ? 196 GLY   A O   1 
ATOM   1420 N N   . GLY   A 1 184 ? 22.215 -0.269  30.078 1.00 17.04 ? 197 GLY   A N   1 
ATOM   1421 C CA  . GLY   A 1 184 ? 23.453 -1.010  30.088 1.00 15.64 ? 197 GLY   A CA  1 
ATOM   1422 C C   . GLY   A 1 184 ? 23.851 -1.413  31.492 1.00 17.19 ? 197 GLY   A C   1 
ATOM   1423 O O   . GLY   A 1 184 ? 23.479 -0.769  32.478 1.00 16.91 ? 197 GLY   A O   1 
ATOM   1424 N N   . PRO   A 1 185 ? 24.626 -2.488  31.609 1.00 18.83 ? 198 PRO   A N   1 
ATOM   1425 C CA  . PRO   A 1 185 ? 24.977 -3.001  32.937 1.00 22.76 ? 198 PRO   A CA  1 
ATOM   1426 C C   . PRO   A 1 185 ? 26.152 -2.257  33.548 1.00 19.76 ? 198 PRO   A C   1 
ATOM   1427 O O   . PRO   A 1 185 ? 27.093 -1.857  32.857 1.00 20.67 ? 198 PRO   A O   1 
ATOM   1428 C CB  . PRO   A 1 185 ? 25.342 -4.463  32.656 1.00 22.93 ? 198 PRO   A CB  1 
ATOM   1429 C CG  . PRO   A 1 185 ? 25.931 -4.415  31.276 1.00 24.19 ? 198 PRO   A CG  1 
ATOM   1430 C CD  . PRO   A 1 185 ? 25.187 -3.322  30.530 1.00 21.09 ? 198 PRO   A CD  1 
ATOM   1431 N N   . LEU   A 1 186 ? 26.085 -2.070  34.864 1.00 19.52 ? 199 LEU   A N   1 
ATOM   1432 C CA  . LEU   A 1 186 ? 27.243 -1.658  35.649 1.00 20.46 ? 199 LEU   A CA  1 
ATOM   1433 C C   . LEU   A 1 186 ? 27.937 -2.925  36.131 1.00 22.39 ? 199 LEU   A C   1 
ATOM   1434 O O   . LEU   A 1 186 ? 27.387 -3.671  36.948 1.00 23.01 ? 199 LEU   A O   1 
ATOM   1435 C CB  . LEU   A 1 186 ? 26.830 -0.776  36.824 1.00 19.31 ? 199 LEU   A CB  1 
ATOM   1436 C CG  . LEU   A 1 186 ? 27.986 -0.326  37.720 1.00 19.46 ? 199 LEU   A CG  1 
ATOM   1437 C CD1 . LEU   A 1 186 ? 28.880 0.660   36.984 1.00 22.44 ? 199 LEU   A CD1 1 
ATOM   1438 C CD2 . LEU   A 1 186 ? 27.471 0.273   39.017 1.00 20.46 ? 199 LEU   A CD2 1 
ATOM   1439 N N   . LEU   A 1 187 ? 29.139 -3.173  35.625 1.00 20.31 ? 200 LEU   A N   1 
ATOM   1440 C CA  . LEU   A 1 187 ? 29.839 -4.430  35.855 1.00 28.21 ? 200 LEU   A CA  1 
ATOM   1441 C C   . LEU   A 1 187 ? 30.932 -4.210  36.892 1.00 30.50 ? 200 LEU   A C   1 
ATOM   1442 O O   . LEU   A 1 187 ? 31.938 -3.547  36.617 1.00 27.95 ? 200 LEU   A O   1 
ATOM   1443 C CB  . LEU   A 1 187 ? 30.408 -4.974  34.548 1.00 23.09 ? 200 LEU   A CB  1 
ATOM   1444 C CG  . LEU   A 1 187 ? 29.344 -5.583  33.635 0.50 25.50 ? 200 LEU   A CG  1 
ATOM   1445 C CD1 . LEU   A 1 187 ? 29.815 -5.600  32.196 0.50 22.52 ? 200 LEU   A CD1 1 
ATOM   1446 C CD2 . LEU   A 1 187 ? 28.995 -6.988  34.103 0.50 28.57 ? 200 LEU   A CD2 1 
ATOM   1447 N N   . CYS   A 1 188 ? 30.725 -4.764  38.082 1.00 32.17 ? 201 CYS   A N   1 
ATOM   1448 C CA  . CYS   A 1 188 ? 31.701 -4.729  39.162 1.00 37.53 ? 201 CYS   A CA  1 
ATOM   1449 C C   . CYS   A 1 188 ? 32.304 -6.118  39.309 1.00 46.33 ? 201 CYS   A C   1 
ATOM   1450 O O   . CYS   A 1 188 ? 31.583 -7.081  39.598 1.00 46.71 ? 201 CYS   A O   1 
ATOM   1451 C CB  . CYS   A 1 188 ? 31.053 -4.290  40.476 1.00 38.48 ? 201 CYS   A CB  1 
ATOM   1452 S SG  . CYS   A 1 188 ? 30.105 -2.756  40.389 1.00 56.56 ? 201 CYS   A SG  1 
ATOM   1453 N N   . ALA   A 1 189 ? 33.618 -6.220  39.106 1.00 51.82 ? 202 ALA   A N   1 
ATOM   1454 C CA  . ALA   A 1 189 ? 34.350 -7.474  39.279 1.00 61.74 ? 202 ALA   A CA  1 
ATOM   1455 C C   . ALA   A 1 189 ? 33.791 -8.590  38.398 1.00 49.05 ? 202 ALA   A C   1 
ATOM   1456 O O   . ALA   A 1 189 ? 33.869 -9.769  38.750 1.00 51.86 ? 202 ALA   A O   1 
ATOM   1457 C CB  . ALA   A 1 189 ? 34.365 -7.908  40.748 1.00 49.91 ? 202 ALA   A CB  1 
ATOM   1458 N N   . GLY   A 1 190 ? 33.226 -8.230  37.245 1.00 44.82 ? 207 GLY   A N   1 
ATOM   1459 C CA  . GLY   A 1 190 ? 32.667 -9.199  36.330 1.00 37.71 ? 207 GLY   A CA  1 
ATOM   1460 C C   . GLY   A 1 190 ? 31.207 -9.537  36.549 1.00 43.16 ? 207 GLY   A C   1 
ATOM   1461 O O   . GLY   A 1 190 ? 30.652 -10.332 35.779 1.00 35.51 ? 207 GLY   A O   1 
ATOM   1462 N N   . VAL   A 1 191 ? 30.567 -8.966  37.566 1.00 41.36 ? 208 VAL   A N   1 
ATOM   1463 C CA  . VAL   A 1 191 ? 29.165 -9.224  37.874 1.00 37.58 ? 208 VAL   A CA  1 
ATOM   1464 C C   . VAL   A 1 191 ? 28.388 -7.923  37.725 1.00 32.21 ? 208 VAL   A C   1 
ATOM   1465 O O   . VAL   A 1 191 ? 28.792 -6.886  38.263 1.00 29.41 ? 208 VAL   A O   1 
ATOM   1466 C CB  . VAL   A 1 191 ? 28.993 -9.809  39.288 1.00 37.09 ? 208 VAL   A CB  1 
ATOM   1467 C CG1 . VAL   A 1 191 ? 27.533 -9.759  39.713 1.00 39.11 ? 208 VAL   A CG1 1 
ATOM   1468 C CG2 . VAL   A 1 191 ? 29.508 -11.237 39.331 1.00 39.98 ? 208 VAL   A CG2 1 
ATOM   1469 N N   . ALA   A 1 192 ? 27.275 -7.981  36.997 1.00 30.92 ? 209 ALA   A N   1 
ATOM   1470 C CA  . ALA   A 1 192 ? 26.441 -6.803  36.774 1.00 31.06 ? 209 ALA   A CA  1 
ATOM   1471 C C   . ALA   A 1 192 ? 25.704 -6.445  38.060 1.00 25.93 ? 209 ALA   A C   1 
ATOM   1472 O O   . ALA   A 1 192 ? 24.770 -7.145  38.466 1.00 26.92 ? 209 ALA   A O   1 
ATOM   1473 C CB  . ALA   A 1 192 ? 25.459 -7.061  35.636 1.00 28.48 ? 209 ALA   A CB  1 
ATOM   1474 N N   . GLN   A 1 193 ? 26.116 -5.352  38.699 1.00 22.38 ? 210 GLN   A N   1 
ATOM   1475 C CA  . GLN   A 1 193 ? 25.492 -4.892  39.930 1.00 22.36 ? 210 GLN   A CA  1 
ATOM   1476 C C   . GLN   A 1 193 ? 24.559 -3.706  39.725 1.00 19.72 ? 210 GLN   A C   1 
ATOM   1477 O O   . GLN   A 1 193 ? 23.877 -3.306  40.674 1.00 18.87 ? 210 GLN   A O   1 
ATOM   1478 C CB  . GLN   A 1 193 ? 26.564 -4.511  40.961 1.00 22.68 ? 210 GLN   A CB  1 
ATOM   1479 C CG  . GLN   A 1 193 ? 27.455 -5.663  41.398 1.00 28.43 ? 210 GLN   A CG  1 
ATOM   1480 C CD  . GLN   A 1 193 ? 26.753 -6.625  42.337 1.00 35.51 ? 210 GLN   A CD  1 
ATOM   1481 O OE1 . GLN   A 1 193 ? 25.660 -6.346  42.831 1.00 38.53 ? 210 GLN   A OE1 1 
ATOM   1482 N NE2 . GLN   A 1 193 ? 27.382 -7.767  42.591 1.00 35.73 ? 210 GLN   A NE2 1 
ATOM   1483 N N   . GLY   A 1 194 ? 24.509 -3.138  38.523 1.00 19.67 ? 211 GLY   A N   1 
ATOM   1484 C CA  . GLY   A 1 194 ? 23.704 -1.954  38.296 1.00 18.84 ? 211 GLY   A CA  1 
ATOM   1485 C C   . GLY   A 1 194 ? 23.242 -1.838  36.860 1.00 16.08 ? 211 GLY   A C   1 
ATOM   1486 O O   . GLY   A 1 194 ? 23.787 -2.472  35.950 1.00 15.94 ? 211 GLY   A O   1 
ATOM   1487 N N   . ILE   A 1 195 ? 22.214 -1.013  36.673 1.00 14.99 ? 212 ILE   A N   1 
ATOM   1488 C CA  . ILE   A 1 195 ? 21.660 -0.695  35.363 1.00 15.74 ? 212 ILE   A CA  1 
ATOM   1489 C C   . ILE   A 1 195 ? 21.609 0.821   35.230 1.00 14.06 ? 212 ILE   A C   1 
ATOM   1490 O O   . ILE   A 1 195 ? 21.085 1.504   36.118 1.00 12.10 ? 212 ILE   A O   1 
ATOM   1491 C CB  . ILE   A 1 195 ? 20.257 -1.305  35.174 1.00 16.43 ? 212 ILE   A CB  1 
ATOM   1492 C CG1 . ILE   A 1 195 ? 20.333 -2.833  35.167 1.00 20.14 ? 212 ILE   A CG1 1 
ATOM   1493 C CG2 . ILE   A 1 195 ? 19.607 -0.788  33.899 1.00 15.50 ? 212 ILE   A CG2 1 
ATOM   1494 C CD1 . ILE   A 1 195 ? 18.987 -3.505  35.027 1.00 20.27 ? 212 ILE   A CD1 1 
ATOM   1495 N N   . VAL   A 1 196 ? 22.155 1.346   34.129 1.00 12.13 ? 213 VAL   A N   1 
ATOM   1496 C CA  . VAL   A 1 196 ? 22.133 2.787   33.897 1.00 13.77 ? 213 VAL   A CA  1 
ATOM   1497 C C   . VAL   A 1 196 ? 20.694 3.277   33.890 1.00 12.76 ? 213 VAL   A C   1 
ATOM   1498 O O   . VAL   A 1 196 ? 19.854 2.773   33.134 1.00 12.20 ? 213 VAL   A O   1 
ATOM   1499 C CB  . VAL   A 1 196 ? 22.836 3.129   32.574 1.00 13.83 ? 213 VAL   A CB  1 
ATOM   1500 C CG1 . VAL   A 1 196 ? 22.978 4.638   32.422 1.00 12.27 ? 213 VAL   A CG1 1 
ATOM   1501 C CG2 . VAL   A 1 196 ? 24.190 2.441   32.483 1.00 12.70 ? 213 VAL   A CG2 1 
ATOM   1502 N N   . SER   A 1 197 ? 20.398 4.270   34.731 1.00 11.72 ? 214 SER   A N   1 
ATOM   1503 C CA  . SER   A 1 197 ? 19.037 4.777   34.849 1.00 13.74 ? 214 SER   A CA  1 
ATOM   1504 C C   . SER   A 1 197 ? 18.896 6.215   34.364 1.00 13.96 ? 214 SER   A C   1 
ATOM   1505 O O   . SER   A 1 197 ? 18.143 6.468   33.420 1.00 13.97 ? 214 SER   A O   1 
ATOM   1506 C CB  . SER   A 1 197 ? 18.560 4.652   36.304 1.00 14.56 ? 214 SER   A CB  1 
ATOM   1507 O OG  . SER   A 1 197 ? 17.200 5.028   36.428 1.00 16.00 ? 214 SER   A OG  1 
ATOM   1508 N N   . TYR   A 1 198 ? 19.618 7.164   34.955 1.00 12.59 ? 215 TYR   A N   1 
ATOM   1509 C CA  . TYR   A 1 198 ? 19.466 8.569   34.580 1.00 14.56 ? 215 TYR   A CA  1 
ATOM   1510 C C   . TYR   A 1 198 ? 20.569 9.384   35.244 1.00 14.33 ? 215 TYR   A C   1 
ATOM   1511 O O   . TYR   A 1 198 ? 21.396 8.863   35.999 1.00 14.21 ? 215 TYR   A O   1 
ATOM   1512 C CB  . TYR   A 1 198 ? 18.085 9.115   34.960 1.00 13.77 ? 215 TYR   A CB  1 
ATOM   1513 C CG  . TYR   A 1 198 ? 17.841 9.251   36.449 1.00 16.02 ? 215 TYR   A CG  1 
ATOM   1514 C CD1 . TYR   A 1 198 ? 17.307 8.201   37.183 1.00 16.06 ? 215 TYR   A CD1 1 
ATOM   1515 C CD2 . TYR   A 1 198 ? 18.131 10.435  37.119 1.00 15.26 ? 215 TYR   A CD2 1 
ATOM   1516 C CE1 . TYR   A 1 198 ? 17.075 8.322   38.541 1.00 18.45 ? 215 TYR   A CE1 1 
ATOM   1517 C CE2 . TYR   A 1 198 ? 17.904 10.565  38.476 1.00 16.90 ? 215 TYR   A CE2 1 
ATOM   1518 C CZ  . TYR   A 1 198 ? 17.376 9.505   39.182 1.00 18.47 ? 215 TYR   A CZ  1 
ATOM   1519 O OH  . TYR   A 1 198 ? 17.147 9.628   40.534 1.00 18.61 ? 215 TYR   A OH  1 
ATOM   1520 N N   . GLY   A 1 199 ? 20.559 10.683  34.957 1.00 14.06 ? 216 GLY   A N   1 
ATOM   1521 C CA  . GLY   A 1 199 ? 21.492 11.629  35.534 1.00 15.10 ? 216 GLY   A CA  1 
ATOM   1522 C C   . GLY   A 1 199 ? 21.149 13.049  35.132 1.00 16.67 ? 216 GLY   A C   1 
ATOM   1523 O O   . GLY   A 1 199 ? 19.977 13.367  34.912 1.00 16.35 ? 216 GLY   A O   1 
ATOM   1524 N N   . ARG   A 1 200 ? 22.157 13.907  35.021 1.00 17.11 ? 217 ARG   A N   1 
ATOM   1525 C CA  . ARG   A 1 200 ? 21.950 15.299  34.654 1.00 19.07 ? 217 ARG   A CA  1 
ATOM   1526 C C   . ARG   A 1 200 ? 22.086 15.492  33.148 1.00 19.59 ? 217 ARG   A C   1 
ATOM   1527 O O   . ARG   A 1 200 ? 22.874 14.815  32.482 1.00 17.49 ? 217 ARG   A O   1 
ATOM   1528 C CB  . ARG   A 1 200 ? 22.944 16.200  35.388 1.00 21.65 ? 217 ARG   A CB  1 
ATOM   1529 C CG  . ARG   A 1 200 ? 22.640 16.372  36.867 1.00 23.17 ? 217 ARG   A CG  1 
ATOM   1530 C CD  . ARG   A 1 200 ? 23.812 16.987  37.610 1.00 30.65 ? 217 ARG   A CD  1 
ATOM   1531 N NE  . ARG   A 1 200 ? 24.301 18.202  36.972 1.00 35.56 ? 217 ARG   A NE  1 
ATOM   1532 C CZ  . ARG   A 1 200 ? 23.766 19.404  37.136 1.00 41.40 ? 217 ARG   A CZ  1 
ATOM   1533 N NH1 . ARG   A 1 200 ? 22.694 19.586  37.890 1.00 45.47 ? 217 ARG   A NH1 1 
ATOM   1534 N NH2 . ARG   A 1 200 ? 24.319 20.450  36.528 1.00 35.52 ? 217 ARG   A NH2 1 
ATOM   1535 N N   . SER   A 1 201 ? 21.304 16.438  32.617 1.00 24.32 ? 218 SER   A N   1 
ATOM   1536 C CA  . SER   A 1 201 ? 21.316 16.698  31.179 1.00 25.47 ? 218 SER   A CA  1 
ATOM   1537 C C   . SER   A 1 201 ? 22.678 17.197  30.713 1.00 23.22 ? 218 SER   A C   1 
ATOM   1538 O O   . SER   A 1 201 ? 23.117 16.877  29.602 1.00 20.50 ? 218 SER   A O   1 
ATOM   1539 C CB  . SER   A 1 201 ? 20.224 17.705  30.816 1.00 25.28 ? 218 SER   A CB  1 
ATOM   1540 O OG  . SER   A 1 201 ? 18.934 17.173  31.063 1.00 35.28 ? 218 SER   A OG  1 
ATOM   1541 N N   . ASP   A 1 202 ? 23.361 17.986  31.542 1.00 19.34 ? 219 ASP   A N   1 
ATOM   1542 C CA  . ASP   A 1 202 ? 24.688 18.482  31.201 1.00 22.39 ? 219 ASP   A CA  1 
ATOM   1543 C C   . ASP   A 1 202 ? 25.788 17.459  31.472 1.00 23.80 ? 219 ASP   A C   1 
ATOM   1544 O O   . ASP   A 1 202 ? 26.970 17.806  31.393 1.00 29.11 ? 219 ASP   A O   1 
ATOM   1545 C CB  . ASP   A 1 202 ? 24.980 19.786  31.953 1.00 21.71 ? 219 ASP   A CB  1 
ATOM   1546 C CG  . ASP   A 1 202 ? 24.866 19.638  33.458 1.00 29.04 ? 219 ASP   A CG  1 
ATOM   1547 O OD1 . ASP   A 1 202 ? 24.532 18.533  33.930 1.00 29.33 ? 219 ASP   A OD1 1 
ATOM   1548 O OD2 . ASP   A 1 202 ? 25.112 20.634  34.171 1.00 33.82 ? 219 ASP   A OD2 1 
ATOM   1549 N N   . ALA   A 1 203 ? 25.417 16.225  31.811 1.00 22.56 ? 220 ALA   A N   1 
ATOM   1550 C CA  . ALA   A 1 203 ? 26.311 15.079  31.954 1.00 23.79 ? 220 ALA   A CA  1 
ATOM   1551 C C   . ALA   A 1 203 ? 27.340 15.241  33.061 1.00 22.99 ? 220 ALA   A C   1 
ATOM   1552 O O   . ALA   A 1 203 ? 28.315 14.481  33.100 1.00 25.60 ? 220 ALA   A O   1 
ATOM   1553 C CB  . ALA   A 1 203 ? 27.037 14.755  30.643 1.00 22.18 ? 220 ALA   A CB  1 
ATOM   1554 N N   . LYS   A 1 204 ? 27.172 16.203  33.952 1.00 25.38 ? 221 LYS   A N   1 
ATOM   1555 C CA  . LYS   A 1 204 ? 28.055 16.264  35.107 1.00 23.38 ? 221 LYS   A CA  1 
ATOM   1556 C C   . LYS   A 1 204 ? 27.731 15.094  36.025 1.00 20.61 ? 221 LYS   A C   1 
ATOM   1557 O O   . LYS   A 1 204 ? 26.593 14.987  36.500 1.00 23.62 ? 221 LYS   A O   1 
ATOM   1558 C CB  . LYS   A 1 204 ? 27.904 17.589  35.847 1.00 27.90 ? 221 LYS   A CB  1 
ATOM   1559 C CG  . LYS   A 1 204 ? 28.577 18.766  35.157 0.50 26.42 ? 221 LYS   A CG  1 
ATOM   1560 C CD  . LYS   A 1 204 ? 28.454 20.031  35.991 0.50 27.67 ? 221 LYS   A CD  1 
ATOM   1561 C CE  . LYS   A 1 204 ? 29.076 21.227  35.290 0.50 26.42 ? 221 LYS   A CE  1 
ATOM   1562 N NZ  . LYS   A 1 204 ? 28.863 22.488  36.053 0.50 31.49 ? 221 LYS   A NZ  1 
ATOM   1563 N N   . PRO   A 1 205 ? 28.677 14.201  36.295 1.00 22.81 ? 224 PRO   A N   1 
ATOM   1564 C CA  . PRO   A 1 205 ? 28.400 13.056  37.165 1.00 25.10 ? 224 PRO   A CA  1 
ATOM   1565 C C   . PRO   A 1 205 ? 28.202 13.515  38.598 1.00 22.89 ? 224 PRO   A C   1 
ATOM   1566 O O   . PRO   A 1 205 ? 28.499 14.673  38.927 1.00 26.02 ? 224 PRO   A O   1 
ATOM   1567 C CB  . PRO   A 1 205 ? 29.661 12.189  37.013 1.00 21.08 ? 224 PRO   A CB  1 
ATOM   1568 C CG  . PRO   A 1 205 ? 30.719 13.137  36.611 1.00 27.78 ? 224 PRO   A CG  1 
ATOM   1569 C CD  . PRO   A 1 205 ? 30.056 14.187  35.777 1.00 24.53 ? 224 PRO   A CD  1 
ATOM   1570 N N   . PRO   A 1 206 ? 27.697 12.646  39.490 1.00 22.50 ? 225 PRO   A N   1 
ATOM   1571 C CA  . PRO   A 1 206 ? 27.356 11.221  39.318 1.00 19.19 ? 225 PRO   A CA  1 
ATOM   1572 C C   . PRO   A 1 206 ? 26.050 10.960  38.579 1.00 17.85 ? 225 PRO   A C   1 
ATOM   1573 O O   . PRO   A 1 206 ? 25.191 11.830  38.461 1.00 17.82 ? 225 PRO   A O   1 
ATOM   1574 C CB  . PRO   A 1 206 ? 27.258 10.706  40.768 1.00 21.11 ? 225 PRO   A CB  1 
ATOM   1575 C CG  . PRO   A 1 206 ? 27.786 11.811  41.651 1.00 25.49 ? 225 PRO   A CG  1 
ATOM   1576 C CD  . PRO   A 1 206 ? 27.519 13.066  40.886 1.00 21.34 ? 225 PRO   A CD  1 
ATOM   1577 N N   . ALA   A 1 207 ? 25.896 9.742   38.071 1.00 16.92 ? 226 ALA   A N   1 
ATOM   1578 C CA  . ALA   A 1 207 ? 24.648 9.250   37.511 1.00 17.30 ? 226 ALA   A CA  1 
ATOM   1579 C C   . ALA   A 1 207 ? 24.010 8.265   38.482 1.00 15.59 ? 226 ALA   A C   1 
ATOM   1580 O O   . ALA   A 1 207 ? 24.650 7.773   39.415 1.00 16.24 ? 226 ALA   A O   1 
ATOM   1581 C CB  . ALA   A 1 207 ? 24.879 8.586   36.148 1.00 15.04 ? 226 ALA   A CB  1 
ATOM   1582 N N   . VAL   A 1 208 ? 22.733 7.976   38.249 1.00 14.84 ? 227 VAL   A N   1 
ATOM   1583 C CA  . VAL   A 1 208 ? 21.946 7.099   39.109 1.00 14.74 ? 227 VAL   A CA  1 
ATOM   1584 C C   . VAL   A 1 208 ? 21.772 5.762   38.403 1.00 16.20 ? 227 VAL   A C   1 
ATOM   1585 O O   . VAL   A 1 208 ? 21.387 5.717   37.228 1.00 15.02 ? 227 VAL   A O   1 
ATOM   1586 C CB  . VAL   A 1 208 ? 20.584 7.723   39.457 1.00 14.78 ? 227 VAL   A CB  1 
ATOM   1587 C CG1 . VAL   A 1 208 ? 19.764 6.767   40.309 1.00 16.43 ? 227 VAL   A CG1 1 
ATOM   1588 C CG2 . VAL   A 1 208 ? 20.781 9.046   40.180 1.00 15.79 ? 227 VAL   A CG2 1 
ATOM   1589 N N   . PHE   A 1 209 ? 22.062 4.678   39.120 1.00 14.18 ? 228 PHE   A N   1 
ATOM   1590 C CA  . PHE   A 1 209 ? 21.980 3.319   38.601 1.00 14.92 ? 228 PHE   A CA  1 
ATOM   1591 C C   . PHE   A 1 209 ? 21.019 2.503   39.454 1.00 15.65 ? 228 PHE   A C   1 
ATOM   1592 O O   . PHE   A 1 209 ? 21.019 2.616   40.682 1.00 15.67 ? 228 PHE   A O   1 
ATOM   1593 C CB  . PHE   A 1 209 ? 23.357 2.638   38.600 1.00 15.24 ? 228 PHE   A CB  1 
ATOM   1594 C CG  . PHE   A 1 209 ? 24.257 3.062   37.471 1.00 15.43 ? 228 PHE   A CG  1 
ATOM   1595 C CD1 . PHE   A 1 209 ? 24.574 4.396   37.274 1.00 15.32 ? 228 PHE   A CD1 1 
ATOM   1596 C CD2 . PHE   A 1 209 ? 24.810 2.117   36.624 1.00 17.11 ? 228 PHE   A CD2 1 
ATOM   1597 C CE1 . PHE   A 1 209 ? 25.408 4.780   36.240 1.00 17.93 ? 228 PHE   A CE1 1 
ATOM   1598 C CE2 . PHE   A 1 209 ? 25.648 2.494   35.593 1.00 15.52 ? 228 PHE   A CE2 1 
ATOM   1599 C CZ  . PHE   A 1 209 ? 25.946 3.827   35.399 1.00 15.85 ? 228 PHE   A CZ  1 
ATOM   1600 N N   . THR   A 1 210 ? 20.203 1.679   38.801 1.00 13.70 ? 229 THR   A N   1 
ATOM   1601 C CA  . THR   A 1 210 ? 19.354 0.743   39.526 1.00 19.31 ? 229 THR   A CA  1 
ATOM   1602 C C   . THR   A 1 210 ? 20.207 -0.340  40.178 1.00 14.90 ? 229 THR   A C   1 
ATOM   1603 O O   . THR   A 1 210 ? 21.129 -0.876  39.561 1.00 16.52 ? 229 THR   A O   1 
ATOM   1604 C CB  . THR   A 1 210 ? 18.335 0.106   38.579 1.00 17.33 ? 229 THR   A CB  1 
ATOM   1605 O OG1 . THR   A 1 210 ? 17.581 1.131   37.921 1.00 19.92 ? 229 THR   A OG1 1 
ATOM   1606 C CG2 . THR   A 1 210 ? 17.381 -0.805  39.341 1.00 15.57 ? 229 THR   A CG2 1 
ATOM   1607 N N   . ARG   A 1 211 ? 19.900 -0.662  41.432 1.00 15.80 ? 230 ARG   A N   1 
ATOM   1608 C CA  . ARG   A 1 211 ? 20.587 -1.750  42.120 1.00 17.08 ? 230 ARG   A CA  1 
ATOM   1609 C C   . ARG   A 1 211 ? 19.999 -3.082  41.670 1.00 20.78 ? 230 ARG   A C   1 
ATOM   1610 O O   . ARG   A 1 211 ? 18.801 -3.326  41.843 1.00 21.98 ? 230 ARG   A O   1 
ATOM   1611 C CB  . ARG   A 1 211 ? 20.466 -1.598  43.635 1.00 22.96 ? 230 ARG   A CB  1 
ATOM   1612 C CG  . ARG   A 1 211 ? 21.240 -0.432  44.218 1.00 25.71 ? 230 ARG   A CG  1 
ATOM   1613 C CD  . ARG   A 1 211 ? 21.064 -0.364  45.728 1.00 30.99 ? 230 ARG   A CD  1 
ATOM   1614 N NE  . ARG   A 1 211 ? 21.813 0.741   46.316 1.00 34.38 ? 230 ARG   A NE  1 
ATOM   1615 C CZ  . ARG   A 1 211 ? 23.029 0.630   46.832 1.00 33.15 ? 230 ARG   A CZ  1 
ATOM   1616 N NH1 . ARG   A 1 211 ? 23.662 -0.532  46.866 1.00 30.92 ? 230 ARG   A NH1 1 
ATOM   1617 N NH2 . ARG   A 1 211 ? 23.626 1.711   47.322 1.00 33.83 ? 230 ARG   A NH2 1 
ATOM   1618 N N   . ILE   A 1 212 ? 20.841 -3.944  41.099 1.00 18.29 ? 231 ILE   A N   1 
ATOM   1619 C CA  . ILE   A 1 212 ? 20.363 -5.236  40.614 1.00 22.43 ? 231 ILE   A CA  1 
ATOM   1620 C C   . ILE   A 1 212 ? 20.120 -6.209  41.766 1.00 20.56 ? 231 ILE   A C   1 
ATOM   1621 O O   . ILE   A 1 212 ? 19.222 -7.056  41.686 1.00 20.45 ? 231 ILE   A O   1 
ATOM   1622 C CB  . ILE   A 1 212 ? 21.351 -5.810  39.582 1.00 24.53 ? 231 ILE   A CB  1 
ATOM   1623 C CG1 . ILE   A 1 212 ? 21.375 -4.934  38.327 1.00 22.00 ? 231 ILE   A CG1 1 
ATOM   1624 C CG2 . ILE   A 1 212 ? 20.994 -7.245  39.212 1.00 26.57 ? 231 ILE   A CG2 1 
ATOM   1625 C CD1 . ILE   A 1 212 ? 22.194 -5.512  37.194 1.00 23.94 ? 231 ILE   A CD1 1 
ATOM   1626 N N   . SER   A 1 213 ? 20.887 -6.092  42.855 1.00 26.81 ? 232 SER   A N   1 
ATOM   1627 C CA  . SER   A 1 213 ? 20.791 -7.051  43.954 1.00 28.19 ? 232 SER   A CA  1 
ATOM   1628 C C   . SER   A 1 213 ? 19.378 -7.140  44.519 1.00 24.89 ? 232 SER   A C   1 
ATOM   1629 O O   . SER   A 1 213 ? 18.946 -8.219  44.941 1.00 28.00 ? 232 SER   A O   1 
ATOM   1630 C CB  . SER   A 1 213 ? 21.776 -6.675  45.058 1.00 29.85 ? 232 SER   A CB  1 
ATOM   1631 O OG  . SER   A 1 213 ? 21.430 -5.432  45.643 1.00 28.43 ? 232 SER   A OG  1 
ATOM   1632 N N   . HIS   A 1 214 ? 18.645 -6.023  44.536 1.00 26.77 ? 233 HIS   A N   1 
ATOM   1633 C CA  . HIS   A 1 214 ? 17.282 -6.040  45.056 1.00 21.61 ? 233 HIS   A CA  1 
ATOM   1634 C C   . HIS   A 1 214 ? 16.361 -6.910  44.212 1.00 23.93 ? 233 HIS   A C   1 
ATOM   1635 O O   . HIS   A 1 214 ? 15.401 -7.487  44.738 1.00 29.78 ? 233 HIS   A O   1 
ATOM   1636 C CB  . HIS   A 1 214 ? 16.726 -4.619  45.134 1.00 24.31 ? 233 HIS   A CB  1 
ATOM   1637 C CG  . HIS   A 1 214 ? 17.311 -3.796  46.238 1.00 30.59 ? 233 HIS   A CG  1 
ATOM   1638 N ND1 . HIS   A 1 214 ? 17.823 -4.352  47.391 1.00 36.79 ? 233 HIS   A ND1 1 
ATOM   1639 C CD2 . HIS   A 1 214 ? 17.465 -2.457  46.365 1.00 31.61 ? 233 HIS   A CD2 1 
ATOM   1640 C CE1 . HIS   A 1 214 ? 18.267 -3.391  48.181 1.00 38.15 ? 233 HIS   A CE1 1 
ATOM   1641 N NE2 . HIS   A 1 214 ? 18.062 -2.232  47.581 1.00 36.40 ? 233 HIS   A NE2 1 
ATOM   1642 N N   . TYR   A 1 215 ? 16.624 -7.014  42.910 1.00 22.94 ? 234 TYR   A N   1 
ATOM   1643 C CA  . TYR   A 1 215 ? 15.707 -7.664  41.983 1.00 26.20 ? 234 TYR   A CA  1 
ATOM   1644 C C   . TYR   A 1 215 ? 16.207 -9.025  41.512 1.00 28.79 ? 234 TYR   A C   1 
ATOM   1645 O O   . TYR   A 1 215 ? 15.717 -9.541  40.503 1.00 24.48 ? 234 TYR   A O   1 
ATOM   1646 C CB  . TYR   A 1 215 ? 15.441 -6.749  40.788 1.00 24.03 ? 234 TYR   A CB  1 
ATOM   1647 C CG  . TYR   A 1 215 ? 15.079 -5.345  41.205 1.00 24.94 ? 234 TYR   A CG  1 
ATOM   1648 C CD1 . TYR   A 1 215 ? 16.030 -4.337  41.209 1.00 24.27 ? 234 TYR   A CD1 1 
ATOM   1649 C CD2 . TYR   A 1 215 ? 13.792 -5.034  41.619 1.00 24.61 ? 234 TYR   A CD2 1 
ATOM   1650 C CE1 . TYR   A 1 215 ? 15.709 -3.053  41.602 1.00 21.79 ? 234 TYR   A CE1 1 
ATOM   1651 C CE2 . TYR   A 1 215 ? 13.460 -3.753  42.013 1.00 26.05 ? 234 TYR   A CE2 1 
ATOM   1652 C CZ  . TYR   A 1 215 ? 14.423 -2.767  42.003 1.00 20.55 ? 234 TYR   A CZ  1 
ATOM   1653 O OH  . TYR   A 1 215 ? 14.103 -1.489  42.396 1.00 21.25 ? 234 TYR   A OH  1 
ATOM   1654 N N   . ARG   A 1 216 ? 17.169 -9.618  42.221 1.00 27.26 ? 235 ARG   A N   1 
ATOM   1655 C CA  . ARG   A 1 216 ? 17.652 -10.944 41.837 1.00 35.07 ? 235 ARG   A CA  1 
ATOM   1656 C C   . ARG   A 1 216 ? 16.556 -12.002 41.842 1.00 35.20 ? 235 ARG   A C   1 
ATOM   1657 O O   . ARG   A 1 216 ? 16.464 -12.759 40.860 1.00 34.51 ? 235 ARG   A O   1 
ATOM   1658 C CB  . ARG   A 1 216 ? 18.824 -11.354 42.735 1.00 42.52 ? 235 ARG   A CB  1 
ATOM   1659 C CG  . ARG   A 1 216 ? 20.182 -11.174 42.091 1.00 45.43 ? 235 ARG   A CG  1 
ATOM   1660 C CD  . ARG   A 1 216 ? 20.227 -11.803 40.703 1.00 47.49 ? 235 ARG   A CD  1 
ATOM   1661 N NE  . ARG   A 1 216 ? 19.833 -13.208 40.710 1.00 51.96 ? 235 ARG   A NE  1 
ATOM   1662 C CZ  . ARG   A 1 216 ? 20.679 -14.224 40.816 1.00 53.16 ? 235 ARG   A CZ  1 
ATOM   1663 N NH1 . ARG   A 1 216 ? 21.982 -14.028 40.933 1.00 53.47 ? 235 ARG   A NH1 1 
ATOM   1664 N NH2 . ARG   A 1 216 ? 20.206 -15.467 40.804 1.00 52.68 ? 235 ARG   A NH2 1 
ATOM   1665 N N   . PRO   A 1 217 ? 15.718 -12.136 42.881 1.00 38.30 ? 236 PRO   A N   1 
ATOM   1666 C CA  . PRO   A 1 217 ? 14.628 -13.124 42.785 1.00 35.29 ? 236 PRO   A CA  1 
ATOM   1667 C C   . PRO   A 1 217 ? 13.670 -12.843 41.641 1.00 32.50 ? 236 PRO   A C   1 
ATOM   1668 O O   . PRO   A 1 217 ? 13.153 -13.781 41.023 1.00 36.48 ? 236 PRO   A O   1 
ATOM   1669 C CB  . PRO   A 1 217 ? 13.936 -13.015 44.153 1.00 37.46 ? 236 PRO   A CB  1 
ATOM   1670 C CG  . PRO   A 1 217 ? 14.970 -12.450 45.058 1.00 34.89 ? 236 PRO   A CG  1 
ATOM   1671 C CD  . PRO   A 1 217 ? 15.742 -11.492 44.208 1.00 37.66 ? 236 PRO   A CD  1 
ATOM   1672 N N   . TRP   A 1 218 ? 13.421 -11.566 41.340 1.00 32.41 ? 237 TRP   A N   1 
