data_9JN4
# 
_entry.id   9JN4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JN4         pdb_00009jn4 10.2210/pdb9jn4/pdb 
WWPDB D_1300051706 ?            ?                   
# 
_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       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JN4 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yunyunyang0219@163.com 
_pdbx_contact_author.name_first         Yunyun 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6042-3617 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.L.'     1 ? 
'Yang, Y.Y.'   2 ? 
'Huang, J.-W.' 3 ? 
'Chen, C.-C.'  4 ? 
'Guo, R.-T.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1265 
_citation.page_last                 1273 
_citation.title                     
'Structural Insights into the N-N Bond-Formation Mechanism of the Heme-Dependent Piperazate Synthase KtzT' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06124 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, Y.'    1 ? 
primary 'Li, Y.'      2 ? 
primary 'Yao, L.'     3 ? 
primary 'Dai, K.'     4 ? 
primary 'Fu, X.'      5 ? 
primary 'Ge, A.'      6 ? 
primary 'Huang, J.W.' 7 ? 
primary 'Guo, R.T.'   8 ? 
primary 'Chen, C.C.'  9 ? 
# 
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 'FMN-binding protein'             23249.340 4    ? C197A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   4    ? ?     ? ? 
3 water       nat water                             18.015    1006 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        KtzT,Regulator 
# 
_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       
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_strand_id                 B,D,A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLY n 
1 3   ALA n 
1 4   GLY n 
1 5   ALA n 
1 6   MET n 
1 7   PHE n 
1 8   VAL n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  TYR n 
1 13  HIS n 
1 14  ALA n 
1 15  PRO n 
1 16  GLU n 
1 17  ASP n 
1 18  ARG n 
1 19  TRP n 
1 20  LEU n 
1 21  VAL n 
1 22  ASP n 
1 23  LEU n 
1 24  VAL n 
1 25  ARG n 
1 26  GLY n 
1 27  HIS n 
1 28  PRO n 
1 29  LEU n 
1 30  ALA n 
1 31  GLN n 
1 32  LEU n 
1 33  ALA n 
1 34  SER n 
1 35  ASN n 
1 36  GLY n 
1 37  ALA n 
1 38  GLY n 
1 39  GLY n 
1 40  ALA n 
1 41  ALA n 
1 42  PRO n 
1 43  HIS n 
1 44  ILE n 
1 45  THR n 
1 46  HIS n 
1 47  VAL n 
1 48  PRO n 
1 49  ILE n 
1 50  ILE n 
1 51  VAL n 
1 52  ASP n 
1 53  PRO n 
1 54  GLU n 
1 55  LEU n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  VAL n 
1 60  ASP n 
1 61  ARG n 
1 62  LEU n 
1 63  VAL n 
1 64  GLY n 
1 65  ILE n 
1 66  THR n 
1 67  LEU n 
1 68  TRP n 
1 69  GLY n 
1 70  HIS n 
1 71  MET n 
1 72  ASN n 
1 73  ARG n 
1 74  ALA n 
1 75  ASN n 
1 76  PRO n 
1 77  HIS n 
1 78  TRP n 
1 79  ALA n 
1 80  ALA n 
1 81  LEU n 
1 82  GLY n 
1 83  GLY n 
1 84  ALA n 
1 85  ALA n 
1 86  ASN n 
1 87  VAL n 
1 88  VAL n 
1 89  ALA n 
1 90  THR n 
1 91  PHE n 
1 92  ALA n 
1 93  GLY n 
1 94  PRO n 
1 95  ASN n 
1 96  ALA n 
1 97  TYR n 
1 98  VAL n 
1 99  SER n 
1 100 PRO n 
1 101 ALA n 
1 102 VAL n 
1 103 TYR n 
1 104 ARG n 
1 105 THR n 
1 106 ALA n 
1 107 PRO n 
1 108 ALA n 
1 109 ALA n 
1 110 PRO n 
1 111 THR n 
1 112 TRP n 
1 113 ASN n 
1 114 PHE n 
1 115 THR n 
1 116 SER n 
1 117 VAL n 
1 118 GLN n 
1 119 VAL n 
1 120 ARG n 
1 121 GLY n 
1 122 GLU n 
1 123 LEU n 
1 124 ARG n 
1 125 LYS n 
1 126 VAL n 
1 127 GLU n 
1 128 SER n 
1 129 ALA n 
1 130 ASP n 
1 131 ASP n 
1 132 THR n 
1 133 LEU n 
1 134 ALA n 
1 135 THR n 
1 136 VAL n 
1 137 ARG n 
1 138 ALA n 
1 139 THR n 
1 140 VAL n 
1 141 ALA n 
1 142 ALA n 
1 143 LEU n 
1 144 GLU n 
1 145 SER n 
1 146 ARG n 
1 147 PHE n 
1 148 GLY n 
1 149 ALA n 
1 150 GLY n 
1 151 TRP n 
1 152 ASP n 
1 153 MET n 
1 154 THR n 
1 155 GLY n 
1 156 SER n 
1 157 LEU n 
1 158 ASP n 
1 159 TYR n 
1 160 PHE n 
1 161 ARG n 
1 162 ARG n 
1 163 ILE n 
1 164 LEU n 
1 165 PRO n 
1 166 GLY n 
1 167 VAL n 
1 168 GLY n 
1 169 ALA n 
1 170 PHE n 
1 171 ARG n 
1 172 LEU n 
1 173 ARG n 
1 174 VAL n 
1 175 ALA n 
1 176 GLU n 
1 177 ALA n 
1 178 ASP n 
1 179 GLY n 
1 180 MET n 
1 181 PHE n 
1 182 LYS n 
1 183 LEU n 
1 184 SER n 
1 185 GLN n 
1 186 GLU n 
1 187 GLN n 
1 188 GLN n 
1 189 PRO n 
1 190 ALA n 
1 191 ILE n 
1 192 ARG n 
1 193 ARG n 
1 194 ARG n 
1 195 VAL n 
1 196 ARG n 
1 197 HIS n 
1 198 SER n 
1 199 PHE n 
1 200 GLY n 
1 201 GLY n 
1 202 ALA n 
1 203 GLU n 
1 204 ALA n 
1 205 THR n 
1 206 ARG n 
1 207 ALA n 
1 208 VAL n 
1 209 ALA n 
1 210 GLY n 
1 211 LEU n 
1 212 MET n 
1 213 ASP n 
1 214 ARG n 
1 215 LEU n 
1 216 PRO n 
1 217 THR n 
1 218 GLU 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                   218 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KUTG_08928 
_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      'Kutzneria sp. 744' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     345341 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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   ALA 1   -4  ?   ?   ?   B . n 
A 1 2   GLY 2   -3  ?   ?   ?   B . n 
A 1 3   ALA 3   -2  ?   ?   ?   B . n 
A 1 4   GLY 4   -1  -1  GLY GLY B . n 
A 1 5   ALA 5   0   0   ALA ALA B . n 
A 1 6   MET 6   1   1   MET MET B . n 
A 1 7   PHE 7   2   2   PHE PHE B . n 
A 1 8   VAL 8   3   3   VAL VAL B . n 
A 1 9   PRO 9   4   4   PRO PRO B . n 
A 1 10  GLY 10  5   5   GLY GLY B . n 
A 1 11  PRO 11  6   6   PRO PRO B . n 
A 1 12  TYR 12  7   7   TYR TYR B . n 
A 1 13  HIS 13  8   8   HIS HIS B . n 
A 1 14  ALA 14  9   9   ALA ALA B . n 
A 1 15  PRO 15  10  10  PRO PRO B . n 
A 1 16  GLU 16  11  11  GLU GLU B . n 
A 1 17  ASP 17  12  12  ASP ASP B . n 
A 1 18  ARG 18  13  13  ARG ARG B . n 
A 1 19  TRP 19  14  14  TRP TRP B . n 
A 1 20  LEU 20  15  15  LEU LEU B . n 
A 1 21  VAL 21  16  16  VAL VAL B . n 
A 1 22  ASP 22  17  17  ASP ASP B . n 
A 1 23  LEU 23  18  18  LEU LEU B . n 
A 1 24  VAL 24  19  19  VAL VAL B . n 
A 1 25  ARG 25  20  20  ARG ARG B . n 
A 1 26  GLY 26  21  21  GLY GLY B . n 
A 1 27  HIS 27  22  22  HIS HIS B . n 
A 1 28  PRO 28  23  23  PRO PRO B . n 
A 1 29  LEU 29  24  24  LEU LEU B . n 
A 1 30  ALA 30  25  25  ALA ALA B . n 
A 1 31  GLN 31  26  26  GLN GLN B . n 
A 1 32  LEU 32  27  27  LEU LEU B . n 
A 1 33  ALA 33  28  28  ALA ALA B . n 
A 1 34  SER 34  29  29  SER SER B . n 
A 1 35  ASN 35  30  30  ASN ASN B . n 
A 1 36  GLY 36  31  31  GLY GLY B . n 
A 1 37  ALA 37  32  32  ALA ALA B . n 
A 1 38  GLY 38  33  33  GLY GLY B . n 
A 1 39  GLY 39  34  34  GLY GLY B . n 
A 1 40  ALA 40  35  35  ALA ALA B . n 
A 1 41  ALA 41  36  36  ALA ALA B . n 
A 1 42  PRO 42  37  37  PRO PRO B . n 
A 1 43  HIS 43  38  38  HIS HIS B . n 
A 1 44  ILE 44  39  39  ILE ILE B . n 
A 1 45  THR 45  40  40  THR THR B . n 
A 1 46  HIS 46  41  41  HIS HIS B . n 
A 1 47  VAL 47  42  42  VAL VAL B . n 
A 1 48  PRO 48  43  43  PRO PRO B . n 
A 1 49  ILE 49  44  44  ILE ILE B . n 
A 1 50  ILE 50  45  45  ILE ILE B . n 
A 1 51  VAL 51  46  46  VAL VAL B . n 
A 1 52  ASP 52  47  47  ASP ASP B . n 
A 1 53  PRO 53  48  48  PRO PRO B . n 
A 1 54  GLU 54  49  49  GLU GLU B . n 
A 1 55  LEU 55  50  50  LEU LEU B . n 
A 1 56  ASP 56  51  51  ASP ASP B . n 
A 1 57  GLY 57  52  52  GLY GLY B . n 
A 1 58  PRO 58  53  53  PRO PRO B . n 
A 1 59  VAL 59  54  54  VAL VAL B . n 
A 1 60  ASP 60  55  55  ASP ASP B . n 
A 1 61  ARG 61  56  56  ARG ARG B . n 
A 1 62  LEU 62  57  57  LEU LEU B . n 
A 1 63  VAL 63  58  58  VAL VAL B . n 
A 1 64  GLY 64  59  59  GLY GLY B . n 
A 1 65  ILE 65  60  60  ILE ILE B . n 
A 1 66  THR 66  61  61  THR THR B . n 
A 1 67  LEU 67  62  62  LEU LEU B . n 
A 1 68  TRP 68  63  63  TRP TRP B . n 
A 1 69  GLY 69  64  64  GLY GLY B . n 
A 1 70  HIS 70  65  65  HIS HIS B . n 
A 1 71  MET 71  66  66  MET MET B . n 
A 1 72  ASN 72  67  67  ASN ASN B . n 
A 1 73  ARG 73  68  68  ARG ARG B . n 
A 1 74  ALA 74  69  69  ALA ALA B . n 
A 1 75  ASN 75  70  70  ASN ASN B . n 
A 1 76  PRO 76  71  71  PRO PRO B . n 
A 1 77  HIS 77  72  72  HIS HIS B . n 
A 1 78  TRP 78  73  73  TRP TRP B . n 
A 1 79  ALA 79  74  74  ALA ALA B . n 
A 1 80  ALA 80  75  75  ALA ALA B . n 
A 1 81  LEU 81  76  76  LEU LEU B . n 
A 1 82  GLY 82  77  77  GLY GLY B . n 
A 1 83  GLY 83  78  78  GLY GLY B . n 
A 1 84  ALA 84  79  79  ALA ALA B . n 
A 1 85  ALA 85  80  80  ALA ALA B . n 
A 1 86  ASN 86  81  81  ASN ASN B . n 
A 1 87  VAL 87  82  82  VAL VAL B . n 
A 1 88  VAL 88  83  83  VAL VAL B . n 
A 1 89  ALA 89  84  84  ALA ALA B . n 
A 1 90  THR 90  85  85  THR THR B . n 
A 1 91  PHE 91  86  86  PHE PHE B . n 
A 1 92  ALA 92  87  87  ALA ALA B . n 
A 1 93  GLY 93  88  88  GLY GLY B . n 
A 1 94  PRO 94  89  89  PRO PRO B . n 
A 1 95  ASN 95  90  90  ASN ASN B . n 
A 1 96  ALA 96  91  91  ALA ALA B . n 
A 1 97  TYR 97  92  92  TYR TYR B . n 
A 1 98  VAL 98  93  93  VAL VAL B . n 
A 1 99  SER 99  94  94  SER SER B . n 
A 1 100 PRO 100 95  95  PRO PRO B . n 
A 1 101 ALA 101 96  96  ALA ALA B . n 
A 1 102 VAL 102 97  97  VAL VAL B . n 
A 1 103 TYR 103 98  98  TYR TYR B . n 
A 1 104 ARG 104 99  99  ARG ARG B . n 
A 1 105 THR 105 100 100 THR THR B . n 
A 1 106 ALA 106 101 101 ALA ALA B . n 
A 1 107 PRO 107 102 102 PRO PRO B . n 
A 1 108 ALA 108 103 103 ALA ALA B . n 
A 1 109 ALA 109 104 104 ALA ALA B . n 
A 1 110 PRO 110 105 105 PRO PRO B . n 
A 1 111 THR 111 106 106 THR THR B . n 
A 1 112 TRP 112 107 107 TRP TRP B . n 
A 1 113 ASN 113 108 108 ASN ASN B . n 
A 1 114 PHE 114 109 109 PHE PHE B . n 
A 1 115 THR 115 110 110 THR THR B . n 
A 1 116 SER 116 111 111 SER SER B . n 
A 1 117 VAL 117 112 112 VAL VAL B . n 
A 1 118 GLN 118 113 113 GLN GLN B . n 
A 1 119 VAL 119 114 114 VAL VAL B . n 
A 1 120 ARG 120 115 115 ARG ARG B . n 
A 1 121 GLY 121 116 116 GLY GLY B . n 
A 1 122 GLU 122 117 117 GLU GLU B . n 
A 1 123 LEU 123 118 118 LEU LEU B . n 
A 1 124 ARG 124 119 119 ARG ARG B . n 
A 1 125 LYS 125 120 120 LYS LYS B . n 
A 1 126 VAL 126 121 121 VAL VAL B . n 
A 1 127 GLU 127 122 122 GLU GLU B . n 
A 1 128 SER 128 123 123 SER SER B . n 
A 1 129 ALA 129 124 124 ALA ALA B . n 
A 1 130 ASP 130 125 125 ASP ASP B . n 
A 1 131 ASP 131 126 126 ASP ASP B . n 
A 1 132 THR 132 127 127 THR THR B . n 
A 1 133 LEU 133 128 128 LEU LEU B . n 
A 1 134 ALA 134 129 129 ALA ALA B . n 
A 1 135 THR 135 130 130 THR THR B . n 
A 1 136 VAL 136 131 131 VAL VAL B . n 
A 1 137 ARG 137 132 132 ARG ARG B . n 
A 1 138 ALA 138 133 133 ALA ALA B . n 
A 1 139 THR 139 134 134 THR THR B . n 
A 1 140 VAL 140 135 135 VAL VAL B . n 
A 1 141 ALA 141 136 136 ALA ALA B . n 
A 1 142 ALA 142 137 137 ALA ALA B . n 
A 1 143 LEU 143 138 138 LEU LEU B . n 
A 1 144 GLU 144 139 139 GLU GLU B . n 
A 1 145 SER 145 140 140 SER SER B . n 
A 1 146 ARG 146 141 141 ARG ARG B . n 
A 1 147 PHE 147 142 142 PHE PHE B . n 
A 1 148 GLY 148 143 143 GLY GLY B . n 
A 1 149 ALA 149 144 144 ALA ALA B . n 
A 1 150 GLY 150 145 145 GLY GLY B . n 
A 1 151 TRP 151 146 146 TRP TRP B . n 
A 1 152 ASP 152 147 147 ASP ASP B . n 
A 1 153 MET 153 148 148 MET MET B . n 
A 1 154 THR 154 149 149 THR THR B . n 
A 1 155 GLY 155 150 150 GLY GLY B . n 
A 1 156 SER 156 151 151 SER SER B . n 
A 1 157 LEU 157 152 152 LEU LEU B . n 
A 1 158 ASP 158 153 153 ASP ASP B . n 
A 1 159 TYR 159 154 154 TYR TYR B . n 
A 1 160 PHE 160 155 155 PHE PHE B . n 
A 1 161 ARG 161 156 156 ARG ARG B . n 
A 1 162 ARG 162 157 157 ARG ARG B . n 
A 1 163 ILE 163 158 158 ILE ILE B . n 
A 1 164 LEU 164 159 159 LEU LEU B . n 
A 1 165 PRO 165 160 160 PRO PRO B . n 
A 1 166 GLY 166 161 161 GLY GLY B . n 
A 1 167 VAL 167 162 162 VAL VAL B . n 
A 1 168 GLY 168 163 163 GLY GLY B . n 
A 1 169 ALA 169 164 164 ALA ALA B . n 
A 1 170 PHE 170 165 165 PHE PHE B . n 
A 1 171 ARG 171 166 166 ARG ARG B . n 
A 1 172 LEU 172 167 167 LEU LEU B . n 
A 1 173 ARG 173 168 168 ARG ARG B . n 
A 1 174 VAL 174 169 169 VAL VAL B . n 
A 1 175 ALA 175 170 170 ALA ALA B . n 
A 1 176 GLU 176 171 171 GLU GLU B . n 
A 1 177 ALA 177 172 172 ALA ALA B . n 
A 1 178 ASP 178 173 173 ASP ASP B . n 
A 1 179 GLY 179 174 174 GLY GLY B . n 
A 1 180 MET 180 175 175 MET MET B . n 
A 1 181 PHE 181 176 176 PHE PHE B . n 
A 1 182 LYS 182 177 177 LYS LYS B . n 
A 1 183 LEU 183 178 178 LEU LEU B . n 
A 1 184 SER 184 179 179 SER SER B . n 
A 1 185 GLN 185 180 180 GLN GLN B . n 
A 1 186 GLU 186 181 181 GLU GLU B . n 
A 1 187 GLN 187 182 182 GLN GLN B . n 
A 1 188 GLN 188 183 183 GLN GLN B . n 
A 1 189 PRO 189 184 184 PRO PRO B . n 
A 1 190 ALA 190 185 185 ALA ALA B . n 
A 1 191 ILE 191 186 186 ILE ILE B . n 
A 1 192 ARG 192 187 187 ARG ARG B . n 
A 1 193 ARG 193 188 188 ARG ARG B . n 
A 1 194 ARG 194 189 189 ARG ARG B . n 
A 1 195 VAL 195 190 190 VAL VAL B . n 
A 1 196 ARG 196 191 191 ARG ARG B . n 
A 1 197 HIS 197 192 192 HIS HIS B . n 
A 1 198 SER 198 193 193 SER SER B . n 
A 1 199 PHE 199 194 194 PHE PHE B . n 
A 1 200 GLY 200 195 195 GLY GLY B . n 
A 1 201 GLY 201 196 196 GLY GLY B . n 
A 1 202 ALA 202 197 197 ALA ALA B . n 
A 1 203 GLU 203 198 198 GLU GLU B . n 
A 1 204 ALA 204 199 199 ALA ALA B . n 
A 1 205 THR 205 200 200 THR THR B . n 
A 1 206 ARG 206 201 201 ARG ARG B . n 
A 1 207 ALA 207 202 202 ALA ALA B . n 
A 1 208 VAL 208 203 203 VAL VAL B . n 
A 1 209 ALA 209 204 204 ALA ALA B . n 
A 1 210 GLY 210 205 205 GLY GLY B . n 
A 1 211 LEU 211 206 206 LEU LEU B . n 
A 1 212 MET 212 207 207 MET MET B . n 
A 1 213 ASP 213 208 208 ASP ASP B . n 
A 1 214 ARG 214 209 209 ARG ARG B . n 
A 1 215 LEU 215 210 210 LEU LEU B . n 
A 1 216 PRO 216 211 211 PRO PRO B . n 
A 1 217 THR 217 212 ?   ?   ?   B . n 
A 1 218 GLU 218 213 ?   ?   ?   B . n 
B 1 1   ALA 1   -4  ?   ?   ?   D . n 
B 1 2   GLY 2   -3  ?   ?   ?   D . n 
B 1 3   ALA 3   -2  ?   ?   ?   D . n 
B 1 4   GLY 4   -1  ?   ?   ?   D . n 
B 1 5   ALA 5   0   0   ALA ALA D . n 
B 1 6   MET 6   1   1   MET MET D . n 
B 1 7   PHE 7   2   2   PHE PHE D . n 
B 1 8   VAL 8   3   3   VAL VAL D . n 
B 1 9   PRO 9   4   4   PRO PRO D . n 
B 1 10  GLY 10  5   5   GLY GLY D . n 
B 1 11  PRO 11  6   6   PRO PRO D . n 
B 1 12  TYR 12  7   7   TYR TYR D . n 
B 1 13  HIS 13  8   8   HIS HIS D . n 
B 1 14  ALA 14  9   9   ALA ALA D . n 
B 1 15  PRO 15  10  10  PRO PRO D . n 
B 1 16  GLU 16  11  11  GLU GLU D . n 
B 1 17  ASP 17  12  12  ASP ASP D . n 
B 1 18  ARG 18  13  13  ARG ARG D . n 
B 1 19  TRP 19  14  14  TRP TRP D . n 
B 1 20  LEU 20  15  15  LEU LEU D . n 
B 1 21  VAL 21  16  16  VAL VAL D . n 
B 1 22  ASP 22  17  17  ASP ASP D . n 
B 1 23  LEU 23  18  18  LEU LEU D . n 
B 1 24  VAL 24  19  19  VAL VAL D . n 
B 1 25  ARG 25  20  20  ARG ARG D . n 
B 1 26  GLY 26  21  21  GLY GLY D . n 
B 1 27  HIS 27  22  22  HIS HIS D . n 
B 1 28  PRO 28  23  23  PRO PRO D . n 
B 1 29  LEU 29  24  24  LEU LEU D . n 
B 1 30  ALA 30  25  25  ALA ALA D . n 
B 1 31  GLN 31  26  26  GLN GLN D . n 
B 1 32  LEU 32  27  27  LEU LEU D . n 
B 1 33  ALA 33  28  28  ALA ALA D . n 
B 1 34  SER 34  29  29  SER SER D . n 
B 1 35  ASN 35  30  30  ASN ASN D . n 
B 1 36  GLY 36  31  31  GLY GLY D . n 
B 1 37  ALA 37  32  32  ALA ALA D . n 
B 1 38  GLY 38  33  33  GLY GLY D . n 
B 1 39  GLY 39  34  34  GLY GLY D . n 
B 1 40  ALA 40  35  35  ALA ALA D . n 
B 1 41  ALA 41  36  36  ALA ALA D . n 
B 1 42  PRO 42  37  37  PRO PRO D . n 
B 1 43  HIS 43  38  38  HIS HIS D . n 
B 1 44  ILE 44  39  39  ILE ILE D . n 
B 1 45  THR 45  40  40  THR THR D . n 
B 1 46  HIS 46  41  41  HIS HIS D . n 
B 1 47  VAL 47  42  42  VAL VAL D . n 
B 1 48  PRO 48  43  43  PRO PRO D . n 
B 1 49  ILE 49  44  44  ILE ILE D . n 
B 1 50  ILE 50  45  45  ILE ILE D . n 
B 1 51  VAL 51  46  46  VAL VAL D . n 
B 1 52  ASP 52  47  47  ASP ASP D . n 
B 1 53  PRO 53  48  48  PRO PRO D . n 
B 1 54  GLU 54  49  49  GLU GLU D . n 
B 1 55  LEU 55  50  50  LEU LEU D . n 
B 1 56  ASP 56  51  51  ASP ASP D . n 
B 1 57  GLY 57  52  52  GLY GLY D . n 
B 1 58  PRO 58  53  53  PRO PRO D . n 
B 1 59  VAL 59  54  54  VAL VAL D . n 
B 1 60  ASP 60  55  55  ASP ASP D . n 
B 1 61  ARG 61  56  56  ARG ARG D . n 
B 1 62  LEU 62  57  57  LEU LEU D . n 
B 1 63  VAL 63  58  58  VAL VAL D . n 
B 1 64  GLY 64  59  59  GLY GLY D . n 
B 1 65  ILE 65  60  60  ILE ILE D . n 
B 1 66  THR 66  61  61  THR THR D . n 
B 1 67  LEU 67  62  62  LEU LEU D . n 
B 1 68  TRP 68  63  63  TRP TRP D . n 
B 1 69  GLY 69  64  64  GLY GLY D . n 
B 1 70  HIS 70  65  65  HIS HIS D . n 
B 1 71  MET 71  66  66  MET MET D . n 
B 1 72  ASN 72  67  67  ASN ASN D . n 
B 1 73  ARG 73  68  68  ARG ARG D . n 
B 1 74  ALA 74  69  69  ALA ALA D . n 
B 1 75  ASN 75  70  70  ASN ASN D . n 
B 1 76  PRO 76  71  71  PRO PRO D . n 
B 1 77  HIS 77  72  72  HIS HIS D . n 
B 1 78  TRP 78  73  73  TRP TRP D . n 
B 1 79  ALA 79  74  74  ALA ALA D . n 
B 1 80  ALA 80  75  75  ALA ALA D . n 
B 1 81  LEU 81  76  76  LEU LEU D . n 
B 1 82  GLY 82  77  77  GLY GLY D . n 
B 1 83  GLY 83  78  78  GLY GLY D . n 
B 1 84  ALA 84  79  79  ALA ALA D . n 
B 1 85  ALA 85  80  80  ALA ALA D . n 
B 1 86  ASN 86  81  81  ASN ASN D . n 
B 1 87  VAL 87  82  82  VAL VAL D . n 
B 1 88  VAL 88  83  83  VAL VAL D . n 
B 1 89  ALA 89  84  84  ALA ALA D . n 
B 1 90  THR 90  85  85  THR THR D . n 
B 1 91  PHE 91  86  86  PHE PHE D . n 
B 1 92  ALA 92  87  87  ALA ALA D . n 
B 1 93  GLY 93  88  88  GLY GLY D . n 
B 1 94  PRO 94  89  89  PRO PRO D . n 
B 1 95  ASN 95  90  90  ASN ASN D . n 
B 1 96  ALA 96  91  91  ALA ALA D . n 
B 1 97  TYR 97  92  92  TYR TYR D . n 
B 1 98  VAL 98  93  93  VAL VAL D . n 
B 1 99  SER 99  94  94  SER SER D . n 
B 1 100 PRO 100 95  95  PRO PRO D . n 
B 1 101 ALA 101 96  96  ALA ALA D . n 
B 1 102 VAL 102 97  97  VAL VAL D . n 
B 1 103 TYR 103 98  98  TYR TYR D . n 
B 1 104 ARG 104 99  99  ARG ARG D . n 
B 1 105 THR 105 100 100 THR THR D . n 
B 1 106 ALA 106 101 101 ALA ALA D . n 
B 1 107 PRO 107 102 102 PRO PRO D . n 
B 1 108 ALA 108 103 103 ALA ALA D . n 
B 1 109 ALA 109 104 104 ALA ALA D . n 
B 1 110 PRO 110 105 105 PRO PRO D . n 
B 1 111 THR 111 106 106 THR THR D . n 
B 1 112 TRP 112 107 107 TRP TRP D . n 
B 1 113 ASN 113 108 108 ASN ASN D . n 
B 1 114 PHE 114 109 109 PHE PHE D . n 
B 1 115 THR 115 110 110 THR THR D . n 
B 1 116 SER 116 111 111 SER SER D . n 
B 1 117 VAL 117 112 112 VAL VAL D . n 
B 1 118 GLN 118 113 113 GLN GLN D . n 
B 1 119 VAL 119 114 114 VAL VAL D . n 
B 1 120 ARG 120 115 115 ARG ARG D . n 
B 1 121 GLY 121 116 116 GLY GLY D . n 
B 1 122 GLU 122 117 117 GLU GLU D . n 
B 1 123 LEU 123 118 118 LEU LEU D . n 
B 1 124 ARG 124 119 119 ARG ARG D . n 
B 1 125 LYS 125 120 120 LYS LYS D . n 
B 1 126 VAL 126 121 121 VAL VAL D . n 
B 1 127 GLU 127 122 122 GLU GLU D . n 
B 1 128 SER 128 123 123 SER SER D . n 
B 1 129 ALA 129 124 124 ALA ALA D . n 
B 1 130 ASP 130 125 125 ASP ASP D . n 
B 1 131 ASP 131 126 126 ASP ASP D . n 
B 1 132 THR 132 127 127 THR THR D . n 
B 1 133 LEU 133 128 128 LEU LEU D . n 
B 1 134 ALA 134 129 129 ALA ALA D . n 
B 1 135 THR 135 130 130 THR THR D . n 
B 1 136 VAL 136 131 131 VAL VAL D . n 
B 1 137 ARG 137 132 132 ARG ARG D . n 
B 1 138 ALA 138 133 133 ALA ALA D . n 
B 1 139 THR 139 134 134 THR THR D . n 
B 1 140 VAL 140 135 135 VAL VAL D . n 
B 1 141 ALA 141 136 136 ALA ALA D . n 
B 1 142 ALA 142 137 137 ALA ALA D . n 
B 1 143 LEU 143 138 138 LEU LEU D . n 
B 1 144 GLU 144 139 139 GLU GLU D . n 
B 1 145 SER 145 140 140 SER SER D . n 
B 1 146 ARG 146 141 141 ARG ARG D . n 
B 1 147 PHE 147 142 142 PHE PHE D . n 
B 1 148 GLY 148 143 143 GLY GLY D . n 
B 1 149 ALA 149 144 144 ALA ALA D . n 
B 1 150 GLY 150 145 145 GLY GLY D . n 
B 1 151 TRP 151 146 146 TRP TRP D . n 
B 1 152 ASP 152 147 147 ASP ASP D . n 
B 1 153 MET 153 148 148 MET MET D . n 
B 1 154 THR 154 149 149 THR THR D . n 
B 1 155 GLY 155 150 150 GLY GLY D . n 
B 1 156 SER 156 151 151 SER SER D . n 
B 1 157 LEU 157 152 152 LEU LEU D . n 
B 1 158 ASP 158 153 153 ASP ASP D . n 
B 1 159 TYR 159 154 154 TYR TYR D . n 
B 1 160 PHE 160 155 155 PHE PHE D . n 
B 1 161 ARG 161 156 156 ARG ARG D . n 
B 1 162 ARG 162 157 157 ARG ARG D . n 
B 1 163 ILE 163 158 158 ILE ILE D . n 
B 1 164 LEU 164 159 159 LEU LEU D . n 
B 1 165 PRO 165 160 160 PRO PRO D . n 
B 1 166 GLY 166 161 161 GLY GLY D . n 
B 1 167 VAL 167 162 162 VAL VAL D . n 
B 1 168 GLY 168 163 163 GLY GLY D . n 
B 1 169 ALA 169 164 164 ALA ALA D . n 
B 1 170 PHE 170 165 165 PHE PHE D . n 
B 1 171 ARG 171 166 166 ARG ARG D . n 
B 1 172 LEU 172 167 167 LEU LEU D . n 
B 1 173 ARG 173 168 168 ARG ARG D . n 
B 1 174 VAL 174 169 169 VAL VAL D . n 
B 1 175 ALA 175 170 170 ALA ALA D . n 
B 1 176 GLU 176 171 171 GLU GLU D . n 
B 1 177 ALA 177 172 172 ALA ALA D . n 
B 1 178 ASP 178 173 173 ASP ASP D . n 
B 1 179 GLY 179 174 174 GLY GLY D . n 
B 1 180 MET 180 175 175 MET MET D . n 
B 1 181 PHE 181 176 176 PHE PHE D . n 
B 1 182 LYS 182 177 177 LYS LYS D . n 
B 1 183 LEU 183 178 178 LEU LEU D . n 
B 1 184 SER 184 179 179 SER SER D . n 
B 1 185 GLN 185 180 180 GLN GLN D . n 
B 1 186 GLU 186 181 181 GLU GLU D . n 
B 1 187 GLN 187 182 182 GLN GLN D . n 
B 1 188 GLN 188 183 183 GLN GLN D . n 
B 1 189 PRO 189 184 184 PRO PRO D . n 
B 1 190 ALA 190 185 185 ALA ALA D . n 
B 1 191 ILE 191 186 186 ILE ILE D . n 
B 1 192 ARG 192 187 187 ARG ARG D . n 
B 1 193 ARG 193 188 188 ARG ARG D . n 
B 1 194 ARG 194 189 189 ARG ARG D . n 
B 1 195 VAL 195 190 190 VAL VAL D . n 
B 1 196 ARG 196 191 191 ARG ARG D . n 
B 1 197 HIS 197 192 192 HIS HIS D . n 
B 1 198 SER 198 193 193 SER SER D . n 
B 1 199 PHE 199 194 194 PHE PHE D . n 
B 1 200 GLY 200 195 195 GLY GLY D . n 
B 1 201 GLY 201 196 196 GLY GLY D . n 
B 1 202 ALA 202 197 197 ALA ALA D . n 
B 1 203 GLU 203 198 198 GLU GLU D . n 
B 1 204 ALA 204 199 199 ALA ALA D . n 
B 1 205 THR 205 200 200 THR THR D . n 
B 1 206 ARG 206 201 201 ARG ARG D . n 
B 1 207 ALA 207 202 202 ALA ALA D . n 
B 1 208 VAL 208 203 203 VAL VAL D . n 
B 1 209 ALA 209 204 204 ALA ALA D . n 
B 1 210 GLY 210 205 205 GLY GLY D . n 
B 1 211 LEU 211 206 206 LEU LEU D . n 
B 1 212 MET 212 207 207 MET MET D . n 
B 1 213 ASP 213 208 208 ASP ASP D . n 
B 1 214 ARG 214 209 209 ARG ARG D . n 
B 1 215 LEU 215 210 210 LEU LEU D . n 
B 1 216 PRO 216 211 211 PRO PRO D . n 
B 1 217 THR 217 212 ?   ?   ?   D . n 
B 1 218 GLU 218 213 ?   ?   ?   D . n 
C 1 1   ALA 1   -4  ?   ?   ?   A . n 
C 1 2   GLY 2   -3  ?   ?   ?   A . n 
C 1 3   ALA 3   -2  ?   ?   ?   A . n 
C 1 4   GLY 4   -1  -1  GLY GLY A . n 
C 1 5   ALA 5   0   0   ALA ALA A . n 
C 1 6   MET 6   1   1   MET MET A . n 
C 1 7   PHE 7   2   2   PHE PHE A . n 
C 1 8   VAL 8   3   3   VAL VAL A . n 
C 1 9   PRO 9   4   4   PRO PRO A . n 
C 1 10  GLY 10  5   5   GLY GLY A . n 
C 1 11  PRO 11  6   6   PRO PRO A . n 
C 1 12  TYR 12  7   7   TYR TYR A . n 
C 1 13  HIS 13  8   8   HIS HIS A . n 
C 1 14  ALA 14  9   9   ALA ALA A . n 
C 1 15  PRO 15  10  10  PRO PRO A . n 
C 1 16  GLU 16  11  11  GLU GLU A . n 
C 1 17  ASP 17  12  12  ASP ASP A . n 
C 1 18  ARG 18  13  13  ARG ARG A . n 
C 1 19  TRP 19  14  14  TRP TRP A . n 
C 1 20  LEU 20  15  15  LEU LEU A . n 
C 1 21  VAL 21  16  16  VAL VAL A . n 
C 1 22  ASP 22  17  17  ASP ASP A . n 
C 1 23  LEU 23  18  18  LEU LEU A . n 
C 1 24  VAL 24  19  19  VAL VAL A . n 
C 1 25  ARG 25  20  20  ARG ARG A . n 
C 1 26  GLY 26  21  21  GLY GLY A . n 
C 1 27  HIS 27  22  22  HIS HIS A . n 
C 1 28  PRO 28  23  23  PRO PRO A . n 
C 1 29  LEU 29  24  24  LEU LEU A . n 
C 1 30  ALA 30  25  25  ALA ALA A . n 
C 1 31  GLN 31  26  26  GLN GLN A . n 
C 1 32  LEU 32  27  27  LEU LEU A . n 
C 1 33  ALA 33  28  28  ALA ALA A . n 
C 1 34  SER 34  29  29  SER SER A . n 
C 1 35  ASN 35  30  30  ASN ASN A . n 
C 1 36  GLY 36  31  31  GLY GLY A . n 
C 1 37  ALA 37  32  32  ALA ALA A . n 
C 1 38  GLY 38  33  33  GLY GLY A . n 
C 1 39  GLY 39  34  34  GLY GLY A . n 
C 1 40  ALA 40  35  35  ALA ALA A . n 
C 1 41  ALA 41  36  36  ALA ALA A . n 
C 1 42  PRO 42  37  37  PRO PRO A . n 
C 1 43  HIS 43  38  38  HIS HIS A . n 
C 1 44  ILE 44  39  39  ILE ILE A . n 
C 1 45  THR 45  40  40  THR THR A . n 
C 1 46  HIS 46  41  41  HIS HIS A . n 
C 1 47  VAL 47  42  42  VAL VAL A . n 
C 1 48  PRO 48  43  43  PRO PRO A . n 
C 1 49  ILE 49  44  44  ILE ILE A . n 
C 1 50  ILE 50  45  45  ILE ILE A . n 
C 1 51  VAL 51  46  46  VAL VAL A . n 
C 1 52  ASP 52  47  47  ASP ASP A . n 
C 1 53  PRO 53  48  48  PRO PRO A . n 
C 1 54  GLU 54  49  49  GLU GLU A . n 
C 1 55  LEU 55  50  50  LEU LEU A . n 
C 1 56  ASP 56  51  51  ASP ASP A . n 
C 1 57  GLY 57  52  52  GLY GLY A . n 
C 1 58  PRO 58  53  53  PRO PRO A . n 
C 1 59  VAL 59  54  54  VAL VAL A . n 
C 1 60  ASP 60  55  55  ASP ASP A . n 
C 1 61  ARG 61  56  56  ARG ARG A . n 
C 1 62  LEU 62  57  57  LEU LEU A . n 
C 1 63  VAL 63  58  58  VAL VAL A . n 
C 1 64  GLY 64  59  59  GLY GLY A . n 
C 1 65  ILE 65  60  60  ILE ILE A . n 
C 1 66  THR 66  61  61  THR THR A . n 
C 1 67  LEU 67  62  62  LEU LEU A . n 
C 1 68  TRP 68  63  63  TRP TRP A . n 
C 1 69  GLY 69  64  64  GLY GLY A . n 
C 1 70  HIS 70  65  65  HIS HIS A . n 
C 1 71  MET 71  66  66  MET MET A . n 
C 1 72  ASN 72  67  67  ASN ASN A . n 
C 1 73  ARG 73  68  68  ARG ARG A . n 
C 1 74  ALA 74  69  69  ALA ALA A . n 
C 1 75  ASN 75  70  70  ASN ASN A . n 
C 1 76  PRO 76  71  71  PRO PRO A . n 
C 1 77  HIS 77  72  72  HIS HIS A . n 
C 1 78  TRP 78  73  73  TRP TRP A . n 
C 1 79  ALA 79  74  74  ALA ALA A . n 
C 1 80  ALA 80  75  75  ALA ALA A . n 
C 1 81  LEU 81  76  76  LEU LEU A . n 
C 1 82  GLY 82  77  77  GLY GLY A . n 
C 1 83  GLY 83  78  78  GLY GLY A . n 
C 1 84  ALA 84  79  79  ALA ALA A . n 
C 1 85  ALA 85  80  80  ALA ALA A . n 
C 1 86  ASN 86  81  81  ASN ASN A . n 
C 1 87  VAL 87  82  82  VAL VAL A . n 
C 1 88  VAL 88  83  83  VAL VAL A . n 
C 1 89  ALA 89  84  84  ALA ALA A . n 
C 1 90  THR 90  85  85  THR THR A . n 
C 1 91  PHE 91  86  86  PHE PHE A . n 
C 1 92  ALA 92  87  87  ALA ALA A . n 
C 1 93  GLY 93  88  88  GLY GLY A . n 
C 1 94  PRO 94  89  89  PRO PRO A . n 
C 1 95  ASN 95  90  90  ASN ASN A . n 
C 1 96  ALA 96  91  91  ALA ALA A . n 
C 1 97  TYR 97  92  92  TYR TYR A . n 
C 1 98  VAL 98  93  93  VAL VAL A . n 
C 1 99  SER 99  94  94  SER SER A . n 
C 1 100 PRO 100 95  95  PRO PRO A . n 
C 1 101 ALA 101 96  96  ALA ALA A . n 
C 1 102 VAL 102 97  97  VAL VAL A . n 
C 1 103 TYR 103 98  98  TYR TYR A . n 
C 1 104 ARG 104 99  99  ARG ARG A . n 
C 1 105 THR 105 100 100 THR THR A . n 
C 1 106 ALA 106 101 101 ALA ALA A . n 
C 1 107 PRO 107 102 102 PRO PRO A . n 
C 1 108 ALA 108 103 103 ALA ALA A . n 
C 1 109 ALA 109 104 104 ALA ALA A . n 
C 1 110 PRO 110 105 105 PRO PRO A . n 
C 1 111 THR 111 106 106 THR THR A . n 
C 1 112 TRP 112 107 107 TRP TRP A . n 
C 1 113 ASN 113 108 108 ASN ASN A . n 
C 1 114 PHE 114 109 109 PHE PHE A . n 
C 1 115 THR 115 110 110 THR THR A . n 
C 1 116 SER 116 111 111 SER SER A . n 
C 1 117 VAL 117 112 112 VAL VAL A . n 
C 1 118 GLN 118 113 113 GLN GLN A . n 
C 1 119 VAL 119 114 114 VAL VAL A . n 
C 1 120 ARG 120 115 115 ARG ARG A . n 
C 1 121 GLY 121 116 116 GLY GLY A . n 
C 1 122 GLU 122 117 117 GLU GLU A . n 
C 1 123 LEU 123 118 118 LEU LEU A . n 
C 1 124 ARG 124 119 119 ARG ARG A . n 
C 1 125 LYS 125 120 120 LYS LYS A . n 
C 1 126 VAL 126 121 121 VAL VAL A . n 
C 1 127 GLU 127 122 122 GLU GLU A . n 
C 1 128 SER 128 123 123 SER SER A . n 
C 1 129 ALA 129 124 124 ALA ALA A . n 
C 1 130 ASP 130 125 125 ASP ASP A . n 
C 1 131 ASP 131 126 126 ASP ASP A . n 
C 1 132 THR 132 127 127 THR THR A . n 
C 1 133 LEU 133 128 128 LEU LEU A . n 
C 1 134 ALA 134 129 129 ALA ALA A . n 
C 1 135 THR 135 130 130 THR THR A . n 
C 1 136 VAL 136 131 131 VAL VAL A . n 
C 1 137 ARG 137 132 132 ARG ARG A . n 
C 1 138 ALA 138 133 133 ALA ALA A . n 
C 1 139 THR 139 134 134 THR THR A . n 
C 1 140 VAL 140 135 135 VAL VAL A . n 
C 1 141 ALA 141 136 136 ALA ALA A . n 
C 1 142 ALA 142 137 137 ALA ALA A . n 
C 1 143 LEU 143 138 138 LEU LEU A . n 
C 1 144 GLU 144 139 139 GLU GLU A . n 
C 1 145 SER 145 140 140 SER SER A . n 
C 1 146 ARG 146 141 141 ARG ARG A . n 
C 1 147 PHE 147 142 142 PHE PHE A . n 
C 1 148 GLY 148 143 143 GLY GLY A . n 
C 1 149 ALA 149 144 144 ALA ALA A . n 
C 1 150 GLY 150 145 145 GLY GLY A . n 
C 1 151 TRP 151 146 146 TRP TRP A . n 
C 1 152 ASP 152 147 147 ASP ASP A . n 
C 1 153 MET 153 148 148 MET MET A . n 
C 1 154 THR 154 149 149 THR THR A . n 
C 1 155 GLY 155 150 150 GLY GLY A . n 
C 1 156 SER 156 151 151 SER SER A . n 
C 1 157 LEU 157 152 152 LEU LEU A . n 
C 1 158 ASP 158 153 153 ASP ASP A . n 
C 1 159 TYR 159 154 154 TYR TYR A . n 
C 1 160 PHE 160 155 155 PHE PHE A . n 
C 1 161 ARG 161 156 156 ARG ARG A . n 
C 1 162 ARG 162 157 157 ARG ARG A . n 
C 1 163 ILE 163 158 158 ILE ILE A . n 
C 1 164 LEU 164 159 159 LEU LEU A . n 
C 1 165 PRO 165 160 160 PRO PRO A . n 
C 1 166 GLY 166 161 161 GLY GLY A . n 
C 1 167 VAL 167 162 162 VAL VAL A . n 
C 1 168 GLY 168 163 163 GLY GLY A . n 
C 1 169 ALA 169 164 164 ALA ALA A . n 
C 1 170 PHE 170 165 165 PHE PHE A . n 
C 1 171 ARG 171 166 166 ARG ARG A . n 
C 1 172 LEU 172 167 167 LEU LEU A . n 
C 1 173 ARG 173 168 168 ARG ARG A . n 
C 1 174 VAL 174 169 169 VAL VAL A . n 
C 1 175 ALA 175 170 170 ALA ALA A . n 
C 1 176 GLU 176 171 171 GLU GLU A . n 
C 1 177 ALA 177 172 172 ALA ALA A . n 
C 1 178 ASP 178 173 173 ASP ASP A . n 
C 1 179 GLY 179 174 174 GLY GLY A . n 
C 1 180 MET 180 175 175 MET MET A . n 
C 1 181 PHE 181 176 176 PHE PHE A . n 
C 1 182 LYS 182 177 177 LYS LYS A . n 
C 1 183 LEU 183 178 178 LEU LEU A . n 
C 1 184 SER 184 179 179 SER SER A . n 
C 1 185 GLN 185 180 180 GLN GLN A . n 
C 1 186 GLU 186 181 181 GLU GLU A . n 
C 1 187 GLN 187 182 182 GLN GLN A . n 
C 1 188 GLN 188 183 183 GLN GLN A . n 
C 1 189 PRO 189 184 184 PRO PRO A . n 
C 1 190 ALA 190 185 185 ALA ALA A . n 
C 1 191 ILE 191 186 186 ILE ILE A . n 
C 1 192 ARG 192 187 187 ARG ARG A . n 
C 1 193 ARG 193 188 188 ARG ARG A . n 
C 1 194 ARG 194 189 189 ARG ARG A . n 
C 1 195 VAL 195 190 190 VAL VAL A . n 
C 1 196 ARG 196 191 191 ARG ARG A . n 
C 1 197 HIS 197 192 192 HIS HIS A . n 
C 1 198 SER 198 193 193 SER SER A . n 
C 1 199 PHE 199 194 194 PHE PHE A . n 
C 1 200 GLY 200 195 195 GLY GLY A . n 
C 1 201 GLY 201 196 196 GLY GLY A . n 
C 1 202 ALA 202 197 197 ALA ALA A . n 
C 1 203 GLU 203 198 198 GLU GLU A . n 
C 1 204 ALA 204 199 199 ALA ALA A . n 
C 1 205 THR 205 200 200 THR THR A . n 
C 1 206 ARG 206 201 201 ARG ARG A . n 
C 1 207 ALA 207 202 202 ALA ALA A . n 
C 1 208 VAL 208 203 203 VAL VAL A . n 
C 1 209 ALA 209 204 204 ALA ALA A . n 
C 1 210 GLY 210 205 205 GLY GLY A . n 
C 1 211 LEU 211 206 206 LEU LEU A . n 
C 1 212 MET 212 207 207 MET MET A . n 
C 1 213 ASP 213 208 208 ASP ASP A . n 
C 1 214 ARG 214 209 209 ARG ARG A . n 
C 1 215 LEU 215 210 210 LEU LEU A . n 
C 1 216 PRO 216 211 211 PRO PRO A . n 
C 1 217 THR 217 212 ?   ?   ?   A . n 
C 1 218 GLU 218 213 ?   ?   ?   A . n 
D 1 1   ALA 1   -4  ?   ?   ?   C . n 
D 1 2   GLY 2   -3  ?   ?   ?   C . n 
D 1 3   ALA 3   -2  ?   ?   ?   C . n 
D 1 4   GLY 4   -1  ?   ?   ?   C . n 
D 1 5   ALA 5   0   0   ALA ALA C . n 
D 1 6   MET 6   1   1   MET MET C . n 
D 1 7   PHE 7   2   2   PHE PHE C . n 
D 1 8   VAL 8   3   3   VAL VAL C . n 
D 1 9   PRO 9   4   4   PRO PRO C . n 
D 1 10  GLY 10  5   5   GLY GLY C . n 
D 1 11  PRO 11  6   6   PRO PRO C . n 
D 1 12  TYR 12  7   7   TYR TYR C . n 
D 1 13  HIS 13  8   8   HIS HIS C . n 
D 1 14  ALA 14  9   9   ALA ALA C . n 
D 1 15  PRO 15  10  10  PRO PRO C . n 
D 1 16  GLU 16  11  11  GLU GLU C . n 
D 1 17  ASP 17  12  12  ASP ASP C . n 
D 1 18  ARG 18  13  13  ARG ARG C . n 
D 1 19  TRP 19  14  14  TRP TRP C . n 
D 1 20  LEU 20  15  15  LEU LEU C . n 
D 1 21  VAL 21  16  16  VAL VAL C . n 
D 1 22  ASP 22  17  17  ASP ASP C . n 
D 1 23  LEU 23  18  18  LEU LEU C . n 
D 1 24  VAL 24  19  19  VAL VAL C . n 
D 1 25  ARG 25  20  20  ARG ARG C . n 
D 1 26  GLY 26  21  21  GLY GLY C . n 
D 1 27  HIS 27  22  22  HIS HIS C . n 
D 1 28  PRO 28  23  23  PRO PRO C . n 
D 1 29  LEU 29  24  24  LEU LEU C . n 
D 1 30  ALA 30  25  25  ALA ALA C . n 
D 1 31  GLN 31  26  26  GLN GLN C . n 
D 1 32  LEU 32  27  27  LEU LEU C . n 
D 1 33  ALA 33  28  28  ALA ALA C . n 
D 1 34  SER 34  29  29  SER SER C . n 
D 1 35  ASN 35  30  30  ASN ASN C . n 
D 1 36  GLY 36  31  31  GLY GLY C . n 
D 1 37  ALA 37  32  32  ALA ALA C . n 
D 1 38  GLY 38  33  33  GLY GLY C . n 
D 1 39  GLY 39  34  34  GLY GLY C . n 
D 1 40  ALA 40  35  35  ALA ALA C . n 
D 1 41  ALA 41  36  36  ALA ALA C . n 
D 1 42  PRO 42  37  37  PRO PRO C . n 
D 1 43  HIS 43  38  38  HIS HIS C . n 
D 1 44  ILE 44  39  39  ILE ILE C . n 
D 1 45  THR 45  40  40  THR THR C . n 
D 1 46  HIS 46  41  41  HIS HIS C . n 
D 1 47  VAL 47  42  42  VAL VAL C . n 
D 1 48  PRO 48  43  43  PRO PRO C . n 
D 1 49  ILE 49  44  44  ILE ILE C . n 
D 1 50  ILE 50  45  45  ILE ILE C . n 
D 1 51  VAL 51  46  46  VAL VAL C . n 
D 1 52  ASP 52  47  47  ASP ASP C . n 
D 1 53  PRO 53  48  48  PRO PRO C . n 
D 1 54  GLU 54  49  49  GLU GLU C . n 
D 1 55  LEU 55  50  50  LEU LEU C . n 
D 1 56  ASP 56  51  51  ASP ASP C . n 
D 1 57  GLY 57  52  52  GLY GLY C . n 
D 1 58  PRO 58  53  53  PRO PRO C . n 
D 1 59  VAL 59  54  54  VAL VAL C . n 
D 1 60  ASP 60  55  55  ASP ASP C . n 
D 1 61  ARG 61  56  56  ARG ARG C . n 
D 1 62  LEU 62  57  57  LEU LEU C . n 
D 1 63  VAL 63  58  58  VAL VAL C . n 
D 1 64  GLY 64  59  59  GLY GLY C . n 
D 1 65  ILE 65  60  60  ILE ILE C . n 
D 1 66  THR 66  61  61  THR THR C . n 
D 1 67  LEU 67  62  62  LEU LEU C . n 
D 1 68  TRP 68  63  63  TRP TRP C . n 
D 1 69  GLY 69  64  64  GLY GLY C . n 
D 1 70  HIS 70  65  65  HIS HIS C . n 
D 1 71  MET 71  66  66  MET MET C . n 
D 1 72  ASN 72  67  67  ASN ASN C . n 
D 1 73  ARG 73  68  68  ARG ARG C . n 
D 1 74  ALA 74  69  69  ALA ALA C . n 
D 1 75  ASN 75  70  70  ASN ASN C . n 
D 1 76  PRO 76  71  71  PRO PRO C . n 
D 1 77  HIS 77  72  72  HIS HIS C . n 
D 1 78  TRP 78  73  73  TRP TRP C . n 
D 1 79  ALA 79  74  74  ALA ALA C . n 
D 1 80  ALA 80  75  75  ALA ALA C . n 
D 1 81  LEU 81  76  76  LEU LEU C . n 
D 1 82  GLY 82  77  77  GLY GLY C . n 
D 1 83  GLY 83  78  78  GLY GLY C . n 
D 1 84  ALA 84  79  79  ALA ALA C . n 
D 1 85  ALA 85  80  80  ALA ALA C . n 
D 1 86  ASN 86  81  81  ASN ASN C . n 
D 1 87  VAL 87  82  82  VAL VAL C . n 
D 1 88  VAL 88  83  83  VAL VAL C . n 
D 1 89  ALA 89  84  84  ALA ALA C . n 
D 1 90  THR 90  85  85  THR THR C . n 
D 1 91  PHE 91  86  86  PHE PHE C . n 
D 1 92  ALA 92  87  87  ALA ALA C . n 
D 1 93  GLY 93  88  88  GLY GLY C . n 
D 1 94  PRO 94  89  89  PRO PRO C . n 
D 1 95  ASN 95  90  90  ASN ASN C . n 
D 1 96  ALA 96  91  91  ALA ALA C . n 
D 1 97  TYR 97  92  92  TYR TYR C . n 
D 1 98  VAL 98  93  93  VAL VAL C . n 
D 1 99  SER 99  94  94  SER SER C . n 
D 1 100 PRO 100 95  95  PRO PRO C . n 
D 1 101 ALA 101 96  96  ALA ALA C . n 
D 1 102 VAL 102 97  97  VAL VAL C . n 
D 1 103 TYR 103 98  98  TYR TYR C . n 
D 1 104 ARG 104 99  99  ARG ARG C . n 
D 1 105 THR 105 100 100 THR THR C . n 
D 1 106 ALA 106 101 101 ALA ALA C . n 
D 1 107 PRO 107 102 102 PRO PRO C . n 
D 1 108 ALA 108 103 103 ALA ALA C . n 
D 1 109 ALA 109 104 104 ALA ALA C . n 
D 1 110 PRO 110 105 105 PRO PRO C . n 
D 1 111 THR 111 106 106 THR THR C . n 
D 1 112 TRP 112 107 107 TRP TRP C . n 
D 1 113 ASN 113 108 108 ASN ASN C . n 
D 1 114 PHE 114 109 109 PHE PHE C . n 
D 1 115 THR 115 110 110 THR THR C . n 
D 1 116 SER 116 111 111 SER SER C . n 
D 1 117 VAL 117 112 112 VAL VAL C . n 
D 1 118 GLN 118 113 113 GLN GLN C . n 
D 1 119 VAL 119 114 114 VAL VAL C . n 
D 1 120 ARG 120 115 115 ARG ARG C . n 
D 1 121 GLY 121 116 116 GLY GLY C . n 
D 1 122 GLU 122 117 117 GLU GLU C . n 
D 1 123 LEU 123 118 118 LEU LEU C . n 
D 1 124 ARG 124 119 119 ARG ARG C . n 
D 1 125 LYS 125 120 120 LYS LYS C . n 
D 1 126 VAL 126 121 121 VAL VAL C . n 
D 1 127 GLU 127 122 122 GLU GLU C . n 
D 1 128 SER 128 123 123 SER SER C . n 
D 1 129 ALA 129 124 124 ALA ALA C . n 
D 1 130 ASP 130 125 125 ASP ASP C . n 
D 1 131 ASP 131 126 126 ASP ASP C . n 
D 1 132 THR 132 127 127 THR THR C . n 
D 1 133 LEU 133 128 128 LEU LEU C . n 
D 1 134 ALA 134 129 129 ALA ALA C . n 
D 1 135 THR 135 130 130 THR THR C . n 
D 1 136 VAL 136 131 131 VAL VAL C . n 
D 1 137 ARG 137 132 132 ARG ARG C . n 
D 1 138 ALA 138 133 133 ALA ALA C . n 
D 1 139 THR 139 134 134 THR THR C . n 
D 1 140 VAL 140 135 135 VAL VAL C . n 
D 1 141 ALA 141 136 136 ALA ALA C . n 
D 1 142 ALA 142 137 137 ALA ALA C . n 
D 1 143 LEU 143 138 138 LEU LEU C . n 
D 1 144 GLU 144 139 139 GLU GLU C . n 
D 1 145 SER 145 140 140 SER SER C . n 
D 1 146 ARG 146 141 141 ARG ARG C . n 
D 1 147 PHE 147 142 142 PHE PHE C . n 
D 1 148 GLY 148 143 143 GLY GLY C . n 
D 1 149 ALA 149 144 144 ALA ALA C . n 
D 1 150 GLY 150 145 145 GLY GLY C . n 
D 1 151 TRP 151 146 146 TRP TRP C . n 
D 1 152 ASP 152 147 147 ASP ASP C . n 
D 1 153 MET 153 148 148 MET MET C . n 
D 1 154 THR 154 149 149 THR THR C . n 
D 1 155 GLY 155 150 150 GLY GLY C . n 
D 1 156 SER 156 151 151 SER SER C . n 
D 1 157 LEU 157 152 152 LEU LEU C . n 
D 1 158 ASP 158 153 153 ASP ASP C . n 
D 1 159 TYR 159 154 154 TYR TYR C . n 
D 1 160 PHE 160 155 155 PHE PHE C . n 
D 1 161 ARG 161 156 156 ARG ARG C . n 
D 1 162 ARG 162 157 157 ARG ARG C . n 
D 1 163 ILE 163 158 158 ILE ILE C . n 
D 1 164 LEU 164 159 159 LEU LEU C . n 
D 1 165 PRO 165 160 160 PRO PRO C . n 
D 1 166 GLY 166 161 161 GLY GLY C . n 
D 1 167 VAL 167 162 162 VAL VAL C . n 
D 1 168 GLY 168 163 163 GLY GLY C . n 
D 1 169 ALA 169 164 164 ALA ALA C . n 
D 1 170 PHE 170 165 165 PHE PHE C . n 
D 1 171 ARG 171 166 166 ARG ARG C . n 
D 1 172 LEU 172 167 167 LEU LEU C . n 
D 1 173 ARG 173 168 168 ARG ARG C . n 
D 1 174 VAL 174 169 169 VAL VAL C . n 
D 1 175 ALA 175 170 170 ALA ALA C . n 
D 1 176 GLU 176 171 171 GLU GLU C . n 
D 1 177 ALA 177 172 172 ALA ALA C . n 
D 1 178 ASP 178 173 173 ASP ASP C . n 
D 1 179 GLY 179 174 174 GLY GLY C . n 
D 1 180 MET 180 175 175 MET MET C . n 
D 1 181 PHE 181 176 176 PHE PHE C . n 
D 1 182 LYS 182 177 177 LYS LYS C . n 
D 1 183 LEU 183 178 178 LEU LEU C . n 
D 1 184 SER 184 179 179 SER SER C . n 
D 1 185 GLN 185 180 180 GLN GLN C . n 
D 1 186 GLU 186 181 181 GLU GLU C . n 
D 1 187 GLN 187 182 182 GLN GLN C . n 
D 1 188 GLN 188 183 183 GLN GLN C . n 
D 1 189 PRO 189 184 184 PRO PRO C . n 
D 1 190 ALA 190 185 185 ALA ALA C . n 
D 1 191 ILE 191 186 186 ILE ILE C . n 
D 1 192 ARG 192 187 187 ARG ARG C . n 
D 1 193 ARG 193 188 188 ARG ARG C . n 
D 1 194 ARG 194 189 189 ARG ARG C . n 
D 1 195 VAL 195 190 190 VAL VAL C . n 
D 1 196 ARG 196 191 191 ARG ARG C . n 
D 1 197 HIS 197 192 192 HIS HIS C . n 
D 1 198 SER 198 193 193 SER SER C . n 
D 1 199 PHE 199 194 194 PHE PHE C . n 
D 1 200 GLY 200 195 195 GLY GLY C . n 
D 1 201 GLY 201 196 196 GLY GLY C . n 
D 1 202 ALA 202 197 197 ALA ALA C . n 
D 1 203 GLU 203 198 198 GLU GLU C . n 
D 1 204 ALA 204 199 199 ALA ALA C . n 
D 1 205 THR 205 200 200 THR THR C . n 
D 1 206 ARG 206 201 201 ARG ARG C . n 
D 1 207 ALA 207 202 202 ALA ALA C . n 
D 1 208 VAL 208 203 203 VAL VAL C . n 
D 1 209 ALA 209 204 204 ALA ALA C . n 
D 1 210 GLY 210 205 205 GLY GLY C . n 
D 1 211 LEU 211 206 206 LEU LEU C . n 
D 1 212 MET 212 207 207 MET MET C . n 
D 1 213 ASP 213 208 208 ASP ASP C . n 
D 1 214 ARG 214 209 209 ARG ARG C . n 
D 1 215 LEU 215 210 210 LEU LEU C . n 
D 1 216 PRO 216 211 211 PRO PRO C . n 
D 1 217 THR 217 212 ?   ?   ?   C . n 
D 1 218 GLU 218 213 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HEM 1   301 301  HEM HEM B . 
F 2 HEM 1   301 301  HEM HEM D . 
G 2 HEM 1   301 301  HEM HEM A . 
H 2 HEM 1   301 301  HEM HEM C . 
I 3 HOH 1   401 937  HOH HOH B . 
I 3 HOH 2   402 867  HOH HOH B . 
I 3 HOH 3   403 294  HOH HOH B . 
I 3 HOH 4   404 912  HOH HOH B . 
I 3 HOH 5   405 479  HOH HOH B . 
I 3 HOH 6   406 1006 HOH HOH B . 
I 3 HOH 7   407 922  HOH HOH B . 
I 3 HOH 8   408 534  HOH HOH B . 
I 3 HOH 9   409 675  HOH HOH B . 
I 3 HOH 10  410 667  HOH HOH B . 
I 3 HOH 11  411 865  HOH HOH B . 
I 3 HOH 12  412 649  HOH HOH B . 
I 3 HOH 13  413 685  HOH HOH B . 
I 3 HOH 14  414 295  HOH HOH B . 
I 3 HOH 15  415 445  HOH HOH B . 
I 3 HOH 16  416 331  HOH HOH B . 
I 3 HOH 17  417 436  HOH HOH B . 
I 3 HOH 18  418 707  HOH HOH B . 
I 3 HOH 19  419 192  HOH HOH B . 
I 3 HOH 20  420 125  HOH HOH B . 
I 3 HOH 21  421 563  HOH HOH B . 
I 3 HOH 22  422 659  HOH HOH B . 
I 3 HOH 23  423 71   HOH HOH B . 
I 3 HOH 24  424 169  HOH HOH B . 
I 3 HOH 25  425 443  HOH HOH B . 
I 3 HOH 26  426 868  HOH HOH B . 
I 3 HOH 27  427 637  HOH HOH B . 
I 3 HOH 28  428 89   HOH HOH B . 
I 3 HOH 29  429 546  HOH HOH B . 
I 3 HOH 30  430 352  HOH HOH B . 
I 3 HOH 31  431 17   HOH HOH B . 
I 3 HOH 32  432 288  HOH HOH B . 
I 3 HOH 33  433 689  HOH HOH B . 
I 3 HOH 34  434 122  HOH HOH B . 
I 3 HOH 35  435 917  HOH HOH B . 
I 3 HOH 36  436 171  HOH HOH B . 
I 3 HOH 37  437 383  HOH HOH B . 
I 3 HOH 38  438 679  HOH HOH B . 
I 3 HOH 39  439 431  HOH HOH B . 
I 3 HOH 40  440 119  HOH HOH B . 
I 3 HOH 41  441 230  HOH HOH B . 
I 3 HOH 42  442 433  HOH HOH B . 
I 3 HOH 43  443 301  HOH HOH B . 
I 3 HOH 44  444 862  HOH HOH B . 
I 3 HOH 45  445 639  HOH HOH B . 
I 3 HOH 46  446 105  HOH HOH B . 
I 3 HOH 47  447 683  HOH HOH B . 
I 3 HOH 48  448 460  HOH HOH B . 
I 3 HOH 49  449 796  HOH HOH B . 
I 3 HOH 50  450 258  HOH HOH B . 
I 3 HOH 51  451 286  HOH HOH B . 
I 3 HOH 52  452 486  HOH HOH B . 
I 3 HOH 53  453 54   HOH HOH B . 
I 3 HOH 54  454 425  HOH HOH B . 
I 3 HOH 55  455 315  HOH HOH B . 
I 3 HOH 56  456 251  HOH HOH B . 
I 3 HOH 57  457 61   HOH HOH B . 
I 3 HOH 58  458 523  HOH HOH B . 
I 3 HOH 59  459 85   HOH HOH B . 
I 3 HOH 60  460 619  HOH HOH B . 
I 3 HOH 61  461 229  HOH HOH B . 
I 3 HOH 62  462 126  HOH HOH B . 
I 3 HOH 63  463 371  HOH HOH B . 
I 3 HOH 64  464 10   HOH HOH B . 
I 3 HOH 65  465 346  HOH HOH B . 
I 3 HOH 66  466 668  HOH HOH B . 
I 3 HOH 67  467 564  HOH HOH B . 
I 3 HOH 68  468 141  HOH HOH B . 
I 3 HOH 69  469 38   HOH HOH B . 
I 3 HOH 70  470 521  HOH HOH B . 
I 3 HOH 71  471 48   HOH HOH B . 
I 3 HOH 72  472 52   HOH HOH B . 
I 3 HOH 73  473 498  HOH HOH B . 
I 3 HOH 74  474 173  HOH HOH B . 
I 3 HOH 75  475 566  HOH HOH B . 
I 3 HOH 76  476 421  HOH HOH B . 
I 3 HOH 77  477 312  HOH HOH B . 
I 3 HOH 78  478 273  HOH HOH B . 
I 3 HOH 79  479 389  HOH HOH B . 
I 3 HOH 80  480 275  HOH HOH B . 
I 3 HOH 81  481 113  HOH HOH B . 
I 3 HOH 82  482 493  HOH HOH B . 
I 3 HOH 83  483 341  HOH HOH B . 
I 3 HOH 84  484 481  HOH HOH B . 
I 3 HOH 85  485 202  HOH HOH B . 
I 3 HOH 86  486 387  HOH HOH B . 
I 3 HOH 87  487 188  HOH HOH B . 
I 3 HOH 88  488 115  HOH HOH B . 
I 3 HOH 89  489 130  HOH HOH B . 
I 3 HOH 90  490 239  HOH HOH B . 
I 3 HOH 91  491 363  HOH HOH B . 