ATOM   1673 C CA  . TRP   A 1 218 ? 12.554 -11.227 40.217 1.00 31.50 ? 237 TRP   A CA  1 
ATOM   1674 C C   . TRP   A 1 218 ? 13.209 -11.579 38.887 1.00 32.31 ? 237 TRP   A C   1 
ATOM   1675 O O   . TRP   A 1 218 ? 12.543 -12.081 37.975 1.00 33.06 ? 237 TRP   A O   1 
ATOM   1676 C CB  . TRP   A 1 218 ? 12.192 -9.743  40.270 1.00 26.87 ? 237 TRP   A CB  1 
ATOM   1677 C CG  . TRP   A 1 218 ? 11.230 -9.318  39.207 1.00 26.39 ? 237 TRP   A CG  1 
ATOM   1678 C CD1 . TRP   A 1 218 ? 9.876  -9.479  39.215 1.00 27.91 ? 237 TRP   A CD1 1 
ATOM   1679 C CD2 . TRP   A 1 218 ? 11.548 -8.651  37.980 1.00 25.55 ? 237 TRP   A CD2 1 
ATOM   1680 N NE1 . TRP   A 1 218 ? 9.330  -8.958  38.066 1.00 25.14 ? 237 TRP   A NE1 1 
ATOM   1681 C CE2 . TRP   A 1 218 ? 10.336 -8.443  37.291 1.00 27.15 ? 237 TRP   A CE2 1 
ATOM   1682 C CE3 . TRP   A 1 218 ? 12.740 -8.212  37.396 1.00 23.18 ? 237 TRP   A CE3 1 
ATOM   1683 C CZ2 . TRP   A 1 218 ? 10.282 -7.815  36.049 1.00 22.90 ? 237 TRP   A CZ2 1 
ATOM   1684 C CZ3 . TRP   A 1 218 ? 12.685 -7.589  36.163 1.00 23.13 ? 237 TRP   A CZ3 1 
ATOM   1685 C CH2 . TRP   A 1 218 ? 11.464 -7.396  35.503 1.00 23.02 ? 237 TRP   A CH2 1 
ATOM   1686 N N   . ILE   A 1 219 ? 14.513 -11.318 38.757 1.00 32.65 ? 238 ILE   A N   1 
ATOM   1687 C CA  . ILE   A 1 219 ? 15.237 -11.713 37.552 1.00 34.49 ? 238 ILE   A CA  1 
ATOM   1688 C C   . ILE   A 1 219 ? 15.324 -13.232 37.452 1.00 34.31 ? 238 ILE   A C   1 
ATOM   1689 O O   . ILE   A 1 219 ? 15.415 -13.786 36.349 1.00 31.83 ? 238 ILE   A O   1 
ATOM   1690 C CB  . ILE   A 1 219 ? 16.630 -11.053 37.535 1.00 31.82 ? 238 ILE   A CB  1 
ATOM   1691 C CG1 . ILE   A 1 219 ? 16.494 -9.531  37.487 1.00 28.87 ? 238 ILE   A CG1 1 
ATOM   1692 C CG2 . ILE   A 1 219 ? 17.453 -11.527 36.346 1.00 31.03 ? 238 ILE   A CG2 1 
ATOM   1693 C CD1 . ILE   A 1 219 ? 17.801 -8.803  37.685 1.00 28.50 ? 238 ILE   A CD1 1 
ATOM   1694 N N   . ASN   A 1 220 ? 15.250 -13.931 38.587 1.00 35.71 ? 239 ASN   A N   1 
ATOM   1695 C CA  . ASN   A 1 220 ? 15.343 -15.386 38.590 1.00 34.93 ? 239 ASN   A CA  1 
ATOM   1696 C C   . ASN   A 1 220 ? 14.188 -16.050 37.852 1.00 35.56 ? 239 ASN   A C   1 
ATOM   1697 O O   . ASN   A 1 220 ? 14.264 -17.254 37.582 1.00 37.77 ? 239 ASN   A O   1 
ATOM   1698 C CB  . ASN   A 1 220 ? 15.406 -15.906 40.027 1.00 39.99 ? 239 ASN   A CB  1 
ATOM   1699 C CG  . ASN   A 1 220 ? 16.784 -16.415 40.403 1.00 43.40 ? 239 ASN   A CG  1 
ATOM   1700 O OD1 . ASN   A 1 220 ? 17.740 -16.269 39.643 1.00 46.40 ? 239 ASN   A OD1 1 
ATOM   1701 N ND2 . ASN   A 1 220 ? 16.892 -17.015 41.583 1.00 46.20 ? 239 ASN   A ND2 1 
ATOM   1702 N N   . GLN   A 1 221 ? 13.123 -15.306 37.535 1.00 34.83 ? 240 GLN   A N   1 
ATOM   1703 C CA  . GLN   A 1 221 ? 12.055 -15.848 36.700 1.00 37.72 ? 240 GLN   A CA  1 
ATOM   1704 C C   . GLN   A 1 221 ? 12.604 -16.353 35.373 1.00 37.86 ? 240 GLN   A C   1 
ATOM   1705 O O   . GLN   A 1 221 ? 12.239 -17.438 34.906 1.00 37.66 ? 240 GLN   A O   1 
ATOM   1706 C CB  . GLN   A 1 221 ? 10.983 -14.783 36.450 1.00 37.76 ? 240 GLN   A CB  1 
ATOM   1707 C CG  . GLN   A 1 221 ? 10.240 -14.316 37.683 1.00 38.17 ? 240 GLN   A CG  1 
ATOM   1708 C CD  . GLN   A 1 221 ? 9.164  -13.299 37.355 1.00 41.86 ? 240 GLN   A CD  1 
ATOM   1709 O OE1 . GLN   A 1 221 ? 8.029  -13.658 37.040 1.00 37.69 ? 240 GLN   A OE1 1 
ATOM   1710 N NE2 . GLN   A 1 221 ? 9.517  -12.021 37.423 1.00 33.44 ? 240 GLN   A NE2 1 
ATOM   1711 N N   . ILE   A 1 222 ? 13.486 -15.568 34.747 1.00 40.37 ? 241 ILE   A N   1 
ATOM   1712 C CA  . ILE   A 1 222 ? 14.044 -15.962 33.458 1.00 43.32 ? 241 ILE   A CA  1 
ATOM   1713 C C   . ILE   A 1 222 ? 15.075 -17.074 33.602 1.00 44.58 ? 241 ILE   A C   1 
ATOM   1714 O O   . ILE   A 1 222 ? 15.152 -17.959 32.744 1.00 49.87 ? 241 ILE   A O   1 
ATOM   1715 C CB  . ILE   A 1 222 ? 14.664 -14.746 32.762 1.00 39.29 ? 241 ILE   A CB  1 
ATOM   1716 N N   . LEU   A 1 223 ? 15.865 -17.051 34.671 1.00 47.55 ? 242 LEU   A N   1 
ATOM   1717 C CA  . LEU   A 1 223 ? 16.924 -18.037 34.865 1.00 44.01 ? 242 LEU   A CA  1 
ATOM   1718 C C   . LEU   A 1 223 ? 16.363 -19.380 35.324 1.00 48.90 ? 242 LEU   A C   1 
ATOM   1719 O O   . LEU   A 1 223 ? 15.323 -19.449 35.980 1.00 43.42 ? 242 LEU   A O   1 
ATOM   1720 C CB  . LEU   A 1 223 ? 17.946 -17.521 35.865 1.00 44.43 ? 242 LEU   A CB  1 
HETATM 1721 C C14 . A1AO9 B 2 .   ? 19.310 8.972   30.428 1.00 17.96 ? 301 A1AO9 A C14 1 
HETATM 1722 C C17 . A1AO9 B 2 .   ? 15.563 10.780  32.613 1.00 20.32 ? 301 A1AO9 A C17 1 
HETATM 1723 C C21 . A1AO9 B 2 .   ? 15.808 8.399   31.184 1.00 21.11 ? 301 A1AO9 A C21 1 
HETATM 1724 C C10 . A1AO9 B 2 .   ? 23.877 10.156  32.900 1.00 17.11 ? 301 A1AO9 A C10 1 
HETATM 1725 C C11 . A1AO9 B 2 .   ? 23.326 8.945   32.559 1.00 17.72 ? 301 A1AO9 A C11 1 
HETATM 1726 C C12 . A1AO9 B 2 .   ? 22.119 8.811   31.912 1.00 16.63 ? 301 A1AO9 A C12 1 
HETATM 1727 C C16 . A1AO9 B 2 .   ? 16.665 11.495  32.115 1.00 18.87 ? 301 A1AO9 A C16 1 
HETATM 1728 C C22 . A1AO9 B 2 .   ? 15.146 10.926  33.928 1.00 20.07 ? 301 A1AO9 A C22 1 
HETATM 1729 C C23 . A1AO9 B 2 .   ? 15.821 11.794  34.779 1.00 19.55 ? 301 A1AO9 A C23 1 
HETATM 1730 C C24 . A1AO9 B 2 .   ? 15.380 11.953  36.190 1.00 22.10 ? 301 A1AO9 A C24 1 
HETATM 1731 C C27 . A1AO9 B 2 .   ? 14.032 11.097  37.921 1.00 24.35 ? 301 A1AO9 A C27 1 
HETATM 1732 C C28 . A1AO9 B 2 .   ? 16.915 12.505  34.296 1.00 19.07 ? 301 A1AO9 A C28 1 
HETATM 1733 C C29 . A1AO9 B 2 .   ? 17.332 12.359  32.983 1.00 18.21 ? 301 A1AO9 A C29 1 
HETATM 1734 C C4  . A1AO9 B 2 .   ? 19.782 11.437  30.777 1.00 17.21 ? 301 A1AO9 A C4  1 
HETATM 1735 C C5  . A1AO9 B 2 .   ? 20.141 10.123  30.915 1.00 16.08 ? 301 A1AO9 A C5  1 
HETATM 1736 C C6  . A1AO9 B 2 .   ? 21.412 9.967   31.583 1.00 14.92 ? 301 A1AO9 A C6  1 
HETATM 1737 C C7  . A1AO9 B 2 .   ? 21.959 11.216  31.924 1.00 15.87 ? 301 A1AO9 A C7  1 
HETATM 1738 C C9  . A1AO9 B 2 .   ? 23.184 11.310  32.578 1.00 15.54 ? 301 A1AO9 A C9  1 
HETATM 1739 F F13 . A1AO9 B 2 .   ? 24.008 7.813   32.875 1.00 17.78 ? 301 A1AO9 A F13 1 
HETATM 1740 N N15 . A1AO9 B 2 .   ? 17.081 11.335  30.762 1.00 20.23 ? 301 A1AO9 A N15 1 
HETATM 1741 O O19 . A1AO9 B 2 .   ? 14.293 10.343  30.377 1.00 28.51 ? 301 A1AO9 A O19 1 
HETATM 1742 O O2  . A1AO9 B 2 .   ? 18.328 11.669  28.668 1.00 21.42 ? 301 A1AO9 A O2  1 
HETATM 1743 O O20 . A1AO9 B 2 .   ? 13.602 9.074   32.370 1.00 25.12 ? 301 A1AO9 A O20 1 
HETATM 1744 O O25 . A1AO9 B 2 .   ? 15.766 12.824  36.929 1.00 17.94 ? 301 A1AO9 A O25 1 
HETATM 1745 O O26 . A1AO9 B 2 .   ? 14.505 11.018  36.555 1.00 23.64 ? 301 A1AO9 A O26 1 
HETATM 1746 O O3  . A1AO9 B 2 .   ? 18.258 13.472  30.360 1.00 21.67 ? 301 A1AO9 A O3  1 
HETATM 1747 S S1  . A1AO9 B 2 .   ? 18.332 12.085  30.035 1.00 21.64 ? 301 A1AO9 A S1  1 
HETATM 1748 S S18 . A1AO9 B 2 .   ? 14.654 9.657   31.585 1.00 24.09 ? 301 A1AO9 A S18 1 
HETATM 1749 S S8  . A1AO9 B 2 .   ? 20.935 12.531  31.434 1.00 17.13 ? 301 A1AO9 A S8  1 
HETATM 1750 O O   . HOH   C 3 .   ? 32.454 19.574  20.241 1.00 33.76 ? 401 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 6.114  -12.385 37.509 1.00 23.96 ? 402 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 9.385  6.129   32.186 1.00 19.17 ? 403 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 11.029 12.573  45.744 1.00 31.89 ? 404 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? 26.672 11.874  34.129 1.00 27.11 ? 405 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 22.740 -15.476 32.538 1.00 31.03 ? 406 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 26.225 -10.960 36.393 1.00 39.73 ? 407 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 5.947  7.992   16.369 1.00 43.33 ? 408 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 38.783 -2.058  19.396 1.00 30.67 ? 409 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 26.540 -8.695  21.834 1.00 16.38 ? 410 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 30.046 -8.818  20.474 1.00 24.53 ? 411 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 22.889 -21.745 18.405 1.00 37.15 ? 412 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 25.174 14.358  38.965 1.00 22.54 ? 413 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 33.844 7.683   25.579 1.00 25.39 ? 414 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 32.390 -5.013  20.889 1.00 24.52 ? 415 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 18.941 -2.508  17.735 1.00 13.63 ? 416 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 23.650 -4.619  42.901 1.00 22.42 ? 417 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 8.876  -4.933  19.221 1.00 29.48 ? 418 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 33.382 10.379  37.146 1.00 18.17 ? 419 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 16.092 15.918  40.763 1.00 38.06 ? 420 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 28.052 7.879   35.595 1.00 20.72 ? 421 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 15.078 8.216   41.509 1.00 19.49 ? 422 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 30.500 14.347  31.556 1.00 27.14 ? 423 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 32.616 8.564   47.958 1.00 25.28 ? 424 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 45.453 -8.216  26.651 1.00 50.24 ? 425 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 19.461 6.617   27.010 1.00 25.25 ? 426 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 16.775 4.079   38.968 1.00 20.80 ? 427 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 25.011 -10.085 10.693 1.00 26.04 ? 428 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 15.554 12.384  40.965 1.00 28.08 ? 429 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 24.110 4.814   46.523 1.00 30.16 ? 430 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 20.951 -11.057 46.553 1.00 48.56 ? 431 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? 24.899 12.896  35.674 1.00 15.09 ? 432 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 28.738 -6.836  21.411 1.00 23.54 ? 433 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 35.195 13.574  28.547 1.00 24.17 ? 434 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 16.257 -19.454 26.855 1.00 40.53 ? 435 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? 29.690 5.148   23.981 1.00 18.95 ? 436 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 24.371 1.608   24.730 1.00 12.87 ? 437 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 23.299 15.696  24.845 1.00 17.87 ? 438 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 4.540  -5.055  34.533 1.00 33.22 ? 439 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 17.966 -22.498 25.730 1.00 40.38 ? 440 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 31.410 -6.723  22.702 1.00 17.32 ? 441 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 24.725 0.817   27.428 1.00 12.93 ? 442 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? 26.382 4.379   45.613 1.00 22.89 ? 443 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 23.559 -3.342  45.557 1.00 31.16 ? 444 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 11.962 -17.142 21.288 1.00 38.26 ? 445 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 28.915 -3.255  5.888  1.00 34.44 ? 446 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 17.074 16.912  46.145 1.00 40.49 ? 447 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? 34.531 8.054   38.409 1.00 25.23 ? 448 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 15.559 1.207   41.745 1.00 24.07 ? 449 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? 30.606 10.497  19.019 1.00 29.15 ? 450 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 26.622 2.295   47.050 1.00 37.84 ? 451 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 18.287 17.154  34.069 1.00 30.92 ? 452 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? 37.543 12.568  32.906 1.00 30.74 ? 453 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 38.353 4.306   32.048 1.00 21.61 ? 454 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 31.869 -8.098  8.773  1.00 30.27 ? 455 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? 23.224 5.731   21.119 1.00 25.87 ? 456 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 17.597 8.265   23.318 1.00 28.70 ? 457 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? 21.073 19.383  34.194 1.00 38.30 ? 458 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 5.582  4.723   23.154 1.00 37.56 ? 459 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? 1.788  9.821   19.235 1.00 37.84 ? 460 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 37.118 8.625   39.258 1.00 33.22 ? 461 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? 20.431 -19.643 27.592 1.00 39.47 ? 462 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 18.177 16.185  36.196 1.00 27.80 ? 463 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 17.775 -22.279 36.127 1.00 31.48 ? 464 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 28.868 -15.022 14.049 1.00 31.81 ? 465 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ILE A 1   ? 0.2506 0.1810 0.1296 -0.0168 0.0143  0.0628  16  ILE A N   
2    C CA  . ILE A 1   ? 0.2808 0.2118 0.1722 -0.0140 0.0152  0.0516  16  ILE A CA  
3    C C   . ILE A 1   ? 0.2906 0.2222 0.1928 -0.0172 0.0220  0.0513  16  ILE A C   
4    O O   . ILE A 1   ? 0.2981 0.2334 0.1969 -0.0235 0.0292  0.0521  16  ILE A O   
5    C CB  . ILE A 1   ? 0.2699 0.2059 0.1616 -0.0140 0.0147  0.0408  16  ILE A CB  
6    C CG1 . ILE A 1   ? 0.2628 0.1973 0.1448 -0.0108 0.0074  0.0414  16  ILE A CG1 
7    C CG2 . ILE A 1   ? 0.2888 0.2243 0.1982 -0.0114 0.0128  0.0299  16  ILE A CG2 
8    C CD1 . ILE A 1   ? 0.2938 0.2203 0.1771 -0.0058 0.0003  0.0413  16  ILE A CD1 
9    N N   . ILE A 2   ? 0.2924 0.2196 0.2065 -0.0139 0.0203  0.0497  17  ILE A N   
10   C CA  . ILE A 2   ? 0.3248 0.2520 0.2519 -0.0162 0.0259  0.0497  17  ILE A CA  
11   C C   . ILE A 2   ? 0.3125 0.2408 0.2548 -0.0144 0.0250  0.0370  17  ILE A C   
12   O O   . ILE A 2   ? 0.3174 0.2410 0.2610 -0.0101 0.0166  0.0312  17  ILE A O   
13   C CB  . ILE A 2   ? 0.3118 0.2327 0.2446 -0.0144 0.0247  0.0565  17  ILE A CB  
14   C CG1 . ILE A 2   ? 0.3056 0.2251 0.2302 -0.0158 0.0234  0.0689  17  ILE A CG1 
15   C CG2 . ILE A 2   ? 0.3406 0.2615 0.2885 -0.0167 0.0301  0.0564  17  ILE A CG2 
16   C CD1 . ILE A 2   ? 0.2573 0.1712 0.1940 -0.0141 0.0228  0.0743  17  ILE A CD1 
17   N N   . GLY A 3   ? 0.2991 0.2323 0.2530 -0.0186 0.0329  0.0327  18  GLY A N   
18   C CA  . GLY A 3   ? 0.2890 0.2237 0.2645 -0.0171 0.0316  0.0203  18  GLY A CA  
19   C C   . GLY A 3   ? 0.3135 0.2515 0.2951 -0.0153 0.0269  0.0095  18  GLY A C   
20   O O   . GLY A 3   ? 0.3362 0.2727 0.3375 -0.0125 0.0200  -0.0002 18  GLY A O   
21   N N   . GLY A 4   ? 0.2909 0.2328 0.2581 -0.0171 0.0292  0.0109  19  GLY A N   
22   C CA  . GLY A 4   ? 0.2917 0.2371 0.2667 -0.0156 0.0250  0.0005  19  GLY A CA  
23   C C   . GLY A 4   ? 0.3372 0.2919 0.3253 -0.0218 0.0382  -0.0096 19  GLY A C   
24   O O   . GLY A 4   ? 0.3823 0.3397 0.3724 -0.0281 0.0510  -0.0088 19  GLY A O   
25   N N   . THR A 5   ? 0.3237 0.2825 0.3216 -0.0208 0.0357  -0.0199 20  THR A N   
26   C CA  . THR A 5   ? 0.3402 0.3078 0.3524 -0.0274 0.0496  -0.0327 20  THR A CA  
27   C C   . THR A 5   ? 0.3126 0.2831 0.3056 -0.0297 0.0515  -0.0331 20  THR A C   
28   O O   . THR A 5   ? 0.3048 0.2712 0.2835 -0.0242 0.0390  -0.0263 20  THR A O   
29   C CB  . THR A 5   ? 0.3319 0.3029 0.3865 -0.0244 0.0456  -0.0494 20  THR A CB  
30   O OG1 . THR A 5   ? 0.4613 0.4291 0.5218 -0.0175 0.0285  -0.0519 20  THR A OG1 
31   C CG2 . THR A 5   ? 0.3966 0.3635 0.4707 -0.0215 0.0404  -0.0490 20  THR A CG2 
32   N N   . GLU A 6   ? 0.3517 0.3286 0.3438 -0.0389 0.0682  -0.0418 21  GLU A N   
33   C CA  . GLU A 6   ? 0.3761 0.3558 0.3511 -0.0425 0.0711  -0.0446 21  GLU A CA  
34   C C   . GLU A 6   ? 0.3419 0.3243 0.3417 -0.0349 0.0596  -0.0557 21  GLU A C   
35   O O   . GLU A 6   ? 0.3205 0.3065 0.3585 -0.0326 0.0587  -0.0696 21  GLU A O   
36   C CB  . GLU A 6   ? 0.4238 0.4085 0.3935 -0.0559 0.0932  -0.0549 21  GLU A CB  
37   C CG  . GLU A 6   ? 0.4811 0.4607 0.4050 -0.0656 0.0994  -0.0419 21  GLU A CG  
38   C CD  . GLU A 6   ? 0.5508 0.5338 0.4619 -0.0779 0.1155  -0.0544 21  GLU A CD  
39   O OE1 . GLU A 6   ? 0.5540 0.5436 0.4866 -0.0750 0.1155  -0.0697 21  GLU A OE1 
40   O OE2 . GLU A 6   ? 0.6090 0.5870 0.4881 -0.0914 0.1279  -0.0490 21  GLU A OE2 
41   N N   . SER A 7   ? 0.3208 0.3007 0.3013 -0.0313 0.0495  -0.0491 22  SER A N   
42   C CA  . SER A 7   ? 0.3451 0.3266 0.3464 -0.0255 0.0388  -0.0586 22  SER A CA  
43   C C   . SER A 7   ? 0.3443 0.3351 0.3625 -0.0324 0.0531  -0.0770 22  SER A C   
44   O O   . SER A 7   ? 0.4158 0.4099 0.4157 -0.0428 0.0710  -0.0797 22  SER A O   
45   C CB  . SER A 7   ? 0.3540 0.3302 0.3295 -0.0208 0.0259  -0.0467 22  SER A CB  
46   O OG  . SER A 7   ? 0.3914 0.3590 0.3509 -0.0160 0.0161  -0.0313 22  SER A OG  
47   N N   . LYS A 8   ? 0.3505 0.3441 0.4041 -0.0276 0.0451  -0.0902 23  LYS A N   
48   C CA  . LYS A 8   ? 0.3391 0.3414 0.4106 -0.0333 0.0575  -0.1087 23  LYS A CA  
49   C C   . LYS A 8   ? 0.3759 0.3776 0.4097 -0.0365 0.0589  -0.1022 23  LYS A C   
50   O O   . LYS A 8   ? 0.3790 0.3746 0.3954 -0.0294 0.0423  -0.0888 23  LYS A O   
51   C CB  . LYS A 8   ? 0.4333 0.4374 0.5542 -0.0263 0.0444  -0.1224 23  LYS A CB  
52   C CG  . LYS A 8   ? 0.5405 0.5433 0.7016 -0.0224 0.0380  -0.1279 23  LYS A CG  
53   C CD  . LYS A 8   ? 0.5227 0.5263 0.7368 -0.0165 0.0232  -0.1420 23  LYS A CD  
54   C CE  . LYS A 8   ? 0.6154 0.6163 0.8710 -0.0129 0.0138  -0.1469 23  LYS A CE  
55   N NZ  . LYS A 8   ? 0.6704 0.6713 0.9836 -0.0080 -0.0023 -0.1612 23  LYS A NZ  
56   N N   . PRO A 9   ? 0.4018 0.4085 0.4205 -0.0480 0.0784  -0.1114 24  PRO A N   
57   C CA  . PRO A 9   ? 0.3888 0.3933 0.3680 -0.0519 0.0781  -0.1039 24  PRO A CA  
58   C C   . PRO A 9   ? 0.3781 0.3836 0.3718 -0.0437 0.0632  -0.1073 24  PRO A C   
59   O O   . PRO A 9   ? 0.3413 0.3526 0.3749 -0.0416 0.0635  -0.1248 24  PRO A O   
60   C CB  . PRO A 9   ? 0.3887 0.3976 0.3558 -0.0676 0.1028  -0.1184 24  PRO A CB  
61   C CG  . PRO A 9   ? 0.4091 0.4253 0.4233 -0.0698 0.1159  -0.1392 24  PRO A CG  
62   C CD  . PRO A 9   ? 0.3495 0.3628 0.3856 -0.0593 0.1022  -0.1297 24  PRO A CD  
63   N N   . HIS A 10  ? 0.3652 0.3647 0.3292 -0.0390 0.0497  -0.0904 25  HIS A N   
64   C CA  . HIS A 10  ? 0.3683 0.3669 0.3392 -0.0318 0.0349  -0.0900 25  HIS A CA  
65   C C   . HIS A 10  ? 0.3245 0.3202 0.3316 -0.0213 0.0183  -0.0916 25  HIS A C   
66   O O   . HIS A 10  ? 0.3511 0.3463 0.3750 -0.0165 0.0073  -0.0961 25  HIS A O   
67   C CB  . HIS A 10  ? 0.3874 0.3929 0.3639 -0.0384 0.0451  -0.1072 25  HIS A CB  
68   C CG  . HIS A 10  ? 0.3906 0.3969 0.3308 -0.0519 0.0627  -0.1085 25  HIS A CG  
69   N ND1 . HIS A 10  ? 0.3899 0.3896 0.2858 -0.0547 0.0581  -0.0906 25  HIS A ND1 
70   C CD2 . HIS A 10  ? 0.3967 0.4079 0.3374 -0.0646 0.0845  -0.1254 25  HIS A CD2 
71   C CE1 . HIS A 10  ? 0.4364 0.4354 0.3041 -0.0688 0.0740  -0.0949 25  HIS A CE1 
72   N NE2 . HIS A 10  ? 0.5164 0.5221 0.4080 -0.0757 0.0915  -0.1163 25  HIS A NE2 
73   N N   . SER A 11  ? 0.3163 0.3084 0.3348 -0.0183 0.0150  -0.0875 26  SER A N   
74   C CA  . SER A 11  ? 0.3532 0.3383 0.3970 -0.0096 -0.0043 -0.0852 26  SER A CA  
75   C C   . SER A 11  ? 0.3425 0.3163 0.3574 -0.0041 -0.0196 -0.0658 26  SER A C   
76   O O   . SER A 11  ? 0.3625 0.3270 0.3892 0.0014  -0.0368 -0.0619 26  SER A O   
77   C CB  . SER A 11  ? 0.3425 0.3274 0.4107 -0.0094 -0.0026 -0.0896 26  SER A CB  
78   O OG  . SER A 11  ? 0.3294 0.3109 0.3685 -0.0113 0.0032  -0.0765 26  SER A OG  
79   N N   . ARG A 12  ? 0.3510 0.3241 0.3292 -0.0066 -0.0139 -0.0539 27  ARG A N   
80   C CA  . ARG A 12  ? 0.3244 0.2880 0.2777 -0.0025 -0.0250 -0.0376 27  ARG A CA  
81   C C   . ARG A 12  ? 0.2984 0.2652 0.2310 -0.0046 -0.0221 -0.0345 27  ARG A C   
82   O O   . ARG A 12  ? 0.2679 0.2340 0.1743 -0.0072 -0.0174 -0.0240 27  ARG A O   
83   C CB  . ARG A 12  ? 0.3048 0.2634 0.2396 -0.0028 -0.0223 -0.0253 27  ARG A CB  
84   C CG  . ARG A 12  ? 0.3252 0.2820 0.2794 -0.0021 -0.0228 -0.0294 27  ARG A CG  
85   C CD  . ARG A 12  ? 0.3678 0.3131 0.3323 0.0031  -0.0403 -0.0272 27  ARG A CD  
86   N NE  . ARG A 12  ? 0.5120 0.4537 0.4919 0.0036  -0.0429 -0.0295 27  ARG A NE  
87   C CZ  . ARG A 12  ? 0.5034 0.4463 0.5174 0.0045  -0.0485 -0.0411 27  ARG A CZ  
88   N NH1 . ARG A 12  ? 0.4677 0.4156 0.5065 0.0051  -0.0517 -0.0524 27  ARG A NH1 
89   N NH2 . ARG A 12  ? 0.5659 0.5048 0.5928 0.0049  -0.0517 -0.0422 27  ARG A NH2 
90   N N   . PRO A 13  ? 0.3003 0.2701 0.2465 -0.0037 -0.0260 -0.0435 28  PRO A N   
91   C CA  . PRO A 13  ? 0.2976 0.2715 0.2264 -0.0068 -0.0222 -0.0433 28  PRO A CA  
92   C C   . PRO A 13  ? 0.2982 0.2650 0.2037 -0.0037 -0.0306 -0.0276 28  PRO A C   
93   O O   . PRO A 13  ? 0.2656 0.2350 0.1547 -0.0065 -0.0284 -0.0252 28  PRO A O   
94   C CB  . PRO A 13  ? 0.3080 0.2860 0.2643 -0.0055 -0.0260 -0.0581 28  PRO A CB  
95   C CG  . PRO A 13  ? 0.3126 0.2833 0.2936 0.0007  -0.0400 -0.0577 28  PRO A CG  
96   C CD  . PRO A 13  ? 0.2958 0.2640 0.2755 0.0003  -0.0365 -0.0536 28  PRO A CD  
97   N N   . TYR A 14  ? 0.2857 0.2430 0.1898 0.0010  -0.0398 -0.0178 29  TYR A N   
98   C CA  . TYR A 14  ? 0.2924 0.2426 0.1778 0.0030  -0.0451 -0.0046 29  TYR A CA  
99   C C   . TYR A 14  ? 0.2852 0.2348 0.1520 0.0009  -0.0386 0.0060  29  TYR A C   
100  O O   . TYR A 14  ? 0.2598 0.2056 0.1149 0.0017  -0.0409 0.0155  29  TYR A O   
101  C CB  . TYR A 14  ? 0.3100 0.2479 0.1994 0.0067  -0.0561 0.0000  29  TYR A CB  
102  C CG  . TYR A 14  ? 0.3201 0.2540 0.2206 0.0072  -0.0583 -0.0029 29  TYR A CG  
103  C CD1 . TYR A 14  ? 0.2786 0.2093 0.1687 0.0064  -0.0535 0.0038  29  TYR A CD1 
104  C CD2 . TYR A 14  ? 0.3382 0.2714 0.2632 0.0085  -0.0660 -0.0127 29  TYR A CD2 
105  C CE1 . TYR A 14  ? 0.3568 0.2836 0.2578 0.0067  -0.0561 0.0007  29  TYR A CE1 
106  C CE2 . TYR A 14  ? 0.3277 0.2567 0.2659 0.0089  -0.0699 -0.0155 29  TYR A CE2 
107  C CZ  . TYR A 14  ? 0.3229 0.2487 0.2477 0.0079  -0.0648 -0.0088 29  TYR A CZ  
108  O OH  . TYR A 14  ? 0.3532 0.2745 0.2917 0.0082  -0.0693 -0.0119 29  TYR A OH  
109  N N   . MET A 15  ? 0.3191 0.1580 0.1489 0.0195  0.0581  -0.0126 30  MET A N   
110  C CA  . MET A 15  ? 0.3405 0.1766 0.1603 0.0210  0.0537  -0.0091 30  MET A CA  
111  C C   . MET A 15  ? 0.3222 0.1748 0.1451 0.0239  0.0511  -0.0160 30  MET A C   
112  O O   . MET A 15  ? 0.3174 0.1861 0.1442 0.0252  0.0533  -0.0209 30  MET A O   
113  C CB  . MET A 15  ? 0.2843 0.1161 0.0923 0.0218  0.0537  0.0012  30  MET A CB  
114  C CG  . MET A 15  ? 0.3290 0.1480 0.1379 0.0183  0.0533  0.0088  30  MET A CG  