I 3 HOH 92  492 354  HOH HOH B . 
I 3 HOH 93  493 463  HOH HOH B . 
I 3 HOH 94  494 691  HOH HOH B . 
I 3 HOH 95  495 128  HOH HOH B . 
I 3 HOH 96  496 164  HOH HOH B . 
I 3 HOH 97  497 300  HOH HOH B . 
I 3 HOH 98  498 910  HOH HOH B . 
I 3 HOH 99  499 712  HOH HOH B . 
I 3 HOH 100 500 309  HOH HOH B . 
I 3 HOH 101 501 289  HOH HOH B . 
I 3 HOH 102 502 5    HOH HOH B . 
I 3 HOH 103 503 526  HOH HOH B . 
I 3 HOH 104 504 110  HOH HOH B . 
I 3 HOH 105 505 193  HOH HOH B . 
I 3 HOH 106 506 723  HOH HOH B . 
I 3 HOH 107 507 579  HOH HOH B . 
I 3 HOH 108 508 98   HOH HOH B . 
I 3 HOH 109 509 423  HOH HOH B . 
I 3 HOH 110 510 284  HOH HOH B . 
I 3 HOH 111 511 690  HOH HOH B . 
I 3 HOH 112 512 973  HOH HOH B . 
I 3 HOH 113 513 474  HOH HOH B . 
I 3 HOH 114 514 199  HOH HOH B . 
I 3 HOH 115 515 198  HOH HOH B . 
I 3 HOH 116 516 70   HOH HOH B . 
I 3 HOH 117 517 447  HOH HOH B . 
I 3 HOH 118 518 653  HOH HOH B . 
I 3 HOH 119 519 231  HOH HOH B . 
I 3 HOH 120 520 434  HOH HOH B . 
I 3 HOH 121 521 298  HOH HOH B . 
I 3 HOH 122 522 506  HOH HOH B . 
I 3 HOH 123 523 529  HOH HOH B . 
I 3 HOH 124 524 505  HOH HOH B . 
I 3 HOH 125 525 104  HOH HOH B . 
I 3 HOH 126 526 355  HOH HOH B . 
I 3 HOH 127 527 326  HOH HOH B . 
I 3 HOH 128 528 3    HOH HOH B . 
I 3 HOH 129 529 73   HOH HOH B . 
I 3 HOH 130 530 140  HOH HOH B . 
I 3 HOH 131 531 518  HOH HOH B . 
I 3 HOH 132 532 631  HOH HOH B . 
I 3 HOH 133 533 684  HOH HOH B . 
I 3 HOH 134 534 187  HOH HOH B . 
I 3 HOH 135 535 109  HOH HOH B . 
I 3 HOH 136 536 240  HOH HOH B . 
I 3 HOH 137 537 397  HOH HOH B . 
I 3 HOH 138 538 242  HOH HOH B . 
I 3 HOH 139 539 235  HOH HOH B . 
I 3 HOH 140 540 317  HOH HOH B . 
I 3 HOH 141 541 515  HOH HOH B . 
I 3 HOH 142 542 236  HOH HOH B . 
I 3 HOH 143 543 243  HOH HOH B . 
I 3 HOH 144 544 4    HOH HOH B . 
I 3 HOH 145 545 159  HOH HOH B . 
I 3 HOH 146 546 291  HOH HOH B . 
I 3 HOH 147 547 626  HOH HOH B . 
I 3 HOH 148 548 255  HOH HOH B . 
I 3 HOH 149 549 147  HOH HOH B . 
I 3 HOH 150 550 527  HOH HOH B . 
I 3 HOH 151 551 293  HOH HOH B . 
I 3 HOH 152 552 582  HOH HOH B . 
I 3 HOH 153 553 623  HOH HOH B . 
I 3 HOH 154 554 303  HOH HOH B . 
I 3 HOH 155 555 72   HOH HOH B . 
I 3 HOH 156 556 368  HOH HOH B . 
I 3 HOH 157 557 33   HOH HOH B . 
I 3 HOH 158 558 81   HOH HOH B . 
I 3 HOH 159 559 551  HOH HOH B . 
I 3 HOH 160 560 607  HOH HOH B . 
I 3 HOH 161 561 163  HOH HOH B . 
I 3 HOH 162 562 1000 HOH HOH B . 
I 3 HOH 163 563 150  HOH HOH B . 
I 3 HOH 164 564 580  HOH HOH B . 
I 3 HOH 165 565 67   HOH HOH B . 
I 3 HOH 166 566 930  HOH HOH B . 
I 3 HOH 167 567 201  HOH HOH B . 
I 3 HOH 168 568 145  HOH HOH B . 
I 3 HOH 169 569 600  HOH HOH B . 
I 3 HOH 170 570 186  HOH HOH B . 
I 3 HOH 171 571 903  HOH HOH B . 
I 3 HOH 172 572 325  HOH HOH B . 
I 3 HOH 173 573 555  HOH HOH B . 
I 3 HOH 174 574 550  HOH HOH B . 
I 3 HOH 175 575 259  HOH HOH B . 
I 3 HOH 176 576 565  HOH HOH B . 
I 3 HOH 177 577 507  HOH HOH B . 
I 3 HOH 178 578 916  HOH HOH B . 
I 3 HOH 179 579 674  HOH HOH B . 
I 3 HOH 180 580 588  HOH HOH B . 
I 3 HOH 181 581 950  HOH HOH B . 
I 3 HOH 182 582 500  HOH HOH B . 
I 3 HOH 183 583 606  HOH HOH B . 
I 3 HOH 184 584 343  HOH HOH B . 
I 3 HOH 185 585 913  HOH HOH B . 
I 3 HOH 186 586 629  HOH HOH B . 
I 3 HOH 187 587 416  HOH HOH B . 
I 3 HOH 188 588 802  HOH HOH B . 
I 3 HOH 189 589 915  HOH HOH B . 
I 3 HOH 190 590 932  HOH HOH B . 
I 3 HOH 191 591 769  HOH HOH B . 
I 3 HOH 192 592 596  HOH HOH B . 
I 3 HOH 193 593 694  HOH HOH B . 
I 3 HOH 194 594 924  HOH HOH B . 
I 3 HOH 195 595 911  HOH HOH B . 
I 3 HOH 196 596 571  HOH HOH B . 
I 3 HOH 197 597 970  HOH HOH B . 
I 3 HOH 198 598 753  HOH HOH B . 
I 3 HOH 199 599 816  HOH HOH B . 
I 3 HOH 200 600 265  HOH HOH B . 
I 3 HOH 201 601 528  HOH HOH B . 
I 3 HOH 202 602 779  HOH HOH B . 
I 3 HOH 203 603 914  HOH HOH B . 
I 3 HOH 204 604 512  HOH HOH B . 
I 3 HOH 205 605 780  HOH HOH B . 
I 3 HOH 206 606 191  HOH HOH B . 
I 3 HOH 207 607 448  HOH HOH B . 
I 3 HOH 208 608 645  HOH HOH B . 
I 3 HOH 209 609 791  HOH HOH B . 
I 3 HOH 210 610 672  HOH HOH B . 
I 3 HOH 211 611 863  HOH HOH B . 
I 3 HOH 212 612 923  HOH HOH B . 
I 3 HOH 213 613 919  HOH HOH B . 
I 3 HOH 214 614 611  HOH HOH B . 
I 3 HOH 215 615 594  HOH HOH B . 
I 3 HOH 216 616 161  HOH HOH B . 
I 3 HOH 217 617 717  HOH HOH B . 
I 3 HOH 218 618 347  HOH HOH B . 
I 3 HOH 219 619 754  HOH HOH B . 
I 3 HOH 220 620 643  HOH HOH B . 
I 3 HOH 221 621 605  HOH HOH B . 
I 3 HOH 222 622 972  HOH HOH B . 
I 3 HOH 223 623 971  HOH HOH B . 
I 3 HOH 224 624 790  HOH HOH B . 
I 3 HOH 225 625 751  HOH HOH B . 
I 3 HOH 226 626 511  HOH HOH B . 
I 3 HOH 227 627 909  HOH HOH B . 
I 3 HOH 228 628 524  HOH HOH B . 
I 3 HOH 229 629 570  HOH HOH B . 
I 3 HOH 230 630 736  HOH HOH B . 
I 3 HOH 231 631 934  HOH HOH B . 
I 3 HOH 232 632 848  HOH HOH B . 
I 3 HOH 233 633 718  HOH HOH B . 
I 3 HOH 234 634 200  HOH HOH B . 
I 3 HOH 235 635 823  HOH HOH B . 
I 3 HOH 236 636 151  HOH HOH B . 
I 3 HOH 237 637 549  HOH HOH B . 
I 3 HOH 238 638 996  HOH HOH B . 
I 3 HOH 239 639 477  HOH HOH B . 
I 3 HOH 240 640 737  HOH HOH B . 
I 3 HOH 241 641 357  HOH HOH B . 
I 3 HOH 242 642 488  HOH HOH B . 
I 3 HOH 243 643 502  HOH HOH B . 
I 3 HOH 244 644 146  HOH HOH B . 
I 3 HOH 245 645 992  HOH HOH B . 
I 3 HOH 246 646 634  HOH HOH B . 
I 3 HOH 247 647 995  HOH HOH B . 
I 3 HOH 248 648 949  HOH HOH B . 
I 3 HOH 249 649 801  HOH HOH B . 
I 3 HOH 250 650 450  HOH HOH B . 
I 3 HOH 251 651 931  HOH HOH B . 
I 3 HOH 252 652 847  HOH HOH B . 
I 3 HOH 253 653 943  HOH HOH B . 
J 3 HOH 1   401 212  HOH HOH D . 
J 3 HOH 2   402 504  HOH HOH D . 
J 3 HOH 3   403 826  HOH HOH D . 
J 3 HOH 4   404 269  HOH HOH D . 
J 3 HOH 5   405 713  HOH HOH D . 
J 3 HOH 6   406 137  HOH HOH D . 
J 3 HOH 7   407 185  HOH HOH D . 
J 3 HOH 8   408 548  HOH HOH D . 
J 3 HOH 9   409 375  HOH HOH D . 
J 3 HOH 10  410 947  HOH HOH D . 
J 3 HOH 11  411 1004 HOH HOH D . 
J 3 HOH 12  412 540  HOH HOH D . 
J 3 HOH 13  413 562  HOH HOH D . 
J 3 HOH 14  414 247  HOH HOH D . 
J 3 HOH 15  415 190  HOH HOH D . 
J 3 HOH 16  416 999  HOH HOH D . 
J 3 HOH 17  417 327  HOH HOH D . 
J 3 HOH 18  418 990  HOH HOH D . 
J 3 HOH 19  419 74   HOH HOH D . 
J 3 HOH 20  420 642  HOH HOH D . 
J 3 HOH 21  421 854  HOH HOH D . 
J 3 HOH 22  422 8    HOH HOH D . 
J 3 HOH 23  423 285  HOH HOH D . 
J 3 HOH 24  424 822  HOH HOH D . 
J 3 HOH 25  425 59   HOH HOH D . 
J 3 HOH 26  426 953  HOH HOH D . 
J 3 HOH 27  427 799  HOH HOH D . 
J 3 HOH 28  428 257  HOH HOH D . 
J 3 HOH 29  429 381  HOH HOH D . 
J 3 HOH 30  430 388  HOH HOH D . 
J 3 HOH 31  431 552  HOH HOH D . 
J 3 HOH 32  432 333  HOH HOH D . 
J 3 HOH 33  433 688  HOH HOH D . 
J 3 HOH 34  434 271  HOH HOH D . 
J 3 HOH 35  435 651  HOH HOH D . 
J 3 HOH 36  436 778  HOH HOH D . 
J 3 HOH 37  437 482  HOH HOH D . 
J 3 HOH 38  438 394  HOH HOH D . 
J 3 HOH 39  439 57   HOH HOH D . 
J 3 HOH 40  440 370  HOH HOH D . 
J 3 HOH 41  441 196  HOH HOH D . 
J 3 HOH 42  442 497  HOH HOH D . 
J 3 HOH 43  443 41   HOH HOH D . 
J 3 HOH 44  444 127  HOH HOH D . 
J 3 HOH 45  445 553  HOH HOH D . 
J 3 HOH 46  446 96   HOH HOH D . 
J 3 HOH 47  447 338  HOH HOH D . 
J 3 HOH 48  448 647  HOH HOH D . 
J 3 HOH 49  449 824  HOH HOH D . 
J 3 HOH 50  450 46   HOH HOH D . 
J 3 HOH 51  451 542  HOH HOH D . 
J 3 HOH 52  452 279  HOH HOH D . 
J 3 HOH 53  453 962  HOH HOH D . 
J 3 HOH 54  454 237  HOH HOH D . 
J 3 HOH 55  455 177  HOH HOH D . 
J 3 HOH 56  456 165  HOH HOH D . 
J 3 HOH 57  457 412  HOH HOH D . 
J 3 HOH 58  458 249  HOH HOH D . 
J 3 HOH 59  459 62   HOH HOH D . 
J 3 HOH 60  460 440  HOH HOH D . 
J 3 HOH 61  461 208  HOH HOH D . 
J 3 HOH 62  462 283  HOH HOH D . 
J 3 HOH 63  463 53   HOH HOH D . 
J 3 HOH 64  464 120  HOH HOH D . 
J 3 HOH 65  465 459  HOH HOH D . 
J 3 HOH 66  466 467  HOH HOH D . 
J 3 HOH 67  467 603  HOH HOH D . 
J 3 HOH 68  468 102  HOH HOH D . 
J 3 HOH 69  469 121  HOH HOH D . 
J 3 HOH 70  470 217  HOH HOH D . 
J 3 HOH 71  471 252  HOH HOH D . 
J 3 HOH 72  472 42   HOH HOH D . 
J 3 HOH 73  473 22   HOH HOH D . 
J 3 HOH 74  474 444  HOH HOH D . 
J 3 HOH 75  475 666  HOH HOH D . 
J 3 HOH 76  476 90   HOH HOH D . 
J 3 HOH 77  477 152  HOH HOH D . 
J 3 HOH 78  478 154  HOH HOH D . 
J 3 HOH 79  479 420  HOH HOH D . 
J 3 HOH 80  480 220  HOH HOH D . 
J 3 HOH 81  481 1001 HOH HOH D . 
J 3 HOH 82  482 720  HOH HOH D . 
J 3 HOH 83  483 248  HOH HOH D . 
J 3 HOH 84  484 410  HOH HOH D . 
J 3 HOH 85  485 369  HOH HOH D . 
J 3 HOH 86  486 92   HOH HOH D . 
J 3 HOH 87  487 93   HOH HOH D . 
J 3 HOH 88  488 56   HOH HOH D . 
J 3 HOH 89  489 853  HOH HOH D . 
J 3 HOH 90  490 153  HOH HOH D . 
J 3 HOH 91  491 215  HOH HOH D . 
J 3 HOH 92  492 812  HOH HOH D . 
J 3 HOH 93  493 390  HOH HOH D . 
J 3 HOH 94  494 480  HOH HOH D . 
J 3 HOH 95  495 342  HOH HOH D . 
J 3 HOH 96  496 55   HOH HOH D . 
J 3 HOH 97  497 422  HOH HOH D . 
J 3 HOH 98  498 97   HOH HOH D . 
J 3 HOH 99  499 297  HOH HOH D . 
J 3 HOH 100 500 308  HOH HOH D . 
J 3 HOH 101 501 305  HOH HOH D . 
J 3 HOH 102 502 99   HOH HOH D . 
J 3 HOH 103 503 974  HOH HOH D . 
J 3 HOH 104 504 277  HOH HOH D . 
J 3 HOH 105 505 79   HOH HOH D . 
J 3 HOH 106 506 68   HOH HOH D . 
J 3 HOH 107 507 344  HOH HOH D . 
J 3 HOH 108 508 24   HOH HOH D . 
J 3 HOH 109 509 270  HOH HOH D . 
J 3 HOH 110 510 501  HOH HOH D . 
J 3 HOH 111 511 466  HOH HOH D . 
J 3 HOH 112 512 319  HOH HOH D . 
J 3 HOH 113 513 13   HOH HOH D . 
J 3 HOH 114 514 34   HOH HOH D . 
J 3 HOH 115 515 702  HOH HOH D . 
J 3 HOH 116 516 296  HOH HOH D . 
J 3 HOH 117 517 2    HOH HOH D . 
J 3 HOH 118 518 335  HOH HOH D . 
J 3 HOH 119 519 358  HOH HOH D . 
J 3 HOH 120 520 398  HOH HOH D . 
J 3 HOH 121 521 880  HOH HOH D . 
J 3 HOH 122 522 106  HOH HOH D . 
J 3 HOH 123 523 576  HOH HOH D . 
J 3 HOH 124 524 6    HOH HOH D . 
J 3 HOH 125 525 376  HOH HOH D . 
J 3 HOH 126 526 280  HOH HOH D . 
J 3 HOH 127 527 472  HOH HOH D . 
J 3 HOH 128 528 968  HOH HOH D . 
J 3 HOH 129 529 727  HOH HOH D . 
J 3 HOH 130 530 36   HOH HOH D . 
J 3 HOH 131 531 411  HOH HOH D . 
J 3 HOH 132 532 194  HOH HOH D . 
J 3 HOH 133 533 365  HOH HOH D . 
J 3 HOH 134 534 18   HOH HOH D . 
J 3 HOH 135 535 221  HOH HOH D . 
J 3 HOH 136 536 955  HOH HOH D . 
J 3 HOH 137 537 435  HOH HOH D . 
J 3 HOH 138 538 83   HOH HOH D . 
J 3 HOH 139 539 869  HOH HOH D . 
J 3 HOH 140 540 857  HOH HOH D . 
J 3 HOH 141 541 360  HOH HOH D . 
J 3 HOH 142 542 809  HOH HOH D . 
J 3 HOH 143 543 183  HOH HOH D . 
J 3 HOH 144 544 261  HOH HOH D . 
J 3 HOH 145 545 490  HOH HOH D . 
J 3 HOH 146 546 621  HOH HOH D . 
J 3 HOH 147 547 610  HOH HOH D . 
J 3 HOH 148 548 944  HOH HOH D . 
J 3 HOH 149 549 75   HOH HOH D . 
J 3 HOH 150 550 484  HOH HOH D . 
J 3 HOH 151 551 1002 HOH HOH D . 
J 3 HOH 152 552 427  HOH HOH D . 
J 3 HOH 153 553 569  HOH HOH D . 
J 3 HOH 154 554 538  HOH HOH D . 
J 3 HOH 155 555 856  HOH HOH D . 
J 3 HOH 156 556 692  HOH HOH D . 
J 3 HOH 157 557 50   HOH HOH D . 
J 3 HOH 158 558 800  HOH HOH D . 
J 3 HOH 159 559 403  HOH HOH D . 
J 3 HOH 160 560 671  HOH HOH D . 
J 3 HOH 161 561 409  HOH HOH D . 
J 3 HOH 162 562 149  HOH HOH D . 
J 3 HOH 163 563 86   HOH HOH D . 
J 3 HOH 164 564 814  HOH HOH D . 
J 3 HOH 165 565 470  HOH HOH D . 
J 3 HOH 166 566 320  HOH HOH D . 
J 3 HOH 167 567 476  HOH HOH D . 
J 3 HOH 168 568 864  HOH HOH D . 
J 3 HOH 169 569 952  HOH HOH D . 
J 3 HOH 170 570 987  HOH HOH D . 
J 3 HOH 171 571 998  HOH HOH D . 
J 3 HOH 172 572 328  HOH HOH D . 
J 3 HOH 173 573 452  HOH HOH D . 
J 3 HOH 174 574 228  HOH HOH D . 
J 3 HOH 175 575 132  HOH HOH D . 
J 3 HOH 176 576 709  HOH HOH D . 
J 3 HOH 177 577 496  HOH HOH D . 
J 3 HOH 178 578 1005 HOH HOH D . 
J 3 HOH 179 579 362  HOH HOH D . 
J 3 HOH 180 580 750  HOH HOH D . 
J 3 HOH 181 581 535  HOH HOH D . 
J 3 HOH 182 582 941  HOH HOH D . 
J 3 HOH 183 583 578  HOH HOH D . 
J 3 HOH 184 584 172  HOH HOH D . 
J 3 HOH 185 585 797  HOH HOH D . 
J 3 HOH 186 586 808  HOH HOH D . 
J 3 HOH 187 587 806  HOH HOH D . 
J 3 HOH 188 588 817  HOH HOH D . 
J 3 HOH 189 589 776  HOH HOH D . 
J 3 HOH 190 590 815  HOH HOH D . 
J 3 HOH 191 591 591  HOH HOH D . 
J 3 HOH 192 592 927  HOH HOH D . 
J 3 HOH 193 593 825  HOH HOH D . 
J 3 HOH 194 594 757  HOH HOH D . 
J 3 HOH 195 595 760  HOH HOH D . 
J 3 HOH 196 596 733  HOH HOH D . 
J 3 HOH 197 597 969  HOH HOH D . 
J 3 HOH 198 598 986  HOH HOH D . 
J 3 HOH 199 599 559  HOH HOH D . 
J 3 HOH 200 600 741  HOH HOH D . 
J 3 HOH 201 601 256  HOH HOH D . 
J 3 HOH 202 602 961  HOH HOH D . 
J 3 HOH 203 603 695  HOH HOH D . 
J 3 HOH 204 604 858  HOH HOH D . 
J 3 HOH 205 605 616  HOH HOH D . 
J 3 HOH 206 606 811  HOH HOH D . 
J 3 HOH 207 607 782  HOH HOH D . 
J 3 HOH 208 608 860  HOH HOH D . 
J 3 HOH 209 609 633  HOH HOH D . 
J 3 HOH 210 610 871  HOH HOH D . 
J 3 HOH 211 611 755  HOH HOH D . 
J 3 HOH 212 612 746  HOH HOH D . 
J 3 HOH 213 613 417  HOH HOH D . 
J 3 HOH 214 614 803  HOH HOH D . 
J 3 HOH 215 615 635  HOH HOH D . 
J 3 HOH 216 616 761  HOH HOH D . 
J 3 HOH 217 617 818  HOH HOH D . 
J 3 HOH 218 618 726  HOH HOH D . 
J 3 HOH 219 619 807  HOH HOH D . 
J 3 HOH 220 620 866  HOH HOH D . 
J 3 HOH 221 621 219  HOH HOH D . 
J 3 HOH 222 622 929  HOH HOH D . 
J 3 HOH 223 623 586  HOH HOH D . 
J 3 HOH 224 624 957  HOH HOH D . 
J 3 HOH 225 625 933  HOH HOH D . 
J 3 HOH 226 626 861  HOH HOH D . 
J 3 HOH 227 627 855  HOH HOH D . 
J 3 HOH 228 628 508  HOH HOH D . 
J 3 HOH 229 629 852  HOH HOH D . 
J 3 HOH 230 630 810  HOH HOH D . 
J 3 HOH 231 631 413  HOH HOH D . 
J 3 HOH 232 632 1003 HOH HOH D . 
J 3 HOH 233 633 732  HOH HOH D . 
J 3 HOH 234 634 581  HOH HOH D . 
J 3 HOH 235 635 991  HOH HOH D . 
J 3 HOH 236 636 719  HOH HOH D . 
J 3 HOH 237 637 729  HOH HOH D . 
J 3 HOH 238 638 509  HOH HOH D . 
J 3 HOH 239 639 386  HOH HOH D . 
J 3 HOH 240 640 226  HOH HOH D . 
J 3 HOH 241 641 765  HOH HOH D . 
J 3 HOH 242 642 351  HOH HOH D . 
J 3 HOH 243 643 792  HOH HOH D . 
J 3 HOH 244 644 859  HOH HOH D . 
J 3 HOH 245 645 658  HOH HOH D . 
J 3 HOH 246 646 449  HOH HOH D . 
J 3 HOH 247 647 663  HOH HOH D . 
J 3 HOH 248 648 758  HOH HOH D . 
J 3 HOH 249 649 323  HOH HOH D . 
J 3 HOH 250 650 516  HOH HOH D . 
J 3 HOH 251 651 798  HOH HOH D . 
J 3 HOH 252 652 819  HOH HOH D . 
J 3 HOH 253 653 900  HOH HOH D . 
J 3 HOH 254 654 942  HOH HOH D . 
J 3 HOH 255 655 821  HOH HOH D . 
J 3 HOH 256 656 514  HOH HOH D . 
J 3 HOH 257 657 609  HOH HOH D . 
J 3 HOH 258 658 960  HOH HOH D . 
J 3 HOH 259 659 648  HOH HOH D . 
J 3 HOH 260 660 805  HOH HOH D . 
J 3 HOH 261 661 742  HOH HOH D . 
J 3 HOH 262 662 954  HOH HOH D . 
J 3 HOH 263 663 993  HOH HOH D . 
J 3 HOH 264 664 777  HOH HOH D . 
J 3 HOH 265 665 764  HOH HOH D . 
J 3 HOH 266 666 783  HOH HOH D . 
J 3 HOH 267 667 787  HOH HOH D . 
J 3 HOH 268 668 785  HOH HOH D . 
J 3 HOH 269 669 813  HOH HOH D . 
J 3 HOH 270 670 994  HOH HOH D . 
J 3 HOH 271 671 901  HOH HOH D . 
J 3 HOH 272 672 956  HOH HOH D . 
J 3 HOH 273 673 899  HOH HOH D . 
J 3 HOH 274 674 820  HOH HOH D . 
J 3 HOH 275 675 804  HOH HOH D . 
J 3 HOH 276 676 902  HOH HOH D . 
K 3 HOH 1   401 881  HOH HOH A . 
K 3 HOH 2   402 1007 HOH HOH A . 
K 3 HOH 3   403 677  HOH HOH A . 
K 3 HOH 4   404 893  HOH HOH A . 
K 3 HOH 5   405 887  HOH HOH A . 
K 3 HOH 6   406 608  HOH HOH A . 
K 3 HOH 7   407 438  HOH HOH A . 
K 3 HOH 8   408 656  HOH HOH A . 
K 3 HOH 9   409 967  HOH HOH A . 
K 3 HOH 10  410 966  HOH HOH A . 
K 3 HOH 11  411 475  HOH HOH A . 
K 3 HOH 12  412 876  HOH HOH A . 
K 3 HOH 13  413 665  HOH HOH A . 
K 3 HOH 14  414 873  HOH HOH A . 
K 3 HOH 15  415 877  HOH HOH A . 
K 3 HOH 16  416 558  HOH HOH A . 
K 3 HOH 17  417 980  HOH HOH A . 
K 3 HOH 18  418 889  HOH HOH A . 
K 3 HOH 19  419 211  HOH HOH A . 
K 3 HOH 20  420 266  HOH HOH A . 
K 3 HOH 21  421 539  HOH HOH A . 
K 3 HOH 22  422 483  HOH HOH A . 
K 3 HOH 23  423 29   HOH HOH A . 
K 3 HOH 24  424 406  HOH HOH A . 
K 3 HOH 25  425 88   HOH HOH A . 
K 3 HOH 26  426 920  HOH HOH A . 
K 3 HOH 27  427 272  HOH HOH A . 
K 3 HOH 28  428 65   HOH HOH A . 
K 3 HOH 29  429 832  HOH HOH A . 
K 3 HOH 30  430 350  HOH HOH A . 
K 3 HOH 31  431 339  HOH HOH A . 
K 3 HOH 32  432 349  HOH HOH A . 
K 3 HOH 33  433 274  HOH HOH A . 
K 3 HOH 34  434 585  HOH HOH A . 
K 3 HOH 35  435 513  HOH HOH A . 
K 3 HOH 36  436 14   HOH HOH A . 
K 3 HOH 37  437 532  HOH HOH A . 
K 3 HOH 38  438 111  HOH HOH A . 
K 3 HOH 39  439 456  HOH HOH A . 
K 3 HOH 40  440 503  HOH HOH A . 
K 3 HOH 41  441 232  HOH HOH A . 
K 3 HOH 42  442 179  HOH HOH A . 
K 3 HOH 43  443 12   HOH HOH A . 
K 3 HOH 44  444 80   HOH HOH A . 
K 3 HOH 45  445 292  HOH HOH A . 
K 3 HOH 46  446 374  HOH HOH A . 
K 3 HOH 47  447 306  HOH HOH A . 
K 3 HOH 48  448 378  HOH HOH A . 
K 3 HOH 49  449 928  HOH HOH A . 
K 3 HOH 50  450 561  HOH HOH A . 
K 3 HOH 51  451 592  HOH HOH A . 
K 3 HOH 52  452 77   HOH HOH A . 
K 3 HOH 53  453 604  HOH HOH A . 
K 3 HOH 54  454 51   HOH HOH A . 
K 3 HOH 55  455 525  HOH HOH A . 
K 3 HOH 56  456 426  HOH HOH A . 
K 3 HOH 57  457 356  HOH HOH A . 
K 3 HOH 58  458 43   HOH HOH A . 
K 3 HOH 59  459 58   HOH HOH A . 
K 3 HOH 60  460 264  HOH HOH A . 
K 3 HOH 61  461 47   HOH HOH A . 
K 3 HOH 62  462 314  HOH HOH A . 
K 3 HOH 63  463 108  HOH HOH A . 
K 3 HOH 64  464 468  HOH HOH A . 
K 3 HOH 65  465 30   HOH HOH A . 
K 3 HOH 66  466 204  HOH HOH A . 
K 3 HOH 67  467 660  HOH HOH A . 
K 3 HOH 68  468 222  HOH HOH A . 
K 3 HOH 69  469 430  HOH HOH A . 
K 3 HOH 70  470 918  HOH HOH A . 
K 3 HOH 71  471 652  HOH HOH A . 
K 3 HOH 72  472 979  HOH HOH A . 
K 3 HOH 73  473 233  HOH HOH A . 
K 3 HOH 74  474 560  HOH HOH A . 
K 3 HOH 75  475 590  HOH HOH A . 
K 3 HOH 76  476 176  HOH HOH A . 
K 3 HOH 77  477 584  HOH HOH A . 
K 3 HOH 78  478 380  HOH HOH A . 
K 3 HOH 79  479 290  HOH HOH A . 
K 3 HOH 80  480 428  HOH HOH A . 
K 3 HOH 81  481 617  HOH HOH A . 
K 3 HOH 82  482 168  HOH HOH A . 
K 3 HOH 83  483 638  HOH HOH A . 
K 3 HOH 84  484 624  HOH HOH A . 
K 3 HOH 85  485 25   HOH HOH A . 
K 3 HOH 86  486 415  HOH HOH A . 
K 3 HOH 87  487 66   HOH HOH A . 
K 3 HOH 88  488 384  HOH HOH A . 
K 3 HOH 89  489 21   HOH HOH A . 
K 3 HOH 90  490 833  HOH HOH A . 
K 3 HOH 91  491 682  HOH HOH A . 
K 3 HOH 92  492 37   HOH HOH A . 
K 3 HOH 93  493 316  HOH HOH A . 
K 3 HOH 94  494 282  HOH HOH A . 
K 3 HOH 95  495 495  HOH HOH A . 
K 3 HOH 96  496 267  HOH HOH A . 
K 3 HOH 97  497 336  HOH HOH A . 
K 3 HOH 98  498 299  HOH HOH A . 
K 3 HOH 99  499 174  HOH HOH A . 
K 3 HOH 100 500 167  HOH HOH A . 
K 3 HOH 101 501 184  HOH HOH A . 
K 3 HOH 102 502 348  HOH HOH A . 
K 3 HOH 103 503 263  HOH HOH A . 
K 3 HOH 104 504 405  HOH HOH A . 
K 3 HOH 105 505 491  HOH HOH A . 
K 3 HOH 106 506 166  HOH HOH A . 
K 3 HOH 107 507 464  HOH HOH A . 
K 3 HOH 108 508 908  HOH HOH A . 
K 3 HOH 109 509 136  HOH HOH A . 
K 3 HOH 110 510 60   HOH HOH A . 
K 3 HOH 111 511 975  HOH HOH A . 
K 3 HOH 112 512 831  HOH HOH A . 
K 3 HOH 113 513 107  HOH HOH A . 
K 3 HOH 114 514 372  HOH HOH A . 
K 3 HOH 115 515 281  HOH HOH A . 
K 3 HOH 116 516 965  HOH HOH A . 
K 3 HOH 117 517 322  HOH HOH A . 
K 3 HOH 118 518 946  HOH HOH A . 
K 3 HOH 119 519 461  HOH HOH A . 
K 3 HOH 120 520 250  HOH HOH A . 
K 3 HOH 121 521 614  HOH HOH A . 
K 3 HOH 122 522 510  HOH HOH A . 
K 3 HOH 123 523 628  HOH HOH A . 
K 3 HOH 124 524 225  HOH HOH A . 
K 3 HOH 125 525 662  HOH HOH A . 
K 3 HOH 126 526 332  HOH HOH A . 
K 3 HOH 127 527 451  HOH HOH A . 
K 3 HOH 128 528 499  HOH HOH A . 
K 3 HOH 129 529 117  HOH HOH A . 
K 3 HOH 130 530 400  HOH HOH A . 
K 3 HOH 131 531 245  HOH HOH A . 
K 3 HOH 132 532 175  HOH HOH A . 
K 3 HOH 133 533 531  HOH HOH A . 
K 3 HOH 134 534 103  HOH HOH A . 
K 3 HOH 135 535 632  HOH HOH A . 
K 3 HOH 136 536 182  HOH HOH A . 
K 3 HOH 137 537 69   HOH HOH A . 
K 3 HOH 138 538 399  HOH HOH A . 
K 3 HOH 139 539 583  HOH HOH A . 
K 3 HOH 140 540 262  HOH HOH A . 
K 3 HOH 141 541 457  HOH HOH A . 
K 3 HOH 142 542 849  HOH HOH A . 
K 3 HOH 143 543 353  HOH HOH A . 
K 3 HOH 144 544 657  HOH HOH A . 
K 3 HOH 145 545 710  HOH HOH A . 
K 3 HOH 146 546 602  HOH HOH A . 
K 3 HOH 147 547 875  HOH HOH A . 
K 3 HOH 148 548 646  HOH HOH A . 
K 3 HOH 149 549 494  HOH HOH A . 
K 3 HOH 150 550 921  HOH HOH A . 
K 3 HOH 151 551 157  HOH HOH A . 
K 3 HOH 152 552 11   HOH HOH A . 
K 3 HOH 153 553 678  HOH HOH A . 
K 3 HOH 154 554 392  HOH HOH A . 
K 3 HOH 155 555 622  HOH HOH A . 
K 3 HOH 156 556 894  HOH HOH A . 
K 3 HOH 157 557 839  HOH HOH A . 
K 3 HOH 158 558 195  HOH HOH A . 
K 3 HOH 159 559 676  HOH HOH A . 
K 3 HOH 160 560 35   HOH HOH A . 
K 3 HOH 161 561 123  HOH HOH A . 
K 3 HOH 162 562 26   HOH HOH A . 
K 3 HOH 163 563 100  HOH HOH A . 
K 3 HOH 164 564 554  HOH HOH A . 
K 3 HOH 165 565 19   HOH HOH A . 
K 3 HOH 166 566 556  HOH HOH A . 
K 3 HOH 167 567 408  HOH HOH A . 
K 3 HOH 168 568 711  HOH HOH A . 
K 3 HOH 169 569 432  HOH HOH A . 
K 3 HOH 170 570 740  HOH HOH A . 
K 3 HOH 171 571 878  HOH HOH A . 
K 3 HOH 172 572 701  HOH HOH A . 
K 3 HOH 173 573 907  HOH HOH A . 
K 3 HOH 174 574 874  HOH HOH A . 
K 3 HOH 175 575 766  HOH HOH A . 
K 3 HOH 176 576 982  HOH HOH A . 
K 3 HOH 177 577 771  HOH HOH A . 
K 3 HOH 178 578 627  HOH HOH A . 
K 3 HOH 179 579 725  HOH HOH A . 
K 3 HOH 180 580 730  HOH HOH A . 
K 3 HOH 181 581 735  HOH HOH A . 
K 3 HOH 182 582 568  HOH HOH A . 
K 3 HOH 183 583 981  HOH HOH A . 
K 3 HOH 184 584 644  HOH HOH A . 
K 3 HOH 185 585 522  HOH HOH A . 
K 3 HOH 186 586 487  HOH HOH A . 
K 3 HOH 187 587 536  HOH HOH A . 
K 3 HOH 188 588 595  HOH HOH A . 
K 3 HOH 189 589 302  HOH HOH A . 
K 3 HOH 190 590 978  HOH HOH A . 
K 3 HOH 191 591 728  HOH HOH A . 
K 3 HOH 192 592 744  HOH HOH A . 
K 3 HOH 193 593 888  HOH HOH A . 
K 3 HOH 194 594 640  HOH HOH A . 
K 3 HOH 195 595 948  HOH HOH A . 
K 3 HOH 196 596 841  HOH HOH A . 
K 3 HOH 197 597 545  HOH HOH A . 
K 3 HOH 198 598 997  HOH HOH A . 
K 3 HOH 199 599 879  HOH HOH A . 
K 3 HOH 200 600 925  HOH HOH A . 
K 3 HOH 201 601 533  HOH HOH A . 
K 3 HOH 202 602 722  HOH HOH A . 
K 3 HOH 203 603 882  HOH HOH A . 
K 3 HOH 204 604 985  HOH HOH A . 
K 3 HOH 205 605 772  HOH HOH A . 
K 3 HOH 206 606 593  HOH HOH A . 
K 3 HOH 207 607 906  HOH HOH A . 
K 3 HOH 208 608 478  HOH HOH A . 
K 3 HOH 209 609 620  HOH HOH A . 
K 3 HOH 210 610 625  HOH HOH A . 
K 3 HOH 211 611 418  HOH HOH A . 
K 3 HOH 212 612 485  HOH HOH A . 
K 3 HOH 213 613 721  HOH HOH A . 
K 3 HOH 214 614 547  HOH HOH A . 
K 3 HOH 215 615 615  HOH HOH A . 
K 3 HOH 216 616 84   HOH HOH A . 
K 3 HOH 217 617 897  HOH HOH A . 
K 3 HOH 218 618 598  HOH HOH A . 
K 3 HOH 219 619 845  HOH HOH A . 
K 3 HOH 220 620 752  HOH HOH A . 
K 3 HOH 221 621 655  HOH HOH A . 
K 3 HOH 222 622 465  HOH HOH A . 
K 3 HOH 223 623 572  HOH HOH A . 
K 3 HOH 224 624 573  HOH HOH A . 
K 3 HOH 225 625 846  HOH HOH A . 
K 3 HOH 226 626 891  HOH HOH A . 
K 3 HOH 227 627 307  HOH HOH A . 
K 3 HOH 228 628 462  HOH HOH A . 
K 3 HOH 229 629 393  HOH HOH A . 
K 3 HOH 230 630 989  HOH HOH A . 
K 3 HOH 231 631 789  HOH HOH A . 
K 3 HOH 232 632 441  HOH HOH A . 
K 3 HOH 233 633 905  HOH HOH A . 
K 3 HOH 234 634 840  HOH HOH A . 
K 3 HOH 235 635 976  HOH HOH A . 
K 3 HOH 236 636 886  HOH HOH A . 
K 3 HOH 237 637 898  HOH HOH A . 
K 3 HOH 238 638 214  HOH HOH A . 
K 3 HOH 239 639 759  HOH HOH A . 
K 3 HOH 240 640 745  HOH HOH A . 
K 3 HOH 241 641 958  HOH HOH A . 
K 3 HOH 242 642 395  HOH HOH A . 
K 3 HOH 243 643 851  HOH HOH A . 
K 3 HOH 244 644 850  HOH HOH A . 
K 3 HOH 245 645 795  HOH HOH A . 
K 3 HOH 246 646 773  HOH HOH A . 
K 3 HOH 247 647 786  HOH HOH A . 
K 3 HOH 248 648 715  HOH HOH A . 
K 3 HOH 249 649 784  HOH HOH A . 
K 3 HOH 250 650 959  HOH HOH A . 
K 3 HOH 251 651 896  HOH HOH A . 
K 3 HOH 252 652 774  HOH HOH A . 
K 3 HOH 253 653 781  HOH HOH A . 
K 3 HOH 254 654 890  HOH HOH A . 
K 3 HOH 255 655 988  HOH HOH A . 
K 3 HOH 256 656 770  HOH HOH A . 
K 3 HOH 257 657 977  HOH HOH A . 
K 3 HOH 258 658 775  HOH HOH A . 
K 3 HOH 259 659 768  HOH HOH A . 
K 3 HOH 260 660 788  HOH HOH A . 
L 3 HOH 1   401 706  HOH HOH C . 
L 3 HOH 2   402 837  HOH HOH C . 
L 3 HOH 3   403 883  HOH HOH C . 
L 3 HOH 4   404 268  HOH HOH C . 
L 3 HOH 5   405 630  HOH HOH C . 
L 3 HOH 6   406 938  HOH HOH C . 
L 3 HOH 7   407 32   HOH HOH C . 
L 3 HOH 8   408 574  HOH HOH C . 
L 3 HOH 9   409 587  HOH HOH C . 
L 3 HOH 10  410 827  HOH HOH C . 
L 3 HOH 11  411 612  HOH HOH C . 
L 3 HOH 12  412 673  HOH HOH C . 
L 3 HOH 13  413 78   HOH HOH C . 
L 3 HOH 14  414 234  HOH HOH C . 
L 3 HOH 15  415 253  HOH HOH C . 
L 3 HOH 16  416 696  HOH HOH C . 
L 3 HOH 17  417 379  HOH HOH C . 
L 3 HOH 18  418 209  HOH HOH C . 
L 3 HOH 19  419 244  HOH HOH C . 
L 3 HOH 20  420 517  HOH HOH C . 
L 3 HOH 21  421 241  HOH HOH C . 
L 3 HOH 22  422 144  HOH HOH C . 
L 3 HOH 23  423 334  HOH HOH C . 
L 3 HOH 24  424 419  HOH HOH C . 
L 3 HOH 25  425 210  HOH HOH C . 
L 3 HOH 26  426 687  HOH HOH C . 
L 3 HOH 27  427 20   HOH HOH C . 
L 3 HOH 28  428 404  HOH HOH C . 
L 3 HOH 29  429 9    HOH HOH C . 
L 3 HOH 30  430 142  HOH HOH C . 
L 3 HOH 31  431 44   HOH HOH C . 
L 3 HOH 32  432 155  HOH HOH C . 
L 3 HOH 33  433 148  HOH HOH C . 
L 3 HOH 34  434 124  HOH HOH C . 
L 3 HOH 35  435 31   HOH HOH C . 
L 3 HOH 36  436 276  HOH HOH C . 
L 3 HOH 37  437 28   HOH HOH C . 
L 3 HOH 38  438 158  HOH HOH C . 
L 3 HOH 39  439 206  HOH HOH C . 
L 3 HOH 40  440 82   HOH HOH C . 
L 3 HOH 41  441 49   HOH HOH C . 
L 3 HOH 42  442 698  HOH HOH C . 
L 3 HOH 43  443 313  HOH HOH C . 
L 3 HOH 44  444 318  HOH HOH C . 
L 3 HOH 45  445 453  HOH HOH C . 
L 3 HOH 46  446 345  HOH HOH C . 
L 3 HOH 47  447 95   HOH HOH C . 
L 3 HOH 48  448 439  HOH HOH C . 
L 3 HOH 49  449 131  HOH HOH C . 
L 3 HOH 50  450 708  HOH HOH C . 
L 3 HOH 51  451 197  HOH HOH C . 
L 3 HOH 52  452 654  HOH HOH C . 
L 3 HOH 53  453 207  HOH HOH C . 
L 3 HOH 54  454 329  HOH HOH C . 
L 3 HOH 55  455 134  HOH HOH C . 
L 3 HOH 56  456 76   HOH HOH C . 
L 3 HOH 57  457 686  HOH HOH C . 
L 3 HOH 58  458 697  HOH HOH C . 
L 3 HOH 59  459 473  HOH HOH C . 
L 3 HOH 60  460 681  HOH HOH C . 
L 3 HOH 61  461 116  HOH HOH C . 
L 3 HOH 62  462 87   HOH HOH C . 
L 3 HOH 63  463 377  HOH HOH C . 
L 3 HOH 64  464 138  HOH HOH C . 
L 3 HOH 65  465 402  HOH HOH C . 
L 3 HOH 66  466 337  HOH HOH C . 
L 3 HOH 67  467 189  HOH HOH C . 
L 3 HOH 68  468 359  HOH HOH C . 
L 3 HOH 69  469 872  HOH HOH C . 
L 3 HOH 70  470 330  HOH HOH C . 
L 3 HOH 71  471 227  HOH HOH C . 
L 3 HOH 72  472 205  HOH HOH C . 
L 3 HOH 73  473 112  HOH HOH C . 
L 3 HOH 74  474 223  HOH HOH C . 
L 3 HOH 75  475 838  HOH HOH C . 
L 3 HOH 76  476 557  HOH HOH C . 
L 3 HOH 77  477 935  HOH HOH C . 
L 3 HOH 78  478 218  HOH HOH C . 
L 3 HOH 79  479 705  HOH HOH C . 
L 3 HOH 80  480 45   HOH HOH C . 
L 3 HOH 81  481 442  HOH HOH C . 
L 3 HOH 82  482 7    HOH HOH C . 
L 3 HOH 83  483 407  HOH HOH C . 
L 3 HOH 84  484 216  HOH HOH C . 
L 3 HOH 85  485 599  HOH HOH C . 
L 3 HOH 86  486 340  HOH HOH C . 
L 3 HOH 87  487 64   HOH HOH C . 
L 3 HOH 88  488 396  HOH HOH C . 
L 3 HOH 89  489 661  HOH HOH C . 
L 3 HOH 90  490 139  HOH HOH C . 
L 3 HOH 91  491 577  HOH HOH C . 
L 3 HOH 92  492 541  HOH HOH C . 
L 3 HOH 93  493 160  HOH HOH C . 
L 3 HOH 94  494 469  HOH HOH C . 
L 3 HOH 95  495 458  HOH HOH C . 
L 3 HOH 96  496 27   HOH HOH C . 
L 3 HOH 97  497 260  HOH HOH C . 
L 3 HOH 98  498 636  HOH HOH C . 
L 3 HOH 99  499 118  HOH HOH C . 
L 3 HOH 100 500 246  HOH HOH C . 
L 3 HOH 101 501 1    HOH HOH C . 
L 3 HOH 102 502 39   HOH HOH C . 
L 3 HOH 103 503 455  HOH HOH C . 
L 3 HOH 104 504 143  HOH HOH C . 
L 3 HOH 105 505 15   HOH HOH C . 
L 3 HOH 106 506 424  HOH HOH C . 
L 3 HOH 107 507 704  HOH HOH C . 
L 3 HOH 108 508 530  HOH HOH C . 
L 3 HOH 109 509 129  HOH HOH C . 
L 3 HOH 110 510 213  HOH HOH C . 
L 3 HOH 111 511 40   HOH HOH C . 
L 3 HOH 112 512 91   HOH HOH C . 
L 3 HOH 113 513 373  HOH HOH C . 
L 3 HOH 114 514 699  HOH HOH C . 
L 3 HOH 115 515 203  HOH HOH C . 
L 3 HOH 116 516 224  HOH HOH C . 
L 3 HOH 117 517 324  HOH HOH C . 
L 3 HOH 118 518 567  HOH HOH C . 
L 3 HOH 119 519 454  HOH HOH C . 
L 3 HOH 120 520 361  HOH HOH C . 
L 3 HOH 121 521 664  HOH HOH C . 
L 3 HOH 122 522 178  HOH HOH C . 
L 3 HOH 123 523 181  HOH HOH C . 
L 3 HOH 124 524 829  HOH HOH C . 
L 3 HOH 125 525 94   HOH HOH C . 
L 3 HOH 126 526 162  HOH HOH C . 
L 3 HOH 127 527 23   HOH HOH C . 
L 3 HOH 128 528 401  HOH HOH C . 
L 3 HOH 129 529 680  HOH HOH C . 
L 3 HOH 130 530 101  HOH HOH C . 
L 3 HOH 131 531 254  HOH HOH C . 
L 3 HOH 132 532 63   HOH HOH C . 
L 3 HOH 133 533 520  HOH HOH C . 
L 3 HOH 134 534 287  HOH HOH C . 
L 3 HOH 135 535 366  HOH HOH C . 
L 3 HOH 136 536 437  HOH HOH C . 
L 3 HOH 137 537 589  HOH HOH C . 
L 3 HOH 138 538 170  HOH HOH C . 
L 3 HOH 139 539 693  HOH HOH C . 
L 3 HOH 140 540 446  HOH HOH C . 
L 3 HOH 141 541 278  HOH HOH C . 
L 3 HOH 142 542 544  HOH HOH C . 
L 3 HOH 143 543 114  HOH HOH C . 
L 3 HOH 144 544 310  HOH HOH C . 
L 3 HOH 145 545 964  HOH HOH C . 
L 3 HOH 146 546 724  HOH HOH C . 
L 3 HOH 147 547 16   HOH HOH C . 
L 3 HOH 148 548 180  HOH HOH C . 
L 3 HOH 149 549 703  HOH HOH C . 
L 3 HOH 150 550 489  HOH HOH C . 
L 3 HOH 151 551 836  HOH HOH C . 
L 3 HOH 152 552 892  HOH HOH C . 
L 3 HOH 153 553 156  HOH HOH C . 
L 3 HOH 154 554 471  HOH HOH C . 
L 3 HOH 155 555 700  HOH HOH C . 
L 3 HOH 156 556 885  HOH HOH C . 
L 3 HOH 157 557 492  HOH HOH C . 
L 3 HOH 158 558 984  HOH HOH C . 
L 3 HOH 159 559 926  HOH HOH C . 
L 3 HOH 160 560 767  HOH HOH C . 
L 3 HOH 161 561 748  HOH HOH C . 
L 3 HOH 162 562 963  HOH HOH C . 
L 3 HOH 163 563 613  HOH HOH C . 
L 3 HOH 164 564 734  HOH HOH C . 
L 3 HOH 165 565 641  HOH HOH C . 
L 3 HOH 166 566 618  HOH HOH C . 
L 3 HOH 167 567 830  HOH HOH C . 
L 3 HOH 168 568 834  HOH HOH C . 
L 3 HOH 169 569 238  HOH HOH C . 
L 3 HOH 170 570 716  HOH HOH C . 
L 3 HOH 171 571 321  HOH HOH C . 
L 3 HOH 172 572 714  HOH HOH C . 
L 3 HOH 173 573 670  HOH HOH C . 
L 3 HOH 174 574 756  HOH HOH C . 
L 3 HOH 175 575 414  HOH HOH C . 
L 3 HOH 176 576 747  HOH HOH C . 
L 3 HOH 177 577 731  HOH HOH C . 
L 3 HOH 178 578 133  HOH HOH C . 
L 3 HOH 179 579 936  HOH HOH C . 
L 3 HOH 180 580 940  HOH HOH C . 
L 3 HOH 181 581 385  HOH HOH C . 
L 3 HOH 182 582 519  HOH HOH C . 
L 3 HOH 183 583 601  HOH HOH C . 
L 3 HOH 184 584 842  HOH HOH C . 
L 3 HOH 185 585 763  HOH HOH C . 
L 3 HOH 186 586 429  HOH HOH C . 
L 3 HOH 187 587 828  HOH HOH C . 
L 3 HOH 188 588 983  HOH HOH C . 
L 3 HOH 189 589 391  HOH HOH C . 
L 3 HOH 190 590 835  HOH HOH C . 
L 3 HOH 191 591 870  HOH HOH C . 
L 3 HOH 192 592 738  HOH HOH C . 
L 3 HOH 193 593 382  HOH HOH C . 
L 3 HOH 194 594 739  HOH HOH C . 
L 3 HOH 195 595 367  HOH HOH C . 
L 3 HOH 196 596 543  HOH HOH C . 
L 3 HOH 197 597 304  HOH HOH C . 
L 3 HOH 198 598 945  HOH HOH C . 
L 3 HOH 199 599 749  HOH HOH C . 
L 3 HOH 200 600 904  HOH HOH C . 
L 3 HOH 201 601 669  HOH HOH C . 
L 3 HOH 202 602 135  HOH HOH C . 
L 3 HOH 203 603 364  HOH HOH C . 
L 3 HOH 204 604 844  HOH HOH C . 
L 3 HOH 205 605 597  HOH HOH C . 
L 3 HOH 206 606 884  HOH HOH C . 
L 3 HOH 207 607 895  HOH HOH C . 
L 3 HOH 208 608 311  HOH HOH C . 
L 3 HOH 209 609 537  HOH HOH C . 
L 3 HOH 210 610 650  HOH HOH C . 
L 3 HOH 211 611 762  HOH HOH C . 
L 3 HOH 212 612 939  HOH HOH C . 
L 3 HOH 213 613 575  HOH HOH C . 
L 3 HOH 214 614 794  HOH HOH C . 
L 3 HOH 215 615 793  HOH HOH C . 
L 3 HOH 216 616 743  HOH HOH C . 
L 3 HOH 217 617 843  HOH HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JN4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.817 
_cell.length_a_esd                 ? 
_cell.length_b                     101.256 
_cell.length_b_esd                 ? 
_cell.length_c                     111.066 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JN4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JN4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.20 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M ammonium acetate, 0.1 M Tris pH 8.0,  
1.0 M sodium citrate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JN4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.81 
_reflns.d_resolution_low                               25.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     91871 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.917 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.083 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       383395 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   1.000 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.073 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.81 1.87  ? ? ? ? ? ? 8810 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.494 ? ? 0.495 0.258 ? 1  1 0.930 0.982 ? 95.7 ? 0.419 ? ? ? ? ? ? ? ? ? 
1.87 1.95  ? ? ? ? ? ? 9063 ? ? ? ? ? ? ? ? ? ? ? 3.9 0.549 ? ? 0.358 0.174 ? 2  1 0.966 0.991 ? 98.3 ? 0.312 ? ? ? ? ? ? ? ? ? 
1.95 2.04  ? ? ? ? ? ? 9128 ? ? ? ? ? ? ? ? ? ? ? 4.2 0.603 ? ? 0.268 0.127 ? 3  1 0.980 0.995 ? 98.9 ? 0.235 ? ? ? ? ? ? ? ? ? 
2.04 2.15  ? ? ? ? ? ? 9176 ? ? ? ? ? ? ? ? ? ? ? 4.3 0.691 ? ? 0.189 0.089 ? 4  1 0.990 0.998 ? 99.0 ? 0.166 ? ? ? ? ? ? ? ? ? 
2.15 2.28  ? ? ? ? ? ? 9171 ? ? ? ? ? ? ? ? ? ? ? 4.3 0.778 ? ? 0.152 0.072 ? 5  1 0.994 0.998 ? 99.1 ? 0.134 ? ? ? ? ? ? ? ? ? 
2.28 2.46  ? ? ? ? ? ? 9198 ? ? ? ? ? ? ? ? ? ? ? 4.0 0.958 ? ? 0.124 0.060 ? 6  1 0.994 0.999 ? 98.8 ? 0.107 ? ? ? ? ? ? ? ? ? 
2.46 2.70  ? ? ? ? ? ? 9160 ? ? ? ? ? ? ? ? ? ? ? 4.3 1.202 ? ? 0.097 0.046 ? 7  1 0.997 0.999 ? 98.5 ? 0.085 ? ? ? ? ? ? ? ? ? 
2.70 3.09  ? ? ? ? ? ? 9248 ? ? ? ? ? ? ? ? ? ? ? 4.5 1.183 ? ? 0.072 0.033 ? 8  1 0.998 0.999 ? 98.8 ? 0.064 ? ? ? ? ? ? ? ? ? 
3.09 3.90  ? ? ? ? ? ? 9375 ? ? ? ? ? ? ? ? ? ? ? 4.5 1.291 ? ? 0.056 0.026 ? 9  1 0.998 1.000 ? 99.4 ? 0.050 ? ? ? ? ? ? ? ? ? 
3.90 25.00 ? ? ? ? ? ? 9542 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.176 ? ? 0.057 0.027 ? 10 1 0.997 0.999 ? 97.9 ? 0.050 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            1.48 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -2.05 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.57 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.423 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JN4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.81 
_refine.ls_d_res_low                             24.69 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     87035 
_refine.ls_number_reflns_R_free                  4588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.47 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21548 
_refine.ls_R_factor_R_free                       0.25272 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21346 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.145 
_refine.pdbx_overall_ESU_R_Free                  0.139 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.357 
_refine.overall_SU_ML                            0.103 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.81 
_refine_hist.d_res_low                        24.69 
_refine_hist.number_atoms_solvent             1006 
_refine_hist.number_atoms_total               7610 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6432 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         172 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.013  6808  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  6258  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.787  1.690  9350  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.427  1.595  14322 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.498  5.000  846   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 30.721 19.130 368   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.514 15.000 928   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.903 15.000 76    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.200  832   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  7898  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1642  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.141  2.173  3396  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.141  2.172  3395  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.128  3.249  4238  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.128  3.250  4239  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.711  2.403  3412  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.711  2.403  3410  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.158  3.480  5112  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.253  26.843 8145  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.024  25.983 7817  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.81 
_refine_ls_shell.d_res_low                        1.856 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             282 
_refine_ls_shell.number_reflns_R_work             5564 
_refine_ls_shell.percent_reflns_obs               85.13 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.288 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.301 
# 
_struct.entry_id                     9JN4 
_struct.title                        'Crystal structure of KtzT-C197A in complex with HEME' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9JN4 
_struct_keywords.text            'Heme-dependent piperazate synthase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8CF72_KUTS7 
_struct_ref.pdbx_db_accession          A8CF72 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAALGGAA
NVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYFRRILP
GVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGCEATRAVAGLMDRLPTE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JN4 B 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
2 1 9JN4 D 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
3 1 9JN4 A 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
4 1 9JN4 C 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JN4 ALA B 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  1  
1 9JN4 GLY B 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  2  
1 9JN4 ALA B 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  3  
1 9JN4 GLY B 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  4  
1 9JN4 ALA B 5   ? UNP A8CF72 ?   ?   'expression tag'      0   5  
1 9JN4 ALA B 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 6  
2 9JN4 ALA D 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  7  
2 9JN4 GLY D 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  8  
2 9JN4 ALA D 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  9  
2 9JN4 GLY D 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  10 
2 9JN4 ALA D 5   ? UNP A8CF72 ?   ?   'expression tag'      0   11 
2 9JN4 ALA D 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 12 
3 9JN4 ALA A 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  13 
3 9JN4 GLY A 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  14 
3 9JN4 ALA A 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  15 
3 9JN4 GLY A 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  16 
3 9JN4 ALA A 5   ? UNP A8CF72 ?   ?   'expression tag'      0   17 
3 9JN4 ALA A 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 18 
4 9JN4 ALA C 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  19 
4 9JN4 GLY C 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  20 
4 9JN4 ALA C 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  21 
4 9JN4 GLY C 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  22 
4 9JN4 ALA C 5   ? UNP A8CF72 ?   ?   'expression tag'      0   23 
4 9JN4 ALA C 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 24 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6720  ? 
1 MORE         -73   ? 
1 'SSA (A^2)'  17810 ? 
2 'ABSA (A^2)' 6750  ? 
2 MORE         -76   ? 
2 'SSA (A^2)'  17650 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,I,J 
2 1 C,D,G,H,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 9   ? HIS A 13  ? PRO B 4   HIS B 8   5 ? 5  
HELX_P HELX_P2  AA2 ASP A 17  ? HIS A 27  ? ASP B 12  HIS B 22  1 ? 11 
HELX_P HELX_P3  AA3 GLY A 36  ? ALA A 40  ? GLY B 31  ALA B 35  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 75  ? LEU A 81  ? ASN B 70  LEU B 76  1 ? 7  
HELX_P HELX_P5  AA5 SER A 99  ? ARG A 104 ? SER B 94  ARG B 99  1 ? 6  
HELX_P HELX_P6  AA6 SER A 128 ? GLY A 148 ? SER B 123 GLY B 143 1 ? 21 
HELX_P HELX_P7  AA7 MET A 153 ? GLY A 155 ? MET B 148 GLY B 150 5 ? 3  
HELX_P HELX_P8  AA8 SER A 156 ? ILE A 163 ? SER B 151 ILE B 158 1 ? 8  
HELX_P HELX_P9  AA9 GLN A 188 ? GLY A 200 ? GLN B 183 GLY B 195 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 202 ? LEU A 215 ? ALA B 197 LEU B 210 1 ? 14 
HELX_P HELX_P11 AB2 PRO B 9   ? HIS B 13  ? PRO D 4   HIS D 8   5 ? 5  
HELX_P HELX_P12 AB3 ASP B 17  ? HIS B 27  ? ASP D 12  HIS D 22  1 ? 11 
HELX_P HELX_P13 AB4 GLY B 36  ? ALA B 40  ? GLY D 31  ALA D 35  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 75  ? GLY B 82  ? ASN D 70  GLY D 77  1 ? 8  
HELX_P HELX_P15 AB6 SER B 99  ? TYR B 103 ? SER D 94  TYR D 98  5 ? 5  
HELX_P HELX_P16 AB7 SER B 128 ? GLY B 148 ? SER D 123 GLY D 143 1 ? 21 
HELX_P HELX_P17 AB8 MET B 153 ? GLY B 155 ? MET D 148 GLY D 150 5 ? 3  
HELX_P HELX_P18 AB9 SER B 156 ? LEU B 164 ? SER D 151 LEU D 159 1 ? 9  
HELX_P HELX_P19 AC1 GLN B 188 ? GLY B 200 ? GLN D 183 GLY D 195 1 ? 13 
HELX_P HELX_P20 AC2 ALA B 202 ? ARG B 214 ? ALA D 197 ARG D 209 1 ? 13 
HELX_P HELX_P21 AC3 PRO C 9   ? HIS C 13  ? PRO A 4   HIS A 8   5 ? 5  
HELX_P HELX_P22 AC4 ASP C 17  ? HIS C 27  ? ASP A 12  HIS A 22  1 ? 11 
HELX_P HELX_P23 AC5 GLY C 36  ? ALA C 40  ? GLY A 31  ALA A 35  5 ? 5  
HELX_P HELX_P24 AC6 ASN C 75  ? GLY C 82  ? ASN A 70  GLY A 77  1 ? 8  
HELX_P HELX_P25 AC7 SER C 99  ? ARG C 104 ? SER A 94  ARG A 99  1 ? 6  
HELX_P HELX_P26 AC8 SER C 128 ? GLY C 148 ? SER A 123 GLY A 143 1 ? 21 
HELX_P HELX_P27 AC9 MET C 153 ? GLY C 155 ? MET A 148 GLY A 150 5 ? 3  
HELX_P HELX_P28 AD1 SER C 156 ? LEU C 164 ? SER A 151 LEU A 159 1 ? 9  
HELX_P HELX_P29 AD2 GLN C 188 ? GLY C 200 ? GLN A 183 GLY A 195 1 ? 13 
HELX_P HELX_P30 AD3 ALA C 202 ? ARG C 214 ? ALA A 197 ARG A 209 1 ? 13 
HELX_P HELX_P31 AD4 PRO D 9   ? HIS D 13  ? PRO C 4   HIS C 8   5 ? 5  
HELX_P HELX_P32 AD5 ASP D 17  ? HIS D 27  ? ASP C 12  HIS C 22  1 ? 11 
HELX_P HELX_P33 AD6 GLY D 36  ? ALA D 40  ? GLY C 31  ALA C 35  5 ? 5  
HELX_P HELX_P34 AD7 ASN D 75  ? GLY D 82  ? ASN C 70  GLY C 77  1 ? 8  
HELX_P HELX_P35 AD8 SER D 128 ? GLY D 148 ? SER C 123 GLY C 143 1 ? 21 
HELX_P HELX_P36 AD9 MET D 153 ? GLY D 155 ? MET C 148 GLY C 150 5 ? 3  
HELX_P HELX_P37 AE1 SER D 156 ? LEU D 164 ? SER C 151 LEU C 159 1 ? 9  
HELX_P HELX_P38 AE2 GLN D 188 ? GLY D 200 ? GLN C 183 GLY C 195 1 ? 13 
HELX_P HELX_P39 AE3 ALA D 202 ? ARG D 214 ? ALA C 197 ARG C 209 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 70 NE2 ? ? ? 1_555 E HEM . FE ? ? B HIS 65  B HEM 301 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc2 metalc ? ? B HIS 70 NE2 ? ? ? 1_555 F HEM . FE ? ? D HIS 65  D HEM 301 1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc3 metalc ? ? C HIS 70 NE2 ? ? ? 1_555 G HEM . FE ? ? A HIS 65  A HEM 301 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc4 metalc ? ? D HIS 70 NE2 ? ? ? 1_555 H HEM . FE ? ? C HIS 65  C HEM 301 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc5 metalc ? ? H HEM .  FE  ? ? ? 1_555 L HOH . O  ? ? C HEM 301 C HOH 511 1_555 ? ? ? ? ? ? ? 2.577 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 70 ? B HIS 65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NA ? E HEM . ? B HEM 301 ? 1_555 95.7  ? 
2  NE2 ? A HIS 70 ? B HIS 65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NB ? E HEM . ? B HEM 301 ? 1_555 87.5  ? 
3  NA  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NB ? E HEM . ? B HEM 301 ? 1_555 92.1  ? 
4  NE2 ? A HIS 70 ? B HIS 65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC ? E HEM . ? B HEM 301 ? 1_555 94.3  ? 
5  NA  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC ? E HEM . ? B HEM 301 ? 1_555 169.8 ? 
6  NB  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC ? E HEM . ? B HEM 301 ? 1_555 85.8  ? 
7  NE2 ? A HIS 70 ? B HIS 65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND ? E HEM . ? B HEM 301 ? 1_555 100.5 ? 
8  NA  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND ? E HEM . ? B HEM 301 ? 1_555 89.1  ? 
9  NB  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND ? E HEM . ? B HEM 301 ? 1_555 171.7 ? 
10 NC  ? E HEM .  ? B HEM 301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND ? E HEM . ? B HEM 301 ? 1_555 91.5  ? 
11 NE2 ? B HIS 70 ? D HIS 65  ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NA ? F HEM . ? D HEM 301 ? 1_555 95.6  ? 
12 NE2 ? B HIS 70 ? D HIS 65  ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NB ? F HEM . ? D HEM 301 ? 1_555 89.6  ? 
13 NA  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NB ? F HEM . ? D HEM 301 ? 1_555 90.2  ? 
14 NE2 ? B HIS 70 ? D HIS 65  ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NC ? F HEM . ? D HEM 301 ? 1_555 97.8  ? 
15 NA  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NC ? F HEM . ? D HEM 301 ? 1_555 166.1 ? 
16 NB  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 NC ? F HEM . ? D HEM 301 ? 1_555 86.3  ? 
17 NE2 ? B HIS 70 ? D HIS 65  ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 ND ? F HEM . ? D HEM 301 ? 1_555 102.0 ? 
18 NA  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 ND ? F HEM . ? D HEM 301 ? 1_555 89.8  ? 
19 NB  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 ND ? F HEM . ? D HEM 301 ? 1_555 168.3 ? 
20 NC  ? F HEM .  ? D HEM 301 ? 1_555 FE ? F HEM . ? D HEM 301 ? 1_555 ND ? F HEM . ? D HEM 301 ? 1_555 91.0  ? 
21 NE2 ? C HIS 70 ? A HIS 65  ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NA ? G HEM . ? A HEM 301 ? 1_555 97.2  ? 
22 NE2 ? C HIS 70 ? A HIS 65  ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NB ? G HEM . ? A HEM 301 ? 1_555 90.5  ? 
23 NA  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NB ? G HEM . ? A HEM 301 ? 1_555 89.7  ? 
24 NE2 ? C HIS 70 ? A HIS 65  ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NC ? G HEM . ? A HEM 301 ? 1_555 97.4  ? 
25 NA  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NC ? G HEM . ? A HEM 301 ? 1_555 165.3 ? 
26 NB  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 NC ? G HEM . ? A HEM 301 ? 1_555 88.0  ? 
27 NE2 ? C HIS 70 ? A HIS 65  ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 ND ? G HEM . ? A HEM 301 ? 1_555 101.8 ? 