115  S SD  . MET A 15  ? 0.3307 0.1355 0.1382 0.0153  0.0500  0.0067  30  MET A SD  
116  C CE  . MET A 15  ? 0.3261 0.1306 0.1255 0.0187  0.0445  0.0089  30  MET A CE  
117  N N   . ALA A 16  ? 0.2731 0.1227 0.0945 0.0245  0.0467  -0.0175 31  ALA A N   
118  C CA  . ALA A 16  ? 0.2823 0.1454 0.1054 0.0273  0.0439  -0.0238 31  ALA A CA  
119  C C   . ALA A 16  ? 0.3013 0.1539 0.1072 0.0311  0.0400  -0.0181 31  ALA A C   
120  O O   . ALA A 16  ? 0.2912 0.1263 0.0912 0.0307  0.0379  -0.0139 31  ALA A O   
121  C CB  . ALA A 16  ? 0.2659 0.1379 0.1059 0.0250  0.0417  -0.0326 31  ALA A CB  
122  N N   . TYR A 17  ? 0.3264 0.1908 0.1240 0.0344  0.0384  -0.0177 32  TYR A N   
123  C CA  . TYR A 17  ? 0.3074 0.1657 0.0904 0.0380  0.0320  -0.0095 32  TYR A CA  
124  C C   . TYR A 17  ? 0.3145 0.1786 0.0990 0.0417  0.0285  -0.0191 32  TYR A C   
125  O O   . TYR A 17  ? 0.3477 0.2315 0.1378 0.0416  0.0307  -0.0266 32  TYR A O   
126  C CB  . TYR A 17  ? 0.3149 0.1880 0.0914 0.0369  0.0303  0.0029  32  TYR A CB  
127  C CG  . TYR A 17  ? 0.3673 0.2400 0.1432 0.0375  0.0200  0.0171  32  TYR A CG  
128  C CD1 . TYR A 17  ? 0.3973 0.2540 0.1774 0.0359  0.0152  0.0287  32  TYR A CD1 
129  C CD2 . TYR A 17  ? 0.3677 0.2566 0.1405 0.0394  0.0146  0.0194  32  TYR A CD2 
130  C CE1 . TYR A 17  ? 0.3680 0.2229 0.1509 0.0363  0.0050  0.0422  32  TYR A CE1 
131  C CE2 . TYR A 17  ? 0.3449 0.2329 0.1195 0.0397  0.0038  0.0345  32  TYR A CE2 
132  C CZ  . TYR A 17  ? 0.3568 0.2268 0.1374 0.0383  -0.0010 0.0459  32  TYR A CZ  
133  O OH  . TYR A 17  ? 0.4975 0.3652 0.2831 0.0385  -0.0124 0.0613  32  TYR A OH  
134  N N   . LEU A 18  ? 0.3109 0.1637 0.1014 0.0433  0.0217  -0.0188 33  LEU A N   
135  C CA  . LEU A 18  ? 0.3117 0.1683 0.1062 0.0470  0.0182  -0.0295 33  LEU A CA  
136  C C   . LEU A 18  ? 0.3216 0.1836 0.1183 0.0502  0.0074  -0.0189 33  LEU A C   
137  O O   . LEU A 18  ? 0.3265 0.1779 0.1289 0.0499  0.0005  -0.0074 33  LEU A O   
138  C CB  . LEU A 18  ? 0.3047 0.1494 0.1108 0.0455  0.0180  -0.0391 33  LEU A CB  
139  C CG  . LEU A 18  ? 0.3645 0.2199 0.1911 0.0365  0.0237  -0.0409 33  LEU A CG  
140  C CD1 . LEU A 18  ? 0.2836 0.1466 0.1311 0.0320  0.0217  -0.0485 33  LEU A CD1 
141  C CD2 . LEU A 18  ? 0.3232 0.1990 0.1591 0.0335  0.0283  -0.0446 33  LEU A CD2 
142  N N   . GLU A 19  ? 0.3251 0.2043 0.1186 0.0529  0.0055  -0.0224 34  GLU A N   
143  C CA  . GLU A 19  ? 0.3353 0.2215 0.1324 0.0561  -0.0058 -0.0131 34  GLU A CA  
144  C C   . GLU A 19  ? 0.3641 0.2488 0.1700 0.0604  -0.0088 -0.0278 34  GLU A C   
145  O O   . GLU A 19  ? 0.3742 0.2712 0.1762 0.0615  -0.0037 -0.0413 34  GLU A O   
146  C CB  . GLU A 19  ? 0.3750 0.2857 0.1616 0.0549  -0.0064 -0.0054 34  GLU A CB  
147  C CG  . GLU A 19  ? 0.4072 0.3238 0.1948 0.0547  -0.0186 0.0155  34  GLU A CG  
148  C CD  . GLU A 19  ? 0.4246 0.3426 0.2222 0.0596  -0.0298 0.0156  34  GLU A CD  
149  O OE1 . GLU A 19  ? 0.4267 0.3263 0.2379 0.0631  -0.0336 0.0090  34  GLU A OE1 
150  O OE2 . GLU A 19  ? 0.4236 0.3630 0.2163 0.0597  -0.0351 0.0219  34  GLU A OE2 
151  N N   . ILE A 20  ? 0.3502 0.2208 0.1695 0.0628  -0.0169 -0.0265 35  ILE A N   
152  C CA  . ILE A 20  ? 0.4255 0.2927 0.2558 0.0664  -0.0193 -0.0426 35  ILE A CA  
153  C C   . ILE A 20  ? 0.4460 0.3198 0.2863 0.0715  -0.0324 -0.0356 35  ILE A C   
154  O O   . ILE A 20  ? 0.4406 0.3087 0.2882 0.0721  -0.0420 -0.0187 35  ILE A O   
155  C CB  . ILE A 20  ? 0.4081 0.2565 0.2494 0.0647  -0.0181 -0.0500 35  ILE A CB  
156  C CG1 . ILE A 20  ? 0.3482 0.1914 0.1796 0.0589  -0.0062 -0.0543 35  ILE A CG1 
157  C CG2 . ILE A 20  ? 0.3429 0.1909 0.1966 0.0677  -0.0203 -0.0682 35  ILE A CG2 
158  C CD1 . ILE A 20  ? 0.3557 0.1834 0.1923 0.0553  -0.0064 -0.0480 35  ILE A CD1 
159  N N   . VAL A 21  ? 0.4390 0.3248 0.2809 0.0751  -0.0333 -0.0479 36  VAL A N   
160  C CA  . VAL A 21  ? 0.4662 0.3597 0.3190 0.0804  -0.0462 -0.0428 36  VAL A CA  
161  C C   . VAL A 21  ? 0.4947 0.3798 0.3653 0.0844  -0.0492 -0.0605 36  VAL A C   
162  O O   . VAL A 21  ? 0.4683 0.3557 0.3357 0.0836  -0.0403 -0.0801 36  VAL A O   
163  C CB  . VAL A 21  ? 0.5099 0.4283 0.3506 0.0811  -0.0457 -0.0426 36  VAL A CB  
164  C CG1 . VAL A 21  ? 0.4959 0.4228 0.3495 0.0867  -0.0595 -0.0391 36  VAL A CG1 
165  C CG2 . VAL A 21  ? 0.4980 0.4284 0.3233 0.0764  -0.0439 -0.0251 36  VAL A CG2 
166  N N   . THR A 22  A 0.5345 0.4103 0.4252 0.0883  -0.0618 -0.0540 36  THR A N   
167  C CA  . THR A 22  A 0.5714 0.4417 0.4827 0.0925  -0.0659 -0.0717 36  THR A CA  
168  C C   . THR A 22  A 0.6174 0.5023 0.5367 0.0987  -0.0757 -0.0730 36  THR A C   
169  O O   . THR A 22  A 0.5849 0.4842 0.4942 0.0992  -0.0802 -0.0584 36  THR A O   
170  C CB  . THR A 22  A 0.6213 0.4733 0.5550 0.0935  -0.0738 -0.0677 36  THR A CB  
171  O OG1 . THR A 22  A 0.6247 0.4758 0.5696 0.0969  -0.0885 -0.0459 36  THR A OG1 
172  C CG2 . THR A 22  A 0.5704 0.4101 0.4948 0.0869  -0.0647 -0.0641 36  THR A CG2 
173  N N   . SER A 23  B 0.6423 0.5256 0.5804 0.1028  -0.0790 -0.0914 36  SER A N   
174  C CA  . SER A 23  B 0.7144 0.6112 0.6631 0.1092  -0.0887 -0.0948 36  SER A CA  
175  C C   . SER A 23  B 0.6480 0.5400 0.6194 0.1146  -0.1071 -0.0764 36  SER A C   
176  O O   . SER A 23  B 0.6405 0.5212 0.6148 0.1126  -0.1119 -0.0574 36  SER A O   
177  C CB  . SER A 23  B 0.7250 0.6232 0.6863 0.1114  -0.0850 -0.1229 36  SER A CB  
178  O OG  . SER A 23  B 0.7757 0.6798 0.7181 0.1047  -0.0684 -0.1368 36  SER A OG  
179  N N   . PRO A 26  ? 0.5386 0.4053 0.4822 0.0973  -0.1186 0.0227  38  PRO A N   
180  C CA  . PRO A 26  ? 0.5938 0.4445 0.5341 0.0922  -0.1125 0.0286  38  PRO A CA  
181  C C   . PRO A 26  ? 0.6245 0.4784 0.5397 0.0871  -0.0941 0.0156  38  PRO A C   
182  O O   . PRO A 26  ? 0.5921 0.4501 0.5030 0.0884  -0.0853 -0.0063 38  PRO A O   
183  C CB  . PRO A 26  ? 0.6259 0.4561 0.5963 0.0960  -0.1176 0.0164  38  PRO A CB  
184  C CG  . PRO A 26  ? 0.6940 0.5278 0.6886 0.1031  -0.1331 0.0179  38  PRO A CG  
185  C CD  . PRO A 26  ? 0.5702 0.4268 0.5462 0.1044  -0.1301 0.0134  38  PRO A CD  
186  N N   . SER A 27  ? 0.5161 0.3682 0.4164 0.0811  -0.0887 0.0293  39  SER A N   
187  C CA  . SER A 27  ? 0.4960 0.3520 0.3741 0.0763  -0.0726 0.0202  39  SER A CA  
188  C C   . SER A 27  ? 0.5020 0.3391 0.3832 0.0726  -0.0667 0.0188  39  SER A C   
189  O O   . SER A 27  ? 0.5415 0.3661 0.4354 0.0719  -0.0745 0.0322  39  SER A O   
190  C CB  . SER A 27  ? 0.4841 0.3595 0.3404 0.0719  -0.0696 0.0350  39  SER A CB  
191  O OG  . SER A 27  ? 0.6579 0.5326 0.5173 0.0694  -0.0799 0.0601  39  SER A OG  
192  N N   . LYS A 28  ? 0.4398 0.2754 0.3101 0.0699  -0.0533 0.0029  40  LYS A N   
193  C CA  . LYS A 28  ? 0.4376 0.2587 0.3079 0.0656  -0.0464 0.0006  40  LYS A CA  
194  C C   . LYS A 28  ? 0.4233 0.2511 0.2720 0.0606  -0.0350 0.0042  40  LYS A C   
195  O O   . LYS A 28  ? 0.4093 0.2524 0.2448 0.0606  -0.0297 0.0005  40  LYS A O   
196  C CB  . LYS A 28  ? 0.3803 0.1934 0.2602 0.0657  -0.0414 -0.0219 40  LYS A CB  
197  C CG  . LYS A 28  ? 0.5096 0.3158 0.4148 0.0703  -0.0518 -0.0292 40  LYS A CG  
198  C CD  . LYS A 28  ? 0.5306 0.3307 0.4447 0.0682  -0.0457 -0.0512 40  LYS A CD  
199  C CE  . LYS A 28  ? 0.3736 0.1842 0.2741 0.0667  -0.0355 -0.0679 40  LYS A CE  
200  N NZ  . LYS A 28  ? 0.4168 0.2423 0.3355 0.0570  -0.0265 -0.0809 40  LYS A NZ  
201  N N   . PHE A 29  ? 0.3473 0.1643 0.1944 0.0562  -0.0313 0.0107  41  PHE A N   
202  C CA  . PHE A 29  ? 0.3415 0.1631 0.1719 0.0516  -0.0211 0.0140  41  PHE A CA  
203  C C   . PHE A 29  ? 0.3910 0.1998 0.2232 0.0479  -0.0136 0.0049  41  PHE A C   
204  O O   . PHE A 29  ? 0.3912 0.1872 0.2349 0.0467  -0.0175 0.0072  41  PHE A O   
205  C CB  . PHE A 29  ? 0.3837 0.2090 0.2083 0.0489  -0.0248 0.0355  41  PHE A CB  
206  C CG  . PHE A 29  ? 0.4157 0.2567 0.2376 0.0507  -0.0329 0.0470  41  PHE A CG  
207  C CD1 . PHE A 29  ? 0.4350 0.2968 0.2415 0.0494  -0.0275 0.0465  41  PHE A CD1 
208  C CD2 . PHE A 29  ? 0.4091 0.2453 0.2451 0.0533  -0.0462 0.0580  41  PHE A CD2 
209  C CE1 . PHE A 29  ? 0.4402 0.3201 0.2430 0.0499  -0.0349 0.0572  41  PHE A CE1 
210  C CE2 . PHE A 29  ? 0.4604 0.3127 0.2938 0.0542  -0.0547 0.0706  41  PHE A CE2 
211  C CZ  . PHE A 29  ? 0.4419 0.3171 0.2573 0.0521  -0.0488 0.0703  41  PHE A CZ  
212  N N   . CYS A 30  ? 0.3431 0.1564 0.1652 0.0457  -0.0032 -0.0052 42  CYS A N   
213  C CA  . CYS A 30  ? 0.3430 0.1469 0.1659 0.0413  0.0037  -0.0135 42  CYS A CA  
214  C C   . CYS A 30  ? 0.3373 0.1454 0.1482 0.0379  0.0128  -0.0109 42  CYS A C   
215  O O   . CYS A 30  ? 0.3228 0.1426 0.1256 0.0391  0.0149  -0.0067 42  CYS A O   
216  C CB  . CYS A 30  ? 0.3250 0.1287 0.1532 0.0416  0.0060  -0.0324 42  CYS A CB  
217  S SG  . CYS A 30  ? 0.4243 0.2208 0.2725 0.0429  -0.0022 -0.0407 42  CYS A SG  
218  N N   . GLY A 31  ? 0.3065 0.1065 0.1177 0.0331  0.0180  -0.0138 43  GLY A N   
219  C CA  . GLY A 31  ? 0.3057 0.1081 0.1095 0.0299  0.0263  -0.0132 43  GLY A CA  
220  C C   . GLY A 31  ? 0.3019 0.1213 0.1220 0.0252  0.0291  -0.0221 43  GLY A C   
221  O O   . GLY A 31  ? 0.2780 0.1078 0.1124 0.0240  0.0260  -0.0298 43  GLY A O   
222  N N   . GLY A 32  ? 0.2938 0.1197 0.1165 0.0221  0.0340  -0.0199 44  GLY A N   
223  C CA  . GLY A 32  ? 0.2616 0.1032 0.1015 0.0174  0.0353  -0.0255 44  GLY A CA  
224  C C   . GLY A 32  ? 0.2935 0.1345 0.1324 0.0157  0.0402  -0.0219 44  GLY A C   
225  O O   . GLY A 32  ? 0.2854 0.1187 0.1133 0.0182  0.0427  -0.0164 44  GLY A O   
226  N N   . PHE A 33  ? 0.2771 0.1260 0.1275 0.0116  0.0414  -0.0253 45  PHE A N   
227  C CA  . PHE A 33  ? 0.3397 0.1856 0.1904 0.0102  0.0459  -0.0229 45  PHE A CA  
228  C C   . PHE A 33  ? 0.2903 0.1489 0.1547 0.0091  0.0462  -0.0304 45  PHE A C   
229  O O   . PHE A 33  ? 0.2386 0.1038 0.1103 0.0066  0.0438  -0.0346 45  PHE A O   
230  C CB  . PHE A 33  ? 0.3073 0.1386 0.1508 0.0054  0.0485  -0.0157 45  PHE A CB  
231  C CG  . PHE A 33  ? 0.3527 0.1848 0.1987 0.0000  0.0465  -0.0168 45  PHE A CG  
232  C CD1 . PHE A 33  ? 0.3680 0.2000 0.2124 0.0001  0.0429  -0.0174 45  PHE A CD1 
233  C CD2 . PHE A 33  ? 0.3717 0.2041 0.2212 -0.0055 0.0487  -0.0179 45  PHE A CD2 
234  C CE1 . PHE A 33  ? 0.3864 0.2225 0.2353 -0.0050 0.0414  -0.0205 45  PHE A CE1 
235  C CE2 . PHE A 33  ? 0.3871 0.2215 0.2374 -0.0113 0.0475  -0.0196 45  PHE A CE2 
236  C CZ  . PHE A 33  ? 0.3824 0.2205 0.2337 -0.0110 0.0438  -0.0216 45  PHE A CZ  
237  N N   . LEU A 34  ? 0.2714 0.1338 0.1393 0.0112  0.0491  -0.0328 46  LEU A N   
238  C CA  . LEU A 34  ? 0.3195 0.1922 0.2006 0.0109  0.0495  -0.0405 46  LEU A CA  
239  C C   . LEU A 34  ? 0.3209 0.1820 0.2031 0.0057  0.0525  -0.0374 46  LEU A C   
240  O O   . LEU A 34  ? 0.3501 0.1986 0.2279 0.0045  0.0565  -0.0319 46  LEU A O   
241  C CB  . LEU A 34  ? 0.3113 0.1926 0.1971 0.0149  0.0518  -0.0456 46  LEU A CB  
242  C CG  . LEU A 34  ? 0.3196 0.2160 0.2193 0.0169  0.0507  -0.0563 46  LEU A CG  
243  C CD1 . LEU A 34  ? 0.3045 0.2181 0.2069 0.0199  0.0458  -0.0628 46  LEU A CD1 
244  C CD2 . LEU A 34  ? 0.3479 0.2498 0.2525 0.0200  0.0542  -0.0609 46  LEU A CD2 
245  N N   . ILE A 35  ? 0.3186 0.1836 0.2062 0.0026  0.0507  -0.0408 47  ILE A N   
246  C CA  . ILE A 35  ? 0.3697 0.2232 0.2564 -0.0036 0.0542  -0.0382 47  ILE A CA  
247  C C   . ILE A 35  ? 0.4030 0.2597 0.3020 -0.0029 0.0558  -0.0446 47  ILE A C   
248  O O   . ILE A 35  ? 0.5065 0.3512 0.4084 -0.0064 0.0597  -0.0421 47  ILE A O   
249  C CB  . ILE A 35  ? 0.3944 0.2486 0.2772 -0.0091 0.0524  -0.0379 47  ILE A CB  
250  C CG1 . ILE A 35  ? 0.3570 0.2287 0.2497 -0.0059 0.0476  -0.0463 47  ILE A CG1 
251  C CG2 . ILE A 35  ? 0.4135 0.2631 0.2863 -0.0103 0.0510  -0.0323 47  ILE A CG2 
252  C CD1 . ILE A 35  ? 0.4900 0.3653 0.3816 -0.0106 0.0457  -0.0478 47  ILE A CD1 
253  N N   . ARG A 36  ? 0.4012 0.2739 0.3087 0.0019  0.0522  -0.0529 48  ARG A N   
254  C CA  . ARG A 36  ? 0.3587 0.2357 0.2780 0.0039  0.0530  -0.0600 48  ARG A CA  
255  C C   . ARG A 36  ? 0.3783 0.2724 0.3014 0.0115  0.0493  -0.0672 48  ARG A C   
256  O O   . ARG A 36  ? 0.3425 0.2444 0.2597 0.0141  0.0467  -0.0665 48  ARG A O   
257  C CB  . ARG A 36  ? 0.4461 0.3226 0.3690 -0.0002 0.0526  -0.0631 48  ARG A CB  
258  C CG  . ARG A 36  ? 0.5144 0.3730 0.4354 -0.0086 0.0578  -0.0575 48  ARG A CG  
259  C CD  . ARG A 36  ? 0.6189 0.4774 0.5435 -0.0137 0.0584  -0.0614 48  ARG A CD  
260  N NE  . ARG A 36  ? 0.7208 0.5658 0.6555 -0.0182 0.0623  -0.0606 48  ARG A NE  
261  C CZ  . ARG A 36  ? 0.7429 0.5907 0.6925 -0.0149 0.0624  -0.0670 48  ARG A CZ  
262  N NH1 . ARG A 36  ? 0.8150 0.6784 0.7673 -0.0077 0.0593  -0.0748 48  ARG A NH1 
263  N NH2 . ARG A 36  ? 0.8203 0.6551 0.7836 -0.0191 0.0643  -0.0646 48  ARG A NH2 
264  N N   . ARG A 37  ? 0.4255 0.1716 0.2480 -0.0384 0.0547  -0.0252 49  ARG A N   
265  C CA  . ARG A 37  ? 0.4737 0.2317 0.3037 -0.0441 0.0503  -0.0334 49  ARG A CA  
266  C C   . ARG A 37  ? 0.4442 0.2166 0.2800 -0.0527 0.0473  -0.0384 49  ARG A C   
267  O O   . ARG A 37  ? 0.4210 0.2067 0.2591 -0.0533 0.0409  -0.0430 49  ARG A O   
268  C CB  . ARG A 37  ? 0.5686 0.3195 0.4029 -0.0505 0.0551  -0.0384 49  ARG A CB  
269  C CG  . ARG A 37  ? 0.5891 0.3303 0.4202 -0.0423 0.0555  -0.0365 49  ARG A CG  
270  C CD  . ARG A 37  ? 0.5758 0.3219 0.4132 -0.0470 0.0540  -0.0455 49  ARG A CD  
271  N NE  . ARG A 37  ? 0.6843 0.4187 0.5209 -0.0415 0.0564  -0.0449 49  ARG A NE  
272  C CZ  . ARG A 37  ? 0.6649 0.4020 0.5059 -0.0428 0.0550  -0.0521 49  ARG A CZ  
273  N NH1 . ARG A 37  ? 0.6446 0.3960 0.4893 -0.0486 0.0511  -0.0602 49  ARG A NH1 
274  N NH2 . ARG A 37  ? 0.5413 0.2666 0.3823 -0.0375 0.0576  -0.0514 49  ARG A NH2 
275  N N   . ASN A 38  ? 0.4658 0.2391 0.3055 -0.0588 0.0518  -0.0369 50  ASN A N   
276  C CA  . ASN A 38  ? 0.4469 0.2442 0.2991 -0.0656 0.0479  -0.0404 50  ASN A CA  
277  C C   . ASN A 38  ? 0.3855 0.1938 0.2412 -0.0610 0.0469  -0.0336 50  ASN A C   
278  O O   . ASN A 38  ? 0.3609 0.1868 0.2282 -0.0667 0.0458  -0.0356 50  ASN A O   
279  C CB  . ASN A 38  ? 0.4376 0.2344 0.2988 -0.0789 0.0536  -0.0476 50  ASN A CB  
280  C CG  . ASN A 38  ? 0.6063 0.3776 0.4625 -0.0816 0.0651  -0.0445 50  ASN A CG  
281  O OD1 . ASN A 38  ? 0.5705 0.3297 0.4177 -0.0739 0.0689  -0.0353 50  ASN A OD1 
282  N ND2 . ASN A 38  ? 0.6239 0.3932 0.4883 -0.0897 0.0695  -0.0507 50  ASN A ND2 
283  N N   . PHE A 39  ? 0.3741 0.1736 0.2208 -0.0505 0.0470  -0.0267 51  PHE A N   
284  C CA  . PHE A 39  ? 0.3630 0.1720 0.2121 -0.0455 0.0465  -0.0214 51  PHE A CA  
285  C C   . PHE A 39  ? 0.3468 0.1596 0.1924 -0.0339 0.0395  -0.0186 51  PHE A C   
286  O O   . PHE A 39  ? 0.3136 0.1128 0.1495 -0.0271 0.0389  -0.0173 51  PHE A O   
287  C CB  . PHE A 39  ? 0.3729 0.1664 0.2143 -0.0452 0.0559  -0.0161 51  PHE A CB  
288  C CG  . PHE A 39  ? 0.4501 0.2456 0.3003 -0.0571 0.0637  -0.0184 51  PHE A CG  
289  C CD1 . PHE A 39  ? 0.4372 0.2517 0.2995 -0.0607 0.0638  -0.0190 51  PHE A CD1 
290  C CD2 . PHE A 39  ? 0.4933 0.2716 0.3415 -0.0649 0.0714  -0.0205 51  PHE A CD2 
291  C CE1 . PHE A 39  ? 0.4553 0.2734 0.3282 -0.0720 0.0713  -0.0220 51  PHE A CE1 
292  C CE2 . PHE A 39  ? 0.5821 0.3627 0.4412 -0.0768 0.0793  -0.0236 51  PHE A CE2 
293  C CZ  . PHE A 39  ? 0.5139 0.3152 0.3856 -0.0805 0.0792  -0.0244 51  PHE A CZ  
294  N N   . VAL A 40  ? 0.3136 0.1452 0.1688 -0.0318 0.0345  -0.0181 52  VAL A N   
295  C CA  . VAL A 40  ? 0.2827 0.1200 0.1388 -0.0219 0.0285  -0.0162 52  VAL A CA  
296  C C   . VAL A 40  ? 0.3170 0.1607 0.1760 -0.0176 0.0296  -0.0134 52  VAL A C   
297  O O   . VAL A 40  ? 0.3116 0.1661 0.1791 -0.0228 0.0318  -0.0137 52  VAL A O   
298  C CB  . VAL A 40  ? 0.2957 0.1488 0.1614 -0.0226 0.0218  -0.0181 52  VAL A CB  
299  C CG1 . VAL A 40  ? 0.2545 0.1151 0.1256 -0.0136 0.0172  -0.0159 52  VAL A CG1 
300  C CG2 . VAL A 40  ? 0.2977 0.1440 0.1579 -0.0247 0.0207  -0.0212 52  VAL A CG2 
301  N N   . LEU A 41  ? 0.2655 0.1036 0.1182 -0.0080 0.0281  -0.0117 53  LEU A N   
302  C CA  . LEU A 41  ? 0.2879 0.1322 0.1421 -0.0026 0.0286  -0.0105 53  LEU A CA  
303  C C   . LEU A 41  ? 0.2832 0.1419 0.1502 0.0024  0.0219  -0.0124 53  LEU A C   
304  O O   . LEU A 41  ? 0.3010 0.1577 0.1684 0.0073  0.0174  -0.0136 53  LEU A O   
305  C CB  . LEU A 41  ? 0.3301 0.1600 0.1685 0.0054  0.0309  -0.0083 53  LEU A CB  
306  C CG  . LEU A 41  ? 0.4237 0.2589 0.2597 0.0104  0.0330  -0.0075 53  LEU A CG  
307  C CD1 . LEU A 41  ? 0.3628 0.2037 0.2037 0.0019  0.0401  -0.0063 53  LEU A CD1 
308  C CD2 . LEU A 41  ? 0.5018 0.3223 0.3188 0.0189  0.0350  -0.0046 53  LEU A CD2 
309  N N   . THR A 42  ? 0.2649 0.1377 0.1433 0.0012  0.0219  -0.0128 54  THR A N   
310  C CA  . THR A 42  ? 0.2230 0.1086 0.1157 0.0055  0.0166  -0.0141 54  THR A CA  
311  C C   . THR A 42  ? 0.2763 0.1712 0.1759 0.0080  0.0185  -0.0153 54  THR A C   
312  O O   . THR A 42  ? 0.2984 0.1898 0.1901 0.0068  0.0240  -0.0149 54  THR A O   
313  C CB  . THR A 42  ? 0.2583 0.1540 0.1618 0.0004  0.0135  -0.0132 54  THR A CB  
314  O OG1 . THR A 42  ? 0.2574 0.1625 0.1741 0.0055  0.0093  -0.0130 54  THR A OG1 
315  C CG2 . THR A 42  ? 0.2876 0.1930 0.1974 -0.0070 0.0161  -0.0130 54  THR A CG2 
316  N N   . ALA A 43  ? 0.2208 0.1270 0.1355 0.0117  0.0147  -0.0167 55  ALA A N   
317  C CA  . ALA A 43  ? 0.2321 0.1482 0.1561 0.0145  0.0162  -0.0189 55  ALA A CA  
318  C C   . ALA A 43  ? 0.2342 0.1624 0.1694 0.0082  0.0183  -0.0175 55  ALA A C   
319  O O   . ALA A 43  ? 0.2094 0.1428 0.1508 0.0037  0.0156  -0.0152 55  ALA A O   
320  C CB  . ALA A 43  ? 0.2134 0.1353 0.1512 0.0214  0.0117  -0.0217 55  ALA A CB  
321  N N   . ALA A 44  ? 0.2411 0.1751 0.1789 0.0084  0.0229  -0.0194 56  ALA A N   
322  C CA  . ALA A 44  ? 0.2366 0.1834 0.1863 0.0025  0.0256  -0.0190 56  ALA A CA  
323  C C   . ALA A 44  ? 0.2576 0.2189 0.2278 0.0048  0.0203  -0.0187 56  ALA A C   
324  O O   . ALA A 44  ? 0.2476 0.2200 0.2280 -0.0001 0.0193  -0.0173 56  ALA A O   
325  C CB  . ALA A 44  ? 0.2307 0.1803 0.1785 0.0026  0.0330  -0.0213 56  ALA A CB  
326  N N   . HIS A 45  ? 0.1891 0.1504 0.1663 0.0123  0.0170  -0.0200 57  HIS A N   
327  C CA  . HIS A 45  ? 0.2151 0.1877 0.2119 0.0153  0.0129  -0.0184 57  HIS A CA  
328  C C   . HIS A 45  ? 0.2324 0.2052 0.2299 0.0132  0.0079  -0.0131 57  HIS A C   
329  O O   . HIS A 45  ? 0.2302 0.2127 0.2421 0.0154  0.0046  -0.0098 57  HIS A O   
330  C CB  . HIS A 45  ? 0.2189 0.1898 0.2245 0.0233  0.0118  -0.0218 57  HIS A CB  
331  C CG  . HIS A 45  ? 0.2317 0.1913 0.2306 0.0261  0.0088  -0.0216 57  HIS A CG  
332  N ND1 . HIS A 45  ? 0.2126 0.1627 0.1990 0.0290  0.0096  -0.0262 57  HIS A ND1 
333  C CD2 . HIS A 45  ? 0.2302 0.1873 0.2336 0.0268  0.0052  -0.0173 57  HIS A CD2 
334  C CE1 . HIS A 45  ? 0.2145 0.1575 0.2000 0.0310  0.0064  -0.0256 57  HIS A CE1 
335  N NE2 . HIS A 45  ? 0.2840 0.2307 0.2796 0.0294  0.0044  -0.0201 57  HIS A NE2 
336  N N   . CYS A 46  ? 0.2134 0.1756 0.1951 0.0097  0.0074  -0.0119 58  CYS A N   
337  C CA  . CYS A 46  ? 0.2793 0.2421 0.2590 0.0073  0.0033  -0.0077 58  CYS A CA  
338  C C   . CYS A 46  ? 0.2573 0.2308 0.2387 0.0006  0.0024  -0.0069 58  CYS A C   
339  O O   . CYS A 46  ? 0.2922 0.2687 0.2712 -0.0014 -0.0016 -0.0041 58  CYS A O   
340  C CB  . CYS A 46  ? 0.2309 0.1789 0.1942 0.0063  0.0036  -0.0081 58  CYS A CB  
341  S SG  . CYS A 46  ? 0.3687 0.3067 0.3323 0.0142  0.0033  -0.0102 58  CYS A SG  
342  N N   . ALA A 47  ? 0.2333 0.2134 0.2189 -0.0031 0.0060  -0.0099 59  ALA A N   
343  C CA  . ALA A 47  ? 0.2479 0.2399 0.2381 -0.0101 0.0052  -0.0108 59  ALA A CA  
344  C C   . ALA A 47  ? 0.3067 0.3155 0.3119 -0.0069 -0.0013 -0.0076 59  ALA A C   
345  O O   . ALA A 47  ? 0.2585 0.2721 0.2757 0.0003  -0.0026 -0.0052 59  ALA A O   
346  C CB  . ALA A 47  ? 0.3317 0.3282 0.3266 -0.0143 0.0118  -0.0148 59  ALA A CB  
347  N N   . GLY A 48  ? 0.3699 0.3874 0.3740 -0.0117 -0.0055 -0.0076 60  GLY A N   
348  C CA  . GLY A 48  ? 0.3709 0.4061 0.3870 -0.0083 -0.0125 -0.0042 60  GLY A CA  
349  C C   . GLY A 48  ? 0.3814 0.4304 0.3996 -0.0162 -0.0153 -0.0087 60  GLY A C   
350  O O   . GLY A 48  ? 0.4535 0.5013 0.4713 -0.0242 -0.0101 -0.0148 60  GLY A O   
351  N N   . ARG A 49  ? 0.3901 0.4529 0.4108 -0.0138 -0.0233 -0.0059 61  ARG A N   
352  C CA  . ARG A 49  ? 0.3695 0.4473 0.3920 -0.0212 -0.0275 -0.0119 61  ARG A CA  
353  C C   . ARG A 49  ? 0.3891 0.4551 0.3928 -0.0275 -0.0272 -0.0151 61  ARG A C   
354  O O   . ARG A 49  ? 0.3708 0.4324 0.3717 -0.0370 -0.0229 -0.0226 61  ARG A O   
355  C CB  . ARG A 49  ? 0.4557 0.5557 0.4884 -0.0150 -0.0372 -0.0081 61  ARG A CB  
356  C CG  . ARG A 49  ? 0.4994 0.6213 0.5408 -0.0217 -0.0425 -0.0162 61  ARG A CG  
357  C CD  . ARG A 49  ? 0.4717 0.6024 0.5316 -0.0275 -0.0372 -0.0232 61  ARG A CD  
358  N NE  . ARG A 49  ? 0.6301 0.7775 0.7100 -0.0193 -0.0402 -0.0197 61  ARG A NE  
359  C CZ  . ARG A 49  ? 0.6401 0.8021 0.7401 -0.0225 -0.0373 -0.0255 61  ARG A CZ  
360  N NH1 . ARG A 49  ? 0.5692 0.7310 0.6723 -0.0343 -0.0306 -0.0347 61  ARG A NH1 
361  N NH2 . ARG A 49  ? 0.5891 0.7657 0.7074 -0.0137 -0.0404 -0.0220 61  ARG A NH2 
362  N N   . SER A 50  ? 0.3966 0.4559 0.3876 -0.0223 -0.0306 -0.0095 63  SER A N   
363  C CA  . SER A 50  ? 0.3384 0.3867 0.3115 -0.0271 -0.0303 -0.0126 63  SER A CA  
364  C C   . SER A 50  ? 0.3215 0.3470 0.2831 -0.0235 -0.0248 -0.0084 63  SER A C   
365  O O   . SER A 50  ? 0.3202 0.3426 0.2847 -0.0152 -0.0249 -0.0010 63  SER A O   
366  C CB  . SER A 50  ? 0.3962 0.4576 0.3625 -0.0243 -0.0387 -0.0106 63  SER A CB  
367  O OG  . SER A 50  ? 0.3671 0.4164 0.3155 -0.0275 -0.0374 -0.0131 63  SER A OG  
368  N N   . ILE A 51  ? 0.3006 0.3105 0.2507 -0.0295 -0.0198 -0.0135 64  ILE A N   
369  C CA  . ILE A 51  ? 0.3274 0.3168 0.2664 -0.0263 -0.0153 -0.0109 64  ILE A CA  
370  C C   . ILE A 51  ? 0.3225 0.3037 0.2464 -0.0305 -0.0153 -0.0150 64  ILE A C   
371  O O   . ILE A 51  ? 0.3318 0.3125 0.2530 -0.0387 -0.0140 -0.0223 64  ILE A O   
372  C CB  . ILE A 51  ? 0.3340 0.3099 0.2739 -0.0274 -0.0083 -0.0127 64  ILE A CB  
373  C CG1 . ILE A 51  ? 0.3130 0.2978 0.2677 -0.0231 -0.0079 -0.0101 64  ILE A CG1 
374  C CG2 . ILE A 51  ? 0.3018 0.2588 0.2307 -0.0231 -0.0052 -0.0109 64  ILE A CG2 
375  C CD1 . ILE A 51  ? 0.3104 0.2836 0.2642 -0.0232 -0.0010 -0.0118 64  ILE A CD1 
376  N N   . THR A 52  ? 0.2870 0.2616 0.2023 -0.0252 -0.0159 -0.0107 65  THR A N   
377  C CA  . THR A 52  ? 0.2856 0.2512 0.1864 -0.0280 -0.0149 -0.0144 65  THR A CA  
378  C C   . THR A 52  ? 0.2873 0.2333 0.1825 -0.0245 -0.0096 -0.0131 65  THR A C   
379  O O   . THR A 52  ? 0.2913 0.2349 0.1910 -0.0176 -0.0090 -0.0071 65  THR A O   
380  C CB  . THR A 52  ? 0.3264 0.3029 0.2210 -0.0247 -0.0197 -0.0110 65  THR A CB  
381  O OG1 . THR A 52  ? 0.4470 0.4437 0.3468 -0.0268 -0.0261 -0.0126 65  THR A OG1 
382  C CG2 . THR A 52  ? 0.3385 0.3062 0.2180 -0.0277 -0.0179 -0.0161 65  THR A CG2 
383  N N   . VAL A 53  ? 0.2913 0.2235 0.1779 -0.0291 -0.0057 -0.0190 66  VAL A N   
384  C CA  . VAL A 53  ? 0.2818 0.1959 0.1630 -0.0255 -0.0013 -0.0187 66  VAL A CA  
385  C C   . VAL A 53  ? 0.3044 0.2126 0.1755 -0.0244 -0.0007 -0.0203 66  VAL A C   
386  O O   . VAL A 53  ? 0.3301 0.2393 0.1940 -0.0298 -0.0011 -0.0259 66  VAL A O   
387  C CB  . VAL A 53  ? 0.3208 0.2217 0.1991 -0.0298 0.0034  -0.0228 66  VAL A CB  
388  C CG1 . VAL A 53  ? 0.3490 0.2321 0.2207 -0.0245 0.0069  -0.0222 66  VAL A CG1 
389  C CG2 . VAL A 53  ? 0.3773 0.2846 0.2653 -0.0309 0.0042  -0.0212 66  VAL A CG2 
390  N N   . THR A 54  ? 0.2720 0.1746 0.1436 -0.0176 0.0005  -0.0164 67  THR A N   
391  C CA  . THR A 54  ? 0.2962 0.1922 0.1597 -0.0160 0.0025  -0.0181 67  THR A CA  
392  C C   . THR A 54  ? 0.2973 0.1765 0.1587 -0.0131 0.0061  -0.0208 67  THR A C   
393  O O   . THR A 54  ? 0.2854 0.1616 0.1538 -0.0078 0.0063  -0.0180 67  THR A O   
394  C CB  . THR A 54  ? 0.3257 0.2294 0.1929 -0.0105 0.0019  -0.0117 67  THR A CB  
395  O OG1 . THR A 54  ? 0.3290 0.2482 0.1961 -0.0119 -0.0019 -0.0082 67  THR A OG1 
396  C CG2 . THR A 54  ? 0.3157 0.2128 0.1750 -0.0090 0.0053  -0.0137 67  THR A CG2 
397  N N   . LEU A 55  ? 0.2878 0.1566 0.1401 -0.0160 0.0086  -0.0266 68  LEU A N   
398  C CA  . LEU A 55  ? 0.2746 0.1271 0.1238 -0.0125 0.0117  -0.0291 68  LEU A CA  
399  C C   . LEU A 55  ? 0.2860 0.1344 0.1310 -0.0098 0.0138  -0.0319 68  LEU A C   
400  O O   . LEU A 55  ? 0.2801 0.1365 0.1212 -0.0124 0.0137  -0.0330 68  LEU A O   
401  C CB  . LEU A 55  ? 0.2742 0.1149 0.1175 -0.0177 0.0142  -0.0334 68  LEU A CB  
402  C CG  . LEU A 55  ? 0.2666 0.1100 0.1137 -0.0215 0.0140  -0.0314 68  LEU A CG  
403  C CD1 . LEU A 55  ? 0.3093 0.1402 0.1509 -0.0281 0.0182  -0.0359 68  LEU A CD1 
404  C CD2 . LEU A 55  ? 0.2795 0.1203 0.1307 -0.0146 0.0137  -0.0265 68  LEU A CD2 
405  N N   . GLY A 56  ? 0.2922 0.1290 0.1378 -0.0041 0.0156  -0.0331 69  GLY A N   
406  C CA  . GLY A 56  ? 0.3145 0.1481 0.1591 -0.0012 0.0182  -0.0363 69  GLY A CA  
407  C C   . GLY A 56  ? 0.3652 0.2088 0.2145 0.0014  0.0188  -0.0337 69  GLY A C   
408  O O   . GLY A 56  ? 0.3740 0.2181 0.2192 0.0012  0.0219  -0.0365 69  GLY A O   
409  N N   . ALA A 57  ? 0.3072 0.1592 0.1661 0.0039  0.0167  -0.0279 70  ALA A N   
410  C CA  . ALA A 57  ? 0.3445 0.2060 0.2104 0.0061  0.0182  -0.0235 70  ALA A CA  
411  C C   . ALA A 57  ? 0.3659 0.2253 0.2452 0.0126  0.0192  -0.0236 70  ALA A C   
412  O O   . ALA A 57  ? 0.3937 0.2500 0.2787 0.0156  0.0164  -0.0243 70  ALA A O   
413  C CB  . ALA A 57  ? 0.3224 0.1957 0.1917 0.0041  0.0155  -0.0168 70  ALA A CB  
414  N N   . HIS A 58  ? 0.2969 0.1585 0.1811 0.0146  0.0235  -0.0237 71  HIS A N   
415  C CA  . HIS A 58  ? 0.3282 0.1919 0.2293 0.0196  0.0249  -0.0235 71  HIS A CA  
416  C C   . HIS A 58  ? 0.3140 0.1868 0.2238 0.0189  0.0276  -0.0160 71  HIS A C   
417  O O   . HIS A 58  ? 0.2710 0.1470 0.1940 0.0208  0.0259  -0.0135 71  HIS A O   
418  C CB  . HIS A 58  ? 0.4035 0.2631 0.3082 0.0228  0.0289  -0.0294 71  HIS A CB  
419  C CG  . HIS A 58  ? 0.3798 0.2425 0.3044 0.0276  0.0298  -0.0314 71  HIS A CG  
420  N ND1 . HIS A 58  ? 0.3910 0.2547 0.3255 0.0317  0.0241  -0.0349 71  HIS A ND1 
421  C CD2 . HIS A 58  ? 0.3903 0.2583 0.3287 0.0284  0.0356  -0.0306 71  HIS A CD2 
422  C CE1 . HIS A 58  ? 0.3807 0.2518 0.3355 0.0344  0.0251  -0.0373 71  HIS A CE1 
423  N NE2 . HIS A 58  ? 0.4225 0.2925 0.3794 0.0328  0.0335  -0.0352 71  HIS A NE2 
424  N N   . ASN A 59  ? 0.3164 0.1929 0.2183 0.0165  0.0320  -0.0123 72  ASN A N   
425  C CA  . ASN A 59  ? 0.3820 0.2661 0.2877 0.0161  0.0345  -0.0029 72  ASN A CA  
426  C C   . ASN A 59  ? 0.3836 0.2728 0.2788 0.0133  0.0291  0.0014  72  ASN A C   
427  O O   . ASN A 59  ? 0.3921 0.2818 0.2716 0.0099  0.0270  -0.0015 72  ASN A O   
428  C CB  . ASN A 59  ? 0.3524 0.2386 0.2522 0.0157  0.0422  -0.0001 72  ASN A CB  
429  C CG  . ASN A 59  ? 0.4849 0.3770 0.3901 0.0166  0.0465  0.0111  72  ASN A CG  
430  O OD1 . ASN A 59  ? 0.4845 0.3807 0.3906 0.0168  0.0424  0.0176  72  ASN A OD1 
431  N ND2 . ASN A 59  ? 0.4799 0.3721 0.3890 0.0175  0.0555  0.0139  72  ASN A ND2 
432  N N   . ILE A 60  ? 0.3584 0.2520 0.2640 0.0147  0.0268  0.0075  73  ILE A N   
433  C CA  . ILE A 60  ? 0.4003 0.3006 0.2996 0.0128  0.0214  0.0113  73  ILE A CA  
434  C C   . ILE A 60  ? 0.4281 0.3369 0.3223 0.0135  0.0227  0.0212  73  ILE A C   
435  O O   . ILE A 60  ? 0.3895 0.3062 0.2765 0.0121  0.0176  0.0239  73  ILE A O   
436  C CB  . ILE A 60  ? 0.3239 0.2246 0.2370 0.0144  0.0176  0.0113  73  ILE A CB  
437  C CG1 . ILE A 60  ? 0.3710 0.2768 0.2768 0.0114  0.0117  0.0109  73  ILE A CG1 
438  C CG2 . ILE A 60  ? 0.3222 0.2262 0.2511 0.0180  0.0202  0.0191  73  ILE A CG2 
439  C CD1 . ILE A 60  ? 0.3944 0.2951 0.2870 0.0072  0.0101  0.0030  73  ILE A CD1 
440  N N   . THR A 61  ? 0.4330 0.3410 0.3305 0.0158  0.0296  0.0267  74  THR A N   
441  C CA  . THR A 61  ? 0.4645 0.3794 0.3569 0.0180  0.0318  0.0383  74  THR A CA  
442  C C   . THR A 61  ? 0.5379 0.4579 0.4078 0.0163  0.0324  0.0386  74  THR A C   
443  O O   . THR A 61  ? 0.5293 0.4584 0.3889 0.0179  0.0297  0.0462  74  THR A O   
444  C CB  . THR A 61  ? 0.5504 0.4610 0.4577 0.0212  0.0406  0.0454  74  THR A CB  
445  O OG1 . THR A 61  ? 0.4868 0.3925 0.3920 0.0201  0.0477  0.0407  74  THR A OG1 
446  C CG2 . THR A 61  ? 0.4797 0.3860 0.4106 0.0227  0.0397  0.0431  74  THR A CG2 
447  N N   . GLU A 62  ? 0.4418 0.3571 0.3038 0.0139  0.0355  0.0299  75  GLU A N   
448  C CA  . GLU A 62  ? 0.4924 0.4125 0.3329 0.0121  0.0363  0.0277  75  GLU A CA  
449  C C   . GLU A 62  ? 0.4515 0.3681 0.2845 0.0076  0.0320  0.0144  75  GLU A C   
450  O O   . GLU A 62  ? 0.4490 0.3562 0.2916 0.0069  0.0328  0.0073  75  GLU A O   
451  C CB  . GLU A 62  ? 0.5435 0.4608 0.3807 0.0138  0.0468  0.0302  75  GLU A CB  
452  C CG  . GLU A 62  ? 0.5125 0.4365 0.3419 0.0175  0.0513  0.0441  75  GLU A CG  
453  C CD  . GLU A 62  ? 0.5118 0.4468 0.3160 0.0173  0.0468  0.0448  75  GLU A CD  
454  O OE1 . GLU A 62  ? 0.5228 0.4599 0.3171 0.0132  0.0410  0.0331  75  GLU A OE1 
455  O OE2 . GLU A 62  ? 0.5077 0.4493 0.3020 0.0213  0.0492  0.0569  75  GLU A OE2 
456  N N   . GLU A 63  ? 0.4999 0.4243 0.3162 0.0047  0.0274  0.0110  76  GLU A N   
457  C CA  . GLU A 63  ? 0.5109 0.4317 0.3214 -0.0004 0.0234  -0.0015 76  GLU A CA  
458  C C   . GLU A 63  ? 0.4685 0.3789 0.2761 -0.0011 0.0297  -0.0102 76  GLU A C   
459  O O   . GLU A 63  ? 0.5046 0.4165 0.3045 0.0006  0.0360  -0.0092 76  GLU A O   
460  C CB  . GLU A 63  ? 0.5424 0.4755 0.3370 -0.0036 0.0175  -0.0046 76  GLU A CB  
461  C CG  . GLU A 63  ? 0.7711 0.7152 0.5510 -0.0002 0.0195  0.0026  76  GLU A CG  
462  C CD  . GLU A 63  ? 1.0223 0.9827 0.7910 -0.0013 0.0108  0.0027  76  GLU A CD  
463  O OE1 . GLU A 63  ? 0.8472 0.8122 0.6257 -0.0025 0.0039  0.0035  76  GLU A OE1 
464  O OE2 . GLU A 63  ? 1.0530 1.0227 0.8032 -0.0006 0.0108  0.0013  76  GLU A OE2 
465  N N   . GLU A 64  ? 0.3580 0.2577 0.1719 -0.0031 0.0283  -0.0183 77  GLU A N   
466  C CA  . GLU A 64  ? 0.4259 0.3148 0.2391 -0.0029 0.0333  -0.0270 77  GLU A CA  
467  C C   . GLU A 64  ? 0.4104 0.2954 0.2127 -0.0081 0.0308  -0.0380 77  GLU A C   
468  O O   . GLU A 64  ? 0.4001 0.2892 0.1996 -0.0123 0.0250  -0.0395 77  GLU A O   
469  C CB  . GLU A 64  ? 0.4162 0.2944 0.2455 0.0004  0.0339  -0.0275 77  GLU A CB  
470  C CG  . GLU A 64  ? 0.4617 0.3430 0.3056 0.0050  0.0365  -0.0191 77  GLU A CG  
471  C CD  . GLU A 64  ? 0.4612 0.3347 0.3206 0.0082  0.0348  -0.0211 77  GLU A CD  
472  O OE1 . GLU A 64  ? 0.3967 0.2648 0.2547 0.0069  0.0299  -0.0246 77  GLU A OE1 
473  O OE2 . GLU A 64  ? 0.4747 0.3481 0.3477 0.0120  0.0385  -0.0194 77  GLU A OE2 
474  N N   . ASP A 65  ? 0.3883 0.2654 0.1862 -0.0080 0.0358  -0.0463 78  ASP A N   
475  C CA  . ASP A 65  ? 0.4196 0.2905 0.2096 -0.0128 0.0348  -0.0577 78  ASP A CA  
476  C C   . ASP A 65  ? 0.4223 0.2833 0.2244 -0.0139 0.0313  -0.0591 78  ASP A C   
477  O O   . ASP A 65  ? 0.3812 0.2421 0.1852 -0.0185 0.0288  -0.0648 78  ASP A O   
478  C CB  . ASP A 65  ? 0.4556 0.3250 0.2472 -0.0108 0.0403  -0.0641 78  ASP A CB  
479  C CG  . ASP A 65  ? 0.5815 0.4512 0.3750 -0.0147 0.0381  -0.0737 78  ASP A CG  
480  O OD1 . ASP A 65  ? 0.5551 0.4349 0.3403 -0.0191 0.0346  -0.0773 78  ASP A OD1 
481  O OD2 . ASP A 65  ? 0.6673 0.5276 0.4712 -0.0129 0.0397  -0.0776 78  ASP A OD2 
482  N N   . THR A 66  ? 0.4675 0.3207 0.2779 -0.0095 0.0314  -0.0540 79  THR A N   
483  C CA  . THR A 66  ? 0.4293 0.2748 0.2502 -0.0094 0.0284  -0.0533 79  THR A CA  
484  C C   . THR A 66  ? 0.4115 0.2593 0.2302 -0.0128 0.0240  -0.0496 79  THR A C   
485  O O   . THR A 66  ? 0.3724 0.2139 0.1976 -0.0131 0.0223  -0.0486 79  THR A O   
486  C CB  . THR A 66  ? 0.3971 0.2367 0.2301 -0.0021 0.0296  -0.0500 79  THR A CB  
487  O OG1 . THR A 66  ? 0.3651 0.2092 0.2004 0.0012  0.0300  -0.0444 79  THR A OG1 
488  C CG2 . THR A 66  ? 0.4035 0.2422 0.2417 0.0013  0.0334  -0.0543 79  THR A CG2 
489  N N   . TRP A 67  ? 0.3605 0.2237 0.1776 -0.0145 0.0213  -0.0448 80  TRP A N   
490  C CA  . TRP A 67  ? 0.3523 0.2236 0.1741 -0.0168 0.0163  -0.0399 80  TRP A CA  
491  C C   . TRP A 67  ? 0.3801 0.2494 0.1982 -0.0242 0.0143  -0.0468 80  TRP A C   
492  O O   . TRP A 67  ? 0.3394 0.2076 0.1491 -0.0287 0.0153  -0.0552 80  TRP A O   
493  C CB  . TRP A 67  ? 0.3560 0.2443 0.1764 -0.0159 0.0138  -0.0332 80  TRP A CB  
494  C CG  . TRP A 67  ? 0.3911 0.2818 0.2206 -0.0095 0.0155  -0.0239 80  TRP A CG  
495  C CD1 . TRP A 67  ? 0.4297 0.3112 0.2672 -0.0048 0.0194  -0.0233 80  TRP A CD1 
496  C CD2 . TRP A 67  ? 0.4361 0.3393 0.2692 -0.0070 0.0135  -0.0145 80  TRP A CD2 
497  N NE1 . TRP A 67  ? 0.3974 0.2848 0.2445 -0.0005 0.0204  -0.0150 80  TRP A NE1 
498  C CE2 . TRP A 67  ? 0.3751 0.2746 0.2193 -0.0016 0.0172  -0.0088 80  TRP A CE2 
499  C CE3 . TRP A 67  ? 0.4266 0.3439 0.2556 -0.0084 0.0087  -0.0105 80  TRP A CE3 
500  C CZ2 . TRP A 67  ? 0.3530 0.2603 0.2045 0.0020  0.0175  0.0012  80  TRP A CZ2 
501  C CZ3 . TRP A 67  ? 0.4184 0.3440 0.2534 -0.0038 0.0083  0.0003  80  TRP A CZ3 
502  C CH2 . TRP A 67  ? 0.4138 0.3333 0.2600 0.0012  0.0131  0.0063  80  TRP A CH2 
503  N N   . GLN A 68  ? 0.3425 0.2115 0.1678 -0.0257 0.0120  -0.0438 81  GLN A N   
504  C CA  . GLN A 68  ? 0.3394 0.2096 0.1646 -0.0335 0.0104  -0.0491 81  GLN A CA  
505  C C   . GLN A 68  ? 0.3319 0.2154 0.1656 -0.0338 0.0062  -0.0429 81  GLN A C   
506  O O   . GLN A 68  ? 0.3003 0.1794 0.1412 -0.0304 0.0068  -0.0376 81  GLN A O   
507  C CB  . GLN A 68  ? 0.3142 0.1649 0.1397 -0.0353 0.0147  -0.0530 81  GLN A CB  
508  C CG  . GLN A 68  ? 0.4001 0.2421 0.2246 -0.0339 0.0185  -0.0578 81  GLN A CG  
509  C CD  . GLN A 68  ? 0.4194 0.2481 0.2498 -0.0347 0.0221  -0.0584 81  GLN A CD  
510  O OE1 . GLN A 68  ? 0.4297 0.2551 0.2619 -0.0397 0.0227  -0.0583 81  GLN A OE1 
511  N NE2 . GLN A 68  ? 0.3903 0.2113 0.2232 -0.0298 0.0248  -0.0586 81  GLN A NE2 
512  N N   . LYS A 69  ? 0.3454 0.2461 0.1783 -0.0374 0.0016  -0.0442 82  LYS A N   
513  C CA  . LYS A 69  ? 0.3610 0.2763 0.2031 -0.0375 -0.0029 -0.0390 82  LYS A CA  
514  C C   . LYS A 69  ? 0.3608 0.2792 0.2077 -0.0461 -0.0038 -0.0461 82  LYS A C   
515  O O   . LYS A 69  ? 0.3944 0.3161 0.2367 -0.0525 -0.0047 -0.0553 82  LYS A O   
516  C CB  . LYS A 69  ? 0.3707 0.3047 0.2100 -0.0343 -0.0080 -0.0345 82  LYS A CB  
517  C CG  . LYS A 69  ? 0.4075 0.3407 0.2479 -0.0257 -0.0066 -0.0243 82  LYS A CG  
518  C CD  . LYS A 69  ? 0.4085 0.3600 0.2507 -0.0219 -0.0117 -0.0166 82  LYS A CD  
519  C CE  . LYS A 69  ? 0.5367 0.4863 0.3786 -0.0142 -0.0088 -0.0067 82  LYS A CE  
520  N NZ  . LYS A 69  ? 0.5439 0.4816 0.3977 -0.0105 -0.0049 -0.0029 82  LYS A NZ  
521  N N   . LEU A 70  ? 0.3482 0.2662 0.2053 -0.0464 -0.0030 -0.0426 83  LEU A N   
522  C CA  . LEU A 70  ? 0.3328 0.2527 0.1970 -0.0548 -0.0020 -0.0484 83  LEU A CA  
523  C C   . LEU A 70  ? 0.3675 0.3036 0.2442 -0.0537 -0.0054 -0.0436 83  LEU A C   
524  O O   . LEU A 70  ? 0.2702 0.2067 0.1507 -0.0464 -0.0058 -0.0353 83  LEU A O   
525  C CB  . LEU A 70  ? 0.4044 0.3021 0.2674 -0.0569 0.0056  -0.0497 83  LEU A CB  
526  C CG  . LEU A 70  ? 0.4221 0.3005 0.2744 -0.0565 0.0100  -0.0537 83  LEU A CG  
527  C CD1 . LEU A 70  ? 0.4326 0.3023 0.2800 -0.0465 0.0107  -0.0469 83  LEU A CD1 
528  C CD2 . LEU A 70  ? 0.4725 0.3327 0.3252 -0.0622 0.0170  -0.0575 83  LEU A CD2 
529  N N   . GLU A 71  ? 0.3960 0.3457 0.2807 -0.0611 -0.0079 -0.0498 84  GLU A N   
530  C CA  . GLU A 71  ? 0.3511 0.3176 0.2496 -0.0606 -0.0110 -0.0467 84  GLU A CA  
531  C C   . GLU A 71  ? 0.3600 0.3166 0.2665 -0.0644 -0.0039 -0.0467 84  GLU A C   
532  O O   . GLU A 71  ? 0.3274 0.2709 0.2319 -0.0717 0.0022  -0.0526 84  GLU A O   
533  C CB  . GLU A 71  ? 0.3715 0.3609 0.2766 -0.0662 -0.0178 -0.0540 84  GLU A CB  
534  C CG  . GLU A 71  ? 0.5033 0.5020 0.3968 -0.0635 -0.0242 -0.0558 84  GLU A CG  
535  C CD  . GLU A 71  ? 0.4916 0.4874 0.3791 -0.0724 -0.0235 -0.0688 84  GLU A CD  
536  O OE1 . GLU A 71  ? 0.5762 0.5798 0.4745 -0.0815 -0.0236 -0.0784 84  GLU A OE1 
537  O OE2 . GLU A 71  ? 0.5374 0.5232 0.4106 -0.0706 -0.0223 -0.0703 84  GLU A OE2 
538  N N   . VAL A 72  ? 0.3288 0.2910 0.2439 -0.0592 -0.0039 -0.0399 85  VAL A N   
539  C CA  . VAL A 72  ? 0.3395 0.2952 0.2616 -0.0621 0.0030  -0.0395 85  VAL A CA  
540  C C   . VAL A 72  ? 0.3594 0.3323 0.2963 -0.0707 0.0025  -0.0459 85  VAL A C   
541  O O   . VAL A 72  ? 0.3566 0.3515 0.3035 -0.0692 -0.0047 -0.0463 85  VAL A O   
542  C CB  . VAL A 72  ? 0.3398 0.2957 0.2656 -0.0529 0.0033  -0.0313 85  VAL A CB  
543  C CG1 . VAL A 72  ? 0.2945 0.2462 0.2265 -0.0557 0.0106  -0.0312 85  VAL A CG1 
544  C CG2 . VAL A 72  ? 0.2887 0.2284 0.2023 -0.0452 0.0040  -0.0265 85  VAL A CG2 
545  N N   . ILE A 73  ? 0.3137 0.2764 0.2528 -0.0795 0.0105  -0.0510 86  ILE A N   
546  C CA  . ILE A 73  ? 0.3773 0.3556 0.3329 -0.0892 0.0116  -0.0585 86  ILE A CA  
547  C C   . ILE A 73  ? 0.4087 0.3881 0.3750 -0.0899 0.0189  -0.0552 86  ILE A C   
548  O O   . ILE A 73  ? 0.3915 0.3885 0.3753 -0.0963 0.0193  -0.0605 86  ILE A O   
549  C CB  . ILE A 73  ? 0.3489 0.3173 0.3033 -0.1006 0.0164  -0.0683 86  ILE A CB  
550  C CG1 . ILE A 73  ? 0.4975 0.4907 0.4678 -0.1091 0.0106  -0.0794 86  ILE A CG1 
551  C CG2 . ILE A 73  ? 0.4495 0.3977 0.4044 -0.1062 0.0296  -0.0671 86  ILE A CG2 
552  C CD1 . ILE A 73  ? 0.6286 0.6133 0.6001 -0.1210 0.0149  -0.0911 86  ILE A CD1 
553  N N   . LYS A 74  ? 0.3392 0.3019 0.2960 -0.0832 0.0245  -0.0473 87  LYS A N   
554  C CA  . LYS A 74  ? 0.3798 0.3431 0.3439 -0.0830 0.0319  -0.0442 87  LYS A CA  
555  C C   . LYS A 74  ? 0.3144 0.2673 0.2677 -0.0714 0.0321  -0.0357 87  LYS A C   
556  O O   . LYS A 74  ? 0.3240 0.2587 0.2613 -0.0668 0.0324  -0.0326 87  LYS A O   
557  C CB  . LYS A 74  ? 0.3897 0.3377 0.3529 -0.0925 0.0443  -0.0466 87  LYS A CB  
558  C CG  . LYS A 74  ? 0.4057 0.3552 0.3757 -0.0929 0.0534  -0.0435 87  LYS A CG  
559  C CD  . LYS A 74  ? 0.4674 0.4459 0.4596 -0.0943 0.0491  -0.0473 87  LYS A CD  
560  C CE  . LYS A 74  ? 0.4549 0.4361 0.4549 -0.0948 0.0592  -0.0450 87  LYS A CE  
561  N NZ  . LYS A 74  ? 0.4499 0.4601 0.4734 -0.0952 0.0549  -0.0491 87  LYS A NZ  
562  N N   . GLN A 75  ? 0.3159 0.2815 0.2794 -0.0666 0.0319  -0.0332 88  GLN A N   
563  C CA  . GLN A 75  ? 0.2814 0.2401 0.2381 -0.0560 0.0322  -0.0272 88  GLN A CA  
564  C C   . GLN A 75  ? 0.2959 0.2503 0.2532 -0.0572 0.0425  -0.0262 88  GLN A C   
565  O O   . GLN A 75  ? 0.3094 0.2802 0.2823 -0.0593 0.0445  -0.0282 88  GLN A O   
566  C CB  . GLN A 75  ? 0.2835 0.2598 0.2514 -0.0484 0.0235  -0.0253 88  GLN A CB  
567  C CG  . GLN A 75  ? 0.3144 0.2968 0.2812 -0.0470 0.0141  -0.0252 88  GLN A CG  
568  C CD  . GLN A 75  ? 0.4114 0.4098 0.3896 -0.0390 0.0066  -0.0217 88  GLN A CD  
569  O OE1 . GLN A 75  ? 0.3349 0.3312 0.3157 -0.0315 0.0075  -0.0182 88  GLN A OE1 
570  N NE2 . GLN A 75  ? 0.4489 0.4633 0.4339 -0.0402 -0.0008 -0.0227 88  GLN A NE2 
571  N N   . PHE A 76  ? 0.2780 0.2109 0.2179 -0.0553 0.0492  -0.0230 89  PHE A N   
572  C CA  . PHE A 76  ? 0.3096 0.2357 0.2452 -0.0559 0.0601  -0.0209 89  PHE A CA  
573  C C   . PHE A 76  ? 0.2854 0.2098 0.2136 -0.0441 0.0584  -0.0176 89  PHE A C   
574  O O   . PHE A 76  ? 0.2661 0.1739 0.1768 -0.0377 0.0587  -0.0144 89  PHE A O   
575  C CB  . PHE A 76  ? 0.3169 0.2199 0.2371 -0.0608 0.0691  -0.0187 89  PHE A CB  
576  C CG  . PHE A 76  ? 0.4065 0.3029 0.3230 -0.0638 0.0823  -0.0160 89  PHE A CG  
577  C CD1 . PHE A 76  ? 0.4315 0.3441 0.3595 -0.0630 0.0859  -0.0170 89  PHE A CD1 
578  C CD2 . PHE A 76  ? 0.5192 0.3925 0.4205 -0.0669 0.0921  -0.0121 89  PHE A CD2 
579  C CE1 . PHE A 76  ? 0.4474 0.3541 0.3710 -0.0657 0.0993  -0.0143 89  PHE A CE1 
580  C CE2 . PHE A 76  ? 0.5731 0.4391 0.4694 -0.0694 0.1056  -0.0082 89  PHE A CE2 
581  C CZ  . PHE A 76  ? 0.4813 0.3644 0.3883 -0.0689 0.1094  -0.0093 89  PHE A CZ  
582  N N   . ARG A 77  ? 0.2852 0.2277 0.2283 -0.0409 0.0563  -0.0193 90  ARG A N   
583  C CA  . ARG A 77  ? 0.3130 0.2556 0.2519 -0.0307 0.0560  -0.0182 90  ARG A CA  
584  C C   . ARG A 77  ? 0.3027 0.2354 0.2287 -0.0304 0.0674  -0.0164 90  ARG A C   
585  O O   . ARG A 77  ? 0.3047 0.2363 0.2323 -0.0388 0.0767  -0.0161 90  ARG A O   
586  C CB  . ARG A 77  ? 0.2607 0.2249 0.2207 -0.0276 0.0518  -0.0210 90  ARG A CB  
587  C CG  . ARG A 77  ? 0.3758 0.3450 0.3422 -0.0209 0.0408  -0.0206 90  ARG A CG  
588  C CD  . ARG A 77  ? 0.4156 0.4027 0.4009 -0.0245 0.0347  -0.0215 90  ARG A CD  
589  N NE  . ARG A 77  ? 0.4632 0.4685 0.4676 -0.0236 0.0365  -0.0240 90  ARG A NE  
590  C CZ  . ARG A 77  ? 0.5702 0.5852 0.5873 -0.0157 0.0321  -0.0239 90  ARG A CZ  
591  N NH1 . ARG A 77  ? 0.5055 0.5136 0.5189 -0.0084 0.0261  -0.0216 90  ARG A NH1 
592  N NH2 . ARG A 77  ? 0.5258 0.5575 0.5613 -0.0151 0.0343  -0.0266 90  ARG A NH2 
593  N N   . HIS A 78  ? 0.2725 0.1983 0.1855 -0.0206 0.0668  -0.0153 91  HIS A N   
594  C CA  . HIS A 78  ? 0.3205 0.2391 0.2194 -0.0183 0.0770  -0.0134 91  HIS A CA  
595  C C   . HIS A 78  ? 0.3231 0.2590 0.2380 -0.0216 0.0837  -0.0165 91  HIS A C   
596  O O   . HIS A 78  ? 0.2944 0.2474 0.2277 -0.0189 0.0778  -0.0208 91  HIS A O   
597  C CB  . HIS A 78  ? 0.3562 0.2685 0.2400 -0.0060 0.0729  -0.0136 91  HIS A CB  
598  C CG  . HIS A 78  ? 0.3529 0.2547 0.2153 -0.0021 0.0825  -0.0104 91  HIS A CG  
599  N ND1 . HIS A 78  ? 0.3596 0.2711 0.2235 -0.0005 0.0900  -0.0125 91  HIS A ND1 
600  C CD2 . HIS A 78  ? 0.4029 0.2853 0.2410 0.0013  0.0859  -0.0048 91  HIS A CD2 
601  C CE1 . HIS A 78  ? 0.4081 0.3068 0.2480 0.0036  0.0979  -0.0080 91  HIS A CE1 
602  N NE2 . HIS A 78  ? 0.4448 0.3254 0.2687 0.0051  0.0954  -0.0028 91  HIS A NE2 
603  N N   . PRO A 79  ? 0.3259 0.2578 0.2355 -0.0275 0.0965  -0.0143 92  PRO A N   
604  C CA  . PRO A 79  ? 0.3185 0.2686 0.2469 -0.0323 0.1038  -0.0180 92  PRO A CA  
605  C C   . PRO A 79  ? 0.3077 0.2702 0.2403 -0.0230 0.1029  -0.0221 92  PRO A C   
606  O O   . PRO A 79  ? 0.3418 0.3232 0.2958 -0.0253 0.1050  -0.0266 92  PRO A O   
607  C CB  . PRO A 79  ? 0.4153 0.3538 0.3323 -0.0395 0.1195  -0.0136 92  PRO A CB  
608  C CG  . PRO A 79  ? 0.3733 0.2872 0.2606 -0.0336 0.1203  -0.0070 92  PRO A CG  
609  C CD  . PRO A 79  ? 0.3334 0.2435 0.2209 -0.0301 0.1058  -0.0080 92  PRO A CD  
610  N N   . LYS A 80  ? 0.3240 0.2775 0.2382 -0.0125 0.0996  -0.0216 93  LYS A N   
611  C CA  . LYS A 80  ? 0.3095 0.2744 0.2276 -0.0035 0.0986  -0.0272 93  LYS A CA  
612  C C   . LYS A 80  ? 0.2805 0.2509 0.2095 0.0037  0.0848  -0.0314 93  LYS A C   
613  O O   . LYS A 80  ? 0.2705 0.2458 0.1993 0.0124  0.0825  -0.0367 93  LYS A O   
614  C CB  . LYS A 80  ? 0.3190 0.2725 0.2094 0.0037  0.1055  -0.0255 93  LYS A CB  
615  C CG  . LYS A 80  ? 0.4116 0.3641 0.2946 -0.0019 0.1218  -0.0222 93  LYS A CG  
616  C CD  . LYS A 80  ? 0.5564 0.4916 0.4057 0.0043  0.1287  -0.0164 93  LYS A CD  
617  C CE  . LYS A 80  ? 0.6272 0.5598 0.4690 -0.0019 0.1468  -0.0117 93  LYS A CE  
618  N NZ  . LYS A 80  ? 0.6648 0.5776 0.4713 0.0039  0.1543  -0.0032 93  LYS A NZ  
619  N N   . TYR A 81  ? 0.2586 0.2284 0.1974 0.0001  0.0763  -0.0296 94  TYR A N   
620  C CA  . TYR A 81  ? 0.2482 0.2222 0.1980 0.0063  0.0646  -0.0322 94  TYR A CA  
621  C C   . TYR A 81  ? 0.2748 0.2674 0.2490 0.0091  0.0634  -0.0375 94  TYR A C   
622  O O   . TYR A 81  ? 0.2287 0.2342 0.2189 0.0036  0.0674  -0.0381 94  TYR A O   
623  C CB  . TYR A 81  ? 0.3022 0.2727 0.2566 0.0013  0.0573  -0.0284 94  TYR A CB  
624  C CG  . TYR A 81  ? 0.2721 0.2485 0.2410 0.0063  0.0469  -0.0298 94  TYR A CG  
625  C CD1 . TYR A 81  ? 0.2349 0.2043 0.1978 0.0145  0.0418  -0.0318 94  TYR A CD1 
626  C CD2 . TYR A 81  ? 0.2651 0.2543 0.2540 0.0031  0.0425  -0.0289 94  TYR A CD2 
627  C CE1 . TYR A 81  ? 0.2416 0.2152 0.2190 0.0186  0.0340  -0.0325 94  TYR A CE1 
628  C CE2 . TYR A 81  ? 0.2643 0.2574 0.2652 0.0082  0.0342  -0.0284 94  TYR A CE2 
629  C CZ  . TYR A 81  ? 0.2789 0.2633 0.2745 0.0154  0.0307  -0.0300 94  TYR A CZ  
630  O OH  . TYR A 81  ? 0.2981 0.2851 0.3069 0.0199  0.0240  -0.0290 94  TYR A OH  
631  N N   . ASN A 82  ? 0.2270 0.2211 0.2054 0.0180  0.0579  -0.0421 95  ASN A N   
632  C CA  . ASN A 82  ? 0.2388 0.2479 0.2409 0.0222  0.0563  -0.0474 95  ASN A CA  
633  C C   . ASN A 82  ? 0.2163 0.2267 0.2338 0.0243  0.0462  -0.0454 95  ASN A C   
634  O O   . ASN A 82  ? 0.1988 0.1988 0.2085 0.0280  0.0405  -0.0450 95  ASN A O   
635  C CB  . ASN A 82  ? 0.2343 0.2441 0.2317 0.0306  0.0588  -0.0552 95  ASN A CB  
636  C CG  . ASN A 82  ? 0.2157 0.2408 0.2383 0.0347  0.0594  -0.0617 95  ASN A CG  
637  O OD1 . ASN A 82  ? 0.2038 0.2320 0.2447 0.0383  0.0524  -0.0627 95  ASN A OD1 
638  N ND2 . ASN A 82  ? 0.2242 0.2584 0.2480 0.0344  0.0687  -0.0659 95  ASN A ND2 
639  N N   . THR A 83  ? 0.2166 0.2402 0.2560 0.0223  0.0443  -0.0439 96  THR A N   
640  C CA  . THR A 83  ? 0.2443 0.2688 0.2956 0.0236  0.0355  -0.0396 96  THR A CA  
641  C C   . THR A 83  ? 0.2496 0.2723 0.3123 0.0323  0.0313  -0.0426 96  THR A C   
642  O O   . THR A 83  ? 0.2824 0.3010 0.3501 0.0339  0.0250  -0.0383 96  THR A O   
643  C CB  . THR A 83  ? 0.2503 0.2908 0.3211 0.0203  0.0340  -0.0369 96  THR A CB  
644  O OG1 . THR A 83  ? 0.2816 0.3353 0.3674 0.0223  0.0398  -0.0422 96  THR A OG1 
645  C CG2 . THR A 83  ? 0.2515 0.2920 0.3127 0.0107  0.0353  -0.0334 96  THR A CG2 
646  N N   . SER A 84  ? 0.2326 0.2582 0.3000 0.0376  0.0352  -0.0504 97  SER A N   
647  C CA  . SER A 84  ? 0.1877 0.2114 0.2685 0.0453  0.0319  -0.0552 97  SER A CA  
648  C C   . SER A 84  ? 0.2478 0.2612 0.3132 0.0490  0.0319  -0.0619 97  SER A C   
649  O O   . SER A 84  ? 0.2823 0.2884 0.3513 0.0522  0.0269  -0.0629 97  SER A O   