28 NA  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 ND ? G HEM . ? A HEM 301 ? 1_555 88.7  ? 
29 NB  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 ND ? G HEM . ? A HEM 301 ? 1_555 167.7 ? 
30 NC  ? G HEM .  ? A HEM 301 ? 1_555 FE ? G HEM . ? A HEM 301 ? 1_555 ND ? G HEM . ? A HEM 301 ? 1_555 90.4  ? 
31 NE2 ? D HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NA ? H HEM . ? C HEM 301 ? 1_555 97.7  ? 
32 NE2 ? D HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NB ? H HEM . ? C HEM 301 ? 1_555 88.1  ? 
33 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NB ? H HEM . ? C HEM 301 ? 1_555 91.2  ? 
34 NE2 ? D HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 97.1  ? 
35 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 164.8 ? 
36 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 NC ? H HEM . ? C HEM 301 ? 1_555 86.0  ? 
37 NE2 ? D HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 102.6 ? 
38 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 87.7  ? 
39 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 169.3 ? 
40 NC  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 ND ? H HEM . ? C HEM 301 ? 1_555 92.2  ? 
41 NE2 ? D HIS 70 ? C HIS 65  ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? L HOH . ? C HOH 511 ? 1_555 162.3 ? 
42 NA  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? L HOH . ? C HOH 511 ? 1_555 85.6  ? 
43 NB  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? L HOH . ? C HOH 511 ? 1_555 74.4  ? 
44 NC  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? L HOH . ? C HOH 511 ? 1_555 79.3  ? 
45 ND  ? H HEM .  ? C HEM 301 ? 1_555 FE ? H HEM . ? C HEM 301 ? 1_555 O  ? L HOH . ? C HOH 511 ? 1_555 94.9  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 106 A . ? ALA 101 B PRO 107 A ? PRO 102 B 1 -2.13  
2 ALA 106 B . ? ALA 101 D PRO 107 B ? PRO 102 D 1 -12.68 
3 ALA 106 C . ? ALA 101 A PRO 107 C ? PRO 102 A 1 -0.57  
4 ALA 106 D . ? ALA 101 C PRO 107 D ? PRO 102 C 1 -6.32  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
AA4 ? 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 
AA1 7 8 ? 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 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 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 GLU A 176 ? LYS A 182 ? GLU B 171 LYS B 177 
AA1 2 THR A 111 ? VAL A 126 ? THR B 106 VAL B 121 
AA1 3 VAL A 167 ? ARG A 173 ? VAL B 162 ARG B 168 
AA1 4 THR A 66  ? ASN A 72  ? THR B 61  ASN B 67  
AA1 5 HIS A 43  ? VAL A 51  ? HIS B 38  VAL B 46  
AA1 6 LEU A 29  ? SER A 34  ? LEU B 24  SER B 29  
AA1 7 ASN A 86  ? VAL A 98  ? ASN B 81  VAL B 93  
AA1 8 THR A 111 ? VAL A 126 ? THR B 106 VAL B 121 
AA2 1 GLU B 176 ? LYS B 182 ? GLU D 171 LYS D 177 
AA2 2 THR B 111 ? LYS B 125 ? THR D 106 LYS D 120 
AA2 3 VAL B 167 ? ARG B 173 ? VAL D 162 ARG D 168 
AA2 4 THR B 66  ? ASN B 72  ? THR D 61  ASN D 67  
AA2 5 HIS B 43  ? VAL B 51  ? HIS D 38  VAL D 46  
AA2 6 LEU B 29  ? SER B 34  ? LEU D 24  SER D 29  
AA2 7 ALA B 85  ? VAL B 98  ? ALA D 80  VAL D 93  
AA2 8 THR B 111 ? LYS B 125 ? THR D 106 LYS D 120 
AA3 1 GLU C 176 ? LYS C 182 ? GLU A 171 LYS A 177 
AA3 2 THR C 111 ? VAL C 126 ? THR A 106 VAL A 121 
AA3 3 VAL C 167 ? ARG C 173 ? VAL A 162 ARG A 168 
AA3 4 THR C 66  ? ASN C 72  ? THR A 61  ASN A 67  
AA3 5 HIS C 43  ? VAL C 51  ? HIS A 38  VAL A 46  
AA3 6 LEU C 29  ? SER C 34  ? LEU A 24  SER A 29  
AA3 7 ASN C 86  ? VAL C 98  ? ASN A 81  VAL A 93  
AA3 8 THR C 111 ? VAL C 126 ? THR A 106 VAL A 121 
AA4 1 LEU D 29  ? SER D 34  ? LEU C 24  SER C 29  
AA4 2 HIS D 43  ? VAL D 51  ? HIS C 38  VAL C 46  
AA4 3 THR D 66  ? ASN D 72  ? THR C 61  ASN C 67  
AA4 4 VAL D 167 ? LYS D 182 ? VAL C 162 LYS C 177 
AA4 5 THR D 111 ? LYS D 125 ? THR C 106 LYS C 120 
AA4 6 ALA D 85  ? VAL D 98  ? ALA C 80  VAL C 93  
AA4 7 LEU D 29  ? SER D 34  ? LEU C 24  SER C 29  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 176 ? O GLU B 171 N ARG A 120 ? N ARG B 115 
AA1 2 3 N ARG A 124 ? N ARG B 119 O ARG A 171 ? O ARG B 166 
AA1 3 4 O GLY A 168 ? O GLY B 163 N MET A 71  ? N MET B 66  
AA1 4 5 O TRP A 68  ? O TRP B 63  N ILE A 50  ? N ILE B 45  
AA1 5 6 O THR A 45  ? O THR B 40  N LEU A 32  ? N LEU B 27  
AA1 6 7 N ALA A 33  ? N ALA B 28  O VAL A 88  ? O VAL B 83  
AA1 7 8 N VAL A 98  ? N VAL B 93  O THR A 111 ? O THR B 106 
AA2 1 2 O LYS B 182 ? O LYS D 177 N PHE B 114 ? N PHE D 109 
AA2 2 3 N ARG B 124 ? N ARG D 119 O ARG B 171 ? O ARG D 166 
AA2 3 4 O PHE B 170 ? O PHE D 165 N GLY B 69  ? N GLY D 64  
AA2 4 5 O TRP B 68  ? O TRP D 63  N ILE B 50  ? N ILE D 45  
AA2 5 6 O THR B 45  ? O THR D 40  N LEU B 32  ? N LEU D 27  
AA2 6 7 N ALA B 33  ? N ALA D 28  O VAL B 88  ? O VAL D 83  
AA2 7 8 N PHE B 91  ? N PHE D 86  O VAL B 117 ? O VAL D 112 
AA3 1 2 O LYS C 182 ? O LYS A 177 N PHE C 114 ? N PHE A 109 
AA3 2 3 N VAL C 126 ? N VAL A 121 O ALA C 169 ? O ALA A 164 
AA3 3 4 O GLY C 168 ? O GLY A 163 N MET C 71  ? N MET A 66  
AA3 4 5 O TRP C 68  ? O TRP A 63  N ILE C 50  ? N ILE A 45  
AA3 5 6 O THR C 45  ? O THR A 40  N LEU C 32  ? N LEU A 27  
AA3 6 7 N GLN C 31  ? N GLN A 26  O THR C 90  ? O THR A 85  
AA3 7 8 N PHE C 91  ? N PHE A 86  O VAL C 117 ? O VAL A 112 
AA4 1 2 N LEU D 32  ? N LEU C 27  O THR D 45  ? O THR C 40  
AA4 2 3 N ILE D 50  ? N ILE C 45  O TRP D 68  ? O TRP C 63  
AA4 3 4 N MET D 71  ? N MET C 66  O GLY D 168 ? O GLY C 163 
AA4 4 5 O GLU D 176 ? O GLU C 171 N ARG D 120 ? N ARG C 115 
AA4 5 6 O VAL D 117 ? O VAL C 112 N PHE D 91  ? N PHE C 86  
AA4 6 7 O VAL D 88  ? O VAL C 83  N ALA D 33  ? N ALA C 28  
# 
_pdbx_entry_details.entry_id                   9JN4 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 401 ? ? O B HOH 578 ? ? 1.09 
2  1 O   C HOH 551 ? ? O C HOH 558 ? ? 1.69 
3  1 O   A MET 148 ? ? O A HOH 401 ? ? 1.85 
4  1 O   A HOH 542 ? ? O A HOH 625 ? ? 1.87 
5  1 NH2 D ARG 168 ? ? O D HOH 401 ? ? 1.90 
6  1 O   D HOH 498 ? ? O D HOH 503 ? ? 1.95 
7  1 O   D HOH 619 ? ? O D HOH 662 ? ? 1.99 
8  1 O   C HOH 598 ? ? O C HOH 601 ? ? 2.00 
9  1 CD2 D LEU 159 ? ? O D HOH 403 ? ? 2.02 
10 1 O1D B HEM 301 ? ? O B HOH 401 ? ? 2.02 
11 1 O   A HOH 654 ? ? O A HOH 657 ? ? 2.04 
12 1 OG1 B THR 40  ? ? O B HOH 402 ? ? 2.05 
13 1 O   D HOH 492 ? ? O D HOH 551 ? ? 2.06 
14 1 O   A HOH 516 ? ? O C HOH 568 ? ? 2.06 
15 1 O2D A HEM 301 ? ? O A HOH 402 ? ? 2.09 
16 1 O   D HOH 588 ? ? O D HOH 635 ? ? 2.09 
17 1 O   A HOH 543 ? ? O A HOH 601 ? ? 2.11 
18 1 O   B HOH 402 ? ? O D HOH 539 ? ? 2.11 
19 1 O   B HOH 508 ? ? O D HOH 597 ? ? 2.12 
20 1 O   B HOH 550 ? ? O B HOH 589 ? ? 2.12 
21 1 O   A HOH 604 ? ? O C HOH 590 ? ? 2.12 
22 1 O   B HOH 512 ? ? O B HOH 528 ? ? 2.12 
23 1 O   B HOH 546 ? ? O D HOH 411 ? ? 2.13 
24 1 O   A MET 207 ? ? O A HOH 403 ? ? 2.13 
25 1 O   B HOH 457 ? ? O B HOH 597 ? ? 2.13 
26 1 O   B HOH 648 ? ? O D HOH 661 ? ? 2.14 
27 1 O   B HOH 583 ? ? O B HOH 593 ? ? 2.15 
28 1 O   A HOH 547 ? ? O A HOH 562 ? ? 2.16 
29 1 O   D HOH 406 ? ? O D HOH 592 ? ? 2.17 
30 1 O   A HOH 558 ? ? O A HOH 607 ? ? 2.17 
31 1 O   B HOH 609 ? ? O D HOH 419 ? ? 2.18 
32 1 O   C HOH 525 ? ? O C HOH 559 ? ? 2.19 
33 1 CE2 A TYR 92  ? ? O C HOH 401 ? ? 2.19 
34 1 OE1 C GLU 139 ? ? O C HOH 401 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 562 ? ? 1_555 O D HOH 587 ? ? 3_645 1.99 
2 1 O B HOH 653 ? ? 1_555 O D HOH 673 ? ? 3_645 2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_1             205 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_2             205 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.329 
_pdbx_validate_rmsd_bond.bond_target_value         1.232 
_pdbx_validate_rmsd_bond.bond_deviation            0.097 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE D ARG 115 ? ? CZ D ARG 115 ? ? NH2 D ARG 115 ? ? 116.34 120.30 -3.96 0.50 N 
2 1 NE A ARG 115 ? ? CZ A ARG 115 ? ? NH1 A ARG 115 ? ? 123.49 120.30 3.19  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP B 47  ? ? -33.74  110.46 
2  1 ALA B 144 ? ? -142.55 40.06  
3  1 LEU B 178 ? ? -141.13 37.93  
4  1 ASP D 47  ? ? -34.47  108.86 
5  1 ALA D 144 ? ? -147.15 39.71  
6  1 PHE D 176 ? ? -117.62 78.16  
7  1 ASP A 47  ? ? -32.15  113.68 
8  1 HIS C 22  ? ? -146.76 59.06  
9  1 ASP C 47  ? ? -26.96  108.73 
10 1 ALA C 144 ? ? -148.96 41.71  
11 1 PHE C 176 ? ? -114.40 76.42  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? B HOH 652 ? 5.99  . 
2  1 O ? B HOH 653 ? 7.55  . 
3  1 O ? D HOH 665 ? 5.92  . 
4  1 O ? D HOH 666 ? 5.95  . 
5  1 O ? D HOH 667 ? 5.97  . 
6  1 O ? D HOH 668 ? 6.23  . 
7  1 O ? D HOH 669 ? 6.34  . 
8  1 O ? D HOH 670 ? 6.51  . 
9  1 O ? D HOH 671 ? 6.60  . 
10 1 O ? D HOH 672 ? 6.65  . 
11 1 O ? D HOH 673 ? 6.97  . 
12 1 O ? D HOH 674 ? 7.05  . 
13 1 O ? D HOH 675 ? 7.06  . 
14 1 O ? D HOH 676 ? 8.33  . 
15 1 O ? A HOH 649 ? 5.82  . 
16 1 O ? A HOH 650 ? 5.85  . 
17 1 O ? A HOH 651 ? 6.00  . 
18 1 O ? A HOH 652 ? 6.08  . 
19 1 O ? A HOH 653 ? 6.15  . 
20 1 O ? A HOH 654 ? 6.29  . 
21 1 O ? A HOH 655 ? 6.58  . 
22 1 O ? A HOH 656 ? 6.66  . 
23 1 O ? A HOH 657 ? 6.77  . 
24 1 O ? A HOH 658 ? 8.14  . 
25 1 O ? A HOH 659 ? 8.40  . 
26 1 O ? A HOH 660 ? 10.17 . 
27 1 O ? C HOH 616 ? 6.27  . 
28 1 O ? C HOH 617 ? 6.31  . 
# 
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 B ALA -4  ? A ALA 1   
2  1 Y 1 B GLY -3  ? A GLY 2   
3  1 Y 1 B ALA -2  ? A ALA 3   
4  1 Y 1 B THR 212 ? A THR 217 
5  1 Y 1 B GLU 213 ? A GLU 218 
6  1 Y 1 D ALA -4  ? B ALA 1   
7  1 Y 1 D GLY -3  ? B GLY 2   
8  1 Y 1 D ALA -2  ? B ALA 3   
9  1 Y 1 D GLY -1  ? B GLY 4   
10 1 Y 1 D THR 212 ? B THR 217 
11 1 Y 1 D GLU 213 ? B GLU 218 
12 1 Y 1 A ALA -4  ? C ALA 1   
13 1 Y 1 A GLY -3  ? C GLY 2   
14 1 Y 1 A ALA -2  ? C ALA 3   
15 1 Y 1 A THR 212 ? C THR 217 
16 1 Y 1 A GLU 213 ? C GLU 218 
17 1 Y 1 C ALA -4  ? D ALA 1   
18 1 Y 1 C GLY -3  ? D GLY 2   
19 1 Y 1 C ALA -2  ? D ALA 3   
20 1 Y 1 C GLY -1  ? D GLY 4   
21 1 Y 1 C THR 212 ? D THR 217 
22 1 Y 1 C GLU 213 ? D GLU 218 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
PHE N    N  N N 325 
PHE CA   C  N S 326 
PHE C    C  N N 327 
PHE O    O  N N 328 
PHE CB   C  N N 329 
PHE CG   C  Y N 330 
PHE CD1  C  Y N 331 
PHE CD2  C  Y N 332 
PHE CE1  C  Y N 333 
PHE CE2  C  Y N 334 
PHE CZ   C  Y N 335 
PHE OXT  O  N N 336 
PHE H    H  N N 337 
PHE H2   H  N N 338 
PHE HA   H  N N 339 
PHE HB2  H  N N 340 
PHE HB3  H  N N 341 
PHE HD1  H  N N 342 
PHE HD2  H  N N 343 
PHE HE1  H  N N 344 
PHE HE2  H  N N 345 
PHE HZ   H  N N 346 
PHE HXT  H  N N 347 
PRO N    N  N N 348 
PRO CA   C  N S 349 
PRO C    C  N N 350 
PRO O    O  N N 351 
PRO CB   C  N N 352 
PRO CG   C  N N 353 
PRO CD   C  N N 354 
PRO OXT  O  N N 355 
PRO H    H  N N 356 
PRO HA   H  N N 357 
PRO HB2  H  N N 358 
PRO HB3  H  N N 359 
PRO HG2  H  N N 360 
PRO HG3  H  N N 361 
PRO HD2  H  N N 362 
PRO HD3  H  N N 363 
PRO HXT  H  N N 364 
SER N    N  N N 365 
SER CA   C  N S 366 
SER C    C  N N 367 
SER O    O  N N 368 
SER CB   C  N N 369 
SER OG   O  N N 370 
SER OXT  O  N N 371 
SER H    H  N N 372 
SER H2   H  N N 373 
SER HA   H  N N 374 
SER HB2  H  N N 375 
SER HB3  H  N N 376 
SER HG   H  N N 377 
SER HXT  H  N N 378 
THR N    N  N N 379 
THR CA   C  N S 380 
THR C    C  N N 381 
THR O    O  N N 382 
THR CB   C  N R 383 
THR OG1  O  N N 384 
THR CG2  C  N N 385 
THR OXT  O  N N 386 
THR H    H  N N 387 
THR H2   H  N N 388 
THR HA   H  N N 389 
THR HB   H  N N 390 
THR HG1  H  N N 391 
THR HG21 H  N N 392 
THR HG22 H  N N 393 
THR HG23 H  N N 394 
THR HXT  H  N N 395 
TRP N    N  N N 396 
TRP CA   C  N S 397 
TRP C    C  N N 398 
TRP O    O  N N 399 
TRP CB   C  N N 400 
TRP CG   C  Y N 401 
TRP CD1  C  Y N 402 
TRP CD2  C  Y N 403 
TRP NE1  N  Y N 404 
TRP CE2  C  Y N 405 
TRP CE3  C  Y N 406 
TRP CZ2  C  Y N 407 
TRP CZ3  C  Y N 408 
TRP CH2  C  Y N 409 
TRP OXT  O  N N 410 
TRP H    H  N N 411 
TRP H2   H  N N 412 
TRP HA   H  N N 413 
TRP HB2  H  N N 414 
TRP HB3  H  N N 415 
TRP HD1  H  N N 416 
TRP HE1  H  N N 417 
TRP HE3  H  N N 418 
TRP HZ2  H  N N 419 
TRP HZ3  H  N N 420 
TRP HH2  H  N N 421 
TRP HXT  H  N N 422 
TYR N    N  N N 423 
TYR CA   C  N S 424 
TYR C    C  N N 425 
TYR O    O  N N 426 
TYR CB   C  N N 427 
TYR CG   C  Y N 428 
TYR CD1  C  Y N 429 
TYR CD2  C  Y N 430 
TYR CE1  C  Y N 431 
TYR CE2  C  Y N 432 
TYR CZ   C  Y N 433 
TYR OH   O  N N 434 
TYR OXT  O  N N 435 
TYR H    H  N N 436 
TYR H2   H  N N 437 
TYR HA   H  N N 438 
TYR HB2  H  N N 439 
TYR HB3  H  N N 440 
TYR HD1  H  N N 441 
TYR HD2  H  N N 442 
TYR HE1  H  N N 443 
TYR HE2  H  N N 444 
TYR HH   H  N N 445 
TYR HXT  H  N N 446 
VAL N    N  N N 447 
VAL CA   C  N S 448 
VAL C    C  N N 449 
VAL O    O  N N 450 
VAL CB   C  N N 451 
VAL CG1  C  N N 452 
VAL CG2  C  N N 453 
VAL OXT  O  N N 454 
VAL H    H  N N 455 
VAL H2   H  N N 456 
VAL HA   H  N N 457 
VAL HB   H  N N 458 
VAL HG11 H  N N 459 
VAL HG12 H  N N 460 
VAL HG13 H  N N 461 
VAL HG21 H  N N 462 
VAL HG22 H  N N 463 
VAL HG23 H  N N 464 
VAL HXT  H  N N 465 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFA0911400 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JN4 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011011 
_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]   0.009876 
_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]   0.009004 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
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   . GLY A 1 4   ? 34.304 8.087   35.490  1.00 41.24  ?  -1  GLY B N   1 
ATOM   2    C  CA  . GLY A 1 4   ? 34.782 7.085   34.496  1.00 36.04  ?  -1  GLY B CA  1 
ATOM   3    C  C   . GLY A 1 4   ? 36.183 7.413   34.001  1.00 32.68  ?  -1  GLY B C   1 
ATOM   4    O  O   . GLY A 1 4   ? 36.440 8.590   33.644  1.00 31.76  ?  -1  GLY B O   1 
ATOM   5    N  N   . ALA A 1 5   ? 37.069 6.418   33.956  1.00 27.66  ?  0   ALA B N   1 
ATOM   6    C  CA  . ALA A 1 5   ? 38.498 6.602   33.595  1.00 25.51  ?  0   ALA B CA  1 
ATOM   7    C  C   . ALA A 1 5   ? 38.684 6.602   32.071  1.00 23.49  ?  0   ALA B C   1 
ATOM   8    O  O   . ALA A 1 5   ? 39.766 7.032   31.616  1.00 22.34  ?  0   ALA B O   1 
ATOM   9    C  CB  . ALA A 1 5   ? 39.326 5.513   34.211  1.00 26.35  ?  0   ALA B CB  1 
ATOM   10   N  N   . MET A 1 6   ? 37.729 6.042   31.328  1.00 22.78  ?  1   MET B N   1 
ATOM   11   C  CA  . MET A 1 6   ? 37.738 6.048   29.845  1.00 20.61  ?  1   MET B CA  1 
ATOM   12   C  C   . MET A 1 6   ? 36.423 6.636   29.351  1.00 21.01  ?  1   MET B C   1 
ATOM   13   O  O   . MET A 1 6   ? 35.360 6.261   29.875  1.00 22.07  ?  1   MET B O   1 
ATOM   14   C  CB  . MET A 1 6   ? 37.920 4.649   29.263  1.00 21.37  ?  1   MET B CB  1 
ATOM   15   C  CG  . MET A 1 6   ? 37.785 4.571   27.749  1.00 20.43  ?  1   MET B CG  1 
ATOM   16   S  SD  . MET A 1 6   ? 37.920 2.850   27.245  1.00 25.97  ?  1   MET B SD  1 
ATOM   17   C  CE  . MET A 1 6   ? 38.088 2.948   25.470  1.00 25.57  ?  1   MET B CE  1 
ATOM   18   N  N   . PHE A 1 7   ? 36.485 7.539   28.384  1.00 19.91  ?  2   PHE B N   1 
ATOM   19   C  CA  . PHE A 1 7   ? 35.276 8.192   27.838  1.00 19.28  ?  2   PHE B CA  1 
ATOM   20   C  C   . PHE A 1 7   ? 34.657 7.277   26.772  1.00 19.32  ?  2   PHE B C   1 
ATOM   21   O  O   . PHE A 1 7   ? 35.321 7.021   25.742  1.00 19.10  ?  2   PHE B O   1 
ATOM   22   C  CB  . PHE A 1 7   ? 35.679 9.531   27.230  1.00 20.24  ?  2   PHE B CB  1 
ATOM   23   C  CG  . PHE A 1 7   ? 34.533 10.332  26.684  1.00 21.21  ?  2   PHE B CG  1 
ATOM   24   C  CD1 . PHE A 1 7   ? 33.529 10.780  27.534  1.00 25.06  ?  2   PHE B CD1 1 
ATOM   25   C  CD2 . PHE A 1 7   ? 34.447 10.626  25.333  1.00 23.65  ?  2   PHE B CD2 1 
ATOM   26   C  CE1 . PHE A 1 7   ? 32.458 11.517  27.048  1.00 25.00  ?  2   PHE B CE1 1 
ATOM   27   C  CE2 . PHE A 1 7   ? 33.373 11.358  24.853  1.00 24.81  ?  2   PHE B CE2 1 
ATOM   28   C  CZ  . PHE A 1 7   ? 32.400 11.816  25.706  1.00 25.23  ?  2   PHE B CZ  1 
ATOM   29   N  N   . VAL A 1 8   ? 33.419 6.840   26.970  1.00 18.68  ?  3   VAL B N   1 
ATOM   30   C  CA  . VAL A 1 8   ? 32.707 5.979   25.987  1.00 18.57  ?  3   VAL B CA  1 
ATOM   31   C  C   . VAL A 1 8   ? 31.295 6.508   25.881  1.00 22.14  ?  3   VAL B C   1 
ATOM   32   O  O   . VAL A 1 8   ? 30.515 6.324   26.830  1.00 25.39  ?  3   VAL B O   1 
ATOM   33   C  CB  . VAL A 1 8   ? 32.719 4.484   26.368  1.00 19.11  ?  3   VAL B CB  1 
ATOM   34   C  CG1 . VAL A 1 8   ? 32.070 3.591   25.304  1.00 19.25  ?  3   VAL B CG1 1 
ATOM   35   C  CG2 . VAL A 1 8   ? 34.110 4.015   26.672  1.00 18.02  ?  3   VAL B CG2 1 
ATOM   36   N  N   . PRO A 1 9   ? 30.952 7.172   24.752  1.00 22.95  ?  4   PRO B N   1 
ATOM   37   C  CA  . PRO A 1 9   ? 29.584 7.607   24.503  1.00 24.12  ?  4   PRO B CA  1 
ATOM   38   C  C   . PRO A 1 9   ? 28.640 6.407   24.619  1.00 25.04  ?  4   PRO B C   1 
ATOM   39   O  O   . PRO A 1 9   ? 28.987 5.271   24.243  1.00 22.68  ?  4   PRO B O   1 
ATOM   40   C  CB  . PRO A 1 9   ? 29.629 8.213   23.083  1.00 24.70  ?  4   PRO B CB  1 
ATOM   41   C  CG  . PRO A 1 9   ? 31.080 8.639   22.924  1.00 25.69  ?  4   PRO B CG  1 
ATOM   42   C  CD  . PRO A 1 9   ? 31.849 7.547   23.640  1.00 25.33  ?  4   PRO B CD  1 
ATOM   43   N  N   . GLY A 1 10  ? 27.424 6.669   25.102  1.00 25.24  ?  5   GLY B N   1 
ATOM   44   C  CA  . GLY A 1 10  ? 26.430 5.619   25.378  1.00 25.53  ?  5   GLY B CA  1 
ATOM   45   C  C   . GLY A 1 10  ? 26.210 4.673   24.195  1.00 24.26  ?  5   GLY B C   1 
ATOM   46   O  O   . GLY A 1 10  ? 26.056 3.466   24.379  1.00 27.92  ?  5   GLY B O   1 
ATOM   47   N  N   . PRO A 1 11  ? 26.142 5.157   22.942  1.00 24.49  ?  6   PRO B N   1 
ATOM   48   C  CA  . PRO A 1 11  ? 25.871 4.263   21.820  1.00 25.43  ?  6   PRO B CA  1 
ATOM   49   C  C   . PRO A 1 11  ? 26.960 3.197   21.619  1.00 24.31  ?  6   PRO B C   1 
ATOM   50   O  O   . PRO A 1 11  ? 26.695 2.192   20.998  1.00 22.21  ?  6   PRO B O   1 
ATOM   51   C  CB  . PRO A 1 11  ? 25.783 5.194   20.606  1.00 25.56  ?  6   PRO B CB  1 
ATOM   52   C  CG  . PRO A 1 11  ? 25.524 6.568   21.195  1.00 26.86  ?  6   PRO B CG  1 
ATOM   53   C  CD  . PRO A 1 11  ? 26.188 6.573   22.547  1.00 25.91  ?  6   PRO B CD  1 
ATOM   54   N  N   . TYR A 1 12  ? 28.153 3.423   22.170  1.00 21.37  ?  7   TYR B N   1 
ATOM   55   C  CA  . TYR A 1 12  ? 29.341 2.605   21.886  1.00 20.79  ?  7   TYR B CA  1 
ATOM   56   C  C   . TYR A 1 12  ? 29.669 1.685   23.052  1.00 22.20  ?  7   TYR B C   1 
ATOM   57   O  O   . TYR A 1 12  ? 30.707 1.005   22.975  1.00 19.63  ?  7   TYR B O   1 
ATOM   58   C  CB  . TYR A 1 12  ? 30.505 3.524   21.554  1.00 19.86  ?  7   TYR B CB  1 
ATOM   59   C  CG  . TYR A 1 12  ? 30.250 4.418   20.380  1.00 21.14  ?  7   TYR B CG  1 
ATOM   60   C  CD1 . TYR A 1 12  ? 29.401 4.017   19.355  1.00 20.39  ?  7   TYR B CD1 1 
ATOM   61   C  CD2 . TYR A 1 12  ? 30.810 5.682   20.328  1.00 19.46  ?  7   TYR B CD2 1 
ATOM   62   C  CE1 . TYR A 1 12  ? 29.137 4.855   18.289  1.00 21.59  ?  7   TYR B CE1 1 
ATOM   63   C  CE2 . TYR A 1 12  ? 30.594 6.516   19.243  1.00 21.45  ?  7   TYR B CE2 1 
ATOM   64   C  CZ  . TYR A 1 12  ? 29.740 6.096   18.230  1.00 20.37  ?  7   TYR B CZ  1 
ATOM   65   O  OH  . TYR A 1 12  ? 29.467 6.880   17.156  1.00 22.26  ?  7   TYR B OH  1 
ATOM   66   N  N   . HIS A 1 13  ? 28.794 1.581   24.051  1.00 22.38  ?  8   HIS B N   1 
ATOM   67   C  CA  . HIS A 1 13  ? 28.912 0.562   25.130  1.00 23.91  ?  8   HIS B CA  1 
ATOM   68   C  C   . HIS A 1 13  ? 28.732 -0.851  24.533  1.00 23.89  ?  8   HIS B C   1 
ATOM   69   O  O   . HIS A 1 13  ? 27.867 -1.070  23.626  1.00 23.32  ?  8   HIS B O   1 
ATOM   70   C  CB  . HIS A 1 13  ? 27.966 0.899   26.301  1.00 26.93  ?  8   HIS B CB  1 
ATOM   71   C  CG  . HIS A 1 13  ? 28.304 2.135   27.089  1.00 31.00  ?  8   HIS B CG  1 
ATOM   72   N  ND1 . HIS A 1 13  ? 27.855 2.337   28.396  1.00 40.20  ?  8   HIS B ND1 1 
ATOM   73   C  CD2 . HIS A 1 13  ? 29.036 3.234   26.799  1.00 34.64  ?  8   HIS B CD2 1 
ATOM   74   C  CE1 . HIS A 1 13  ? 28.299 3.502   28.848  1.00 38.57  ?  8   HIS B CE1 1 
ATOM   75   N  NE2 . HIS A 1 13  ? 29.006 4.081   27.882  1.00 35.56  ?  8   HIS B NE2 1 
ATOM   76   N  N   . ALA A 1 14  ? 29.506 -1.826  25.017  1.00 23.30  ?  9   ALA B N   1 
ATOM   77   C  CA  . ALA A 1 14  ? 29.326 -3.247  24.638  1.00 24.34  ?  9   ALA B CA  1 
ATOM   78   C  C   . ALA A 1 14  ? 27.913 -3.678  25.012  1.00 26.12  ?  9   ALA B C   1 
ATOM   79   O  O   . ALA A 1 14  ? 27.392 -3.220  26.030  1.00 22.59  ?  9   ALA B O   1 
ATOM   80   C  CB  . ALA A 1 14  ? 30.327 -4.127  25.318  1.00 25.74  ?  9   ALA B CB  1 
ATOM   81   N  N   . PRO A 1 15  ? 27.289 -4.586  24.231  1.00 28.27  ?  10  PRO B N   1 
ATOM   82   C  CA  . PRO A 1 15  ? 26.014 -5.198  24.611  1.00 29.24  ?  10  PRO B CA  1 
ATOM   83   C  C   . PRO A 1 15  ? 26.087 -6.010  25.912  1.00 30.49  ?  10  PRO B C   1 
ATOM   84   O  O   . PRO A 1 15  ? 25.117 -6.028  26.633  1.00 28.61  ?  10  PRO B O   1 
ATOM   85   C  CB  . PRO A 1 15  ? 25.714 -6.155  23.445  1.00 31.92  ?  10  PRO B CB  1 
ATOM   86   C  CG  . PRO A 1 15  ? 26.508 -5.606  22.292  1.00 31.79  ?  10  PRO B CG  1 
ATOM   87   C  CD  . PRO A 1 15  ? 27.768 -5.069  22.921  1.00 30.74  ?  10  PRO B CD  1 
ATOM   88   N  N   . GLU A 1 16  ? 27.211 -6.703  26.151  1.00 27.81  ?  11  GLU B N   1 
ATOM   89   C  CA  . GLU A 1 16  ? 27.416 -7.617  27.312  1.00 30.72  ?  11  GLU B CA  1 
ATOM   90   C  C   . GLU A 1 16  ? 28.848 -7.435  27.803  1.00 27.24  ?  11  GLU B C   1 
ATOM   91   O  O   . GLU A 1 16  ? 29.747 -7.236  26.930  1.00 21.23  ?  11  GLU B O   1 
ATOM   92   C  CB  . GLU A 1 16  ? 27.247 -9.102  26.955  1.00 35.48  ?  11  GLU B CB  1 
ATOM   93   C  CG  . GLU A 1 16  ? 25.953 -9.467  26.232  1.00 43.46  ?  11  GLU B CG  1 
ATOM   94   C  CD  . GLU A 1 16  ? 24.651 -9.422  27.025  1.00 51.56  ?  11  GLU B CD  1 
ATOM   95   O  OE1 . GLU A 1 16  ? 23.579 -9.347  26.380  1.00 59.94  ?  11  GLU B OE1 1 
ATOM   96   O  OE2 . GLU A 1 16  ? 24.694 -9.469  28.277  1.00 57.73  -1 11  GLU B OE2 1 
ATOM   97   N  N   . ASP A 1 17  ? 29.071 -7.561  29.116  1.00 24.28  ?  12  ASP B N   1 
ATOM   98   C  CA  . ASP A 1 17  ? 30.440 -7.527  29.697  1.00 26.62  ?  12  ASP B CA  1 
ATOM   99   C  C   . ASP A 1 17  ? 31.346 -8.544  28.987  1.00 23.44  ?  12  ASP B C   1 
ATOM   100  O  O   . ASP A 1 17  ? 32.538 -8.266  28.875  1.00 23.24  ?  12  ASP B O   1 
ATOM   101  C  CB  . ASP A 1 17  ? 30.460 -7.840  31.192  1.00 26.96  ?  12  ASP B CB  1 
ATOM   102  C  CG  . ASP A 1 17  ? 29.798 -6.798  32.066  1.00 30.57  ?  12  ASP B CG  1 
ATOM   103  O  OD1 . ASP A 1 17  ? 29.970 -5.591  31.797  1.00 30.94  ?  12  ASP B OD1 1 
ATOM   104  O  OD2 . ASP A 1 17  ? 29.137 -7.215  33.031  1.00 36.12  -1 12  ASP B OD2 1 
ATOM   105  N  N   . ARG A 1 18  ? 30.813 -9.689  28.559  1.00 23.52  ?  13  ARG B N   1 
ATOM   106  C  CA  . ARG A 1 18  ? 31.594 -10.757 27.867  1.00 25.41  ?  13  ARG B CA  1 
ATOM   107  C  C   . ARG A 1 18  ? 32.362 -10.206 26.649  1.00 21.39  ?  13  ARG B C   1 
ATOM   108  O  O   . ARG A 1 18  ? 33.437 -10.749 26.352  1.00 21.24  ?  13  ARG B O   1 
ATOM   109  C  CB  . ARG A 1 18  ? 30.697 -11.905 27.395  1.00 27.53  ?  13  ARG B CB  1 
ATOM   110  C  CG  . ARG A 1 18  ? 31.434 -12.977 26.604  1.00 31.23  ?  13  ARG B CG  1 
ATOM   111  C  CD  . ARG A 1 18  ? 32.436 -13.779 27.410  1.00 35.55  ?  13  ARG B CD  1 
ATOM   112  N  NE  . ARG A 1 18  ? 31.689 -14.733 28.217  1.00 45.99  ?  13  ARG B NE  1 
ATOM   113  C  CZ  . ARG A 1 18  ? 31.555 -16.036 27.964  1.00 48.31  ?  13  ARG B CZ  1 
ATOM   114  N  NH1 . ARG A 1 18  ? 32.172 -16.594 26.934  1.00 48.16  ?  13  ARG B NH1 1 
ATOM   115  N  NH2 . ARG A 1 18  ? 30.821 -16.785 28.774  1.00 49.09  ?  13  ARG B NH2 1 
ATOM   116  N  N   . TRP A 1 19  ? 31.833 -9.204  25.946  1.00 20.15  ?  14  TRP B N   1 
ATOM   117  C  CA  . TRP A 1 19  ? 32.491 -8.637  24.738  1.00 18.75  ?  14  TRP B CA  1 
ATOM   118  C  C   . TRP A 1 19  ? 33.887 -8.100  25.101  1.00 17.48  ?  14  TRP B C   1 
ATOM   119  O  O   . TRP A 1 19  ? 34.764 -8.162  24.242  1.00 16.72  ?  14  TRP B O   1 
ATOM   120  C  CB  . TRP A 1 19  ? 31.664 -7.532  24.100  1.00 20.26  ?  14  TRP B CB  1 
ATOM   121  C  CG  . TRP A 1 19  ? 30.502 -8.034  23.307  1.00 23.02  ?  14  TRP B CG  1 
ATOM   122  C  CD1 . TRP A 1 19  ? 29.571 -8.959  23.701  1.00 24.92  ?  14  TRP B CD1 1 
ATOM   123  C  CD2 . TRP A 1 19  ? 30.137 -7.622  21.990  1.00 23.80  ?  14  TRP B CD2 1 
ATOM   124  N  NE1 . TRP A 1 19  ? 28.633 -9.132  22.720  1.00 26.37  ?  14  TRP B NE1 1 
ATOM   125  C  CE2 . TRP A 1 19  ? 28.968 -8.341  21.647  1.00 26.33  ?  14  TRP B CE2 1 
ATOM   126  C  CE3 . TRP A 1 19  ? 30.674 -6.712  21.071  1.00 24.50  ?  14  TRP B CE3 1 
ATOM   127  C  CZ2 . TRP A 1 19  ? 28.340 -8.178  20.416  1.00 27.23  ?  14  TRP B CZ2 1 
ATOM   128  C  CZ3 . TRP A 1 19  ? 30.041 -6.548  19.863  1.00 25.51  ?  14  TRP B CZ3 1 
ATOM   129  C  CH2 . TRP A 1 19  ? 28.892 -7.264  19.545  1.00 25.63  ?  14  TRP B CH2 1 
ATOM   130  N  N   . LEU A 1 20  ? 34.057 -7.519  26.295  1.00 18.03  ?  15  LEU B N   1 
ATOM   131  C  CA  . LEU A 1 20  ? 35.369 -6.962  26.724  1.00 18.02  ?  15  LEU B CA  1 
ATOM   132  C  C   . LEU A 1 20  ? 36.347 -8.119  26.956  1.00 18.91  ?  15  LEU B C   1 
ATOM   133  O  O   . LEU A 1 20  ? 37.499 -7.986  26.557  1.00 18.09  ?  15  LEU B O   1 
ATOM   134  C  CB  . LEU A 1 20  ? 35.199 -6.121  27.988  1.00 17.65  ?  15  LEU B CB  1 
ATOM   135  C  CG  . LEU A 1 20  ? 34.550 -4.751  27.780  1.00 17.57  ?  15  LEU B CG  1 
ATOM   136  C  CD1 . LEU A 1 20  ? 33.029 -4.846  27.703  1.00 18.45  ?  15  LEU B CD1 1 
ATOM   137  C  CD2 . LEU A 1 20  ? 34.964 -3.799  28.876  1.00 16.68  ?  15  LEU B CD2 1 
ATOM   138  N  N   . VAL A 1 21  ? 35.895 -9.208  27.589  1.00 18.19  ?  16  VAL B N   1 
ATOM   139  C  CA  . VAL A 1 21  ? 36.751 -10.406 27.842  1.00 18.97  ?  16  VAL B CA  1 
ATOM   140  C  C   . VAL A 1 21  ? 37.134 -10.979 26.484  1.00 16.80  ?  16  VAL B C   1 
ATOM   141  O  O   . VAL A 1 21  ? 38.317 -11.315 26.304  1.00 17.35  ?  16  VAL B O   1 
ATOM   142  C  CB  . VAL A 1 21  ? 36.066 -11.472 28.726  1.00 19.24  ?  16  VAL B CB  1 
ATOM   143  C  CG1 . VAL A 1 21  ? 36.946 -12.684 28.910  1.00 19.67  ?  16  VAL B CG1 1 
ATOM   144  C  CG2 . VAL A 1 21  ? 35.626 -10.936 30.089  1.00 19.76  ?  16  VAL B CG2 1 
ATOM   145  N  N   . ASP A 1 22  ? 36.186 -11.061 25.548  1.00 15.93  ?  17  ASP B N   1 
ATOM   146  C  CA  . ASP A 1 22  ? 36.447 -11.617 24.195  1.00 18.33  ?  17  ASP B CA  1 
ATOM   147  C  C   . ASP A 1 22  ? 37.562 -10.817 23.501  1.00 16.42  ?  17  ASP B C   1 
ATOM   148  O  O   . ASP A 1 22  ? 38.431 -11.437 22.829  1.00 17.35  ?  17  ASP B O   1 
ATOM   149  C  CB  . ASP A 1 22  ? 35.208 -11.589 23.306  1.00 20.62  ?  17  ASP B CB  1 
ATOM   150  C  CG  . ASP A 1 22  ? 34.092 -12.543 23.701  1.00 24.67  ?  17  ASP B CG  1 
ATOM   151  O  OD1 . ASP A 1 22  ? 34.343 -13.492 24.488  1.00 23.60  ?  17  ASP B OD1 1 
ATOM   152  O  OD2 . ASP A 1 22  ? 32.943 -12.305 23.213  1.00 28.68  -1 17  ASP B OD2 1 
ATOM   153  N  N   . LEU A 1 23  ? 37.542 -9.493  23.613  1.00 15.84  ?  18  LEU B N   1 
ATOM   154  C  CA  . LEU A 1 23  ? 38.533 -8.637  22.896  1.00 17.11  ?  18  LEU B CA  1 
ATOM   155  C  C   . LEU A 1 23  ? 39.912 -8.848  23.540  1.00 15.97  ?  18  LEU B C   1 
ATOM   156  O  O   . LEU A 1 23  ? 40.947 -9.005  22.828  1.00 16.37  ?  18  LEU B O   1 
ATOM   157  C  CB  . LEU A 1 23  ? 38.058 -7.178  22.943  1.00 19.05  ?  18  LEU B CB  1 
ATOM   158  C  CG  . LEU A 1 23  ? 38.814 -6.192  22.045  1.00 21.46  ?  18  LEU B CG  1 
ATOM   159  C  CD1 . LEU A 1 23  ? 38.020 -4.911  21.847  1.00 26.11  ?  18  LEU B CD1 1 
ATOM   160  C  CD2 . LEU A 1 23  ? 40.160 -5.818  22.634  1.00 24.73  ?  18  LEU B CD2 1 
ATOM   161  N  N   . VAL A 1 24  ? 39.958 -8.914  24.861  1.00 16.38  ?  19  VAL B N   1 
ATOM   162  C  CA  . VAL A 1 24  ? 41.234 -9.199  25.571  1.00 15.49  ?  19  VAL B CA  1 
ATOM   163  C  C   . VAL A 1 24  ? 41.792 -10.546 25.086  1.00 17.85  ?  19  VAL B C   1 
ATOM   164  O  O   . VAL A 1 24  ? 42.996 -10.600 24.812  1.00 16.61  ?  19  VAL B O   1 
ATOM   165  C  CB  . VAL A 1 24  ? 41.055 -9.132  27.102  1.00 16.30  ?  19  VAL B CB  1 
ATOM   166  C  CG1 . VAL A 1 24  ? 42.149 -9.837  27.818  1.00 16.47  ?  19  VAL B CG1 1 
ATOM   167  C  CG2 . VAL A 1 24  ? 40.920 -7.697  27.594  1.00 16.02  ?  19  VAL B CG2 1 
ATOM   168  N  N   . ARG A 1 25  ? 40.975 -11.603 24.985  1.00 16.99  ?  20  ARG B N   1 
ATOM   169  C  CA  . ARG A 1 25  ? 41.451 -12.923 24.498  1.00 18.02  ?  20  ARG B CA  1 
ATOM   170  C  C   . ARG A 1 25  ? 41.898 -12.826 23.033  1.00 18.12  ?  20  ARG B C   1 
ATOM   171  O  O   . ARG A 1 25  ? 42.868 -13.504 22.668  1.00 19.94  ?  20  ARG B O   1 
ATOM   172  C  CB  . ARG A 1 25  ? 40.386 -14.012 24.682  1.00 20.68  ?  20  ARG B CB  1 
ATOM   173  C  CG  . ARG A 1 25  ? 40.085 -14.343 26.142  1.00 23.88  ?  20  ARG B CG  1 
ATOM   174  C  CD  . ARG A 1 25  ? 39.212 -15.575 26.163  1.00 24.77  ?  20  ARG B CD  1 
ATOM   175  N  NE  . ARG A 1 25  ? 38.494 -15.819 27.399  1.00 25.32  ?  20  ARG B NE  1 
ATOM   176  C  CZ  . ARG A 1 25  ? 38.990 -16.408 28.462  1.00 26.35  ?  20  ARG B CZ  1 
ATOM   177  N  NH1 . ARG A 1 25  ? 40.256 -16.773 28.492  1.00 28.91  ?  20  ARG B NH1 1 
ATOM   178  N  NH2 . ARG A 1 25  ? 38.228 -16.592 29.525  1.00 27.90  ?  20  ARG B NH2 1 
ATOM   179  N  N   . GLY A 1 26  ? 41.202 -12.050 22.214  1.00 17.09  ?  21  GLY B N   1 
ATOM   180  C  CA  . GLY A 1 26  ? 41.449 -11.968 20.762  1.00 15.96  ?  21  GLY B CA  1 
ATOM   181  C  C   . GLY A 1 26  ? 42.666 -11.127 20.427  1.00 14.90  ?  21  GLY B C   1 
ATOM   182  O  O   . GLY A 1 26  ? 43.137 -11.252 19.305  1.00 15.58  ?  21  GLY B O   1 
ATOM   183  N  N   . HIS A 1 27  ? 43.103 -10.233 21.337  1.00 14.01  ?  22  HIS B N   1 
ATOM   184  C  CA  . HIS A 1 27  ? 44.099 -9.146  21.081  1.00 14.76  ?  22  HIS B CA  1 
ATOM   185  C  C   . HIS A 1 27  ? 45.030 -8.972  22.272  1.00 14.47  ?  22  HIS B C   1 
ATOM   186  O  O   . HIS A 1 27  ? 45.147 -7.901  22.878  1.00 16.41  ?  22  HIS B O   1 
ATOM   187  C  CB  . HIS A 1 27  ? 43.342 -7.872  20.668  1.00 15.86  ?  22  HIS B CB  1 
ATOM   188  C  CG  . HIS A 1 27  ? 42.367 -8.160  19.590  1.00 14.66  ?  22  HIS B CG  1 
ATOM   189  N  ND1 . HIS A 1 27  ? 42.755 -8.211  18.263  1.00 14.58  ?  22  HIS B ND1 1 
ATOM   190  C  CD2 . HIS A 1 27  ? 41.053 -8.479  19.618  1.00 15.73  ?  22  HIS B CD2 1 
ATOM   191  C  CE1 . HIS A 1 27  ? 41.708 -8.516  17.528  1.00 15.13  ?  22  HIS B CE1 1 
ATOM   192  N  NE2 . HIS A 1 27  ? 40.673 -8.711  18.332  1.00 13.46  ?  22  HIS B NE2 1 
ATOM   193  N  N   . PRO A 1 28  ? 45.765 -10.045 22.607  1.00 14.51  ?  23  PRO B N   1 
ATOM   194  C  CA  . PRO A 1 28  ? 46.588 -10.092 23.817  1.00 15.34  ?  23  PRO B CA  1 
ATOM   195  C  C   . PRO A 1 28  ? 47.788 -9.155  23.857  1.00 14.23  ?  23  PRO B C   1 
ATOM   196  O  O   . PRO A 1 28  ? 48.246 -8.947  24.983  1.00 14.21  ?  23  PRO B O   1 
ATOM   197  C  CB  . PRO A 1 28  ? 47.190 -11.493 23.842  1.00 15.21  ?  23  PRO B CB  1 
ATOM   198  C  CG  . PRO A 1 28  ? 47.121 -11.928 22.414  1.00 15.18  ?  23  PRO B CG  1 
ATOM   199  C  CD  . PRO A 1 28  ? 45.872 -11.278 21.831  1.00 13.68  ?  23  PRO B CD  1 
ATOM   200  N  N   . LEU A 1 29  ? 48.224 -8.636  22.703  1.00 14.10  ?  24  LEU B N   1 
ATOM   201  C  CA  . LEU A 1 29  ? 49.361 -7.694  22.650  1.00 13.26  ?  24  LEU B CA  1 
ATOM   202  C  C   . LEU A 1 29  ? 48.809 -6.293  23.019  1.00 13.97  ?  24  LEU B C   1 
ATOM   203  O  O   . LEU A 1 29  ? 48.462 -5.522  22.150  1.00 13.87  ?  24  LEU B O   1 
ATOM   204  C  CB  . LEU A 1 29  ? 50.113 -7.740  21.328  1.00 15.02  ?  24  LEU B CB  1 
ATOM   205  C  CG  . LEU A 1 29  ? 51.495 -7.052  21.397  1.00 15.22  ?  24  LEU B CG  1 
ATOM   206  C  CD1 . LEU A 1 29  ? 52.475 -7.852  22.268  1.00 15.96  ?  24  LEU B CD1 1 
ATOM   207  C  CD2 . LEU A 1 29  ? 52.091 -6.709  20.030  1.00 13.82  ?  24  LEU B CD2 1 
ATOM   208  N  N   . ALA A 1 30  ? 48.757 -5.998  24.307  1.00 14.41  ?  25  ALA B N   1 
ATOM   209  C  CA  . ALA A 1 30  ? 48.224 -4.748  24.876  1.00 14.90  ?  25  ALA B CA  1 
ATOM   210  C  C   . ALA A 1 30  ? 49.274 -3.659  24.889  1.00 15.27  ?  25  ALA B C   1 
ATOM   211  O  O   . ALA A 1 30  ? 50.531 -3.967  24.896  1.00 16.15  ?  25  ALA B O   1 
ATOM   212  C  CB  . ALA A 1 30  ? 47.721 -4.984  26.276  1.00 15.43  ?  25  ALA B CB  1 
ATOM   213  N  N   . GLN A 1 31  ? 48.793 -2.418  25.006  1.00 14.64  ?  26  GLN B N   1 
ATOM   214  C  CA  . GLN A 1 31  ? 49.707 -1.273  25.276  1.00 14.73  ?  26  GLN B CA  1 
ATOM   215  C  C   . GLN A 1 31  ? 49.602 -0.938  26.762  1.00 14.26  ?  26  GLN B C   1 
ATOM   216  O  O   . GLN A 1 31  ? 48.510 -0.589  27.263  1.00 13.27  ?  26  GLN B O   1 
ATOM   217  C  CB  . GLN A 1 31  ? 49.402 -0.044  24.418  1.00 14.83  ?  26  GLN B CB  1 
ATOM   218  C  CG  . GLN A 1 31  ? 49.623 -0.266  22.936  1.00 15.23  ?  26  GLN B CG  1 
ATOM   219  C  CD  . GLN A 1 31  ? 49.397 1.016   22.157  1.00 14.94  ?  26  GLN B CD  1 
ATOM   220  O  OE1 . GLN A 1 31  ? 49.618 2.104   22.659  1.00 18.06  ?  26  GLN B OE1 1 
ATOM   221  N  NE2 . GLN A 1 31  ? 48.911 0.892   20.933  1.00 16.53  ?  26  GLN B NE2 1 
ATOM   222  N  N   . LEU A 1 32  ? 50.687 -1.160  27.480  1.00 14.75  ?  27  LEU B N   1 
ATOM   223  C  CA  . LEU A 1 32  ? 50.735 -0.935  28.940  1.00 16.11  ?  27  LEU B CA  1 
ATOM   224  C  C   . LEU A 1 32  ? 51.256 0.483   29.154  1.00 15.49  ?  27  LEU B C   1 
ATOM   225  O  O   . LEU A 1 32  ? 52.333 0.744   28.678  1.00 16.29  ?  27  LEU B O   1 
ATOM   226  C  CB  . LEU A 1 32  ? 51.686 -1.942  29.594  1.00 16.00  ?  27  LEU B CB  1 
ATOM   227  C  CG  . LEU A 1 32  ? 51.864 -1.770  31.093  1.00 16.60  ?  27  LEU B CG  1 
ATOM   228  C  CD1 . LEU A 1 32  ? 50.570 -2.085  31.826  1.00 16.16  ?  27  LEU B CD1 1 
ATOM   229  C  CD2 . LEU A 1 32  ? 52.999 -2.653  31.605  1.00 16.37  ?  27  LEU B CD2 1 
ATOM   230  N  N   . ALA A 1 33  ? 50.527 1.313   29.895  1.00 15.20  ?  28  ALA B N   1 
ATOM   231  C  CA  . ALA A 1 33  ? 50.884 2.725   30.121  1.00 15.21  ?  28  ALA B CA  1 
ATOM   232  C  C   . ALA A 1 33  ? 50.981 2.981   31.627  1.00 15.30  ?  28  ALA B C   1 
ATOM   233  O  O   . ALA A 1 33  ? 50.070 2.604   32.371  1.00 16.45  ?  28  ALA B O   1 
ATOM   234  C  CB  . ALA A 1 33  ? 49.894 3.675   29.457  1.00 14.96  ?  28  ALA B CB  1 
ATOM   235  N  N   . SER A 1 34  ? 52.018 3.690   32.033  1.00 15.77  ?  29  SER B N   1 
ATOM   236  C  CA  . SER A 1 34  ? 52.119 4.265   33.392  1.00 18.35  ?  29  SER B CA  1 
ATOM   237  C  C   . SER A 1 34  ? 52.702 5.669   33.265  1.00 18.17  ?  29  SER B C   1 
ATOM   238  O  O   . SER A 1 34  ? 53.297 5.984   32.227  1.00 17.66  ?  29  SER B O   1 
ATOM   239  C  CB  . SER A 1 34  ? 52.961 3.399   34.266  1.00 19.30  ?  29  SER B CB  1 
ATOM   240  O  OG  . SER A 1 34  ? 54.278 3.334   33.746  1.00 17.35  ?  29  SER B OG  1 
ATOM   241  N  N   . ASN A 1 35  ? 52.529 6.459   34.318  1.00 17.89  ?  30  ASN B N   1 
ATOM   242  C  CA  . ASN A 1 35  ? 52.909 7.881   34.365  1.00 17.90  ?  30  ASN B CA  1 
ATOM   243  C  C   . ASN A 1 35  ? 54.421 7.991   34.158  1.00 17.93  ?  30  ASN B C   1 
ATOM   244  O  O   . ASN A 1 35  ? 55.184 7.185   34.735  1.00 17.46  ?  30  ASN B O   1 
ATOM   245  C  CB  . ASN A 1 35  ? 52.502 8.548   35.669  1.00 16.82  ?  30  ASN B CB  1 
ATOM   246  C  CG  . ASN A 1 35  ? 51.028 8.783   35.779  1.00 20.22  ?  30  ASN B CG  1 
ATOM   247  O  OD1 . ASN A 1 35  ? 50.303 8.664   34.781  1.00 19.51  ?  30  ASN B OD1 1 
ATOM   248  N  ND2 . ASN A 1 35  ? 50.592 9.174   36.977  1.00 21.23  ?  30  ASN B ND2 1 
ATOM   249  N  N   . GLY A 1 36  ? 54.821 9.013   33.415  1.00 18.82  ?  31  GLY B N   1 
ATOM   250  C  CA  . GLY A 1 36  ? 56.211 9.471   33.365  1.00 20.82  ?  31  GLY B CA  1 
ATOM   251  C  C   . GLY A 1 36  ? 56.558 10.242  34.629  1.00 22.87  ?  31  GLY B C   1 
ATOM   252  O  O   . GLY A 1 36  ? 55.673 10.880  35.196  1.00 23.33  ?  31  GLY B O   1 
ATOM   253  N  N   . ALA A 1 37  ? 57.820 10.183  35.044  1.00 25.31  ?  32  ALA B N   1 
ATOM   254  C  CA  . ALA A 1 37  ? 58.325 10.919  36.229  1.00 27.87  ?  32  ALA B CA  1 
ATOM   255  C  C   . ALA A 1 37  ? 58.412 12.403  35.867  1.00 27.84  ?  32  ALA B C   1 
ATOM   256  O  O   . ALA A 1 37  ? 58.816 12.700  34.695  1.00 26.04  ?  32  ALA B O   1 
ATOM   257  C  CB  . ALA A 1 37  ? 59.659 10.367  36.647  1.00 23.99  ?  32  ALA B CB  1 
ATOM   258  N  N   . GLY A 1 38  ? 57.995 13.260  36.813  1.00 28.80  ?  33  GLY B N   1 
ATOM   259  C  CA  . GLY A 1 38  ? 58.235 14.711  36.824  1.00 33.12  ?  33  GLY B CA  1 
ATOM   260  C  C   . GLY A 1 38  ? 57.658 15.365  35.584  1.00 39.85  ?  33  GLY B C   1 
ATOM   261  O  O   . GLY A 1 38  ? 58.401 16.083  34.882  1.00 39.88  ?  33  GLY B O   1 
ATOM   262  N  N   . GLY A 1 39  ? 56.392 15.065  35.289  1.00 37.43  ?  34  GLY B N   1 
ATOM   263  C  CA  . GLY A 1 39  ? 55.653 15.673  34.169  1.00 42.20  ?  34  GLY B CA  1 
ATOM   264  C  C   . GLY A 1 39  ? 56.013 15.114  32.794  1.00 37.29  ?  34  GLY B C   1 
ATOM   265  O  O   . GLY A 1 39  ? 55.409 15.638  31.834  1.00 39.50  ?  34  GLY B O   1 
ATOM   266  N  N   . ALA A 1 40  ? 56.910 14.114  32.667  1.00 32.24  ?  35  ALA B N   1 
ATOM   267  C  CA  . ALA A 1 40  ? 57.269 13.490  31.361  1.00 28.21  ?  35  ALA B CA  1 
ATOM   268  C  C   . ALA A 1 40  ? 56.038 12.750  30.861  1.00 22.45  ?  35  ALA B C   1 
ATOM   269  O  O   . ALA A 1 40  ? 55.143 12.511  31.691  1.00 22.38  ?  35  ALA B O   1 
ATOM   270  C  CB  . ALA A 1 40  ? 58.454 12.553  31.408  1.00 28.49  ?  35  ALA B CB  1 
ATOM   271  N  N   . ALA A 1 41  ? 55.994 12.434  29.566  1.00 21.26  ?  36  ALA B N   1 
ATOM   272  C  CA  . ALA A 1 41  ? 54.868 11.672  28.971  1.00 19.00  ?  36  ALA B CA  1 
ATOM   273  C  C   . ALA A 1 41  ? 54.896 10.257  29.545  1.00 18.19  ?  36  ALA B C   1 
ATOM   274  O  O   . ALA A 1 41  ? 55.971 9.784   29.967  1.00 17.14  ?  36  ALA B O   1 
ATOM   275  C  CB  . ALA A 1 41  ? 54.919 11.667  27.457  1.00 18.56  ?  36  ALA B CB  1 
ATOM   276  N  N   . PRO A 1 42  ? 53.730 9.570   29.605  1.00 17.79  ?  37  PRO B N   1 
ATOM   277  C  CA  . PRO A 1 42  ? 53.669 8.168   30.021  1.00 16.68  ?  37  PRO B CA  1 
ATOM   278  C  C   . PRO A 1 42  ? 54.677 7.261   29.290  1.00 16.99  ?  37  PRO B C   1 
ATOM   279  O  O   . PRO A 1 42  ? 54.956 7.505   28.132  1.00 15.37  ?  37  PRO B O   1 
ATOM   280  C  CB  . PRO A 1 42  ? 52.223 7.778   29.679  1.00 18.37  ?  37  PRO B CB  1 
ATOM   281  C  CG  . PRO A 1 42  ? 51.456 9.088   29.857  1.00 16.18  ?  37  PRO B CG  1 
ATOM   282  C  CD  . PRO A 1 42  ? 52.387 10.119  29.311  1.00 16.34  ?  37  PRO B CD  1 
ATOM   283  N  N   . HIS A 1 43  ? 55.166 6.229   29.991  1.00 17.15  ?  38  HIS B N   1 
ATOM   284  C  CA  . HIS A 1 43  ? 55.878 5.060   29.424  1.00 19.29  ?  38  HIS B CA  1 
ATOM   285  C  C   . HIS A 1 43  ? 54.824 4.172   28.766  1.00 17.35  ?  38  HIS B C   1 
ATOM   286  O  O   . HIS A 1 43  ? 53.745 4.042   29.357  1.00 18.10  ?  38  HIS B O   1 
ATOM   287  C  CB  . HIS A 1 43  ? 56.589 4.205   30.491  1.00 22.32  ?  38  HIS B CB  1 
ATOM   288  C  CG  . HIS A 1 43  ? 57.549 4.959   31.321  1.00 26.08  ?  38  HIS B CG  1 
ATOM   289  N  ND1 . HIS A 1 43  ? 58.888 4.957   31.051  1.00 32.70  ?  38  HIS B ND1 1 
ATOM   290  C  CD2 . HIS A 1 43  ? 57.375 5.665   32.450  1.00 27.04  ?  38  HIS B CD2 1 
ATOM   291  C  CE1 . HIS A 1 43  ? 59.502 5.673   31.968  1.00 30.32  ?  38  HIS B CE1 1 
ATOM   292  N  NE2 . HIS A 1 43  ? 58.603 6.122   32.821  1.00 27.72  ?  38  HIS B NE2 1 
ATOM   293  N  N   . ILE A 1 44  ? 55.068 3.735   27.538  1.00 15.78  ?  39  ILE B N   1 
ATOM   294  C  CA  . ILE A 1 44  ? 54.142 2.824   26.805  1.00 15.70  ?  39  ILE B CA  1 
ATOM   295  C  C   . ILE A 1 44  ? 54.949 1.620   26.319  1.00 17.08  ?  39  ILE B C   1 
ATOM   296  O  O   . ILE A 1 44  ? 56.003 1.812   25.614  1.00 13.68  ?  39  ILE B O   1 
ATOM   297  C  CB  . ILE A 1 44  ? 53.529 3.557   25.603  1.00 18.07  ?  39  ILE B CB  1 
ATOM   298  C  CG1 . ILE A 1 44  ? 52.861 4.890   25.957  1.00 17.32  ?  39  ILE B CG1 1 
ATOM   299  C  CG2 . ILE A 1 44  ? 52.595 2.591   24.894  1.00 19.32  ?  39  ILE B CG2 1 
ATOM   300  C  CD1 . ILE A 1 44  ? 51.469 4.682   26.480  1.00 16.77  ?  39  ILE B CD1 1 
ATOM   301  N  N   . THR A 1 45  ? 54.530 0.412   26.679  1.00 16.27  ?  40  THR B N   1 
ATOM   302  C  CA  . THR A 1 45  ? 55.197 -0.807  26.185  1.00 16.17  ?  40  THR B CA  1 
ATOM   303  C  C   . THR A 1 45  ? 54.143 -1.766  25.650  1.00 14.85  ?  40  THR B C   1 
ATOM   304  O  O   . THR A 1 45  ? 53.139 -1.909  26.365  1.00 16.13  ?  40  THR B O   1 
ATOM   305  C  CB  . THR A 1 45  ? 56.033 -1.472  27.283  1.00 15.11  ?  40  THR B CB  1 
ATOM   306  O  OG1 . THR A 1 45  ? 57.006 -0.533  27.745  1.00 13.35  ?  40  THR B OG1 1 
ATOM   307  C  CG2 . THR A 1 45  ? 56.714 -2.713  26.750  1.00 18.40  ?  40  THR B CG2 1 
ATOM   308  N  N   . HIS A 1 46  ? 54.362 -2.348  24.451  1.00 16.03  ?  41  HIS B N   1 
ATOM   309  C  CA  . HIS A 1 46  ? 53.514 -3.476  23.959  1.00 15.16  ?  41  HIS B CA  1 
ATOM   310  C  C   . HIS A 1 46  ? 53.896 -4.775  24.658  1.00 14.63  ?  41  HIS B C   1 
ATOM   311  O  O   . HIS A 1 46  ? 55.045 -5.173  24.603  1.00 18.26  ?  41  HIS B O   1 
ATOM   312  C  CB  . HIS A 1 46  ? 53.566 -3.677  22.467  1.00 16.71  ?  41  HIS B CB  1 
ATOM   313  C  CG  . HIS A 1 46  ? 52.778 -2.684  21.681  1.00 19.36  ?  41  HIS B CG  1 
ATOM   314  N  ND1 . HIS A 1 46  ? 53.308 -1.459  21.342  1.00 22.88  ?  41  HIS B ND1 1 
ATOM   315  C  CD2 . HIS A 1 46  ? 51.559 -2.767  21.094  1.00 23.78  ?  41  HIS B CD2 1 
ATOM   316  C  CE1 . HIS A 1 46  ? 52.419 -0.793  20.627  1.00 22.67  ?  41  HIS B CE1 1 
ATOM   317  N  NE2 . HIS A 1 46  ? 51.337 -1.589  20.436  1.00 23.57  ?  41  HIS B NE2 1 
ATOM   318  N  N   . VAL A 1 47  ? 52.963 -5.367  25.370  1.00 13.68  ?  42  VAL B N   1 
ATOM   319  C  CA  . VAL A 1 47  ? 53.218 -6.536  26.261  1.00 15.46  ?  42  VAL B CA  1 