650  C CB  . SER A 84  ? 0.2093 0.2460 0.3129 0.0497  0.0353  -0.0610 97  SER A CB  
651  O OG  . SER A 84  ? 0.2637 0.3100 0.3640 0.0462  0.0424  -0.0631 97  SER A OG  
652  N N   . THR A 85  ? 0.2224 0.2356 0.2705 0.0489  0.0374  -0.0667 98  THR A N   
653  C CA  . THR A 85  ? 0.2491 0.2542 0.2805 0.0536  0.0363  -0.0734 98  THR A CA  
654  C C   . THR A 85  ? 0.2506 0.2427 0.2604 0.0510  0.0329  -0.0674 98  THR A C   
655  O O   . THR A 85  ? 0.2457 0.2314 0.2437 0.0556  0.0299  -0.0723 98  THR A O   
656  C CB  . THR A 85  ? 0.2476 0.2574 0.2660 0.0558  0.0437  -0.0799 98  THR A CB  
657  O OG1 . THR A 85  ? 0.2451 0.2515 0.2439 0.0498  0.0493  -0.0726 98  THR A OG1 
658  C CG2 . THR A 85  ? 0.2464 0.2700 0.2868 0.0577  0.0483  -0.0858 98  THR A CG2 
659  N N   . LEU A 86  ? 0.2279 0.2171 0.2333 0.0440  0.0330  -0.0579 99  LEU A N   
660  C CA  . LEU A 86  ? 0.2232 0.1999 0.2105 0.0411  0.0301  -0.0520 99  LEU A CA  
661  C C   . LEU A 86  ? 0.2479 0.2162 0.2087 0.0428  0.0336  -0.0531 99  LEU A C   
662  O O   . LEU A 86  ? 0.2207 0.1779 0.1667 0.0439  0.0302  -0.0510 99  LEU A O   
663  C CB  . LEU A 86  ? 0.2584 0.2294 0.2527 0.0443  0.0226  -0.0525 99  LEU A CB  
664  C CG  . LEU A 86  ? 0.2949 0.2707 0.3116 0.0430  0.0191  -0.0484 99  LEU A CG  
665  C CD1 . LEU A 86  ? 0.2268 0.1936 0.2419 0.0431  0.0139  -0.0451 99  LEU A CD1 
666  C CD2 . LEU A 86  ? 0.2863 0.2693 0.3078 0.0368  0.0212  -0.0416 99  LEU A CD2 
667  N N   . HIS A 87  ? 0.2502 0.2234 0.2042 0.0436  0.0408  -0.0560 100 HIS A N   
668  C CA  . HIS A 87  ? 0.2532 0.2176 0.1796 0.0449  0.0456  -0.0543 100 HIS A CA  
669  C C   . HIS A 87  ? 0.2784 0.2336 0.1939 0.0366  0.0495  -0.0445 100 HIS A C   
670  O O   . HIS A 87  ? 0.2942 0.2555 0.2228 0.0290  0.0525  -0.0411 100 HIS A O   
671  C CB  . HIS A 87  ? 0.2746 0.2470 0.1962 0.0477  0.0538  -0.0593 100 HIS A CB  
672  C CG  . HIS A 87  ? 0.3320 0.3112 0.2580 0.0568  0.0503  -0.0707 100 HIS A CG  
673  N ND1 . HIS A 87  ? 0.3449 0.3309 0.2624 0.0614  0.0567  -0.0772 100 HIS A ND1 
674  C CD2 . HIS A 87  ? 0.3486 0.3292 0.2876 0.0619  0.0416  -0.0776 100 HIS A CD2 
675  C CE1 . HIS A 87  ? 0.4289 0.4205 0.3538 0.0691  0.0512  -0.0886 100 HIS A CE1 
676  N NE2 . HIS A 87  ? 0.3762 0.3644 0.3152 0.0692  0.0422  -0.0890 100 HIS A NE2 
677  N N   . HIS A 88  ? 0.2626 0.2036 0.1550 0.0383  0.0492  -0.0406 101 HIS A N   
678  C CA  . HIS A 88  ? 0.3215 0.2508 0.2033 0.0310  0.0525  -0.0321 101 HIS A CA  
679  C C   . HIS A 88  ? 0.2694 0.2004 0.1680 0.0250  0.0465  -0.0299 101 HIS A C   
680  O O   . HIS A 88  ? 0.2514 0.1847 0.1571 0.0164  0.0499  -0.0262 101 HIS A O   
681  C CB  . HIS A 88  ? 0.3061 0.2363 0.1832 0.0244  0.0644  -0.0283 101 HIS A CB  
682  C CG  . HIS A 88  ? 0.3352 0.2677 0.1986 0.0303  0.0714  -0.0309 101 HIS A CG  
683  N ND1 . HIS A 88  ? 0.3223 0.2429 0.1587 0.0376  0.0727  -0.0288 101 HIS A ND1 
684  C CD2 . HIS A 88  ? 0.3248 0.2707 0.1972 0.0306  0.0776  -0.0356 101 HIS A CD2 
685  C CE1 . HIS A 88  ? 0.3518 0.2785 0.1794 0.0422  0.0794  -0.0320 101 HIS A CE1 
686  N NE2 . HIS A 88  ? 0.4203 0.3623 0.2699 0.0378  0.0829  -0.0365 101 HIS A NE2 
687  N N   . ASP A 89  ? 0.2595 0.1902 0.1647 0.0299  0.0377  -0.0326 102 ASP A N   
688  C CA  . ASP A 89  ? 0.2616 0.1941 0.1812 0.0259  0.0319  -0.0304 102 ASP A CA  
689  C C   . ASP A 89  ? 0.2838 0.2020 0.1885 0.0229  0.0308  -0.0255 102 ASP A C   
690  O O   . ASP A 89  ? 0.2648 0.1764 0.1656 0.0271  0.0253  -0.0262 102 ASP A O   
691  C CB  . ASP A 89  ? 0.2427 0.1807 0.1771 0.0321  0.0248  -0.0353 102 ASP A CB  
692  C CG  . ASP A 89  ? 0.2739 0.2151 0.2237 0.0286  0.0202  -0.0319 102 ASP A CG  
693  O OD1 . ASP A 89  ? 0.2286 0.1718 0.1797 0.0216  0.0216  -0.0271 102 ASP A OD1 
694  O OD2 . ASP A 89  ? 0.2454 0.1875 0.2059 0.0330  0.0152  -0.0342 102 ASP A OD2 
695  N N   . ILE A 90  ? 0.2493 0.1632 0.1474 0.0152  0.0367  -0.0211 103 ILE A N   
696  C CA  . ILE A 90  ? 0.2668 0.1662 0.1516 0.0115  0.0372  -0.0170 103 ILE A CA  
697  C C   . ILE A 90  ? 0.2650 0.1672 0.1565 0.0006  0.0413  -0.0147 103 ILE A C   
698  O O   . ILE A 90  ? 0.2510 0.1613 0.1489 -0.0039 0.0474  -0.0150 103 ILE A O   
699  C CB  . ILE A 90  ? 0.2889 0.1732 0.1503 0.0161  0.0418  -0.0146 103 ILE A CB  
700  C CG1 . ILE A 90  ? 0.3058 0.1735 0.1548 0.0135  0.0421  -0.0105 103 ILE A CG1 
701  C CG2 . ILE A 90  ? 0.3497 0.2350 0.2050 0.0133  0.0519  -0.0128 103 ILE A CG2 
702  C CD1 . ILE A 90  ? 0.3308 0.1826 0.1566 0.0201  0.0453  -0.0070 103 ILE A CD1 
703  N N   . MET A 91  ? 0.3258 0.1290 0.1377 -0.0295 0.0007  0.0222  104 MET A N   
704  C CA  . MET A 91  ? 0.3239 0.1217 0.1419 -0.0329 0.0067  0.0197  104 MET A CA  
705  C C   . MET A 91  ? 0.3257 0.1183 0.1492 -0.0296 0.0080  0.0219  104 MET A C   
706  O O   . MET A 91  ? 0.3226 0.1197 0.1504 -0.0259 0.0036  0.0227  104 MET A O   
707  C CB  . MET A 91  ? 0.3301 0.1362 0.1567 -0.0370 0.0065  0.0130  104 MET A CB  
708  C CG  . MET A 91  ? 0.3381 0.1411 0.1718 -0.0405 0.0118  0.0096  104 MET A CG  
709  S SD  . MET A 91  ? 0.3823 0.1963 0.2244 -0.0450 0.0118  0.0029  104 MET A SD  
710  C CE  . MET A 91  ? 0.3418 0.1658 0.1906 -0.0411 0.0053  0.0016  104 MET A CE  
711  N N   . LEU A 92  ? 0.3323 0.1152 0.1563 -0.0313 0.0146  0.0227  105 LEU A N   
712  C CA  . LEU A 92  ? 0.3646 0.1412 0.1947 -0.0292 0.0175  0.0238  105 LEU A CA  
713  C C   . LEU A 92  ? 0.3922 0.1715 0.2323 -0.0336 0.0200  0.0167  105 LEU A C   
714  O O   . LEU A 92  ? 0.3906 0.1701 0.2312 -0.0387 0.0233  0.0130  105 LEU A O   
715  C CB  . LEU A 92  ? 0.3872 0.1510 0.2122 -0.0281 0.0239  0.0291  105 LEU A CB  
716  C CG  . LEU A 92  ? 0.4563 0.2165 0.2719 -0.0222 0.0221  0.0376  105 LEU A CG  
717  C CD1 . LEU A 92  ? 0.4630 0.2105 0.2733 -0.0220 0.0297  0.0426  105 LEU A CD1 
718  C CD2 . LEU A 92  ? 0.4889 0.2507 0.3087 -0.0164 0.0186  0.0409  105 LEU A CD2 
719  N N   . LEU A 93  ? 0.3309 0.1127 0.1786 -0.0316 0.0184  0.0150  106 LEU A N   
720  C CA  . LEU A 93  ? 0.3438 0.1290 0.2005 -0.0351 0.0204  0.0083  106 LEU A CA  
721  C C   . LEU A 93  ? 0.3674 0.1430 0.2284 -0.0345 0.0257  0.0083  106 LEU A C   
722  O O   . LEU A 93  ? 0.3854 0.1568 0.2469 -0.0296 0.0250  0.0125  106 LEU A O   
723  C CB  . LEU A 93  ? 0.3079 0.1044 0.1707 -0.0333 0.0148  0.0054  106 LEU A CB  
724  C CG  . LEU A 93  ? 0.3161 0.1226 0.1768 -0.0338 0.0098  0.0046  106 LEU A CG  
725  C CD1 . LEU A 93  ? 0.3096 0.1260 0.1777 -0.0316 0.0053  0.0021  106 LEU A CD1 
726  C CD2 . LEU A 93  ? 0.3534 0.1626 0.2133 -0.0393 0.0126  0.0009  106 LEU A CD2 
727  N N   . LYS A 94  ? 0.3729 0.1453 0.2375 -0.0396 0.0311  0.0035  107 LYS A N   
728  C CA  . LYS A 94  ? 0.3760 0.1428 0.2472 -0.0397 0.0366  0.0018  107 LYS A CA  
729  C C   . LYS A 94  ? 0.3712 0.1461 0.2512 -0.0412 0.0354  -0.0051 107 LYS A C   
730  O O   . LYS A 94  ? 0.3530 0.1379 0.2365 -0.0452 0.0346  -0.0107 107 LYS A O   
731  C CB  . LYS A 94  ? 0.4045 0.1700 0.2780 -0.0433 0.0426  0.0004  107 LYS A CB  
732  C CG  . LYS A 94  ? 0.4676 0.2266 0.3475 -0.0424 0.0486  0.0003  107 LYS A CG  
733  C CD  . LYS A 94  ? 0.5261 0.2920 0.4162 -0.0459 0.0502  -0.0079 107 LYS A CD  
734  C CE  . LYS A 94  ? 0.5321 0.2912 0.4287 -0.0448 0.0560  -0.0083 107 LYS A CE  
735  N NZ  . LYS A 94  ? 0.6304 0.3829 0.5269 -0.0458 0.0619  -0.0058 107 LYS A NZ  
736  N N   . LEU A 95  ? 0.4024 0.1736 0.2859 -0.0375 0.0354  -0.0042 108 LEU A N   
737  C CA  . LEU A 95  ? 0.3758 0.1541 0.2669 -0.0383 0.0345  -0.0104 108 LEU A CA  
738  C C   . LEU A 95  ? 0.4286 0.2090 0.3275 -0.0419 0.0399  -0.0163 108 LEU A C   
739  O O   . LEU A 95  ? 0.4186 0.1916 0.3187 -0.0421 0.0450  -0.0145 108 LEU A O   
740  C CB  . LEU A 95  ? 0.3743 0.1478 0.2664 -0.0327 0.0327  -0.0072 108 LEU A CB  
741  C CG  . LEU A 95  ? 0.3767 0.1545 0.2645 -0.0274 0.0263  -0.0005 108 LEU A CG  
742  C CD1 . LEU A 95  ? 0.3827 0.1589 0.2741 -0.0213 0.0246  0.0031  108 LEU A CD1 
743  C CD2 . LEU A 95  ? 0.3094 0.1006 0.1972 -0.0289 0.0206  -0.0033 108 LEU A CD2 
744  N N   . LYS A 96  ? 0.4101 0.2010 0.3145 -0.0447 0.0388  -0.0233 109 LYS A N   
745  C CA  . LYS A 96  ? 0.4428 0.2373 0.3543 -0.0486 0.0431  -0.0296 109 LYS A CA  
746  C C   . LYS A 96  ? 0.4367 0.2226 0.3524 -0.0464 0.0474  -0.0293 109 LYS A C   
747  O O   . LYS A 96  ? 0.4959 0.2780 0.4151 -0.0488 0.0527  -0.0310 109 LYS A O   
748  C CB  . LYS A 96  ? 0.4830 0.2909 0.3986 -0.0509 0.0404  -0.0364 109 LYS A CB  
749  C CG  . LYS A 96  ? 0.5058 0.3178 0.4285 -0.0541 0.0440  -0.0434 109 LYS A CG  
750  C CD  . LYS A 96  ? 0.5549 0.3711 0.4797 -0.0591 0.0467  -0.0463 109 LYS A CD  
751  C CE  . LYS A 96  ? 0.5116 0.3420 0.4367 -0.0618 0.0431  -0.0496 109 LYS A CE  
752  N NZ  . LYS A 96  ? 0.5880 0.4284 0.5173 -0.0621 0.0414  -0.0556 109 LYS A NZ  
753  N N   . GLU A 97  ? 0.4367 0.2193 0.3525 -0.0419 0.0456  -0.0271 110 GLU A N   
754  C CA  . GLU A 97  ? 0.5049 0.2793 0.4249 -0.0391 0.0498  -0.0260 110 GLU A CA  
755  C C   . GLU A 97  ? 0.4773 0.2424 0.3930 -0.0329 0.0485  -0.0170 110 GLU A C   
756  O O   . GLU A 97  ? 0.4543 0.2198 0.3634 -0.0310 0.0439  -0.0124 110 GLU A O   
757  C CB  . GLU A 97  ? 0.4536 0.2336 0.3794 -0.0392 0.0496  -0.0323 110 GLU A CB  
758  C CG  . GLU A 97  ? 0.4286 0.2129 0.3526 -0.0356 0.0440  -0.0312 110 GLU A CG  
759  C CD  . GLU A 97  ? 0.5012 0.2974 0.4231 -0.0384 0.0395  -0.0349 110 GLU A CD  
760  O OE1 . GLU A 97  ? 0.5112 0.3128 0.4331 -0.0431 0.0403  -0.0379 110 GLU A OE1 
761  O OE2 . GLU A 97  ? 0.4868 0.2874 0.4078 -0.0358 0.0352  -0.0346 110 GLU A OE2 
762  N N   . LYS A 98  ? 0.4815 0.2387 0.4009 -0.0297 0.0527  -0.0144 111 LYS A N   
763  C CA  . LYS A 98  ? 0.4768 0.2264 0.3935 -0.0231 0.0517  -0.0054 111 LYS A CA  
764  C C   . LYS A 98  ? 0.4728 0.2253 0.3916 -0.0190 0.0477  -0.0052 111 LYS A C   
765  O O   . LYS A 98  ? 0.5214 0.2773 0.4463 -0.0201 0.0492  -0.0112 111 LYS A O   
766  C CB  . LYS A 98  ? 0.5177 0.2580 0.4383 -0.0209 0.0585  -0.0018 111 LYS A CB  
767  C CG  . LYS A 98  ? 0.5893 0.3242 0.5066 -0.0224 0.0624  0.0018  111 LYS A CG  
768  C CD  . LYS A 98  ? 0.6626 0.3893 0.5855 -0.0210 0.0701  0.0037  111 LYS A CD  
769  C CE  . LYS A 98  ? 0.7325 0.4529 0.6516 -0.0206 0.0739  0.0095  111 LYS A CE  
770  N NZ  . LYS A 98  ? 0.8441 0.5611 0.7560 -0.0142 0.0706  0.0202  111 LYS A NZ  
771  N N   . ALA A 99  ? 0.4136 0.1652 0.3271 -0.0143 0.0426  0.0016  112 ALA A N   
772  C CA  . ALA A 99  ? 0.4220 0.1759 0.3380 -0.0095 0.0389  0.0031  112 ALA A CA  
773  C C   . ALA A 99  ? 0.4457 0.1936 0.3680 -0.0048 0.0430  0.0069  112 ALA A C   
774  O O   . ALA A 99  ? 0.4723 0.2135 0.3953 -0.0040 0.0479  0.0107  112 ALA A O   
775  C CB  . ALA A 99  ? 0.4359 0.1951 0.3466 -0.0056 0.0313  0.0094  112 ALA A CB  
776  N N   . SER A 100 ? 0.4643 0.2151 0.3916 -0.0015 0.0413  0.0061  113 SER A N   
777  C CA  . SER A 100 ? 0.4471 0.1935 0.3810 0.0033  0.0449  0.0096  113 SER A CA  
778  C C   . SER A 100 ? 0.4393 0.1854 0.3718 0.0107  0.0403  0.0195  113 SER A C   
779  O O   . SER A 100 ? 0.4508 0.2026 0.3818 0.0128  0.0341  0.0201  113 SER A O   
780  C CB  . SER A 100 ? 0.4341 0.1844 0.3748 0.0024  0.0463  0.0025  113 SER A CB  
781  O OG  . SER A 100 ? 0.4476 0.1997 0.3893 -0.0043 0.0501  -0.0067 113 SER A OG  
782  N N   . LEU A 101 ? 0.4654 0.2058 0.3988 0.0147  0.0432  0.0271  114 LEU A N   
783  C CA  . LEU A 101 ? 0.4508 0.1925 0.3834 0.0220  0.0387  0.0370  114 LEU A CA  
784  C C   . LEU A 101 ? 0.4735 0.2185 0.4148 0.0263  0.0379  0.0373  114 LEU A C   
785  O O   . LEU A 101 ? 0.5155 0.2568 0.4635 0.0274  0.0435  0.0371  114 LEU A O   
786  C CB  . LEU A 101 ? 0.4914 0.2271 0.4225 0.0251  0.0423  0.0452  114 LEU A CB  
787  C CG  . LEU A 101 ? 0.5405 0.2732 0.4626 0.0220  0.0429  0.0467  114 LEU A CG  
788  C CD1 . LEU A 101 ? 0.5881 0.3156 0.5091 0.0263  0.0465  0.0558  114 LEU A CD1 
789  C CD2 . LEU A 101 ? 0.5244 0.2623 0.4374 0.0220  0.0348  0.0480  114 LEU A CD2 
790  N N   . THR A 102 ? 0.4307 0.1827 0.3719 0.0287  0.0313  0.0377  115 THR A N   
791  C CA  . THR A 102 ? 0.4602 0.2167 0.4100 0.0328  0.0301  0.0378  115 THR A CA  
792  C C   . THR A 102 ? 0.4686 0.2313 0.4188 0.0393  0.0229  0.0460  115 THR A C   
793  O O   . THR A 102 ? 0.4335 0.1964 0.3768 0.0412  0.0194  0.0522  115 THR A O   
794  C CB  . THR A 102 ? 0.4875 0.2485 0.4394 0.0291  0.0295  0.0285  115 THR A CB  
795  O OG1 . THR A 102 ? 0.3832 0.1521 0.3300 0.0276  0.0226  0.0271  115 THR A OG1 
796  C CG2 . THR A 102 ? 0.4414 0.1984 0.3928 0.0223  0.0358  0.0198  115 THR A CG2 
797  N N   . LEU A 103 ? 0.4539 0.2225 0.4121 0.0429  0.0207  0.0460  116 LEU A N   
798  C CA  . LEU A 103 ? 0.4413 0.2180 0.4011 0.0485  0.0132  0.0523  116 LEU A CA  
799  C C   . LEU A 103 ? 0.4628 0.2500 0.4171 0.0452  0.0057  0.0493  116 LEU A C   
800  O O   . LEU A 103 ? 0.4268 0.2223 0.3798 0.0480  -0.0012 0.0544  116 LEU A O   
801  C CB  . LEU A 103 ? 0.4879 0.2706 0.4587 0.0515  0.0124  0.0510  116 LEU A CB  
802  C CG  . LEU A 103 ? 0.6141 0.3985 0.5871 0.0476  0.0141  0.0415  116 LEU A CG  
803  C CD1 . LEU A 103 ? 0.6739 0.4681 0.6548 0.0512  0.0094  0.0417  116 LEU A CD1 
804  C CD2 . LEU A 103 ? 0.5269 0.3050 0.5032 0.0447  0.0220  0.0361  116 LEU A CD2 
805  N N   . ALA A 104 ? 0.4507 0.2395 0.4025 0.0388  0.0067  0.0406  117 ALA A N   
806  C CA  . ALA A 104 ? 0.3879 0.1880 0.3363 0.0352  0.0002  0.0369  117 ALA A CA  
807  C C   . ALA A 104 ? 0.4103 0.2080 0.3490 0.0303  0.0005  0.0356  117 ALA A C   
808  O O   . ALA A 104 ? 0.3928 0.1994 0.3279 0.0279  -0.0050 0.0341  117 ALA A O   
809  C CB  . ALA A 104 ? 0.4148 0.2205 0.3678 0.0321  0.0007  0.0287  117 ALA A CB  
810  N N   . VAL A 105 ? 0.4147 0.2007 0.3495 0.0285  0.0071  0.0360  118 VAL A N   
811  C CA  . VAL A 105 ? 0.4027 0.1853 0.3287 0.0238  0.0084  0.0349  118 VAL A CA  
812  C C   . VAL A 105 ? 0.4172 0.1908 0.3388 0.0274  0.0111  0.0434  118 VAL A C   
813  O O   . VAL A 105 ? 0.3539 0.1166 0.2785 0.0295  0.0179  0.0458  118 VAL A O   
814  C CB  . VAL A 105 ? 0.3894 0.1667 0.3151 0.0175  0.0146  0.0267  118 VAL A CB  
815  C CG1 . VAL A 105 ? 0.4296 0.2039 0.3469 0.0126  0.0158  0.0259  118 VAL A CG1 
816  C CG2 . VAL A 105 ? 0.3215 0.1084 0.2515 0.0148  0.0122  0.0191  118 VAL A CG2 
817  N N   . GLY A 106 ? 0.3370 0.1150 0.2514 0.0281  0.0062  0.0479  119 GLY A N   
818  C CA  . GLY A 106 ? 0.3513 0.1223 0.2604 0.0320  0.0083  0.0566  119 GLY A CA  
819  C C   . GLY A 106 ? 0.3870 0.1600 0.2858 0.0289  0.0059  0.0573  119 GLY A C   
820  O O   . GLY A 106 ? 0.3677 0.1489 0.2640 0.0245  0.0016  0.0517  119 GLY A O   
821  N N   . THR A 107 ? 0.4192 0.1843 0.3121 0.0317  0.0094  0.0647  120 THR A N   
822  C CA  . THR A 107 ? 0.4285 0.1935 0.3108 0.0293  0.0085  0.0663  120 THR A CA  
823  C C   . THR A 107 ? 0.4327 0.2071 0.3094 0.0343  0.0008  0.0733  120 THR A C   
824  O O   . THR A 107 ? 0.4687 0.2448 0.3485 0.0411  -0.0009 0.0804  120 THR A O   
825  C CB  . THR A 107 ? 0.4978 0.2481 0.3767 0.0291  0.0178  0.0698  120 THR A CB  
826  O OG1 . THR A 107 ? 0.5309 0.2771 0.4081 0.0214  0.0219  0.0619  120 THR A OG1 
827  C CG2 . THR A 107 ? 0.5309 0.2800 0.4002 0.0335  0.0170  0.0794  120 THR A CG2 
828  N N   . LEU A 108 ? 0.4459 0.2272 0.3145 0.0310  -0.0039 0.0710  121 LEU A N   
829  C CA  . LEU A 108 ? 0.5045 0.2951 0.3663 0.0348  -0.0112 0.0766  121 LEU A CA  
830  C C   . LEU A 108 ? 0.5500 0.3327 0.4019 0.0376  -0.0071 0.0847  121 LEU A C   
831  O O   . LEU A 108 ? 0.5416 0.3185 0.3868 0.0330  -0.0032 0.0823  121 LEU A O   
832  C CB  . LEU A 108 ? 0.5111 0.3127 0.3693 0.0298  -0.0176 0.0699  121 LEU A CB  
833  C CG  . LEU A 108 ? 0.5103 0.3225 0.3608 0.0325  -0.0254 0.0738  121 LEU A CG  
834  C CD1 . LEU A 108 ? 0.4834 0.3039 0.3401 0.0391  -0.0309 0.0789  121 LEU A CD1 
835  C CD2 . LEU A 108 ? 0.5167 0.3383 0.3649 0.0267  -0.0303 0.0659  121 LEU A CD2 
836  N N   . PRO A 109 ? 0.5964 0.3790 0.4474 0.0452  -0.0076 0.0945  122 PRO A N   
837  C CA  . PRO A 109 ? 0.7210 0.4955 0.5627 0.0486  -0.0028 0.1032  122 PRO A CA  
838  C C   . PRO A 109 ? 0.6770 0.4600 0.5060 0.0484  -0.0088 0.1049  122 PRO A C   
839  O O   . PRO A 109 ? 0.6601 0.4571 0.4881 0.0489  -0.0180 0.1032  122 PRO A O   
840  C CB  . PRO A 109 ? 0.6590 0.4323 0.5055 0.0575  -0.0018 0.1133  122 PRO A CB  
841  C CG  . PRO A 109 ? 0.6679 0.4552 0.5215 0.0592  -0.0107 0.1110  122 PRO A CG  
842  C CD  . PRO A 109 ? 0.6210 0.4105 0.4801 0.0514  -0.0120 0.0988  122 PRO A CD  
843  N N   . PHE A 110 ? 0.6628 0.4371 0.4825 0.0475  -0.0032 0.1081  123 PHE A N   
844  C CA  . PHE A 110 ? 0.6918 0.4723 0.4981 0.0474  -0.0074 0.1102  123 PHE A CA  
845  C C   . PHE A 110 ? 0.6996 0.4786 0.4992 0.0554  -0.0055 0.1226  123 PHE A C   
846  O O   . PHE A 110 ? 0.7360 0.5065 0.5409 0.0563  0.0034  0.1262  123 PHE A O   
847  C CB  . PHE A 110 ? 0.7554 0.5287 0.5559 0.0400  -0.0026 0.1041  123 PHE A CB  
848  C CG  . PHE A 110 ? 0.7163 0.4975 0.5196 0.0326  -0.0074 0.0927  123 PHE A CG  
849  C CD1 . PHE A 110 ? 0.6969 0.4798 0.5124 0.0297  -0.0080 0.0858  123 PHE A CD1 
850  C CD2 . PHE A 110 ? 0.7248 0.5115 0.5184 0.0287  -0.0108 0.0893  123 PHE A CD2 
851  C CE1 . PHE A 110 ? 0.6392 0.4294 0.4574 0.0235  -0.0119 0.0762  123 PHE A CE1 
852  C CE2 . PHE A 110 ? 0.6944 0.4880 0.4911 0.0222  -0.0144 0.0793  123 PHE A CE2 
853  C CZ  . PHE A 110 ? 0.6092 0.4047 0.4185 0.0197  -0.0149 0.0731  123 PHE A CZ  
854  N N   . PRO A 111 ? 0.6994 0.4918 0.4924 0.0600  -0.0138 0.1272  124 PRO A N   
855  C CA  . PRO A 111 ? 0.7271 0.5247 0.5187 0.0665  -0.0127 0.1375  124 PRO A CA  
856  C C   . PRO A 111 ? 0.8203 0.6121 0.6028 0.0648  -0.0067 0.1398  124 PRO A C   
857  O O   . PRO A 111 ? 0.8314 0.6175 0.6076 0.0587  -0.0046 0.1334  124 PRO A O   
858  C CB  . PRO A 111 ? 0.7088 0.5240 0.4950 0.0702  -0.0244 0.1395  124 PRO A CB  
859  C CG  . PRO A 111 ? 0.6924 0.5101 0.4719 0.0641  -0.0304 0.1296  124 PRO A CG  
860  C CD  . PRO A 111 ? 0.7097 0.5175 0.5008 0.0579  -0.0248 0.1213  124 PRO A CD  
861  N N   . SER A 112 ? 0.8777 0.6712 0.6602 0.0705  -0.0038 0.1491  125 SER A N   
862  C CA  . SER A 112 ? 0.9571 0.7456 0.7316 0.0700  0.0021  0.1525  125 SER A CA  
863  C C   . SER A 112 ? 0.9742 0.7730 0.7339 0.0689  -0.0046 0.1516  125 SER A C   
864  O O   . SER A 112 ? 1.2553 1.0491 1.0074 0.0665  0.0001  0.1515  125 SER A O   
865  C CB  . SER A 112 ? 1.0744 0.8617 0.8530 0.0767  0.0070  0.1628  125 SER A CB  
866  O OG  . SER A 112 ? 0.9448 0.7465 0.7220 0.0829  -0.0013 0.1690  125 SER A OG  
867  N N   . GLN A 113 ? 0.9343 0.7476 0.6902 0.0704  -0.0153 0.1504  126 GLN A N   
868  C CA  . GLN A 113 ? 0.8725 0.6974 0.6149 0.0692  -0.0223 0.1486  126 GLN A CA  
869  C C   . GLN A 113 ? 0.8252 0.6556 0.5656 0.0641  -0.0299 0.1384  126 GLN A C   
870  O O   . GLN A 113 ? 0.8728 0.7073 0.6214 0.0651  -0.0348 0.1362  126 GLN A O   
871  C CB  . GLN A 113 ? 0.9208 0.7610 0.6598 0.0758  -0.0290 0.1567  126 GLN A CB  
872  C CG  . GLN A 113 ? 0.8109 0.6464 0.5496 0.0810  -0.0222 0.1668  126 GLN A CG  
873  C CD  . GLN A 113 ? 0.7544 0.6053 0.4850 0.0861  -0.0292 0.1734  126 GLN A CD  
874  O OE1 . GLN A 113 ? 0.8189 0.6759 0.5553 0.0921  -0.0318 0.1801  126 GLN A OE1 
875  N NE2 . GLN A 113 ? 0.8355 0.6928 0.5528 0.0836  -0.0323 0.1711  126 GLN A NE2 
876  N N   . PHE A 114 ? 0.8113 0.6417 0.5414 0.0585  -0.0307 0.1320  127 PHE A N   
877  C CA  . PHE A 114 ? 0.8160 0.6521 0.5429 0.0529  -0.0380 0.1218  127 PHE A CA  
878  C C   . PHE A 114 ? 0.8306 0.6805 0.5453 0.0523  -0.0443 0.1203  127 PHE A C   
879  O O   . PHE A 114 ? 0.8169 0.6630 0.5227 0.0490  -0.0402 0.1188  127 PHE A O   
880  C CB  . PHE A 114 ? 0.7416 0.5636 0.4692 0.0452  -0.0323 0.1137  127 PHE A CB  
881  C CG  . PHE A 114 ? 0.7207 0.5406 0.4647 0.0423  -0.0319 0.1078  127 PHE A CG  
882  C CD1 . PHE A 114 ? 0.6949 0.5231 0.4454 0.0361  -0.0372 0.0971  127 PHE A CD1 
883  C CD2 . PHE A 114 ? 0.7383 0.5482 0.4916 0.0458  -0.0258 0.1130  127 PHE A CD2 
884  C CE1 . PHE A 114 ? 0.6482 0.4752 0.4136 0.0338  -0.0366 0.0919  127 PHE A CE1 
885  C CE2 . PHE A 114 ? 0.7304 0.5389 0.4984 0.0430  -0.0253 0.1071  127 PHE A CE2 
886  C CZ  . PHE A 114 ? 0.6712 0.4885 0.4449 0.0372  -0.0309 0.0968  127 PHE A CZ  
887  N N   . ASN A 115 ? 0.8910 0.7575 0.6062 0.0552  -0.0540 0.1204  128 ASN A N   
888  C CA  . ASN A 115 ? 0.8862 0.7679 0.5911 0.0541  -0.0607 0.1179  128 ASN A CA  
889  C C   . ASN A 115 ? 0.8625 0.7457 0.5640 0.0460  -0.0642 0.1053  128 ASN A C   
890  O O   . ASN A 115 ? 0.8665 0.7463 0.5756 0.0425  -0.0664 0.0988  128 ASN A O   
891  C CB  . ASN A 115 ? 0.8704 0.7704 0.5787 0.0595  -0.0699 0.1220  128 ASN A CB  
892  C CG  . ASN A 115 ? 0.9340 0.8518 0.6352 0.0563  -0.0790 0.1151  128 ASN A CG  
893  O OD1 . ASN A 115 ? 0.9830 0.9078 0.6738 0.0567  -0.0795 0.1175  128 ASN A OD1 
894  N ND2 . ASN A 115 ? 0.8595 0.7848 0.5669 0.0530  -0.0860 0.1062  128 ASN A ND2 
895  N N   . PHE A 116 ? 0.8248 0.7127 0.5153 0.0428  -0.0642 0.1020  129 PHE A N   
896  C CA  . PHE A 116 ? 0.8012 0.6943 0.4889 0.0353  -0.0683 0.0900  129 PHE A CA  
897  C C   . PHE A 116 ? 0.7714 0.6822 0.4643 0.0358  -0.0792 0.0857  129 PHE A C   
898  O O   . PHE A 116 ? 0.6740 0.6006 0.3625 0.0388  -0.0847 0.0880  129 PHE A O   
899  C CB  . PHE A 116 ? 0.7831 0.6793 0.4585 0.0327  -0.0660 0.0883  129 PHE A CB  
900  C CG  . PHE A 116 ? 0.7230 0.6244 0.3964 0.0248  -0.0689 0.0758  129 PHE A CG  
901  C CD1 . PHE A 116 ? 0.7463 0.6661 0.4182 0.0238  -0.0774 0.0703  129 PHE A CD1 
902  C CD2 . PHE A 116 ? 0.7222 0.6106 0.3964 0.0182  -0.0627 0.0695  129 PHE A CD2 
903  C CE1 . PHE A 116 ? 0.7149 0.6391 0.3866 0.0164  -0.0791 0.0584  129 PHE A CE1 
904  C CE2 . PHE A 116 ? 0.6733 0.5664 0.3472 0.0110  -0.0645 0.0584  129 PHE A CE2 
905  C CZ  . PHE A 116 ? 0.6150 0.5256 0.2879 0.0101  -0.0724 0.0528  129 PHE A CZ  
906  N N   . VAL A 117 ? 0.7214 0.6302 0.4243 0.0326  -0.0821 0.0793  130 VAL A N   
907  C CA  . VAL A 117 ? 0.7267 0.6512 0.4385 0.0336  -0.0916 0.0758  130 VAL A CA  
908  C C   . VAL A 117 ? 0.6539 0.5911 0.3624 0.0273  -0.0972 0.0648  130 VAL A C   
909  O O   . VAL A 117 ? 0.6350 0.5670 0.3470 0.0198  -0.0942 0.0556  130 VAL A O   
910  C CB  . VAL A 117 ? 0.6812 0.6021 0.4125 0.0322  -0.0902 0.0729  130 VAL A CB  
911  C CG1 . VAL A 117 ? 0.6973 0.6350 0.4389 0.0333  -0.0996 0.0694  130 VAL A CG1 
912  C CG2 . VAL A 117 ? 0.6976 0.6061 0.4332 0.0380  -0.0838 0.0830  130 VAL A CG2 
913  N N   . PRO A 118 ? 0.6754 0.6311 0.3812 0.0294  -0.1039 0.0648  131 PRO A N   
914  C CA  . PRO A 118 ? 0.6531 0.6222 0.3577 0.0231  -0.1087 0.0534  131 PRO A CA  
915  C C   . PRO A 118 ? 0.5770 0.5539 0.2957 0.0201  -0.1152 0.0454  131 PRO A C   
916  O O   . PRO A 118 ? 0.5494 0.5241 0.2780 0.0241  -0.1173 0.0499  131 PRO A O   
917  C CB  . PRO A 118 ? 0.6223 0.6087 0.3188 0.0271  -0.1133 0.0581  131 PRO A CB  