ATOM   320  C  C   . VAL A 1 47  ? 52.093 -7.513  26.063  1.00 13.61  ?  42  VAL B C   1 
ATOM   321  O  O   . VAL A 1 47  ? 50.924 -7.082  25.954  1.00 15.10  ?  42  VAL B O   1 
ATOM   322  C  CB  . VAL A 1 47  ? 53.316 -6.145  27.755  1.00 15.45  ?  42  VAL B CB  1 
ATOM   323  C  CG1 . VAL A 1 47  ? 54.483 -5.224  28.002  1.00 17.68  ?  42  VAL B CG1 1 
ATOM   324  C  CG2 . VAL A 1 47  ? 52.030 -5.496  28.261  1.00 16.50  ?  42  VAL B CG2 1 
ATOM   325  N  N   . PRO A 1 48  ? 52.441 -8.816  26.052  1.00 17.15  ?  43  PRO B N   1 
ATOM   326  C  CA  . PRO A 1 48  ? 51.460 -9.890  25.966  1.00 15.83  ?  43  PRO B CA  1 
ATOM   327  C  C   . PRO A 1 48  ? 50.809 -10.107 27.314  1.00 14.81  ?  43  PRO B C   1 
ATOM   328  O  O   . PRO A 1 48  ? 51.511 -10.339 28.352  1.00 16.55  ?  43  PRO B O   1 
ATOM   329  C  CB  . PRO A 1 48  ? 52.285 -11.119 25.553  1.00 16.83  ?  43  PRO B CB  1 
ATOM   330  C  CG  . PRO A 1 48  ? 53.625 -10.861 26.190  1.00 17.36  ?  43  PRO B CG  1 
ATOM   331  C  CD  . PRO A 1 48  ? 53.802 -9.362  26.125  1.00 15.88  ?  43  PRO B CD  1 
ATOM   332  N  N   . ILE A 1 49  ? 49.484 -10.106 27.271  1.00 15.37  ?  44  ILE B N   1 
ATOM   333  C  CA  . ILE A 1 49  ? 48.692 -10.186 28.518  1.00 14.24  ?  44  ILE B CA  1 
ATOM   334  C  C   . ILE A 1 49  ? 47.578 -11.212 28.331  1.00 16.01  ?  44  ILE B C   1 
ATOM   335  O  O   . ILE A 1 49  ? 46.842 -11.127 27.312  1.00 14.22  ?  44  ILE B O   1 
ATOM   336  C  CB  . ILE A 1 49  ? 48.137 -8.812  28.954  1.00 13.63  ?  44  ILE B CB  1 
ATOM   337  C  CG1 . ILE A 1 49  ? 49.255 -7.780  29.179  1.00 12.50  ?  44  ILE B CG1 1 
ATOM   338  C  CG2 . ILE A 1 49  ? 47.257 -8.996  30.154  1.00 12.59  ?  44  ILE B CG2 1 
ATOM   339  C  CD1 . ILE A 1 49  ? 48.746 -6.485  29.774  1.00 14.13  ?  44  ILE B CD1 1 
ATOM   340  N  N   . ILE A 1 50  ? 47.375 -12.085 29.334  1.00 14.91  ?  45  ILE B N   1 
ATOM   341  C  CA  . ILE A 1 50  ? 46.285 -13.102 29.265  1.00 15.50  ?  45  ILE B CA  1 
ATOM   342  C  C   . ILE A 1 50  ? 45.445 -13.047 30.528  1.00 15.99  ?  45  ILE B C   1 
ATOM   343  O  O   . ILE A 1 50  ? 45.914 -12.605 31.557  1.00 16.08  ?  45  ILE B O   1 
ATOM   344  C  CB  . ILE A 1 50  ? 46.841 -14.530 29.072  1.00 16.12  ?  45  ILE B CB  1 
ATOM   345  C  CG1 . ILE A 1 50  ? 47.792 -14.973 30.201  1.00 17.74  ?  45  ILE B CG1 1 
ATOM   346  C  CG2 . ILE A 1 50  ? 47.486 -14.668 27.702  1.00 16.83  ?  45  ILE B CG2 1 
ATOM   347  C  CD1 . ILE A 1 50  ? 47.916 -16.499 30.316  1.00 18.52  ?  45  ILE B CD1 1 
ATOM   348  N  N   . VAL A 1 51  ? 44.249 -13.593 30.441  1.00 19.48  ?  46  VAL B N   1 
ATOM   349  C  CA  . VAL A 1 51  ? 43.416 -13.871 31.634  1.00 18.58  ?  46  VAL B CA  1 
ATOM   350  C  C   . VAL A 1 51  ? 44.085 -14.950 32.490  1.00 17.58  ?  46  VAL B C   1 
ATOM   351  O  O   . VAL A 1 51  ? 44.560 -15.936 31.981  1.00 19.21  ?  46  VAL B O   1 
ATOM   352  C  CB  . VAL A 1 51  ? 42.006 -14.278 31.175  1.00 21.58  ?  46  VAL B CB  1 
ATOM   353  C  CG1 . VAL A 1 51  ? 41.173 -14.842 32.302  1.00 23.60  ?  46  VAL B CG1 1 
ATOM   354  C  CG2 . VAL A 1 51  ? 41.294 -13.124 30.484  1.00 21.49  ?  46  VAL B CG2 1 
ATOM   355  N  N   . ASP A 1 52  ? 44.021 -14.788 33.802  1.00 19.18  ?  47  ASP B N   1 
ATOM   356  C  CA  . ASP A 1 52  ? 44.358 -15.801 34.825  1.00 21.13  ?  47  ASP B CA  1 
ATOM   357  C  C   . ASP A 1 52  ? 43.988 -17.172 34.302  1.00 17.99  ?  47  ASP B C   1 
ATOM   358  O  O   . ASP A 1 52  ? 42.826 -17.457 34.091  1.00 21.90  ?  47  ASP B O   1 
ATOM   359  C  CB  . ASP A 1 52  ? 43.699 -15.449 36.150  1.00 22.06  ?  47  ASP B CB  1 
ATOM   360  C  CG  . ASP A 1 52  ? 43.911 -16.444 37.268  1.00 23.66  ?  47  ASP B CG  1 
ATOM   361  O  OD1 . ASP A 1 52  ? 44.738 -17.403 37.093  1.00 21.98  ?  47  ASP B OD1 1 
ATOM   362  O  OD2 . ASP A 1 52  ? 43.303 -16.191 38.349  1.00 22.30  -1 47  ASP B OD2 1 
ATOM   363  N  N   . PRO A 1 53  ? 44.991 -18.016 33.999  1.00 20.33  ?  48  PRO B N   1 
ATOM   364  C  CA  . PRO A 1 53  ? 44.752 -19.365 33.474  1.00 20.31  ?  48  PRO B CA  1 
ATOM   365  C  C   . PRO A 1 53  ? 44.133 -20.336 34.478  1.00 21.95  ?  48  PRO B C   1 
ATOM   366  O  O   . PRO A 1 53  ? 43.682 -21.379 34.061  1.00 22.52  ?  48  PRO B O   1 
ATOM   367  C  CB  . PRO A 1 53  ? 46.160 -19.881 33.160  1.00 22.41  ?  48  PRO B CB  1 
ATOM   368  C  CG  . PRO A 1 53  ? 47.052 -19.110 34.087  1.00 20.49  ?  48  PRO B CG  1 
ATOM   369  C  CD  . PRO A 1 53  ? 46.435 -17.728 34.154  1.00 20.74  ?  48  PRO B CD  1 
ATOM   370  N  N   . GLU A 1 54  ? 44.191 -19.990 35.764  1.00 23.74  ?  49  GLU B N   1 
ATOM   371  C  CA  . GLU A 1 54  ? 43.601 -20.782 36.882  1.00 23.13  ?  49  GLU B CA  1 
ATOM   372  C  C   . GLU A 1 54  ? 42.084 -20.534 36.987  1.00 26.22  ?  49  GLU B C   1 
ATOM   373  O  O   . GLU A 1 54  ? 41.438 -21.234 37.785  1.00 25.41  ?  49  GLU B O   1 
ATOM   374  C  CB  . GLU A 1 54  ? 44.331 -20.479 38.190  1.00 23.43  ?  49  GLU B CB  1 
ATOM   375  C  CG  . GLU A 1 54  ? 45.821 -20.764 38.089  1.00 24.81  ?  49  GLU B CG  1 
ATOM   376  C  CD  . GLU A 1 54  ? 46.225 -22.139 37.568  1.00 26.10  ?  49  GLU B CD  1 
ATOM   377  O  OE1 . GLU A 1 54  ? 47.133 -22.205 36.714  1.00 25.61  ?  49  GLU B OE1 1 
ATOM   378  O  OE2 . GLU A 1 54  ? 45.637 -23.164 38.027  1.00 32.30  -1 49  GLU B OE2 1 
ATOM   379  N  N   . LEU A 1 55  ? 41.496 -19.621 36.213  1.00 26.15  ?  50  LEU B N   1 
ATOM   380  C  CA  . LEU A 1 55  ? 40.053 -19.351 36.326  1.00 30.24  ?  50  LEU B CA  1 
ATOM   381  C  C   . LEU A 1 55  ? 39.265 -20.507 35.709  1.00 35.96  ?  50  LEU B C   1 
ATOM   382  O  O   . LEU A 1 55  ? 39.541 -20.871 34.543  1.00 39.04  ?  50  LEU B O   1 
ATOM   383  C  CB  . LEU A 1 55  ? 39.720 -18.036 35.627  1.00 31.83  ?  50  LEU B CB  1 
ATOM   384  C  CG  . LEU A 1 55  ? 40.000 -16.778 36.437  1.00 30.51  ?  50  LEU B CG  1 
ATOM   385  C  CD1 . LEU A 1 55  ? 39.326 -15.587 35.770  1.00 31.09  ?  50  LEU B CD1 1 
ATOM   386  C  CD2 . LEU A 1 55  ? 39.535 -16.919 37.887  1.00 32.14  ?  50  LEU B CD2 1 
ATOM   387  N  N   . ASP A 1 56  ? 38.342 -21.068 36.485  1.00 37.74  ?  51  ASP B N   1 
ATOM   388  C  CA  . ASP A 1 56  ? 37.245 -21.935 35.986  1.00 47.62  ?  51  ASP B CA  1 
ATOM   389  C  C   . ASP A 1 56  ? 35.946 -21.118 35.958  1.00 52.00  ?  51  ASP B C   1 
ATOM   390  O  O   . ASP A 1 56  ? 35.916 -19.978 36.489  1.00 53.76  ?  51  ASP B O   1 
ATOM   391  C  CB  . ASP A 1 56  ? 37.069 -23.182 36.859  1.00 47.85  ?  51  ASP B CB  1 
ATOM   392  C  CG  . ASP A 1 56  ? 38.350 -23.978 37.015  1.00 49.42  ?  51  ASP B CG  1 
ATOM   393  O  OD1 . ASP A 1 56  ? 38.995 -23.847 38.086  1.00 51.29  ?  51  ASP B OD1 1 
ATOM   394  O  OD2 . ASP A 1 56  ? 38.698 -24.712 36.063  1.00 44.06  -1 51  ASP B OD2 1 
ATOM   395  N  N   . GLY A 1 57  ? 34.907 -21.714 35.387  1.00 54.23  ?  52  GLY B N   1 
ATOM   396  C  CA  . GLY A 1 57  ? 33.614 -21.067 35.126  1.00 55.16  ?  52  GLY B CA  1 
ATOM   397  C  C   . GLY A 1 57  ? 33.719 -20.188 33.888  1.00 56.78  ?  52  GLY B C   1 
ATOM   398  O  O   . GLY A 1 57  ? 34.828 -19.917 33.416  1.00 56.00  ?  52  GLY B O   1 
ATOM   399  N  N   . PRO A 1 58  ? 32.571 -19.738 33.332  1.00 54.61  ?  53  PRO B N   1 
ATOM   400  C  CA  . PRO A 1 58  ? 32.584 -18.767 32.245  1.00 48.20  ?  53  PRO B CA  1 
ATOM   401  C  C   . PRO A 1 58  ? 33.126 -17.474 32.861  1.00 41.16  ?  53  PRO B C   1 
ATOM   402  O  O   . PRO A 1 58  ? 32.774 -17.176 33.986  1.00 41.89  ?  53  PRO B O   1 
ATOM   403  C  CB  . PRO A 1 58  ? 31.115 -18.663 31.813  1.00 53.15  ?  53  PRO B CB  1 
ATOM   404  C  CG  . PRO A 1 58  ? 30.346 -19.031 33.072  1.00 54.59  ?  53  PRO B CG  1 
ATOM   405  C  CD  . PRO A 1 58  ? 31.205 -20.076 33.763  1.00 53.86  ?  53  PRO B CD  1 
ATOM   406  N  N   . VAL A 1 59  ? 34.008 -16.787 32.142  1.00 34.96  ?  54  VAL B N   1 
ATOM   407  C  CA  . VAL A 1 59  ? 34.519 -15.452 32.540  1.00 31.77  ?  54  VAL B CA  1 
ATOM   408  C  C   . VAL A 1 59  ? 33.674 -14.431 31.791  1.00 28.23  ?  54  VAL B C   1 
ATOM   409  O  O   . VAL A 1 59  ? 33.851 -14.292 30.584  1.00 27.24  ?  54  VAL B O   1 
ATOM   410  C  CB  . VAL A 1 59  ? 36.019 -15.296 32.240  1.00 31.85  ?  54  VAL B CB  1 
ATOM   411  C  CG1 . VAL A 1 59  ? 36.574 -14.020 32.839  1.00 30.43  ?  54  VAL B CG1 1 
ATOM   412  C  CG2 . VAL A 1 59  ? 36.803 -16.505 32.730  1.00 34.59  ?  54  VAL B CG2 1 
ATOM   413  N  N   . ASP A 1 60  ? 32.782 -13.743 32.492  1.00 28.76  ?  55  ASP B N   1 
ATOM   414  C  CA  . ASP A 1 60  ? 31.850 -12.783 31.852  1.00 30.72  ?  55  ASP B CA  1 
ATOM   415  C  C   . ASP A 1 60  ? 32.323 -11.356 32.097  1.00 28.38  ?  55  ASP B C   1 
ATOM   416  O  O   . ASP A 1 60  ? 31.994 -10.497 31.284  1.00 29.00  ?  55  ASP B O   1 
ATOM   417  C  CB  . ASP A 1 60  ? 30.422 -13.027 32.340  1.00 35.71  ?  55  ASP B CB  1 
ATOM   418  C  CG  . ASP A 1 60  ? 29.907 -14.392 31.923  1.00 40.69  ?  55  ASP B CG  1 
ATOM   419  O  OD1 . ASP A 1 60  ? 30.092 -14.742 30.735  1.00 41.73  ?  55  ASP B OD1 1 
ATOM   420  O  OD2 . ASP A 1 60  ? 29.375 -15.112 32.794  1.00 48.98  -1 55  ASP B OD2 1 
ATOM   421  N  N   . ARG A 1 61  ? 33.091 -11.116 33.156  1.00 27.36  ?  56  ARG B N   1 
ATOM   422  C  CA  . ARG A 1 61  ? 33.454 -9.755  33.617  1.00 28.69  ?  56  ARG B CA  1 
ATOM   423  C  C   . ARG A 1 61  ? 34.962 -9.709  33.811  1.00 24.52  ?  56  ARG B C   1 
ATOM   424  O  O   . ARG A 1 61  ? 35.509 -10.608 34.473  1.00 25.96  ?  56  ARG B O   1 
ATOM   425  C  CB  . ARG A 1 61  ? 32.762 -9.405  34.942  1.00 33.02  ?  56  ARG B CB  1 
ATOM   426  C  CG  . ARG A 1 61  ? 31.316 -8.937  34.800  1.00 40.28  ?  56  ARG B CG  1 
ATOM   427  C  CD  . ARG A 1 61  ? 30.575 -8.963  36.129  1.00 44.24  ?  56  ARG B CD  1 
ATOM   428  N  NE  . ARG A 1 61  ? 30.617 -10.318 36.687  1.00 52.00  ?  56  ARG B NE  1 
ATOM   429  C  CZ  . ARG A 1 61  ? 29.788 -11.318 36.379  1.00 52.85  ?  56  ARG B CZ  1 
ATOM   430  N  NH1 . ARG A 1 61  ? 29.963 -12.509 36.928  1.00 59.57  ?  56  ARG B NH1 1 
ATOM   431  N  NH2 . ARG A 1 61  ? 28.784 -11.140 35.536  1.00 55.71  ?  56  ARG B NH2 1 
ATOM   432  N  N   . LEU A 1 62  ? 35.601 -8.647  33.341  1.00 22.38  ?  57  LEU B N   1 
ATOM   433  C  CA  . LEU A 1 62  ? 37.047 -8.443  33.617  1.00 20.91  ?  57  LEU B CA  1 
ATOM   434  C  C   . LEU A 1 62  ? 37.265 -7.940  35.055  1.00 20.35  ?  57  LEU B C   1 
ATOM   435  O  O   . LEU A 1 62  ? 38.322 -8.307  35.665  1.00 20.81  ?  57  LEU B O   1 
ATOM   436  C  CB  . LEU A 1 62  ? 37.612 -7.454  32.596  1.00 20.62  ?  57  LEU B CB  1 
ATOM   437  C  CG  . LEU A 1 62  ? 37.773 -8.005  31.192  1.00 20.02  ?  57  LEU B CG  1 
ATOM   438  C  CD1 . LEU A 1 62  ? 38.126 -6.903  30.203  1.00 20.35  ?  57  LEU B CD1 1 
ATOM   439  C  CD2 . LEU A 1 62  ? 38.827 -9.095  31.199  1.00 19.96  ?  57  LEU B CD2 1 
ATOM   440  N  N   . VAL A 1 63  ? 36.363 -7.116  35.587  1.00 20.99  ?  58  VAL B N   1 
ATOM   441  C  CA  . VAL A 1 63  ? 36.586 -6.452  36.909  1.00 22.32  ?  58  VAL B CA  1 
ATOM   442  C  C   . VAL A 1 63  ? 36.677 -7.573  37.950  1.00 22.66  ?  58  VAL B C   1 
ATOM   443  O  O   . VAL A 1 63  ? 35.798 -8.417  37.983  1.00 23.58  ?  58  VAL B O   1 
ATOM   444  C  CB  . VAL A 1 63  ? 35.528 -5.394  37.295  1.00 21.85  ?  58  VAL B CB  1 
ATOM   445  C  CG1 . VAL A 1 63  ? 35.622 -5.017  38.774  1.00 21.26  ?  58  VAL B CG1 1 
ATOM   446  C  CG2 . VAL A 1 63  ? 35.620 -4.132  36.447  1.00 23.28  ?  58  VAL B CG2 1 
ATOM   447  N  N   . GLY A 1 64  ? 37.738 -7.576  38.746  1.00 21.85  ?  59  GLY B N   1 
ATOM   448  C  CA  . GLY A 1 64  ? 37.935 -8.540  39.831  1.00 25.10  ?  59  GLY B CA  1 
ATOM   449  C  C   . GLY A 1 64  ? 38.808 -9.702  39.406  1.00 26.38  ?  59  GLY B C   1 
ATOM   450  O  O   . GLY A 1 64  ? 39.233 -10.451 40.289  1.00 29.81  ?  59  GLY B O   1 
ATOM   451  N  N   . ILE A 1 65  ? 39.129 -9.856  38.119  1.00 25.95  ?  60  ILE B N   1 
ATOM   452  C  CA  . ILE A 1 65  ? 40.043 -10.946 37.696  1.00 22.79  ?  60  ILE B CA  1 
ATOM   453  C  C   . ILE A 1 65  ? 41.458 -10.383 37.629  1.00 20.43  ?  60  ILE B C   1 
ATOM   454  O  O   . ILE A 1 65  ? 41.616 -9.135  37.538  1.00 19.94  ?  60  ILE B O   1 
ATOM   455  C  CB  . ILE A 1 65  ? 39.627 -11.660 36.395  1.00 26.56  ?  60  ILE B CB  1 
ATOM   456  C  CG1 . ILE A 1 65  ? 39.977 -10.873 35.137  1.00 23.94  ?  60  ILE B CG1 1 
ATOM   457  C  CG2 . ILE A 1 65  ? 38.169 -12.100 36.407  1.00 26.06  ?  60  ILE B CG2 1 
ATOM   458  C  CD1 . ILE A 1 65  ? 39.524 -11.563 33.868  1.00 28.22  ?  60  ILE B CD1 1 
ATOM   459  N  N   . THR A 1 66  ? 42.433 -11.291 37.739  1.00 19.63  ?  61  THR B N   1 
ATOM   460  C  CA  . THR A 1 66  ? 43.881 -10.985 37.625  1.00 19.14  ?  61  THR B CA  1 
ATOM   461  C  C   . THR A 1 66  ? 44.329 -11.360 36.208  1.00 19.53  ?  61  THR B C   1 
ATOM   462  O  O   . THR A 1 66  ? 44.048 -12.484 35.778  1.00 22.54  ?  61  THR B O   1 
ATOM   463  C  CB  . THR A 1 66  ? 44.713 -11.675 38.705  1.00 21.63  ?  61  THR B CB  1 
ATOM   464  O  OG1 . THR A 1 66  ? 44.195 -11.307 39.989  1.00 22.24  ?  61  THR B OG1 1 
ATOM   465  C  CG2 . THR A 1 66  ? 46.177 -11.317 38.627  1.00 21.87  ?  61  THR B CG2 1 
ATOM   466  N  N   . LEU A 1 67  ? 44.989 -10.430 35.529  1.00 16.73  ?  62  LEU B N   1 
ATOM   467  C  CA  . LEU A 1 67  ? 45.671 -10.644 34.233  1.00 17.62  ?  62  LEU B CA  1 
ATOM   468  C  C   . LEU A 1 67  ? 47.135 -10.942 34.517  1.00 15.49  ?  62  LEU B C   1 
ATOM   469  O  O   . LEU A 1 67  ? 47.689 -10.419 35.518  1.00 17.84  ?  62  LEU B O   1 
ATOM   470  C  CB  . LEU A 1 67  ? 45.507 -9.419  33.329  1.00 17.73  ?  62  LEU B CB  1 
ATOM   471  C  CG  . LEU A 1 67  ? 44.074 -8.931  33.154  1.00 18.67  ?  62  LEU B CG  1 
ATOM   472  C  CD1 . LEU A 1 67  ? 44.073 -7.650  32.322  1.00 19.16  ?  62  LEU B CD1 1 
ATOM   473  C  CD2 . LEU A 1 67  ? 43.199 -10.003 32.494  1.00 19.37  ?  62  LEU B CD2 1 
ATOM   474  N  N   . TRP A 1 68  ? 47.720 -11.795 33.688  1.00 14.75  ?  63  TRP B N   1 
ATOM   475  C  CA  . TRP A 1 68  ? 49.148 -12.156 33.749  1.00 15.97  ?  63  TRP B CA  1 
ATOM   476  C  C   . TRP A 1 68  ? 49.832 -11.565 32.535  1.00 15.40  ?  63  TRP B C   1 
ATOM   477  O  O   . TRP A 1 68  ? 49.294 -11.650 31.457  1.00 14.66  ?  63  TRP B O   1 
ATOM   478  C  CB  . TRP A 1 68  ? 49.302 -13.678 33.722  1.00 17.42  ?  63  TRP B CB  1 
ATOM   479  C  CG  . TRP A 1 68  ? 48.850 -14.419 34.949  1.00 16.16  ?  63  TRP B CG  1 
ATOM   480  C  CD1 . TRP A 1 68  ? 47.887 -14.095 35.863  1.00 18.78  ?  63  TRP B CD1 1 
ATOM   481  C  CD2 . TRP A 1 68  ? 49.263 -15.760 35.251  1.00 15.99  ?  63  TRP B CD2 1 
ATOM   482  N  NE1 . TRP A 1 68  ? 47.733 -15.129 36.769  1.00 17.74  ?  63  TRP B NE1 1 
ATOM   483  C  CE2 . TRP A 1 68  ? 48.575 -16.159 36.423  1.00 17.19  ?  63  TRP B CE2 1 
ATOM   484  C  CE3 . TRP A 1 68  ? 50.155 -16.660 34.639  1.00 16.72  ?  63  TRP B CE3 1 
ATOM   485  C  CZ2 . TRP A 1 68  ? 48.787 -17.422 36.989  1.00 18.65  ?  63  TRP B CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 68  ? 50.382 -17.899 35.224  1.00 17.29  ?  63  TRP B CZ3 1 
ATOM   487  C  CH2 . TRP A 1 68  ? 49.759 -18.233 36.429  1.00 18.43  ?  63  TRP B CH2 1 
ATOM   488  N  N   . GLY A 1 69  ? 51.062 -11.115 32.682  1.00 14.14  ?  64  GLY B N   1 
ATOM   489  C  CA  . GLY A 1 69  ? 51.800 -10.606 31.527  1.00 14.33  ?  64  GLY B CA  1 
ATOM   490  C  C   . GLY A 1 69  ? 53.280 -10.594 31.794  1.00 14.32  ?  64  GLY B C   1 
ATOM   491  O  O   . GLY A 1 69  ? 53.676 -10.913 32.913  1.00 14.48  ?  64  GLY B O   1 
ATOM   492  N  N   . HIS A 1 70  ? 54.077 -10.297 30.791  1.00 14.07  ?  65  HIS B N   1 
ATOM   493  C  CA  . HIS A 1 70  ? 55.538 -10.122 30.981  1.00 15.72  ?  65  HIS B CA  1 
ATOM   494  C  C   . HIS A 1 70  ? 56.035 -9.013  30.061  1.00 17.14  ?  65  HIS B C   1 
ATOM   495  O  O   . HIS A 1 70  ? 55.318 -8.609  29.106  1.00 17.02  ?  65  HIS B O   1 
ATOM   496  C  CB  . HIS A 1 70  ? 56.329 -11.399 30.774  1.00 16.23  ?  65  HIS B CB  1 
ATOM   497  C  CG  . HIS A 1 70  ? 56.403 -11.955 29.385  1.00 15.31  ?  65  HIS B CG  1 
ATOM   498  N  ND1 . HIS A 1 70  ? 55.356 -12.691 28.812  1.00 15.40  ?  65  HIS B ND1 1 
ATOM   499  C  CD2 . HIS A 1 70  ? 57.455 -12.059 28.552  1.00 17.60  ?  65  HIS B CD2 1 
ATOM   500  C  CE1 . HIS A 1 70  ? 55.724 -13.149 27.640  1.00 16.64  ?  65  HIS B CE1 1 
ATOM   501  N  NE2 . HIS A 1 70  ? 57.072 -12.784 27.440  1.00 16.49  ?  65  HIS B NE2 1 
ATOM   502  N  N   . MET A 1 71  ? 57.257 -8.580  30.334  1.00 17.15  ?  66  MET B N   1 
ATOM   503  C  CA  . MET A 1 71  ? 57.965 -7.571  29.538  1.00 17.85  ?  66  MET B CA  1 
ATOM   504  C  C   . MET A 1 71  ? 59.459 -7.813  29.751  1.00 16.98  ?  66  MET B C   1 
ATOM   505  O  O   . MET A 1 71  ? 59.833 -8.790  30.433  1.00 17.63  ?  66  MET B O   1 
ATOM   506  C  CB  . MET A 1 71  ? 57.548 -6.152  29.943  1.00 19.30  ?  66  MET B CB  1 
ATOM   507  C  CG  . MET A 1 71  ? 58.048 -5.731  31.277  1.00 22.85  ?  66  MET B CG  1 
ATOM   508  S  SD  . MET A 1 71  ? 57.713 -3.942  31.480  1.00 30.41  ?  66  MET B SD  1 
ATOM   509  C  CE  . MET A 1 71  ? 56.183 -4.145  32.338  1.00 25.43  ?  66  MET B CE  1 
ATOM   510  N  N   . ASN A 1 72  ? 60.280 -7.020  29.095  1.00 16.71  ?  67  ASN B N   1 
ATOM   511  C  CA  . ASN A 1 72  ? 61.755 -7.147  29.181  1.00 17.89  ?  67  ASN B CA  1 
ATOM   512  C  C   . ASN A 1 72  ? 62.221 -6.407  30.444  1.00 20.07  ?  67  ASN B C   1 
ATOM   513  O  O   . ASN A 1 72  ? 61.880 -5.237  30.581  1.00 21.08  ?  67  ASN B O   1 
ATOM   514  C  CB  . ASN A 1 72  ? 62.325 -6.647  27.865  1.00 18.14  ?  67  ASN B CB  1 
ATOM   515  C  CG  . ASN A 1 72  ? 63.813 -6.792  27.771  1.00 19.14  ?  67  ASN B CG  1 
ATOM   516  O  OD1 . ASN A 1 72  ? 64.453 -7.303  28.683  1.00 18.91  ?  67  ASN B OD1 1 
ATOM   517  N  ND2 . ASN A 1 72  ? 64.312 -6.433  26.611  1.00 20.55  ?  67  ASN B ND2 1 
ATOM   518  N  N   . ARG A 1 73  ? 63.000 -7.050  31.326  1.00 19.09  ?  68  ARG B N   1 
ATOM   519  C  CA  . ARG A 1 73  ? 63.571 -6.341  32.507  1.00 22.70  ?  68  ARG B CA  1 
ATOM   520  C  C   . ARG A 1 73  ? 64.508 -5.207  32.097  1.00 20.74  ?  68  ARG B C   1 
ATOM   521  O  O   . ARG A 1 73  ? 64.626 -4.254  32.874  1.00 30.03  ?  68  ARG B O   1 
ATOM   522  C  CB  . ARG A 1 73  ? 64.288 -7.346  33.417  1.00 24.87  ?  68  ARG B CB  1 
ATOM   523  C  CG  . ARG A 1 73  ? 63.323 -8.130  34.286  1.00 23.82  ?  68  ARG B CG  1 
ATOM   524  C  CD  . ARG A 1 73  ? 64.065 -9.170  35.131  1.00 25.63  ?  68  ARG B CD  1 
ATOM   525  N  NE  . ARG A 1 73  ? 63.066 -9.815  35.929  1.00 22.81  ?  68  ARG B NE  1 
ATOM   526  C  CZ  . ARG A 1 73  ? 62.832 -9.620  37.203  1.00 26.27  ?  68  ARG B CZ  1 
ATOM   527  N  NH1 . ARG A 1 73  ? 63.596 -8.814  37.931  1.00 27.02  ?  68  ARG B NH1 1 
ATOM   528  N  NH2 . ARG A 1 73  ? 61.842 -10.289 37.770  1.00 27.96  ?  68  ARG B NH2 1 
ATOM   529  N  N   . ALA A 1 74  ? 65.146 -5.328  30.941  1.00 24.24  ?  69  ALA B N   1 
ATOM   530  C  CA  . ALA A 1 74  ? 66.116 -4.377  30.375  1.00 25.16  ?  69  ALA B CA  1 
ATOM   531  C  C   . ALA A 1 74  ? 65.393 -3.106  29.928  1.00 25.99  ?  69  ALA B C   1 
ATOM   532  O  O   . ALA A 1 74  ? 66.096 -2.136  29.611  1.00 25.07  ?  69  ALA B O   1 
ATOM   533  C  CB  . ALA A 1 74  ? 66.858 -5.013  29.226  1.00 28.78  ?  69  ALA B CB  1 
ATOM   534  N  N   . ASN A 1 75  ? 64.067 -3.181  29.763  1.00 23.59  ?  70  ASN B N   1 
ATOM   535  C  CA  . ASN A 1 75  ? 63.198 -2.039  29.377  1.00 22.01  ?  70  ASN B CA  1 
ATOM   536  C  C   . ASN A 1 75  ? 63.114 -1.081  30.575  1.00 18.40  ?  70  ASN B C   1 
ATOM   537  O  O   . ASN A 1 75  ? 62.666 -1.462  31.660  1.00 18.20  ?  70  ASN B O   1 
ATOM   538  C  CB  . ASN A 1 75  ? 61.855 -2.574  28.865  1.00 22.91  ?  70  ASN B CB  1 
ATOM   539  C  CG  . ASN A 1 75  ? 60.925 -1.481  28.398  1.00 25.34  ?  70  ASN B CG  1 
ATOM   540  O  OD1 . ASN A 1 75  ? 61.136 -0.293  28.692  1.00 21.04  ?  70  ASN B OD1 1 
ATOM   541  N  ND2 . ASN A 1 75  ? 59.893 -1.894  27.694  1.00 21.49  ?  70  ASN B ND2 1 
ATOM   542  N  N   . PRO A 1 76  ? 63.502 0.214   30.445  1.00 17.88  ?  71  PRO B N   1 
ATOM   543  C  CA  . PRO A 1 76  ? 63.408 1.172   31.555  1.00 17.43  ?  71  PRO B CA  1 
ATOM   544  C  C   . PRO A 1 76  ? 62.034 1.212   32.217  1.00 19.80  ?  71  PRO B C   1 
ATOM   545  O  O   . PRO A 1 76  ? 61.867 1.570   33.393  1.00 18.74  ?  71  PRO B O   1 
ATOM   546  C  CB  . PRO A 1 76  ? 63.646 2.519   30.888  1.00 19.02  ?  71  PRO B CB  1 
ATOM   547  C  CG  . PRO A 1 76  ? 64.550 2.196   29.713  1.00 21.65  ?  71  PRO B CG  1 
ATOM   548  C  CD  . PRO A 1 76  ? 64.139 0.805   29.262  1.00 21.25  ?  71  PRO B CD  1 
ATOM   549  N  N   . HIS A 1 77  ? 61.033 0.843   31.426  1.00 18.58  ?  72  HIS B N   1 
ATOM   550  C  CA  . HIS A 1 77  ? 59.641 0.844   31.897  1.00 18.48  ?  72  HIS B CA  1 
ATOM   551  C  C   . HIS A 1 77  ? 59.532 -0.120  33.091  1.00 18.78  ?  72  HIS B C   1 
ATOM   552  O  O   . HIS A 1 77  ? 58.840 0.198   34.077  1.00 17.18  ?  72  HIS B O   1 
ATOM   553  C  CB  . HIS A 1 77  ? 58.731 0.442   30.738  1.00 16.72  ?  72  HIS B CB  1 
ATOM   554  C  CG  . HIS A 1 77  ? 57.323 0.752   31.051  1.00 16.71  ?  72  HIS B CG  1 
ATOM   555  N  ND1 . HIS A 1 77  ? 56.308 0.551   30.140  1.00 16.68  ?  72  HIS B ND1 1 
ATOM   556  C  CD2 . HIS A 1 77  ? 56.760 1.252   32.164  1.00 17.99  ?  72  HIS B CD2 1 
ATOM   557  C  CE1 . HIS A 1 77  ? 55.181 0.909   30.696  1.00 16.32  ?  72  HIS B CE1 1 
ATOM   558  N  NE2 . HIS A 1 77  ? 55.440 1.402   31.900  1.00 17.18  ?  72  HIS B NE2 1 
ATOM   559  N  N   . TRP A 1 78  ? 60.263 -1.227  33.051  1.00 18.09  ?  73  TRP B N   1 
ATOM   560  C  CA  . TRP A 1 78  ? 60.267 -2.194  34.183  1.00 19.14  ?  73  TRP B CA  1 
ATOM   561  C  C   . TRP A 1 78  ? 60.722 -1.536  35.509  1.00 21.22  ?  73  TRP B C   1 
ATOM   562  O  O   . TRP A 1 78  ? 59.945 -1.600  36.477  1.00 19.42  ?  73  TRP B O   1 
ATOM   563  C  CB  . TRP A 1 78  ? 61.070 -3.431  33.802  1.00 18.78  ?  73  TRP B CB  1 
ATOM   564  C  CG  . TRP A 1 78  ? 61.180 -4.442  34.892  1.00 20.02  ?  73  TRP B CG  1 
ATOM   565  C  CD1 . TRP A 1 78  ? 62.262 -4.629  35.698  1.00 21.80  ?  73  TRP B CD1 1 
ATOM   566  C  CD2 . TRP A 1 78  ? 60.163 -5.358  35.348  1.00 20.72  ?  73  TRP B CD2 1 
ATOM   567  N  NE1 . TRP A 1 78  ? 61.982 -5.580  36.632  1.00 20.71  ?  73  TRP B NE1 1 
ATOM   568  C  CE2 . TRP A 1 78  ? 60.715 -6.062  36.433  1.00 21.17  ?  73  TRP B CE2 1 
ATOM   569  C  CE3 . TRP A 1 78  ? 58.855 -5.685  34.940  1.00 20.48  ?  73  TRP B CE3 1 
ATOM   570  C  CZ2 . TRP A 1 78  ? 60.023 -7.091  37.073  1.00 20.81  ?  73  TRP B CZ2 1 
ATOM   571  C  CZ3 . TRP A 1 78  ? 58.160 -6.671  35.590  1.00 18.15  ?  73  TRP B CZ3 1 
ATOM   572  C  CH2 . TRP A 1 78  ? 58.743 -7.379  36.634  1.00 20.97  ?  73  TRP B CH2 1 
ATOM   573  N  N   . ALA A 1 79  ? 61.911 -0.902  35.561  1.00 22.56  ?  74  ALA B N   1 
ATOM   574  C  CA  . ALA A 1 79  ? 62.395 -0.151  36.743  1.00 24.69  ?  74  ALA B CA  1 
ATOM   575  C  C   . ALA A 1 79  ? 61.423 0.995   37.099  1.00 26.30  ?  74  ALA B C   1 
ATOM   576  O  O   . ALA A 1 79  ? 61.228 1.233   38.307  1.00 26.10  ?  74  ALA B O   1 
ATOM   577  C  CB  . ALA A 1 79  ? 63.814 0.347   36.511  1.00 25.17  ?  74  ALA B CB  1 
ATOM   578  N  N   . ALA A 1 80  ? 60.799 1.645   36.099  1.00 23.71  ?  75  ALA B N   1 
ATOM   579  C  CA  . ALA A 1 80  ? 59.909 2.826   36.257  1.00 23.85  ?  75  ALA B CA  1 
ATOM   580  C  C   . ALA A 1 80  ? 58.648 2.420   37.027  1.00 25.56  ?  75  ALA B C   1 
ATOM   581  O  O   . ALA A 1 80  ? 58.057 3.260   37.738  1.00 28.85  ?  75  ALA B O   1 
ATOM   582  C  CB  . ALA A 1 80  ? 59.545 3.417   34.913  1.00 21.96  ?  75  ALA B CB  1 
ATOM   583  N  N   . LEU A 1 81  ? 58.239 1.158   36.925  1.00 26.07  ?  76  LEU B N   1 
ATOM   584  C  CA  . LEU A 1 81  ? 56.947 0.732   37.524  1.00 27.67  ?  76  LEU B CA  1 
ATOM   585  C  C   . LEU A 1 81  ? 57.068 0.661   39.054  1.00 33.43  ?  76  LEU B C   1 
ATOM   586  O  O   . LEU A 1 81  ? 56.024 0.802   39.752  1.00 35.57  ?  76  LEU B O   1 
ATOM   587  C  CB  . LEU A 1 81  ? 56.563 -0.596  36.883  1.00 25.64  ?  76  LEU B CB  1 
ATOM   588  C  CG  . LEU A 1 81  ? 55.972 -0.436  35.481  1.00 22.67  ?  76  LEU B CG  1 
ATOM   589  C  CD1 . LEU A 1 81  ? 56.012 -1.745  34.756  1.00 23.95  ?  76  LEU B CD1 1 
ATOM   590  C  CD2 . LEU A 1 81  ? 54.544 0.085   35.552  1.00 23.55  ?  76  LEU B CD2 1 
ATOM   591  N  N   . GLY A 1 82  ? 58.292 0.527   39.560  1.00 32.84  ?  77  GLY B N   1 
ATOM   592  C  CA  . GLY A 1 82  ? 58.540 0.547   41.012  1.00 39.39  ?  77  GLY B CA  1 
ATOM   593  C  C   . GLY A 1 82  ? 57.655 -0.475  41.693  1.00 47.94  ?  77  GLY B C   1 
ATOM   594  O  O   . GLY A 1 82  ? 57.546 -1.608  41.153  1.00 56.19  ?  77  GLY B O   1 
ATOM   595  N  N   . GLY A 1 83  ? 56.996 -0.076  42.782  1.00 47.01  ?  78  GLY B N   1 
ATOM   596  C  CA  . GLY A 1 83  ? 56.181 -0.962  43.629  1.00 49.81  ?  78  GLY B CA  1 
ATOM   597  C  C   . GLY A 1 83  ? 54.825 -1.230  43.012  1.00 50.91  ?  78  GLY B C   1 
ATOM   598  O  O   . GLY A 1 83  ? 54.767 -1.989  42.032  1.00 69.00  ?  78  GLY B O   1 
ATOM   599  N  N   . ALA A 1 84  ? 53.774 -0.620  43.565  1.00 51.72  ?  79  ALA B N   1 
ATOM   600  C  CA  . ALA A 1 84  ? 52.358 -0.878  43.216  1.00 47.28  ?  79  ALA B CA  1 
ATOM   601  C  C   . ALA A 1 84  ? 51.846 0.201   42.247  1.00 44.18  ?  79  ALA B C   1 
ATOM   602  O  O   . ALA A 1 84  ? 50.891 0.947   42.613  1.00 50.89  ?  79  ALA B O   1 
ATOM   603  C  CB  . ALA A 1 84  ? 51.533 -0.929  44.476  1.00 48.14  ?  79  ALA B CB  1 
ATOM   604  N  N   . ALA A 1 85  ? 52.428 0.269   41.048  1.00 33.34  ?  80  ALA B N   1 
ATOM   605  C  CA  . ALA A 1 85  ? 52.107 1.300   40.024  1.00 29.28  ?  80  ALA B CA  1 
ATOM   606  C  C   . ALA A 1 85  ? 50.653 1.168   39.533  1.00 25.15  ?  80  ALA B C   1 
ATOM   607  O  O   . ALA A 1 85  ? 50.201 0.071   39.268  1.00 22.91  ?  80  ALA B O   1 
ATOM   608  C  CB  . ALA A 1 85  ? 53.089 1.236   38.891  1.00 27.96  ?  80  ALA B CB  1 
ATOM   609  N  N   . ASN A 1 86  ? 49.949 2.291   39.420  1.00 22.46  ?  81  ASN B N   1 
ATOM   610  C  CA  . ASN A 1 86  ? 48.605 2.331   38.832  1.00 23.42  ?  81  ASN B CA  1 
ATOM   611  C  C   . ASN A 1 86  ? 48.832 2.361   37.333  1.00 22.54  ?  81  ASN B C   1 
ATOM   612  O  O   . ASN A 1 86  ? 49.583 3.245   36.853  1.00 23.38  ?  81  ASN B O   1 
ATOM   613  C  CB  . ASN A 1 86  ? 47.794 3.522   39.348  1.00 25.77  ?  81  ASN B CB  1 
ATOM   614  C  CG  . ASN A 1 86  ? 47.520 3.363   40.822  1.00 29.13  ?  81  ASN B CG  1 
ATOM   615  O  OD1 . ASN A 1 86  ? 47.129 2.282   41.236  1.00 31.86  ?  81  ASN B OD1 1 
ATOM   616  N  ND2 . ASN A 1 86  ? 47.752 4.401   41.612  1.00 27.32  ?  81  ASN B ND2 1 
ATOM   617  N  N   . VAL A 1 87  ? 48.262 1.398   36.618  1.00 20.32  ?  82  VAL B N   1 
ATOM   618  C  CA  . VAL A 1 87  ? 48.549 1.245   35.167  1.00 18.57  ?  82  VAL B CA  1 
ATOM   619  C  C   . VAL A 1 87  ? 47.229 1.161   34.427  1.00 16.10  ?  82  VAL B C   1 
ATOM   620  O  O   . VAL A 1 87  ? 46.203 0.914   35.031  1.00 16.47  ?  82  VAL B O   1 
ATOM   621  C  CB  . VAL A 1 87  ? 49.470 0.054   34.852  1.00 18.24  ?  82  VAL B CB  1 
ATOM   622  C  CG1 . VAL A 1 87  ? 50.772 0.166   35.649  1.00 20.89  ?  82  VAL B CG1 1 
ATOM   623  C  CG2 . VAL A 1 87  ? 48.783 -1.303  35.036  1.00 17.81  ?  82  VAL B CG2 1 
ATOM   624  N  N   . VAL A 1 88  ? 47.307 1.387   33.135  1.00 16.28  ?  83  VAL B N   1 
ATOM   625  C  CA  . VAL A 1 88  ? 46.207 1.076   32.192  1.00 15.81  ?  83  VAL B CA  1 
ATOM   626  C  C   . VAL A 1 88  ? 46.789 0.141   31.159  1.00 15.27  ?  83  VAL B C   1 
ATOM   627  O  O   . VAL A 1 88  ? 47.959 0.364   30.732  1.00 17.03  ?  83  VAL B O   1 
ATOM   628  C  CB  . VAL A 1 88  ? 45.563 2.309   31.544  1.00 16.77  ?  83  VAL B CB  1 
ATOM   629  C  CG1 . VAL A 1 88  ? 46.592 3.206   30.872  1.00 15.85  ?  83  VAL B CG1 1 
ATOM   630  C  CG2 . VAL A 1 88  ? 44.498 1.869   30.553  1.00 17.84  ?  83  VAL B CG2 1 
ATOM   631  N  N   . ALA A 1 89  ? 46.061 -0.911  30.811  1.00 14.87  ?  84  ALA B N   1 
ATOM   632  C  CA  . ALA A 1 89  ? 46.503 -1.717  29.638  1.00 13.55  ?  84  ALA B CA  1 
ATOM   633  C  C   . ALA A 1 89  ? 45.373 -1.644  28.639  1.00 13.60  ?  84  ALA B C   1 
ATOM   634  O  O   . ALA A 1 89  ? 44.207 -1.805  29.089  1.00 15.81  ?  84  ALA B O   1 
ATOM   635  C  CB  . ALA A 1 89  ? 46.859 -3.116  30.034  1.00 14.59  ?  84  ALA B CB  1 
ATOM   636  N  N   . THR A 1 90  ? 45.682 -1.250  27.402  1.00 14.21  ?  85  THR B N   1 
ATOM   637  C  CA  . THR A 1 90  ? 44.684 -1.010  26.325  1.00 12.79  ?  85  THR B CA  1 
ATOM   638  C  C   . THR A 1 90  ? 44.860 -2.106  25.273  1.00 14.87  ?  85  THR B C   1 
ATOM   639  O  O   . THR A 1 90  ? 45.994 -2.358  24.830  1.00 13.55  ?  85  THR B O   1 
ATOM   640  C  CB  . THR A 1 90  ? 44.826 0.350   25.666  1.00 12.77  ?  85  THR B CB  1 
ATOM   641  O  OG1 . THR A 1 90  ? 44.860 1.306   26.736  1.00 15.46  ?  85  THR B OG1 1 
ATOM   642  C  CG2 . THR A 1 90  ? 43.723 0.641   24.657  1.00 14.30  ?  85  THR B CG2 1 
ATOM   643  N  N   . PHE A 1 91  ? 43.762 -2.707  24.904  1.00 13.49  ?  86  PHE B N   1 
ATOM   644  C  CA  . PHE A 1 91  ? 43.665 -3.838  23.966  1.00 15.02  ?  86  PHE B CA  1 
ATOM   645  C  C   . PHE A 1 91  ? 42.863 -3.299  22.793  1.00 15.79  ?  86  PHE B C   1 
ATOM   646  O  O   . PHE A 1 91  ? 41.841 -2.691  23.025  1.00 17.35  ?  86  PHE B O   1 
ATOM   647  C  CB  . PHE A 1 91  ? 42.988 -5.030  24.618  1.00 14.06  ?  86  PHE B CB  1 
ATOM   648  C  CG  . PHE A 1 91  ? 43.641 -5.570  25.853  1.00 13.89  ?  86  PHE B CG  1 
ATOM   649  C  CD1 . PHE A 1 91  ? 43.407 -5.004  27.087  1.00 14.30  ?  86  PHE B CD1 1 
ATOM   650  C  CD2 . PHE A 1 91  ? 44.381 -6.740  25.791  1.00 13.68  ?  86  PHE B CD2 1 
ATOM   651  C  CE1 . PHE A 1 91  ? 44.003 -5.505  28.230  1.00 14.52  ?  86  PHE B CE1 1 
ATOM   652  C  CE2 . PHE A 1 91  ? 44.942 -7.279  26.942  1.00 14.52  ?  86  PHE B CE2 1 
ATOM   653  C  CZ  . PHE A 1 91  ? 44.773 -6.640  28.152  1.00 15.53  ?  86  PHE B CZ  1 
ATOM   654  N  N   . ALA A 1 92  ? 43.395 -3.397  21.591  1.00 14.22  ?  87  ALA B N   1 
ATOM   655  C  CA  . ALA A 1 92  ? 42.851 -2.763  20.371  1.00 16.96  ?  87  ALA B CA  1 
ATOM   656  C  C   . ALA A 1 92  ? 42.371 -3.898  19.463  1.00 16.80  ?  87  ALA B C   1 
ATOM   657  O  O   . ALA A 1 92  ? 43.218 -4.741  19.094  1.00 16.94  ?  87  ALA B O   1 
ATOM   658  C  CB  . ALA A 1 92  ? 43.949 -1.912  19.716  1.00 17.16  ?  87  ALA B CB  1 
ATOM   659  N  N   . GLY A 1 93  ? 41.064 -3.960  19.180  1.00 15.83  ?  88  GLY B N   1 
ATOM   660  C  CA  . GLY A 1 93  ? 40.483 -5.024  18.357  1.00 15.55  ?  88  GLY B CA  1 
ATOM   661  C  C   . GLY A 1 93  ? 40.283 -4.590  16.899  1.00 15.91  ?  88  GLY B C   1 
ATOM   662  O  O   . GLY A 1 93  ? 40.923 -3.656  16.410  1.00 15.15  ?  88  GLY B O   1 
ATOM   663  N  N   . PRO A 1 94  ? 39.314 -5.221  16.204  1.00 15.81  ?  89  PRO B N   1 
ATOM   664  C  CA  . PRO A 1 94  ? 38.988 -4.900  14.817  1.00 16.43  ?  89  PRO B CA  1 
ATOM   665  C  C   . PRO A 1 94  ? 38.631 -3.425  14.655  1.00 14.24  ?  89  PRO B C   1 
ATOM   666  O  O   . PRO A 1 94  ? 38.048 -2.836  15.565  1.00 14.03  ?  89  PRO B O   1 
ATOM   667  C  CB  . PRO A 1 94  ? 37.751 -5.771  14.556  1.00 16.69  ?  89  PRO B CB  1 
ATOM   668  C  CG  . PRO A 1 94  ? 37.970 -6.966  15.455  1.00 15.72  ?  89  PRO B CG  1 
ATOM   669  C  CD  . PRO A 1 94  ? 38.478 -6.311  16.718  1.00 17.74  ?  89  PRO B CD  1 
ATOM   670  N  N   . ASN A 1 95  ? 39.015 -2.859  13.525  1.00 14.14  ?  90  ASN B N   1 
ATOM   671  C  CA  . ASN A 1 95  ? 38.786 -1.423  13.251  1.00 14.78  ?  90  ASN B CA  1 
ATOM   672  C  C   . ASN A 1 95  ? 38.814 -1.214  11.744  1.00 15.35  ?  90  ASN B C   1 
ATOM   673  O  O   . ASN A 1 95  ? 39.509 -1.990  11.052  1.00 15.60  ?  90  ASN B O   1 
ATOM   674  C  CB  . ASN A 1 95  ? 39.793 -0.540  13.988  1.00 14.33  ?  90  ASN B CB  1 
ATOM   675  C  CG  . ASN A 1 95  ? 41.202 -0.661  13.443  1.00 15.03  ?  90  ASN B CG  1 
ATOM   676  O  OD1 . ASN A 1 95  ? 41.582 0.098   12.546  1.00 15.16  ?  90  ASN B OD1 1 
ATOM   677  N  ND2 . ASN A 1 95  ? 41.934 -1.644  13.926  1.00 15.24  ?  90  ASN B ND2 1 
ATOM   678  N  N   . ALA A 1 96  ? 38.143 -0.169  11.269  1.00 14.74  ?  91  ALA B N   1 
ATOM   679  C  CA  . ALA A 1 96  ? 38.136 0.209   9.835   1.00 13.30  ?  91  ALA B CA  1 
ATOM   680  C  C   . ALA A 1 96  ? 37.627 1.633   9.652   1.00 12.76  ?  91  ALA B C   1 
ATOM   681  O  O   . ALA A 1 96  ? 36.569 2.023   10.254  1.00 12.99  ?  91  ALA B O   1 
ATOM   682  C  CB  . ALA A 1 96  ? 37.322 -0.766  9.057   1.00 14.45  ?  91  ALA B CB  1 
ATOM   683  N  N   . TYR A 1 97  ? 38.322 2.400   8.815   1.00 13.34  ?  92  TYR B N   1 
ATOM   684  C  CA  . TYR A 1 97  ? 37.850 3.736   8.349   1.00 13.83  ?  92  TYR B CA  1 
ATOM   685  C  C   . TYR A 1 97  ? 36.488 3.603   7.654   1.00 13.73  ?  92  TYR B C   1 
ATOM   686  O  O   . TYR A 1 97  ? 36.228 2.579   6.928   1.00 13.30  ?  92  TYR B O   1 
ATOM   687  C  CB  . TYR A 1 97  ? 38.825 4.321   7.350   1.00 14.33  ?  92  TYR B CB  1 
ATOM   688  C  CG  . TYR A 1 97  ? 38.399 5.626   6.752   1.00 13.77  ?  92  TYR B CG  1 
ATOM   689  C  CD1 . TYR A 1 97  ? 38.573 6.787   7.492   1.00 15.22  ?  92  TYR B CD1 1 
ATOM   690  C  CD2 . TYR A 1 97  ? 37.924 5.717   5.459   1.00 12.55  ?  92  TYR B CD2 1 
ATOM   691  C  CE1 . TYR A 1 97  ? 38.194 8.016   6.989   1.00 15.96  ?  92  TYR B CE1 1 
ATOM   692  C  CE2 . TYR A 1 97  ? 37.619 6.950   4.913   1.00 16.32  ?  92  TYR B CE2 1 
ATOM   693  C  CZ  . TYR A 1 97  ? 37.736 8.106   5.687   1.00 16.43  ?  92  TYR B CZ  1 
ATOM   694  O  OH  . TYR A 1 97  ? 37.446 9.360   5.249   1.00 14.12  ?  92  TYR B OH  1 
ATOM   695  N  N   . VAL A 1 98  ? 35.631 4.572   7.903   1.00 14.09  ?  93  VAL B N   1 
ATOM   696  C  CA  . VAL A 1 98  ? 34.233 4.584   7.384   1.00 15.95  ?  93  VAL B CA  1 
ATOM   697  C  C   . VAL A 1 98  ? 34.099 5.793   6.440   1.00 15.09  ?  93  VAL B C   1 
ATOM   698  O  O   . VAL A 1 98  ? 34.057 6.978   6.944   1.00 13.17  ?  93  VAL B O   1 
ATOM   699  C  CB  . VAL A 1 98  ? 33.175 4.629   8.505   1.00 14.63  ?  93  VAL B CB  1 
ATOM   700  C  CG1 . VAL A 1 98  ? 31.778 4.645   7.885   1.00 15.74  ?  93  VAL B CG1 1 
ATOM   701  C  CG2 . VAL A 1 98  ? 33.324 3.498   9.516   1.00 13.23  ?  93  VAL B CG2 1 
ATOM   702  N  N   . SER A 1 99  ? 34.045 5.528   5.144   1.00 13.28  ?  94  SER B N   1 
ATOM   703  C  CA  . SER A 1 99  ? 33.867 6.563   4.100   1.00 15.09  ?  94  SER B CA  1 
ATOM   704  C  C   . SER A 1 99  ? 32.382 6.889   4.057   1.00 16.59  ?  94  SER B C   1 
ATOM   705  O  O   . SER A 1 99  ? 31.588 5.952   4.050   1.00 14.83  ?  94  SER B O   1 
ATOM   706  C  CB  . SER A 1 99  ? 34.374 6.137   2.747   1.00 15.20  ?  94  SER B CB  1 
ATOM   707  O  OG  . SER A 1 99  ? 34.076 7.120   1.761   1.00 17.06  ?  94  SER B OG  1 
ATOM   708  N  N   . PRO A 1 100 ? 31.980 8.180   4.065   1.00 16.59  ?  95  PRO B N   1 
ATOM   709  C  CA  . PRO A 1 100 ? 30.608 8.564   3.753   1.00 17.46  ?  95  PRO B CA  1 
ATOM   710  C  C   . PRO A 1 100 ? 30.083 8.103   2.392   1.00 18.88  ?  95  PRO B C   1 
ATOM   711  O  O   . PRO A 1 100 ? 28.867 7.973   2.319   1.00 18.04  ?  95  PRO B O   1 
ATOM   712  C  CB  . PRO A 1 100 ? 30.613 10.088  3.775   1.00 17.26  ?  95  PRO B CB  1 
ATOM   713  C  CG  . PRO A 1 100 ? 31.759 10.367  4.744   1.00 16.51  ?  95  PRO B CG  1 
ATOM   714  C  CD  . PRO A 1 100 ? 32.808 9.365   4.330   1.00 18.09  ?  95  PRO B CD  1 
ATOM   715  N  N   . ALA A 1 101 ? 30.967 7.721   1.460   1.00 18.35  ?  96  ALA B N   1 
ATOM   716  C  CA  . ALA A 1 101 ? 30.595 7.033   0.199   1.00 19.41  ?  96  ALA B CA  1 
ATOM   717  C  C   . ALA A 1 101 ? 29.835 5.748   0.505   1.00 19.78  ?  96  ALA B C   1 
ATOM   718  O  O   . ALA A 1 101 ? 28.963 5.388   -0.286  1.00 25.04  ?  96  ALA B O   1 
ATOM   719  C  CB  . ALA A 1 101 ? 31.810 6.729   -0.644  1.00 21.16  ?  96  ALA B CB  1 
ATOM   720  N  N   . VAL A 1 102 ? 30.101 5.089   1.618   1.00 18.16  ?  97  VAL B N   1 
ATOM   721  C  CA  . VAL A 1 102 ? 29.402 3.826   2.003   1.00 19.70  ?  97  VAL B CA  1 
ATOM   722  C  C   . VAL A 1 102 ? 28.001 4.178   2.482   1.00 21.68  ?  97  VAL B C   1 
ATOM   723  O  O   . VAL A 1 102 ? 27.071 3.375   2.249   1.00 24.89  ?  97  VAL B O   1 
ATOM   724  C  CB  . VAL A 1 102 ? 30.211 3.091   3.083   1.00 19.96  ?  97  VAL B CB  1 
ATOM   725  C  CG1 . VAL A 1 102 ? 29.454 1.912   3.673   1.00 20.93  ?  97  VAL B CG1 1 
ATOM   726  C  CG2 . VAL A 1 102 ? 31.602 2.672   2.569   1.00 19.20  ?  97  VAL B CG2 1 
ATOM   727  N  N   . TYR A 1 103 ? 27.842 5.304   3.194   1.00 21.86  ?  98  TYR B N   1 
ATOM   728  C  CA  . TYR A 1 103 ? 26.543 5.743   3.762   1.00 20.38  ?  98  TYR B CA  1 
ATOM   729  C  C   . TYR A 1 103 ? 25.540 5.995   2.643   1.00 22.17  ?  98  TYR B C   1 
ATOM   730  O  O   . TYR A 1 103 ? 24.318 5.738   2.868   1.00 22.78  ?  98  TYR B O   1 
ATOM   731  C  CB  . TYR A 1 103 ? 26.683 7.052   4.546   1.00 19.11  ?  98  TYR B CB  1 
ATOM   732  C  CG  . TYR A 1 103 ? 27.514 6.999   5.788   1.00 18.70  ?  98  TYR B CG  1 
ATOM   733  C  CD1 . TYR A 1 103 ? 27.768 5.809   6.439   1.00 20.64  ?  98  TYR B CD1 1 
ATOM   734  C  CD2 . TYR A 1 103 ? 27.894 8.166   6.422   1.00 19.02  ?  98  TYR B CD2 1 
ATOM   735  C  CE1 . TYR A 1 103 ? 28.501 5.767   7.613   1.00 21.35  ?  98  TYR B CE1 1 
ATOM   736  C  CE2 . TYR A 1 103 ? 28.638 8.145   7.586   1.00 18.48  ?  98  TYR B CE2 1 
ATOM   737  C  CZ  . TYR A 1 103 ? 28.947 6.947   8.193   1.00 22.38  ?  98  TYR B CZ  1 
ATOM   738  O  OH  . TYR A 1 103 ? 29.661 6.924   9.371   1.00 20.20  ?  98  TYR B OH  1 
ATOM   739  N  N   . ARG A 1 104 ? 26.030 6.613   1.558   1.00 22.48  ?  99  ARG B N   1 
ATOM   740  C  CA  . ARG A 1 104 ? 25.263 7.050   0.357   1.00 27.28  ?  99  ARG B CA  1 
ATOM   741  C  C   . ARG A 1 104 ? 24.267 8.158   0.734   1.00 31.38  ?  99  ARG B C   1 
ATOM   742  O  O   . ARG A 1 104 ? 23.227 8.277   0.044   1.00 35.76  ?  99  ARG B O   1 
ATOM   743  C  CB  . ARG A 1 104 ? 24.539 5.865   -0.292  1.00 29.34  ?  99  ARG B CB  1 
ATOM   744  C  CG  . ARG A 1 104 ? 25.466 4.733   -0.709  1.00 28.53  ?  99  ARG B CG  1 
ATOM   745  C  CD  . ARG A 1 104 ? 24.907 3.914   -1.861  1.00 29.76  ?  99  ARG B CD  1 
ATOM   746  N  NE  . ARG A 1 104 ? 23.523 3.430   -1.750  1.00 30.94  ?  99  ARG B NE  1 
ATOM   747  C  CZ  . ARG A 1 104 ? 23.134 2.306   -1.140  1.00 30.27  ?  99  ARG B CZ  1 
ATOM   748  N  NH1 . ARG A 1 104 ? 24.016 1.514   -0.551  1.00 29.90  ?  99  ARG B NH1 1 
ATOM   749  N  NH2 . ARG A 1 104 ? 21.854 1.950   -1.169  1.00 32.13  ?  99  ARG B NH2 1 
ATOM   750  N  N   . THR A 1 105 ? 24.568 8.911   1.790   1.00 26.80  ?  100 THR B N   1 
ATOM   751  C  CA  . THR A 1 105 ? 23.706 9.948   2.431   1.00 28.37  ?  100 THR B CA  1 
ATOM   752  C  C   . THR A 1 105 ? 24.482 11.257  2.445   1.00 25.74  ?  100 THR B C   1 
ATOM   753  O  O   . THR A 1 105 ? 25.712 11.209  2.322   1.00 24.06  ?  100 THR B O   1 
ATOM   754  C  CB  . THR A 1 105 ? 23.329 9.622   3.887   1.00 29.21  ?  100 THR B CB  1 
ATOM   755  O  OG1 . THR A 1 105 ? 24.481 9.396   4.715   1.00 29.97  ?  100 THR B OG1 1 
ATOM   756  C  CG2 . THR A 1 105 ? 22.392 8.448   3.994   1.00 32.05  ?  100 THR B CG2 1 
ATOM   757  N  N   . ALA A 1 106 ? 23.781 12.374  2.573   1.00 25.52  ?  101 ALA B N   1 
ATOM   758  C  CA  . ALA A 1 106 ? 24.376 13.723  2.661   1.00 25.57  ?  101 ALA B CA  1 
ATOM   759  C  C   . ALA A 1 106 ? 23.456 14.599  3.495   1.00 27.19  ?  101 ALA B C   1 
ATOM   760  O  O   . ALA A 1 106 ? 22.256 14.449  3.383   1.00 27.70  ?  101 ALA B O   1 
ATOM   761  C  CB  . ALA A 1 106 ? 24.557 14.312  1.279   1.00 26.90  ?  101 ALA B CB  1 
ATOM   762  N  N   . PRO A 1 107 ? 23.987 15.486  4.370   1.00 25.16  ?  102 PRO B N   1 
ATOM   763  C  CA  . PRO A 1 107 ? 25.431 15.595  4.571   1.00 23.28  ?  102 PRO B CA  1 
ATOM   764  C  C   . PRO A 1 107 ? 25.950 14.505  5.527   1.00 19.78  ?  102 PRO B C   1 
ATOM   765  O  O   . PRO A 1 107 ? 25.161 13.821  6.190   1.00 19.57  ?  102 PRO B O   1 
ATOM   766  C  CB  . PRO A 1 107 ? 25.540 16.982  5.220   1.00 23.59  ?  102 PRO B CB  1 
ATOM   767  C  CG  . PRO A 1 107 ? 24.338 17.016  6.128   1.00 26.38  ?  102 PRO B CG  1 
ATOM   768  C  CD  . PRO A 1 107 ? 23.243 16.379  5.276   1.00 26.08  ?  102 PRO B CD  1 
ATOM   769  N  N   . ALA A 1 108 ? 27.280 14.408  5.678   1.00 19.25  ?  103 ALA B N   1 
ATOM   770  C  CA  . ALA A 1 108 ? 27.891 13.359  6.528   1.00 18.42  ?  103 ALA B CA  1 
ATOM   771  C  C   . ALA A 1 108 ? 29.298 13.752  6.893   1.00 17.90  ?  103 ALA B C   1 
ATOM   772  O  O   . ALA A 1 108 ? 29.805 14.682  6.257   1.00 15.32  ?  103 ALA B O   1 
ATOM   773  C  CB  . ALA A 1 108 ? 27.924 12.040  5.778   1.00 18.11  ?  103 ALA B CB  1 
ATOM   774  N  N   . ALA A 1 109 ? 29.925 12.973  7.783   1.00 17.94  ?  104 ALA B N   1 
ATOM   775  C  CA  . ALA A 1 109 ? 31.373 13.103  8.077   1.00 18.75  ?  104 ALA B CA  1 
ATOM   776  C  C   . ALA A 1 109 ? 31.971 11.705  8.149   1.00 17.64  ?  104 ALA B C   1 
ATOM   777  O  O   . ALA A 1 109 ? 31.274 10.741  8.458   1.00 19.44  ?  104 ALA B O   1 
ATOM   778  C  CB  . ALA A 1 109 ? 31.588 13.892  9.351   1.00 18.59  ?  104 ALA B CB  1 
ATOM   779  N  N   . PRO A 1 110 ? 33.257 11.511  7.797   1.00 16.44  ?  105 PRO B N   1 
ATOM   780  C  CA  . PRO A 1 110 ? 33.817 10.182  7.881   1.00 16.32  ?  105 PRO B CA  1 
ATOM   781  C  C   . PRO A 1 110 ? 33.977 9.859   9.361   1.00 15.56  ?  105 PRO B C   1 
ATOM   782  O  O   . PRO A 1 110 ? 33.875 10.753  10.194  1.00 15.46  ?  105 PRO B O   1 
ATOM   783  C  CB  . PRO A 1 110 ? 35.178 10.302  7.165   1.00 17.13  ?  105 PRO B CB  1 
ATOM   784  C  CG  . PRO A 1 110 ? 35.052 11.584  6.357   1.00 16.59  ?  105 PRO B CG  1 
ATOM   785  C  CD  . PRO A 1 110 ? 34.186 12.474  7.213   1.00 16.39  ?  105 PRO B CD  1 
ATOM   786  N  N   . THR A 1 111 ? 34.260 8.601   9.684   1.00 15.25  ?  106 THR B N   1 
ATOM   787  C  CA  . THR A 1 111 ? 34.614 8.218   11.053  1.00 15.23  ?  106 THR B CA  1 
ATOM   788  C  C   . THR A 1 111 ? 35.519 7.004   10.947  1.00 16.40  ?  106 THR B C   1 
ATOM   789  O  O   . THR A 1 111 ? 35.868 6.616   9.788   1.00 15.29  ?  106 THR B O   1 
ATOM   790  C  CB  . THR A 1 111 ? 33.370 8.038   11.942  1.00 17.24  ?  106 THR B CB  1 
ATOM   791  O  OG1 . THR A 1 111 ? 33.891 8.113   13.272  1.00 17.47  ?  106 THR B OG1 1 
ATOM   792  C  CG2 . THR A 1 111 ? 32.612 6.726   11.753  1.00 15.27  ?  106 THR B CG2 1 
ATOM   793  N  N   . TRP A 1 112 ? 35.935 6.494   12.103  1.00 16.50  ?  107 TRP B N   1 
ATOM   794  C  CA  . TRP A 1 112 ? 36.730 5.253   12.209  1.00 16.58  ?  107 TRP B CA  1 
ATOM   795  C  C   . TRP A 1 112 ? 35.999 4.330   13.176  1.00 19.30  ?  107 TRP B C   1 
ATOM   796  O  O   . TRP A 1 112 ? 35.800 4.753   14.323  1.00 18.09  ?  107 TRP B O   1 
ATOM   797  C  CB  . TRP A 1 112 ? 38.172 5.545   12.672  1.00 15.34  ?  107 TRP B CB  1 
ATOM   798  C  CG  . TRP A 1 112 ? 39.139 4.519   12.150  1.00 13.57  ?  107 TRP B CG  1 
ATOM   799  C  CD1 . TRP A 1 112 ? 39.236 3.227   12.556  1.00 14.36  ?  107 TRP B CD1 1 
ATOM   800  C  CD2 . TRP A 1 112 ? 40.182 4.699   11.168  1.00 13.73  ?  107 TRP B CD2 1 
ATOM   801  N  NE1 . TRP A 1 112 ? 40.229 2.577   11.865  1.00 13.58  ?  107 TRP B NE1 1 
ATOM   802  C  CE2 . TRP A 1 112 ? 40.816 3.452   11.001  1.00 13.52  ?  107 TRP B CE2 1 
ATOM   803  C  CE3 . TRP A 1 112 ? 40.636 5.789   10.411  1.00 14.39  ?  107 TRP B CE3 1 
ATOM   804  C  CZ2 . TRP A 1 112 ? 41.855 3.272   10.105  1.00 15.99  ?  107 TRP B CZ2 1 
ATOM   805  C  CZ3 . TRP A 1 112 ? 41.652 5.606   9.509   1.00 14.27  ?  107 TRP B CZ3 1 
ATOM   806  C  CH2 . TRP A 1 112 ? 42.264 4.377   9.376   1.00 15.47  ?  107 TRP B CH2 1 
ATOM   807  N  N   . ASN A 1 113 ? 35.491 3.191   12.700  1.00 16.28  ?  108 ASN B N   1 
ATOM   808  C  CA  . ASN A 1 113 ? 34.890 2.171   13.587  1.00 14.44  ?  108 ASN B CA  1 
ATOM   809  C  C   . ASN A 1 113 ? 36.052 1.430   14.241  1.00 14.18  ?  108 ASN B C   1 
ATOM   810  O  O   . ASN A 1 113 ? 37.021 1.080   13.520  1.00 14.95  ?  108 ASN B O   1 
ATOM   811  C  CB  . ASN A 1 113 ? 33.967 1.254   12.794  1.00 15.10  ?  108 ASN B CB  1 
ATOM   812  C  CG  . ASN A 1 113 ? 32.607 1.876   12.535  1.00 15.51  ?  108 ASN B CG  1 
ATOM   813  O  OD1 . ASN A 1 113 ? 32.370 3.025   12.889  1.00 18.04  ?  108 ASN B OD1 1 
ATOM   814  N  ND2 . ASN A 1 113 ? 31.704 1.105   11.965  1.00 14.47  ?  108 ASN B ND2 1 
ATOM   815  N  N   . PHE A 1 114 ? 36.030 1.258   15.547  1.00 13.87  ?  109 PHE B N   1 
ATOM   816  C  CA  . PHE A 1 114 ? 37.114 0.576   16.273  1.00 13.94  ?  109 PHE B CA  1 
ATOM   817  C  C   . PHE A 1 114 ? 36.578 0.006   17.570  1.00 14.53  ?  109 PHE B C   1 
ATOM   818  O  O   . PHE A 1 114 ? 35.502 0.429   18.057  1.00 15.54  ?  109 PHE B O   1 
ATOM   819  C  CB  . PHE A 1 114 ? 38.314 1.502   16.522  1.00 13.82  ?  109 PHE B CB  1 
ATOM   820  C  CG  . PHE A 1 114 ? 38.161 2.547   17.609  1.00 13.86  ?  109 PHE B CG  1 
ATOM   821  C  CD1 . PHE A 1 114 ? 37.539 3.762   17.349  1.00 15.72  ?  109 PHE B CD1 1 
ATOM   822  C  CD2 . PHE A 1 114 ? 38.608 2.305   18.896  1.00 15.48  ?  109 PHE B CD2 1 
ATOM   823  C  CE1 . PHE A 1 114 ? 37.435 4.749   18.318  1.00 17.06  ?  109 PHE B CE1 1 
ATOM   824  C  CE2 . PHE A 1 114 ? 38.492 3.283   19.873  1.00 16.07  ?  109 PHE B CE2 1 
ATOM   825  C  CZ  . PHE A 1 114 ? 37.893 4.496   19.591  1.00 16.06  ?  109 PHE B CZ  1 
ATOM   826  N  N   . THR A 1 115 ? 37.385 -0.872  18.138  1.00 14.52  ?  110 THR B N   1 
ATOM   827  C  CA  . THR A 1 115 ? 37.082 -1.571  19.392  1.00 14.56  ?  110 THR B CA  1 
ATOM   828  C  C   . THR A 1 115 ? 38.296 -1.390  20.288  1.00 15.08  ?  110 THR B C   1 
ATOM   829  O  O   . THR A 1 115 ? 39.459 -1.500  19.817  1.00 15.59  ?  110 THR B O   1 
ATOM   830  C  CB  . THR A 1 115 ? 36.736 -3.039  19.123  1.00 15.36  ?  110 THR B CB  1 
ATOM   831  O  OG1 . THR A 1 115 ? 37.861 -3.552  18.406  1.00 16.69  ?  110 THR B OG1 1 
ATOM   832  C  CG2 . THR A 1 115 ? 35.434 -3.207  18.386  1.00 15.99  ?  110 THR B CG2 1 
ATOM   833  N  N   . SER A 1 116 ? 38.046 -1.132  21.555  1.00 16.33  ?  111 SER B N   1 
ATOM   834  C  CA  . SER A 1 116 ? 39.155 -0.956  22.518  1.00 16.18  ?  111 SER B CA  1 
ATOM   835  C  C   . SER A 1 116 ? 38.672 -1.427  23.878  1.00 15.37  ?  111 SER B C   1 
ATOM   836  O  O   . SER A 1 116 ? 37.490 -1.152  24.202  1.00 15.43  ?  111 SER B O   1 
ATOM   837  C  CB  . SER A 1 116 ? 39.560 0.506   22.588  1.00 19.20  ?  111 SER B CB  1 
ATOM   838  O  OG  . SER A 1 116 ? 40.621 0.660   23.505  1.00 29.43  ?  111 SER B OG  1 
ATOM   839  N  N   . VAL A 1 117 ? 39.567 -2.006  24.671  1.00 13.14  ?  112 VAL B N   1 
ATOM   840  C  CA  . VAL A 1 117 ? 39.259 -2.267  26.091  1.00 13.59  ?  112 VAL B CA  1 
ATOM   841  C  C   . VAL A 1 117 ? 40.398 -1.649  26.874  1.00 12.69  ?  112 VAL B C   1 
ATOM   842  O  O   . VAL A 1 117 ? 41.564 -1.926  26.529  1.00 14.83  ?  112 VAL B O   1 
ATOM   843  C  CB  . VAL A 1 117 ? 39.092 -3.771  26.344  1.00 13.39  ?  112 VAL B CB  1 
ATOM   844  C  CG1 . VAL A 1 117 ? 39.132 -4.134  27.813  1.00 15.76  ?  112 VAL B CG1 1 
ATOM   845  C  CG2 . VAL A 1 117 ? 37.814 -4.286  25.677  1.00 16.06  ?  112 VAL B CG2 1 
ATOM   846  N  N   . GLN A 1 118 ? 40.076 -0.836  27.862  1.00 14.29  ?  113 GLN B N   1 
ATOM   847  C  CA  . GLN A 1 118 ? 41.090 -0.284  28.797  1.00 13.74  ?  113 GLN B CA  1 
ATOM   848  C  C   . GLN A 1 118 ? 40.870 -0.869  30.186  1.00 13.73  ?  113 GLN B C   1 
ATOM   849  O  O   . GLN A 1 118 ? 39.793 -0.672  30.728  1.00 16.13  ?  113 GLN B O   1 
ATOM   850  C  CB  . GLN A 1 118 ? 41.022 1.243   28.823  1.00 15.32  ?  113 GLN B CB  1 
ATOM   851  C  CG  . GLN A 1 118 ? 41.461 1.888   27.505  1.00 13.55  ?  113 GLN B CG  1 
ATOM   852  C  CD  . GLN A 1 118 ? 41.282 3.379   27.485  1.00 16.18  ?  113 GLN B CD  1 
ATOM   853  O  OE1 . GLN A 1 118 ? 41.182 4.001   28.526  1.00 16.76  ?  113 GLN B OE1 1 
ATOM   854  N  NE2 . GLN A 1 118 ? 41.339 3.971   26.304  1.00 18.26  ?  113 GLN B NE2 1 
ATOM   855  N  N   . VAL A 1 119 ? 41.822 -1.606  30.711  1.00 15.72  ?  114 VAL B N   1 
ATOM   856  C  CA  . VAL A 1 119 ? 41.718 -2.148  32.090  1.00 16.96  ?  114 VAL B CA  1 
ATOM   857  C  C   . VAL A 1 119 ? 42.661 -1.316  32.956  1.00 16.29  ?  114 VAL B C   1 
ATOM   858  O  O   . VAL A 1 119 ? 43.766 -1.024  32.528  1.00 16.60  ?  114 VAL B O   1 
ATOM   859  C  CB  . VAL A 1 119 ? 42.024 -3.652  32.192  1.00 18.94  ?  114 VAL B CB  1 
ATOM   860  C  CG1 . VAL A 1 119 ? 41.018 -4.472  31.408  1.00 22.16  ?  114 VAL B CG1 1 
ATOM   861  C  CG2 . VAL A 1 119 ? 43.476 -3.966  31.803  1.00 20.01  ?  114 VAL B CG2 1 
ATOM   862  N  N   . ARG A 1 120 ? 42.248 -1.023  34.166  1.00 17.35  ?  115 ARG B N   1 
ATOM   863  C  CA  . ARG A 1 120 ? 43.067 -0.258  35.129  1.00 17.58  ?  115 ARG B CA  1 
ATOM   864  C  C   . ARG A 1 120 ? 43.162 -1.027  36.432  1.00 18.26  ?  115 ARG B C   1 
ATOM   865  O  O   . ARG A 1 120 ? 42.155 -1.652  36.849  1.00 20.44  ?  115 ARG B O   1 
ATOM   866  C  CB  . ARG A 1 120 ? 42.452 1.126   35.315  1.00 18.72  ?  115 ARG B CB  1 
ATOM   867  C  CG  . ARG A 1 120 ? 42.718 2.060   34.146  1.00 18.60  ?  115 ARG B CG  1 
ATOM   868  C  CD  . ARG A 1 120 ? 42.079 3.424   34.327  1.00 18.68  ?  115 ARG B CD  1 
ATOM   869  N  NE  . ARG A 1 120 ? 42.600 4.333   33.305  1.00 18.83  ?  115 ARG B NE  1 
ATOM   870  C  CZ  . ARG A 1 120 ? 42.225 4.353   32.026  1.00 19.44  ?  115 ARG B CZ  1 
ATOM   871  N  NH1 . ARG A 1 120 ? 41.264 3.558   31.558  1.00 18.50  ?  115 ARG B NH1 1 
ATOM   872  N  NH2 . ARG A 1 120 ? 42.793 5.215   31.218  1.00 20.45  ?  115 ARG B NH2 1 
ATOM   873  N  N   . GLY A 1 121 ? 44.329 -0.957  37.036  1.00 19.53  ?  116 GLY B N   1 
ATOM   874  C  CA  . GLY A 1 121 ? 44.570 -1.499  38.384  1.00 22.15  ?  116 GLY B CA  1 
ATOM   875  C  C   . GLY A 1 121 ? 46.025 -1.364  38.747  1.00 23.36  ?  116 GLY B C   1 
ATOM   876  O  O   . GLY A 1 121 ? 46.760 -0.668  37.997  1.00 22.99  ?  116 GLY B O   1 
ATOM   877  N  N   . GLU A 1 122 ? 46.439 -2.022  39.821  1.00 24.69  ?  117 GLU B N   1 
ATOM   878  C  CA  . GLU A 1 122 ? 47.829 -1.945  40.348  1.00 26.29  ?  117 GLU B CA  1 
ATOM   879  C  C   . GLU A 1 122 ? 48.649 -3.053  39.703  1.00 25.50  ?  117 GLU B C   1 
ATOM   880  O  O   . GLU A 1 122 ? 48.248 -4.210  39.831  1.00 28.44  ?  117 GLU B O   1 
ATOM   881  C  CB  . GLU A 1 122 ? 47.883 -2.192  41.854  1.00 31.95  ?  117 GLU B CB  1 
ATOM   882  C  CG  . GLU A 1 122 ? 47.650 -0.991  42.724  1.00 38.60  ?  117 GLU B CG  1 
ATOM   883  C  CD  . GLU A 1 122 ? 47.813 -1.333  44.208  1.00 46.73  ?  117 GLU B CD  1 
ATOM   884  O  OE1 . GLU A 1 122 ? 48.681 -2.200  44.542  1.00 44.58  ?  117 GLU B OE1 1 
ATOM   885  O  OE2 . GLU A 1 122 ? 47.052 -0.769  45.025  1.00 50.78  -1 117 GLU B OE2 1 
ATOM   886  N  N   . LEU A 1 123 ? 49.759 -2.727  39.042  1.00 22.98  ?  118 LEU B N   1 
ATOM   887  C  CA  . LEU A 1 123 ? 50.646 -3.779  38.516  1.00 24.52  ?  118 LEU B CA  1 
ATOM   888  C  C   . LEU A 1 123 ? 51.491 -4.287  39.679  1.00 25.08  ?  118 LEU B C   1 
ATOM   889  O  O   . LEU A 1 123 ? 52.134 -3.440  40.351  1.00 26.17  ?  118 LEU B O   1 
ATOM   890  C  CB  . LEU A 1 123 ? 51.518 -3.212  37.402  1.00 22.86  ?  118 LEU B CB  1 
ATOM   891  C  CG  . LEU A 1 123 ? 52.381 -4.240  36.671  1.00 23.24  ?  118 LEU B CG  1 
ATOM   892  C  CD1 . LEU A 1 123 ? 52.496 -3.875  35.201  1.00 24.88  ?  118 LEU B CD1 1 
ATOM   893  C  CD2 . LEU A 1 123 ? 53.797 -4.355  37.283  1.00 25.07  ?  118 LEU B CD2 1 
ATOM   894  N  N   . ARG A 1 124 ? 51.446 -5.594  39.937  1.00 22.76  ?  119 ARG B N   1 
ATOM   895  C  CA  . ARG A 1 124 ? 52.296 -6.262  40.955  1.00 25.13  ?  119 ARG B CA  1 
ATOM   896  C  C   . ARG A 1 124 ? 53.337 -7.083  40.202  1.00 22.08  ?  119 ARG B C   1 
ATOM   897  O  O   . ARG A 1 124 ? 52.920 -7.904  39.422  1.00 21.07  ?  119 ARG B O   1 
ATOM   898  C  CB  . ARG A 1 124 ? 51.416 -7.129  41.873  1.00 29.53  ?  119 ARG B CB  1 
ATOM   899  C  CG  . ARG A 1 124 ? 52.188 -8.092  42.767  1.00 38.13  ?  119 ARG B CG  1 
ATOM   900  C  CD  . ARG A 1 124 ? 51.384 -9.138  43.546  1.00 41.90  ?  119 ARG B CD  1 
ATOM   901  N  NE  . ARG A 1 124 ? 50.354 -9.853  42.781  1.00 45.08  ?  119 ARG B NE  1 
ATOM   902  C  CZ  . ARG A 1 124 ? 49.995 -11.126 42.970  1.00 45.90  ?  119 ARG B CZ  1 
ATOM   903  N  NH1 . ARG A 1 124 ? 50.586 -11.866 43.900  1.00 52.74  ?  119 ARG B NH1 1 
ATOM   904  N  NH2 . ARG A 1 124 ? 49.036 -11.661 42.229  1.00 44.44  ?  119 ARG B NH2 1 
ATOM   905  N  N   . LYS A 1 125 ? 54.629 -6.887  40.448  1.00 20.84  ?  120 LYS B N   1 
ATOM   906  C  CA  . LYS A 1 125 ? 55.690 -7.695  39.815  1.00 22.00  ?  120 LYS B CA  1 
ATOM   907  C  C   . LYS A 1 125 ? 55.722 -9.052  40.515  1.00 26.26  ?  120 LYS B C   1 
ATOM   908  O  O   . LYS A 1 125 ? 55.379 -9.121  41.711  1.00 22.71  ?  120 LYS B O   1 
ATOM   909  C  CB  . LYS A 1 125 ? 57.045 -6.998  39.884  1.00 19.76  ?  120 LYS B CB  1 
ATOM   910  C  CG  . LYS A 1 125 ? 57.073 -5.615  39.280  1.00 21.45  ?  120 LYS B CG  1 
ATOM   911  C  CD  . LYS A 1 125 ? 58.378 -4.924  39.472  1.00 23.98  ?  120 LYS B CD  1 
ATOM   912  C  CE  . LYS A 1 125 ? 58.496 -3.714  38.585  1.00 26.05  ?  120 LYS B CE  1 
ATOM   913  N  NZ  . LYS A 1 125 ? 59.650 -2.888  38.967  1.00 27.44  ?  120 LYS B NZ  1 
ATOM   914  N  N   . VAL A 1 126 ? 56.019 -10.085 39.728  1.00 25.04  ?  121 VAL B N   1 
ATOM   915  C  CA  . VAL A 1 126 ? 56.408 -11.442 40.161  1.00 28.80  ?  121 VAL B CA  1 
ATOM   916  C  C   . VAL A 1 126 ? 57.943 -11.482 40.155  1.00 30.60  ?  121 VAL B C   1 
ATOM   917  O  O   . VAL A 1 126 ? 58.526 -11.203 39.095  1.00 32.90  ?  121 VAL B O   1 
ATOM   918  C  CB  . VAL A 1 126 ? 55.810 -12.436 39.152  1.00 34.77  ?  121 VAL B CB  1 
ATOM   919  C  CG1 . VAL A 1 126 ? 56.536 -13.753 39.207  1.00 35.31  ?  121 VAL B CG1 1 
ATOM   920  C  CG2 . VAL A 1 126 ? 54.319 -12.592 39.332  1.00 34.94  ?  121 VAL B CG2 1 
ATOM   921  N  N   . GLU A 1 127 ? 58.609 -11.799 41.262  1.00 28.11  ?  122 GLU B N   1 
ATOM   922  C  CA  . GLU A 1 127 ? 60.089 -11.865 41.217  1.00 31.12  ?  122 GLU B CA  1 
ATOM   923  C  C   . GLU A 1 127 ? 60.588 -13.312 41.147  1.00 36.03  ?  122 GLU B C   1 
ATOM   924  O  O   . GLU A 1 127 ? 61.668 -13.506 40.539  1.00 36.84  ?  122 GLU B O   1 
ATOM   925  C  CB  . GLU A 1 127 ? 60.685 -11.057 42.361  1.00 35.09  ?  122 GLU B CB  1 
ATOM   926  C  CG  . GLU A 1 127 ? 60.369 -9.569  42.260  1.00 35.54  ?  122 GLU B CG  1 
ATOM   927  C  CD  . GLU A 1 127 ? 61.042 -8.814  41.128  1.00 35.84  ?  122 GLU B CD  1 
ATOM   928  O  OE1 . GLU A 1 127 ? 61.832 -9.434  40.372  1.00 38.55  ?  122 GLU B OE1 1 
ATOM   929  O  OE2 . GLU A 1 127 ? 60.776 -7.601  41.009  1.00 39.63  -1 122 GLU B OE2 1 
ATOM   930  N  N   . SER A 1 128 ? 59.864 -14.288 41.701  1.00 30.57  ?  123 SER B N   1 
ATOM   931  C  CA  . SER A 1 128 ? 60.325 -15.695 41.745  1.00 30.40  ?  123 SER B CA  1 
ATOM   932  C  C   . SER A 1 128 ? 60.435 -16.250 40.324  1.00 30.61  ?  123 SER B C   1 
ATOM   933  O  O   . SER A 1 128 ? 59.535 -15.957 39.462  1.00 27.47  ?  123 SER B O   1 
ATOM   934  C  CB  . SER A 1 128 ? 59.425 -16.558 42.568  1.00 35.27  ?  123 SER B CB  1 
ATOM   935  O  OG  . SER A 1 128 ? 58.441 -17.157 41.742  1.00 36.17  ?  123 SER B OG  1 
ATOM   936  N  N   . ALA A 1 129 ? 61.475 -17.052 40.108  1.00 28.26  ?  124 ALA B N   1 
ATOM   937  C  CA  . ALA A 1 129 ? 61.738 -17.770 38.849  1.00 31.73  ?  124 ALA B CA  1 
ATOM   938  C  C   . ALA A 1 129 ? 60.549 -18.711 38.577  1.00 29.16  ?  124 ALA B C   1 
ATOM   939  O  O   . ALA A 1 129 ? 60.188 -18.854 37.397  1.00 25.06  ?  124 ALA B O   1 
ATOM   940  C  CB  . ALA A 1 129 ? 63.064 -18.503 38.919  1.00 32.04  ?  124 ALA B CB  1 
ATOM   941  N  N   . ASP A 1 130 ? 59.924 -19.270 39.615  1.00 26.27  ?  125 ASP B N   1 
ATOM   942  C  CA  . ASP A 1 130 ? 58.888 -20.329 39.418  1.00 29.81  ?  125 ASP B CA  1 
ATOM   943  C  C   . ASP A 1 130 ? 57.621 -19.617 38.904  1.00 26.06  ?  125 ASP B C   1 
ATOM   944  O  O   . ASP A 1 130 ? 56.978 -20.155 37.961  1.00 23.66  ?  125 ASP B O   1 
ATOM   945  C  CB  . ASP A 1 130 ? 58.723 -21.241 40.652  1.00 37.55  ?  125 ASP B CB  1 
ATOM   946  C  CG  . ASP A 1 130 ? 59.714 -22.422 40.740  1.00 48.22  ?  125 ASP B CG  1 
ATOM   947  O  OD1 . ASP A 1 130 ? 59.356 -23.490 41.403  1.00 43.93  ?  125 ASP B OD1 1 
ATOM   948  O  OD2 . ASP A 1 130 ? 60.861 -22.303 40.159  1.00 50.77  -1 125 ASP B OD2 1 
ATOM   949  N  N   . ASP A 1 131 ? 57.309 -18.418 39.407  1.00 22.99  ?  126 ASP B N   1 
ATOM   950  C  CA  . ASP A 1 131 ? 56.160 -17.614 38.905  1.00 25.59  ?  126 ASP B CA  1 
ATOM   951  C  C   . ASP A 1 131 ? 56.437 -16.925 37.561  1.00 21.52  ?  126 ASP B C   1 
ATOM   952  O  O   . ASP A 1 131 ? 55.440 -16.700 36.799  1.00 21.73  ?  126 ASP B O   1 
ATOM   953  C  CB  . ASP A 1 131 ? 55.738 -16.542 39.900  1.00 28.17  ?  126 ASP B CB  1 
ATOM   954  C  CG  . ASP A 1 131 ? 55.269 -17.077 41.227  1.00 30.72  ?  126 ASP B CG  1 
ATOM   955  O  OD1 . ASP A 1 131 ? 54.814 -18.246 41.260  1.00 32.42  ?  126 ASP B OD1 1 
ATOM   956  O  OD2 . ASP A 1 131 ? 55.393 -16.312 42.209  1.00 28.91  -1 126 ASP B OD2 1 
ATOM   957  N  N   . THR A 1 132 ? 57.686 -16.572 37.263  1.00 19.59  ?  127 THR B N   1 
ATOM   958  C  CA  . THR A 1 132 ? 58.122 -16.081 35.940  1.00 17.20  ?  127 THR B CA  1 
ATOM   959  C  C   . THR A 1 132 ? 57.915 -17.199 34.929  1.00 18.95  ?  127 THR B C   1 
ATOM   960  O  O   . THR A 1 132 ? 57.241 -16.982 33.893  1.00 19.09  ?  127 THR B O   1 
ATOM   961  C  CB  . THR A 1 132 ? 59.588 -15.602 35.986  1.00 18.81  ?  127 THR B CB  1 
ATOM   962  O  OG1 . THR A 1 132 ? 59.656 -14.565 36.963  1.00 17.90  ?  127 THR B OG1 1 
ATOM   963  C  CG2 . THR A 1 132 ? 60.060 -15.097 34.640  1.00 20.23  ?  127 THR B CG2 1 
ATOM   964  N  N   . LEU A 1 133 ? 58.396 -18.401 35.252  1.00 15.90  ?  128 LEU B N   1 
ATOM   965  C  CA  . LEU A 1 133 ? 58.275 -19.554 34.335  1.00 17.02  ?  128 LEU B CA  1 
ATOM   966  C  C   . LEU A 1 133 ? 56.790 -19.858 34.118  1.00 16.87  ?  128 LEU B C   1 
ATOM   967  O  O   . LEU A 1 133 ? 56.401 -20.010 32.984  1.00 17.22  ?  128 LEU B O   1 
ATOM   968  C  CB  . LEU A 1 133 ? 59.019 -20.753 34.925  1.00 18.01  ?  128 LEU B CB  1 
ATOM   969  C  CG  . LEU A 1 133 ? 59.033 -21.986 34.047  1.00 17.43  ?  128 LEU B CG  1 
ATOM   970  C  CD1 . LEU A 1 133 ? 59.803 -21.762 32.764  1.00 16.13  ?  128 LEU B CD1 1 
ATOM   971  C  CD2 . LEU A 1 133 ? 59.571 -23.185 34.797  1.00 17.94  ?  128 LEU B CD2 1 
ATOM   972  N  N   . ALA A 1 134 ? 55.985 -19.925 35.156  1.00 15.41  ?  129 ALA B N   1 
ATOM   973  C  CA  . ALA A 1 134 ? 54.527 -20.150 34.989  1.00 18.51  ?  129 ALA B CA  1 
ATOM   974  C  C   . ALA A 1 134 ? 53.962 -19.125 34.001  1.00 19.00  ?  129 ALA B C   1 
ATOM   975  O  O   . ALA A 1 134 ? 53.077 -19.513 33.197  1.00 19.53  ?  129 ALA B O   1 
ATOM   976  C  CB  . ALA A 1 134 ? 53.760 -20.041 36.267  1.00 18.64  ?  129 ALA B CB  1 
ATOM   977  N  N   . THR A 1 135 ? 54.333 -17.849 34.169  1.00 16.73  ?  130 THR B N   1 
ATOM   978  C  CA  . THR A 1 135 ? 53.772 -16.769 33.338  1.00 16.10  ?  130 THR B CA  1 
ATOM   979  C  C   . THR A 1 135 ? 54.039 -17.099 31.869  1.00 15.99  ?  130 THR B C   1 
ATOM   980  O  O   . THR A 1 135 ? 53.046 -17.057 31.087  1.00 16.38  ?  130 THR B O   1 
ATOM   981  C  CB  . THR A 1 135 ? 54.270 -15.373 33.681  1.00 14.81  ?  130 THR B CB  1 
ATOM   982  O  OG1 . THR A 1 135 ? 54.040 -15.206 35.072  1.00 16.17  ?  130 THR B OG1 1 
ATOM   983  C  CG2 . THR A 1 135 ? 53.545 -14.311 32.869  1.00 16.44  ?  130 THR B CG2 1 
ATOM   984  N  N   . VAL A 1 136 ? 55.279 -17.390 31.472  1.00 16.70  ?  131 VAL B N   1 
ATOM   985  C  CA  . VAL A 1 136 ? 55.594 -17.571 30.018  1.00 16.21  ?  131 VAL B CA  1 
ATOM   986  C  C   . VAL A 1 136 ? 54.984 -18.882 29.483  1.00 16.47  ?  131 VAL B C   1 
ATOM   987  O  O   . VAL A 1 136 ? 54.434 -18.838 28.358  1.00 15.91  ?  131 VAL B O   1 
ATOM   988  C  CB  . VAL A 1 136 ? 57.098 -17.458 29.672  1.00 17.75  ?  131 VAL B CB  1 
ATOM   989  C  CG1 . VAL A 1 136 ? 57.693 -16.111 30.015  1.00 17.55  ?  131 VAL B CG1 1 
ATOM   990  C  CG2 . VAL A 1 136 ? 57.900 -18.572 30.276  1.00 17.90  ?  131 VAL B CG2 1 
ATOM   991  N  N   . ARG A 1 137 ? 55.002 -19.988 30.257  1.00 16.41  ?  132 ARG B N   1 
ATOM   992  C  CA  . ARG A 1 137 ? 54.328 -21.264 29.874  1.00 16.01  ?  132 ARG B CA  1 
ATOM   993  C  C   . ARG A 1 137 ? 52.813 -21.049 29.687  1.00 16.20  ?  132 ARG B C   1 
ATOM   994  O  O   . ARG A 1 137 ? 52.292 -21.585 28.742  1.00 16.48  ?  132 ARG B O   1 
ATOM   995  C  CB  . ARG A 1 137 ? 54.626 -22.371 30.900  1.00 16.60  ?  132 ARG B CB  1 
ATOM   996  C  CG  . ARG A 1 137 ? 56.135 -22.577 31.038  1.00 17.28  ?  132 ARG B CG  1 
ATOM   997  C  CD  . ARG A 1 137 ? 56.501 -23.928 31.624  1.00 17.62  ?  132 ARG B CD  1 
ATOM   998  N  NE  . ARG A 1 137 ? 55.904 -24.147 32.925  1.00 17.51  ?  132 ARG B NE  1 
ATOM   999  C  CZ  . ARG A 1 137 ? 56.260 -25.101 33.758  1.00 19.19  ?  132 ARG B CZ  1 
ATOM   1000 N  NH1 . ARG A 1 137 ? 57.254 -25.931 33.457  1.00 22.12  ?  132 ARG B NH1 1 
ATOM   1001 N  NH2 . ARG A 1 137 ? 55.623 -25.219 34.894  1.00 18.86  ?  132 ARG B NH2 1 
ATOM   1002 N  N   . ALA A 1 138 ? 52.131 -20.318 30.563  1.00 15.30  ?  133 ALA B N   1 
ATOM   1003 C  CA  . ALA A 1 138 ? 50.685 -20.074 30.480  1.00 14.37  ?  133 ALA B CA  1 
ATOM   1004 C  C   . ALA A 1 138 ? 50.416 -19.284 29.217  1.00 14.86  ?  133 ALA B C   1 
ATOM   1005 O  O   . ALA A 1 138 ? 49.328 -19.519 28.527  1.00 12.78  ?  133 ALA B O   1 
ATOM   1006 C  CB  . ALA A 1 138 ? 50.178 -19.344 31.684  1.00 14.33  ?  133 ALA B CB  1 
ATOM   1007 N  N   . THR A 1 139 ? 51.333 -18.362 28.939  1.00 14.24  ?  134 THR B N   1 
ATOM   1008 C  CA  . THR A 1 139 ? 51.165 -17.463 27.776  1.00 15.58  ?  134 THR B CA  1 
ATOM   1009 C  C   . THR A 1 139 ? 51.311 -18.297 26.494  1.00 14.86  ?  134 THR B C   1 
ATOM   1010 O  O   . THR A 1 139 ? 50.471 -18.161 25.588  1.00 14.39  ?  134 THR B O   1 
ATOM   1011 C  CB  . THR A 1 139 ? 52.105 -16.258 27.841  1.00 15.87  ?  134 THR B CB  1 
ATOM   1012 O  OG1 . THR A 1 139 ? 51.878 -15.499 29.043  1.00 15.86  ?  134 THR B OG1 1 
ATOM   1013 C  CG2 . THR A 1 139 ? 51.942 -15.373 26.616  1.00 15.34  ?  134 THR B CG2 1 
ATOM   1014 N  N   . VAL A 1 140 ? 52.317 -19.166 26.411  1.00 16.18  ?  135 VAL B N   1 
ATOM   1015 C  CA  . VAL A 1 140 ? 52.426 -20.095 25.240  1.00 16.31  ?  135 VAL B CA  1 
ATOM   1016 C  C   . VAL A 1 140 ? 51.112 -20.873 25.132  1.00 17.56  ?  135 VAL B C   1 
ATOM   1017 O  O   . VAL A 1 140 ? 50.573 -21.000 23.989  1.00 17.12  ?  135 VAL B O   1 
ATOM   1018 C  CB  . VAL A 1 140 ? 53.630 -21.036 25.363  1.00 16.89  ?  135 VAL B CB  1 
ATOM   1019 C  CG1 . VAL A 1 140 ? 53.636 -22.060 24.234  1.00 17.98  ?  135 VAL B CG1 1 
ATOM   1020 C  CG2 . VAL A 1 140 ? 54.945 -20.261 25.347  1.00 16.95  ?  135 VAL B CG2 1 
ATOM   1021 N  N   . ALA A 1 141 ? 50.628 -21.475 26.217  1.00 16.19  ?  136 ALA B N   1 
ATOM   1022 C  CA  . ALA A 1 141 ? 49.463 -22.399 26.101  1.00 16.87  ?  136 ALA B CA  1 
ATOM   1023 C  C   . ALA A 1 141 ? 48.236 -21.634 25.564  1.00 20.22  ?  136 ALA B C   1 
ATOM   1024 O  O   . ALA A 1 141 ? 47.482 -22.183 24.671  1.00 21.38  ?  136 ALA B O   1 
ATOM   1025 C  CB  . ALA A 1 141 ? 49.169 -23.092 27.410  1.00 16.54  ?  136 ALA B CB  1 
ATOM   1026 N  N   . ALA A 1 142 ? 48.024 -20.409 26.044  1.00 19.27  ?  137 ALA B N   1 
ATOM   1027 C  CA  . ALA A 1 142 ? 46.870 -19.575 25.659  1.00 17.54  ?  137 ALA B CA  1 
ATOM   1028 C  C   . ALA A 1 142 ? 47.079 -19.065 24.231  1.00 16.20  ?  137 ALA B C   1 
ATOM   1029 O  O   . ALA A 1 142 ? 46.089 -19.102 23.468  1.00 18.23  ?  137 ALA B O   1 
ATOM   1030 C  CB  . ALA A 1 142 ? 46.676 -18.449 26.633  1.00 17.95  ?  137 ALA B CB  1 
ATOM   1031 N  N   . LEU A 1 143 ? 48.290 -18.640 23.849  1.00 13.36  ?  138 LEU B N   1 
ATOM   1032 C  CA  . LEU A 1 143 ? 48.434 -17.965 22.530  1.00 15.71  ?  138 LEU B CA  1 
ATOM   1033 C  C   . LEU A 1 143 ? 48.684 -19.009 21.426  1.00 16.58  ?  138 LEU B C   1 
ATOM   1034 O  O   . LEU A 1 143 ? 48.159 -18.814 20.308  1.00 17.59  ?  138 LEU B O   1 
ATOM   1035 C  CB  . LEU A 1 143 ? 49.541 -16.906 22.494  1.00 15.47  ?  138 LEU B CB  1 
ATOM   1036 C  CG  . LEU A 1 143 ? 49.500 -15.732 23.469  1.00 18.20  ?  138 LEU B CG  1 
ATOM   1037 C  CD1 . LEU A 1 143 ? 50.275 -14.546 22.937  1.00 16.48  ?  138 LEU B CD1 1 
ATOM   1038 C  CD2 . LEU A 1 143 ? 48.128 -15.361 23.976  1.00 19.22  ?  138 LEU B CD2 1 
ATOM   1039 N  N   . GLU A 1 144 ? 49.489 -20.051 21.673  1.00 16.70  ?  139 GLU B N   1 
ATOM   1040 C  CA  . GLU A 1 144 ? 49.773 -21.031 20.598  1.00 15.83  ?  139 GLU B CA  1 
ATOM   1041 C  C   . GLU A 1 144 ? 48.449 -21.653 20.153  1.00 17.37  ?  139 GLU B C   1 
ATOM   1042 O  O   . GLU A 1 144 ? 48.259 -21.809 18.946  1.00 18.25  ?  139 GLU B O   1 
ATOM   1043 C  CB  . GLU A 1 144 ? 50.815 -22.059 21.008  1.00 17.72  ?  139 GLU B CB  1 
ATOM   1044 C  CG  . GLU A 1 144 ? 51.225 -22.960 19.858  1.00 17.70  ?  139 GLU B CG  1 
ATOM   1045 C  CD  . GLU A 1 144 ? 51.971 -22.325 18.687  1.00 17.63  ?  139 GLU B CD  1 
ATOM   1046 O  OE1 . GLU A 1 144 ? 52.515 -21.213 18.827  1.00 17.93  ?  139 GLU B OE1 1 
ATOM   1047 O  OE2 . GLU A 1 144 ? 52.015 -22.976 17.612  1.00 20.39  -1 139 GLU B OE2 1 
ATOM   1048 N  N   . SER A 1 145 ? 47.562 -21.999 21.096  1.00 20.29  ?  140 SER B N   1 
ATOM   1049 C  CA  . SER A 1 145 ? 46.240 -22.622 20.798  1.00 22.64  ?  140 SER B CA  1 
ATOM   1050 C  C   . SER A 1 145 ? 45.394 -21.670 19.943  1.00 22.95  ?  140 SER B C   1 
ATOM   1051 O  O   . SER A 1 145 ? 44.764 -22.127 18.982  1.00 25.37  ?  140 SER B O   1 
ATOM   1052 C  CB  . SER A 1 145 ? 45.510 -23.008 22.050  1.00 22.82  ?  140 SER B CB  1 
ATOM   1053 O  OG  . SER A 1 145 ? 45.303 -21.870 22.875  1.00 29.71  ?  140 SER B OG  1 
ATOM   1054 N  N   . ARG A 1 146 ? 45.377 -20.375 20.246  1.00 21.43  ?  141 ARG B N   1 
ATOM   1055 C  CA  . ARG A 1 146 ? 44.454 -19.425 19.570  1.00 20.43  ?  141 ARG B CA  1 
ATOM   1056 C  C   . ARG A 1 146 ? 45.040 -18.898 18.263  1.00 18.90  ?  141 ARG B C   1 
ATOM   1057 O  O   . ARG A 1 146 ? 44.253 -18.627 17.349  1.00 18.66  ?  141 ARG B O   1 
ATOM   1058 C  CB  . ARG A 1 146 ? 44.104 -18.275 20.511  1.00 23.10  ?  141 ARG B CB  1 
ATOM   1059 C  CG  . ARG A 1 146 ? 43.009 -17.356 19.985  1.00 25.44  ?  141 ARG B CG  1 
ATOM   1060 C  CD  . ARG A 1 146 ? 42.614 -16.369 21.062  1.00 28.11  ?  141 ARG B CD  1 
ATOM   1061 N  NE  . ARG A 1 146 ? 42.149 -17.077 22.240  1.00 32.59  ?  141 ARG B NE  1 
ATOM   1062 C  CZ  . ARG A 1 146 ? 40.869 -17.193 22.604  1.00 35.85  ?  141 ARG B CZ  1 
ATOM   1063 N  NH1 . ARG A 1 146 ? 39.920 -16.597 21.900  1.00 35.12  ?  141 ARG B NH1 1 
ATOM   1064 N  NH2 . ARG A 1 146 ? 40.553 -17.886 23.688  1.00 37.50  ?  141 ARG B NH2 1 
ATOM   1065 N  N   . PHE A 1 147 ? 46.348 -18.654 18.184  1.00 14.71  ?  142 PHE B N   1 
ATOM   1066 C  CA  . PHE A 1 147 ? 46.951 -17.887 17.065  1.00 16.00  ?  142 PHE B CA  1 
ATOM   1067 C  C   . PHE A 1 147 ? 48.015 -18.705 16.317  1.00 16.12  ?  142 PHE B C   1 
ATOM   1068 O  O   . PHE A 1 147 ? 48.513 -18.195 15.296  1.00 15.99  ?  142 PHE B O   1 
ATOM   1069 C  CB  . PHE A 1 147 ? 47.561 -16.586 17.578  1.00 15.30  ?  142 PHE B CB  1 
ATOM   1070 C  CG  . PHE A 1 147 ? 46.609 -15.717 18.348  1.00 15.82  ?  142 PHE B CG  1 
ATOM   1071 C  CD1 . PHE A 1 147 ? 45.618 -14.994 17.690  1.00 16.57  ?  142 PHE B CD1 1 
ATOM   1072 C  CD2 . PHE A 1 147 ? 46.698 -15.620 19.732  1.00 15.29  ?  142 PHE B CD2 1 
ATOM   1073 C  CE1 . PHE A 1 147 ? 44.723 -14.211 18.414  1.00 17.02  ?  142 PHE B CE1 1 
ATOM   1074 C  CE2 . PHE A 1 147 ? 45.800 -14.852 20.452  1.00 15.70  ?  142 PHE B CE2 1 
ATOM   1075 C  CZ  . PHE A 1 147 ? 44.802 -14.161 19.794  1.00 17.05  ?  142 PHE B CZ  1 
ATOM   1076 N  N   . GLY A 1 148 ? 48.357 -19.894 16.823  1.00 18.68  ?  143 GLY B N   1 
ATOM   1077 C  CA  . GLY A 1 148 ? 49.587 -20.584 16.410  1.00 18.97  ?  143 GLY B CA  1 
ATOM   1078 C  C   . GLY A 1 148 ? 49.303 -21.638 15.362  1.00 21.57  ?  143 GLY B C   1 
ATOM   1079 O  O   . GLY A 1 148 ? 48.222 -21.601 14.743  1.00 19.56  ?  143 GLY B O   1 
ATOM   1080 N  N   . ALA A 1 149 ? 50.211 -22.600 15.253  1.00 21.96  ?  144 ALA B N   1 
ATOM   1081 C  CA  . ALA A 1 149 ? 50.260 -23.603 14.171  1.00 23.37  ?  144 ALA B CA  1 
ATOM   1082 C  C   . ALA A 1 149 ? 50.699 -24.950 14.752  1.00 23.39  ?  144 ALA B C   1 
ATOM   1083 O  O   . ALA A 1 149 ? 51.425 -25.673 14.072  1.00 27.67  ?  144 ALA B O   1 
ATOM   1084 C  CB  . ALA A 1 149 ? 51.169 -23.091 13.077  1.00 23.92  ?  144 ALA B CB  1 
ATOM   1085 N  N   . GLY A 1 150 ? 50.199 -25.285 15.942  1.00 24.33  ?  145 GLY B N   1 
ATOM   1086 C  CA  . GLY A 1 150 ? 50.300 -26.603 16.590  1.00 22.59  ?  145 GLY B CA  1 
ATOM   1087 C  C   . GLY A 1 150 ? 51.683 -26.854 17.167  1.00 23.39  ?  145 GLY B C   1 
ATOM   1088 O  O   . GLY A 1 150 ? 52.055 -28.041 17.334  1.00 23.63  ?  145 GLY B O   1 
ATOM   1089 N  N   . TRP A 1 151 ? 52.444 -25.801 17.466  1.00 19.76  ?  146 TRP B N   1 
ATOM   1090 C  CA  . TRP A 1 151 ? 53.791 -25.966 18.069  1.00 20.41  ?  146 TRP B CA  1 
ATOM   1091 C  C   . TRP A 1 151 ? 53.651 -26.572 19.466  1.00 19.75  ?  146 TRP B C   1 
ATOM   1092 O  O   . TRP A 1 151 ? 52.772 -26.156 20.245  1.00 22.06  ?  146 TRP B O   1 
ATOM   1093 C  CB  . TRP A 1 151 ? 54.576 -24.660 18.078  1.00 18.92  ?  146 TRP B CB  1 
ATOM   1094 C  CG  . TRP A 1 151 ? 55.964 -24.784 18.632  1.00 17.49  ?  146 TRP B CG  1 
ATOM   1095 C  CD1 . TRP A 1 151 ? 57.039 -25.399 18.063  1.00 17.95  ?  146 TRP B CD1 1 
ATOM   1096 C  CD2 . TRP A 1 151 ? 56.423 -24.258 19.886  1.00 16.59  ?  146 TRP B CD2 1 
ATOM   1097 N  NE1 . TRP A 1 151 ? 58.134 -25.320 18.895  1.00 18.08  ?  146 TRP B NE1 1 
ATOM   1098 C  CE2 . TRP A 1 151 ? 57.790 -24.613 20.011  1.00 16.47  ?  146 TRP B CE2 1 
ATOM   1099 C  CE3 . TRP A 1 151 ? 55.827 -23.520 20.908  1.00 15.53  ?  146 TRP B CE3 1 
ATOM   1100 C  CZ2 . TRP A 1 151 ? 58.556 -24.197 21.086  1.00 15.67  ?  146 TRP B CZ2 1 
ATOM   1101 C  CZ3 . TRP A 1 151 ? 56.582 -23.140 21.986  1.00 16.24  ?  146 TRP B CZ3 1 
ATOM   1102 C  CH2 . TRP A 1 151 ? 57.942 -23.452 22.061  1.00 16.23  ?  146 TRP B CH2 1 
ATOM   1103 N  N   . ASP A 1 152 ? 54.497 -27.552 19.765  1.00 20.16  ?  147 ASP B N   1 
ATOM   1104 C  CA  . ASP A 1 152 ? 54.555 -28.236 21.081  1.00 17.99  ?  147 ASP B CA  1 
ATOM   1105 C  C   . ASP A 1 152 ? 55.748 -27.671 21.841  1.00 18.76  ?  147 ASP B C   1 
ATOM   1106 O  O   . ASP A 1 152 ? 56.898 -27.824 21.373  1.00 19.61  ?  147 ASP B O   1 
ATOM   1107 C  CB  . ASP A 1 152 ? 54.588 -29.749 20.826  1.00 19.85  ?  147 ASP B CB  1 
ATOM   1108 C  CG  . ASP A 1 152 ? 54.756 -30.590 22.054  1.00 18.70  ?  147 ASP B CG  1 
ATOM   1109 O  OD1 . ASP A 1 152 ? 54.711 -30.005 23.137  1.00 19.32  ?  147 ASP B OD1 1 
ATOM   1110 O  OD2 . ASP A 1 152 ? 54.899 -31.848 21.928  1.00 22.26  -1 147 ASP B OD2 1 
ATOM   1111 N  N   . MET A 1 153 ? 55.506 -27.010 22.967  1.00 17.38  ?  148 MET B N   1 
ATOM   1112 C  CA  . MET A 1 153 ? 56.577 -26.363 23.766  1.00 19.63  ?  148 MET B CA  1 
ATOM   1113 C  C   . MET A 1 153 ? 57.423 -27.408 24.520  1.00 20.36  ?  148 MET B C   1 
ATOM   1114 O  O   . MET A 1 153 ? 58.486 -26.996 25.047  1.00 19.38  ?  148 MET B O   1 
ATOM   1115 C  CB  . MET A 1 153 ? 55.990 -25.360 24.759  1.00 18.21  ?  148 MET B CB  1 
ATOM   1116 C  CG  . MET A 1 153 ? 55.350 -25.990 26.025  1.00 18.60  ?  148 MET B CG  1 
ATOM   1117 S  SD  . MET A 1 153 ? 54.660 -24.733 27.129  1.00 21.03  ?  148 MET B SD  1 
ATOM   1118 C  CE  . MET A 1 153 ? 53.032 -24.528 26.418  1.00 22.39  ?  148 MET B CE  1 
ATOM   1119 N  N   . THR A 1 154 ? 57.007 -28.691 24.566  1.00 20.39  ?  149 THR B N   1 
ATOM   1120 C  CA  . THR A 1 154 ? 57.659 -29.722 25.424  1.00 21.54  ?  149 THR B CA  1 
ATOM   1121 C  C   . THR A 1 154 ? 59.181 -29.714 25.238  1.00 22.36  ?  149 THR B C   1 
ATOM   1122 O  O   . THR A 1 154 ? 59.904 -29.617 26.268  1.00 24.02  ?  149 THR B O   1 
ATOM   1123 C  CB  . THR A 1 154 ? 57.091 -31.118 25.186  1.00 22.60  ?  149 THR B CB  1 
ATOM   1124 O  OG1 . THR A 1 154 ? 55.654 -31.078 25.359  1.00 22.69  ?  149 THR B OG1 1 
ATOM   1125 C  CG2 . THR A 1 154 ? 57.737 -32.091 26.146  1.00 22.40  ?  149 THR B CG2 1 
ATOM   1126 N  N   . GLY A 1 155 ? 59.646 -29.790 23.987  1.00 23.99  ?  150 GLY B N   1 
ATOM   1127 C  CA  . GLY A 1 155 ? 61.079 -29.842 23.630  1.00 22.38  ?  150 GLY B CA  1 
ATOM   1128 C  C   . GLY A 1 155 ? 61.843 -28.584 24.027  1.00 23.56  ?  150 GLY B C   1 
ATOM   1129 O  O   . GLY A 1 155 ? 63.085 -28.601 23.966  1.00 22.22  ?  150 GLY B O   1 
ATOM   1130 N  N   . SER A 1 156 ? 61.159 -27.505 24.419  1.00 20.15  ?  151 SER B N   1 
ATOM   1131 C  CA  . SER A 1 156 ? 61.774 -26.185 24.743  1.00 20.01  ?  151 SER B CA  1 
ATOM   1132 C  C   . SER A 1 156 ? 61.581 -25.806 26.222  1.00 19.63  ?  151 SER B C   1 
ATOM   1133 O  O   . SER A 1 156 ? 61.959 -24.690 26.640  1.00 19.27  ?  151 SER B O   1 
ATOM   1134 C  CB  . SER A 1 156 ? 61.214 -25.129 23.829  1.00 19.62  ?  151 SER B CB  1 
ATOM   1135 O  OG  . SER A 1 156 ? 61.492 -25.442 22.474  1.00 17.44  ?  151 SER B OG  1 
ATOM   1136 N  N   . LEU A 1 157 ? 61.004 -26.695 27.027  1.00 21.75  ?  152 LEU B N   1 
ATOM   1137 C  CA  . LEU A 1 157 ? 60.689 -26.351 28.433  1.00 22.23  ?  152 LEU B CA  1 
ATOM   1138 C  C   . LEU A 1 157 ? 61.969 -26.020 29.189  1.00 23.35  ?  152 LEU B C   1 
ATOM   1139 O  O   . LEU A 1 157 ? 61.960 -25.022 29.928  1.00 22.22  ?  152 LEU B O   1 
ATOM   1140 C  CB  . LEU A 1 157 ? 59.899 -27.477 29.096  1.00 26.17  ?  152 LEU B CB  1 
ATOM   1141 C  CG  . LEU A 1 157 ? 58.435 -27.555 28.673  1.00 26.78  ?  152 LEU B CG  1 
ATOM   1142 C  CD1 . LEU A 1 157 ? 57.808 -28.839 29.175  1.00 32.76  ?  152 LEU B CD1 1 
ATOM   1143 C  CD2 . LEU A 1 157 ? 57.658 -26.361 29.168  1.00 30.38  ?  152 LEU B CD2 1 
ATOM   1144 N  N   . ASP A 1 158 ? 63.054 -26.774 28.987  1.00 23.14  ?  153 ASP B N   1 
ATOM   1145 C  CA  . ASP A 1 158 ? 64.341 -26.446 29.656  1.00 25.00  ?  153 ASP B CA  1 
ATOM   1146 C  C   . ASP A 1 158 ? 64.920 -25.179 29.018  1.00 22.77  ?  153 ASP B C   1 
ATOM   1147 O  O   . ASP A 1 158 ? 65.510 -24.371 29.740  1.00 19.60  ?  153 ASP B O   1 
ATOM   1148 C  CB  . ASP A 1 158 ? 65.324 -27.623 29.650  1.00 29.47  ?  153 ASP B CB  1 
ATOM   1149 C  CG  . ASP A 1 158 ? 65.022 -28.696 30.695  1.00 35.40  ?  153 ASP B CG  1 
ATOM   1150 O  OD1 . ASP A 1 158 ? 65.363 -29.860 30.425  1.00 43.14  ?  153 ASP B OD1 1 
ATOM   1151 O  OD2 . ASP A 1 158 ? 64.511 -28.354 31.796  1.00 36.87  -1 153 ASP B OD2 1 
ATOM   1152 N  N   . TYR A 1 159 ? 64.725 -24.994 27.711  1.00 22.75  ?  154 TYR B N   1 
ATOM   1153 C  CA  . TYR A 1 159 ? 65.187 -23.771 27.000  1.00 20.81  ?  154 TYR B CA  1 
ATOM   1154 C  C   . TYR A 1 159 ? 64.580 -22.517 27.626  1.00 20.01  ?  154 TYR B C   1 
ATOM   1155 O  O   . TYR A 1 159 ? 65.304 -21.594 27.906  1.00 19.57  ?  154 TYR B O   1 
ATOM   1156 C  CB  . TYR A 1 159 ? 64.848 -23.839 25.518  1.00 20.52  ?  154 TYR B CB  1 
ATOM   1157 C  CG  . TYR A 1 159 ? 65.260 -22.598 24.775  1.00 21.39  ?  154 TYR B CG  1 
ATOM   1158 C  CD1 . TYR A 1 159 ? 66.604 -22.286 24.565  1.00 19.71  ?  154 TYR B CD1 1 
ATOM   1159 C  CD2 . TYR A 1 159 ? 64.300 -21.749 24.259  1.00 20.17  ?  154 TYR B CD2 1 
ATOM   1160 C  CE1 . TYR A 1 159 ? 66.964 -21.136 23.876  1.00 20.95  ?  154 TYR B CE1 1 
ATOM   1161 C  CE2 . TYR A 1 159 ? 64.642 -20.604 23.567  1.00 19.63  ?  154 TYR B CE2 1 
ATOM   1162 C  CZ  . TYR A 1 159 ? 65.980 -20.306 23.349  1.00 21.38  ?  154 TYR B CZ  1 
ATOM   1163 O  OH  . TYR A 1 159 ? 66.280 -19.153 22.661  1.00 22.77  ?  154 TYR B OH  1 
ATOM   1164 N  N   . PHE A 1 160 ? 63.269 -22.531 27.934  1.00 20.67  ?  155 PHE B N   1 
ATOM   1165 C  CA  . PHE A 1 160 ? 62.584 -21.425 28.626  1.00 19.82  ?  155 PHE B CA  1 
ATOM   1166 C  C   . PHE A 1 160 ? 63.335 -21.103 29.918  1.00 22.38  ?  155 PHE B C   1 
ATOM   1167 O  O   . PHE A 1 160 ? 63.479 -19.923 30.239  1.00 21.83  ?  155 PHE B O   1 
ATOM   1168 C  CB  . PHE A 1 160 ? 61.135 -21.775 28.991  1.00 20.28  ?  155 PHE B CB  1 
ATOM   1169 C  CG  . PHE A 1 160 ? 60.176 -21.949 27.835  1.00 18.08  ?  155 PHE B CG  1 
ATOM   1170 C  CD1 . PHE A 1 160 ? 60.543 -21.724 26.517  1.00 17.65  ?  155 PHE B CD1 1 
ATOM   1171 C  CD2 . PHE A 1 160 ? 58.865 -22.296 28.088  1.00 19.41  ?  155 PHE B CD2 1 
ATOM   1172 C  CE1 . PHE A 1 160 ? 59.638 -21.879 25.482  1.00 19.00  ?  155 PHE B CE1 1 
ATOM   1173 C  CE2 . PHE A 1 160 ? 57.939 -22.419 27.055  1.00 19.90  ?  155 PHE B CE2 1 
ATOM   1174 C  CZ  . PHE A 1 160 ? 58.326 -22.220 25.744  1.00 20.42  ?  155 PHE B CZ  1 
ATOM   1175 N  N   . ARG A 1 161 ? 63.739 -22.125 30.677  1.00 18.59  ?  156 ARG B N   1 
ATOM   1176 C  CA  . ARG A 1 161 ? 64.407 -21.904 31.970  1.00 20.73  ?  156 ARG B CA  1 
ATOM   1177 C  C   . ARG A 1 161 ? 65.795 -21.331 31.648  1.00 18.88  ?  156 ARG B C   1 
ATOM   1178 O  O   . ARG A 1 161 ? 66.221 -20.473 32.384  1.00 20.83  ?  156 ARG B O   1 
ATOM   1179 C  CB  . ARG A 1 161 ? 64.463 -23.188 32.811  1.00 21.10  ?  156 ARG B CB  1 
ATOM   1180 C  CG  . ARG A 1 161 ? 63.108 -23.818 33.096  1.00 22.43  ?  156 ARG B CG  1 
ATOM   1181 C  CD  . ARG A 1 161 ? 63.215 -25.056 34.002  1.00 24.25  ?  156 ARG B CD  1 
ATOM   1182 N  NE  . ARG A 1 161 ? 63.768 -24.715 35.306  1.00 27.57  ?  156 ARG B NE  1 
ATOM   1183 C  CZ  . ARG A 1 161 ? 64.245 -25.603 36.189  1.00 30.30  ?  156 ARG B CZ  1 
ATOM   1184 N  NH1 . ARG A 1 161 ? 64.178 -26.894 35.938  1.00 28.51  ?  156 ARG B NH1 1 
ATOM   1185 N  NH2 . ARG A 1 161 ? 64.749 -25.189 37.337  1.00 32.55  ?  156 ARG B NH2 1 
ATOM   1186 N  N   . ARG A 1 162 ? 66.424 -21.753 30.543  1.00 21.42  ?  157 ARG B N   1 
ATOM   1187 C  CA  . ARG A 1 162 ? 67.823 -21.358 30.170  1.00 20.04  ?  157 ARG B CA  1 
ATOM   1188 C  C   . ARG A 1 162 ? 67.866 -19.920 29.606  1.00 19.82  ?  157 ARG B C   1 
ATOM   1189 O  O   . ARG A 1 162 ? 68.971 -19.393 29.523  1.00 22.32  ?  157 ARG B O   1 
ATOM   1190 C  CB  . ARG A 1 162 ? 68.430 -22.302 29.120  1.00 23.32  ?  157 ARG B CB  1 
ATOM   1191 C  CG  . ARG A 1 162 ? 68.860 -23.677 29.614  1.00 24.87  ?  157 ARG B CG  1 
ATOM   1192 C  CD  . ARG A 1 162 ? 69.847 -24.293 28.633  1.00 24.91  ?  157 ARG B CD  1 
ATOM   1193 N  NE  . ARG A 1 162 ? 69.411 -24.497 27.248  1.00 26.47  ?  157 ARG B NE  1 
ATOM   1194 C  CZ  . ARG A 1 162 ? 68.713 -25.549 26.841  1.00 28.06  ?  157 ARG B CZ  1 
ATOM   1195 N  NH1 . ARG A 1 162 ? 68.309 -26.438 27.731  1.00 29.99  ?  157 ARG B NH1 1 
ATOM   1196 N  NH2 . ARG A 1 162 ? 68.358 -25.680 25.581  1.00 28.63  ?  157 ARG B NH2 1 
ATOM   1197 N  N   . ILE A 1 163 ? 66.730 -19.295 29.280  1.00 19.90  ?  158 ILE B N   1 
ATOM   1198 C  CA  . ILE A 1 163 ? 66.649 -17.901 28.745  1.00 19.85  ?  158 ILE B CA  1 
ATOM   1199 C  C   . ILE A 1 163 ? 65.765 -17.022 29.656  1.00 18.63  ?  158 ILE B C   1 
ATOM   1200 O  O   . ILE A 1 163 ? 65.402 -15.925 29.231  1.00 23.28  ?  158 ILE B O   1 
ATOM   1201 C  CB  . ILE A 1 163 ? 66.148 -17.850 27.292  1.00 18.74  ?  158 ILE B CB  1 
ATOM   1202 C  CG1 . ILE A 1 163 ? 64.751 -18.454 27.126  1.00 21.06  ?  158 ILE B CG1 1 
ATOM   1203 C  CG2 . ILE A 1 163 ? 67.105 -18.469 26.322  1.00 20.57  ?  158 ILE B CG2 1 
ATOM   1204 C  CD1 . ILE A 1 163 ? 63.993 -17.858 26.001  1.00 20.66  ?  158 ILE B CD1 1 
ATOM   1205 N  N   . LEU A 1 164 ? 65.500 -17.415 30.889  1.00 20.14  ?  159 LEU B N   1 
ATOM   1206 C  CA  . LEU A 1 164 ? 64.467 -16.802 31.777  1.00 19.75  ?  159 LEU B CA  1 
ATOM   1207 C  C   . LEU A 1 164 ? 64.832 -15.474 32.431  1.00 21.43  ?  159 LEU B C   1 
ATOM   1208 O  O   . LEU A 1 164 ? 63.927 -14.733 32.797  1.00 22.52  ?  159 LEU B O   1 
ATOM   1209 C  CB  . LEU A 1 164 ? 64.083 -17.802 32.874  1.00 22.01  ?  159 LEU B CB  1 
ATOM   1210 C  CG  . LEU A 1 164 ? 62.770 -17.541 33.613  1.00 22.64  ?  159 LEU B CG  1 
ATOM   1211 C  CD1 . LEU A 1 164 ? 61.537 -17.776 32.729  1.00 24.49  ?  159 LEU B CD1 1 
ATOM   1212 C  CD2 . LEU A 1 164 ? 62.661 -18.420 34.835  1.00 24.27  ?  159 LEU B CD2 1 
ATOM   1213 N  N   . PRO A 1 165 ? 66.084 -15.175 32.852  1.00 21.70  ?  160 PRO B N   1 
ATOM   1214 C  CA  . PRO A 1 165 ? 66.322 -13.997 33.691  1.00 21.94  ?  160 PRO B CA  1 
ATOM   1215 C  C   . PRO A 1 165 ? 65.842 -12.626 33.132  1.00 22.69  ?  160 PRO B C   1 
ATOM   1216 O  O   . PRO A 1 165 ? 65.546 -11.723 33.945  1.00 22.33  ?  160 PRO B O   1 
ATOM   1217 C  CB  . PRO A 1 165 ? 67.859 -13.997 33.881  1.00 22.59  ?  160 PRO B CB  1 
ATOM   1218 C  CG  . PRO A 1 165 ? 68.285 -15.436 33.628  1.00 22.18  ?  160 PRO B CG  1 
ATOM   1219 C  CD  . PRO A 1 165 ? 67.291 -15.983 32.616  1.00 21.83  ?  160 PRO B CD  1 
ATOM   1220 N  N   . GLY A 1 166 ? 65.720 -12.504 31.808  1.00 21.86  ?  161 GLY B N   1 
ATOM   1221 C  CA  . GLY A 1 166 ? 65.342 -11.275 31.082  1.00 19.10  ?  161 GLY B CA  1 
ATOM   1222 C  C   . GLY A 1 166 ? 63.837 -11.013 31.218  1.00 18.12  ?  161 GLY B C   1 
ATOM   1223 O  O   . GLY A 1 166 ? 63.415 -9.878  31.048  1.00 14.06  ?  161 GLY B O   1 
ATOM   1224 N  N   . VAL A 1 167 ? 63.045 -12.032 31.573  1.00 18.32  ?  162 VAL B N   1 
ATOM   1225 C  CA  . VAL A 1 167 ? 61.560 -11.862 31.744  1.00 19.26  ?  162 VAL B CA  1 
ATOM   1226 C  C   . VAL A 1 167 ? 61.221 -11.064 33.004  1.00 18.19  ?  162 VAL B C   1 
ATOM   1227 O  O   . VAL A 1 167 ? 61.651 -11.469 34.111  1.00 19.73  ?  162 VAL B O   1 
ATOM   1228 C  CB  . VAL A 1 167 ? 60.862 -13.228 31.785  1.00 17.98  ?  162 VAL B CB  1 
ATOM   1229 C  CG1 . VAL A 1 167 ? 59.364 -13.115 31.947  1.00 18.02  ?  162 VAL B CG1 1 
ATOM   1230 C  CG2 . VAL A 1 167 ? 61.239 -14.026 30.556  1.00 18.53  ?  162 VAL B CG2 1 
ATOM   1231 N  N   . GLY A 1 168 ? 60.401 -10.012 32.847  1.00 17.34  ?  163 GLY B N   1 
ATOM   1232 C  CA  . GLY A 1 168 ? 59.755 -9.258  33.932  1.00 16.58  ?  163 GLY B CA  1 
ATOM   1233 C  C   . GLY A 1 168 ? 58.298 -9.631  33.984  1.00 17.34  ?  163 GLY B C   1 
ATOM   1234 O  O   . GLY A 1 168 ? 57.485 -9.035  33.201  1.00 17.57  ?  163 GLY B O   1 
ATOM   1235 N  N   . ALA A 1 169 ? 57.931 -10.627 34.792  1.00 17.57  ?  164 ALA B N   1 
ATOM   1236 C  CA  . ALA A 1 169 ? 56.516 -11.077 34.847  1.00 16.91  ?  164 ALA B CA  1 
ATOM   1237 C  C   . ALA A 1 169 ? 55.730 -10.206 35.826  1.00 17.35  ?  164 ALA B C   1 
ATOM   1238 O  O   . ALA A 1 169 ? 56.306 -9.742  36.847  1.00 17.58  ?  164 ALA B O   1 
ATOM   1239 C  CB  . ALA A 1 169 ? 56.381 -12.556 35.157  1.00 17.86  ?  164 ALA B CB  1 
ATOM   1240 N  N   . PHE A 1 170 ? 54.420 -10.055 35.600  1.00 17.95  ?  165 PHE B N   1 
ATOM   1241 C  CA  . PHE A 1 170 ? 53.561 -9.190  36.434  1.00 17.75  ?  165 PHE B CA  1 
ATOM   1242 C  C   . PHE A 1 170 ? 52.138 -9.744  36.485  1.00 17.26  ?  165 PHE B C   1 
ATOM   1243 O  O   . PHE A 1 170 ? 51.736 -10.644 35.750  1.00 17.59  ?  165 PHE B O   1 
ATOM   1244 C  CB  . PHE A 1 170 ? 53.652 -7.732  35.959  1.00 18.41  ?  165 PHE B CB  1 
ATOM   1245 C  CG  . PHE A 1 170 ? 53.236 -7.442  34.534  1.00 17.27  ?  165 PHE B CG  1 
ATOM   1246 C  CD1 . PHE A 1 170 ? 51.913 -7.273  34.209  1.00 19.66  ?  165 PHE B CD1 1 
ATOM   1247 C  CD2 . PHE A 1 170 ? 54.157 -7.345  33.524  1.00 20.49  ?  165 PHE B CD2 1 
ATOM   1248 C  CE1 . PHE A 1 170 ? 51.543 -6.952  32.915  1.00 19.31  ?  165 PHE B CE1 1 
ATOM   1249 C  CE2 . PHE A 1 170 ? 53.786 -7.086  32.215  1.00 19.22  ?  165 PHE B CE2 1 
ATOM   1250 C  CZ  . PHE A 1 170 ? 52.471 -6.909  31.914  1.00 17.95  ?  165 PHE B CZ  1 
ATOM   1251 N  N   . ARG A 1 171 ? 51.404 -9.213  37.425  1.00 17.52  ?  166 ARG B N   1 
ATOM   1252 C  CA  . ARG A 1 171 ? 49.992 -9.555  37.672  1.00 17.75  ?  166 ARG B CA  1 
ATOM   1253 C  C   . ARG A 1 171 ? 49.258 -8.221  37.674  1.00 21.88  ?  166 ARG B C   1 