918  C CG  . PRO A 118 ? 0.6360 0.6230 0.3365 0.0354  -0.1147 0.0705  131 PRO A CG  
919  C CD  . PRO A 118 ? 0.6624 0.6278 0.3656 0.0374  -0.1065 0.0758  131 PRO A CD  
920  N N   . PRO A 119 ? 0.4903 0.4764 0.2114 0.0133  -0.1180 0.0336  132 PRO A N   
921  C CA  . PRO A 119 ? 0.4994 0.4927 0.2355 0.0099  -0.1234 0.0256  132 PRO A CA  
922  C C   . PRO A 119 ? 0.5061 0.5165 0.2496 0.0153  -0.1319 0.0292  132 PRO A C   
923  O O   . PRO A 119 ? 0.5212 0.5409 0.2576 0.0207  -0.1344 0.0368  132 PRO A O   
924  C CB  . PRO A 119 ? 0.5633 0.5637 0.2990 0.0017  -0.1231 0.0127  132 PRO A CB  
925  C CG  . PRO A 119 ? 0.5632 0.5671 0.2831 0.0027  -0.1209 0.0148  132 PRO A CG  
926  C CD  . PRO A 119 ? 0.5684 0.5569 0.2795 0.0080  -0.1151 0.0267  132 PRO A CD  
927  N N   . GLY A 120 ? 0.4975 0.5126 0.2564 0.0135  -0.1362 0.0238  133 GLY A N   
928  C CA  . GLY A 120 ? 0.4906 0.5217 0.2599 0.0180  -0.1440 0.0262  133 GLY A CA  
929  C C   . GLY A 120 ? 0.5246 0.5488 0.3053 0.0242  -0.1427 0.0350  133 GLY A C   
930  O O   . GLY A 120 ? 0.6764 0.7126 0.4691 0.0272  -0.1488 0.0358  133 GLY A O   
931  N N   . ARG A 121 ? 0.5023 0.5085 0.2812 0.0258  -0.1340 0.0410  134 ARG A N   
932  C CA  . ARG A 121 ? 0.5503 0.5491 0.3402 0.0314  -0.1310 0.0491  134 ARG A CA  
933  C C   . ARG A 121 ? 0.5453 0.5422 0.3544 0.0275  -0.1291 0.0421  134 ARG A C   
934  O O   . ARG A 121 ? 0.5026 0.4966 0.3150 0.0202  -0.1263 0.0325  134 ARG A O   
935  C CB  . ARG A 121 ? 0.5596 0.5397 0.3409 0.0339  -0.1219 0.0572  134 ARG A CB  
936  C CG  . ARG A 121 ? 0.6311 0.6114 0.4005 0.0423  -0.1227 0.0699  134 ARG A CG  
937  C CD  . ARG A 121 ? 0.5704 0.5665 0.3266 0.0434  -0.1304 0.0696  134 ARG A CD  
938  N NE  . ARG A 121 ? 0.5863 0.5770 0.3273 0.0449  -0.1249 0.0758  134 ARG A NE  
939  C CZ  . ARG A 121 ? 0.6247 0.6143 0.3622 0.0519  -0.1224 0.0882  134 ARG A CZ  
940  N NH1 . ARG A 121 ? 0.6080 0.6012 0.3557 0.0583  -0.1244 0.0961  134 ARG A NH1 
941  N NH2 . ARG A 121 ? 0.6614 0.6458 0.3856 0.0523  -0.1173 0.0930  134 ARG A NH2 
942  N N   . MET A 122 ? 0.5129 0.5115 0.3348 0.0326  -0.1303 0.0474  135 MET A N   
943  C CA  . MET A 122 ? 0.5104 0.5060 0.3504 0.0304  -0.1278 0.0427  135 MET A CA  
944  C C   . MET A 122 ? 0.4831 0.4609 0.3253 0.0328  -0.1190 0.0487  135 MET A C   
945  O O   . MET A 122 ? 0.5163 0.4895 0.3550 0.0394  -0.1177 0.0589  135 MET A O   
946  C CB  . MET A 122 ? 0.5339 0.5440 0.3879 0.0342  -0.1350 0.0438  135 MET A CB  
947  C CG  . MET A 122 ? 0.5715 0.5985 0.4306 0.0293  -0.1423 0.0338  135 MET A CG  
948  S SD  . MET A 122 ? 0.6746 0.6970 0.5465 0.0205  -0.1374 0.0210  135 MET A SD  
949  C CE  . MET A 122 ? 0.5894 0.6328 0.4663 0.0157  -0.1464 0.0104  135 MET A CE  
950  N N   . CYS A 123 ? 0.4153 0.3836 0.2635 0.0274  -0.1129 0.0423  136 CYS A N   
951  C CA  . CYS A 123 ? 0.4195 0.3714 0.2692 0.0284  -0.1044 0.0463  136 CYS A CA  
952  C C   . CYS A 123 ? 0.3910 0.3405 0.2566 0.0255  -0.1013 0.0403  136 CYS A C   
953  O O   . CYS A 123 ? 0.4154 0.3751 0.2905 0.0225  -0.1051 0.0333  136 CYS A O   
954  C CB  . CYS A 123 ? 0.4359 0.3760 0.2718 0.0248  -0.0982 0.0458  136 CYS A CB  
955  S SG  . CYS A 123 ? 0.6471 0.5904 0.4628 0.0276  -0.1014 0.0516  136 CYS A SG  
956  N N   . ARG A 124 ? 0.3447 0.2810 0.2132 0.0265  -0.0942 0.0432  137 ARG A N   
957  C CA  . ARG A 124 ? 0.3393 0.2724 0.2218 0.0246  -0.0905 0.0388  137 ARG A CA  
958  C C   . ARG A 124 ? 0.3422 0.2629 0.2209 0.0199  -0.0827 0.0354  137 ARG A C   
959  O O   . ARG A 124 ? 0.3348 0.2458 0.2025 0.0201  -0.0786 0.0392  137 ARG A O   
960  C CB  . ARG A 124 ? 0.3814 0.3114 0.2731 0.0308  -0.0894 0.0452  137 ARG A CB  
961  C CG  . ARG A 124 ? 0.4687 0.4115 0.3666 0.0360  -0.0968 0.0491  137 ARG A CG  
962  C CD  . ARG A 124 ? 0.4661 0.4045 0.3738 0.0420  -0.0945 0.0555  137 ARG A CD  
963  N NE  . ARG A 124 ? 0.6216 0.5734 0.5386 0.0464  -0.1015 0.0581  137 ARG A NE  
964  C CZ  . ARG A 124 ? 0.5971 0.5579 0.5279 0.0451  -0.1045 0.0527  137 ARG A CZ  
965  N NH1 . ARG A 124 ? 0.5465 0.5046 0.4833 0.0397  -0.1010 0.0447  137 ARG A NH1 
966  N NH2 . ARG A 124 ? 0.5951 0.5684 0.5342 0.0493  -0.1110 0.0557  137 ARG A NH2 
967  N N   . VAL A 125 ? 0.2999 0.2215 0.1882 0.0159  -0.0804 0.0284  138 VAL A N   
968  C CA  . VAL A 125 ? 0.3063 0.2180 0.1936 0.0117  -0.0732 0.0251  138 VAL A CA  
969  C C   . VAL A 125 ? 0.3369 0.2482 0.2385 0.0122  -0.0705 0.0227  138 VAL A C   
970  O O   . VAL A 125 ? 0.2880 0.2085 0.2005 0.0130  -0.0740 0.0201  138 VAL A O   
971  C CB  . VAL A 125 ? 0.3115 0.2254 0.1932 0.0054  -0.0725 0.0185  138 VAL A CB  
972  C CG1 . VAL A 125 ? 0.3715 0.2971 0.2634 0.0030  -0.0763 0.0119  138 VAL A CG1 
973  C CG2 . VAL A 125 ? 0.2801 0.1843 0.1605 0.0016  -0.0650 0.0160  138 VAL A CG2 
974  N N   . ALA A 126 ? 0.3226 0.2235 0.2242 0.0117  -0.0640 0.0234  139 ALA A N   
975  C CA  . ALA A 126 ? 0.3037 0.2035 0.2172 0.0125  -0.0609 0.0215  139 ALA A CA  
976  C C   . ALA A 126 ? 0.3011 0.1953 0.2137 0.0078  -0.0547 0.0170  139 ALA A C   
977  O O   . ALA A 126 ? 0.3120 0.1997 0.2146 0.0050  -0.0518 0.0171  139 ALA A O   
978  C CB  . ALA A 126 ? 0.2856 0.1790 0.2019 0.0179  -0.0592 0.0275  139 ALA A CB  
979  N N   . GLY A 127 ? 0.2519 0.1491 0.1752 0.0072  -0.0528 0.0132  140 GLY A N   
980  C CA  . GLY A 127 ? 0.2509 0.1447 0.1746 0.0034  -0.0472 0.0092  140 GLY A CA  
981  C C   . GLY A 127 ? 0.2401 0.1397 0.1764 0.0038  -0.0459 0.0057  140 GLY A C   
982  O O   . GLY A 127 ? 0.2652 0.1715 0.2105 0.0067  -0.0492 0.0060  140 GLY A O   
983  N N   . TRP A 128 ? 0.2377 0.1352 0.1748 0.0011  -0.0408 0.0027  141 TRP A N   
984  C CA  . TRP A 128 ? 0.2615 0.1645 0.2095 0.0014  -0.0385 -0.0004 141 TRP A CA  
985  C C   . TRP A 128 ? 0.3031 0.2121 0.2531 -0.0025 -0.0372 -0.0046 141 TRP A C   
986  O O   . TRP A 128 ? 0.3092 0.2219 0.2665 -0.0028 -0.0337 -0.0069 141 TRP A O   
987  C CB  . TRP A 128 ? 0.2616 0.1594 0.2102 0.0018  -0.0334 -0.0007 141 TRP A CB  
988  C CG  . TRP A 128 ? 0.2618 0.1535 0.2106 0.0058  -0.0334 0.0028  141 TRP A CG  
989  C CD1 . TRP A 128 ? 0.2993 0.1930 0.2572 0.0100  -0.0336 0.0039  141 TRP A CD1 
990  C CD2 . TRP A 128 ? 0.2790 0.1612 0.2192 0.0060  -0.0323 0.0058  141 TRP A CD2 
991  N NE1 . TRP A 128 ? 0.2790 0.1650 0.2345 0.0128  -0.0328 0.0073  141 TRP A NE1 
992  C CE2 . TRP A 128 ? 0.2663 0.1450 0.2112 0.0104  -0.0318 0.0086  141 TRP A CE2 
993  C CE3 . TRP A 128 ? 0.2697 0.1457 0.1992 0.0029  -0.0311 0.0066  141 TRP A CE3 
994  C CZ2 . TRP A 128 ? 0.2761 0.1452 0.2155 0.0119  -0.0299 0.0121  141 TRP A CZ2 
995  C CZ3 . TRP A 128 ? 0.2904 0.1569 0.2145 0.0044  -0.0293 0.0102  141 TRP A CZ3 
996  C CH2 . TRP A 128 ? 0.2871 0.1501 0.2163 0.0089  -0.0286 0.0129  141 TRP A CH2 
997  N N   . GLY A 129 ? 0.2499 0.1601 0.1936 -0.0053 -0.0396 -0.0055 142 GLY A N   
998  C CA  . GLY A 129 ? 0.2707 0.1853 0.2157 -0.0092 -0.0376 -0.0094 142 GLY A CA  
999  C C   . GLY A 129 ? 0.2646 0.1881 0.2223 -0.0084 -0.0384 -0.0121 142 GLY A C   
1000 O O   . GLY A 129 ? 0.2475 0.1742 0.2137 -0.0047 -0.0405 -0.0109 142 GLY A O   
1001 N N   . ARG A 130 ? 0.2529 0.1802 0.2127 -0.0119 -0.0360 -0.0157 143 ARG A N   
1002 C CA  . ARG A 130 ? 0.2169 0.1522 0.1894 -0.0117 -0.0356 -0.0186 143 ARG A CA  
1003 C C   . ARG A 130 ? 0.2166 0.1565 0.1924 -0.0104 -0.0418 -0.0190 143 ARG A C   
1004 O O   . ARG A 130 ? 0.2406 0.1794 0.2073 -0.0116 -0.0461 -0.0186 143 ARG A O   
1005 C CB  . ARG A 130 ? 0.2114 0.1489 0.1842 -0.0161 -0.0318 -0.0223 143 ARG A CB  
1006 C CG  . ARG A 130 ? 0.2669 0.2018 0.2379 -0.0174 -0.0255 -0.0219 143 ARG A CG  
1007 C CD  . ARG A 130 ? 0.2573 0.1945 0.2292 -0.0215 -0.0215 -0.0251 143 ARG A CD  
1008 N NE  . ARG A 130 ? 0.2802 0.2171 0.2532 -0.0221 -0.0153 -0.0243 143 ARG A NE  
1009 C CZ  . ARG A 130 ? 0.3263 0.2686 0.3105 -0.0205 -0.0106 -0.0245 143 ARG A CZ  
1010 N NH1 . ARG A 130 ? 0.2669 0.2145 0.2630 -0.0183 -0.0108 -0.0256 143 ARG A NH1 
1011 N NH2 . ARG A 130 ? 0.3680 0.3109 0.3520 -0.0209 -0.0054 -0.0234 143 ARG A NH2 
1012 N N   . THR A 131 ? 0.2477 0.1934 0.2370 -0.0076 -0.0421 -0.0195 144 THR A N   
1013 C CA  . THR A 131 ? 0.2582 0.2100 0.2534 -0.0063 -0.0479 -0.0202 144 THR A CA  
1014 C C   . THR A 131 ? 0.2462 0.2046 0.2464 -0.0103 -0.0483 -0.0257 144 THR A C   
1015 O O   . THR A 131 ? 0.2411 0.2062 0.2478 -0.0099 -0.0530 -0.0275 144 THR A O   
1016 C CB  . THR A 131 ? 0.2495 0.2044 0.2578 -0.0015 -0.0477 -0.0184 144 THR A CB  
1017 O OG1 . THR A 131 ? 0.2620 0.2191 0.2806 -0.0016 -0.0414 -0.0202 144 THR A OG1 
1018 C CG2 . THR A 131 ? 0.3283 0.2766 0.3314 0.0024  -0.0479 -0.0133 144 THR A CG2 
1019 N N   . GLY A 132 ? 0.2216 0.1786 0.2194 -0.0142 -0.0434 -0.0287 145 GLY A N   
1020 C CA  . GLY A 132 ? 0.1967 0.1588 0.1988 -0.0185 -0.0427 -0.0344 145 GLY A CA  
1021 C C   . GLY A 132 ? 0.2134 0.1724 0.2137 -0.0217 -0.0355 -0.0361 145 GLY A C   
1022 O O   . GLY A 132 ? 0.1911 0.1453 0.1878 -0.0205 -0.0315 -0.0329 145 GLY A O   
1023 N N   . VAL A 133 ? 0.2621 0.2244 0.2654 -0.0260 -0.0338 -0.0414 146 VAL A N   
1024 C CA  . VAL A 133 ? 0.2487 0.2088 0.2523 -0.0291 -0.0263 -0.0431 146 VAL A CA  
1025 C C   . VAL A 133 ? 0.2091 0.1708 0.2255 -0.0260 -0.0199 -0.0410 146 VAL A C   
1026 O O   . VAL A 133 ? 0.2503 0.2172 0.2806 -0.0238 -0.0195 -0.0419 146 VAL A O   
1027 C CB  . VAL A 133 ? 0.2742 0.2376 0.2804 -0.0341 -0.0250 -0.0496 146 VAL A CB  
1028 C CG1 . VAL A 133 ? 0.2922 0.2530 0.2998 -0.0369 -0.0164 -0.0508 146 VAL A CG1 
1029 C CG2 . VAL A 133 ? 0.3036 0.2661 0.2957 -0.0369 -0.0314 -0.0515 146 VAL A CG2 
1030 N N   . LEU A 134 ? 0.2201 0.1780 0.2322 -0.0256 -0.0149 -0.0381 147 LEU A N   
1031 C CA  . LEU A 134 ? 0.2843 0.2441 0.3061 -0.0225 -0.0085 -0.0354 147 LEU A CA  
1032 C C   . LEU A 134 ? 0.2534 0.2140 0.2792 -0.0172 -0.0109 -0.0317 147 LEU A C   
1033 O O   . LEU A 134 ? 0.2308 0.1934 0.2638 -0.0140 -0.0060 -0.0293 147 LEU A O   
1034 C CB  . LEU A 134 ? 0.2239 0.1889 0.2609 -0.0232 -0.0024 -0.0384 147 LEU A CB  
1035 C CG  . LEU A 134 ? 0.2781 0.2424 0.3133 -0.0286 0.0006  -0.0430 147 LEU A CG  
1036 C CD1 . LEU A 134 ? 0.3300 0.2992 0.3820 -0.0292 0.0068  -0.0462 147 LEU A CD1 
1037 C CD2 . LEU A 134 ? 0.3057 0.2657 0.3312 -0.0304 0.0049  -0.0410 147 LEU A CD2 
1038 N N   . LYS A 135 ? 0.2328 0.1922 0.2542 -0.0159 -0.0179 -0.0310 148 LYS A N   
1039 C CA  . LYS A 135 ? 0.2370 0.1964 0.2620 -0.0108 -0.0198 -0.0275 148 LYS A CA  
1040 C C   . LYS A 135 ? 0.2672 0.2209 0.2818 -0.0096 -0.0190 -0.0239 148 LYS A C   
1041 O O   . LYS A 135 ? 0.2703 0.2194 0.2730 -0.0126 -0.0193 -0.0240 148 LYS A O   
1042 C CB  . LYS A 135 ? 0.2775 0.2378 0.3020 -0.0097 -0.0273 -0.0275 148 LYS A CB  
1043 C CG  . LYS A 135 ? 0.2928 0.2598 0.3284 -0.0110 -0.0290 -0.0316 148 LYS A CG  
1044 C CD  . LYS A 135 ? 0.3082 0.2800 0.3608 -0.0084 -0.0237 -0.0318 148 LYS A CD  
1045 C CE  . LYS A 135 ? 0.3281 0.3030 0.3883 -0.0120 -0.0180 -0.0361 148 LYS A CE  
1046 N NZ  . LYS A 135 ? 0.3137 0.2932 0.3912 -0.0090 -0.0122 -0.0358 148 LYS A NZ  
1047 N N   . PRO A 136 ? 0.3076 0.2617 0.3266 -0.0053 -0.0176 -0.0211 150 PRO A N   
1048 C CA  . PRO A 136 ? 0.2822 0.2310 0.2915 -0.0044 -0.0172 -0.0186 150 PRO A CA  
1049 C C   . PRO A 136 ? 0.2704 0.2134 0.2703 -0.0042 -0.0231 -0.0171 150 PRO A C   
1050 O O   . PRO A 136 ? 0.2545 0.1986 0.2560 -0.0036 -0.0279 -0.0174 150 PRO A O   
1051 C CB  . PRO A 136 ? 0.2767 0.2285 0.2947 0.0004  -0.0141 -0.0167 150 PRO A CB  
1052 C CG  . PRO A 136 ? 0.3174 0.2739 0.3478 0.0028  -0.0155 -0.0172 150 PRO A CG  
1053 C CD  . PRO A 136 ? 0.2726 0.2318 0.3058 -0.0011 -0.0157 -0.0205 150 PRO A CD  
1054 N N   . GLY A 137 ? 0.2874 0.2245 0.2775 -0.0045 -0.0224 -0.0155 151 GLY A N   
1055 C CA  . GLY A 137 ? 0.2538 0.1846 0.2356 -0.0037 -0.0267 -0.0134 151 GLY A CA  
1056 C C   . GLY A 137 ? 0.2699 0.2015 0.2588 0.0012  -0.0290 -0.0113 151 GLY A C   
1057 O O   . GLY A 137 ? 0.2951 0.2302 0.2931 0.0040  -0.0262 -0.0112 151 GLY A O   
1058 N N   . SER A 138 ? 0.2572 0.1858 0.2420 0.0023  -0.0339 -0.0093 152 SER A N   
1059 C CA  . SER A 138 ? 0.2692 0.1988 0.2611 0.0070  -0.0363 -0.0069 152 SER A CA  
1060 C C   . SER A 138 ? 0.3153 0.2397 0.3065 0.0098  -0.0331 -0.0051 152 SER A C   
1061 O O   . SER A 138 ? 0.3395 0.2574 0.3214 0.0081  -0.0312 -0.0048 152 SER A O   
1062 C CB  . SER A 138 ? 0.2768 0.2049 0.2638 0.0079  -0.0422 -0.0046 152 SER A CB  
1063 O OG  . SER A 138 ? 0.4018 0.3331 0.3980 0.0123  -0.0449 -0.0024 152 SER A OG  
1064 N N   . ASP A 139 ? 0.3003 0.2277 0.3017 0.0139  -0.0323 -0.0043 153 ASP A N   
1065 C CA  . ASP A 139 ? 0.3484 0.2712 0.3497 0.0167  -0.0291 -0.0030 153 ASP A CA  
1066 C C   . ASP A 139 ? 0.3473 0.2622 0.3420 0.0182  -0.0313 0.0002  153 ASP A C   
1067 O O   . ASP A 139 ? 0.3856 0.2938 0.3748 0.0182  -0.0283 0.0004  153 ASP A O   
1068 C CB  . ASP A 139 ? 0.3819 0.3098 0.3959 0.0211  -0.0276 -0.0026 153 ASP A CB  
1069 C CG  . ASP A 139 ? 0.4171 0.3531 0.4393 0.0202  -0.0251 -0.0049 153 ASP A CG  
1070 O OD1 . ASP A 139 ? 0.4062 0.3439 0.4244 0.0162  -0.0246 -0.0070 153 ASP A OD1 
1071 O OD2 . ASP A 139 ? 0.4320 0.3725 0.4651 0.0238  -0.0232 -0.0044 153 ASP A OD2 
1072 N N   . THR A 140 ? 0.2902 0.2060 0.2856 0.0196  -0.0363 0.0026  154 THR A N   
1073 C CA  . THR A 140 ? 0.2930 0.2022 0.2834 0.0220  -0.0383 0.0067  154 THR A CA  
1074 C C   . THR A 140 ? 0.2824 0.1908 0.2638 0.0197  -0.0424 0.0080  154 THR A C   
1075 O O   . THR A 140 ? 0.2355 0.1496 0.2164 0.0167  -0.0447 0.0056  154 THR A O   
1076 C CB  . THR A 140 ? 0.3596 0.2718 0.3603 0.0273  -0.0406 0.0097  154 THR A CB  
1077 O OG1 . THR A 140 ? 0.3548 0.2765 0.3632 0.0272  -0.0447 0.0086  154 THR A OG1 
1078 C CG2 . THR A 140 ? 0.4135 0.3248 0.4216 0.0301  -0.0359 0.0090  154 THR A CG2 
1079 N N   . LEU A 141 ? 0.2775 0.1784 0.2517 0.0213  -0.0429 0.0120  155 LEU A N   
1080 C CA  . LEU A 141 ? 0.3006 0.1999 0.2649 0.0198  -0.0463 0.0141  155 LEU A CA  
1081 C C   . LEU A 141 ? 0.2821 0.1904 0.2507 0.0215  -0.0527 0.0154  155 LEU A C   
1082 O O   . LEU A 141 ? 0.3472 0.2581 0.3231 0.0260  -0.0552 0.0187  155 LEU A O   
1083 C CB  . LEU A 141 ? 0.3034 0.1927 0.2606 0.0220  -0.0445 0.0189  155 LEU A CB  
1084 C CG  . LEU A 141 ? 0.2993 0.1857 0.2450 0.0211  -0.0470 0.0221  155 LEU A CG  
1085 C CD1 . LEU A 141 ? 0.2876 0.1722 0.2249 0.0153  -0.0449 0.0182  155 LEU A CD1 
1086 C CD2 . LEU A 141 ? 0.3736 0.2501 0.3147 0.0244  -0.0446 0.0278  155 LEU A CD2 
1087 N N   . GLN A 142 ? 0.3488 0.2002 0.2623 0.0896  -0.0951 -0.0834 156 GLN A N   
1088 C CA  . GLN A 142 ? 0.3354 0.2078 0.2536 0.0854  -0.0896 -0.0741 156 GLN A CA  
1089 C C   . GLN A 142 ? 0.3339 0.2125 0.2597 0.0742  -0.0909 -0.0663 156 GLN A C   
1090 O O   . GLN A 142 ? 0.3370 0.2079 0.2667 0.0663  -0.0943 -0.0687 156 GLN A O   
1091 C CB  . GLN A 142 ? 0.3423 0.2299 0.2615 0.0802  -0.0849 -0.0780 156 GLN A CB  
1092 C CG  . GLN A 142 ? 0.4110 0.2945 0.3231 0.0921  -0.0816 -0.0839 156 GLN A CG  
1093 C CD  . GLN A 142 ? 0.4130 0.3075 0.3258 0.0999  -0.0753 -0.0774 156 GLN A CD  
1094 O OE1 . GLN A 142 ? 0.4094 0.3216 0.3295 0.0918  -0.0715 -0.0722 156 GLN A OE1 
1095 N NE2 . GLN A 142 ? 0.4889 0.3734 0.3943 0.1158  -0.0742 -0.0778 156 GLN A NE2 
1096 N N   . GLU A 143 ? 0.3300 0.2241 0.2585 0.0742  -0.0879 -0.0565 157 GLU A N   
1097 C CA  . GLU A 143 ? 0.3283 0.2329 0.2625 0.0653  -0.0882 -0.0481 157 GLU A CA  
1098 C C   . GLU A 143 ? 0.3169 0.2482 0.2535 0.0604  -0.0850 -0.0437 157 GLU A C   
1099 O O   . GLU A 143 ? 0.3330 0.2738 0.2692 0.0665  -0.0826 -0.0426 157 GLU A O   
1100 C CB  . GLU A 143 ? 0.3446 0.2384 0.2791 0.0721  -0.0892 -0.0388 157 GLU A CB  
1101 C CG  . GLU A 143 ? 0.3879 0.2859 0.3190 0.0849  -0.0868 -0.0323 157 GLU A CG  
1102 C CD  . GLU A 143 ? 0.5532 0.4398 0.4839 0.0925  -0.0864 -0.0220 157 GLU A CD  
1103 O OE1 . GLU A 143 ? 0.5684 0.4497 0.5032 0.0860  -0.0871 -0.0176 157 GLU A OE1 
1104 O OE2 . GLU A 143 ? 0.5852 0.4674 0.5114 0.1057  -0.0845 -0.0175 157 GLU A OE2 
1105 N N   . VAL A 144 ? 0.3091 0.2529 0.2487 0.0495  -0.0851 -0.0415 158 VAL A N   
1106 C CA  . VAL A 144 ? 0.2992 0.2683 0.2404 0.0433  -0.0833 -0.0395 158 VAL A CA  
1107 C C   . VAL A 144 ? 0.3234 0.3043 0.2658 0.0392  -0.0845 -0.0300 158 VAL A C   
1108 O O   . VAL A 144 ? 0.3240 0.2937 0.2671 0.0372  -0.0853 -0.0268 158 VAL A O   
1109 C CB  . VAL A 144 ? 0.2906 0.2641 0.2308 0.0343  -0.0809 -0.0494 158 VAL A CB  
1110 C CG1 . VAL A 144 ? 0.2879 0.2554 0.2275 0.0263  -0.0816 -0.0512 158 VAL A CG1 
1111 C CG2 . VAL A 144 ? 0.2998 0.2970 0.2418 0.0282  -0.0790 -0.0497 158 VAL A CG2 
1112 N N   . LYS A 145 ? 0.3004 0.3052 0.2437 0.0386  -0.0845 -0.0251 159 LYS A N   
1113 C CA  . LYS A 145 ? 0.3198 0.3408 0.2626 0.0364  -0.0856 -0.0158 159 LYS A CA  
1114 C C   . LYS A 145 ? 0.2977 0.3327 0.2379 0.0249  -0.0855 -0.0217 159 LYS A C   
1115 O O   . LYS A 145 ? 0.3036 0.3505 0.2440 0.0194  -0.0851 -0.0298 159 LYS A O   
1116 C CB  . LYS A 145 ? 0.3377 0.3800 0.2824 0.0433  -0.0866 -0.0072 159 LYS A CB  
1117 C CG  . LYS A 145 ? 0.3887 0.4429 0.3319 0.0472  -0.0872 0.0060  159 LYS A CG  
1118 C CD  . LYS A 145 ? 0.3838 0.4644 0.3292 0.0539  -0.0886 0.0140  159 LYS A CD  
1119 C CE  . LYS A 145 ? 0.3970 0.4860 0.3403 0.0622  -0.0879 0.0296  159 LYS A CE  
1120 N NZ  . LYS A 145 ? 0.4139 0.4750 0.3574 0.0729  -0.0844 0.0376  159 LYS A NZ  
1121 N N   . LEU A 146 ? 0.3108 0.3435 0.2488 0.0214  -0.0850 -0.0175 160 LEU A N   
1122 C CA  . LEU A 146 ? 0.3077 0.3501 0.2412 0.0119  -0.0841 -0.0228 160 LEU A CA  
1123 C C   . LEU A 146 ? 0.3547 0.4149 0.2843 0.0126  -0.0847 -0.0128 160 LEU A C   
1124 O O   . LEU A 146 ? 0.3177 0.3762 0.2492 0.0199  -0.0844 -0.0005 160 LEU A O   
1125 C CB  . LEU A 146 ? 0.2958 0.3183 0.2298 0.0074  -0.0818 -0.0280 160 LEU A CB  
1126 C CG  . LEU A 146 ? 0.3011 0.3072 0.2372 0.0077  -0.0811 -0.0383 160 LEU A CG  
1127 C CD1 . LEU A 146 ? 0.3277 0.3196 0.2644 0.0033  -0.0794 -0.0426 160 LEU A CD1 
1128 C CD2 . LEU A 146 ? 0.3216 0.3390 0.2556 0.0045  -0.0797 -0.0472 160 LEU A CD2 
1129 N N   . ARG A 147 ? 0.3041 0.3806 0.2271 0.0057  -0.0848 -0.0181 161 ARG A N   
1130 C CA  . ARG A 147 ? 0.3543 0.4511 0.2707 0.0069  -0.0856 -0.0102 161 ARG A CA  
1131 C C   . ARG A 147 ? 0.3158 0.4047 0.2279 0.0035  -0.0818 -0.0084 161 ARG A C   
1132 O O   . ARG A 147 ? 0.3101 0.3900 0.2202 -0.0035 -0.0797 -0.0184 161 ARG A O   
1133 C CB  . ARG A 147 ? 0.3913 0.5143 0.3020 0.0021  -0.0893 -0.0182 161 ARG A CB  
1134 C CG  . ARG A 147 ? 0.4003 0.5483 0.3022 0.0051  -0.0914 -0.0108 161 ARG A CG  
1135 C CD  . ARG A 147 ? 0.4257 0.5974 0.3212 -0.0022 -0.0959 -0.0229 161 ARG A CD  
1136 N NE  . ARG A 147 ? 0.4573 0.6580 0.3446 0.0029  -0.0999 -0.0160 161 ARG A NE  
1137 C CZ  . ARG A 147 ? 0.4612 0.6697 0.3361 0.0044  -0.0987 -0.0130 161 ARG A CZ  
1138 N NH1 . ARG A 147 ? 0.4531 0.6426 0.3231 0.0007  -0.0932 -0.0157 161 ARG A NH1 
1139 N NH2 . ARG A 147 ? 0.4016 0.6390 0.2684 0.0107  -0.1029 -0.0066 161 ARG A NH2 
1140 N N   . LEU A 148 ? 0.3258 0.4185 0.2371 0.0093  -0.0798 0.0056  162 LEU A N   
1141 C CA  . LEU A 148 ? 0.3307 0.4207 0.2381 0.0072  -0.0754 0.0099  162 LEU A CA  
1142 C C   . LEU A 148 ? 0.3339 0.4459 0.2275 0.0040  -0.0764 0.0038  162 LEU A C   
1143 O O   . LEU A 148 ? 0.3420 0.4767 0.2285 0.0089  -0.0791 0.0089  162 LEU A O   
1144 C CB  . LEU A 148 ? 0.3663 0.4540 0.2782 0.0152  -0.0718 0.0281  162 LEU A CB  
1145 C CG  . LEU A 148 ? 0.4350 0.4954 0.3600 0.0142  -0.0682 0.0327  162 LEU A CG  
1146 C CD1 . LEU A 148 ? 0.3788 0.4214 0.3115 0.0138  -0.0716 0.0250  162 LEU A CD1 
1147 C CD2 . LEU A 148 ? 0.4044 0.4625 0.3348 0.0217  -0.0632 0.0515  162 LEU A CD2 
1148 N N   . MET A 149 ? 0.3295 0.4348 0.2184 -0.0035 -0.0743 -0.0074 163 MET A N   
1149 C CA  . MET A 149 ? 0.3554 0.4771 0.2302 -0.0076 -0.0752 -0.0170 163 MET A CA  
1150 C C   . MET A 149 ? 0.3684 0.4981 0.2327 -0.0039 -0.0711 -0.0084 163 MET A C   
1151 O O   . MET A 149 ? 0.3479 0.4671 0.2182 -0.0004 -0.0660 0.0036  163 MET A O   
1152 C CB  . MET A 149 ? 0.3262 0.4352 0.1998 -0.0164 -0.0734 -0.0330 163 MET A CB  
1153 C CG  . MET A 149 ? 0.3683 0.4728 0.2502 -0.0197 -0.0766 -0.0422 163 MET A CG  
1154 S SD  . MET A 149 ? 0.4425 0.5750 0.3216 -0.0202 -0.0840 -0.0463 163 MET A SD  
1155 C CE  . MET A 149 ? 0.3672 0.5127 0.2289 -0.0267 -0.0837 -0.0580 163 MET A CE  
1156 N N   . ASP A 150 ? 0.3639 0.5127 0.2127 -0.0047 -0.0733 -0.0151 164 ASP A N   
1157 C CA  . ASP A 150 ? 0.4134 0.5698 0.2486 -0.0008 -0.0688 -0.0096 164 ASP A CA  
1158 C C   . ASP A 150 ? 0.4010 0.5374 0.2371 -0.0053 -0.0616 -0.0130 164 ASP A C   
1159 O O   . ASP A 150 ? 0.3941 0.5166 0.2340 -0.0129 -0.0614 -0.0258 164 ASP A O   
1160 C CB  . ASP A 150 ? 0.4390 0.6180 0.2557 -0.0017 -0.0736 -0.0206 164 ASP A CB  
1161 C CG  . ASP A 150 ? 0.5649 0.7598 0.3656 0.0075  -0.0707 -0.0105 164 ASP A CG  
1162 O OD1 . ASP A 150 ? 0.6325 0.8374 0.4363 0.0175  -0.0699 0.0068  164 ASP A OD1 
1163 O OD2 . ASP A 150 ? 0.6943 0.8909 0.4786 0.0058  -0.0685 -0.0193 164 ASP A OD2 
1164 N N   . PRO A 151 ? 0.4590 0.5943 0.2925 0.0000  -0.0549 -0.0006 165 PRO A N   
1165 C CA  . PRO A 151 ? 0.4426 0.5611 0.2791 -0.0037 -0.0478 -0.0019 165 PRO A CA  
1166 C C   . PRO A 151 ? 0.4286 0.5444 0.2507 -0.0094 -0.0466 -0.0192 165 PRO A C   
1167 O O   . PRO A 151 ? 0.3822 0.4821 0.2092 -0.0138 -0.0421 -0.0243 165 PRO A O   
1168 C CB  . PRO A 151 ? 0.3997 0.5245 0.2334 0.0044  -0.0408 0.0156  165 PRO A CB  
1169 C CG  . PRO A 151 ? 0.4873 0.6252 0.3238 0.0121  -0.0436 0.0288  165 PRO A CG  
1170 C CD  . PRO A 151 ? 0.4485 0.5987 0.2778 0.0104  -0.0526 0.0170  165 PRO A CD  
1171 N N   . GLN A 152 ? 0.4224 0.5537 0.2269 -0.0093 -0.0504 -0.0286 166 GLN A N   
1172 C CA  . GLN A 152 ? 0.4831 0.6101 0.2728 -0.0150 -0.0487 -0.0459 166 GLN A CA  
1173 C C   . GLN A 152 ? 0.4665 0.5785 0.2662 -0.0242 -0.0500 -0.0599 166 GLN A C   
1174 O O   . GLN A 152 ? 0.4219 0.5230 0.2135 -0.0289 -0.0455 -0.0722 166 GLN A O   
1175 C CB  . GLN A 152 ? 0.5612 0.7091 0.3314 -0.0136 -0.0542 -0.0541 166 GLN A CB  
1176 C CG  . GLN A 152 ? 0.6699 0.8355 0.4293 -0.0021 -0.0530 -0.0388 166 GLN A CG  
1177 C CD  . GLN A 152 ? 0.7652 0.9563 0.5081 0.0007  -0.0613 -0.0453 166 GLN A CD  
1178 O OE1 . GLN A 152 ? 0.8402 1.0278 0.5836 -0.0072 -0.0658 -0.0619 166 GLN A OE1 
1179 N NE2 . GLN A 152 ? 0.6927 0.9024 0.4290 0.0125  -0.0613 -0.0297 166 GLN A NE2 
1180 N N   . ALA A 153 ? 0.4251 0.5354 0.2414 -0.0257 -0.0552 -0.0575 167 ALA A N   
1181 C CA  . ALA A 153 ? 0.3639 0.4602 0.1901 -0.0324 -0.0555 -0.0687 167 ALA A CA  
1182 C C   . ALA A 153 ? 0.4035 0.4793 0.2380 -0.0326 -0.0485 -0.0664 167 ALA A C   
1183 O O   . ALA A 153 ? 0.4236 0.4868 0.2612 -0.0370 -0.0461 -0.0767 167 ALA A O   
1184 C CB  . ALA A 153 ? 0.3467 0.4482 0.1870 -0.0321 -0.0625 -0.0657 167 ALA A CB  
1185 N N   . CYS A 154 ? 0.3924 0.4659 0.2314 -0.0277 -0.0451 -0.0528 168 CYS A N   