ATOM   1254 O  O   . ARG A 1 171 ? 49.784 -7.221  38.254  1.00 23.30  ?  166 ARG B O   1 
ATOM   1255 C  CB  . ARG A 1 171 ? 49.895 -10.281 39.008  1.00 17.46  ?  166 ARG B CB  1 
ATOM   1256 C  CG  . ARG A 1 171 ? 50.675 -11.579 39.089  1.00 18.57  ?  166 ARG B CG  1 
ATOM   1257 C  CD  . ARG A 1 171 ? 49.981 -12.595 38.168  1.00 19.51  ?  166 ARG B CD  1 
ATOM   1258 N  NE  . ARG A 1 171 ? 50.537 -13.940 38.132  1.00 21.09  ?  166 ARG B NE  1 
ATOM   1259 C  CZ  . ARG A 1 171 ? 51.527 -14.354 37.327  1.00 21.03  ?  166 ARG B CZ  1 
ATOM   1260 N  NH1 . ARG A 1 171 ? 52.113 -13.527 36.479  1.00 19.38  ?  166 ARG B NH1 1 
ATOM   1261 N  NH2 . ARG A 1 171 ? 51.921 -15.610 37.365  1.00 20.95  ?  166 ARG B NH2 1 
ATOM   1262 N  N   . LEU A 1 172 ? 48.065 -8.185  37.097  1.00 21.55  ?  167 LEU B N   1 
ATOM   1263 C  CA  . LEU A 1 172 ? 47.270 -6.947  37.105  1.00 22.43  ?  167 LEU B CA  1 
ATOM   1264 C  C   . LEU A 1 172 ? 45.859 -7.296  37.533  1.00 21.79  ?  167 LEU B C   1 
ATOM   1265 O  O   . LEU A 1 172 ? 45.158 -7.958  36.760  1.00 21.76  ?  167 LEU B O   1 
ATOM   1266 C  CB  . LEU A 1 172 ? 47.295 -6.334  35.705  1.00 22.97  ?  167 LEU B CB  1 
ATOM   1267 C  CG  . LEU A 1 172 ? 46.524 -5.038  35.518  1.00 20.96  ?  167 LEU B CG  1 
ATOM   1268 C  CD1 . LEU A 1 172 ? 46.987 -3.966  36.522  1.00 22.44  ?  167 LEU B CD1 1 
ATOM   1269 C  CD2 . LEU A 1 172 ? 46.736 -4.563  34.086  1.00 21.83  ?  167 LEU B CD2 1 
ATOM   1270 N  N   . ARG A 1 173 ? 45.501 -6.921  38.762  1.00 22.69  ?  168 ARG B N   1 
ATOM   1271 C  CA  . ARG A 1 173 ? 44.133 -7.124  39.283  1.00 24.72  ?  168 ARG B CA  1 
ATOM   1272 C  C   . ARG A 1 173 ? 43.282 -5.991  38.706  1.00 22.15  ?  168 ARG B C   1 
ATOM   1273 O  O   . ARG A 1 173 ? 43.549 -4.795  38.995  1.00 22.53  ?  168 ARG B O   1 
ATOM   1274 C  CB  . ARG A 1 173 ? 44.156 -7.175  40.817  1.00 29.73  ?  168 ARG B CB  1 
ATOM   1275 C  CG  . ARG A 1 173 ? 42.783 -7.224  41.466  1.00 36.95  ?  168 ARG B CG  1 
ATOM   1276 C  CD  . ARG A 1 173 ? 42.018 -8.462  41.065  1.00 44.59  ?  168 ARG B CD  1 
ATOM   1277 N  NE  . ARG A 1 173 ? 41.531 -9.209  42.225  1.00 54.21  ?  168 ARG B NE  1 
ATOM   1278 C  CZ  . ARG A 1 173 ? 41.393 -10.545 42.295  1.00 61.35  ?  168 ARG B CZ  1 
ATOM   1279 N  NH1 . ARG A 1 173 ? 40.939 -11.088 43.416  1.00 69.52  ?  168 ARG B NH1 1 
ATOM   1280 N  NH2 . ARG A 1 173 ? 41.712 -11.336 41.273  1.00 52.21  ?  168 ARG B NH2 1 
ATOM   1281 N  N   . VAL A 1 174 ? 42.288 -6.339  37.908  1.00 20.44  ?  169 VAL B N   1 
ATOM   1282 C  CA  . VAL A 1 174 ? 41.463 -5.336  37.199  1.00 22.60  ?  169 VAL B CA  1 
ATOM   1283 C  C   . VAL A 1 174 ? 40.520 -4.661  38.219  1.00 22.77  ?  169 VAL B C   1 
ATOM   1284 O  O   . VAL A 1 174 ? 39.633 -5.331  38.719  1.00 22.11  ?  169 VAL B O   1 
ATOM   1285 C  CB  . VAL A 1 174 ? 40.716 -5.991  36.027  1.00 21.12  ?  169 VAL B CB  1 
ATOM   1286 C  CG1 . VAL A 1 174 ? 39.791 -4.981  35.361  1.00 19.95  ?  169 VAL B CG1 1 
ATOM   1287 C  CG2 . VAL A 1 174 ? 41.701 -6.598  35.032  1.00 19.73  ?  169 VAL B CG2 1 
ATOM   1288 N  N   . ALA A 1 175 ? 40.716 -3.359  38.473  1.00 23.50  ?  170 ALA B N   1 
ATOM   1289 C  CA  . ALA A 1 175 ? 39.869 -2.505  39.347  1.00 24.92  ?  170 ALA B CA  1 
ATOM   1290 C  C   . ALA A 1 175 ? 38.733 -1.890  38.529  1.00 24.14  ?  170 ALA B C   1 
ATOM   1291 O  O   . ALA A 1 175 ? 37.637 -1.752  39.056  1.00 23.76  ?  170 ALA B O   1 
ATOM   1292 C  CB  . ALA A 1 175 ? 40.715 -1.408  39.946  1.00 25.17  ?  170 ALA B CB  1 
ATOM   1293 N  N   . GLU A 1 176 ? 39.038 -1.483  37.289  1.00 22.82  ?  171 GLU B N   1 
ATOM   1294 C  CA  . GLU A 1 176 ? 38.109 -0.817  36.355  1.00 22.96  ?  171 GLU B CA  1 
ATOM   1295 C  C   . GLU A 1 176 ? 38.339 -1.394  34.960  1.00 20.70  ?  171 GLU B C   1 
ATOM   1296 O  O   . GLU A 1 176 ? 39.512 -1.624  34.589  1.00 17.28  ?  171 GLU B O   1 
ATOM   1297 C  CB  . GLU A 1 176 ? 38.367 0.690   36.244  1.00 26.81  ?  171 GLU B CB  1 
ATOM   1298 C  CG  . GLU A 1 176 ? 38.580 1.396   37.565  1.00 33.85  ?  171 GLU B CG  1 
ATOM   1299 C  CD  . GLU A 1 176 ? 38.232 2.880   37.558  1.00 40.03  ?  171 GLU B CD  1 
ATOM   1300 O  OE1 . GLU A 1 176 ? 38.021 3.420   38.674  1.00 51.76  ?  171 GLU B OE1 1 
ATOM   1301 O  OE2 . GLU A 1 176 ? 38.128 3.502   36.441  1.00 39.39  -1 171 GLU B OE2 1 
ATOM   1302 N  N   . ALA A 1 177 ? 37.266 -1.614  34.221  1.00 20.39  ?  172 ALA B N   1 
ATOM   1303 C  CA  . ALA A 1 177 ? 37.337 -2.093  32.826  1.00 21.28  ?  172 ALA B CA  1 
ATOM   1304 C  C   . ALA A 1 177 ? 36.354 -1.262  32.013  1.00 22.60  ?  172 ALA B C   1 
ATOM   1305 O  O   . ALA A 1 177 ? 35.202 -1.144  32.463  1.00 23.45  ?  172 ALA B O   1 
ATOM   1306 C  CB  . ALA A 1 177 ? 37.005 -3.550  32.746  1.00 23.56  ?  172 ALA B CB  1 
ATOM   1307 N  N   . ASP A 1 178 ? 36.801 -0.685  30.892  1.00 18.73  ?  173 ASP B N   1 
ATOM   1308 C  CA  . ASP A 1 178 ? 35.911 0.118   30.019  1.00 21.15  ?  173 ASP B CA  1 
ATOM   1309 C  C   . ASP A 1 178 ? 36.132 -0.367  28.604  1.00 18.57  ?  173 ASP B C   1 
ATOM   1310 O  O   . ASP A 1 178 ? 37.202 -0.844  28.340  1.00 16.43  ?  173 ASP B O   1 
ATOM   1311 C  CB  . ASP A 1 178 ? 36.220 1.605   30.144  1.00 22.33  ?  173 ASP B CB  1 
ATOM   1312 C  CG  . ASP A 1 178 ? 35.919 2.138   31.539  1.00 26.79  ?  173 ASP B CG  1 
ATOM   1313 O  OD1 . ASP A 1 178 ? 34.717 2.260   31.810  1.00 28.63  ?  173 ASP B OD1 1 
ATOM   1314 O  OD2 . ASP A 1 178 ? 36.895 2.373   32.367  1.00 29.91  -1 173 ASP B OD2 1 
ATOM   1315 N  N   . GLY A 1 179 ? 35.103 -0.325  27.787  1.00 18.17  ?  174 GLY B N   1 
ATOM   1316 C  CA  . GLY A 1 179 ? 35.155 -0.880  26.430  1.00 19.86  ?  174 GLY B CA  1 
ATOM   1317 C  C   . GLY A 1 179 ? 34.513 0.073   25.469  1.00 18.60  ?  174 GLY B C   1 
ATOM   1318 O  O   . GLY A 1 179 ? 33.314 0.476   25.754  1.00 17.48  ?  174 GLY B O   1 
ATOM   1319 N  N   . MET A 1 180 ? 35.269 0.484   24.440  1.00 18.21  ?  175 MET B N   1 
ATOM   1320 C  CA  . MET A 1 180 ? 34.713 1.248   23.295  1.00 16.65  ?  175 MET B CA  1 
ATOM   1321 C  C   . MET A 1 180 ? 34.355 0.289   22.163  1.00 17.58  ?  175 MET B C   1 
ATOM   1322 O  O   . MET A 1 180 ? 35.250 -0.360  21.640  1.00 16.86  ?  175 MET B O   1 
ATOM   1323 C  CB  . MET A 1 180 ? 35.693 2.286   22.748  1.00 18.79  ?  175 MET B CB  1 
ATOM   1324 C  CG  . MET A 1 180 ? 35.127 3.022   21.538  1.00 18.76  ?  175 MET B CG  1 
ATOM   1325 S  SD  . MET A 1 180 ? 34.212 4.472   21.985  1.00 20.89  ?  175 MET B SD  1 
ATOM   1326 C  CE  . MET A 1 180 ? 35.480 5.567   22.617  1.00 20.92  ?  175 MET B CE  1 
ATOM   1327 N  N   . PHE A 1 181 ? 33.062 0.172   21.816  1.00 16.19  ?  176 PHE B N   1 
ATOM   1328 C  CA  . PHE A 1 181 ? 32.642 -0.600  20.634  1.00 16.68  ?  176 PHE B CA  1 
ATOM   1329 C  C   . PHE A 1 181 ? 32.000 0.374   19.634  1.00 18.34  ?  176 PHE B C   1 
ATOM   1330 O  O   . PHE A 1 181 ? 30.732 0.510   19.544  1.00 16.19  ?  176 PHE B O   1 
ATOM   1331 C  CB  . PHE A 1 181 ? 31.803 -1.791  21.075  1.00 18.03  ?  176 PHE B CB  1 
ATOM   1332 C  CG  . PHE A 1 181 ? 32.588 -2.805  21.867  1.00 17.63  ?  176 PHE B CG  1 
ATOM   1333 C  CD1 . PHE A 1 181 ? 32.885 -2.583  23.202  1.00 18.70  ?  176 PHE B CD1 1 
ATOM   1334 C  CD2 . PHE A 1 181 ? 33.132 -3.919  21.246  1.00 20.05  ?  176 PHE B CD2 1 
ATOM   1335 C  CE1 . PHE A 1 181 ? 33.599 -3.518  23.924  1.00 19.16  ?  176 PHE B CE1 1 
ATOM   1336 C  CE2 . PHE A 1 181 ? 33.879 -4.838  21.967  1.00 18.67  ?  176 PHE B CE2 1 
ATOM   1337 C  CZ  . PHE A 1 181 ? 34.121 -4.629  23.298  1.00 19.65  ?  176 PHE B CZ  1 
ATOM   1338 N  N   . LYS A 1 182 ? 32.862 1.057   18.880  1.00 16.30  ?  177 LYS B N   1 
ATOM   1339 C  CA  . LYS A 1 182 ? 32.407 2.100   17.936  1.00 16.01  ?  177 LYS B CA  1 
ATOM   1340 C  C   . LYS A 1 182 ? 32.144 1.447   16.567  1.00 16.86  ?  177 LYS B C   1 
ATOM   1341 O  O   . LYS A 1 182 ? 33.087 1.172   15.809  1.00 14.34  ?  177 LYS B O   1 
ATOM   1342 C  CB  . LYS A 1 182 ? 33.397 3.256   17.914  1.00 17.36  ?  177 LYS B CB  1 
ATOM   1343 C  CG  . LYS A 1 182 ? 33.029 4.377   16.982  1.00 17.36  ?  177 LYS B CG  1 
ATOM   1344 C  CD  . LYS A 1 182 ? 33.948 5.558   17.122  1.00 20.03  ?  177 LYS B CD  1 
ATOM   1345 C  CE  . LYS A 1 182 ? 33.587 6.702   16.208  1.00 23.23  ?  177 LYS B CE  1 
ATOM   1346 N  NZ  . LYS A 1 182 ? 32.519 6.325   15.248  1.00 27.42  ?  177 LYS B NZ  1 
ATOM   1347 N  N   . LEU A 1 183 ? 30.866 1.168   16.293  1.00 15.82  ?  178 LEU B N   1 
ATOM   1348 C  CA  . LEU A 1 183 ? 30.443 0.212   15.243  1.00 16.97  ?  178 LEU B CA  1 
ATOM   1349 C  C   . LEU A 1 183 ? 29.202 0.768   14.535  1.00 16.58  ?  178 LEU B C   1 
ATOM   1350 O  O   . LEU A 1 183 ? 28.338 -0.044  14.231  1.00 17.00  ?  178 LEU B O   1 
ATOM   1351 C  CB  . LEU A 1 183 ? 30.161 -1.127  15.925  1.00 17.46  ?  178 LEU B CB  1 
ATOM   1352 C  CG  . LEU A 1 183 ? 31.375 -1.843  16.535  1.00 18.66  ?  178 LEU B CG  1 
ATOM   1353 C  CD1 . LEU A 1 183 ? 30.926 -3.062  17.317  1.00 19.72  ?  178 LEU B CD1 1 
ATOM   1354 C  CD2 . LEU A 1 183 ? 32.371 -2.274  15.457  1.00 18.91  ?  178 LEU B CD2 1 
ATOM   1355 N  N   . SER A 1 184 ? 29.158 2.087   14.323  1.00 15.47  ?  179 SER B N   1 
ATOM   1356 C  CA  . SER A 1 184 ? 28.105 2.814   13.582  1.00 18.65  ?  179 SER B CA  1 
ATOM   1357 C  C   . SER A 1 184 ? 26.746 2.788   14.323  1.00 18.21  ?  179 SER B C   1 
ATOM   1358 O  O   . SER A 1 184 ? 25.727 3.042   13.657  1.00 20.63  ?  179 SER B O   1 
ATOM   1359 C  CB  . SER A 1 184 ? 27.971 2.266   12.169  1.00 19.14  ?  179 SER B CB  1 
ATOM   1360 O  OG  . SER A 1 184 ? 29.216 2.373   11.476  1.00 20.15  ?  179 SER B OG  1 
ATOM   1361 N  N   . GLN A 1 185 ? 26.705 2.549   15.624  1.00 17.46  ?  180 GLN B N   1 
ATOM   1362 C  CA  . GLN A 1 185 ? 25.432 2.583   16.412  1.00 21.10  ?  180 GLN B CA  1 
ATOM   1363 C  C   . GLN A 1 185 ? 24.767 3.971   16.334  1.00 23.81  ?  180 GLN B C   1 
ATOM   1364 O  O   . GLN A 1 185 ? 23.516 4.053   16.461  1.00 25.03  ?  180 GLN B O   1 
ATOM   1365 C  CB  . GLN A 1 185 ? 25.636 2.196   17.873  1.00 21.04  ?  180 GLN B CB  1 
ATOM   1366 C  CG  . GLN A 1 185 ? 26.089 0.757   18.097  1.00 20.17  ?  180 GLN B CG  1 
ATOM   1367 C  CD  . GLN A 1 185 ? 27.596 0.680   18.209  1.00 20.36  ?  180 GLN B CD  1 
ATOM   1368 O  OE1 . GLN A 1 185 ? 28.302 1.344   17.462  1.00 17.10  ?  180 GLN B OE1 1 
ATOM   1369 N  NE2 . GLN A 1 185 ? 28.085 -0.075  19.181  1.00 19.11  ?  180 GLN B NE2 1 
ATOM   1370 N  N   . GLU A 1 186 ? 25.524 5.029   16.074  1.00 23.46  ?  181 GLU B N   1 
ATOM   1371 C  CA  . GLU A 1 186 ? 24.988 6.417   15.997  1.00 23.99  ?  181 GLU B CA  1 
ATOM   1372 C  C   . GLU A 1 186 ? 24.216 6.613   14.679  1.00 26.13  ?  181 GLU B C   1 
ATOM   1373 O  O   . GLU A 1 186 ? 23.487 7.592   14.601  1.00 25.13  ?  181 GLU B O   1 
ATOM   1374 C  CB  . GLU A 1 186 ? 26.120 7.429   16.140  1.00 27.30  ?  181 GLU B CB  1 
ATOM   1375 C  CG  . GLU A 1 186 ? 26.937 7.687   14.871  1.00 26.68  ?  181 GLU B CG  1 
ATOM   1376 C  CD  . GLU A 1 186 ? 27.901 6.613   14.358  1.00 26.64  ?  181 GLU B CD  1 
ATOM   1377 O  OE1 . GLU A 1 186 ? 28.129 5.584   15.076  1.00 25.47  ?  181 GLU B OE1 1 
ATOM   1378 O  OE2 . GLU A 1 186 ? 28.463 6.830   13.228  1.00 23.89  -1 181 GLU B OE2 1 
ATOM   1379 N  N   . GLN A 1 187 ? 24.432 5.775   13.651  1.00 22.59  ?  182 GLN B N   1 
ATOM   1380 C  CA  . GLN A 1 187 ? 23.755 5.910   12.326  1.00 21.89  ?  182 GLN B CA  1 
ATOM   1381 C  C   . GLN A 1 187 ? 22.347 5.299   12.363  1.00 23.01  ?  182 GLN B C   1 
ATOM   1382 O  O   . GLN A 1 187 ? 22.112 4.388   13.194  1.00 23.59  ?  182 GLN B O   1 
ATOM   1383 C  CB  . GLN A 1 187 ? 24.541 5.186   11.239  1.00 21.15  ?  182 GLN B CB  1 
ATOM   1384 C  CG  . GLN A 1 187 ? 25.922 5.759   10.969  1.00 22.08  ?  182 GLN B CG  1 
ATOM   1385 C  CD  . GLN A 1 187 ? 25.877 7.216   10.599  1.00 22.63  ?  182 GLN B CD  1 
ATOM   1386 O  OE1 . GLN A 1 187 ? 25.098 7.637   9.742   1.00 26.69  ?  182 GLN B OE1 1 
ATOM   1387 N  NE2 . GLN A 1 187 ? 26.719 7.997   11.251  1.00 21.22  ?  182 GLN B NE2 1 
ATOM   1388 N  N   . GLN A 1 188 ? 21.481 5.746   11.446  1.00 25.54  ?  183 GLN B N   1 
ATOM   1389 C  CA  . GLN A 1 188 ? 20.129 5.164   11.218  1.00 27.32  ?  183 GLN B CA  1 
ATOM   1390 C  C   . GLN A 1 188 ? 20.296 3.704   10.808  1.00 28.74  ?  183 GLN B C   1 
ATOM   1391 O  O   . GLN A 1 188 ? 21.265 3.337   10.144  1.00 28.04  ?  183 GLN B O   1 
ATOM   1392 C  CB  . GLN A 1 188 ? 19.377 5.977   10.161  1.00 30.79  ?  183 GLN B CB  1 
ATOM   1393 C  CG  . GLN A 1 188 ? 18.959 7.356   10.638  1.00 34.57  ?  183 GLN B CG  1 
ATOM   1394 C  CD  . GLN A 1 188 ? 17.994 7.233   11.794  1.00 40.17  ?  183 GLN B CD  1 
ATOM   1395 O  OE1 . GLN A 1 188 ? 16.935 6.613   11.689  1.00 45.13  ?  183 GLN B OE1 1 
ATOM   1396 N  NE2 . GLN A 1 188 ? 18.374 7.781   12.937  1.00 45.52  ?  183 GLN B NE2 1 
ATOM   1397 N  N   . PRO A 1 189 ? 19.344 2.813   11.153  1.00 28.58  ?  184 PRO B N   1 
ATOM   1398 C  CA  . PRO A 1 189 ? 19.505 1.381   10.894  1.00 29.23  ?  184 PRO B CA  1 
ATOM   1399 C  C   . PRO A 1 189 ? 19.820 0.988   9.447   1.00 29.49  ?  184 PRO B C   1 
ATOM   1400 O  O   . PRO A 1 189 ? 20.613 0.077   9.250   1.00 30.36  ?  184 PRO B O   1 
ATOM   1401 C  CB  . PRO A 1 189 ? 18.131 0.814   11.273  1.00 30.38  ?  184 PRO B CB  1 
ATOM   1402 C  CG  . PRO A 1 189 ? 17.644 1.770   12.320  1.00 29.57  ?  184 PRO B CG  1 
ATOM   1403 C  CD  . PRO A 1 189 ? 18.057 3.127   11.803  1.00 31.05  ?  184 PRO B CD  1 
ATOM   1404 N  N   . ALA A 1 190 ? 19.196 1.647   8.467   1.00 27.79  ?  185 ALA B N   1 
ATOM   1405 C  CA  . ALA A 1 190 ? 19.432 1.347   7.039   1.00 26.06  ?  185 ALA B CA  1 
ATOM   1406 C  C   . ALA A 1 190 ? 20.905 1.655   6.687   1.00 24.69  ?  185 ALA B C   1 
ATOM   1407 O  O   . ALA A 1 190 ? 21.470 0.975   5.834   1.00 22.64  ?  185 ALA B O   1 
ATOM   1408 C  CB  . ALA A 1 190 ? 18.481 2.125   6.181   1.00 28.25  ?  185 ALA B CB  1 
ATOM   1409 N  N   . ILE A 1 191 ? 21.483 2.670   7.319   1.00 23.30  ?  186 ILE B N   1 
ATOM   1410 C  CA  . ILE A 1 191 ? 22.887 3.109   7.081   1.00 25.78  ?  186 ILE B CA  1 
ATOM   1411 C  C   . ILE A 1 191 ? 23.854 2.132   7.781   1.00 23.20  ?  186 ILE B C   1 
ATOM   1412 O  O   . ILE A 1 191 ? 24.917 1.787   7.175   1.00 20.63  ?  186 ILE B O   1 
ATOM   1413 C  CB  . ILE A 1 191 ? 23.091 4.560   7.557   1.00 24.43  ?  186 ILE B CB  1 
ATOM   1414 C  CG1 . ILE A 1 191 ? 22.051 5.534   7.004   1.00 26.38  ?  186 ILE B CG1 1 
ATOM   1415 C  CG2 . ILE A 1 191 ? 24.497 5.008   7.225   1.00 24.07  ?  186 ILE B CG2 1 
ATOM   1416 C  CD1 . ILE A 1 191 ? 21.981 5.578   5.488   1.00 27.52  ?  186 ILE B CD1 1 
ATOM   1417 N  N   . ARG A 1 192 ? 23.529 1.669   8.985   1.00 21.95  ?  187 ARG B N   1 
ATOM   1418 C  CA  . ARG A 1 192 ? 24.355 0.655   9.710   1.00 24.40  ?  187 ARG B CA  1 
ATOM   1419 C  C   . ARG A 1 192 ? 24.457 -0.598  8.836   1.00 23.63  ?  187 ARG B C   1 
ATOM   1420 O  O   . ARG A 1 192 ? 25.570 -1.174  8.693   1.00 18.96  ?  187 ARG B O   1 
ATOM   1421 C  CB  . ARG A 1 192 ? 23.763 0.177   11.044  1.00 26.66  ?  187 ARG B CB  1 
ATOM   1422 C  CG  . ARG A 1 192 ? 23.526 1.255   12.083  1.00 31.43  ?  187 ARG B CG  1 
ATOM   1423 C  CD  . ARG A 1 192 ? 23.153 0.611   13.423  1.00 33.43  ?  187 ARG B CD  1 
ATOM   1424 N  NE  . ARG A 1 192 ? 22.269 1.510   14.131  1.00 41.40  ?  187 ARG B NE  1 
ATOM   1425 C  CZ  . ARG A 1 192 ? 20.969 1.314   14.336  1.00 43.59  ?  187 ARG B CZ  1 
ATOM   1426 N  NH1 . ARG A 1 192 ? 20.389 0.194   13.944  1.00 43.07  ?  187 ARG B NH1 1 
ATOM   1427 N  NH2 . ARG A 1 192 ? 20.262 2.232   14.973  1.00 45.28  ?  187 ARG B NH2 1 
ATOM   1428 N  N   . ARG A 1 193 ? 23.327 -1.012  8.262   1.00 22.25  ?  188 ARG B N   1 
ATOM   1429 C  CA  . ARG A 1 193 ? 23.268 -2.170  7.341   1.00 23.43  ?  188 ARG B CA  1 
ATOM   1430 C  C   . ARG A 1 193 ? 24.183 -1.943  6.125   1.00 20.27  ?  188 ARG B C   1 
ATOM   1431 O  O   . ARG A 1 193 ? 24.876 -2.915  5.745   1.00 20.16  ?  188 ARG B O   1 
ATOM   1432 C  CB  . ARG A 1 193 ? 21.820 -2.384  6.910   1.00 27.03  ?  188 ARG B CB  1 
ATOM   1433 C  CG  . ARG A 1 193 ? 21.573 -3.668  6.137   1.00 33.38  ?  188 ARG B CG  1 
ATOM   1434 C  CD  . ARG A 1 193 ? 20.070 -3.862  5.975   1.00 36.42  ?  188 ARG B CD  1 
ATOM   1435 N  NE  . ARG A 1 193 ? 19.763 -4.614  4.773   1.00 40.00  ?  188 ARG B NE  1 
ATOM   1436 C  CZ  . ARG A 1 193 ? 19.805 -5.939  4.668   1.00 45.34  ?  188 ARG B CZ  1 
ATOM   1437 N  NH1 . ARG A 1 193 ? 20.156 -6.692  5.702   1.00 47.02  ?  188 ARG B NH1 1 
ATOM   1438 N  NH2 . ARG A 1 193 ? 19.510 -6.502  3.507   1.00 43.58  ?  188 ARG B NH2 1 
ATOM   1439 N  N   . ARG A 1 194 ? 24.177 -0.739  5.533   1.00 19.14  ?  189 ARG B N   1 
ATOM   1440 C  CA  . ARG A 1 194 ? 25.040 -0.423  4.375   1.00 21.36  ?  189 ARG B CA  1 
ATOM   1441 C  C   . ARG A 1 194 ? 26.516 -0.580  4.802   1.00 19.52  ?  189 ARG B C   1 
ATOM   1442 O  O   . ARG A 1 194 ? 27.304 -1.182  4.044   1.00 18.11  ?  189 ARG B O   1 
ATOM   1443 C  CB  . ARG A 1 194 ? 24.774 0.973   3.824   1.00 22.18  ?  189 ARG B CB  1 
ATOM   1444 C  CG  . ARG A 1 194 ? 23.472 1.079   3.045   1.00 25.00  ?  189 ARG B CG  1 
ATOM   1445 C  CD  . ARG A 1 194 ? 23.225 2.484   2.544   1.00 26.03  ?  189 ARG B CD  1 
ATOM   1446 N  NE  . ARG A 1 194 ? 21.828 2.558   2.159   1.00 28.31  ?  189 ARG B NE  1 
ATOM   1447 C  CZ  . ARG A 1 194 ? 21.172 3.663   1.892   1.00 30.27  ?  189 ARG B CZ  1 
ATOM   1448 N  NH1 . ARG A 1 194 ? 21.781 4.831   1.945   1.00 27.98  ?  189 ARG B NH1 1 
ATOM   1449 N  NH2 . ARG A 1 194 ? 19.885 3.589   1.579   1.00 34.74  ?  189 ARG B NH2 1 
ATOM   1450 N  N   . VAL A 1 195 ? 26.881 -0.101  5.981   1.00 18.30  ?  190 VAL B N   1 
ATOM   1451 C  CA  . VAL A 1 195 ? 28.301 -0.194  6.454   1.00 17.93  ?  190 VAL B CA  1 
ATOM   1452 C  C   . VAL A 1 195 ? 28.636 -1.678  6.659   1.00 17.77  ?  190 VAL B C   1 
ATOM   1453 O  O   . VAL A 1 195 ? 29.706 -2.132  6.207   1.00 16.50  ?  190 VAL B O   1 
ATOM   1454 C  CB  . VAL A 1 195 ? 28.535 0.635   7.735   1.00 18.41  ?  190 VAL B CB  1 
ATOM   1455 C  CG1 . VAL A 1 195 ? 29.929 0.406   8.298   1.00 18.42  ?  190 VAL B CG1 1 
ATOM   1456 C  CG2 . VAL A 1 195 ? 28.286 2.130   7.504   1.00 19.77  ?  190 VAL B CG2 1 
ATOM   1457 N  N   . ARG A 1 196 ? 27.739 -2.434  7.299   1.00 18.45  ?  191 ARG B N   1 
ATOM   1458 C  CA  . ARG A 1 196 ? 27.959 -3.872  7.621   1.00 20.69  ?  191 ARG B CA  1 
ATOM   1459 C  C   . ARG A 1 196 ? 28.159 -4.656  6.319   1.00 20.34  ?  191 ARG B C   1 
ATOM   1460 O  O   . ARG A 1 196 ? 29.149 -5.449  6.246   1.00 20.11  ?  191 ARG B O   1 
ATOM   1461 C  CB  . ARG A 1 196 ? 26.799 -4.459  8.428   1.00 21.34  ?  191 ARG B CB  1 
ATOM   1462 C  CG  . ARG A 1 196 ? 26.977 -5.922  8.792   1.00 24.73  ?  191 ARG B CG  1 
ATOM   1463 C  CD  . ARG A 1 196 ? 25.955 -6.393  9.803   1.00 27.76  ?  191 ARG B CD  1 
ATOM   1464 N  NE  . ARG A 1 196 ? 24.588 -6.132  9.360   1.00 31.84  ?  191 ARG B NE  1 
ATOM   1465 C  CZ  . ARG A 1 196 ? 23.857 -6.933  8.572   1.00 34.67  ?  191 ARG B CZ  1 
ATOM   1466 N  NH1 . ARG A 1 196 ? 24.350 -8.069  8.114   1.00 35.58  ?  191 ARG B NH1 1 
ATOM   1467 N  NH2 . ARG A 1 196 ? 22.623 -6.592  8.254   1.00 34.32  ?  191 ARG B NH2 1 
ATOM   1468 N  N   . HIS A 1 197 ? 27.268 -4.464  5.332   1.00 20.67  ?  192 HIS B N   1 
ATOM   1469 C  CA  . HIS A 1 197 ? 27.376 -5.149  4.010   1.00 20.50  ?  192 HIS B CA  1 
ATOM   1470 C  C   . HIS A 1 197 ? 28.669 -4.719  3.304   1.00 20.61  ?  192 HIS B C   1 
ATOM   1471 O  O   . HIS A 1 197 ? 29.368 -5.609  2.797   1.00 20.06  ?  192 HIS B O   1 
ATOM   1472 C  CB  . HIS A 1 197 ? 26.132 -4.926  3.160   1.00 23.67  ?  192 HIS B CB  1 
ATOM   1473 C  CG  . HIS A 1 197 ? 24.962 -5.682  3.681   1.00 23.51  ?  192 HIS B CG  1 
ATOM   1474 N  ND1 . HIS A 1 197 ? 25.097 -6.905  4.278   1.00 26.69  ?  192 HIS B ND1 1 
ATOM   1475 C  CD2 . HIS A 1 197 ? 23.639 -5.423  3.650   1.00 27.36  ?  192 HIS B CD2 1 
ATOM   1476 C  CE1 . HIS A 1 197 ? 23.914 -7.342  4.662   1.00 26.34  ?  192 HIS B CE1 1 
ATOM   1477 N  NE2 . HIS A 1 197 ? 23.013 -6.462  4.295   1.00 25.57  ?  192 HIS B NE2 1 
ATOM   1478 N  N   . SER A 1 198 ? 29.013 -3.425  3.318   1.00 20.18  ?  193 SER B N   1 
ATOM   1479 C  CA  . SER A 1 198 ? 30.278 -2.948  2.694   1.00 20.30  ?  193 SER B CA  1 
ATOM   1480 C  C   . SER A 1 198 ? 31.455 -3.695  3.339   1.00 22.35  ?  193 SER B C   1 
ATOM   1481 O  O   . SER A 1 198 ? 32.244 -4.366  2.605   1.00 22.75  ?  193 SER B O   1 
ATOM   1482 C  CB  . SER A 1 198 ? 30.396 -1.462  2.786   1.00 21.43  ?  193 SER B CB  1 
ATOM   1483 O  OG  . SER A 1 198 ? 31.545 -1.007  2.071   1.00 22.64  ?  193 SER B OG  1 
ATOM   1484 N  N   . PHE A 1 199 ? 31.525 -3.699  4.670   1.00 19.31  ?  194 PHE B N   1 
ATOM   1485 C  CA  . PHE A 1 199 ? 32.683 -4.268  5.412   1.00 17.68  ?  194 PHE B CA  1 
ATOM   1486 C  C   . PHE A 1 199 ? 32.723 -5.790  5.246   1.00 17.31  ?  194 PHE B C   1 
ATOM   1487 O  O   . PHE A 1 199 ? 33.808 -6.333  5.334   1.00 16.15  ?  194 PHE B O   1 
ATOM   1488 C  CB  . PHE A 1 199 ? 32.670 -3.804  6.866   1.00 17.80  ?  194 PHE B CB  1 
ATOM   1489 C  CG  . PHE A 1 199 ? 33.090 -2.375  7.129   1.00 18.44  ?  194 PHE B CG  1 
ATOM   1490 C  CD1 . PHE A 1 199 ? 33.738 -1.608  6.165   1.00 20.28  ?  194 PHE B CD1 1 
ATOM   1491 C  CD2 . PHE A 1 199 ? 32.922 -1.824  8.389   1.00 19.57  ?  194 PHE B CD2 1 
ATOM   1492 C  CE1 . PHE A 1 199 ? 34.192 -0.323  6.455   1.00 20.75  ?  194 PHE B CE1 1 
ATOM   1493 C  CE2 . PHE A 1 199 ? 33.369 -0.535  8.671   1.00 19.24  ?  194 PHE B CE2 1 
ATOM   1494 C  CZ  . PHE A 1 199 ? 33.987 0.220   7.695   1.00 17.83  ?  194 PHE B CZ  1 
ATOM   1495 N  N   . GLY A 1 200 ? 31.597 -6.451  4.955   1.00 17.91  ?  195 GLY B N   1 
ATOM   1496 C  CA  . GLY A 1 200 ? 31.567 -7.894  4.683   1.00 18.61  ?  195 GLY B CA  1 
ATOM   1497 C  C   . GLY A 1 200 ? 32.194 -8.306  3.363   1.00 19.12  ?  195 GLY B C   1 
ATOM   1498 O  O   . GLY A 1 200 ? 32.380 -9.508  3.178   1.00 20.91  ?  195 GLY B O   1 
ATOM   1499 N  N   . GLY A 1 201 ? 32.529 -7.366  2.479   1.00 19.72  ?  196 GLY B N   1 
ATOM   1500 C  CA  . GLY A 1 201 ? 32.996 -7.649  1.111   1.00 20.59  ?  196 GLY B CA  1 
ATOM   1501 C  C   . GLY A 1 201 ? 34.493 -7.561  0.965   1.00 22.89  ?  196 GLY B C   1 
ATOM   1502 O  O   . GLY A 1 201 ? 34.960 -7.648  -0.182  1.00 23.94  ?  196 GLY B O   1 
ATOM   1503 N  N   . ALA A 1 202 ? 35.237 -7.423  2.058   1.00 20.27  ?  197 ALA B N   1 
ATOM   1504 C  CA  . ALA A 1 202 ? 36.714 -7.503  2.031   1.00 20.99  ?  197 ALA B CA  1 
ATOM   1505 C  C   . ALA A 1 202 ? 37.206 -8.136  3.317   1.00 20.29  ?  197 ALA B C   1 
ATOM   1506 O  O   . ALA A 1 202 ? 36.725 -7.782  4.408   1.00 20.55  ?  197 ALA B O   1 
ATOM   1507 C  CB  . ALA A 1 202 ? 37.346 -6.139  1.838   1.00 22.12  ?  197 ALA B CB  1 
ATOM   1508 N  N   . GLU A 1 203 ? 38.226 -8.977  3.206   1.00 21.51  ?  198 GLU B N   1 
ATOM   1509 C  CA  . GLU A 1 203 ? 38.775 -9.667  4.384   1.00 22.19  ?  198 GLU B CA  1 
ATOM   1510 C  C   . GLU A 1 203 ? 39.218 -8.628  5.419   1.00 20.96  ?  198 GLU B C   1 
ATOM   1511 O  O   . GLU A 1 203 ? 39.010 -8.882  6.599   1.00 19.66  ?  198 GLU B O   1 
ATOM   1512 C  CB  . GLU A 1 203 ? 39.891 -10.625 3.983   1.00 24.93  ?  198 GLU B CB  1 
ATOM   1513 C  CG  . GLU A 1 203 ? 40.328 -11.516 5.122   1.00 26.58  ?  198 GLU B CG  1 
ATOM   1514 C  CD  . GLU A 1 203 ? 39.288 -12.441 5.740   1.00 33.57  ?  198 GLU B CD  1 
ATOM   1515 O  OE1 . GLU A 1 203 ? 38.161 -12.552 5.188   1.00 33.74  ?  198 GLU B OE1 1 
ATOM   1516 O  OE2 . GLU A 1 203 ? 39.592 -13.024 6.802   1.00 33.74  -1 198 GLU B OE2 1 
ATOM   1517 N  N   . ALA A 1 204 ? 39.823 -7.529  4.993   1.00 19.71  ?  199 ALA B N   1 
ATOM   1518 C  CA  . ALA A 1 204 ? 40.415 -6.505  5.889   1.00 22.40  ?  199 ALA B CA  1 
ATOM   1519 C  C   . ALA A 1 204 ? 39.366 -5.964  6.865   1.00 21.74  ?  199 ALA B C   1 
ATOM   1520 O  O   . ALA A 1 204 ? 39.724 -5.546  7.970   1.00 23.37  ?  199 ALA B O   1 
ATOM   1521 C  CB  . ALA A 1 204 ? 41.010 -5.400  5.072   1.00 25.58  ?  199 ALA B CB  1 
ATOM   1522 N  N   . THR A 1 205 ? 38.106 -5.941  6.453   1.00 19.58  ?  200 THR B N   1 
ATOM   1523 C  CA  . THR A 1 205 ? 36.999 -5.297  7.219   1.00 18.76  ?  200 THR B CA  1 
ATOM   1524 C  C   . THR A 1 205 ? 36.000 -6.325  7.750   1.00 17.53  ?  200 THR B C   1 
ATOM   1525 O  O   . THR A 1 205 ? 35.046 -5.896  8.483   1.00 17.14  ?  200 THR B O   1 
ATOM   1526 C  CB  . THR A 1 205 ? 36.355 -4.229  6.331   1.00 17.51  ?  200 THR B CB  1 
ATOM   1527 O  OG1 . THR A 1 205 ? 35.922 -4.838  5.107   1.00 19.77  ?  200 THR B OG1 1 
ATOM   1528 C  CG2 . THR A 1 205 ? 37.311 -3.083  6.053   1.00 18.23  ?  200 THR B CG2 1 
ATOM   1529 N  N   . ARG A 1 206 ? 36.188 -7.610  7.439   1.00 18.75  ?  201 ARG B N   1 
ATOM   1530 C  CA  . ARG A 1 206 ? 35.211 -8.669  7.779   1.00 20.60  ?  201 ARG B CA  1 
ATOM   1531 C  C   . ARG A 1 206 ? 35.018 -8.788  9.289   1.00 19.35  ?  201 ARG B C   1 
ATOM   1532 O  O   . ARG A 1 206 ? 33.864 -8.999  9.707   1.00 16.05  ?  201 ARG B O   1 
ATOM   1533 C  CB  . ARG A 1 206 ? 35.602 -10.034 7.221   1.00 22.27  ?  201 ARG B CB  1 
ATOM   1534 C  CG  . ARG A 1 206 ? 34.456 -11.034 7.317   1.00 24.30  ?  201 ARG B CG  1 
ATOM   1535 C  CD  . ARG A 1 206 ? 34.624 -12.221 6.383   1.00 24.28  ?  201 ARG B CD  1 
ATOM   1536 N  NE  . ARG A 1 206 ? 35.841 -12.962 6.644   1.00 28.82  ?  201 ARG B NE  1 
ATOM   1537 C  CZ  . ARG A 1 206 ? 35.985 -13.890 7.583   1.00 31.15  ?  201 ARG B CZ  1 
ATOM   1538 N  NH1 . ARG A 1 206 ? 34.985 -14.163 8.395   1.00 33.74  ?  201 ARG B NH1 1 
ATOM   1539 N  NH2 . ARG A 1 206 ? 37.132 -14.524 7.729   1.00 35.89  ?  201 ARG B NH2 1 
ATOM   1540 N  N   . ALA A 1 207 ? 36.084 -8.677  10.084  1.00 16.49  ?  202 ALA B N   1 
ATOM   1541 C  CA  . ALA A 1 207 ? 35.974 -8.813  11.554  1.00 18.63  ?  202 ALA B CA  1 
ATOM   1542 C  C   . ALA A 1 207 ? 35.085 -7.693  12.088  1.00 17.21  ?  202 ALA B C   1 
ATOM   1543 O  O   . ALA A 1 207 ? 34.345 -7.979  13.060  1.00 18.12  ?  202 ALA B O   1 
ATOM   1544 C  CB  . ALA A 1 207 ? 37.324 -8.825  12.228  1.00 18.63  ?  202 ALA B CB  1 
ATOM   1545 N  N   . VAL A 1 208 ? 35.164 -6.483  11.509  1.00 17.13  ?  203 VAL B N   1 
ATOM   1546 C  CA  . VAL A 1 208 ? 34.321 -5.339  11.956  1.00 17.87  ?  203 VAL B CA  1 
ATOM   1547 C  C   . VAL A 1 208 ? 32.862 -5.670  11.629  1.00 17.38  ?  203 VAL B C   1 
ATOM   1548 O  O   . VAL A 1 208 ? 32.005 -5.495  12.493  1.00 17.36  ?  203 VAL B O   1 
ATOM   1549 C  CB  . VAL A 1 208 ? 34.740 -3.980  11.372  1.00 17.88  ?  203 VAL B CB  1 
ATOM   1550 C  CG1 . VAL A 1 208 ? 33.731 -2.926  11.791  1.00 18.72  ?  203 VAL B CG1 1 
ATOM   1551 C  CG2 . VAL A 1 208 ? 36.128 -3.569  11.849  1.00 17.61  ?  203 VAL B CG2 1 
ATOM   1552 N  N   . ALA A 1 209 ? 32.604 -6.181  10.425  1.00 16.89  ?  204 ALA B N   1 
ATOM   1553 C  CA  . ALA A 1 209 ? 31.242 -6.593  9.979   1.00 16.77  ?  204 ALA B CA  1 
ATOM   1554 C  C   . ALA A 1 209 ? 30.679 -7.637  10.948  1.00 17.67  ?  204 ALA B C   1 
ATOM   1555 O  O   . ALA A 1 209 ? 29.446 -7.578  11.270  1.00 19.77  ?  204 ALA B O   1 
ATOM   1556 C  CB  . ALA A 1 209 ? 31.289 -7.144  8.568   1.00 16.24  ?  204 ALA B CB  1 
ATOM   1557 N  N   . GLY A 1 210 ? 31.512 -8.587  11.368  1.00 18.88  ?  205 GLY B N   1 
ATOM   1558 C  CA  . GLY A 1 210 ? 31.130 -9.684  12.284  1.00 20.11  ?  205 GLY B CA  1 
ATOM   1559 C  C   . GLY A 1 210 ? 30.625 -9.163  13.630  1.00 21.07  ?  205 GLY B C   1 
ATOM   1560 O  O   . GLY A 1 210 ? 29.537 -9.630  14.130  1.00 20.29  ?  205 GLY B O   1 
ATOM   1561 N  N   . LEU A 1 211 ? 31.337 -8.190  14.206  1.00 20.18  ?  206 LEU B N   1 
ATOM   1562 C  CA  . LEU A 1 211 ? 30.899 -7.524  15.458  1.00 19.46  ?  206 LEU B CA  1 
ATOM   1563 C  C   . LEU A 1 211 ? 29.597 -6.763  15.187  1.00 20.62  ?  206 LEU B C   1 
ATOM   1564 O  O   . LEU A 1 211 ? 28.666 -6.881  16.012  1.00 21.65  ?  206 LEU B O   1 
ATOM   1565 C  CB  . LEU A 1 211 ? 32.027 -6.626  15.970  1.00 19.18  ?  206 LEU B CB  1 
ATOM   1566 C  CG  . LEU A 1 211 ? 33.253 -7.373  16.495  1.00 19.53  ?  206 LEU B CG  1 
ATOM   1567 C  CD1 . LEU A 1 211 ? 34.350 -6.397  16.825  1.00 22.92  ?  206 LEU B CD1 1 
ATOM   1568 C  CD2 . LEU A 1 211 ? 32.922 -8.199  17.730  1.00 21.74  ?  206 LEU B CD2 1 
ATOM   1569 N  N   . MET A 1 212 ? 29.503 -6.032  14.071  1.00 18.83  ?  207 MET B N   1 
ATOM   1570 C  CA  . MET A 1 212 ? 28.279 -5.269  13.741  1.00 19.71  ?  207 MET B CA  1 
ATOM   1571 C  C   . MET A 1 212 ? 27.103 -6.247  13.602  1.00 21.37  ?  207 MET B C   1 
ATOM   1572 O  O   . MET A 1 212 ? 25.981 -5.893  14.012  1.00 22.51  ?  207 MET B O   1 
ATOM   1573 C  CB  . MET A 1 212 ? 28.448 -4.466  12.447  1.00 19.61  ?  207 MET B CB  1 
ATOM   1574 C  CG  . MET A 1 212 ? 29.501 -3.377  12.581  1.00 20.67  ?  207 MET B CG  1 
ATOM   1575 S  SD  . MET A 1 212 ? 29.798 -2.412  11.092  1.00 20.28  ?  207 MET B SD  1 
ATOM   1576 C  CE  . MET A 1 212 ? 28.219 -1.544  11.025  1.00 21.35  ?  207 MET B CE  1 
ATOM   1577 N  N   . ASP A 1 213 ? 27.344 -7.435  13.061  1.00 22.29  ?  208 ASP B N   1 
ATOM   1578 C  CA  . ASP A 1 213 ? 26.287 -8.455  12.839  1.00 25.89  ?  208 ASP B CA  1 
ATOM   1579 C  C   . ASP A 1 213 ? 25.801 -9.037  14.180  1.00 27.85  ?  208 ASP B C   1 
ATOM   1580 O  O   . ASP A 1 213 ? 24.660 -9.497  14.215  1.00 26.81  ?  208 ASP B O   1 
ATOM   1581 C  CB  . ASP A 1 213 ? 26.774 -9.554  11.899  1.00 29.53  ?  208 ASP B CB  1 
ATOM   1582 C  CG  . ASP A 1 213 ? 25.629 -10.319 11.256  1.00 36.61  ?  208 ASP B CG  1 
ATOM   1583 O  OD1 . ASP A 1 213 ? 25.797 -11.525 11.026  1.00 39.14  ?  208 ASP B OD1 1 
ATOM   1584 O  OD2 . ASP A 1 213 ? 24.582 -9.681  10.959  1.00 39.76  -1 208 ASP B OD2 1 
ATOM   1585 N  N   . ARG A 1 214 ? 26.635 -9.035  15.221  1.00 25.03  ?  209 ARG B N   1 
ATOM   1586 C  CA  . ARG A 1 214 ? 26.343 -9.574  16.580  1.00 28.25  ?  209 ARG B CA  1 
ATOM   1587 C  C   . ARG A 1 214 ? 25.701 -8.508  17.482  1.00 29.06  ?  209 ARG B C   1 
ATOM   1588 O  O   . ARG A 1 214 ? 25.298 -8.869  18.607  1.00 27.65  ?  209 ARG B O   1 
ATOM   1589 C  CB  . ARG A 1 214 ? 27.634 -10.136 17.193  1.00 29.70  ?  209 ARG B CB  1 
ATOM   1590 C  CG  . ARG A 1 214 ? 28.069 -11.439 16.543  1.00 32.03  ?  209 ARG B CG  1 
ATOM   1591 C  CD  . ARG A 1 214 ? 29.120 -12.235 17.294  1.00 36.97  ?  209 ARG B CD  1 
ATOM   1592 N  NE  . ARG A 1 214 ? 30.475 -11.678 17.232  1.00 44.49  ?  209 ARG B NE  1 
ATOM   1593 C  CZ  . ARG A 1 214 ? 31.317 -11.741 16.183  1.00 46.81  ?  209 ARG B CZ  1 
ATOM   1594 N  NH1 . ARG A 1 214 ? 32.525 -11.208 16.272  1.00 41.96  ?  209 ARG B NH1 1 
ATOM   1595 N  NH2 . ARG A 1 214 ? 30.964 -12.327 15.051  1.00 50.37  ?  209 ARG B NH2 1 
ATOM   1596 N  N   . LEU A 1 215 ? 25.554 -7.257  17.033  1.00 27.35  ?  210 LEU B N   1 
ATOM   1597 C  CA  . LEU A 1 215 ? 24.864 -6.214  17.834  1.00 29.25  ?  210 LEU B CA  1 
ATOM   1598 C  C   . LEU A 1 215 ? 23.366 -6.498  17.830  1.00 34.86  ?  210 LEU B C   1 
ATOM   1599 O  O   . LEU A 1 215 ? 22.811 -6.850  16.789  1.00 32.88  ?  210 LEU B O   1 
ATOM   1600 C  CB  . LEU A 1 215 ? 25.117 -4.823  17.261  1.00 29.87  ?  210 LEU B CB  1 
ATOM   1601 C  CG  . LEU A 1 215 ? 26.547 -4.303  17.368  1.00 28.44  ?  210 LEU B CG  1 
ATOM   1602 C  CD1 . LEU A 1 215 ? 26.687 -3.021  16.586  1.00 27.91  ?  210 LEU B CD1 1 
ATOM   1603 C  CD2 . LEU A 1 215 ? 26.977 -4.111  18.816  1.00 30.62  ?  210 LEU B CD2 1 
ATOM   1604 N  N   . PRO A 1 216 ? 22.665 -6.275  18.966  1.00 38.84  ?  211 PRO B N   1 
ATOM   1605 C  CA  . PRO A 1 216 ? 21.242 -6.609  19.074  1.00 40.68  ?  211 PRO B CA  1 
ATOM   1606 C  C   . PRO A 1 216 ? 20.375 -5.992  17.959  1.00 39.64  ?  211 PRO B C   1 
ATOM   1607 O  O   . PRO A 1 216 ? 20.488 -4.809  17.667  1.00 45.41  ?  211 PRO B O   1 
ATOM   1608 C  CB  . PRO A 1 216 ? 20.828 -6.068  20.460  1.00 41.45  ?  211 PRO B CB  1 
ATOM   1609 C  CG  . PRO A 1 216 ? 21.956 -5.142  20.892  1.00 42.16  ?  211 PRO B CG  1 
ATOM   1610 C  CD  . PRO A 1 216 ? 23.196 -5.671  20.199  1.00 41.91  ?  211 PRO B CD  1 
ATOM   1611 N  N   . ALA B 1 5   ? 60.951 8.704   26.303  1.00 36.22  ?  0   ALA D N   1 
ATOM   1612 C  CA  . ALA B 1 5   ? 61.610 7.784   25.329  1.00 37.25  ?  0   ALA D CA  1 
ATOM   1613 C  C   . ALA B 1 5   ? 60.965 6.383   25.352  1.00 36.66  ?  0   ALA D C   1 
ATOM   1614 O  O   . ALA B 1 5   ? 60.124 6.021   26.239  1.00 34.25  ?  0   ALA D O   1 
ATOM   1615 C  CB  . ALA B 1 5   ? 63.116 7.732   25.526  1.00 32.95  ?  0   ALA D CB  1 
ATOM   1616 N  N   . MET B 1 6   ? 61.238 5.664   24.278  1.00 31.19  ?  1   MET D N   1 
ATOM   1617 C  CA  . MET B 1 6   ? 60.632 4.343   24.023  1.00 29.81  ?  1   MET D CA  1 
ATOM   1618 C  C   . MET B 1 6   ? 61.796 3.367   23.966  1.00 27.43  ?  1   MET D C   1 
ATOM   1619 O  O   . MET B 1 6   ? 62.825 3.721   23.366  1.00 25.94  ?  1   MET D O   1 
ATOM   1620 C  CB  . MET B 1 6   ? 59.887 4.387   22.692  1.00 30.23  ?  1   MET D CB  1 
ATOM   1621 C  CG  . MET B 1 6   ? 59.335 3.076   22.229  1.00 29.85  ?  1   MET D CG  1 
ATOM   1622 S  SD  . MET B 1 6   ? 58.712 3.272   20.542  1.00 30.40  ?  1   MET D SD  1 
ATOM   1623 C  CE  . MET B 1 6   ? 57.903 1.684   20.405  1.00 30.88  ?  1   MET D CE  1 
ATOM   1624 N  N   . PHE B 1 7   ? 61.634 2.192   24.552  1.00 23.85  ?  2   PHE D N   1 
ATOM   1625 C  CA  . PHE B 1 7   ? 62.687 1.158   24.540  1.00 26.30  ?  2   PHE D CA  1 
ATOM   1626 C  C   . PHE B 1 7   ? 62.582 0.381   23.234  1.00 23.86  ?  2   PHE D C   1 
ATOM   1627 O  O   . PHE B 1 7   ? 61.539 -0.240  22.993  1.00 24.67  ?  2   PHE D O   1 
ATOM   1628 C  CB  . PHE B 1 7   ? 62.505 0.164   25.680  1.00 24.58  ?  2   PHE D CB  1 
ATOM   1629 C  CG  . PHE B 1 7   ? 63.607 -0.846  25.702  1.00 25.97  ?  2   PHE D CG  1 
ATOM   1630 C  CD1 . PHE B 1 7   ? 64.915 -0.419  25.842  1.00 26.17  ?  2   PHE D CD1 1 
ATOM   1631 C  CD2 . PHE B 1 7   ? 63.350 -2.194  25.538  1.00 26.67  ?  2   PHE D CD2 1 
ATOM   1632 C  CE1 . PHE B 1 7   ? 65.949 -1.342  25.874  1.00 28.49  ?  2   PHE D CE1 1 
ATOM   1633 C  CE2 . PHE B 1 7   ? 64.389 -3.110  25.551  1.00 30.55  ?  2   PHE D CE2 1 
ATOM   1634 C  CZ  . PHE B 1 7   ? 65.682 -2.680  25.722  1.00 28.11  ?  2   PHE D CZ  1 
ATOM   1635 N  N   . VAL B 1 8   ? 63.600 0.430   22.395  1.00 23.03  ?  3   VAL D N   1 
ATOM   1636 C  CA  . VAL B 1 8   ? 63.608 -0.348  21.132  1.00 20.55  ?  3   VAL D CA  1 
ATOM   1637 C  C   . VAL B 1 8   ? 64.939 -1.061  21.049  1.00 21.33  ?  3   VAL D C   1 
ATOM   1638 O  O   . VAL B 1 8   ? 65.962 -0.392  20.871  1.00 19.96  ?  3   VAL D O   1 
ATOM   1639 C  CB  . VAL B 1 8   ? 63.405 0.541   19.898  1.00 19.77  ?  3   VAL D CB  1 
ATOM   1640 C  CG1 . VAL B 1 8   ? 63.385 -0.303  18.646  1.00 19.49  ?  3   VAL D CG1 1 
ATOM   1641 C  CG2 . VAL B 1 8   ? 62.151 1.399   20.028  1.00 20.15  ?  3   VAL D CG2 1 
ATOM   1642 N  N   . PRO B 1 9   ? 64.951 -2.404  21.150  1.00 21.34  ?  4   PRO D N   1 
ATOM   1643 C  CA  . PRO B 1 9   ? 66.187 -3.161  20.953  1.00 24.29  ?  4   PRO D CA  1 
ATOM   1644 C  C   . PRO B 1 9   ? 66.810 -2.868  19.590  1.00 24.85  ?  4   PRO D C   1 
ATOM   1645 O  O   . PRO B 1 9   ? 66.078 -2.776  18.609  1.00 20.45  ?  4   PRO D O   1 
ATOM   1646 C  CB  . PRO B 1 9   ? 65.747 -4.631  21.046  1.00 23.41  ?  4   PRO D CB  1 
ATOM   1647 C  CG  . PRO B 1 9   ? 64.474 -4.587  21.897  1.00 24.63  ?  4   PRO D CG  1 
ATOM   1648 C  CD  . PRO B 1 9   ? 63.820 -3.276  21.506  1.00 23.14  ?  4   PRO D CD  1 
ATOM   1649 N  N   . GLY B 1 10  ? 68.148 -2.835  19.545  1.00 26.15  ?  5   GLY D N   1 
ATOM   1650 C  CA  . GLY B 1 10  ? 68.929 -2.479  18.343  1.00 27.31  ?  5   GLY D CA  1 
ATOM   1651 C  C   . GLY B 1 10  ? 68.379 -3.105  17.064  1.00 25.34  ?  5   GLY D C   1 
ATOM   1652 O  O   . GLY B 1 10  ? 68.140 -2.386  16.099  1.00 23.03  ?  5   GLY D O   1 
ATOM   1653 N  N   . PRO B 1 11  ? 68.143 -4.438  17.033  1.00 24.29  ?  6   PRO D N   1 
ATOM   1654 C  CA  . PRO B 1 11  ? 67.716 -5.135  15.822  1.00 23.66  ?  6   PRO D CA  1 
ATOM   1655 C  C   . PRO B 1 11  ? 66.338 -4.691  15.286  1.00 20.71  ?  6   PRO D C   1 
ATOM   1656 O  O   . PRO B 1 11  ? 66.056 -4.955  14.148  1.00 16.60  ?  6   PRO D O   1 
ATOM   1657 C  CB  . PRO B 1 11  ? 67.641 -6.607  16.269  1.00 25.20  ?  6   PRO D CB  1 
ATOM   1658 C  CG  . PRO B 1 11  ? 68.527 -6.690  17.487  1.00 27.60  ?  6   PRO D CG  1 
ATOM   1659 C  CD  . PRO B 1 11  ? 68.311 -5.363  18.170  1.00 26.69  ?  6   PRO D CD  1 
ATOM   1660 N  N   . TYR B 1 12  ? 65.530 -4.012  16.104  1.00 20.43  ?  7   TYR D N   1 
ATOM   1661 C  CA  . TYR B 1 12  ? 64.127 -3.658  15.757  1.00 18.76  ?  7   TYR D CA  1 
ATOM   1662 C  C   . TYR B 1 12  ? 64.040 -2.185  15.296  1.00 21.59  ?  7   TYR D C   1 
ATOM   1663 O  O   . TYR B 1 12  ? 62.917 -1.674  15.065  1.00 20.08  ?  7   TYR D O   1 
ATOM   1664 C  CB  . TYR B 1 12  ? 63.227 -4.003  16.949  1.00 19.32  ?  7   TYR D CB  1 
ATOM   1665 C  CG  . TYR B 1 12  ? 63.247 -5.457  17.363  1.00 18.85  ?  7   TYR D CG  1 
ATOM   1666 C  CD1 . TYR B 1 12  ? 63.460 -6.453  16.422  1.00 20.15  ?  7   TYR D CD1 1 
ATOM   1667 C  CD2 . TYR B 1 12  ? 63.034 -5.864  18.674  1.00 20.54  ?  7   TYR D CD2 1 
ATOM   1668 C  CE1 . TYR B 1 12  ? 63.515 -7.787  16.786  1.00 19.13  ?  7   TYR D CE1 1 
ATOM   1669 C  CE2 . TYR B 1 12  ? 63.077 -7.200  19.053  1.00 20.42  ?  7   TYR D CE2 1 
ATOM   1670 C  CZ  . TYR B 1 12  ? 63.324 -8.170  18.093  1.00 20.78  ?  7   TYR D CZ  1 
ATOM   1671 O  OH  . TYR B 1 12  ? 63.353 -9.517  18.375  1.00 22.27  ?  7   TYR D OH  1 
ATOM   1672 N  N   . HIS B 1 13  ? 65.175 -1.489  15.142  1.00 20.15  ?  8   HIS D N   1 
ATOM   1673 C  CA  . HIS B 1 13  ? 65.195 -0.098  14.613  1.00 22.73  ?  8   HIS D CA  1 
ATOM   1674 C  C   . HIS B 1 13  ? 64.773 -0.107  13.148  1.00 19.91  ?  8   HIS D C   1 
ATOM   1675 O  O   . HIS B 1 13  ? 65.157 -1.025  12.410  1.00 22.63  ?  8   HIS D O   1 
ATOM   1676 C  CB  . HIS B 1 13  ? 66.562 0.556   14.822  1.00 24.33  ?  8   HIS D CB  1 
ATOM   1677 C  CG  . HIS B 1 13  ? 66.833 0.868   16.244  1.00 29.62  ?  8   HIS D CG  1 
ATOM   1678 N  ND1 . HIS B 1 13  ? 67.391 2.066   16.637  1.00 39.94  ?  8   HIS D ND1 1 
ATOM   1679 C  CD2 . HIS B 1 13  ? 66.557 0.192   17.376  1.00 30.52  ?  8   HIS D CD2 1 
ATOM   1680 C  CE1 . HIS B 1 13  ? 67.463 2.103   17.955  1.00 39.57  ?  8   HIS D CE1 1 
ATOM   1681 N  NE2 . HIS B 1 13  ? 66.957 0.966   18.428  1.00 33.13  ?  8   HIS D NE2 1 
ATOM   1682 N  N   . ALA B 1 14  ? 63.998 0.876   12.729  1.00 20.57  ?  9   ALA D N   1 
ATOM   1683 C  CA  . ALA B 1 14  ? 63.697 1.008   11.292  1.00 22.81  ?  9   ALA D CA  1 
ATOM   1684 C  C   . ALA B 1 14  ? 65.015 1.213   10.545  1.00 23.72  ?  9   ALA D C   1 
ATOM   1685 O  O   . ALA B 1 14  ? 65.953 1.791   11.071  1.00 21.59  ?  9   ALA D O   1 
ATOM   1686 C  CB  . ALA B 1 14  ? 62.701 2.112   11.050  1.00 26.18  ?  9   ALA D CB  1 
ATOM   1687 N  N   . PRO B 1 15  ? 65.144 0.677   9.320   1.00 26.35  ?  10  PRO D N   1 
ATOM   1688 C  CA  . PRO B 1 15  ? 66.295 0.968   8.472   1.00 27.26  ?  10  PRO D CA  1 
ATOM   1689 C  C   . PRO B 1 15  ? 66.467 2.451   8.130   1.00 27.17  ?  10  PRO D C   1 
ATOM   1690 O  O   . PRO B 1 15  ? 67.587 2.840   7.830   1.00 28.56  ?  10  PRO D O   1 
ATOM   1691 C  CB  . PRO B 1 15  ? 65.999 0.284   7.135   1.00 28.07  ?  10  PRO D CB  1 
ATOM   1692 C  CG  . PRO B 1 15  ? 64.827 -0.638  7.400   1.00 30.88  ?  10  PRO D CG  1 
ATOM   1693 C  CD  . PRO B 1 15  ? 64.150 -0.172  8.667   1.00 27.19  ?  10  PRO D CD  1 
ATOM   1694 N  N   . GLU B 1 16  ? 65.372 3.215   8.070   1.00 24.70  ?  11  GLU D N   1 
ATOM   1695 C  CA  . GLU B 1 16  ? 65.359 4.651   7.677   1.00 26.60  ?  11  GLU D CA  1 
ATOM   1696 C  C   . GLU B 1 16  ? 64.283 5.392   8.469   1.00 25.71  ?  11  GLU D C   1 
ATOM   1697 O  O   . GLU B 1 16  ? 63.245 4.768   8.768   1.00 19.58  ?  11  GLU D O   1 
ATOM   1698 C  CB  . GLU B 1 16  ? 64.999 4.882   6.197   1.00 33.77  ?  11  GLU D CB  1 
ATOM   1699 C  CG  . GLU B 1 16  ? 65.796 4.085   5.164   1.00 37.91  ?  11  GLU D CG  1 
ATOM   1700 C  CD  . GLU B 1 16  ? 67.257 4.458   4.949   1.00 44.54  ?  11  GLU D CD  1 
ATOM   1701 O  OE1 . GLU B 1 16  ? 67.613 5.630   5.203   1.00 48.38  ?  11  GLU D OE1 1 
ATOM   1702 O  OE2 . GLU B 1 16  ? 68.045 3.558   4.519   1.00 46.80  -1 11  GLU D OE2 1 
ATOM   1703 N  N   . ASP B 1 17  ? 64.485 6.692   8.695   1.00 23.64  ?  12  ASP D N   1 
ATOM   1704 C  CA  . ASP B 1 17  ? 63.548 7.561   9.439   1.00 23.90  ?  12  ASP D CA  1 
ATOM   1705 C  C   . ASP B 1 17  ? 62.183 7.556   8.744   1.00 23.80  ?  12  ASP D C   1 
ATOM   1706 O  O   . ASP B 1 17  ? 61.166 7.643   9.453   1.00 20.34  ?  12  ASP D O   1 
ATOM   1707 C  CB  . ASP B 1 17  ? 64.078 8.982   9.574   1.00 26.67  ?  12  ASP D CB  1 
ATOM   1708 C  CG  . ASP B 1 17  ? 65.295 9.128   10.471  1.00 28.22  ?  12  ASP D CG  1 
ATOM   1709 O  OD1 . ASP B 1 17  ? 65.385 8.404   11.443  1.00 25.92  ?  12  ASP D OD1 1 
ATOM   1710 O  OD2 . ASP B 1 17  ? 66.138 9.991   10.172  1.00 34.26  -1 12  ASP D OD2 1 
ATOM   1711 N  N   . ARG B 1 18  ? 62.167 7.412   7.422   1.00 22.33  ?  13  ARG D N   1 
ATOM   1712 C  CA  . ARG B 1 18  ? 60.934 7.509   6.610   1.00 24.77  ?  13  ARG D CA  1 
ATOM   1713 C  C   . ARG B 1 18  ? 59.944 6.405   6.999   1.00 21.07  ?  13  ARG D C   1 
ATOM   1714 O  O   . ARG B 1 18  ? 58.716 6.602   6.817   1.00 20.37  ?  13  ARG D O   1 
ATOM   1715 C  CB  . ARG B 1 18  ? 61.265 7.464   5.115   1.00 26.68  ?  13  ARG D CB  1 
ATOM   1716 C  CG  . ARG B 1 18  ? 60.049 7.449   4.207   1.00 33.74  ?  13  ARG D CG  1 
ATOM   1717 C  CD  . ARG B 1 18  ? 59.220 8.702   4.354   1.00 39.17  ?  13  ARG D CD  1 
ATOM   1718 N  NE  . ARG B 1 18  ? 58.173 8.777   3.353   1.00 45.02  ?  13  ARG D NE  1 
ATOM   1719 C  CZ  . ARG B 1 18  ? 58.229 9.488   2.235   1.00 51.05  ?  13  ARG D CZ  1 
ATOM   1720 N  NH1 . ARG B 1 18  ? 59.299 10.214  1.944   1.00 50.72  ?  13  ARG D NH1 1 
ATOM   1721 N  NH2 . ARG B 1 18  ? 57.197 9.461   1.406   1.00 56.20  ?  13  ARG D NH2 1 
ATOM   1722 N  N   . TRP B 1 19  ? 60.427 5.291   7.555   1.00 21.45  ?  14  TRP D N   1 
ATOM   1723 C  CA  . TRP B 1 19  ? 59.520 4.176   7.916   1.00 22.03  ?  14  TRP D CA  1 
ATOM   1724 C  C   . TRP B 1 19  ? 58.575 4.640   9.022   1.00 18.10  ?  14  TRP D C   1 
ATOM   1725 O  O   . TRP B 1 19  ? 57.439 4.130   9.043   1.00 18.20  ?  14  TRP D O   1 
ATOM   1726 C  CB  . TRP B 1 19  ? 60.304 2.953   8.366   1.00 22.29  ?  14  TRP D CB  1 
ATOM   1727 C  CG  . TRP B 1 19  ? 60.892 2.144   7.256   1.00 22.64  ?  14  TRP D CG  1 
ATOM   1728 C  CD1 . TRP B 1 19  ? 61.576 2.574   6.149   1.00 22.58  ?  14  TRP D CD1 1 
ATOM   1729 C  CD2 . TRP B 1 19  ? 60.903 0.713   7.218   1.00 22.06  ?  14  TRP D CD2 1 
ATOM   1730 N  NE1 . TRP B 1 19  ? 61.978 1.501   5.402   1.00 23.52  ?  14  TRP D NE1 1 
ATOM   1731 C  CE2 . TRP B 1 19  ? 61.561 0.343   6.022   1.00 23.38  ?  14  TRP D CE2 1 
ATOM   1732 C  CE3 . TRP B 1 19  ? 60.349 -0.274  8.036   1.00 21.08  ?  14  TRP D CE3 1 
ATOM   1733 C  CZ2 . TRP B 1 19  ? 61.711 -0.992  5.660   1.00 22.43  ?  14  TRP D CZ2 1 
ATOM   1734 C  CZ3 . TRP B 1 19  ? 60.488 -1.586  7.665   1.00 22.98  ?  14  TRP D CZ3 1 
ATOM   1735 C  CH2 . TRP B 1 19  ? 61.194 -1.939  6.512   1.00 23.30  ?  14  TRP D CH2 1 
ATOM   1736 N  N   . LEU B 1 20  ? 59.036 5.515   9.931   1.00 17.89  ?  15  LEU D N   1 
ATOM   1737 C  CA  . LEU B 1 20  ? 58.220 5.968   11.077  1.00 17.86  ?  15  LEU D CA  1 
ATOM   1738 C  C   . LEU B 1 20  ? 57.093 6.858   10.532  1.00 17.24  ?  15  LEU D C   1 
ATOM   1739 O  O   . LEU B 1 20  ? 55.959 6.700   10.946  1.00 17.26  ?  15  LEU D O   1 
ATOM   1740 C  CB  . LEU B 1 20  ? 59.085 6.726   12.076  1.00 19.23  ?  15  LEU D CB  1 
ATOM   1741 C  CG  . LEU B 1 20  ? 59.905 5.895   13.068  1.00 19.89  ?  15  LEU D CG  1 
ATOM   1742 C  CD1 . LEU B 1 20  ? 61.108 5.278   12.351  1.00 20.06  ?  15  LEU D CD1 1 
ATOM   1743 C  CD2 . LEU B 1 20  ? 60.366 6.767   14.263  1.00 19.13  ?  15  LEU D CD2 1 
ATOM   1744 N  N   . VAL B 1 21  ? 57.406 7.721   9.559   1.00 17.08  ?  16  VAL D N   1 
ATOM   1745 C  CA  . VAL B 1 21  ? 56.427 8.630   8.894   1.00 17.45  ?  16  VAL D CA  1 
ATOM   1746 C  C   . VAL B 1 21  ? 55.414 7.762   8.143   1.00 16.74  ?  16  VAL D C   1 
ATOM   1747 O  O   . VAL B 1 21  ? 54.232 8.034   8.248   1.00 16.45  ?  16  VAL D O   1 
ATOM   1748 C  CB  . VAL B 1 21  ? 57.118 9.643   7.954   1.00 18.50  ?  16  VAL D CB  1 
ATOM   1749 C  CG1 . VAL B 1 21  ? 56.120 10.570  7.283   1.00 19.05  ?  16  VAL D CG1 1 
ATOM   1750 C  CG2 . VAL B 1 21  ? 58.167 10.460  8.678   1.00 19.91  ?  16  VAL D CG2 1 
ATOM   1751 N  N   . ASP B 1 22  ? 55.859 6.740   7.404   1.00 18.31  ?  17  ASP D N   1 
ATOM   1752 C  CA  . ASP B 1 22  ? 54.946 5.808   6.662   1.00 20.04  ?  17  ASP D CA  1 
ATOM   1753 C  C   . ASP B 1 22  ? 53.953 5.104   7.600   1.00 18.60  ?  17  ASP D C   1 
ATOM   1754 O  O   . ASP B 1 22  ? 52.768 4.918   7.215   1.00 14.82  ?  17  ASP D O   1 
ATOM   1755 C  CB  . ASP B 1 22  ? 55.742 4.753   5.878   1.00 22.13  ?  17  ASP D CB  1 
ATOM   1756 C  CG  . ASP B 1 22  ? 56.610 5.305   4.761   1.00 25.25  ?  17  ASP D CG  1 
ATOM   1757 O  OD1 . ASP B 1 22  ? 56.406 6.440   4.380   1.00 25.97  ?  17  ASP D OD1 1 
ATOM   1758 O  OD2 . ASP B 1 22  ? 57.524 4.576   4.317   1.00 33.34  -1 17  ASP D OD2 1 
ATOM   1759 N  N   . LEU B 1 23  ? 54.406 4.659   8.774   1.00 17.94  ?  18  LEU D N   1 
ATOM   1760 C  CA  . LEU B 1 23  ? 53.498 3.969   9.729   1.00 19.88  ?  18  LEU D CA  1 
ATOM   1761 C  C   . LEU B 1 23  ? 52.489 4.998   10.247  1.00 18.51  ?  18  LEU D C   1 
ATOM   1762 O  O   . LEU B 1 23  ? 51.298 4.655   10.291  1.00 18.68  ?  18  LEU D O   1 
ATOM   1763 C  CB  . LEU B 1 23  ? 54.298 3.321   10.863  1.00 22.82  ?  18  LEU D CB  1 
ATOM   1764 C  CG  . LEU B 1 23  ? 53.505 2.324   11.717  1.00 25.33  ?  18  LEU D CG  1 
ATOM   1765 C  CD1 . LEU B 1 23  ? 54.420 1.508   12.595  1.00 26.35  ?  18  LEU D CD1 1 
ATOM   1766 C  CD2 . LEU B 1 23  ? 52.500 3.025   12.602  1.00 29.62  ?  18  LEU D CD2 1 
ATOM   1767 N  N   . VAL B 1 24  ? 52.918 6.223   10.572  1.00 18.62  ?  19  VAL D N   1 
ATOM   1768 C  CA  . VAL B 1 24  ? 51.967 7.268   11.073  1.00 19.06  ?  19  VAL D CA  1 
ATOM   1769 C  C   . VAL B 1 24  ? 50.914 7.502   10.004  1.00 17.24  ?  19  VAL D C   1 
ATOM   1770 O  O   . VAL B 1 24  ? 49.728 7.572   10.339  1.00 18.16  ?  19  VAL D O   1 
ATOM   1771 C  CB  . VAL B 1 24  ? 52.663 8.606   11.388  1.00 20.74  ?  19  VAL D CB  1 
ATOM   1772 C  CG1 . VAL B 1 24  ? 51.608 9.699   11.496  1.00 19.35  ?  19  VAL D CG1 1 
ATOM   1773 C  CG2 . VAL B 1 24  ? 53.499 8.497   12.649  1.00 19.06  ?  19  VAL D CG2 1 
ATOM   1774 N  N   . ARG B 1 25  ? 51.338 7.708   8.766   1.00 17.62  ?  20  ARG D N   1 
ATOM   1775 C  CA  . ARG B 1 25  ? 50.382 7.939   7.634   1.00 19.66  ?  20  ARG D CA  1 
ATOM   1776 C  C   . ARG B 1 25  ? 49.452 6.739   7.429   1.00 17.92  ?  20  ARG D C   1 
ATOM   1777 O  O   . ARG B 1 25  ? 48.244 6.935   7.135   1.00 17.16  ?  20  ARG D O   1 
ATOM   1778 C  CB  . ARG B 1 25  ? 51.121 8.256   6.329   1.00 21.21  ?  20  ARG D CB  1 
ATOM   1779 C  CG  . ARG B 1 25  ? 51.858 9.585   6.337   1.00 23.72  ?  20  ARG D CG  1 
ATOM   1780 C  CD  . ARG B 1 25  ? 52.254 10.007  4.932   1.00 26.62  ?  20  ARG D CD  1 
ATOM   1781 N  NE  . ARG B 1 25  ? 53.063 11.225  4.834   1.00 30.15  ?  20  ARG D NE  1 
ATOM   1782 C  CZ  . ARG B 1 25  ? 52.609 12.484  4.883   1.00 34.57  ?  20  ARG D CZ  1 
ATOM   1783 N  NH1 . ARG B 1 25  ? 51.330 12.766  5.105   1.00 33.15  ?  20  ARG D NH1 1 
ATOM   1784 N  NH2 . ARG B 1 25  ? 53.471 13.478  4.762   1.00 38.69  ?  20  ARG D NH2 1 
ATOM   1785 N  N   . GLY B 1 26  ? 49.951 5.521   7.619   1.00 16.86  ?  21  GLY D N   1 
ATOM   1786 C  CA  . GLY B 1 26  ? 49.188 4.291   7.352   1.00 16.80  ?  21  GLY D CA  1 
ATOM   1787 C  C   . GLY B 1 26  ? 48.259 3.900   8.480   1.00 17.12  ?  21  GLY D C   1 
ATOM   1788 O  O   . GLY B 1 26  ? 47.385 3.020   8.218   1.00 17.88  ?  21  GLY D O   1 
ATOM   1789 N  N   . HIS B 1 27  ? 48.422 4.479   9.683   1.00 15.63  ?  22  HIS D N   1 
ATOM   1790 C  CA  . HIS B 1 27  ? 47.726 4.036   10.916  1.00 16.29  ?  22  HIS D CA  1 
ATOM   1791 C  C   . HIS B 1 27  ? 47.367 5.239   11.778  1.00 16.73  ?  22  HIS D C   1 
ATOM   1792 O  O   . HIS B 1 27  ? 47.769 5.354   12.928  1.00 16.93  ?  22  HIS D O   1 
ATOM   1793 C  CB  . HIS B 1 27  ? 48.534 2.938   11.611  1.00 17.06  ?  22  HIS D CB  1 
ATOM   1794 C  CG  . HIS B 1 27  ? 48.933 1.841   10.681  1.00 16.67  ?  22  HIS D CG  1 
ATOM   1795 N  ND1 . HIS B 1 27  ? 48.119 0.744   10.452  1.00 16.11  ?  22  HIS D ND1 1 
ATOM   1796 C  CD2 . HIS B 1 27  ? 50.043 1.657   9.936   1.00 16.99  ?  22  HIS D CD2 1 
ATOM   1797 C  CE1 . HIS B 1 27  ? 48.712 -0.055  9.596   1.00 17.78  ?  22  HIS D CE1 1 
ATOM   1798 N  NE2 . HIS B 1 27  ? 49.894 0.493   9.235   1.00 16.75  ?  22  HIS D NE2 1 
ATOM   1799 N  N   . PRO B 1 28  ? 46.516 6.136   11.253  1.00 14.89  ?  23  PRO D N   1 
ATOM   1800 C  CA  . PRO B 1 28  ? 46.323 7.448   11.875  1.00 15.87  ?  23  PRO D CA  1 
ATOM   1801 C  C   . PRO B 1 28  ? 45.556 7.422   13.200  1.00 14.93  ?  23  PRO D C   1 
ATOM   1802 O  O   . PRO B 1 28  ? 45.559 8.441   13.900  1.00 14.72  ?  23  PRO D O   1 
ATOM   1803 C  CB  . PRO B 1 28  ? 45.504 8.218   10.813  1.00 15.94  ?  23  PRO D CB  1 
ATOM   1804 C  CG  . PRO B 1 28  ? 44.792 7.151   10.031  1.00 15.95  ?  23  PRO D CG  1 
ATOM   1805 C  CD  . PRO B 1 28  ? 45.764 5.984   9.995   1.00 15.64  ?  23  PRO D CD  1 
ATOM   1806 N  N   . LEU B 1 29  ? 44.838 6.332   13.476  1.00 14.45  ?  24  LEU D N   1 
ATOM   1807 C  CA  . LEU B 1 29  ? 44.058 6.280   14.731  1.00 16.13  ?  24  LEU D CA  1 
ATOM   1808 C  C   . LEU B 1 29  ? 45.014 5.871   15.854  1.00 14.85  ?  24  LEU D C   1 
ATOM   1809 O  O   . LEU B 1 29  ? 45.196 4.650   16.118  1.00 14.85  ?  24  LEU D O   1 
ATOM   1810 C  CB  . LEU B 1 29  ? 42.838 5.370   14.608  1.00 16.76  ?  24  LEU D CB  1 
ATOM   1811 C  CG  . LEU B 1 29  ? 41.873 5.475   15.802  1.00 20.28  ?  24  LEU D CG  1 
ATOM   1812 C  CD1 . LEU B 1 29  ? 41.111 6.801   15.780  1.00 21.67  ?  24  LEU D CD1 1 
ATOM   1813 C  CD2 . LEU B 1 29  ? 40.910 4.283   15.856  1.00 19.82  ?  24  LEU D CD2 1 
ATOM   1814 N  N   . ALA B 1 30  ? 45.569 6.887   16.503  1.00 14.26  ?  25  ALA D N   1 
ATOM   1815 C  CA  . ALA B 1 30  ? 46.614 6.774   17.533  1.00 14.51  ?  25  ALA D CA  1 
ATOM   1816 C  C   . ALA B 1 30  ? 45.959 6.616   18.905  1.00 14.38  ?  25  ALA D C   1 
ATOM   1817 O  O   . ALA B 1 30  ? 44.823 7.024   19.085  1.00 16.77  ?  25  ALA D O   1 
ATOM   1818 C  CB  . ALA B 1 30  ? 47.480 7.998   17.469  1.00 14.84  ?  25  ALA D CB  1 
ATOM   1819 N  N   . GLN B 1 31  ? 46.706 6.086   19.859  1.00 14.01  ?  26  GLN D N   1 
ATOM   1820 C  CA  . GLN B 1 31  ? 46.330 6.130   21.286  1.00 15.00  ?  26  GLN D CA  1 
ATOM   1821 C  C   . GLN B 1 31  ? 47.111 7.304   21.861  1.00 15.73  ?  26  GLN D C   1 
ATOM   1822 O  O   . GLN B 1 31  ? 48.375 7.186   21.965  1.00 14.23  ?  26  GLN D O   1 
ATOM   1823 C  CB  . GLN B 1 31  ? 46.646 4.769   21.923  1.00 14.09  ?  26  GLN D CB  1 
ATOM   1824 C  CG  . GLN B 1 31  ? 45.658 3.648   21.588  1.00 15.31  ?  26  GLN D CG  1 
ATOM   1825 C  CD  . GLN B 1 31  ? 45.904 2.339   22.325  1.00 13.86  ?  26  GLN D CD  1 
ATOM   1826 O  OE1 . GLN B 1 31  ? 46.309 2.345   23.477  1.00 17.02  ?  26  GLN D OE1 1 
ATOM   1827 N  NE2 . GLN B 1 31  ? 45.826 1.219   21.618  1.00 14.05  ?  26  GLN D NE2 1 
ATOM   1828 N  N   . LEU B 1 32  ? 46.405 8.356   22.218  1.00 15.72  ?  27  LEU D N   1 
ATOM   1829 C  CA  . LEU B 1 32  ? 46.992 9.560   22.859  1.00 15.34  ?  27  LEU D CA  1 
ATOM   1830 C  C   . LEU B 1 32  ? 47.046 9.319   24.362  1.00 16.38  ?  27  LEU D C   1 
ATOM   1831 O  O   . LEU B 1 32  ? 45.955 9.143   24.951  1.00 11.26  ?  27  LEU D O   1 
ATOM   1832 C  CB  . LEU B 1 32  ? 46.161 10.796  22.489  1.00 15.16  ?  27  LEU D CB  1 
ATOM   1833 C  CG  . LEU B 1 32  ? 46.646 12.142  23.067  1.00 17.34  ?  27  LEU D CG  1 
ATOM   1834 C  CD1 . LEU B 1 32  ? 48.108 12.428  22.741  1.00 19.07  ?  27  LEU D CD1 1 
ATOM   1835 C  CD2 . LEU B 1 32  ? 45.790 13.296  22.550  1.00 19.43  ?  27  LEU D CD2 1 
ATOM   1836 N  N   . ALA B 1 33  ? 48.255 9.375   24.977  1.00 12.96  ?  28  ALA D N   1 
ATOM   1837 C  CA  . ALA B 1 33  ? 48.406 9.117   26.417  1.00 15.41  ?  28  ALA D CA  1 
ATOM   1838 C  C   . ALA B 1 33  ? 48.886 10.398  27.114  1.00 15.95  ?  28  ALA D C   1 
ATOM   1839 O  O   . ALA B 1 33  ? 49.862 10.988  26.639  1.00 14.90  ?  28  ALA D O   1 
ATOM   1840 C  CB  . ALA B 1 33  ? 49.332 7.946   26.697  1.00 14.49  ?  28  ALA D CB  1 
ATOM   1841 N  N   . SER B 1 34  ? 48.306 10.709  28.266  1.00 15.73  ?  29  SER D N   1 
ATOM   1842 C  CA  . SER B 1 34  ? 48.919 11.688  29.193  1.00 17.88  ?  29  SER D CA  1 
ATOM   1843 C  C   . SER B 1 34  ? 48.803 11.236  30.655  1.00 19.33  ?  29  SER D C   1 
ATOM   1844 O  O   . SER B 1 34  ? 48.009 10.337  30.972  1.00 18.41  ?  29  SER D O   1 
ATOM   1845 C  CB  . SER B 1 34  ? 48.348 13.055  28.947  1.00 17.90  ?  29  SER D CB  1 
ATOM   1846 O  OG  . SER B 1 34  ? 46.979 13.048  29.271  1.00 18.86  ?  29  SER D OG  1 
ATOM   1847 N  N   . ASN B 1 35  ? 49.637 11.817  31.516  1.00 18.55  ?  30  ASN D N   1 
ATOM   1848 C  CA  . ASN B 1 35  ? 49.721 11.379  32.927  1.00 20.32  ?  30  ASN D CA  1 
ATOM   1849 C  C   . ASN B 1 35  ? 48.390 11.580  33.651  1.00 18.94  ?  30  ASN D C   1 
ATOM   1850 O  O   . ASN B 1 35  ? 47.668 12.620  33.403  1.00 17.05  ?  30  ASN D O   1 
ATOM   1851 C  CB  . ASN B 1 35  ? 50.836 12.066  33.694  1.00 19.89  ?  30  ASN D CB  1 
ATOM   1852 C  CG  . ASN B 1 35  ? 52.216 11.638  33.251  1.00 22.62  ?  30  ASN D CG  1 
ATOM   1853 O  OD1 . ASN B 1 35  ? 52.418 10.588  32.632  1.00 20.88  ?  30  ASN D OD1 1 
ATOM   1854 N  ND2 . ASN B 1 35  ? 53.196 12.467  33.582  1.00 26.84  ?  30  ASN D ND2 1 
ATOM   1855 N  N   . GLY B 1 36  ? 48.107 10.621  34.544  1.00 18.76  ?  31  GLY D N   1 
ATOM   1856 C  CA  . GLY B 1 36  ? 46.947 10.657  35.437  1.00 21.87  ?  31  GLY D CA  1 
ATOM   1857 C  C   . GLY B 1 36  ? 47.317 11.424  36.694  1.00 24.34  ?  31  GLY D C   1 
ATOM   1858 O  O   . GLY B 1 36  ? 48.393 11.199  37.214  1.00 27.88  ?  31  GLY D O   1 
ATOM   1859 N  N   . ALA B 1 37  ? 46.451 12.310  37.141  1.00 26.33  ?  32  ALA D N   1 
ATOM   1860 C  CA  . ALA B 1 37  ? 46.717 13.178  38.308  1.00 30.31  ?  32  ALA D CA  1 
ATOM   1861 C  C   . ALA B 1 37  ? 46.809 12.272  39.535  1.00 30.31  ?  32  ALA D C   1 
ATOM   1862 O  O   . ALA B 1 37  ? 46.090 11.241  39.574  1.00 29.56  ?  32  ALA D O   1 
ATOM   1863 C  CB  . ALA B 1 37  ? 45.636 14.222  38.426  1.00 30.31  ?  32  ALA D CB  1 
ATOM   1864 N  N   . GLY B 1 38  ? 47.691 12.629  40.469  1.00 32.35  ?  33  GLY D N   1 
ATOM   1865 C  CA  . GLY B 1 38  ? 47.718 12.064  41.830  1.00 36.27  ?  33  GLY D CA  1 
ATOM   1866 C  C   . GLY B 1 38  ? 48.059 10.590  41.785  1.00 34.69  ?  33  GLY D C   1 
ATOM   1867 O  O   . GLY B 1 38  ? 47.450 9.836   42.520  1.00 34.99  ?  33  GLY D O   1 
ATOM   1868 N  N   . GLY B 1 39  ? 48.964 10.220  40.882  1.00 34.84  ?  34  GLY D N   1 
ATOM   1869 C  CA  . GLY B 1 39  ? 49.474 8.850   40.726  1.00 35.09  ?  34  GLY D CA  1 
ATOM   1870 C  C   . GLY B 1 39  ? 48.463 7.910   40.094  1.00 28.89  ?  34  GLY D C   1 
ATOM   1871 O  O   . GLY B 1 39  ? 48.707 6.713   40.132  1.00 30.08  ?  34  GLY D O   1 
ATOM   1872 N  N   . ALA B 1 40  ? 47.389 8.413   39.510  1.00 25.73  ?  35  ALA D N   1 
ATOM   1873 C  CA  . ALA B 1 40  ? 46.401 7.586   38.786  1.00 27.27  ?  35  ALA D CA  1 
ATOM   1874 C  C   . ALA B 1 40  ? 47.029 7.079   37.476  1.00 25.41  ?  35  ALA D C   1 
ATOM   1875 O  O   . ALA B 1 40  ? 47.989 7.699   36.988  1.00 26.38  ?  35  ALA D O   1 
ATOM   1876 C  CB  . ALA B 1 40  ? 45.134 8.369   38.554  1.00 28.21  ?  35  ALA D CB  1 
ATOM   1877 N  N   . ALA B 1 41  ? 46.529 5.965   36.943  1.00 21.75  ?  36  ALA D N   1 
ATOM   1878 C  CA  . ALA B 1 41  ? 46.842 5.503   35.577  1.00 18.87  ?  36  ALA D CA  1 
ATOM   1879 C  C   . ALA B 1 41  ? 46.707 6.667   34.587  1.00 18.38  ?  36  ALA D C   1 
ATOM   1880 O  O   . ALA B 1 41  ? 45.838 7.519   34.731  1.00 16.16  ?  36  ALA D O   1 
ATOM   1881 C  CB  . ALA B 1 41  ? 45.894 4.385   35.186  1.00 18.81  ?  36  ALA D CB  1 
ATOM   1882 N  N   . PRO B 1 42  ? 47.508 6.664   33.509  1.00 15.90  ?  37  PRO D N   1 
ATOM   1883 C  CA  . PRO B 1 42  ? 47.337 7.583   32.386  1.00 16.71  ?  37  PRO D CA  1 
ATOM   1884 C  C   . PRO B 1 42  ? 45.935 7.556   31.791  1.00 15.55  ?  37  PRO D C   1 
ATOM   1885 O  O   . PRO B 1 42  ? 45.318 6.529   31.807  1.00 14.96  ?  37  PRO D O   1 
ATOM   1886 C  CB  . PRO B 1 42  ? 48.353 7.094   31.351  1.00 16.59  ?  37  PRO D CB  1 
ATOM   1887 C  CG  . PRO B 1 42  ? 49.451 6.494   32.201  1.00 17.16  ?  37  PRO D CG  1 
ATOM   1888 C  CD  . PRO B 1 42  ? 48.704 5.825   33.334  1.00 17.33  ?  37  PRO D CD  1 
ATOM   1889 N  N   . HIS B 1 43  ? 45.522 8.696   31.235  1.00 15.59  ?  38  HIS D N   1 
ATOM   1890 C  CA  . HIS B 1 43  ? 44.358 8.842   30.322  1.00 16.53  ?  38  HIS D CA  1 
ATOM   1891 C  C   . HIS B 1 43  ? 44.779 8.329   28.938  1.00 15.30  ?  38  HIS D C   1 
ATOM   1892 O  O   . HIS B 1 43  ? 45.925 8.610   28.516  1.00 15.79  ?  38  HIS D O   1 
ATOM   1893 C  CB  . HIS B 1 43  ? 43.956 10.314  30.211  1.00 17.48  ?  38  HIS D CB  1 
ATOM   1894 C  CG  . HIS B 1 43  ? 43.720 10.970  31.542  1.00 19.28  ?  38  HIS D CG  1 
ATOM   1895 N  ND1 . HIS B 1 43  ? 42.534 10.826  32.214  1.00 24.71  ?  38  HIS D ND1 1 
ATOM   1896 C  CD2 . HIS B 1 43  ? 44.479 11.792  32.283  1.00 23.76  ?  38  HIS D CD2 1 
ATOM   1897 C  CE1 . HIS B 1 43  ? 42.567 11.526  33.327  1.00 25.17  ?  38  HIS D CE1 1 
ATOM   1898 N  NE2 . HIS B 1 43  ? 43.768 12.126  33.385  1.00 23.97  ?  38  HIS D NE2 1 
ATOM   1899 N  N   . ILE B 1 44  ? 43.890 7.615   28.262  1.00 14.33  ?  39  ILE D N   1 
ATOM   1900 C  CA  . ILE B 1 44  ? 44.113 6.999   26.926  1.00 14.01  ?  39  ILE D CA  1 
ATOM   1901 C  C   . ILE B 1 44  ? 42.916 7.306   26.050  1.00 15.39  ?  39  ILE D C   1 
ATOM   1902 O  O   . ILE B 1 44  ? 41.773 7.003   26.528  1.00 15.76  ?  39  ILE D O   1 
ATOM   1903 C  CB  . ILE B 1 44  ? 44.311 5.483   27.043  1.00 15.01  ?  39  ILE D CB  1 
ATOM   1904 C  CG1 . ILE B 1 44  ? 45.398 5.076   28.035  1.00 14.66  ?  39  ILE D CG1 1 
ATOM   1905 C  CG2 . ILE B 1 44  ? 44.502 4.904   25.665  1.00 13.66  ?  39  ILE D CG2 1 
ATOM   1906 C  CD1 . ILE B 1 44  ? 46.803 5.436   27.636  1.00 16.51  ?  39  ILE D CD1 1 
ATOM   1907 N  N   . THR B 1 45  ? 43.131 8.009   24.917  1.00 14.80  ?  40  THR D N   1 
ATOM   1908 C  CA  . THR B 1 45  ? 42.049 8.287   23.930  1.00 16.91  ?  40  THR D CA  1 
ATOM   1909 C  C   . THR B 1 45  ? 42.527 7.880   22.543  1.00 13.94  ?  40  THR D C   1 
ATOM   1910 O  O   . THR B 1 45  ? 43.621 8.271   22.123  1.00 11.91  ?  40  THR D O   1 
ATOM   1911 C  CB  . THR B 1 45  ? 41.555 9.744   23.991  1.00 17.07  ?  40  THR D CB  1 
ATOM   1912 O  OG1 . THR B 1 45  ? 41.260 10.043  25.376  1.00 17.31  ?  40  THR D OG1 1 
ATOM   1913 C  CG2 . THR B 1 45  ? 40.339 9.959   23.104  1.00 19.62  ?  40  THR D CG2 1 
ATOM   1914 N  N   . HIS B 1 46  ? 41.712 7.095   21.832  1.00 15.03  ?  41  HIS D N   1 
ATOM   1915 C  CA  . HIS B 1 46  ? 41.960 6.796   20.402  1.00 14.43  ?  41  HIS D CA  1 
ATOM   1916 C  C   . HIS B 1 46  ? 41.592 8.052   19.610  1.00 15.08  ?  41  HIS D C   1 
ATOM   1917 O  O   . HIS B 1 46  ? 40.446 8.469   19.622  1.00 13.29  ?  41  HIS D O   1 
ATOM   1918 C  CB  . HIS B 1 46  ? 41.203 5.565   19.903  1.00 15.58  ?  41  HIS D CB  1 
ATOM   1919 C  CG  . HIS B 1 46  ? 41.880 4.265   20.215  1.00 20.16  ?  41  HIS D CG  1 
ATOM   1920 N  ND1 . HIS B 1 46  ? 41.741 3.626   21.421  1.00 25.53  ?  41  HIS D ND1 1 
ATOM   1921 C  CD2 . HIS B 1 46  ? 42.684 3.490   19.472  1.00 23.05  ?  41  HIS D CD2 1 
ATOM   1922 C  CE1 . HIS B 1 46  ? 42.429 2.496   21.408  1.00 25.21  ?  41  HIS D CE1 1 
ATOM   1923 N  NE2 . HIS B 1 46  ? 43.001 2.387   20.230  1.00 29.04  ?  41  HIS D NE2 1 
ATOM   1924 N  N   . VAL B 1 47  ? 42.570 8.653   18.960  1.00 14.28  ?  42  VAL D N   1 
ATOM   1925 C  CA  . VAL B 1 47  ? 42.337 9.910   18.205  1.00 14.01  ?  42  VAL D CA  1 
ATOM   1926 C  C   . VAL B 1 47  ? 42.981 9.863   16.812  1.00 13.51  ?  42  VAL D C   1 
ATOM   1927 O  O   . VAL B 1 47  ? 44.102 9.396   16.658  1.00 15.04  ?  42  VAL D O   1 
ATOM   1928 C  CB  . VAL B 1 47  ? 42.866 11.116  18.994  1.00 13.64  ?  42  VAL D CB  1 
ATOM   1929 C  CG1 . VAL B 1 47  ? 42.034 11.382  20.234  1.00 14.80  ?  42  VAL D CG1 1 
ATOM   1930 C  CG2 . VAL B 1 47  ? 44.318 10.931  19.377  1.00 14.43  ?  42  VAL D CG2 1 
ATOM   1931 N  N   . PRO B 1 48  ? 42.331 10.469  15.786  1.00 14.37  ?  43  PRO D N   1 
ATOM   1932 C  CA  . PRO B 1 48  ? 42.881 10.601  14.439  1.00 14.34  ?  43  PRO D CA  1 
ATOM   1933 C  C   . PRO B 1 48  ? 43.947 11.708  14.357  1.00 13.68  ?  43  PRO D C   1 
ATOM   1934 O  O   . PRO B 1 48  ? 43.693 12.865  14.634  1.00 15.06  ?  43  PRO D O   1 
ATOM   1935 C  CB  . PRO B 1 48  ? 41.658 10.940  13.549  1.00 14.36  ?  43  PRO D CB  1 
ATOM   1936 C  CG  . PRO B 1 48  ? 40.755 11.679  14.516  1.00 15.21  ?  43  PRO D CG  1 
ATOM   1937 C  CD  . PRO B 1 48  ? 40.964 11.010  15.862  1.00 16.92  ?  43  PRO D CD  1 
ATOM   1938 N  N   . ILE B 1 49  ? 45.167 11.324  14.037  1.00 13.62  ?  44  ILE D N   1 
ATOM   1939 C  CA  . ILE B 1 49  ? 46.300 12.262  13.981  1.00 13.57  ?  44  ILE D CA  1 
ATOM   1940 C  C   . ILE B 1 49  ? 46.932 12.164  12.591  1.00 14.27  ?  44  ILE D C   1 
ATOM   1941 O  O   . ILE B 1 49  ? 47.169 11.041  12.102  1.00 14.80  ?  44  ILE D O   1 
ATOM   1942 C  CB  . ILE B 1 49  ? 47.320 11.995  15.086  1.00 15.10  ?  44  ILE D CB  1 
ATOM   1943 C  CG1 . ILE B 1 49  ? 46.767 12.267  16.490  1.00 16.56  ?  44  ILE D CG1 1 
ATOM   1944 C  CG2 . ILE B 1 49  ? 48.551 12.832  14.789  1.00 16.20  ?  44  ILE D CG2 1 
ATOM   1945 C  CD1 . ILE B 1 49  ? 47.669 11.830  17.639  1.00 15.85  ?  44  ILE D CD1 1 
ATOM   1946 N  N   . ILE B 1 50  ? 47.240 13.319  12.006  1.00 13.96  ?  45  ILE D N   1 
ATOM   1947 C  CA  . ILE B 1 50  ? 47.896 13.394  10.676  1.00 15.19  ?  45  ILE D CA  1 
ATOM   1948 C  C   . ILE B 1 50  ? 49.122 14.282  10.775  1.00 13.34  ?  45  ILE D C   1 
ATOM   1949 O  O   . ILE B 1 50  ? 49.219 15.144  11.671  1.00 13.19  ?  45  ILE D O   1 
ATOM   1950 C  CB  . ILE B 1 50  ? 46.907 13.964  9.632   1.00 16.41  ?  45  ILE D CB  1 
ATOM   1951 C  CG1 . ILE B 1 50  ? 46.440 15.370  10.019  1.00 16.84  ?  45  ILE D CG1 1 
ATOM   1952 C  CG2 . ILE B 1 50  ? 45.718 13.010  9.413   1.00 15.72  ?  45  ILE D CG2 1 
ATOM   1953 C  CD1 . ILE B 1 50  ? 45.769 16.152  8.861   1.00 18.78  ?  45  ILE D CD1 1 
ATOM   1954 N  N   . VAL B 1 51  ? 49.995 14.109  9.807   1.00 16.36  ?  46  VAL D N   1 
ATOM   1955 C  CA  . VAL B 1 51  ? 51.136 15.035  9.570   1.00 19.25  ?  46  VAL D CA  1 
ATOM   1956 C  C   . VAL B 1 51  ? 50.635 16.392  9.035   1.00 20.73  ?  46  VAL D C   1 
ATOM   1957 O  O   . VAL B 1 51  ? 49.686 16.435  8.192   1.00 17.96  ?  46  VAL D O   1 
ATOM   1958 C  CB  . VAL B 1 51  ? 52.129 14.387  8.588   1.00 21.50  ?  46  VAL D CB  1 
ATOM   1959 C  CG1 . VAL B 1 51  ? 53.021 15.421  7.922   1.00 24.01  ?  46  VAL D CG1 1 
ATOM   1960 C  CG2 . VAL B 1 51  ? 52.916 13.282  9.264   1.00 23.53  ?  46  VAL D CG2 1 
ATOM   1961 N  N   . ASP B 1 52  ? 51.223 17.471  9.545   1.00 20.15  ?  47  ASP D N   1 
ATOM   1962 C  CA  . ASP B 1 52  ? 50.949 18.874  9.107   1.00 20.50  ?  47  ASP D CA  1 
ATOM   1963 C  C   . ASP B 1 52  ? 50.658 18.900  7.605   1.00 20.12  ?  47  ASP D C   1 
ATOM   1964 O  O   . ASP B 1 52  ? 51.549 18.666  6.797   1.00 21.36  ?  47  ASP D O   1 
ATOM   1965 C  CB  . ASP B 1 52  ? 52.170 19.729  9.395   1.00 22.38  ?  47  ASP D CB  1 
ATOM   1966 C  CG  . ASP B 1 52  ? 52.122 21.188  9.004   1.00 23.45  ?  47  ASP D CG  1 
ATOM   1967 O  OD1 . ASP B 1 52  ? 51.104 21.647  8.445   1.00 21.86  ?  47  ASP D OD1 1 
ATOM   1968 O  OD2 . ASP B 1 52  ? 53.147 21.849  9.260   1.00 24.26  -1 47  ASP D OD2 1 
ATOM   1969 N  N   . PRO B 1 53  ? 49.409 19.139  7.158   1.00 20.20  ?  48  PRO D N   1 
ATOM   1970 C  CA  . PRO B 1 53  ? 49.104 19.107  5.729   1.00 23.24  ?  48  PRO D CA  1 
ATOM   1971 C  C   . PRO B 1 53  ? 49.808 20.193  4.878   1.00 27.27  ?  48  PRO D C   1 
ATOM   1972 O  O   . PRO B 1 53  ? 49.779 20.107  3.637   1.00 26.89  ?  48  PRO D O   1 
ATOM   1973 C  CB  . PRO B 1 53  ? 47.589 19.360  5.723   1.00 23.70  ?  48  PRO D CB  1 
ATOM   1974 C  CG  . PRO B 1 53  ? 47.366 20.210  6.973   1.00 22.24  ?  48  PRO D CG  1 
ATOM   1975 C  CD  . PRO B 1 53  ? 48.244 19.492  7.978   1.00 21.78  ?  48  PRO D CD  1 
ATOM   1976 N  N   . GLU B 1 54  ? 50.396 21.204  5.532   1.00 28.54  ?  49  GLU D N   1 
ATOM   1977 C  CA  . GLU B 1 54  ? 51.037 22.366  4.857   1.00 33.13  ?  49  GLU D CA  1 
ATOM   1978 C  C   . GLU B 1 54  ? 52.483 21.988  4.519   1.00 31.80  ?  49  GLU D C   1 
ATOM   1979 O  O   . GLU B 1 54  ? 53.137 22.748  3.801   1.00 30.98  ?  49  GLU D O   1 
ATOM   1980 C  CB  . GLU B 1 54  ? 50.957 23.638  5.714   1.00 37.22  ?  49  GLU D CB  1 
ATOM   1981 C  CG  . GLU B 1 54  ? 49.534 24.018  6.128   1.00 42.41  ?  49  GLU D CG  1 
ATOM   1982 C  CD  . GLU B 1 54  ? 49.375 24.552  7.555   1.00 50.50  ?  49  GLU D CD  1 
ATOM   1983 O  OE1 . GLU B 1 54  ? 50.148 24.097  8.468   1.00 43.42  ?  49  GLU D OE1 1 
ATOM   1984 O  OE2 . GLU B 1 54  ? 48.462 25.415  7.782   1.00 52.40  -1 49  GLU D OE2 1 
ATOM   1985 N  N   . LEU B 1 55  ? 52.947 20.832  4.991   1.00 31.83  ?  50  LEU D N   1 
ATOM   1986 C  CA  . LEU B 1 55  ? 54.293 20.299  4.654   1.00 36.57  ?  50  LEU D CA  1 
ATOM   1987 C  C   . LEU B 1 55  ? 54.216 19.807  3.208   1.00 41.84  ?  50  LEU D C   1 
ATOM   1988 O  O   . LEU B 1 55  ? 53.556 18.785  2.950   1.00 38.92  ?  50  LEU D O   1 
ATOM   1989 C  CB  . LEU B 1 55  ? 54.706 19.192  5.634   1.00 32.71  ?  50  LEU D CB  1 
ATOM   1990 C  CG  . LEU B 1 55  ? 55.204 19.641  7.016   1.00 31.83  ?  50  LEU D CG  1 
ATOM   1991 C  CD1 . LEU B 1 55  ? 55.854 18.467  7.723   1.00 25.85  ?  50  LEU D CD1 1 
ATOM   1992 C  CD2 . LEU B 1 55  ? 56.205 20.792  6.936   1.00 32.49  ?  50  LEU D CD2 1 
ATOM   1993 N  N   . ASP B 1 56  ? 54.785 20.600  2.304   1.00 51.20  ?  51  ASP D N   1 
ATOM   1994 C  CA  . ASP B 1 56  ? 55.038 20.239  0.892   1.00 58.80  ?  51  ASP D CA  1 
ATOM   1995 C  C   . ASP B 1 56  ? 56.433 19.609  0.856   1.00 57.28  ?  51  ASP D C   1 
ATOM   1996 O  O   . ASP B 1 56  ? 57.301 19.994  1.694   1.00 54.76  ?  51  ASP D O   1 
ATOM   1997 C  CB  . ASP B 1 56  ? 54.861 21.458  -0.023  1.00 66.99  ?  51  ASP D CB  1 
ATOM   1998 C  CG  . ASP B 1 56  ? 53.420 21.946  -0.126  1.00 72.21  ?  51  ASP D CG  1 
ATOM   1999 O  OD1 . ASP B 1 56  ? 52.621 21.272  -0.823  1.00 79.45  ?  51  ASP D OD1 1 
ATOM   2000 O  OD2 . ASP B 1 56  ? 53.099 22.994  0.499   1.00 71.71  -1 51  ASP D OD2 1 
ATOM   2001 N  N   . GLY B 1 57  ? 56.608 18.641  -0.041  1.00 49.62  ?  52  GLY D N   1 
ATOM   2002 C  CA  . GLY B 1 57  ? 57.880 17.931  -0.247  1.00 42.79  ?  52  GLY D CA  1 
ATOM   2003 C  C   . GLY B 1 57  ? 57.938 16.672  0.608   1.00 39.03  ?  52  GLY D C   1 
ATOM   2004 O  O   . GLY B 1 57  ? 57.119 16.491  1.515   1.00 34.23  ?  52  GLY D O   1 
ATOM   2005 N  N   . PRO B 1 58  ? 58.905 15.773  0.334   1.00 33.73  ?  53  PRO D N   1 
ATOM   2006 C  CA  . PRO B 1 58  ? 59.038 14.537  1.095   1.00 32.70  ?  53  PRO D CA  1 
ATOM   2007 C  C   . PRO B 1 58  ? 59.226 14.828  2.594   1.00 30.76  ?  53  PRO D C   1 
ATOM   2008 O  O   . PRO B 1 58  ? 60.005 15.670  2.984   1.00 28.43  ?  53  PRO D O   1 
ATOM   2009 C  CB  . PRO B 1 58  ? 60.258 13.844  0.452   1.00 34.37  ?  53  PRO D CB  1 
ATOM   2010 C  CG  . PRO B 1 58  ? 60.351 14.448  -0.931  1.00 34.22  ?  53  PRO D CG  1 
ATOM   2011 C  CD  . PRO B 1 58  ? 59.920 15.884  -0.731  1.00 36.09  ?  53  PRO D CD  1 
ATOM   2012 N  N   . VAL B 1 59  ? 58.448 14.142  3.417   1.00 26.86  ?  54  VAL D N   1 
ATOM   2013 C  CA  . VAL B 1 59  ? 58.586 14.188  4.891   1.00 26.10  ?  54  VAL D CA  1 
ATOM   2014 C  C   . VAL B 1 59  ? 59.296 12.901  5.276   1.00 25.38  ?  54  VAL D C   1 
ATOM   2015 O  O   . VAL B 1 59  ? 58.652 11.828  5.207   1.00 26.63  ?  54  VAL D O   1 
ATOM   2016 C  CB  . VAL B 1 59  ? 57.217 14.356  5.563   1.00 25.80  ?  54  VAL D CB  1 
ATOM   2017 C  CG1 . VAL B 1 59  ? 57.338 14.325  7.075   1.00 26.36  ?  54  VAL D CG1 1 
ATOM   2018 C  CG2 . VAL B 1 59  ? 56.572 15.658  5.116   1.00 28.04  ?  54  VAL D CG2 1 
ATOM   2019 N  N   . ASP B 1 60  ? 60.579 13.015  5.595   1.00 27.80  ?  55  ASP D N   1 
ATOM   2020 C  CA  . ASP B 1 60  ? 61.463 11.858  5.870   1.00 31.10  ?  55  ASP D CA  1 
ATOM   2021 C  C   . ASP B 1 60  ? 61.587 11.591  7.365   1.00 30.27  ?  55  ASP D C   1 
ATOM   2022 O  O   . ASP B 1 60  ? 61.938 10.442  7.697   1.00 35.64  ?  55  ASP D O   1 
ATOM   2023 C  CB  . ASP B 1 60  ? 62.828 12.096  5.245   1.00 34.31  ?  55  ASP D CB  1 
ATOM   2024 C  CG  . ASP B 1 60  ? 62.780 11.900  3.739   1.00 39.67  ?  55  ASP D CG  1 
ATOM   2025 O  OD1 . ASP B 1 60  ? 63.454 12.677  3.028   1.00 42.92  ?  55  ASP D OD1 1 
ATOM   2026 O  OD2 . ASP B 1 60  ? 62.036 10.992  3.288   1.00 44.31  -1 55  ASP D OD2 1 
ATOM   2027 N  N   . ARG B 1 61  ? 61.370 12.603  8.210   1.00 26.61  ?  56  ARG D N   1 
ATOM   2028 C  CA  . ARG B 1 61  ? 61.644 12.552  9.678   1.00 28.30  ?  56  ARG D CA  1 
ATOM   2029 C  C   . ARG B 1 61  ? 60.428 13.131  10.411  1.00 24.45  ?  56  ARG D C   1 
ATOM   2030 O  O   . ARG B 1 61  ? 59.873 14.127  9.916   1.00 22.23  ?  56  ARG D O   1 
ATOM   2031 C  CB  . ARG B 1 61  ? 62.915 13.332  10.066  1.00 32.98  ?  56  ARG D CB  1 
ATOM   2032 C  CG  . ARG B 1 61  ? 64.192 12.494  10.016  1.00 39.08  ?  56  ARG D CG  1 
ATOM   2033 C  CD  . ARG B 1 61  ? 65.483 13.237  10.322  1.00 36.74  ?  56  ARG D CD  1 
ATOM   2034 N  NE  . ARG B 1 61  ? 65.409 14.524  9.659   1.00 40.33  ?  56  ARG D NE  1 
ATOM   2035 C  CZ  . ARG B 1 61  ? 65.619 14.734  8.362   1.00 40.71  ?  56  ARG D CZ  1 
ATOM   2036 N  NH1 . ARG B 1 61  ? 65.967 13.739  7.561   1.00 44.55  ?  56  ARG D NH1 1 
ATOM   2037 N  NH2 . ARG B 1 61  ? 65.479 15.952  7.867   1.00 41.67  ?  56  ARG D NH2 1 
ATOM   2038 N  N   . LEU B 1 62  ? 60.055 12.551  11.558  1.00 23.86  ?  57  LEU D N   1 
ATOM   2039 C  CA  . LEU B 1 62  ? 58.957 13.054  12.410  1.00 20.23  ?  57  LEU D CA  1 
ATOM   2040 C  C   . LEU B 1 62  ? 59.462 14.138  13.357  1.00 21.86  ?  57  LEU D C   1 
ATOM   2041 O  O   . LEU B 1 62  ? 58.711 15.073  13.623  1.00 21.72  ?  57  LEU D O   1 
ATOM   2042 C  CB  . LEU B 1 62  ? 58.366 11.905  13.225  1.00 22.33  ?  57  LEU D CB  1 
ATOM   2043 C  CG  . LEU B 1 62  ? 57.498 10.944  12.431  1.00 23.24  ?  57  LEU D CG  1 
ATOM   2044 C  CD1 . LEU B 1 62  ? 57.133 9.755   13.300  1.00 23.56  ?  57  LEU D CD1 1 
ATOM   2045 C  CD2 . LEU B 1 62  ? 56.257 11.644  11.879  1.00 21.89  ?  57  LEU D CD2 1 
ATOM   2046 N  N   . VAL B 1 63  ? 60.686 14.041  13.864  1.00 22.14  ?  58  VAL D N   1 
ATOM   2047 C  CA  . VAL B 1 63  ? 61.209 15.052  14.830  1.00 22.71  ?  58  VAL D CA  1 
ATOM   2048 C  C   . VAL B 1 63  ? 61.305 16.422  14.148  1.00 22.34  ?  58  VAL D C   1 
ATOM   2049 O  O   . VAL B 1 63  ? 61.814 16.499  13.032  1.00 21.46  ?  58  VAL D O   1 
ATOM   2050 C  CB  . VAL B 1 63  ? 62.530 14.594  15.482  1.00 22.68  ?  58  VAL D CB  1 
ATOM   2051 C  CG1 . VAL B 1 63  ? 63.157 15.710  16.307  1.00 23.52  ?  58  VAL D CG1 1 
ATOM   2052 C  CG2 . VAL B 1 63  ? 62.267 13.360  16.347  1.00 22.34  ?  58  VAL D CG2 1 
ATOM   2053 N  N   . GLY B 1 64  ? 60.674 17.426  14.749  1.00 21.38  ?  59  GLY D N   1 
ATOM   2054 C  CA  . GLY B 1 64  ? 60.662 18.822  14.297  1.00 23.09  ?  59  GLY D CA  1 
ATOM   2055 C  C   . GLY B 1 64  ? 59.393 19.195  13.553  1.00 26.61  ?  59  GLY D C   1 
ATOM   2056 O  O   . GLY B 1 64  ? 59.150 20.390  13.408  1.00 27.77  ?  59  GLY D O   1 
ATOM   2057 N  N   . ILE B 1 65  ? 58.567 18.232  13.149  1.00 25.04  ?  60  ILE D N   1 
ATOM   2058 C  CA  . ILE B 1 65  ? 57.284 18.534  12.463  1.00 23.96  ?  60  ILE D CA  1 
ATOM   2059 C  C   . ILE B 1 65  ? 56.132 18.556  13.474  1.00 21.40  ?  60  ILE D C   1 
ATOM   2060 O  O   . ILE B 1 65  ? 56.284 18.070  14.625  1.00 21.46  ?  60  ILE D O   1 
ATOM   2061 C  CB  . ILE B 1 65  ? 57.074 17.567  11.291  1.00 27.52  ?  60  ILE D CB  1 
ATOM   2062 C  CG1 . ILE B 1 65  ? 56.451 16.242  11.750  1.00 29.07  ?  60  ILE D CG1 1 
ATOM   2063 C  CG2 . ILE B 1 65  ? 58.390 17.367  10.534  1.00 26.54  ?  60  ILE D CG2 1 
ATOM   2064 C  CD1 . ILE B 1 65  ? 55.877 15.405  10.630  1.00 33.94  ?  60  ILE D CD1 1 
ATOM   2065 N  N   . THR B 1 66  ? 55.001 19.125  13.067  1.00 21.13  ?  61  THR D N   1 
ATOM   2066 C  CA  . THR B 1 66  ? 53.808 19.259  13.930  1.00 22.30  ?  61  THR D CA  1 
ATOM   2067 C  C   . THR B 1 66  ? 52.769 18.254  13.422  1.00 20.49  ?  61  THR D C   1 
ATOM   2068 O  O   . THR B 1 66  ? 52.510 18.211  12.210  1.00 21.52  ?  61  THR D O   1 
ATOM   2069 C  CB  . THR B 1 66  ? 53.322 20.717  14.044  1.00 24.14  ?  61  THR D CB  1 
ATOM   2070 O  OG1 . THR B 1 66  ? 54.412 21.519  14.520  1.00 26.20  ?  61  THR D OG1 1 
ATOM   2071 C  CG2 . THR B 1 66  ? 52.167 20.873  15.014  1.00 23.36  ?  61  THR D CG2 1 
ATOM   2072 N  N   . LEU B 1 67  ? 52.207 17.472  14.341  1.00 20.00  ?  62  LEU D N   1 
ATOM   2073 C  CA  . LEU B 1 67  ? 51.063 16.602  14.030  1.00 17.65  ?  62  LEU D CA  1 
ATOM   2074 C  C   . LEU B 1 67  ? 49.802 17.371  14.404  1.00 16.83  ?  62  LEU D C   1 
ATOM   2075 O  O   . LEU B 1 67  ? 49.877 18.206  15.326  1.00 19.20  ?  62  LEU D O   1 
ATOM   2076 C  CB  . LEU B 1 67  ? 51.240 15.267  14.754  1.00 18.72  ?  62  LEU D CB  1 
ATOM   2077 C  CG  . LEU B 1 67  ? 52.547 14.534  14.431  1.00 18.97  ?  62  LEU D CG  1 
ATOM   2078 C  CD1 . LEU B 1 67  ? 52.637 13.215  15.155  1.00 18.29  ?  62  LEU D CD1 1 
ATOM   2079 C  CD2 . LEU B 1 67  ? 52.770 14.341  12.937  1.00 20.60  ?  62  LEU D CD2 1 
ATOM   2080 N  N   . TRP B 1 68  ? 48.734 17.136  13.652  1.00 15.26  ?  63  TRP D N   1 
ATOM   2081 C  CA  . TRP B 1 68  ? 47.384 17.696  13.846  1.00 15.57  ?  63  TRP D CA  1 
ATOM   2082 C  C   . TRP B 1 68  ? 46.439 16.586  14.295  1.00 15.82  ?  63  TRP D C   1 
ATOM   2083 O  O   . TRP B 1 68  ? 46.534 15.485  13.670  1.00 14.86  ?  63  TRP D O   1 
ATOM   2084 C  CB  . TRP B 1 68  ? 46.868 18.285  12.545  1.00 18.17  ?  63  TRP D CB  1 
ATOM   2085 C  CG  . TRP B 1 68  ? 47.515 19.542  12.122  1.00 16.90  ?  63  TRP D CG  1 
ATOM   2086 C  CD1 . TRP B 1 68  ? 48.786 19.969  12.367  1.00 17.41  ?  63  TRP D CD1 1 
ATOM   2087 C  CD2 . TRP B 1 68  ? 46.946 20.461  11.198  1.00 17.03  ?  63  TRP D CD2 1 
ATOM   2088 N  NE1 . TRP B 1 68  ? 49.018 21.140  11.700  1.00 18.20  ?  63  TRP D NE1 1 
ATOM   2089 C  CE2 . TRP B 1 68  ? 47.909 21.468  10.966  1.00 17.71  ?  63  TRP D CE2 1 
ATOM   2090 C  CE3 . TRP B 1 68  ? 45.708 20.539  10.578  1.00 16.48  ?  63  TRP D CE3 1 
ATOM   2091 C  CZ2 . TRP B 1 68  ? 47.660 22.559  10.139  1.00 19.64  ?  63  TRP D CZ2 1 
ATOM   2092 C  CZ3 . TRP B 1 68  ? 45.480 21.604  9.733   1.00 18.42  ?  63  TRP D CZ3 1 
ATOM   2093 C  CH2 . TRP B 1 68  ? 46.414 22.618  9.546   1.00 19.55  ?  63  TRP D CH2 1 
ATOM   2094 N  N   . GLY B 1 69  ? 45.631 16.830  15.340  1.00 14.22  ?  64  GLY D N   1 
ATOM   2095 C  CA  . GLY B 1 69  ? 44.701 15.832  15.848  1.00 15.10  ?  64  GLY D CA  1 
ATOM   2096 C  C   . GLY B 1 69  ? 43.401 16.456  16.312  1.00 15.87  ?  64  GLY D C   1 
ATOM   2097 O  O   . GLY B 1 69  ? 43.326 17.691  16.480  1.00 15.83  ?  64  GLY D O   1 
ATOM   2098 N  N   . HIS B 1 70  ? 42.411 15.646  16.607  1.00 14.71  ?  65  HIS D N   1 
ATOM   2099 C  CA  . HIS B 1 70  ? 41.251 16.151  17.380  1.00 15.22  ?  65  HIS D CA  1 
ATOM   2100 C  C   . HIS B 1 70  ? 40.673 15.059  18.242  1.00 14.54  ?  65  HIS D C   1 
ATOM   2101 O  O   . HIS B 1 70  ? 40.880 13.857  17.979  1.00 13.85  ?  65  HIS D O   1 
ATOM   2102 C  CB  . HIS B 1 70  ? 40.221 16.832  16.484  1.00 16.32  ?  65  HIS D CB  1 
ATOM   2103 C  CG  . HIS B 1 70  ? 39.387 15.896  15.672  1.00 15.46  ?  65  HIS D CG  1 
ATOM   2104 N  ND1 . HIS B 1 70  ? 39.890 15.317  14.545  1.00 14.51  ?  65  HIS D ND1 1 
ATOM   2105 C  CD2 . HIS B 1 70  ? 38.105 15.451  15.818  1.00 16.50  ?  65  HIS D CD2 1 
ATOM   2106 C  CE1 . HIS B 1 70  ? 38.946 14.560  14.007  1.00 16.90  ?  65  HIS D CE1 1 
ATOM   2107 N  NE2 . HIS B 1 70  ? 37.858 14.593  14.771  1.00 15.96  ?  65  HIS D NE2 1 
ATOM   2108 N  N   . MET B 1 71  ? 39.944 15.475  19.255  1.00 15.30  ?  66  MET D N   1 
ATOM   2109 C  CA  . MET B 1 71  ? 39.185 14.566  20.101  1.00 16.05  ?  66  MET D CA  1 
ATOM   2110 C  C   . MET B 1 71  ? 37.886 15.268  20.419  1.00 15.69  ?  66  MET D C   1 
ATOM   2111 O  O   . MET B 1 71  ? 37.694 16.361  19.915  1.00 14.81  ?  66  MET D O   1 
ATOM   2112 C  CB  . MET B 1 71  ? 39.925 14.216  21.395  1.00 18.05  ?  66  MET D CB  1 
ATOM   2113 C  CG  . MET B 1 71  ? 39.955 15.333  22.434  1.00 18.65  ?  66  MET D CG  1 
ATOM   2114 S  SD  . MET B 1 71  ? 40.723 14.786  24.013  1.00 27.33  ?  66  MET D SD  1 
ATOM   2115 C  CE  . MET B 1 71  ? 42.352 14.936  23.315  1.00 24.26  ?  66  MET D CE  1 
ATOM   2116 N  N   . ASN B 1 72  ? 37.062 14.609  21.230  1.00 15.85  ?  67  ASN D N   1 
ATOM   2117 C  CA  . ASN B 1 72  ? 35.795 15.167  21.749  1.00 16.19  ?  67  ASN D CA  1 
ATOM   2118 C  C   . ASN B 1 72  ? 36.116 16.138  22.911  1.00 16.40  ?  67  ASN D C   1 
ATOM   2119 O  O   . ASN B 1 72  ? 36.694 15.705  23.911  1.00 18.06  ?  67  ASN D O   1 
ATOM   2120 C  CB  . ASN B 1 72  ? 34.860 14.071  22.194  1.00 15.43  ?  67  ASN D CB  1 
ATOM   2121 C  CG  . ASN B 1 72  ? 33.480 14.615  22.493  1.00 18.25  ?  67  ASN D CG  1 
ATOM   2122 O  OD1 . ASN B 1 72  ? 33.331 15.813  22.737  1.00 17.90  ?  67  ASN D OD1 1 
ATOM   2123 N  ND2 . ASN B 1 72  ? 32.475 13.755  22.417  1.00 17.88  ?  67  ASN D ND2 1 
ATOM   2124 N  N   . ARG B 1 73  ? 35.740 17.415  22.786  1.00 16.27  ?  68  ARG D N   1 
ATOM   2125 C  CA  . ARG B 1 73  ? 35.924 18.404  23.873  1.00 19.81  ?  68  ARG D CA  1 
ATOM   2126 C  C   . ARG B 1 73  ? 35.257 17.986  25.167  1.00 19.06  ?  68  ARG D C   1 
ATOM   2127 O  O   . ARG B 1 73  ? 35.618 18.547  26.162  1.00 21.18  ?  68  ARG D O   1 
ATOM   2128 C  CB  . ARG B 1 73  ? 35.335 19.758  23.501  1.00 21.80  ?  68  ARG D CB  1 
ATOM   2129 C  CG  . ARG B 1 73  ? 36.429 20.757  23.236  1.00 22.00  ?  68  ARG D CG  1 
ATOM   2130 C  CD  . ARG B 1 73  ? 35.864 22.104  22.925  1.00 20.04  ?  68  ARG D CD  1 
ATOM   2131 N  NE  . ARG B 1 73  ? 36.805 22.595  21.969  1.00 15.55  ?  68  ARG D NE  1 
ATOM   2132 C  CZ  . ARG B 1 73  ? 37.618 23.581  22.179  1.00 15.17  ?  68  ARG D CZ  1 
ATOM   2133 N  NH1 . ARG B 1 73  ? 37.698 24.157  23.361  1.00 18.36  ?  68  ARG D NH1 1 
ATOM   2134 N  NH2 . ARG B 1 73  ? 38.395 23.970  21.207  1.00 18.77  ?  68  ARG D NH2 1 
ATOM   2135 N  N   . ALA B 1 74  ? 34.253 17.098  25.116  1.00 20.91  ?  69  ALA D N   1 
ATOM   2136 C  CA  . ALA B 1 74  ? 33.464 16.632  26.276  1.00 20.29  ?  69  ALA D CA  1 
ATOM   2137 C  C   . ALA B 1 74  ? 34.143 15.413  26.917  1.00 19.17  ?  69  ALA D C   1 
ATOM   2138 O  O   . ALA B 1 74  ? 33.789 15.009  28.034  1.00 19.69  ?  69  ALA D O   1 
ATOM   2139 C  CB  . ALA B 1 74  ? 32.062 16.323  25.836  1.00 20.35  ?  69  ALA D CB  1 
ATOM   2140 N  N   . ASN B 1 75  ? 35.092 14.803  26.226  1.00 19.64  ?  70  ASN D N   1 
ATOM   2141 C  CA  . ASN B 1 75  ? 35.963 13.749  26.790  1.00 18.39  ?  70  ASN D CA  1 
ATOM   2142 C  C   . ASN B 1 75  ? 36.778 14.347  27.934  1.00 17.95  ?  70  ASN D C   1 
ATOM   2143 O  O   . ASN B 1 75  ? 37.601 15.222  27.679  1.00 15.49  ?  70  ASN D O   1 
ATOM   2144 C  CB  . ASN B 1 75  ? 36.898 13.235  25.696  1.00 17.18  ?  70  ASN D CB  1 
ATOM   2145 C  CG  . ASN B 1 75  ? 37.772 12.079  26.094  1.00 18.95  ?  70  ASN D CG  1 
ATOM   2146 O  OD1 . ASN B 1 75  ? 38.024 11.871  27.285  1.00 17.08  ?  70  ASN D OD1 1 
ATOM   2147 N  ND2 . ASN B 1 75  ? 38.248 11.354  25.082  1.00 18.72  ?  70  ASN D ND2 1 
ATOM   2148 N  N   . PRO B 1 76  ? 36.669 13.810  29.180  1.00 16.39  ?  71  PRO D N   1 
ATOM   2149 C  CA  . PRO B 1 76  ? 37.405 14.376  30.315  1.00 18.05  ?  71  PRO D CA  1 
ATOM   2150 C  C   . PRO B 1 76  ? 38.931 14.482  30.098  1.00 17.44  ?  71  PRO D C   1 
ATOM   2151 O  O   . PRO B 1 76  ? 39.596 15.261  30.760  1.00 17.05  ?  71  PRO D O   1 
ATOM   2152 C  CB  . PRO B 1 76  ? 37.026 13.415  31.460  1.00 18.91  ?  71  PRO D CB  1 
ATOM   2153 C  CG  . PRO B 1 76  ? 35.658 12.904  31.053  1.00 21.37  ?  71  PRO D CG  1 
ATOM   2154 C  CD  . PRO B 1 76  ? 35.852 12.647  29.580  1.00 17.98  ?  71  PRO D CD  1 
ATOM   2155 N  N   . HIS B 1 77  ? 39.470 13.724  29.139  1.00 16.52  ?  72  HIS D N   1 
ATOM   2156 C  CA  . HIS B 1 77  ? 40.913 13.728  28.783  1.00 15.98  ?  72  HIS D CA  1 
ATOM   2157 C  C   . HIS B 1 77  ? 41.260 15.149  28.299  1.00 15.72  ?  72  HIS D C   1 
ATOM   2158 O  O   . HIS B 1 77  ? 42.314 15.648  28.560  1.00 19.40  ?  72  HIS D O   1 
ATOM   2159 C  CB  . HIS B 1 77  ? 41.180 12.629  27.754  1.00 15.51  ?  72  HIS D CB  1 
ATOM   2160 C  CG  . HIS B 1 77  ? 42.641 12.367  27.507  1.00 14.13  ?  72  HIS D CG  1 
ATOM   2161 N  ND1 . HIS B 1 77  ? 43.068 11.371  26.675  1.00 14.04  ?  72  HIS D ND1 1 
ATOM   2162 C  CD2 . HIS B 1 77  ? 43.761 12.938  28.006  1.00 15.53  ?  72  HIS D CD2 1 
ATOM   2163 C  CE1 . HIS B 1 77  ? 44.407 11.313  26.650  1.00 13.32  ?  72  HIS D CE1 1 
ATOM   2164 N  NE2 . HIS B 1 77  ? 44.859 12.315  27.403  1.00 15.26  ?  72  HIS D NE2 1 
ATOM   2165 N  N   . TRP B 1 78  ? 40.359 15.795  27.623  1.00 16.53  ?  73  TRP D N   1 
ATOM   2166 C  CA  . TRP B 1 78  ? 40.588 17.173  27.127  1.00 17.69  ?  73  TRP D CA  1 
ATOM   2167 C  C   . TRP B 1 78  ? 40.837 18.104  28.327  1.00 19.16  ?  73  TRP D C   1 
ATOM   2168 O  O   . TRP B 1 78  ? 41.897 18.732  28.359  1.00 17.77  ?  73  TRP D O   1 
ATOM   2169 C  CB  . TRP B 1 78  ? 39.432 17.608  26.227  1.00 17.79  ?  73  TRP D CB  1 
ATOM   2170 C  CG  . TRP B 1 78  ? 39.558 19.025  25.756  1.00 16.79  ?  73  TRP D CG  1 
ATOM   2171 C  CD1 . TRP B 1 78  ? 39.031 20.113  26.383  1.00 16.59  ?  73  TRP D CD1 1 
ATOM   2172 C  CD2 . TRP B 1 78  ? 40.258 19.493  24.594  1.00 15.24  ?  73  TRP D CD2 1 
ATOM   2173 N  NE1 . TRP B 1 78  ? 39.295 21.228  25.647  1.00 19.01  ?  73  TRP D NE1 1 
ATOM   2174 C  CE2 . TRP B 1 78  ? 40.056 20.891  24.552  1.00 17.95  ?  73  TRP D CE2 1 
ATOM   2175 C  CE3 . TRP B 1 78  ? 41.040 18.890  23.595  1.00 15.51  ?  73  TRP D CE3 1 
ATOM   2176 C  CZ2 . TRP B 1 78  ? 40.600 21.684  23.541  1.00 17.90  ?  73  TRP D CZ2 1 
ATOM   2177 C  CZ3 . TRP B 1 78  ? 41.573 19.670  22.586  1.00 15.23  ?  73  TRP D CZ3 1 
ATOM   2178 C  CH2 . TRP B 1 78  ? 41.336 21.061  22.571  1.00 16.56  ?  73  TRP D CH2 1 
ATOM   2179 N  N   . ALA B 1 79  ? 39.998 18.093  29.362  1.00 20.54  ?  74  ALA D N   1 
ATOM   2180 C  CA  . ALA B 1 79  ? 40.192 18.967  30.551  1.00 22.73  ?  74  ALA D CA  1 
ATOM   2181 C  C   . ALA B 1 79  ? 41.488 18.600  31.293  1.00 25.11  ?  74  ALA D C   1 
ATOM   2182 O  O   . ALA B 1 79  ? 42.132 19.498  31.878  1.00 23.13  ?  74  ALA D O   1 
ATOM   2183 C  CB  . ALA B 1 79  ? 38.993 18.886  31.450  1.00 21.62  ?  74  ALA D CB  1 
ATOM   2184 N  N   . ALA B 1 80  ? 41.867 17.319  31.290  1.00 22.33  ?  75  ALA D N   1 
ATOM   2185 C  CA  . ALA B 1 80  ? 42.951 16.809  32.120  1.00 23.25  ?  75  ALA D CA  1 
ATOM   2186 C  C   . ALA B 1 80  ? 44.253 17.202  31.413  1.00 25.75  ?  75  ALA D C   1 
ATOM   2187 O  O   . ALA B 1 80  ? 45.254 17.423  32.082  1.00 26.62  ?  75  ALA D O   1 
ATOM   2188 C  CB  . ALA B 1 80  ? 42.781 15.338  32.338  1.00 27.43  ?  75  ALA D CB  1 