1186 C CA  . CYS A 154 ? 0.3709 0.4289 0.2189 -0.0278 -0.0395 -0.0501 168 CYS A CA  
1187 C C   . CYS A 154 ? 0.4145 0.4717 0.2507 -0.0261 -0.0312 -0.0489 168 CYS A C   
1188 O O   . CYS A 154 ? 0.3860 0.4363 0.2306 -0.0246 -0.0263 -0.0417 168 CYS A O   
1189 C CB  . CYS A 154 ? 0.3753 0.4302 0.2409 -0.0248 -0.0414 -0.0360 168 CYS A CB  
1190 S SG  . CYS A 154 ? 0.3123 0.3593 0.1932 -0.0256 -0.0489 -0.0384 168 CYS A SG  
1191 N N   . SER A 155 ? 0.3945 0.4594 0.2113 -0.0261 -0.0296 -0.0560 169 SER A N   
1192 C CA  . SER A 155 ? 0.4547 0.5185 0.2572 -0.0229 -0.0211 -0.0548 169 SER A CA  
1193 C C   . SER A 155 ? 0.4330 0.4807 0.2356 -0.0251 -0.0137 -0.0624 169 SER A C   
1194 O O   . SER A 155 ? 0.5250 0.5703 0.3213 -0.0211 -0.0054 -0.0576 169 SER A O   
1195 C CB  . SER A 155 ? 0.5294 0.6039 0.3089 -0.0221 -0.0220 -0.0632 169 SER A CB  
1196 O OG  . SER A 155 ? 0.5970 0.6895 0.3744 -0.0176 -0.0280 -0.0543 169 SER A OG  
1197 N N   . HIS A 156 ? 0.4249 0.4625 0.2345 -0.0300 -0.0155 -0.0731 172 HIS A N   
1198 C CA  . HIS A 156 ? 0.4252 0.4480 0.2345 -0.0306 -0.0076 -0.0795 172 HIS A CA  
1199 C C   . HIS A 156 ? 0.3838 0.4026 0.2090 -0.0273 -0.0051 -0.0686 172 HIS A C   
1200 O O   . HIS A 156 ? 0.4776 0.4885 0.3008 -0.0251 0.0029  -0.0700 172 HIS A O   
1201 C CB  . HIS A 156 ? 0.4024 0.4162 0.2149 -0.0358 -0.0093 -0.0929 172 HIS A CB  
1202 C CG  . HIS A 156 ? 0.3590 0.3755 0.1885 -0.0371 -0.0181 -0.0900 172 HIS A CG  
1203 N ND1 . HIS A 156 ? 0.3307 0.3601 0.1623 -0.0383 -0.0268 -0.0874 172 HIS A ND1 
1204 C CD2 . HIS A 156 ? 0.3630 0.3712 0.2068 -0.0363 -0.0192 -0.0894 172 HIS A CD2 
1205 C CE1 . HIS A 156 ? 0.3341 0.3616 0.1808 -0.0382 -0.0323 -0.0849 172 HIS A CE1 
1206 N NE2 . HIS A 156 ? 0.3748 0.3892 0.2286 -0.0370 -0.0281 -0.0866 172 HIS A NE2 
1207 N N   . PHE A 157 ? 0.3652 0.3897 0.2064 -0.0268 -0.0117 -0.0581 173 PHE A N   
1208 C CA  . PHE A 157 ? 0.3863 0.4084 0.2442 -0.0250 -0.0107 -0.0486 173 PHE A CA  
1209 C C   . PHE A 157 ? 0.4038 0.4335 0.2591 -0.0212 -0.0041 -0.0366 173 PHE A C   
1210 O O   . PHE A 157 ? 0.3947 0.4340 0.2452 -0.0193 -0.0047 -0.0286 173 PHE A O   
1211 C CB  . PHE A 157 ? 0.3902 0.4131 0.2662 -0.0263 -0.0197 -0.0426 173 PHE A CB  
1212 C CG  . PHE A 157 ? 0.3245 0.3396 0.2049 -0.0283 -0.0252 -0.0527 173 PHE A CG  
1213 C CD1 . PHE A 157 ? 0.2941 0.2996 0.1783 -0.0277 -0.0230 -0.0597 173 PHE A CD1 
1214 C CD2 . PHE A 157 ? 0.3012 0.3197 0.1816 -0.0294 -0.0320 -0.0542 173 PHE A CD2 
1215 C CE1 . PHE A 157 ? 0.3119 0.3105 0.1996 -0.0280 -0.0270 -0.0677 173 PHE A CE1 
1216 C CE2 . PHE A 157 ? 0.2939 0.3060 0.1788 -0.0302 -0.0362 -0.0621 173 PHE A CE2 
1217 C CZ  . PHE A 157 ? 0.2989 0.3006 0.1873 -0.0294 -0.0334 -0.0689 173 PHE A CZ  
1218 N N   . ARG A 158 ? 0.3291 0.3558 0.1878 -0.0191 0.0028  -0.0345 174 ARG A N   
1219 C CA  . ARG A 158 ? 0.4103 0.4444 0.2644 -0.0145 0.0112  -0.0238 174 ARG A CA  
1220 C C   . ARG A 158 ? 0.4267 0.4708 0.2975 -0.0141 0.0089  -0.0072 174 ARG A C   
1221 O O   . ARG A 158 ? 0.4222 0.4751 0.2849 -0.0100 0.0136  0.0025  174 ARG A O   
1222 C CB  . ARG A 158 ? 0.4787 0.5090 0.3355 -0.0119 0.0189  -0.0243 174 ARG A CB  
1223 C CG  . ARG A 158 ? 0.4742 0.5127 0.3268 -0.0061 0.0290  -0.0126 174 ARG A CG  
1224 C CD  . ARG A 158 ? 0.4368 0.4692 0.2792 -0.0015 0.0390  -0.0179 174 ARG A CD  
1225 N NE  . ARG A 158 ? 0.4380 0.4595 0.2544 -0.0003 0.0437  -0.0313 174 ARG A NE  
1226 C CZ  . ARG A 158 ? 0.4400 0.4598 0.2351 0.0054  0.0539  -0.0313 174 ARG A CZ  
1227 N NH1 . ARG A 158 ? 0.4344 0.4639 0.2305 0.0119  0.0615  -0.0174 174 ARG A NH1 
1228 N NH2 . ARG A 158 ? 0.4450 0.4531 0.2178 0.0047  0.0568  -0.0458 174 ARG A NH2 
1229 N N   . ASP A 159 ? 0.4095 0.4517 0.3032 -0.0180 0.0022  -0.0036 175 ASP A N   
1230 C CA  . ASP A 159 ? 0.4389 0.4878 0.3523 -0.0187 0.0010  0.0121  175 ASP A CA  
1231 C C   . ASP A 159 ? 0.3729 0.4209 0.2914 -0.0204 -0.0065 0.0150  175 ASP A C   
1232 O O   . ASP A 159 ? 0.3512 0.4007 0.2890 -0.0220 -0.0081 0.0269  175 ASP A O   
1233 C CB  . ASP A 159 ? 0.4025 0.4501 0.3400 -0.0222 -0.0009 0.0147  175 ASP A CB  
1234 C CG  . ASP A 159 ? 0.4323 0.4828 0.3656 -0.0193 0.0066  0.0127  175 ASP A CG  
1235 O OD1 . ASP A 159 ? 0.4825 0.5262 0.4123 -0.0194 0.0049  0.0006  175 ASP A OD1 
1236 O OD2 . ASP A 159 ? 0.4859 0.5460 0.4190 -0.0157 0.0151  0.0240  175 ASP A OD2 
1237 N N   . PHE A 160 ? 0.3495 0.3952 0.2523 -0.0202 -0.0107 0.0049  176 PHE A N   
1238 C CA  . PHE A 160 ? 0.3279 0.3747 0.2345 -0.0203 -0.0173 0.0085  176 PHE A CA  
1239 C C   . PHE A 160 ? 0.3764 0.4348 0.2797 -0.0152 -0.0128 0.0240  176 PHE A C   
1240 O O   . PHE A 160 ? 0.4349 0.5018 0.3204 -0.0107 -0.0069 0.0253  176 PHE A O   
1241 C CB  . PHE A 160 ? 0.3393 0.3848 0.2305 -0.0210 -0.0224 -0.0054 176 PHE A CB  
1242 C CG  . PHE A 160 ? 0.3823 0.4331 0.2740 -0.0193 -0.0282 -0.0008 176 PHE A CG  
1243 C CD1 . PHE A 160 ? 0.3509 0.3941 0.2589 -0.0208 -0.0342 0.0015  176 PHE A CD1 
1244 C CD2 . PHE A 160 ? 0.4229 0.4868 0.2977 -0.0153 -0.0276 0.0012  176 PHE A CD2 
1245 C CE1 . PHE A 160 ? 0.3340 0.3821 0.2420 -0.0178 -0.0385 0.0070  176 PHE A CE1 
1246 C CE2 . PHE A 160 ? 0.4044 0.4758 0.2796 -0.0124 -0.0328 0.0065  176 PHE A CE2 
1247 C CZ  . PHE A 160 ? 0.3462 0.4095 0.2383 -0.0135 -0.0377 0.0101  176 PHE A CZ  
1248 N N   . ASP A 161 ? 0.3402 0.3981 0.2600 -0.0151 -0.0151 0.0359  177 ASP A N   
1249 C CA  . ASP A 161 ? 0.3533 0.4218 0.2711 -0.0089 -0.0106 0.0523  177 ASP A CA  
1250 C C   . ASP A 161 ? 0.3611 0.4294 0.2795 -0.0071 -0.0170 0.0537  177 ASP A C   
1251 O O   . ASP A 161 ? 0.3496 0.4067 0.2857 -0.0107 -0.0216 0.0544  177 ASP A O   
1252 C CB  . ASP A 161 ? 0.3564 0.4247 0.2968 -0.0094 -0.0043 0.0695  177 ASP A CB  
1253 C CG  . ASP A 161 ? 0.3719 0.4523 0.3086 -0.0011 0.0034  0.0883  177 ASP A CG  
1254 O OD1 . ASP A 161 ? 0.3809 0.4718 0.2941 0.0059  0.0038  0.0869  177 ASP A OD1 
1255 O OD2 . ASP A 161 ? 0.3763 0.4565 0.3341 -0.0014 0.0092  0.1046  177 ASP A OD2 
1256 N N   . HIS A 162 ? 0.3651 0.4463 0.2635 -0.0010 -0.0175 0.0538  178 HIS A N   
1257 C CA  . HIS A 162 ? 0.3674 0.4522 0.2650 0.0023  -0.0231 0.0563  178 HIS A CA  
1258 C C   . HIS A 162 ? 0.3922 0.4729 0.3091 0.0055  -0.0199 0.0750  178 HIS A C   
1259 O O   . HIS A 162 ? 0.3721 0.4461 0.2975 0.0057  -0.0245 0.0762  178 HIS A O   
1260 C CB  . HIS A 162 ? 0.4169 0.5207 0.2902 0.0093  -0.0238 0.0550  178 HIS A CB  
1261 C CG  . HIS A 162 ? 0.4788 0.5926 0.3520 0.0165  -0.0263 0.0657  178 HIS A CG  
1262 N ND1 . HIS A 162 ? 0.4999 0.6077 0.3824 0.0148  -0.0331 0.0626  178 HIS A ND1 
1263 C CD2 . HIS A 162 ? 0.4600 0.5903 0.3238 0.0271  -0.0223 0.0802  178 HIS A CD2 
1264 C CE1 . HIS A 162 ? 0.4718 0.5919 0.3513 0.0237  -0.0330 0.0749  178 HIS A CE1 
1265 N NE2 . HIS A 162 ? 0.4994 0.6336 0.3675 0.0314  -0.0266 0.0859  178 HIS A NE2 
1266 N N   . ASN A 163 A 0.4152 0.4990 0.3394 0.0083  -0.0110 0.0904  178 ASN A N   
1267 C CA  . ASN A 163 A 0.4094 0.4896 0.3520 0.0119  -0.0058 0.1100  178 ASN A CA  
1268 C C   . ASN A 163 A 0.3841 0.4444 0.3547 0.0028  -0.0076 0.1099  178 ASN A C   
1269 O O   . ASN A 163 A 0.4224 0.4745 0.4102 0.0040  -0.0047 0.1231  178 ASN A O   
1270 C CB  . ASN A 163 A 0.4303 0.5227 0.3705 0.0192  0.0055  0.1277  178 ASN A CB  
1271 C CG  . ASN A 163 A 0.4138 0.5259 0.3236 0.0285  0.0065  0.1254  178 ASN A CG  
1272 O OD1 . ASN A 163 A 0.4189 0.5404 0.3143 0.0343  0.0016  0.1233  178 ASN A OD1 
1273 N ND2 . ASN A 163 A 0.4174 0.5363 0.3165 0.0303  0.0124  0.1252  178 ASN A ND2 
1274 N N   . LEU A 164 ? 0.3708 0.4230 0.3461 -0.0058 -0.0120 0.0950  179 LEU A N   
1275 C CA  . LEU A 164 ? 0.3647 0.3995 0.3643 -0.0144 -0.0158 0.0914  179 LEU A CA  
1276 C C   . LEU A 164 ? 0.3541 0.3776 0.3501 -0.0180 -0.0260 0.0733  179 LEU A C   
1277 O O   . LEU A 164 ? 0.3528 0.3606 0.3663 -0.0231 -0.0304 0.0701  179 LEU A O   
1278 C CB  . LEU A 164 ? 0.3641 0.4000 0.3752 -0.0205 -0.0125 0.0903  179 LEU A CB  
1279 C CG  . LEU A 164 ? 0.4117 0.4561 0.4360 -0.0189 -0.0018 0.1098  179 LEU A CG  
1280 C CD1 . LEU A 164 ? 0.3652 0.4130 0.3998 -0.0247 0.0002  0.1064  179 LEU A CD1 
1281 C CD2 . LEU A 164 ? 0.3799 0.4141 0.4295 -0.0208 0.0008  0.1245  179 LEU A CD2 
1282 N N   . GLN A 165 ? 0.3993 0.3811 0.2391 0.0032  0.0134  -0.0050 180 GLN A N   
1283 C CA  . GLN A 165 ? 0.3644 0.3411 0.2188 0.0040  0.0081  -0.0053 180 GLN A CA  
1284 C C   . GLN A 165 ? 0.3313 0.3214 0.1835 -0.0011 -0.0021 0.0000  180 GLN A C   
1285 O O   . GLN A 165 ? 0.3426 0.3433 0.1790 -0.0066 -0.0070 -0.0008 180 GLN A O   
1286 C CB  . GLN A 165 ? 0.3178 0.2795 0.1740 0.0029  0.0091  -0.0207 180 GLN A CB  
1287 C CG  . GLN A 165 ? 0.3296 0.2797 0.1939 0.0087  0.0170  -0.0255 180 GLN A CG  
1288 C CD  . GLN A 165 ? 0.3469 0.2850 0.2094 0.0083  0.0180  -0.0414 180 GLN A CD  
1289 O OE1 . GLN A 165 ? 0.3627 0.3015 0.2124 0.0033  0.0161  -0.0504 180 GLN A OE1 
1290 N NE2 . GLN A 165 ? 0.2859 0.2121 0.1609 0.0137  0.0204  -0.0450 180 GLN A NE2 
1291 N N   . LEU A 166 ? 0.2970 0.2873 0.1653 0.0004  -0.0051 0.0051  181 LEU A N   
1292 C CA  . LEU A 166 ? 0.3063 0.3115 0.1797 -0.0043 -0.0143 0.0101  181 LEU A CA  
1293 C C   . LEU A 166 ? 0.3149 0.3127 0.1891 -0.0117 -0.0178 -0.0018 181 LEU A C   
1294 O O   . LEU A 166 ? 0.3213 0.3017 0.2000 -0.0100 -0.0130 -0.0083 181 LEU A O   
1295 C CB  . LEU A 166 ? 0.3196 0.3315 0.2127 0.0022  -0.0135 0.0238  181 LEU A CB  
1296 C CG  . LEU A 166 ? 0.3281 0.3459 0.2231 0.0098  -0.0109 0.0378  181 LEU A CG  
1297 C CD1 . LEU A 166 ? 0.2724 0.2898 0.1883 0.0175  -0.0072 0.0474  181 LEU A CD1 
1298 C CD2 . LEU A 166 ? 0.3478 0.3851 0.2336 0.0068  -0.0202 0.0458  181 LEU A CD2 
1299 N N   . CYS A 167 ? 0.3158 0.3261 0.1848 -0.0205 -0.0270 -0.0041 182 CYS A N   
1300 C CA  . CYS A 167 ? 0.2799 0.2842 0.1509 -0.0295 -0.0312 -0.0140 182 CYS A CA  
1301 C C   . CYS A 167 ? 0.3118 0.3312 0.2036 -0.0315 -0.0354 -0.0042 182 CYS A C   
1302 O O   . CYS A 167 ? 0.3108 0.3529 0.2072 -0.0347 -0.0438 0.0031  182 CYS A O   
1303 C CB  . CYS A 167 ? 0.3137 0.3211 0.1656 -0.0397 -0.0385 -0.0249 182 CYS A CB  
1304 S SG  . CYS A 167 ? 0.3936 0.3862 0.2443 -0.0517 -0.0425 -0.0400 182 CYS A SG  
1305 N N   . VAL A 168 ? 0.2596 0.2672 0.1641 -0.0295 -0.0294 -0.0039 183 VAL A N   
1306 C CA  . VAL A 168 ? 0.2654 0.2862 0.1915 -0.0289 -0.0288 0.0060  183 VAL A CA  
1307 C C   . VAL A 168 ? 0.2794 0.2925 0.2107 -0.0390 -0.0292 -0.0006 183 VAL A C   
1308 O O   . VAL A 168 ? 0.2798 0.2682 0.2031 -0.0394 -0.0242 -0.0080 183 VAL A O   
1309 C CB  . VAL A 168 ? 0.2443 0.2577 0.1796 -0.0170 -0.0190 0.0141  183 VAL A CB  
1310 C CG1 . VAL A 168 ? 0.2583 0.2864 0.2162 -0.0156 -0.0167 0.0235  183 VAL A CG1 
1311 C CG2 . VAL A 168 ? 0.2337 0.2510 0.1632 -0.0081 -0.0179 0.0205  183 VAL A CG2 
1312 N N   . GLY A 169 ? 0.2754 0.3098 0.2210 -0.0472 -0.0355 0.0029  184 GLY A N   
1313 C CA  . GLY A 169 ? 0.3038 0.3334 0.2574 -0.0581 -0.0348 -0.0014 184 GLY A CA  
1314 C C   . GLY A 169 ? 0.2919 0.3303 0.2423 -0.0732 -0.0459 -0.0092 184 GLY A C   
1315 O O   . GLY A 169 ? 0.3371 0.3628 0.2669 -0.0772 -0.0504 -0.0199 184 GLY A O   
1316 N N   . ASN A 170 ? 0.3178 0.3783 0.2894 -0.0820 -0.0497 -0.0046 185 ASN A N   
1317 C CA  . ASN A 170 ? 0.3509 0.4210 0.3222 -0.0986 -0.0611 -0.0123 185 ASN A CA  
1318 C C   . ASN A 170 ? 0.3373 0.3753 0.2942 -0.1087 -0.0579 -0.0249 185 ASN A C   
1319 O O   . ASN A 170 ? 0.3266 0.3510 0.2914 -0.1102 -0.0488 -0.0229 185 ASN A O   
1320 C CB  . ASN A 170 ? 0.3525 0.4553 0.3555 -0.1056 -0.0647 -0.0036 185 ASN A CB  
1321 C CG  . ASN A 170 ? 0.3866 0.5056 0.3922 -0.1234 -0.0792 -0.0105 185 ASN A CG  
1322 O OD1 . ASN A 170 ? 0.4547 0.5558 0.4364 -0.1320 -0.0851 -0.0233 185 ASN A OD1 
1323 N ND2 . ASN A 170 ? 0.3304 0.4839 0.3665 -0.1293 -0.0848 -0.0026 185 ASN A ND2 
1324 N N   . PRO A 171 ? 0.3677 0.3915 0.3027 -0.1156 -0.0648 -0.0380 186 PRO A N   
1325 C CA  . PRO A 171 ? 0.3989 0.3882 0.3203 -0.1232 -0.0614 -0.0500 186 PRO A CA  
1326 C C   . PRO A 171 ? 0.4826 0.4721 0.4181 -0.1401 -0.0629 -0.0513 186 PRO A C   
1327 O O   . PRO A 171 ? 0.5252 0.4836 0.4527 -0.1451 -0.0579 -0.0573 186 PRO A O   
1328 C CB  . PRO A 171 ? 0.4647 0.4441 0.3614 -0.1265 -0.0687 -0.0641 186 PRO A CB  
1329 C CG  . PRO A 171 ? 0.4121 0.4259 0.3115 -0.1282 -0.0792 -0.0595 186 PRO A CG  
1330 C CD  . PRO A 171 ? 0.4399 0.4753 0.3587 -0.1152 -0.0746 -0.0423 186 PRO A CD  
1331 N N   . ARG A 172 A 0.5301 0.5534 0.4876 -0.1493 -0.0697 -0.0452 186 ARG A N   
1332 C CA  . ARG A 172 A 0.5698 0.5968 0.5439 -0.1672 -0.0707 -0.0463 186 ARG A CA  
1333 C C   . ARG A 172 A 0.5387 0.5725 0.5359 -0.1645 -0.0583 -0.0339 186 ARG A C   
1334 O O   . ARG A 172 A 0.5095 0.5535 0.5260 -0.1793 -0.0574 -0.0321 186 ARG A O   
1335 C CB  . ARG A 172 A 0.5566 0.6189 0.5449 -0.1808 -0.0857 -0.0475 186 ARG A CB  
1336 C CG  . ARG A 172 A 0.5943 0.6706 0.5666 -0.1751 -0.0975 -0.0505 186 ARG A CG  
1337 C CD  . ARG A 172 A 0.6199 0.7380 0.6117 -0.1859 -0.1130 -0.0468 186 ARG A CD  
1338 N NE  . ARG A 172 A 0.7097 0.8514 0.6971 -0.1734 -0.1207 -0.0390 186 ARG A NE  
1339 C CZ  . ARG A 172 A 0.7890 0.9285 0.7486 -0.1746 -0.1313 -0.0469 186 ARG A CZ  
1340 N NH1 . ARG A 172 A 0.8487 0.9642 0.7832 -0.1874 -0.1354 -0.0642 186 ARG A NH1 
1341 N NH2 . ARG A 172 A 0.7291 0.8894 0.6848 -0.1629 -0.1372 -0.0371 186 ARG A NH2 
1342 N N   . LYS A 173 B 0.3681 0.3966 0.3636 -0.1469 -0.0482 -0.0258 186 LYS A N   
1343 C CA  . LYS A 173 B 0.3502 0.3810 0.3623 -0.1432 -0.0348 -0.0154 186 LYS A CA  
1344 C C   . LYS A 173 B 0.3985 0.3912 0.3886 -0.1327 -0.0244 -0.0161 186 LYS A C   
1345 O O   . LYS A 173 B 0.4425 0.4103 0.4092 -0.1277 -0.0278 -0.0242 186 LYS A O   
1346 C CB  . LYS A 173 B 0.3693 0.4366 0.4055 -0.1317 -0.0330 -0.0035 186 LYS A CB  
1347 C CG  . LYS A 173 B 0.3058 0.4148 0.3702 -0.1417 -0.0433 -0.0002 186 LYS A CG  
1348 C CD  . LYS A 173 B 0.3358 0.4767 0.4321 -0.1320 -0.0360 0.0129  186 LYS A CD  
1349 C CE  . LYS A 173 B 0.3125 0.4979 0.4416 -0.1414 -0.0473 0.0170  186 LYS A CE  
1350 N NZ  . LYS A 173 B 0.2808 0.4972 0.4459 -0.1321 -0.0381 0.0293  186 LYS A NZ  
1351 N N   . THR A 174 ? 0.3407 0.3294 0.3386 -0.1295 -0.0115 -0.0079 187 THR A N   
1352 C CA  . THR A 174 ? 0.3801 0.3360 0.3579 -0.1190 -0.0026 -0.0070 187 THR A CA  
1353 C C   . THR A 174 ? 0.3450 0.3108 0.3259 -0.1011 0.0033  0.0001  187 THR A C   
1354 O O   . THR A 174 ? 0.3698 0.3102 0.3330 -0.0913 0.0081  -0.0001 187 THR A O   
1355 C CB  . THR A 174 ? 0.4373 0.3746 0.4138 -0.1284 0.0082  -0.0033 187 THR A CB  
1356 O OG1 . THR A 174 ? 0.3788 0.3456 0.3813 -0.1315 0.0170  0.0054  187 THR A OG1 
1357 C CG2 . THR A 174 ? 0.3586 0.2777 0.3284 -0.1461 0.0028  -0.0104 187 THR A CG2 
1358 N N   . LYS A 175 ? 0.3429 0.3439 0.3464 -0.0968 0.0025  0.0065  188 LYS A N   
1359 C CA  . LYS A 175 ? 0.3086 0.3173 0.3163 -0.0801 0.0085  0.0133  188 LYS A CA  
1360 C C   . LYS A 175 ? 0.3108 0.3042 0.2980 -0.0692 0.0029  0.0091  188 LYS A C   
1361 O O   . LYS A 175 ? 0.3091 0.3100 0.2916 -0.0711 -0.0079 0.0045  188 LYS A O   
1362 C CB  . LYS A 175 ? 0.3128 0.3621 0.3501 -0.0772 0.0065  0.0211  188 LYS A CB  
1363 C CG  . LYS A 175 ? 0.2989 0.3697 0.3628 -0.0880 0.0124  0.0253  188 LYS A CG  
1364 C CD  . LYS A 175 ? 0.3343 0.4433 0.4305 -0.0795 0.0139  0.0347  188 LYS A CD  
1365 C CE  . LYS A 175 ? 0.4105 0.5421 0.5118 -0.0757 -0.0026 0.0362  188 LYS A CE  
1366 N NZ  . LYS A 175 ? 0.3760 0.5431 0.5094 -0.0653 -0.0021 0.0469  188 LYS A NZ  
1367 N N   . SER A 176 ? 0.3003 0.2729 0.2751 -0.0584 0.0105  0.0103  189 SER A N   
1368 C CA  . SER A 176 ? 0.3066 0.2637 0.2641 -0.0486 0.0068  0.0062  189 SER A CA  
1369 C C   . SER A 176 ? 0.3226 0.2607 0.2717 -0.0385 0.0160  0.0090  189 SER A C   
1370 O O   . SER A 176 ? 0.3137 0.2432 0.2630 -0.0408 0.0246  0.0119  189 SER A O   
1371 C CB  . SER A 176 ? 0.3861 0.3213 0.3253 -0.0550 -0.0002 -0.0041 189 SER A CB  
1372 O OG  . SER A 176 ? 0.4301 0.3486 0.3548 -0.0450 -0.0010 -0.0081 189 SER A OG  
1373 N N   . ALA A 177 ? 0.2888 0.2206 0.2297 -0.0282 0.0143  0.0077  190 ALA A N   
1374 C CA  . ALA A 177 ? 0.3151 0.2233 0.2432 -0.0208 0.0195  0.0071  190 ALA A CA  
1375 C C   . ALA A 177 ? 0.3189 0.1999 0.2296 -0.0252 0.0154  -0.0002 190 ALA A C   
1376 O O   . ALA A 177 ? 0.2920 0.1714 0.1999 -0.0323 0.0089  -0.0058 190 ALA A O   
1377 C CB  . ALA A 177 ? 0.2799 0.1911 0.2076 -0.0097 0.0189  0.0081  190 ALA A CB  
1378 N N   . PHE A 178 ? 0.2965 0.1549 0.1948 -0.0208 0.0186  -0.0002 191 PHE A N   
1379 C CA  . PHE A 178 ? 0.3115 0.1427 0.1940 -0.0236 0.0140  -0.0053 191 PHE A CA  
1380 C C   . PHE A 178 ? 0.2984 0.1110 0.1695 -0.0149 0.0142  -0.0054 191 PHE A C   
1381 O O   . PHE A 178 ? 0.2745 0.0956 0.1502 -0.0073 0.0171  -0.0034 191 PHE A O   
1382 C CB  . PHE A 178 ? 0.2929 0.1139 0.1712 -0.0348 0.0169  -0.0031 191 PHE A CB  
1383 C CG  . PHE A 178 ? 0.3358 0.1295 0.1999 -0.0389 0.0106  -0.0078 191 PHE A CG  
1384 C CD1 . PHE A 178 ? 0.3417 0.1327 0.2059 -0.0378 0.0026  -0.0159 191 PHE A CD1 
1385 C CD2 . PHE A 178 ? 0.3317 0.1009 0.1813 -0.0435 0.0132  -0.0041 191 PHE A CD2 
1386 C CE1 . PHE A 178 ? 0.3539 0.1182 0.2069 -0.0401 -0.0028 -0.0206 191 PHE A CE1 
1387 C CE2 . PHE A 178 ? 0.3480 0.0972 0.1886 -0.0450 0.0066  -0.0070 191 PHE A CE2 
1388 C CZ  . PHE A 178 ? 0.3500 0.1025 0.1969 -0.0418 -0.0013 -0.0147 191 PHE A CZ  
1389 N N   . LYS A 179 ? 0.3117 0.0983 0.1683 -0.0161 0.0100  -0.0075 192 LYS A N   
1390 C CA  . LYS A 179 ? 0.3126 0.0950 0.1647 -0.0082 0.0071  -0.0071 192 LYS A CA  
1391 C C   . LYS A 179 ? 0.3104 0.0911 0.1567 -0.0066 0.0150  -0.0022 192 LYS A C   
1392 O O   . LYS A 179 ? 0.3058 0.0784 0.1450 -0.0129 0.0232  0.0022  192 LYS A O   
1393 C CB  . LYS A 179 ? 0.3191 0.0918 0.1652 -0.0098 0.0010  -0.0070 192 LYS A CB  
1394 C CG  . LYS A 179 ? 0.3377 0.1109 0.1911 -0.0100 -0.0057 -0.0124 192 LYS A CG  
1395 C CD  . LYS A 179 ? 0.3952 0.1565 0.2433 -0.0097 -0.0110 -0.0110 192 LYS A CD  
1396 C CE  . LYS A 179 ? 0.4240 0.1854 0.2816 -0.0080 -0.0163 -0.0170 192 LYS A CE  
1397 N NZ  . LYS A 179 ? 0.4141 0.1713 0.2716 -0.0166 -0.0145 -0.0204 192 LYS A NZ  
1398 N N   . GLY A 180 ? 0.3564 0.1454 0.2066 0.0009  0.0134  -0.0030 193 GLY A N   
1399 C CA  . GLY A 180 ? 0.3317 0.1195 0.1769 0.0032  0.0208  -0.0003 193 GLY A CA  
1400 C C   . GLY A 180 ? 0.3107 0.1067 0.1659 0.0068  0.0291  0.0016  193 GLY A C   
1401 O O   . GLY A 180 ? 0.3252 0.1229 0.1803 0.0108  0.0346  0.0026  193 GLY A O   
1402 N N   . ASP A 181 ? 0.2848 0.0964 0.1534 0.0053  0.0288  0.0023  194 ASP A N   
1403 C CA  . ASP A 181 ? 0.2791 0.1137 0.1648 0.0093  0.0335  0.0057  194 ASP A CA  
1404 C C   . ASP A 181 ? 0.2718 0.1132 0.1635 0.0150  0.0282  0.0034  194 ASP A C   
1405 O O   . ASP A 181 ? 0.3036 0.1618 0.2075 0.0188  0.0311  0.0073  194 ASP A O   
1406 C CB  . ASP A 181 ? 0.2695 0.1249 0.1687 0.0035  0.0346  0.0087  194 ASP A CB  
1407 C CG  . ASP A 181 ? 0.2752 0.1278 0.1726 -0.0030 0.0421  0.0117  194 ASP A CG  
1408 O OD1 . ASP A 181 ? 0.2985 0.1449 0.1921 -0.0001 0.0512  0.0140  194 ASP A OD1 
1409 O OD2 . ASP A 181 ? 0.3093 0.1653 0.2086 -0.0118 0.0396  0.0112  194 ASP A OD2 
1410 N N   . SER A 182 ? 0.2857 0.1146 0.1699 0.0158  0.0210  -0.0022 195 SER A N   
1411 C CA  . SER A 182 ? 0.3105 0.1467 0.2012 0.0203  0.0176  -0.0049 195 SER A CA  
1412 C C   . SER A 182 ? 0.2913 0.1285 0.1861 0.0257  0.0221  -0.0021 195 SER A C   
1413 O O   . SER A 182 ? 0.3191 0.1548 0.2124 0.0250  0.0231  -0.0017 195 SER A O   
1414 C CB  . SER A 182 ? 0.3279 0.1603 0.2179 0.0198  0.0095  -0.0109 195 SER A CB  
1415 O OG  . SER A 182 ? 0.3928 0.2187 0.2777 0.0154  0.0058  -0.0141 195 SER A OG  
1416 N N   . GLY A 183 ? 0.2486 0.1002 0.1532 0.0286  0.0235  0.0003  196 GLY A N   
1417 C CA  . GLY A 183 ? 0.2439 0.0955 0.1535 0.0332  0.0283  0.0038  196 GLY A CA  
1418 C C   . GLY A 183 ? 0.2656 0.1256 0.1822 0.0357  0.0355  0.0114  196 GLY A C   
1419 O O   . GLY A 183 ? 0.2987 0.1596 0.2213 0.0402  0.0397  0.0154  196 GLY A O   
1420 N N   . GLY A 184 ? 0.2878 0.1540 0.2056 0.0331  0.0372  0.0135  197 GLY A N   
1421 C CA  . GLY A 184 ? 0.2623 0.1403 0.1915 0.0362  0.0440  0.0207  197 GLY A CA  
1422 C C   . GLY A 184 ? 0.2708 0.1702 0.2123 0.0383  0.0414  0.0274  197 GLY A C   
1423 O O   . GLY A 184 ? 0.2653 0.1729 0.2044 0.0348  0.0346  0.0256  197 GLY A O   
1424 N N   . PRO A 185 ? 0.2845 0.1927 0.2385 0.0445  0.0468  0.0352  198 PRO A N   
1425 C CA  . PRO A 185 ? 0.3245 0.2517 0.2887 0.0474  0.0431  0.0435  198 PRO A CA  
1426 C C   . PRO A 185 ? 0.2756 0.2258 0.2492 0.0436  0.0382  0.0470  198 PRO A C   
1427 O O   . PRO A 185 ? 0.2831 0.2381 0.2642 0.0417  0.0417  0.0466  198 PRO A O   
1428 C CB  . PRO A 185 ? 0.3240 0.2482 0.2989 0.0567  0.0507  0.0508  198 PRO A CB  
1429 C CG  . PRO A 185 ? 0.3428 0.2576 0.3189 0.0576  0.0591  0.0469  198 PRO A CG  
1430 C CD  . PRO A 185 ? 0.3143 0.2140 0.2728 0.0498  0.0567  0.0367  198 PRO A CD  
1431 N N   . LEU A 186 ? 0.2683 0.2328 0.2408 0.0414  0.0302  0.0500  199 LEU A N   
1432 C CA  . LEU A 186 ? 0.2683 0.2576 0.2514 0.0384  0.0236  0.0552  199 LEU A CA  
1433 C C   . LEU A 186 ? 0.2830 0.2860 0.2817 0.0476  0.0242  0.0681  199 LEU A C   
1434 O O   . LEU A 186 ? 0.2930 0.2949 0.2864 0.0515  0.0220  0.0739  199 LEU A O   
1435 C CB  . LEU A 186 ? 0.2557 0.2520 0.2261 0.0308  0.0140  0.0511  199 LEU A CB  
1436 C CG  . LEU A 186 ? 0.2460 0.2683 0.2250 0.0260  0.0048  0.0556  199 LEU A CG  
1437 C CD1 . LEU A 186 ? 0.2790 0.3063 0.2672 0.0189  0.0051  0.0509  199 LEU A CD1 
1438 C CD2 . LEU A 186 ? 0.2627 0.2898 0.2248 0.0197  -0.0040 0.0518  199 LEU A CD2 
1439 N N   . LEU A 187 ? 0.2457 0.2614 0.2644 0.0514  0.0277  0.0731  200 LEU A N   
1440 C CA  . LEU A 187 ? 0.3361 0.3623 0.3735 0.0626  0.0298  0.0853  200 LEU A CA  
1441 C C   . LEU A 187 ? 0.3496 0.4070 0.4021 0.0614  0.0186  0.0939  200 LEU A C   
1442 O O   . LEU A 187 ? 0.3064 0.3815 0.3742 0.0571  0.0173  0.0926  200 LEU A O   
1443 C CB  . LEU A 187 ? 0.2689 0.2879 0.3206 0.0693  0.0428  0.0845  200 LEU A CB  
1444 C CG  . LEU A 187 ? 0.3148 0.3025 0.3516 0.0726  0.0525  0.0784  200 LEU A CG  
1445 C CD1 . LEU A 187 ? 0.2788 0.2567 0.3203 0.0742  0.0651  0.0726  200 LEU A CD1 
1446 C CD2 . LEU A 187 ? 0.3552 0.3351 0.3954 0.0827  0.0542  0.0871  200 LEU A CD2 
1447 N N   . CYS A 188 ? 0.3702 0.4344 0.4177 0.0646  0.0101  0.1030  201 CYS A N   
1448 C CA  . CYS A 188 ? 0.4244 0.5178 0.4838 0.0645  -0.0028 0.1131  201 CYS A CA  
1449 C C   . CYS A 188 ? 0.5269 0.6271 0.6066 0.0792  -0.0017 0.1283  201 CYS A C   
1450 O O   . CYS A 188 ? 0.5406 0.6240 0.6102 0.0859  0.0011  0.1346  201 CYS A O   
1451 C CB  . CYS A 188 ? 0.4439 0.5396 0.4787 0.0568  -0.0143 0.1128  201 CYS A CB  
1452 S SG  . CYS A 188 ? 0.6861 0.7679 0.6951 0.0419  -0.0143 0.0942  201 CYS A SG  
1453 N N   . ALA A 189 ? 0.5782 0.7027 0.6881 0.0841  -0.0034 0.1344  202 ALA A N   
1454 C CA  . ALA A 189 ? 0.6923 0.8266 0.8268 0.0995  -0.0034 0.1496  202 ALA A CA  
1455 C C   . ALA A 189 ? 0.5413 0.6463 0.6759 0.1107  0.0125  0.1495  202 ALA A C   
1456 O O   . ALA A 189 ? 0.5769 0.6759 0.7175 0.1210  0.0126  0.1596  202 ALA A O   
1457 C CB  . ALA A 189 ? 0.5411 0.6872 0.6679 0.1018  -0.0194 0.1638  202 ALA A CB  
1458 N N   . GLY A 190 ? 0.4983 0.5820 0.6228 0.1062  0.0255  0.1356  207 GLY A N   
1459 C CA  . GLY A 190 ? 0.4188 0.4734 0.5405 0.1146  0.0401  0.1329  207 GLY A CA  
1460 C C   . GLY A 190 ? 0.5069 0.5330 0.6000 0.1113  0.0411  0.1299  207 GLY A C   
1461 O O   . GLY A 190 ? 0.4205 0.4215 0.5073 0.1131  0.0517  0.1233  207 GLY A O   
1462 N N   . VAL A 191 ? 0.4891 0.5195 0.5628 0.1024  0.0302  0.1304  208 VAL A N   
1463 C CA  . VAL A 191 ? 0.4572 0.4645 0.5061 0.0983  0.0316  0.1276  208 VAL A CA  
1464 C C   . VAL A 191 ? 0.3970 0.4006 0.4263 0.0850  0.0297  0.1132  208 VAL A C   
1465 O O   . VAL A 191 ? 0.3560 0.3784 0.3829 0.0775  0.0208  0.1108  208 VAL A O   
1466 C CB  . VAL A 191 ? 0.4515 0.4651 0.4927 0.0992  0.0223  0.1402  208 VAL A CB  
1467 C CG1 . VAL A 191 ? 0.4917 0.4872 0.5070 0.0914  0.0237  0.1352  208 VAL A CG1 
1468 C CG2 . VAL A 191 ? 0.4848 0.4940 0.5404 0.1071  0.0251  0.1465  208 VAL A CG2 
1469 N N   . ALA A 192 ? 0.3933 0.3723 0.4093 0.0823  0.0375  0.1034  209 ALA A N   
1470 C CA  . ALA A 192 ? 0.4026 0.3756 0.4019 0.0715  0.0359  0.0900  209 ALA A CA  
1471 C C   . ALA A 192 ? 0.3411 0.3196 0.3244 0.0655  0.0283  0.0911  209 ALA A C   
1472 O O   . ALA A 192 ? 0.3605 0.3273 0.3352 0.0664  0.0310  0.0940  209 ALA A O   
1473 C CB  . ALA A 192 ? 0.3813 0.3279 0.3728 0.0712  0.0448  0.0805  209 ALA A CB  
1474 N N   . GLN A 193 ? 0.2919 0.2876 0.2708 0.0585  0.0197  0.0882  210 GLN A N   
1475 C CA  . GLN A 193 ? 0.2956 0.2969 0.2569 0.0520  0.0133  0.0873  210 GLN A CA  
1476 C C   . GLN A 193 ? 0.2699 0.2621 0.2173 0.0436  0.0139  0.0719  210 GLN A C   
1477 O O   . GLN A 193 ? 0.2636 0.2577 0.1957 0.0385  0.0112  0.0687  210 GLN A O   
1478 C CB  . GLN A 193 ? 0.2906 0.3172 0.2539 0.0496  0.0018  0.0943  210 GLN A CB  
1479 C CG  . GLN A 193 ? 0.3550 0.3933 0.3322 0.0589  -0.0015 0.1115  210 GLN A CG  
1480 C CD  . GLN A 193 ? 0.4515 0.4825 0.4152 0.0619  -0.0013 0.1219  210 GLN A CD  
1481 O OE1 . GLN A 193 ? 0.4995 0.5214 0.4429 0.0557  0.0010  0.1161  210 GLN A OE1 
1482 N NE2 . GLN A 193 ? 0.4489 0.4838 0.4246 0.0717  -0.0029 0.1380  210 GLN A NE2 
1483 N N   . GLY A 194 ? 0.2714 0.2530 0.2229 0.0422  0.0178  0.0626  211 GLY A N   
1484 C CA  . GLY A 194 ? 0.2678 0.2401 0.2079 0.0353  0.0171  0.0491  211 GLY A CA  
1485 C C   . GLY A 194 ? 0.2385 0.1917 0.1806 0.0366  0.0229  0.0419  211 GLY A C   
1486 O O   . GLY A 194 ? 0.2352 0.1838 0.1867 0.0413  0.0278  0.0457  211 GLY A O   
1487 N N   . ILE A 195 ? 0.2318 0.1737 0.1642 0.0326  0.0223  0.0312  212 ILE A N   
1488 C CA  . ILE A 195 ? 0.2480 0.1713 0.1787 0.0328  0.0251  0.0238  212 ILE A CA  
1489 C C   . ILE A 195 ? 0.2303 0.1500 0.1540 0.0266  0.0202  0.0145  212 ILE A C   
1490 O O   . ILE A 195 ? 0.2063 0.1296 0.1238 0.0234  0.0167  0.0091  212 ILE A O   
1491 C CB  . ILE A 195 ? 0.2618 0.1723 0.1902 0.0353  0.0282  0.0207  212 ILE A CB  
1492 C CG1 . ILE A 195 ? 0.3070 0.2162 0.2420 0.0407  0.0336  0.0298  212 ILE A CG1 
1493 C CG2 . ILE A 195 ? 0.2572 0.1497 0.1819 0.0346  0.0278  0.0124  212 ILE A CG2 
1494 C CD1 . ILE A 195 ? 0.3126 0.2104 0.2472 0.0414  0.0367  0.0271  212 ILE A CD1 
1495 N N   . VAL A 196 ? 0.2086 0.1197 0.1325 0.0247  0.0209  0.0127  213 VAL A N   
1496 C CA  . VAL A 196 ? 0.2342 0.1379 0.1511 0.0186  0.0166  0.0049  213 VAL A CA  
1497 C C   . VAL A 196 ? 0.2283 0.1184 0.1380 0.0197  0.0143  -0.0036 213 VAL A C   
1498 O O   . VAL A 196 ? 0.2255 0.1034 0.1347 0.0237  0.0160  -0.0046 213 VAL A O   
1499 C CB  . VAL A 196 ? 0.2386 0.1320 0.1547 0.0165  0.0194  0.0057  213 VAL A CB  
1500 C CG1 . VAL A 196 ? 0.2239 0.1092 0.1330 0.0091  0.0148  -0.0005 213 VAL A CG1 
1501 C CG2 . VAL A 196 ? 0.2152 0.1240 0.1432 0.0173  0.0240  0.0141  213 VAL A CG2 
1502 N N   . SER A 197 ? 0.2160 0.1082 0.1211 0.0161  0.0101  -0.0103 214 SER A N   
1503 C CA  . SER A 197 ? 0.2460 0.1280 0.1480 0.0183  0.0086  -0.0189 214 SER A CA  
1504 C C   . SER A 197 ? 0.2560 0.1222 0.1522 0.0153  0.0041  -0.0266 214 SER A C   
1505 O O   . SER A 197 ? 0.2618 0.1119 0.1570 0.0184  0.0023  -0.0292 214 SER A O   
1506 C CB  . SER A 197 ? 0.2523 0.1477 0.1532 0.0182  0.0097  -0.0217 214 SER A CB  
1507 O OG  . SER A 197 ? 0.2727 0.1608 0.1743 0.0213  0.0104  -0.0301 214 SER A OG  
1508 N N   . TYR A 198 ? 0.2391 0.1083 0.1311 0.0089  0.0014  -0.0299 215 TYR A N   
1509 C CA  . TYR A 198 ? 0.2719 0.1232 0.1581 0.0058  -0.0027 -0.0373 215 TYR A CA  
1510 C C   . TYR A 198 ? 0.2681 0.1255 0.1509 -0.0035 -0.0052 -0.0394 215 TYR A C   
1511 O O   . TYR A 198 ? 0.2591 0.1364 0.1445 -0.0069 -0.0049 -0.0352 215 TYR A O   
1512 C CB  . TYR A 198 ? 0.2650 0.1074 0.1510 0.0109  -0.0039 -0.0471 215 TYR A CB  
1513 C CG  . TYR A 198 ? 0.2898 0.1451 0.1738 0.0097  -0.0021 -0.0539 215 TYR A CG  
1514 C CD1 . TYR A 198 ? 0.2840 0.1549 0.1714 0.0134  0.0026  -0.0517 215 TYR A CD1 
1515 C CD2 . TYR A 198 ? 0.2844 0.1344 0.1611 0.0041  -0.0045 -0.0628 215 TYR A CD2 
1516 C CE1 . TYR A 198 ? 0.3125 0.1943 0.1943 0.0117  0.0052  -0.0576 215 TYR A CE1 
1517 C CE2 . TYR A 198 ? 0.3035 0.1640 0.1745 0.0025  -0.0024 -0.0702 215 TYR A CE2 
1518 C CZ  . TYR A 198 ? 0.3174 0.1942 0.1901 0.0063  0.0027  -0.0673 215 TYR A CZ  
1519 O OH  . TYR A 198 ? 0.3191 0.2056 0.1825 0.0041  0.0058  -0.0742 215 TYR A OH  
1520 N N   . GLY A 199 ? 0.2726 0.1119 0.1497 -0.0078 -0.0086 -0.0459 216 GLY A N   
1521 C CA  . GLY A 199 ? 0.2865 0.1273 0.1598 -0.0181 -0.0117 -0.0499 216 GLY A CA  
1522 C C   . GLY A 199 ? 0.3176 0.1316 0.1843 -0.0209 -0.0148 -0.0577 216 GLY A C   
1523 O O   . GLY A 199 ? 0.3115 0.1232 0.1865 -0.0123 -0.0143 -0.0596 216 GLY A O   
1524 N N   . ARG A 200 ? 0.3258 0.1341 0.1900 -0.0319 -0.0171 -0.0582 217 ARG A N   
1525 C CA  . ARG A 200 ? 0.3548 0.1481 0.2215 -0.0336 -0.0188 -0.0614 217 ARG A CA  
1526 C C   . ARG A 200 ? 0.3651 0.1460 0.2330 -0.0328 -0.0176 -0.0517 217 ARG A C   
1527 O O   . ARG A 200 ? 0.3405 0.1201 0.2038 -0.0373 -0.0151 -0.0445 217 ARG A O   
1528 C CB  . ARG A 200 ? 0.3894 0.1816 0.2518 -0.0473 -0.0219 -0.0678 217 ARG A CB  
1529 C CG  . ARG A 200 ? 0.4058 0.2090 0.2654 -0.0476 -0.0237 -0.0790 217 ARG A CG  
1530 C CD  . ARG A 200 ? 0.5007 0.3084 0.3553 -0.0632 -0.0282 -0.0844 217 ARG A CD  
1531 N NE  . ARG A 200 ? 0.5667 0.3587 0.4257 -0.0702 -0.0291 -0.0839 217 ARG A NE  
1532 C CZ  . ARG A 200 ? 0.6437 0.4232 0.5060 -0.0673 -0.0292 -0.0911 217 ARG A CZ  
1533 N NH1 . ARG A 200 ? 0.6941 0.4756 0.5578 -0.0576 -0.0279 -0.0999 217 ARG A NH1 
1534 N NH2 . ARG A 200 ? 0.5735 0.3379 0.4382 -0.0749 -0.0301 -0.0896 217 ARG A NH2 
1535 N N   . SER A 201 ? 0.4266 0.1981 0.2995 -0.0276 -0.0188 -0.0519 218 SER A N   
1536 C CA  . SER A 201 ? 0.4460 0.2055 0.3163 -0.0266 -0.0186 -0.0428 218 SER A CA  
1537 C C   . SER A 201 ? 0.4236 0.1725 0.2861 -0.0398 -0.0172 -0.0387 218 SER A C   
1538 O O   . SER A 201 ? 0.3932 0.1363 0.2495 -0.0419 -0.0142 -0.0300 218 SER A O   
1539 C CB  . SER A 201 ? 0.4448 0.1952 0.3207 -0.0196 -0.0214 -0.0445 218 SER A CB  
1540 O OG  . SER A 201 ? 0.5647 0.3257 0.4499 -0.0089 -0.0217 -0.0470 218 SER A OG  
1541 N N   . ASP A 202 ? 0.3749 0.1219 0.2379 -0.0498 -0.0185 -0.0452 219 ASP A N   
1542 C CA  . ASP A 202 ? 0.4172 0.1572 0.2764 -0.0650 -0.0168 -0.0418 219 ASP A CA  
1543 C C   . ASP A 202 ? 0.4307 0.1840 0.2897 -0.0753 -0.0140 -0.0395 219 ASP A C   
1544 O O   . ASP A 202 ? 0.4968 0.2512 0.3580 -0.0907 -0.0123 -0.0376 219 ASP A O   
1545 C CB  . ASP A 202 ? 0.4097 0.1434 0.2716 -0.0731 -0.0201 -0.0501 219 ASP A CB  
1546 C CG  . ASP A 202 ? 0.4971 0.2448 0.3616 -0.0738 -0.0234 -0.0616 219 ASP A CG  
1547 O OD1 . ASP A 202 ? 0.4962 0.2582 0.3600 -0.0679 -0.0232 -0.0624 219 ASP A OD1 
1548 O OD2 . ASP A 202 ? 0.5583 0.3023 0.4242 -0.0805 -0.0262 -0.0699 219 ASP A OD2 
1549 N N   . ALA A 203 ? 0.4105 0.1766 0.2700 -0.0676 -0.0133 -0.0394 220 ALA A N   
1550 C CA  . ALA A 203 ? 0.4108 0.2097 0.2835 -0.0683 -0.0091 -0.0324 220 ALA A CA  
1551 C C   . ALA A 203 ? 0.3887 0.2124 0.2724 -0.0791 -0.0125 -0.0356 220 ALA A C   
1552 O O   . ALA A 203 ? 0.4079 0.2589 0.3058 -0.0816 -0.0097 -0.0285 220 ALA A O   
1553 C CB  . ALA A 203 ? 0.3904 0.1877 0.2647 -0.0713 -0.0012 -0.0216 220 ALA A CB  
1554 N N   . LYS A 204 ? 0.4238 0.2390 0.3017 -0.0854 -0.0188 -0.0462 221 LYS A N   
1555 C CA  . LYS A 204 ? 0.3873 0.2277 0.2732 -0.0954 -0.0241 -0.0501 221 LYS A CA  
1556 C C   . LYS A 204 ? 0.3427 0.2088 0.2315 -0.0854 -0.0258 -0.0492 221 LYS A C   
1557 O O   . LYS A 204 ? 0.3873 0.2443 0.2659 -0.0760 -0.0264 -0.0555 221 LYS A O   
1558 C CB  . LYS A 204 ? 0.4543 0.2761 0.3298 -0.1052 -0.0303 -0.0634 221 LYS A CB  
1559 C CG  . LYS A 204 ? 0.4426 0.2434 0.3179 -0.1197 -0.0297 -0.0635 221 LYS A CG  
1560 C CD  . LYS A 204 ? 0.4630 0.2535 0.3347 -0.1243 -0.0348 -0.0754 221 LYS A CD  
1561 C CE  . LYS A 204 ? 0.4512 0.2253 0.3275 -0.1343 -0.0330 -0.0730 221 LYS A CE  
1562 N NZ  . LYS A 204 ? 0.5194 0.2826 0.3944 -0.1358 -0.0371 -0.0843 221 LYS A NZ  
1563 N N   . PRO A 205 ? 0.3550 0.2531 0.2586 -0.0867 -0.0262 -0.0410 224 PRO A N   
1564 C CA  . PRO A 205 ? 0.3759 0.2965 0.2812 -0.0773 -0.0281 -0.0382 224 PRO A CA  
1565 C C   . PRO A 205 ? 0.3501 0.2757 0.2441 -0.0823 -0.0363 -0.0486 224 PRO A C   
1566 O O   . PRO A 205 ? 0.3950 0.3104 0.2831 -0.0944 -0.0411 -0.0581 224 PRO A O   
1567 C CB  . PRO A 205 ? 0.3076 0.2593 0.2339 -0.0789 -0.0273 -0.0264 224 PRO A CB  
1568 C CG  . PRO A 205 ? 0.3893 0.3415 0.3247 -0.0939 -0.0283 -0.0272 224 PRO A CG  
1569 C CD  . PRO A 205 ? 0.3652 0.2804 0.2864 -0.0966 -0.0243 -0.0332 224 PRO A CD  
1570 N N   . PRO A 206 ? 0.3422 0.2818 0.2310 -0.0740 -0.0376 -0.0477 225 PRO A N   
1571 C CA  . PRO A 206 ? 0.2941 0.2460 0.1890 -0.0608 -0.0328 -0.0369 225 PRO A CA  
1572 C C   . PRO A 206 ? 0.2864 0.2162 0.1755 -0.0492 -0.0250 -0.0380 225 PRO A C   
1573 O O   . PRO A 206 ? 0.2974 0.2038 0.1759 -0.0489 -0.0242 -0.0479 225 PRO A O   
1574 C CB  . PRO A 206 ? 0.3150 0.2857 0.2013 -0.0599 -0.0385 -0.0377 225 PRO A CB  
1575 C CG  . PRO A 206 ? 0.3730 0.3456 0.2501 -0.0739 -0.0474 -0.0483 225 PRO A CG  
1576 C CD  . PRO A 206 ? 0.3309 0.2751 0.2048 -0.0794 -0.0446 -0.0579 225 PRO A CD  
1577 N N   . ALA A 207 ? 0.2695 0.2065 0.1668 -0.0392 -0.0198 -0.0279 226 ALA A N   
1578 C CA  . ALA A 207 ? 0.2810 0.2022 0.1742 -0.0283 -0.0139 -0.0282 226 ALA A CA  
1579 C C   . ALA A 207 ? 0.2563 0.1899 0.1461 -0.0214 -0.0131 -0.0261 226 ALA A C   
1580 O O   . ALA A 207 ? 0.2572 0.2118 0.1482 -0.0235 -0.0168 -0.0213 226 ALA A O   
1581 C CB  . ALA A 207 ? 0.2509 0.1673 0.1532 -0.0234 -0.0079 -0.0193 226 ALA A CB  
1582 N N   . VAL A 208 ? 0.2523 0.1732 0.1384 -0.0134 -0.0085 -0.0291 227 VAL A N   
1583 C CA  . VAL A 208 ? 0.2494 0.1789 0.1319 -0.0076 -0.0058 -0.0277 227 VAL A CA  
1584 C C   . VAL A 208 ? 0.2639 0.1954 0.1561 0.0005  -0.0007 -0.0172 227 VAL A C   
1585 O O   . VAL A 208 ? 0.2524 0.1694 0.1488 0.0041  0.0021  -0.0172 227 VAL A O   
1586 C CB  . VAL A 208 ? 0.2570 0.1731 0.1314 -0.0050 -0.0033 -0.0396 227 VAL A CB  
1587 C CG1 . VAL A 208 ? 0.2755 0.2015 0.1472 0.0000  0.0016  -0.0374 227 VAL A CG1 
1588 C CG2 . VAL A 208 ? 0.2750 0.1863 0.1387 -0.0127 -0.0075 -0.0513 227 VAL A CG2 
1589 N N   . PHE A 209 ? 0.2322 0.1801 0.1264 0.0029  0.0000  -0.0083 228 PHE A N   
1590 C CA  . PHE A 209 ? 0.2381 0.1873 0.1413 0.0103  0.0050  0.0019  228 PHE A CA  
1591 C C   . PHE A 209 ? 0.2480 0.2003 0.1462 0.0141  0.0086  0.0039  228 PHE A C   
1592 O O   . PHE A 209 ? 0.2480 0.2110 0.1365 0.0109  0.0065  0.0034  228 PHE A O   
1593 C CB  . PHE A 209 ? 0.2334 0.1988 0.1470 0.0108  0.0031  0.0135  228 PHE A CB  
1594 C CG  . PHE A 209 ? 0.2337 0.1959 0.1566 0.0086  0.0036  0.0139  228 PHE A CG  
1595 C CD1 . PHE A 209 ? 0.2352 0.1925 0.1543 0.0005  -0.0001 0.0059  228 PHE A CD1 
1596 C CD2 . PHE A 209 ? 0.2506 0.2140 0.1856 0.0143  0.0088  0.0222  228 PHE A CD2 
1597 C CE1 . PHE A 209 ? 0.2667 0.2209 0.1935 -0.0026 0.0017  0.0072  228 PHE A CE1 
1598 C CE2 . PHE A 209 ? 0.2287 0.1899 0.1712 0.0119  0.0113  0.0225  228 PHE A CE2 
1599 C CZ  . PHE A 209 ? 0.2356 0.1927 0.1738 0.0030  0.0079  0.0155  228 PHE A CZ  
1600 N N   . THR A 210 ? 0.2247 0.1674 0.1284 0.0197  0.0143  0.0060  229 THR A N   
1601 C CA  . THR A 210 ? 0.2954 0.2412 0.1971 0.0225  0.0191  0.0099  229 THR A CA  
1602 C C   . THR A 210 ? 0.2348 0.1935 0.1377 0.0243  0.0186  0.0238  229 THR A C   
1603 O O   . THR A 210 ? 0.2515 0.2120 0.1642 0.0274  0.0178  0.0315  229 THR A O   
1604 C CB  . THR A 210 ? 0.2722 0.2044 0.1817 0.0268  0.0244  0.0087  229 THR A CB  
1605 O OG1 . THR A 210 ? 0.3088 0.2296 0.2185 0.0261  0.0229  -0.0030 229 THR A OG1 
1606 C CG2 . THR A 210 ? 0.2491 0.1844 0.1581 0.0279  0.0303  0.0121  229 THR A CG2 
1607 N N   . ARG A 211 ? 0.2467 0.2142 0.1394 0.0227  0.0193  0.0273  230 ARG A N   
1608 C CA  . ARG A 211 ? 0.2596 0.2375 0.1518 0.0252  0.0180  0.0422  230 ARG A CA  
1609 C C   . ARG A 211 ? 0.3070 0.2748 0.2075 0.0308  0.0255  0.0501  230 ARG A C   
1610 O O   . ARG A 211 ? 0.3256 0.2864 0.2229 0.0298  0.0320  0.0465  230 ARG A O   
1611 C CB  . ARG A 211 ? 0.3366 0.3256 0.2104 0.0206  0.0158  0.0439  230 ARG A CB  
1612 C CG  . ARG A 211 ? 0.3710 0.3708 0.2351 0.0142  0.0069  0.0374  230 ARG A CG  
1613 C CD  . ARG A 211 ? 0.4423 0.4515 0.2838 0.0092  0.0051  0.0386  230 ARG A CD  
1614 N NE  . ARG A 211 ? 0.4857 0.5044 0.3161 0.0018  -0.0045 0.0312  230 ARG A NE  
1615 C CZ  . ARG A 211 ? 0.4654 0.4999 0.2943 -0.0004 -0.0157 0.0401  230 ARG A CZ  
1616 N NH1 . ARG A 211 ? 0.4312 0.4741 0.2694 0.0056  -0.0187 0.0574  230 ARG A NH1 
1617 N NH2 . ARG A 211 ? 0.4747 0.5167 0.2939 -0.0088 -0.0246 0.0312  230 ARG A NH2 
1618 N N   . ILE A 212 ? 0.2718 0.2389 0.1842 0.0364  0.0251  0.0602  231 ILE A N   
1619 C CA  . ILE A 212 ? 0.3259 0.2803 0.2460 0.0415  0.0322  0.0670  231 ILE A CA  
1620 C C   . ILE A 212 ? 0.3037 0.2611 0.2162 0.0421  0.0342  0.0795  231 ILE A C   
1621 O O   . ILE A 212 ? 0.3059 0.2515 0.2197 0.0425  0.0415  0.0819  231 ILE A O   
1622 C CB  . ILE A 212 ? 0.3490 0.2992 0.2838 0.0481  0.0326  0.0722  231 ILE A CB  
1623 C CG1 . ILE A 212 ? 0.3181 0.2609 0.2570 0.0465  0.0329  0.0600  231 ILE A CG1 
1624 C CG2 . ILE A 212 ? 0.3774 0.3130 0.3190 0.0535  0.0397  0.0799  231 ILE A CG2 
1625 C CD1 . ILE A 212 ? 0.3408 0.2771 0.2919 0.0524  0.0363  0.0631  231 ILE A CD1 
1626 N N   . SER A 213 ? 0.3808 0.3535 0.2844 0.0412  0.0275  0.0877  232 SER A N   
1627 C CA  . SER A 213 ? 0.4010 0.3757 0.2946 0.0420  0.0283  0.1022  232 SER A CA  
1628 C C   . SER A 213 ? 0.3656 0.3334 0.2466 0.0362  0.0370  0.0981  232 SER A C   
1629 O O   . SER A 213 ? 0.4085 0.3689 0.2864 0.0370  0.0426  0.1093  232 SER A O   
1630 C CB  . SER A 213 ? 0.4195 0.4131 0.3016 0.0403  0.0175  0.1096  232 SER A CB  
1631 O OG  . SER A 213 ? 0.4042 0.4055 0.2703 0.0320  0.0150  0.0968  232 SER A OG  
1632 N N   . HIS A 214 ? 0.3908 0.3606 0.2658 0.0305  0.0388  0.0823  233 HIS A N   
1633 C CA  . HIS A 214 ? 0.3294 0.2956 0.1962 0.0254  0.0483  0.0770  233 HIS A CA  
1634 C C   . HIS A 214 ? 0.3585 0.3101 0.2407 0.0269  0.0569  0.0770  233 HIS A C   
1635 O O   . HIS A 214 ? 0.4348 0.3833 0.3133 0.0232  0.0657  0.0799  233 HIS A O   
1636 C CB  . HIS A 214 ? 0.3638 0.3347 0.2252 0.0208  0.0485  0.0589  233 HIS A CB  
1637 C CG  . HIS A 214 ? 0.4459 0.4294 0.2869 0.0166  0.0425  0.0570  233 HIS A CG  
1638 N ND1 . HIS A 214 ? 0.5277 0.5191 0.3510 0.0149  0.0397  0.0703  233 HIS A ND1 
1639 C CD2 . HIS A 214 ? 0.4595 0.4477 0.2938 0.0131  0.0380  0.0431  233 HIS A CD2 
1640 C CE1 . HIS A 214 ? 0.5475 0.5490 0.3530 0.0100  0.0333  0.0640  233 HIS A CE1 
1641 N NE2 . HIS A 214 ? 0.5238 0.5230 0.3362 0.0087  0.0326  0.0470  233 HIS A NE2 
1642 N N   . TYR A 215 ? 0.3436 0.2861 0.2420 0.0313  0.0548  0.0733  234 TYR A N   
1643 C CA  . TYR A 215 ? 0.3851 0.3132 0.2971 0.0315  0.0612  0.0698  234 TYR A CA  
1644 C C   . TYR A 215 ? 0.4195 0.3348 0.3395 0.0364  0.0629  0.0821  234 TYR A C   
1645 O O   . TYR A 215 ? 0.3658 0.2670 0.2972 0.0370  0.0661  0.0779  234 TYR A O   
1646 C CB  . TYR A 215 ? 0.3560 0.2798 0.2772 0.0320  0.0580  0.0546  234 TYR A CB  
1647 C CG  . TYR A 215 ? 0.3664 0.3003 0.2809 0.0286  0.0557  0.0425  234 TYR A CG  
1648 C CD1 . TYR A 215 ? 0.3577 0.2981 0.2663 0.0293  0.0482  0.0388  234 TYR A CD1 
1649 C CD2 . TYR A 215 ? 0.3609 0.2977 0.2763 0.0247  0.0617  0.0344  234 TYR A CD2 
1650 C CE1 . TYR A 215 ? 0.3267 0.2729 0.2283 0.0261  0.0463  0.0271  234 TYR A CE1 
1651 C CE2 . TYR A 215 ? 0.3786 0.3228 0.2885 0.0228  0.0606  0.0224  234 TYR A CE2 
1652 C CZ  . TYR A 215 ? 0.3104 0.2578 0.2124 0.0236  0.0527  0.0187  234 TYR A CZ  
1653 O OH  . TYR A 215 ? 0.3200 0.2716 0.2160 0.0216  0.0519  0.0062  234 TYR A OH  
1654 N N   . ARG A 216 ? 0.4007 0.3200 0.3151 0.0402  0.0601  0.0970  235 ARG A N   
1655 C CA  . ARG A 216 ? 0.5010 0.4070 0.4246 0.0461  0.0620  0.1088  235 ARG A CA  
1656 C C   . ARG A 216 ? 0.5056 0.3982 0.4337 0.0415  0.0699  0.1096  235 ARG A C   
1657 O O   . ARG A 216 ? 0.4968 0.3763 0.4380 0.0431  0.0713  0.1053  235 ARG A O   
1658 C CB  . ARG A 216 ? 0.5923 0.5101 0.5130 0.0498  0.0544  0.1213  235 ARG A CB  
1659 C CG  . ARG A 216 ? 0.6231 0.5474 0.5557 0.0572  0.0476  0.1215  235 ARG A CG  
1660 C CD  . ARG A 216 ? 0.6484 0.5582 0.5978 0.0608  0.0518  0.1141  235 ARG A CD  
1661 N NE  . ARG A 216 ? 0.7077 0.6042 0.6625 0.0607  0.0561  0.1180  235 ARG A NE  
1662 C CZ  . ARG A 216 ? 0.7205 0.6155 0.6838 0.0665  0.0542  0.1261  235 ARG A CZ  
1663 N NH1 . ARG A 216 ? 0.7180 0.6258 0.6877 0.0731  0.0482  0.1317  235 ARG A NH1 
1664 N NH2 . ARG A 216 ? 0.7185 0.5985 0.6847 0.0656  0.0584  0.1291  235 ARG A NH2 
1665 N N   . PRO A 217 ? 0.5475 0.4430 0.4648 0.0349  0.0754  0.1143  236 PRO A N   
1666 C CA  . PRO A 217 ? 0.5113 0.3939 0.4356 0.0293  0.0836  0.1147  236 PRO A CA  
1667 C C   . PRO A 217 ? 0.4755 0.3479 0.4115 0.0265  0.0887  0.1021  236 PRO A C   
1668 O O   . PRO A 217 ? 0.5264 0.3855 0.4741 0.0241  0.0913  0.0999  236 PRO A O   
1669 C CB  . PRO A 217 ? 0.5409 0.4326 0.4499 0.0219  0.0896  0.1205  236 PRO A CB  
1670 C CG  . PRO A 217 ? 0.5088 0.4152 0.4017 0.0249  0.0813  0.1267  236 PRO A CG  
1671 C CD  . PRO A 217 ? 0.5407 0.4516 0.4385 0.0313  0.0747  0.1190  236 PRO A CD  
1672 N N   . TRP A 218 ? 0.4701 0.3546 0.4067 0.0254  0.0849  0.0878  237 TRP A N   
1673 C CA  . TRP A 218 ? 0.4559 0.3352 0.4057 0.0228  0.0845  0.0727  237 TRP A CA  
1674 C C   . TRP A 218 ? 0.4690 0.3331 0.4255 0.0284  0.0801  0.0702  237 TRP A C   
1675 O O   . TRP A 218 ? 0.4797 0.3305 0.4458 0.0257  0.0816  0.0640  237 TRP A O   
1676 C CB  . TRP A 218 ? 0.3927 0.2875 0.3409 0.0216  0.0807  0.0592  237 TRP A CB  
1677 C CG  . TRP A 218 ? 0.3831 0.2745 0.3451 0.0194  0.0787  0.0449  237 TRP A CG  
1678 C CD1 . TRP A 218 ? 0.3974 0.2913 0.3716 0.0133  0.0838  0.0389  237 TRP A CD1 
1679 C CD2 . TRP A 218 ? 0.3734 0.2590 0.3384 0.0232  0.0706  0.0354  237 TRP A CD2 
1680 N NE1 . TRP A 218 ? 0.3597 0.2504 0.3451 0.0136  0.0775  0.0264  237 TRP A NE1 
1681 C CE2 . TRP A 218 ? 0.3899 0.2741 0.3677 0.0196  0.0694  0.0244  237 TRP A CE2 
1682 C CE3 . TRP A 218 ? 0.3467 0.2289 0.3050 0.0289  0.0643  0.0355  237 TRP A CE3 
1683 C CZ2 . TRP A 218 ? 0.3373 0.2148 0.3181 0.0218  0.0612  0.0145  237 TRP A CZ2 
1684 C CZ3 . TRP A 218 ? 0.3476 0.2227 0.3086 0.0303  0.0581  0.0254  237 TRP A CZ3 
1685 C CH2 . TRP A 218 ? 0.3441 0.2159 0.3146 0.0269  0.0561  0.0154  237 TRP A CH2 
1686 N N   . ILE A 219 ? 0.4741 0.3406 0.4257 0.0356  0.0750  0.0743  238 ILE A N   
1687 C CA  . ILE A 219 ? 0.4985 0.3554 0.4568 0.0404  0.0717  0.0704  238 ILE A CA  
1688 C C   . ILE A 219 ? 0.4965 0.3454 0.4618 0.0403  0.0737  0.0749  238 ILE A C   
1689 O O   . ILE A 219 ? 0.4659 0.3065 0.4371 0.0405  0.0724  0.0675  238 ILE A O   
1690 C CB  . ILE A 219 ? 0.4621 0.3297 0.4173 0.0468  0.0661  0.0726  238 ILE A CB  
1691 C CG1 . ILE A 219 ? 0.4237 0.3005 0.3728 0.0450  0.0620  0.0638  238 ILE A CG1 
1692 C CG2 . ILE A 219 ? 0.4505 0.3145 0.4138 0.0502  0.0639  0.0671  238 ILE A CG2 
1693 C CD1 . ILE A 219 ? 0.4156 0.3056 0.3617 0.0489  0.0564  0.0666  238 ILE A CD1 
1694 N N   . ASN A 220 ? 0.5147 0.3651 0.4772 0.0392  0.0768  0.0869  239 ASN A N   
1695 C CA  . ASN A 220 ? 0.5064 0.3464 0.4743 0.0394  0.0785  0.0924  239 ASN A CA  
1696 C C   . ASN A 220 ? 0.5169 0.3426 0.4916 0.0325  0.0824  0.0845  239 ASN A C   
1697 O O   . ASN A 220 ? 0.5474 0.3614 0.5265 0.0325  0.0835  0.0865  239 ASN A O   
1698 C CB  . ASN A 220 ? 0.5715 0.4155 0.5324 0.0384  0.0801  0.1073  239 ASN A CB  
1699 C CG  . ASN A 220 ? 0.6133 0.4613 0.5745 0.0465  0.0748  0.1171  239 ASN A CG  
1700 O OD1 . ASN A 220 ? 0.6482 0.4986 0.6161 0.0530  0.0712  0.1129  239 ASN A OD1 
1701 N ND2 . ASN A 220 ? 0.6507 0.4998 0.6049 0.0457  0.0744  0.1306  239 ASN A ND2 
1702 N N   . GLN A 221 ? 0.5071 0.3329 0.4832 0.0266  0.0842  0.0759  240 GLN A N   
1703 C CA  . GLN A 221 ? 0.5449 0.3588 0.5293 0.0196  0.0856  0.0670  240 GLN A CA  
1704 C C   . GLN A 221 ? 0.5489 0.3544 0.5351 0.0226  0.0802  0.0585  240 GLN A C   
1705 O O   . GLN A 221 ? 0.5493 0.3420 0.5396 0.0190  0.0811  0.0567  240 GLN A O   
1706 C CB  . GLN A 221 ? 0.5431 0.3605 0.5314 0.0142  0.0863  0.0577  240 GLN A CB  
1707 C CG  . GLN A 221 ? 0.5458 0.3710 0.5336 0.0091  0.0949  0.0645  240 GLN A CG  
1708 C CD  . GLN A 221 ? 0.5847 0.4241 0.5819 0.0042  0.0917  0.0500  240 GLN A CD  
1709 O OE1 . GLN A 221 ? 0.5277 0.3654 0.5388 -0.0037 0.0936  0.0440  240 GLN A OE1 
1710 N NE2 . GLN A 221 ? 0.4751 0.3291 0.4665 0.0090  0.0860  0.0440  240 GLN A NE2 
1711 N N   . ILE A 222 ? 0.5798 0.3923 0.5620 0.0284  0.0751  0.0534  241 ILE A N   
1712 C CA  . ILE A 222 ? 0.6195 0.4254 0.6013 0.0305  0.0714  0.0456  241 ILE A CA  
1713 C C   . ILE A 222 ? 0.6365 0.4371 0.6201 0.0363  0.0742  0.0530  241 ILE A C   
1714 O O   . ILE A 222 ? 0.7074 0.4955 0.6921 0.0360  0.0746  0.0484  241 ILE A O   
1715 C CB  . ILE A 222 ? 0.5669 0.3821 0.5437 0.0336  0.0665  0.0388  241 ILE A CB  
1716 N N   . LEU A 223 ? 0.6714 0.4803 0.6550 0.0418  0.0757  0.0645  242 LEU A N   
1717 C CA  . LEU A 223 ? 0.6267 0.4317 0.6139 0.0487  0.0773  0.0725  242 LEU A CA  
1718 C C   . LEU A 223 ? 0.6927 0.4829 0.6823 0.0458  0.0807  0.0789  242 LEU A C   
1719 O O   . LEU A 223 ? 0.6245 0.4125 0.6127 0.0389  0.0826  0.0821  242 LEU A O   
1720 C CB  . LEU A 223 ? 0.6271 0.4472 0.6140 0.0553  0.0754  0.0833  242 LEU A CB  
# 