ATOM   2189 N  N   . LEU B 1 81  ? 44.222 17.442  30.110  1.00 26.69  ?  76  LEU D N   1 
ATOM   2190 C  CA  . LEU B 1 81  ? 45.466 17.847  29.425  1.00 26.19  ?  76  LEU D CA  1 
ATOM   2191 C  C   . LEU B 1 81  ? 45.962 19.182  30.010  1.00 38.29  ?  76  LEU D C   1 
ATOM   2192 O  O   . LEU B 1 81  ? 47.202 19.316  30.244  1.00 35.76  ?  76  LEU D O   1 
ATOM   2193 C  CB  . LEU B 1 81  ? 45.232 17.877  27.925  1.00 24.03  ?  76  LEU D CB  1 
ATOM   2194 C  CG  . LEU B 1 81  ? 45.161 16.493  27.298  1.00 24.48  ?  76  LEU D CG  1 
ATOM   2195 C  CD1 . LEU B 1 81  ? 44.533 16.560  25.896  1.00 23.85  ?  76  LEU D CD1 1 
ATOM   2196 C  CD2 . LEU B 1 81  ? 46.561 15.880  27.293  1.00 25.00  ?  76  LEU D CD2 1 
ATOM   2197 N  N   . GLY B 1 82  ? 45.043 20.083  30.367  1.00 38.28  ?  77  GLY D N   1 
ATOM   2198 C  CA  . GLY B 1 82  ? 45.432 21.458  30.692  1.00 41.85  ?  77  GLY D CA  1 
ATOM   2199 C  C   . GLY B 1 82  ? 46.233 21.986  29.522  1.00 44.62  ?  77  GLY D C   1 
ATOM   2200 O  O   . GLY B 1 82  ? 45.982 21.445  28.367  1.00 38.27  ?  77  GLY D O   1 
ATOM   2201 N  N   . GLY B 1 83  ? 47.250 22.818  29.818  1.00 48.17  ?  78  GLY D N   1 
ATOM   2202 C  CA  . GLY B 1 83  ? 47.872 23.774  28.873  1.00 47.60  ?  78  GLY D CA  1 
ATOM   2203 C  C   . GLY B 1 83  ? 49.080 23.214  28.143  1.00 47.55  ?  78  GLY D C   1 
ATOM   2204 O  O   . GLY B 1 83  ? 49.127 23.288  26.893  1.00 47.38  ?  78  GLY D O   1 
ATOM   2205 N  N   . ALA B 1 84  ? 50.089 22.749  28.869  1.00 52.07  ?  79  ALA D N   1 
ATOM   2206 C  CA  . ALA B 1 84  ? 51.379 22.330  28.270  1.00 47.20  ?  79  ALA D CA  1 
ATOM   2207 C  C   . ALA B 1 84  ? 51.672 20.881  28.652  1.00 43.34  ?  79  ALA D C   1 
ATOM   2208 O  O   . ALA B 1 84  ? 52.746 20.620  29.210  1.00 46.54  ?  79  ALA D O   1 
ATOM   2209 C  CB  . ALA B 1 84  ? 52.473 23.262  28.704  1.00 47.77  ?  79  ALA D CB  1 
ATOM   2210 N  N   . ALA B 1 85  ? 50.731 19.981  28.354  1.00 41.43  ?  80  ALA D N   1 
ATOM   2211 C  CA  . ALA B 1 85  ? 50.828 18.550  28.719  1.00 36.54  ?  80  ALA D CA  1 
ATOM   2212 C  C   . ALA B 1 85  ? 51.901 17.908  27.847  1.00 29.53  ?  80  ALA D C   1 
ATOM   2213 O  O   . ALA B 1 85  ? 51.856 18.099  26.607  1.00 24.50  ?  80  ALA D O   1 
ATOM   2214 C  CB  . ALA B 1 85  ? 49.520 17.831  28.555  1.00 34.30  ?  80  ALA D CB  1 
ATOM   2215 N  N   . ASN B 1 86  ? 52.821 17.191  28.491  1.00 25.85  ?  81  ASN D N   1 
ATOM   2216 C  CA  . ASN B 1 86  ? 53.774 16.289  27.803  1.00 24.95  ?  81  ASN D CA  1 
ATOM   2217 C  C   . ASN B 1 86  ? 53.037 14.993  27.483  1.00 20.48  ?  81  ASN D C   1 
ATOM   2218 O  O   . ASN B 1 86  ? 52.538 14.347  28.430  1.00 17.74  ?  81  ASN D O   1 
ATOM   2219 C  CB  . ASN B 1 86  ? 55.004 16.030  28.629  1.00 24.26  ?  81  ASN D CB  1 
ATOM   2220 C  CG  . ASN B 1 86  ? 55.746 17.307  28.919  1.00 27.80  ?  81  ASN D CG  1 
ATOM   2221 O  OD1 . ASN B 1 86  ? 55.905 18.133  28.027  1.00 32.21  ?  81  ASN D OD1 1 
ATOM   2222 N  ND2 . ASN B 1 86  ? 56.170 17.460  30.157  1.00 33.68  ?  81  ASN D ND2 1 
ATOM   2223 N  N   . VAL B 1 87  ? 52.919 14.692  26.196  1.00 18.22  ?  82  VAL D N   1 
ATOM   2224 C  CA  . VAL B 1 87  ? 52.082 13.546  25.766  1.00 16.87  ?  82  VAL D CA  1 
ATOM   2225 C  C   . VAL B 1 87  ? 52.892 12.576  24.918  1.00 15.83  ?  82  VAL D C   1 
ATOM   2226 O  O   . VAL B 1 87  ? 53.956 12.923  24.408  1.00 15.64  ?  82  VAL D O   1 
ATOM   2227 C  CB  . VAL B 1 87  ? 50.816 14.008  25.035  1.00 18.25  ?  82  VAL D CB  1 
ATOM   2228 C  CG1 . VAL B 1 87  ? 50.042 14.972  25.895  1.00 19.79  ?  82  VAL D CG1 1 
ATOM   2229 C  CG2 . VAL B 1 87  ? 51.098 14.589  23.670  1.00 20.17  ?  82  VAL D CG2 1 
ATOM   2230 N  N   . VAL B 1 88  ? 52.388 11.350  24.819  1.00 15.06  ?  83  VAL D N   1 
ATOM   2231 C  CA  . VAL B 1 88  ? 52.859 10.364  23.815  1.00 13.85  ?  83  VAL D CA  1 
ATOM   2232 C  C   . VAL B 1 88  ? 51.668 9.983   22.947  1.00 13.78  ?  83  VAL D C   1 
ATOM   2233 O  O   . VAL B 1 88  ? 50.549 9.850   23.458  1.00 14.11  ?  83  VAL D O   1 
ATOM   2234 C  CB  . VAL B 1 88  ? 53.537 9.124   24.438  1.00 13.50  ?  83  VAL D CB  1 
ATOM   2235 C  CG1 . VAL B 1 88  ? 52.691 8.522   25.548  1.00 15.47  ?  83  VAL D CG1 1 
ATOM   2236 C  CG2 . VAL B 1 88  ? 53.848 8.097   23.380  1.00 13.87  ?  83  VAL D CG2 1 
ATOM   2237 N  N   . ALA B 1 89  ? 51.898 9.898   21.651  1.00 12.87  ?  84  ALA D N   1 
ATOM   2238 C  CA  . ALA B 1 89  ? 50.903 9.393   20.689  1.00 12.88  ?  84  ALA D CA  1 
ATOM   2239 C  C   . ALA B 1 89  ? 51.506 8.127   20.089  1.00 14.54  ?  84  ALA D C   1 
ATOM   2240 O  O   . ALA B 1 89  ? 52.651 8.209   19.567  1.00 13.33  ?  84  ALA D O   1 
ATOM   2241 C  CB  . ALA B 1 89  ? 50.570 10.419  19.653  1.00 13.49  ?  84  ALA D CB  1 
ATOM   2242 N  N   . THR B 1 90  ? 50.831 6.984   20.256  1.00 14.29  ?  85  THR D N   1 
ATOM   2243 C  CA  . THR B 1 90  ? 51.326 5.663   19.783  1.00 14.32  ?  85  THR D CA  1 
ATOM   2244 C  C   . THR B 1 90  ? 50.533 5.230   18.544  1.00 13.30  ?  85  THR D C   1 
ATOM   2245 O  O   . THR B 1 90  ? 49.265 5.173   18.590  1.00 14.60  ?  85  THR D O   1 
ATOM   2246 C  CB  . THR B 1 90  ? 51.228 4.578   20.856  1.00 15.15  ?  85  THR D CB  1 
ATOM   2247 O  OG1 . THR B 1 90  ? 51.999 5.016   21.960  1.00 15.90  ?  85  THR D OG1 1 
ATOM   2248 C  CG2 . THR B 1 90  ? 51.768 3.254   20.351  1.00 15.72  ?  85  THR D CG2 1 
ATOM   2249 N  N   . PHE B 1 91  ? 51.240 4.980   17.464  1.00 12.09  ?  86  PHE D N   1 
ATOM   2250 C  CA  . PHE B 1 91  ? 50.664 4.447   16.211  1.00 13.37  ?  86  PHE D CA  1 
ATOM   2251 C  C   . PHE B 1 91  ? 51.072 2.979   16.114  1.00 15.15  ?  86  PHE D C   1 
ATOM   2252 O  O   . PHE B 1 91  ? 52.247 2.616   16.266  1.00 17.35  ?  86  PHE D O   1 
ATOM   2253 C  CB  . PHE B 1 91  ? 51.141 5.257   15.017  1.00 12.70  ?  86  PHE D CB  1 
ATOM   2254 C  CG  . PHE B 1 91  ? 50.893 6.742   15.126  1.00 12.71  ?  86  PHE D CG  1 
ATOM   2255 C  CD1 . PHE B 1 91  ? 51.656 7.535   15.960  1.00 11.73  ?  86  PHE D CD1 1 
ATOM   2256 C  CD2 . PHE B 1 91  ? 49.876 7.355   14.398  1.00 12.45  ?  86  PHE D CD2 1 
ATOM   2257 C  CE1 . PHE B 1 91  ? 51.456 8.892   16.013  1.00 11.16  ?  86  PHE D CE1 1 
ATOM   2258 C  CE2 . PHE B 1 91  ? 49.725 8.733   14.416  1.00 12.69  ?  86  PHE D CE2 1 
ATOM   2259 C  CZ  . PHE B 1 91  ? 50.456 9.484   15.300  1.00 12.40  ?  86  PHE D CZ  1 
ATOM   2260 N  N   . ALA B 1 92  ? 50.106 2.144   15.813  1.00 15.55  ?  87  ALA D N   1 
ATOM   2261 C  CA  . ALA B 1 92  ? 50.296 0.690   15.778  1.00 17.10  ?  87  ALA D CA  1 
ATOM   2262 C  C   . ALA B 1 92  ? 50.013 0.200   14.363  1.00 16.86  ?  87  ALA D C   1 
ATOM   2263 O  O   . ALA B 1 92  ? 48.853 0.333   13.893  1.00 15.46  ?  87  ALA D O   1 
ATOM   2264 C  CB  . ALA B 1 92  ? 49.407 0.028   16.810  1.00 17.46  ?  87  ALA D CB  1 
ATOM   2265 N  N   . GLY B 1 93  ? 51.005 -0.434  13.744  1.00 15.92  ?  88  GLY D N   1 
ATOM   2266 C  CA  . GLY B 1 93  ? 50.855 -0.998  12.395  1.00 15.73  ?  88  GLY D CA  1 
ATOM   2267 C  C   . GLY B 1 93  ? 50.670 -2.509  12.328  1.00 15.12  ?  88  GLY D C   1 
ATOM   2268 O  O   . GLY B 1 93  ? 50.113 -3.152  13.231  1.00 12.53  ?  88  GLY D O   1 
ATOM   2269 N  N   . PRO B 1 94  ? 51.053 -3.114  11.177  1.00 15.81  ?  89  PRO D N   1 
ATOM   2270 C  CA  . PRO B 1 94  ? 50.894 -4.556  10.955  1.00 16.56  ?  89  PRO D CA  1 
ATOM   2271 C  C   . PRO B 1 94  ? 51.522 -5.364  12.106  1.00 15.45  ?  89  PRO D C   1 
ATOM   2272 O  O   . PRO B 1 94  ? 52.551 -4.972  12.707  1.00 15.39  ?  89  PRO D O   1 
ATOM   2273 C  CB  . PRO B 1 94  ? 51.662 -4.777  9.644   1.00 17.33  ?  89  PRO D CB  1 
ATOM   2274 C  CG  . PRO B 1 94  ? 51.525 -3.465  8.905   1.00 16.80  ?  89  PRO D CG  1 
ATOM   2275 C  CD  . PRO B 1 94  ? 51.598 -2.425  9.991   1.00 17.66  ?  89  PRO D CD  1 
ATOM   2276 N  N   . ASN B 1 95  ? 50.916 -6.507  12.420  1.00 15.72  ?  90  ASN D N   1 
ATOM   2277 C  CA  . ASN B 1 95  ? 51.387 -7.338  13.555  1.00 15.23  ?  90  ASN D CA  1 
ATOM   2278 C  C   . ASN B 1 95  ? 50.885 -8.752  13.366  1.00 15.06  ?  90  ASN D C   1 
ATOM   2279 O  O   . ASN B 1 95  ? 49.790 -8.921  12.743  1.00 14.52  ?  90  ASN D O   1 
ATOM   2280 C  CB  . ASN B 1 95  ? 50.970 -6.764  14.913  1.00 15.57  ?  90  ASN D CB  1 
ATOM   2281 C  CG  . ASN B 1 95  ? 49.477 -6.861  15.156  1.00 18.72  ?  90  ASN D CG  1 
ATOM   2282 O  OD1 . ASN B 1 95  ? 49.017 -7.850  15.690  1.00 17.53  ?  90  ASN D OD1 1 
ATOM   2283 N  ND2 . ASN B 1 95  ? 48.745 -5.826  14.772  1.00 16.52  ?  90  ASN D ND2 1 
ATOM   2284 N  N   . ALA B 1 96  ? 51.617 -9.743  13.889  1.00 13.58  ?  91  ALA D N   1 
ATOM   2285 C  CA  . ALA B 1 96  ? 51.172 -11.155 13.827  1.00 13.48  ?  91  ALA D CA  1 
ATOM   2286 C  C   . ALA B 1 96  ? 51.872 -11.997 14.863  1.00 14.94  ?  91  ALA D C   1 
ATOM   2287 O  O   . ALA B 1 96  ? 53.077 -11.791 15.070  1.00 13.98  ?  91  ALA D O   1 
ATOM   2288 C  CB  . ALA B 1 96  ? 51.433 -11.726 12.481  1.00 14.76  ?  91  ALA D CB  1 
ATOM   2289 N  N   . TYR B 1 97  ? 51.152 -12.965 15.403  1.00 15.42  ?  92  TYR D N   1 
ATOM   2290 C  CA  . TYR B 1 97  ? 51.781 -13.974 16.274  1.00 17.51  ?  92  TYR D CA  1 
ATOM   2291 C  C   . TYR B 1 97  ? 52.754 -14.830 15.472  1.00 15.77  ?  92  TYR D C   1 
ATOM   2292 O  O   . TYR B 1 97  ? 52.406 -15.219 14.361  1.00 15.45  ?  92  TYR D O   1 
ATOM   2293 C  CB  . TYR B 1 97  ? 50.705 -14.854 16.880  1.00 15.38  ?  92  TYR D CB  1 
ATOM   2294 C  CG  . TYR B 1 97  ? 51.286 -15.965 17.721  1.00 14.31  ?  92  TYR D CG  1 
ATOM   2295 C  CD1 . TYR B 1 97  ? 51.660 -15.738 19.021  1.00 13.95  ?  92  TYR D CD1 1 
ATOM   2296 C  CD2 . TYR B 1 97  ? 51.332 -17.262 17.256  1.00 15.49  ?  92  TYR D CD2 1 
ATOM   2297 C  CE1 . TYR B 1 97  ? 52.071 -16.761 19.858  1.00 14.31  ?  92  TYR D CE1 1 
ATOM   2298 C  CE2 . TYR B 1 97  ? 51.768 -18.303 18.057  1.00 15.64  ?  92  TYR D CE2 1 
ATOM   2299 C  CZ  . TYR B 1 97  ? 52.155 -18.044 19.366  1.00 15.44  ?  92  TYR D CZ  1 
ATOM   2300 O  OH  . TYR B 1 97  ? 52.553 -19.031 20.191  1.00 15.37  ?  92  TYR D OH  1 
ATOM   2301 N  N   . VAL B 1 98  ? 53.923 -15.117 16.051  1.00 16.09  ?  93  VAL D N   1 
ATOM   2302 C  CA  . VAL B 1 98  ? 54.965 -16.018 15.468  1.00 14.99  ?  93  VAL D CA  1 
ATOM   2303 C  C   . VAL B 1 98  ? 54.973 -17.345 16.243  1.00 14.74  ?  93  VAL D C   1 
ATOM   2304 O  O   . VAL B 1 98  ? 55.554 -17.394 17.371  1.00 14.40  ?  93  VAL D O   1 
ATOM   2305 C  CB  . VAL B 1 98  ? 56.355 -15.376 15.499  1.00 14.20  ?  93  VAL D CB  1 
ATOM   2306 C  CG1 . VAL B 1 98  ? 57.393 -16.296 14.870  1.00 15.95  ?  93  VAL D CG1 1 
ATOM   2307 C  CG2 . VAL B 1 98  ? 56.383 -13.986 14.861  1.00 14.62  ?  93  VAL D CG2 1 
ATOM   2308 N  N   . SER B 1 99  ? 54.453 -18.398 15.604  1.00 15.33  ?  94  SER D N   1 
ATOM   2309 C  CA  . SER B 1 99  ? 54.531 -19.793 16.079  1.00 16.54  ?  94  SER D CA  1 
ATOM   2310 C  C   . SER B 1 99  ? 55.911 -20.343 15.749  1.00 16.08  ?  94  SER D C   1 
ATOM   2311 O  O   . SER B 1 99  ? 56.287 -20.350 14.571  1.00 16.67  ?  94  SER D O   1 
ATOM   2312 C  CB  . SER B 1 99  ? 53.490 -20.645 15.437  1.00 14.87  ?  94  SER D CB  1 
ATOM   2313 O  OG  . SER B 1 99  ? 53.724 -22.004 15.753  1.00 15.59  ?  94  SER D OG  1 
ATOM   2314 N  N   . PRO B 1 100 ? 56.652 -20.917 16.719  1.00 18.80  ?  95  PRO D N   1 
ATOM   2315 C  CA  . PRO B 1 100 ? 57.930 -21.555 16.385  1.00 17.89  ?  95  PRO D CA  1 
ATOM   2316 C  C   . PRO B 1 100 ? 57.773 -22.762 15.450  1.00 18.06  ?  95  PRO D C   1 
ATOM   2317 O  O   . PRO B 1 100 ? 58.760 -23.243 14.915  1.00 17.93  ?  95  PRO D O   1 
ATOM   2318 C  CB  . PRO B 1 100 ? 58.483 -22.006 17.739  1.00 18.51  ?  95  PRO D CB  1 
ATOM   2319 C  CG  . PRO B 1 100 ? 57.746 -21.178 18.758  1.00 18.86  ?  95  PRO D CG  1 
ATOM   2320 C  CD  . PRO B 1 100 ? 56.361 -20.978 18.164  1.00 17.53  ?  95  PRO D CD  1 
ATOM   2321 N  N   . ALA B 1 101 ? 56.541 -23.219 15.197  1.00 18.56  ?  96  ALA D N   1 
ATOM   2322 C  CA  . ALA B 1 101 ? 56.311 -24.276 14.191  1.00 21.24  ?  96  ALA D CA  1 
ATOM   2323 C  C   . ALA B 1 101 ? 56.901 -23.808 12.859  1.00 23.42  ?  96  ALA D C   1 
ATOM   2324 O  O   . ALA B 1 101 ? 57.419 -24.638 12.095  1.00 22.58  ?  96  ALA D O   1 
ATOM   2325 C  CB  . ALA B 1 101 ? 54.841 -24.589 14.081  1.00 20.54  ?  96  ALA D CB  1 
ATOM   2326 N  N   . VAL B 1 102 ? 56.782 -22.511 12.583  1.00 21.74  ?  97  VAL D N   1 
ATOM   2327 C  CA  . VAL B 1 102 ? 57.238 -21.866 11.321  1.00 24.64  ?  97  VAL D CA  1 
ATOM   2328 C  C   . VAL B 1 102 ? 58.763 -21.965 11.217  1.00 23.41  ?  97  VAL D C   1 
ATOM   2329 O  O   . VAL B 1 102 ? 59.264 -22.073 10.083  1.00 23.67  ?  97  VAL D O   1 
ATOM   2330 C  CB  . VAL B 1 102 ? 56.773 -20.403 11.269  1.00 25.71  ?  97  VAL D CB  1 
ATOM   2331 C  CG1 . VAL B 1 102 ? 57.312 -19.701 10.049  1.00 30.38  ?  97  VAL D CG1 1 
ATOM   2332 C  CG2 . VAL B 1 102 ? 55.259 -20.332 11.282  1.00 28.26  ?  97  VAL D CG2 1 
ATOM   2333 N  N   . TYR B 1 103 ? 59.462 -21.874 12.346  1.00 23.61  ?  98  TYR D N   1 
ATOM   2334 C  CA  . TYR B 1 103 ? 60.952 -21.864 12.389  1.00 21.66  ?  98  TYR D CA  1 
ATOM   2335 C  C   . TYR B 1 103 ? 61.491 -23.212 11.912  1.00 24.27  ?  98  TYR D C   1 
ATOM   2336 O  O   . TYR B 1 103 ? 62.590 -23.215 11.328  1.00 25.03  ?  98  TYR D O   1 
ATOM   2337 C  CB  . TYR B 1 103 ? 61.469 -21.612 13.802  1.00 20.76  ?  98  TYR D CB  1 
ATOM   2338 C  CG  . TYR B 1 103 ? 61.161 -20.286 14.441  1.00 19.46  ?  98  TYR D CG  1 
ATOM   2339 C  CD1 . TYR B 1 103 ? 60.718 -19.178 13.734  1.00 20.62  ?  98  TYR D CD1 1 
ATOM   2340 C  CD2 . TYR B 1 103 ? 61.384 -20.133 15.797  1.00 20.77  ?  98  TYR D CD2 1 
ATOM   2341 C  CE1 . TYR B 1 103 ? 60.501 -17.960 14.370  1.00 20.16  ?  98  TYR D CE1 1 
ATOM   2342 C  CE2 . TYR B 1 103 ? 61.139 -18.939 16.453  1.00 20.32  ?  98  TYR D CE2 1 
ATOM   2343 C  CZ  . TYR B 1 103 ? 60.716 -17.837 15.738  1.00 20.89  ?  98  TYR D CZ  1 
ATOM   2344 O  OH  . TYR B 1 103 ? 60.524 -16.681 16.438  1.00 19.47  ?  98  TYR D OH  1 
ATOM   2345 N  N   . ARG B 1 104 ? 60.786 -24.306 12.244  1.00 25.56  ?  99  ARG D N   1 
ATOM   2346 C  CA  . ARG B 1 104 ? 61.212 -25.718 12.031  1.00 30.11  ?  99  ARG D CA  1 
ATOM   2347 C  C   . ARG B 1 104 ? 62.560 -25.944 12.722  1.00 29.43  ?  99  ARG D C   1 
ATOM   2348 O  O   . ARG B 1 104 ? 63.358 -26.737 12.223  1.00 35.17  ?  99  ARG D O   1 
ATOM   2349 C  CB  . ARG B 1 104 ? 61.298 -26.057 10.537  1.00 31.85  ?  99  ARG D CB  1 
ATOM   2350 C  CG  . ARG B 1 104 ? 60.015 -25.791 9.764   1.00 35.15  ?  99  ARG D CG  1 
ATOM   2351 C  CD  . ARG B 1 104 ? 59.961 -26.401 8.369   1.00 37.89  ?  99  ARG D CD  1 
ATOM   2352 N  NE  . ARG B 1 104 ? 61.191 -26.338 7.577   1.00 40.21  ?  99  ARG D NE  1 
ATOM   2353 C  CZ  . ARG B 1 104 ? 61.438 -25.477 6.580   1.00 44.66  ?  99  ARG D CZ  1 
ATOM   2354 N  NH1 . ARG B 1 104 ? 60.559 -24.543 6.252   1.00 46.59  ?  99  ARG D NH1 1 
ATOM   2355 N  NH2 . ARG B 1 104 ? 62.582 -25.545 5.917   1.00 46.00  ?  99  ARG D NH2 1 
ATOM   2356 N  N   . THR B 1 105 ? 62.819 -25.234 13.811  1.00 29.21  ?  100 THR D N   1 
ATOM   2357 C  CA  . THR B 1 105 ? 64.060 -25.396 14.613  1.00 29.54  ?  100 THR D CA  1 
ATOM   2358 C  C   . THR B 1 105 ? 63.648 -25.706 16.038  1.00 26.50  ?  100 THR D C   1 
ATOM   2359 O  O   . THR B 1 105 ? 62.451 -25.542 16.363  1.00 23.78  ?  100 THR D O   1 
ATOM   2360 C  CB  . THR B 1 105 ? 64.955 -24.152 14.569  1.00 30.56  ?  100 THR D CB  1 
ATOM   2361 O  OG1 . THR B 1 105 ? 64.160 -23.080 15.061  1.00 28.99  ?  100 THR D OG1 1 
ATOM   2362 C  CG2 . THR B 1 105 ? 65.468 -23.867 13.175  1.00 37.33  ?  100 THR D CG2 1 
ATOM   2363 N  N   . ALA B 1 106 ? 64.604 -26.151 16.845  1.00 22.48  ?  101 ALA D N   1 
ATOM   2364 C  CA  . ALA B 1 106 ? 64.373 -26.455 18.263  1.00 21.41  ?  101 ALA D CA  1 
ATOM   2365 C  C   . ALA B 1 106 ? 65.677 -26.315 19.026  1.00 24.19  ?  101 ALA D C   1 
ATOM   2366 O  O   . ALA B 1 106 ? 66.749 -26.592 18.468  1.00 23.65  ?  101 ALA D O   1 
ATOM   2367 C  CB  . ALA B 1 106 ? 63.810 -27.844 18.388  1.00 23.71  ?  101 ALA D CB  1 
ATOM   2368 N  N   . PRO B 1 107 ? 65.634 -25.926 20.323  1.00 20.76  ?  102 PRO D N   1 
ATOM   2369 C  CA  . PRO B 1 107 ? 64.434 -25.376 20.957  1.00 21.04  ?  102 PRO D CA  1 
ATOM   2370 C  C   . PRO B 1 107 ? 64.134 -23.932 20.519  1.00 22.05  ?  102 PRO D C   1 
ATOM   2371 O  O   . PRO B 1 107 ? 64.919 -23.328 19.809  1.00 19.15  ?  102 PRO D O   1 
ATOM   2372 C  CB  . PRO B 1 107 ? 64.808 -25.323 22.440  1.00 22.05  ?  102 PRO D CB  1 
ATOM   2373 C  CG  . PRO B 1 107 ? 66.330 -25.112 22.410  1.00 21.50  ?  102 PRO D CG  1 
ATOM   2374 C  CD  . PRO B 1 107 ? 66.802 -25.905 21.213  1.00 23.11  ?  102 PRO D CD  1 
ATOM   2375 N  N   . ALA B 1 108 ? 63.003 -23.384 20.961  1.00 20.07  ?  103 ALA D N   1 
ATOM   2376 C  CA  . ALA B 1 108 ? 62.532 -22.048 20.529  1.00 18.31  ?  103 ALA D CA  1 
ATOM   2377 C  C   . ALA B 1 108 ? 61.506 -21.535 21.516  1.00 16.88  ?  103 ALA D C   1 
ATOM   2378 O  O   . ALA B 1 108 ? 61.114 -22.290 22.406  1.00 16.24  ?  103 ALA D O   1 
ATOM   2379 C  CB  . ALA B 1 108 ? 61.958 -22.142 19.147  1.00 19.04  ?  103 ALA D CB  1 
ATOM   2380 N  N   . ALA B 1 109 ? 61.087 -20.283 21.360  1.00 16.11  ?  104 ALA D N   1 
ATOM   2381 C  CA  . ALA B 1 109 ? 59.954 -19.706 22.101  1.00 17.95  ?  104 ALA D CA  1 
ATOM   2382 C  C   . ALA B 1 109 ? 59.138 -18.892 21.112  1.00 16.28  ?  104 ALA D C   1 
ATOM   2383 O  O   . ALA B 1 109 ? 59.705 -18.340 20.169  1.00 15.92  ?  104 ALA D O   1 
ATOM   2384 C  CB  . ALA B 1 109 ? 60.450 -18.907 23.279  1.00 17.66  ?  104 ALA D CB  1 
ATOM   2385 N  N   . PRO B 1 110 ? 57.803 -18.802 21.270  1.00 16.64  ?  105 PRO D N   1 
ATOM   2386 C  CA  . PRO B 1 110 ? 57.009 -17.946 20.390  1.00 16.20  ?  105 PRO D CA  1 
ATOM   2387 C  C   . PRO B 1 110 ? 57.272 -16.454 20.645  1.00 17.25  ?  105 PRO D C   1 
ATOM   2388 O  O   . PRO B 1 110 ? 57.738 -16.066 21.663  1.00 16.17  ?  105 PRO D O   1 
ATOM   2389 C  CB  . PRO B 1 110 ? 55.556 -18.241 20.763  1.00 15.97  ?  105 PRO D CB  1 
ATOM   2390 C  CG  . PRO B 1 110 ? 55.607 -19.487 21.605  1.00 16.41  ?  105 PRO D CG  1 
ATOM   2391 C  CD  . PRO B 1 110 ? 56.970 -19.455 22.287  1.00 17.98  ?  105 PRO D CD  1 
ATOM   2392 N  N   . THR B 1 111 ? 56.842 -15.605 19.726  1.00 16.74  ?  106 THR D N   1 
ATOM   2393 C  CA  . THR B 1 111 ? 56.816 -14.150 19.983  1.00 15.47  ?  106 THR D CA  1 
ATOM   2394 C  C   . THR B 1 111 ? 55.688 -13.511 19.163  1.00 15.38  ?  106 THR D C   1 
ATOM   2395 O  O   . THR B 1 111 ? 54.778 -14.223 18.573  1.00 16.28  ?  106 THR D O   1 
ATOM   2396 C  CB  . THR B 1 111 ? 58.212 -13.575 19.732  1.00 13.55  ?  106 THR D CB  1 
ATOM   2397 O  OG1 . THR B 1 111 ? 58.268 -12.244 20.245  1.00 14.83  ?  106 THR D OG1 1 
ATOM   2398 C  CG2 . THR B 1 111 ? 58.534 -13.501 18.257  1.00 16.02  ?  106 THR D CG2 1 
ATOM   2399 N  N   . TRP B 1 112 ? 55.643 -12.202 19.223  1.00 14.69  ?  107 TRP D N   1 
ATOM   2400 C  CA  . TRP B 1 112 ? 54.687 -11.408 18.420  1.00 15.74  ?  107 TRP D CA  1 
ATOM   2401 C  C   . TRP B 1 112 ? 55.480 -10.376 17.616  1.00 15.58  ?  107 TRP D C   1 
ATOM   2402 O  O   . TRP B 1 112 ? 56.230 -9.560  18.188  1.00 15.20  ?  107 TRP D O   1 
ATOM   2403 C  CB  . TRP B 1 112 ? 53.590 -10.780 19.290  1.00 16.79  ?  107 TRP D CB  1 
ATOM   2404 C  CG  . TRP B 1 112 ? 52.275 -10.539 18.586  1.00 13.48  ?  107 TRP D CG  1 
ATOM   2405 C  CD1 . TRP B 1 112 ? 52.017 -9.652  17.587  1.00 14.37  ?  107 TRP D CD1 1 
ATOM   2406 C  CD2 . TRP B 1 112 ? 51.050 -11.221 18.825  1.00 14.68  ?  107 TRP D CD2 1 
ATOM   2407 N  NE1 . TRP B 1 112 ? 50.698 -9.711  17.213  1.00 14.73  ?  107 TRP D NE1 1 
ATOM   2408 C  CE2 . TRP B 1 112 ? 50.067 -10.657 17.964  1.00 15.28  ?  107 TRP D CE2 1 
ATOM   2409 C  CE3 . TRP B 1 112 ? 50.647 -12.216 19.721  1.00 14.72  ?  107 TRP D CE3 1 
ATOM   2410 C  CZ2 . TRP B 1 112 ? 48.737 -11.093 17.941  1.00 16.11  ?  107 TRP D CZ2 1 
ATOM   2411 C  CZ3 . TRP B 1 112 ? 49.333 -12.649 19.698  1.00 16.38  ?  107 TRP D CZ3 1 
ATOM   2412 C  CH2 . TRP B 1 112 ? 48.399 -12.127 18.784  1.00 16.04  ?  107 TRP D CH2 1 
ATOM   2413 N  N   . ASN B 1 113 ? 55.394 -10.457 16.288  1.00 15.05  ?  108 ASN D N   1 
ATOM   2414 C  CA  . ASN B 1 113 ? 55.985 -9.409  15.419  1.00 14.42  ?  108 ASN D CA  1 
ATOM   2415 C  C   . ASN B 1 113 ? 54.987 -8.275  15.390  1.00 16.06  ?  108 ASN D C   1 
ATOM   2416 O  O   . ASN B 1 113 ? 53.764 -8.519  15.220  1.00 13.90  ?  108 ASN D O   1 
ATOM   2417 C  CB  . ASN B 1 113 ? 56.309 -9.991  14.056  1.00 15.42  ?  108 ASN D CB  1 
ATOM   2418 C  CG  . ASN B 1 113 ? 57.589 -10.786 14.068  1.00 17.43  ?  108 ASN D CG  1 
ATOM   2419 O  OD1 . ASN B 1 113 ? 58.230 -10.974 15.139  1.00 15.64  ?  108 ASN D OD1 1 
ATOM   2420 N  ND2 . ASN B 1 113 ? 57.870 -11.336 12.894  1.00 15.96  ?  108 ASN D ND2 1 
ATOM   2421 N  N   . PHE B 1 114 ? 55.474 -7.069  15.515  1.00 16.38  ?  109 PHE D N   1 
ATOM   2422 C  CA  . PHE B 1 114 ? 54.618 -5.888  15.562  1.00 14.87  ?  109 PHE D CA  1 
ATOM   2423 C  C   . PHE B 1 114 ? 55.434 -4.658  15.186  1.00 14.89  ?  109 PHE D C   1 
ATOM   2424 O  O   . PHE B 1 114 ? 56.730 -4.641  15.179  1.00 14.60  ?  109 PHE D O   1 
ATOM   2425 C  CB  . PHE B 1 114 ? 53.960 -5.753  16.929  1.00 16.61  ?  109 PHE D CB  1 
ATOM   2426 C  CG  . PHE B 1 114 ? 54.807 -5.180  18.022  1.00 15.85  ?  109 PHE D CG  1 
ATOM   2427 C  CD1 . PHE B 1 114 ? 55.555 -6.013  18.839  1.00 16.95  ?  109 PHE D CD1 1 
ATOM   2428 C  CD2 . PHE B 1 114 ? 54.753 -3.823  18.333  1.00 17.79  ?  109 PHE D CD2 1 
ATOM   2429 C  CE1 . PHE B 1 114 ? 56.307 -5.489  19.884  1.00 17.62  ?  109 PHE D CE1 1 
ATOM   2430 C  CE2 . PHE B 1 114 ? 55.535 -3.310  19.352  1.00 18.06  ?  109 PHE D CE2 1 
ATOM   2431 C  CZ  . PHE B 1 114 ? 56.341 -4.137  20.096  1.00 16.29  ?  109 PHE D CZ  1 
ATOM   2432 N  N   . THR B 1 115 ? 54.671 -3.634  14.884  1.00 14.80  ?  110 THR D N   1 
ATOM   2433 C  CA  . THR B 1 115 ? 55.187 -2.312  14.439  1.00 15.16  ?  110 THR D CA  1 
ATOM   2434 C  C   . THR B 1 115 ? 54.532 -1.219  15.264  1.00 14.93  ?  110 THR D C   1 
ATOM   2435 O  O   . THR B 1 115 ? 53.285 -1.203  15.410  1.00 16.49  ?  110 THR D O   1 
ATOM   2436 C  CB  . THR B 1 115 ? 55.038 -2.160  12.924  1.00 16.28  ?  110 THR D CB  1 
ATOM   2437 O  OG1 . THR B 1 115 ? 53.661 -2.271  12.556  1.00 16.80  ?  110 THR D OG1 1 
ATOM   2438 C  CG2 . THR B 1 115 ? 55.937 -3.156  12.224  1.00 15.56  ?  110 THR D CG2 1 
ATOM   2439 N  N   . SER B 1 116 ? 55.330 -0.321  15.843  1.00 15.75  ?  111 SER D N   1 
ATOM   2440 C  CA  . SER B 1 116 ? 54.768 0.851   16.555  1.00 14.55  ?  111 SER D CA  1 
ATOM   2441 C  C   . SER B 1 116 ? 55.608 2.078   16.332  1.00 14.41  ?  111 SER D C   1 
ATOM   2442 O  O   . SER B 1 116 ? 56.837 1.973   16.250  1.00 17.59  ?  111 SER D O   1 
ATOM   2443 C  CB  . SER B 1 116 ? 54.469 0.602   18.028  1.00 16.19  ?  111 SER D CB  1 
ATOM   2444 O  OG  . SER B 1 116 ? 55.605 0.219   18.766  1.00 21.31  ?  111 SER D OG  1 
ATOM   2445 N  N   . VAL B 1 117 ? 54.936 3.221   16.310  1.00 13.60  ?  112 VAL D N   1 
ATOM   2446 C  CA  . VAL B 1 117 ? 55.611 4.532   16.452  1.00 13.43  ?  112 VAL D CA  1 
ATOM   2447 C  C   . VAL B 1 117 ? 55.069 5.215   17.713  1.00 12.74  ?  112 VAL D C   1 
ATOM   2448 O  O   . VAL B 1 117 ? 53.867 5.382   17.835  1.00 12.27  ?  112 VAL D O   1 
ATOM   2449 C  CB  . VAL B 1 117 ? 55.476 5.388   15.193  1.00 13.12  ?  112 VAL D CB  1 
ATOM   2450 C  CG1 . VAL B 1 117 ? 56.006 6.832   15.389  1.00 13.75  ?  112 VAL D CG1 1 
ATOM   2451 C  CG2 . VAL B 1 117 ? 56.221 4.732   14.052  1.00 15.21  ?  112 VAL D CG2 1 
ATOM   2452 N  N   . GLN B 1 118 ? 55.985 5.689   18.536  1.00 12.51  ?  113 GLN D N   1 
ATOM   2453 C  CA  . GLN B 1 118 ? 55.736 6.574   19.690  1.00 13.65  ?  113 GLN D CA  1 
ATOM   2454 C  C   . GLN B 1 118 ? 56.326 7.940   19.454  1.00 14.69  ?  113 GLN D C   1 
ATOM   2455 O  O   . GLN B 1 118 ? 57.585 8.057   19.251  1.00 18.15  ?  113 GLN D O   1 
ATOM   2456 C  CB  . GLN B 1 118 ? 56.233 5.987   20.984  1.00 14.41  ?  113 GLN D CB  1 
ATOM   2457 C  CG  . GLN B 1 118 ? 55.445 4.764   21.402  1.00 15.42  ?  113 GLN D CG  1 
ATOM   2458 C  CD  . GLN B 1 118 ? 55.991 4.141   22.657  1.00 14.58  ?  113 GLN D CD  1 
ATOM   2459 O  OE1 . GLN B 1 118 ? 56.542 4.820   23.494  1.00 14.45  ?  113 GLN D OE1 1 
ATOM   2460 N  NE2 . GLN B 1 118 ? 55.741 2.860   22.824  1.00 14.91  ?  113 GLN D NE2 1 
ATOM   2461 N  N   . VAL B 1 119 ? 55.460 8.930   19.369  1.00 14.41  ?  114 VAL D N   1 
ATOM   2462 C  CA  . VAL B 1 119 ? 55.873 10.366  19.262  1.00 15.82  ?  114 VAL D CA  1 
ATOM   2463 C  C   . VAL B 1 119 ? 55.572 11.045  20.583  1.00 16.53  ?  114 VAL D C   1 
ATOM   2464 O  O   . VAL B 1 119 ? 54.547 10.786  21.187  1.00 16.93  ?  114 VAL D O   1 
ATOM   2465 C  CB  . VAL B 1 119 ? 55.223 11.158  18.111  1.00 18.29  ?  114 VAL D CB  1 
ATOM   2466 C  CG1 . VAL B 1 119 ? 55.692 10.705  16.745  1.00 17.90  ?  114 VAL D CG1 1 
ATOM   2467 C  CG2 . VAL B 1 119 ? 53.718 11.118  18.194  1.00 19.21  ?  114 VAL D CG2 1 
ATOM   2468 N  N   . ARG B 1 120 ? 56.500 11.868  21.038  1.00 17.66  ?  115 ARG D N   1 
ATOM   2469 C  CA  . ARG B 1 120 ? 56.342 12.613  22.299  1.00 16.62  ?  115 ARG D CA  1 
ATOM   2470 C  C   . ARG B 1 120 ? 56.616 14.098  22.021  1.00 16.65  ?  115 ARG D C   1 
ATOM   2471 O  O   . ARG B 1 120 ? 57.553 14.442  21.174  1.00 17.26  ?  115 ARG D O   1 
ATOM   2472 C  CB  . ARG B 1 120 ? 57.266 12.046  23.380  1.00 16.99  ?  115 ARG D CB  1 
ATOM   2473 C  CG  . ARG B 1 120 ? 56.935 10.614  23.777  1.00 15.12  ?  115 ARG D CG  1 
ATOM   2474 C  CD  . ARG B 1 120 ? 57.997 10.091  24.755  1.00 17.94  ?  115 ARG D CD  1 
ATOM   2475 N  NE  . ARG B 1 120 ? 57.417 8.994   25.498  1.00 17.42  ?  115 ARG D NE  1 
ATOM   2476 C  CZ  . ARG B 1 120 ? 57.187 7.760   25.036  1.00 16.17  ?  115 ARG D CZ  1 
ATOM   2477 N  NH1 . ARG B 1 120 ? 57.517 7.368   23.799  1.00 13.20  ?  115 ARG D NH1 1 
ATOM   2478 N  NH2 . ARG B 1 120 ? 56.651 6.907   25.887  1.00 16.97  ?  115 ARG D NH2 1 
ATOM   2479 N  N   . GLY B 1 121 ? 55.843 14.924  22.725  1.00 14.61  ?  116 GLY D N   1 
ATOM   2480 C  CA  . GLY B 1 121 ? 56.100 16.358  22.858  1.00 15.83  ?  116 GLY D CA  1 
ATOM   2481 C  C   . GLY B 1 121 ? 54.941 17.059  23.523  1.00 18.80  ?  116 GLY D C   1 
ATOM   2482 O  O   . GLY B 1 121 ? 54.120 16.369  24.207  1.00 17.19  ?  116 GLY D O   1 
ATOM   2483 N  N   . GLU B 1 122 ? 54.876 18.383  23.352  1.00 17.77  ?  117 GLU D N   1 
ATOM   2484 C  CA  . GLU B 1 122 ? 53.894 19.231  24.048  1.00 20.20  ?  117 GLU D CA  1 
ATOM   2485 C  C   . GLU B 1 122 ? 52.629 19.313  23.226  1.00 20.09  ?  117 GLU D C   1 
ATOM   2486 O  O   . GLU B 1 122 ? 52.706 19.629  22.039  1.00 23.58  ?  117 GLU D O   1 
ATOM   2487 C  CB  . GLU B 1 122 ? 54.366 20.662  24.240  1.00 26.54  ?  117 GLU D CB  1 
ATOM   2488 C  CG  . GLU B 1 122 ? 55.496 20.744  25.249  1.00 35.84  ?  117 GLU D CG  1 
ATOM   2489 C  CD  . GLU B 1 122 ? 55.838 22.139  25.751  1.00 41.42  ?  117 GLU D CD  1 
ATOM   2490 O  OE1 . GLU B 1 122 ? 54.962 23.039  25.648  1.00 43.25  ?  117 GLU D OE1 1 
ATOM   2491 O  OE2 . GLU B 1 122 ? 56.994 22.319  26.219  1.00 52.32  -1 117 GLU D OE2 1 
ATOM   2492 N  N   . LEU B 1 123 ? 51.509 19.006  23.851  1.00 18.69  ?  118 LEU D N   1 
ATOM   2493 C  CA  . LEU B 1 123 ? 50.221 19.139  23.185  1.00 18.43  ?  118 LEU D CA  1 
ATOM   2494 C  C   . LEU B 1 123 ? 49.696 20.558  23.430  1.00 19.85  ?  118 LEU D C   1 
ATOM   2495 O  O   . LEU B 1 123 ? 49.511 20.958  24.614  1.00 22.41  ?  118 LEU D O   1 
ATOM   2496 C  CB  . LEU B 1 123 ? 49.264 18.074  23.697  1.00 18.16  ?  118 LEU D CB  1 
ATOM   2497 C  CG  . LEU B 1 123 ? 47.942 18.114  22.923  1.00 18.65  ?  118 LEU D CG  1 
ATOM   2498 C  CD1 . LEU B 1 123 ? 47.363 16.723  22.761  1.00 17.76  ?  118 LEU D CD1 1 
ATOM   2499 C  CD2 . LEU B 1 123 ? 46.923 19.001  23.604  1.00 19.49  ?  118 LEU D CD2 1 
ATOM   2500 N  N   . ARG B 1 124 ? 49.401 21.274  22.354  1.00 19.54  ?  119 ARG D N   1 
ATOM   2501 C  CA  . ARG B 1 124 ? 48.744 22.600  22.445  1.00 19.43  ?  119 ARG D CA  1 
ATOM   2502 C  C   . ARG B 1 124 ? 47.315 22.466  21.935  1.00 20.23  ?  119 ARG D C   1 
ATOM   2503 O  O   . ARG B 1 124 ? 47.113 21.952  20.807  1.00 19.54  ?  119 ARG D O   1 
ATOM   2504 C  CB  . ARG B 1 124 ? 49.484 23.668  21.661  1.00 22.06  ?  119 ARG D CB  1 
ATOM   2505 C  CG  . ARG B 1 124 ? 48.817 25.024  21.848  1.00 25.77  ?  119 ARG D CG  1 
ATOM   2506 C  CD  . ARG B 1 124 ? 49.421 26.136  21.024  1.00 29.03  ?  119 ARG D CD  1 
ATOM   2507 N  NE  . ARG B 1 124 ? 49.344 25.955  19.572  1.00 30.22  ?  119 ARG D NE  1 
ATOM   2508 C  CZ  . ARG B 1 124 ? 48.239 26.085  18.827  1.00 31.68  ?  119 ARG D CZ  1 
ATOM   2509 N  NH1 . ARG B 1 124 ? 47.056 26.326  19.373  1.00 34.02  ?  119 ARG D NH1 1 
ATOM   2510 N  NH2 . ARG B 1 124 ? 48.327 25.956  17.518  1.00 31.14  ?  119 ARG D NH2 1 
ATOM   2511 N  N   . LYS B 1 125 ? 46.379 22.942  22.733  1.00 16.35  ?  120 LYS D N   1 
ATOM   2512 C  CA  . LYS B 1 125 ? 44.962 22.976  22.327  1.00 19.03  ?  120 LYS D CA  1 
ATOM   2513 C  C   . LYS B 1 125 ? 44.802 24.132  21.347  1.00 19.06  ?  120 LYS D C   1 
ATOM   2514 O  O   . LYS B 1 125 ? 45.305 25.246  21.620  1.00 16.90  ?  120 LYS D O   1 
ATOM   2515 C  CB  . LYS B 1 125 ? 44.054 23.179  23.527  1.00 19.19  ?  120 LYS D CB  1 
ATOM   2516 C  CG  . LYS B 1 125 ? 44.089 22.047  24.526  1.00 20.51  ?  120 LYS D CG  1 
ATOM   2517 C  CD  . LYS B 1 125 ? 43.406 22.385  25.817  1.00 21.59  ?  120 LYS D CD  1 
ATOM   2518 C  CE  . LYS B 1 125 ? 43.201 21.164  26.673  1.00 20.25  ?  120 LYS D CE  1 
ATOM   2519 N  NZ  . LYS B 1 125 ? 42.597 21.500  27.985  1.00 22.61  ?  120 LYS D NZ  1 
ATOM   2520 N  N   . VAL B 1 126 ? 44.100 23.837  20.267  1.00 19.76  ?  121 VAL D N   1 
ATOM   2521 C  CA  . VAL B 1 126 ? 43.540 24.802  19.290  1.00 20.01  ?  121 VAL D CA  1 
ATOM   2522 C  C   . VAL B 1 126 ? 42.254 25.359  19.884  1.00 19.50  ?  121 VAL D C   1 
ATOM   2523 O  O   . VAL B 1 126 ? 41.381 24.567  20.322  1.00 19.73  ?  121 VAL D O   1 
ATOM   2524 C  CB  . VAL B 1 126 ? 43.310 24.080  17.950  1.00 19.57  ?  121 VAL D CB  1 
ATOM   2525 C  CG1 . VAL B 1 126 ? 42.680 24.964  16.900  1.00 19.81  ?  121 VAL D CG1 1 
ATOM   2526 C  CG2 . VAL B 1 126 ? 44.624 23.546  17.400  1.00 21.01  ?  121 VAL D CG2 1 
ATOM   2527 N  N   . GLU B 1 127 ? 42.120 26.681  19.903  1.00 20.02  ?  122 GLU D N   1 
ATOM   2528 C  CA  . GLU B 1 127 ? 40.838 27.301  20.316  1.00 21.13  ?  122 GLU D CA  1 
ATOM   2529 C  C   . GLU B 1 127 ? 40.142 27.916  19.095  1.00 19.49  ?  122 GLU D C   1 
ATOM   2530 O  O   . GLU B 1 127 ? 38.898 27.998  19.137  1.00 24.13  ?  122 GLU D O   1 
ATOM   2531 C  CB  . GLU B 1 127 ? 41.100 28.292  21.446  1.00 20.20  ?  122 GLU D CB  1 
ATOM   2532 C  CG  . GLU B 1 127 ? 41.594 27.646  22.718  1.00 21.43  ?  122 GLU D CG  1 
ATOM   2533 C  CD  . GLU B 1 127 ? 40.677 26.661  23.415  1.00 21.83  ?  122 GLU D CD  1 
ATOM   2534 O  OE1 . GLU B 1 127 ? 39.518 26.400  22.958  1.00 22.58  ?  122 GLU D OE1 1 
ATOM   2535 O  OE2 . GLU B 1 127 ? 41.118 26.116  24.386  1.00 21.36  -1 122 GLU D OE2 1 
ATOM   2536 N  N   . SER B 1 128 ? 40.901 28.401  18.114  1.00 19.47  ?  123 SER D N   1 
ATOM   2537 C  CA  . SER B 1 128 ? 40.374 29.139  16.941  1.00 20.30  ?  123 SER D CA  1 
ATOM   2538 C  C   . SER B 1 128 ? 39.430 28.263  16.125  1.00 22.21  ?  123 SER D C   1 
ATOM   2539 O  O   . SER B 1 128 ? 39.756 27.120  15.857  1.00 18.55  ?  123 SER D O   1 
ATOM   2540 C  CB  . SER B 1 128 ? 41.467 29.732  16.119  1.00 23.34  ?  123 SER D CB  1 
ATOM   2541 O  OG  . SER B 1 128 ? 41.114 29.778  14.774  1.00 23.11  ?  123 SER D OG  1 
ATOM   2542 N  N   . ALA B 1 129 ? 38.242 28.785  15.819  1.00 24.50  ?  124 ALA D N   1 
ATOM   2543 C  CA  . ALA B 1 129 ? 37.253 28.073  14.985  1.00 26.32  ?  124 ALA D CA  1 
ATOM   2544 C  C   . ALA B 1 129 ? 37.855 27.800  13.604  1.00 26.61  ?  124 ALA D C   1 
ATOM   2545 O  O   . ALA B 1 129 ? 37.654 26.694  13.095  1.00 27.07  ?  124 ALA D O   1 
ATOM   2546 C  CB  . ALA B 1 129 ? 35.976 28.869  14.888  1.00 26.76  ?  124 ALA D CB  1 
ATOM   2547 N  N   . ASP B 1 130 ? 38.592 28.752  13.023  1.00 24.61  ?  125 ASP D N   1 
ATOM   2548 C  CA  . ASP B 1 130 ? 39.203 28.573  11.680  1.00 27.60  ?  125 ASP D CA  1 
ATOM   2549 C  C   . ASP B 1 130 ? 40.195 27.411  11.748  1.00 24.20  ?  125 ASP D C   1 
ATOM   2550 O  O   . ASP B 1 130 ? 40.133 26.555  10.876  1.00 21.73  ?  125 ASP D O   1 
ATOM   2551 C  CB  . ASP B 1 130 ? 39.846 29.846  11.129  1.00 32.96  ?  125 ASP D CB  1 
ATOM   2552 C  CG  . ASP B 1 130 ? 38.914 31.046  11.170  1.00 40.43  ?  125 ASP D CG  1 
ATOM   2553 O  OD1 . ASP B 1 130 ? 39.383 32.125  11.603  1.00 45.62  ?  125 ASP D OD1 1 
ATOM   2554 O  OD2 . ASP B 1 130 ? 37.711 30.891  10.795  1.00 42.31  -1 125 ASP D OD2 1 
ATOM   2555 N  N   . ASP B 1 131 ? 41.064 27.385  12.757  1.00 23.92  ?  126 ASP D N   1 
ATOM   2556 C  CA  . ASP B 1 131 ? 42.111 26.338  12.895  1.00 20.71  ?  126 ASP D CA  1 
ATOM   2557 C  C   . ASP B 1 131 ? 41.444 24.978  13.177  1.00 18.43  ?  126 ASP D C   1 
ATOM   2558 O  O   . ASP B 1 131 ? 41.980 23.932  12.736  1.00 18.48  ?  126 ASP D O   1 
ATOM   2559 C  CB  . ASP B 1 131 ? 43.164 26.797  13.888  1.00 24.08  ?  126 ASP D CB  1 
ATOM   2560 C  CG  . ASP B 1 131 ? 43.979 27.979  13.355  1.00 31.80  ?  126 ASP D CG  1 
ATOM   2561 O  OD1 . ASP B 1 131 ? 44.338 27.967  12.146  1.00 33.00  ?  126 ASP D OD1 1 
ATOM   2562 O  OD2 . ASP B 1 131 ? 44.224 28.927  14.130  1.00 45.36  -1 126 ASP D OD2 1 
ATOM   2563 N  N   . THR B 1 132 ? 40.339 24.965  13.918  1.00 19.09  ?  127 THR D N   1 
ATOM   2564 C  CA  . THR B 1 132 ? 39.585 23.735  14.254  1.00 18.84  ?  127 THR D CA  1 
ATOM   2565 C  C   . THR B 1 132 ? 38.989 23.147  12.962  1.00 19.95  ?  127 THR D C   1 
ATOM   2566 O  O   . THR B 1 132 ? 39.160 21.921  12.713  1.00 17.61  ?  127 THR D O   1 
ATOM   2567 C  CB  . THR B 1 132 ? 38.498 23.996  15.300  1.00 19.06  ?  127 THR D CB  1 
ATOM   2568 O  OG1 . THR B 1 132 ? 39.072 24.534  16.501  1.00 18.53  ?  127 THR D OG1 1 
ATOM   2569 C  CG2 . THR B 1 132 ? 37.707 22.745  15.655  1.00 18.60  ?  127 THR D CG2 1 
ATOM   2570 N  N   . LEU B 1 133 ? 38.273 23.960  12.179  1.00 21.17  ?  128 LEU D N   1 
ATOM   2571 C  CA  . LEU B 1 133 ? 37.676 23.522  10.902  1.00 17.78  ?  128 LEU D CA  1 
ATOM   2572 C  C   . LEU B 1 133 ? 38.774 23.091  9.913   1.00 17.73  ?  128 LEU D C   1 
ATOM   2573 O  O   . LEU B 1 133 ? 38.637 22.057  9.346   1.00 16.60  ?  128 LEU D O   1 
ATOM   2574 C  CB  . LEU B 1 133 ? 36.817 24.665  10.365  1.00 20.53  ?  128 LEU D CB  1 
ATOM   2575 C  CG  . LEU B 1 133 ? 36.113 24.305  9.064   1.00 23.87  ?  128 LEU D CG  1 
ATOM   2576 C  CD1 . LEU B 1 133 ? 35.064 23.220  9.300   1.00 25.81  ?  128 LEU D CD1 1 
ATOM   2577 C  CD2 . LEU B 1 133 ? 35.506 25.535  8.404   1.00 22.86  ?  128 LEU D CD2 1 
ATOM   2578 N  N   . ALA B 1 134 ? 39.912 23.782  9.827   1.00 16.99  ?  129 ALA D N   1 
ATOM   2579 C  CA  . ALA B 1 134 ? 41.085 23.340  9.035   1.00 16.91  ?  129 ALA D CA  1 
ATOM   2580 C  C   . ALA B 1 134 ? 41.558 21.938  9.468   1.00 15.60  ?  129 ALA D C   1 
ATOM   2581 O  O   . ALA B 1 134 ? 41.937 21.129  8.605   1.00 14.19  ?  129 ALA D O   1 
ATOM   2582 C  CB  . ALA B 1 134 ? 42.192 24.340  9.181   1.00 18.52  ?  129 ALA D CB  1 
ATOM   2583 N  N   . THR B 1 135 ? 41.596 21.682  10.771  1.00 16.62  ?  130 THR D N   1 
ATOM   2584 C  CA  . THR B 1 135 ? 42.034 20.371  11.339  1.00 16.58  ?  130 THR D CA  1 
ATOM   2585 C  C   . THR B 1 135 ? 41.151 19.249  10.769  1.00 16.27  ?  130 THR D C   1 
ATOM   2586 O  O   . THR B 1 135 ? 41.667 18.261  10.191  1.00 16.33  ?  130 THR D O   1 
ATOM   2587 C  CB  . THR B 1 135 ? 42.035 20.382  12.882  1.00 16.80  ?  130 THR D CB  1 
ATOM   2588 O  OG1 . THR B 1 135 ? 42.903 21.378  13.441  1.00 18.72  ?  130 THR D OG1 1 
ATOM   2589 C  CG2 . THR B 1 135 ? 42.481 19.052  13.449  1.00 16.68  ?  130 THR D CG2 1 
ATOM   2590 N  N   . VAL B 1 136 ? 39.840 19.355  10.940  1.00 17.06  ?  131 VAL D N   1 
ATOM   2591 C  CA  . VAL B 1 136 ? 38.948 18.242  10.533  1.00 17.14  ?  131 VAL D CA  1 
ATOM   2592 C  C   . VAL B 1 136 ? 38.916 18.107  8.998   1.00 17.78  ?  131 VAL D C   1 
ATOM   2593 O  O   . VAL B 1 136 ? 38.843 16.955  8.544   1.00 18.05  ?  131 VAL D O   1 
ATOM   2594 C  CB  . VAL B 1 136 ? 37.556 18.273  11.189  1.00 20.37  ?  131 VAL D CB  1 
ATOM   2595 C  CG1 . VAL B 1 136 ? 37.659 18.180  12.709  1.00 19.62  ?  131 VAL D CG1 1 
ATOM   2596 C  CG2 . VAL B 1 136 ? 36.713 19.469  10.764  1.00 21.26  ?  131 VAL D CG2 1 
ATOM   2597 N  N   . ARG B 1 137 ? 38.980 19.195  8.233   1.00 17.58  ?  132 ARG D N   1 
ATOM   2598 C  CA  . ARG B 1 137 ? 39.000 19.125  6.756   1.00 17.15  ?  132 ARG D CA  1 
ATOM   2599 C  C   . ARG B 1 137 ? 40.323 18.502  6.280   1.00 16.17  ?  132 ARG D C   1 
ATOM   2600 O  O   . ARG B 1 137 ? 40.305 17.717  5.322   1.00 16.87  ?  132 ARG D O   1 
ATOM   2601 C  CB  . ARG B 1 137 ? 38.863 20.504  6.121   1.00 20.77  ?  132 ARG D CB  1 
ATOM   2602 C  CG  . ARG B 1 137 ? 37.451 21.052  6.110   1.00 22.88  ?  132 ARG D CG  1 
ATOM   2603 C  CD  . ARG B 1 137 ? 37.437 22.423  5.482   1.00 25.16  ?  132 ARG D CD  1 
ATOM   2604 N  NE  . ARG B 1 137 ? 37.663 22.295  4.059   1.00 29.78  ?  132 ARG D NE  1 
ATOM   2605 C  CZ  . ARG B 1 137 ? 37.440 23.234  3.126   1.00 36.35  ?  132 ARG D CZ  1 
ATOM   2606 N  NH1 . ARG B 1 137 ? 36.948 24.419  3.448   1.00 36.07  ?  132 ARG D NH1 1 
ATOM   2607 N  NH2 . ARG B 1 137 ? 37.692 22.956  1.855   1.00 40.21  ?  132 ARG D NH2 1 
ATOM   2608 N  N   . ALA B 1 138 ? 41.468 18.827  6.885   1.00 15.24  ?  133 ALA D N   1 
ATOM   2609 C  CA  . ALA B 1 138 ? 42.746 18.191  6.494   1.00 15.74  ?  133 ALA D CA  1 
ATOM   2610 C  C   . ALA B 1 138 ? 42.689 16.676  6.799   1.00 16.02  ?  133 ALA D C   1 
ATOM   2611 O  O   . ALA B 1 138 ? 43.238 15.867  5.993   1.00 16.48  ?  133 ALA D O   1 
ATOM   2612 C  CB  . ALA B 1 138 ? 43.905 18.877  7.201   1.00 16.55  ?  133 ALA D CB  1 
ATOM   2613 N  N   . THR B 1 139 ? 42.098 16.310  7.947   1.00 17.50  ?  134 THR D N   1 
ATOM   2614 C  CA  . THR B 1 139 ? 41.862 14.893  8.365   1.00 16.78  ?  134 THR D CA  1 
ATOM   2615 C  C   . THR B 1 139 ? 40.943 14.176  7.354   1.00 15.95  ?  134 THR D C   1 
ATOM   2616 O  O   . THR B 1 139 ? 41.224 13.039  7.001   1.00 14.55  ?  134 THR D O   1 
ATOM   2617 C  CB  . THR B 1 139 ? 41.320 14.787  9.792   1.00 15.96  ?  134 THR D CB  1 
ATOM   2618 O  OG1 . THR B 1 139 ? 42.238 15.526  10.569  1.00 15.31  ?  134 THR D OG1 1 
ATOM   2619 C  CG2 . THR B 1 139 ? 41.237 13.368  10.317  1.00 16.10  ?  134 THR D CG2 1 
ATOM   2620 N  N   . VAL B 1 140 ? 39.843 14.791  6.920   1.00 16.81  ?  135 VAL D N   1 
ATOM   2621 C  CA  . VAL B 1 140 ? 39.053 14.180  5.821   1.00 16.23  ?  135 VAL D CA  1 
ATOM   2622 C  C   . VAL B 1 140 ? 39.973 13.987  4.606   1.00 14.92  ?  135 VAL D C   1 
ATOM   2623 O  O   . VAL B 1 140 ? 39.983 12.908  4.040   1.00 13.84  ?  135 VAL D O   1 
ATOM   2624 C  CB  . VAL B 1 140 ? 37.763 14.963  5.490   1.00 16.22  ?  135 VAL D CB  1 
ATOM   2625 C  CG1 . VAL B 1 140 ? 37.196 14.437  4.188   1.00 17.62  ?  135 VAL D CG1 1 
ATOM   2626 C  CG2 . VAL B 1 140 ? 36.721 14.881  6.613   1.00 15.20  ?  135 VAL D CG2 1 
ATOM   2627 N  N   . ALA B 1 141 ? 40.724 15.004  4.224   1.00 18.01  ?  136 ALA D N   1 
ATOM   2628 C  CA  . ALA B 1 141 ? 41.472 15.035  2.951   1.00 19.00  ?  136 ALA D CA  1 
ATOM   2629 C  C   . ALA B 1 141 ? 42.499 13.889  2.971   1.00 20.35  ?  136 ALA D C   1 
ATOM   2630 O  O   . ALA B 1 141 ? 42.573 13.100  1.991   1.00 18.36  ?  136 ALA D O   1 
ATOM   2631 C  CB  . ALA B 1 141 ? 42.058 16.420  2.760   1.00 19.84  ?  136 ALA D CB  1 
ATOM   2632 N  N   . ALA B 1 142 ? 43.203 13.743  4.094   1.00 17.57  ?  137 ALA D N   1 
ATOM   2633 C  CA  . ALA B 1 142 ? 44.288 12.756  4.283   1.00 19.04  ?  137 ALA D CA  1 
ATOM   2634 C  C   . ALA B 1 142 ? 43.698 11.344  4.389   1.00 16.76  ?  137 ALA D C   1 
ATOM   2635 O  O   . ALA B 1 142 ? 44.140 10.471  3.634   1.00 17.24  ?  137 ALA D O   1 
ATOM   2636 C  CB  . ALA B 1 142 ? 45.129 13.115  5.488   1.00 18.46  ?  137 ALA D CB  1 
ATOM   2637 N  N   . LEU B 1 143 ? 42.700 11.120  5.226   1.00 16.22  ?  138 LEU D N   1 
ATOM   2638 C  CA  . LEU B 1 143 ? 42.173 9.739   5.454   1.00 16.64  ?  138 LEU D CA  1 
ATOM   2639 C  C   . LEU B 1 143 ? 41.272 9.278   4.287   1.00 15.13  ?  138 LEU D C   1 
ATOM   2640 O  O   . LEU B 1 143 ? 41.385 8.114   3.900   1.00 14.33  ?  138 LEU D O   1 
ATOM   2641 C  CB  . LEU B 1 143 ? 41.397 9.586   6.766   1.00 17.54  ?  138 LEU D CB  1 
ATOM   2642 C  CG  . LEU B 1 143 ? 42.059 10.033  8.065   1.00 20.28  ?  138 LEU D CG  1 
ATOM   2643 C  CD1 . LEU B 1 143 ? 41.531 9.269   9.251   1.00 18.50  ?  138 LEU D CD1 1 
ATOM   2644 C  CD2 . LEU B 1 143 ? 43.553 10.090  8.026   1.00 19.88  ?  138 LEU D CD2 1 
ATOM   2645 N  N   . GLU B 1 144 ? 40.466 10.139  3.698   1.00 16.32  ?  139 GLU D N   1 
ATOM   2646 C  CA  . GLU B 1 144 ? 39.573 9.703   2.581   1.00 16.99  ?  139 GLU D CA  1 
ATOM   2647 C  C   . GLU B 1 144 ? 40.473 9.314   1.391   1.00 18.96  ?  139 GLU D C   1 
ATOM   2648 O  O   . GLU B 1 144 ? 40.260 8.248   0.734   1.00 17.23  ?  139 GLU D O   1 
ATOM   2649 C  CB  . GLU B 1 144 ? 38.576 10.817  2.254   1.00 17.80  ?  139 GLU D CB  1 
ATOM   2650 C  CG  . GLU B 1 144 ? 37.587 10.376  1.192   1.00 18.38  ?  139 GLU D CG  1 
ATOM   2651 C  CD  . GLU B 1 144 ? 36.641 9.262   1.603   1.00 17.89  ?  139 GLU D CD  1 
ATOM   2652 O  OE1 . GLU B 1 144 ? 36.422 9.059   2.828   1.00 15.91  ?  139 GLU D OE1 1 
ATOM   2653 O  OE2 . GLU B 1 144 ? 36.089 8.594   0.696   1.00 20.54  -1 139 GLU D OE2 1 
ATOM   2654 N  N   . SER B 1 145 ? 41.567 10.047  1.202   1.00 18.41  ?  140 SER D N   1 
ATOM   2655 C  CA  . SER B 1 145 ? 42.547 9.750   0.128   1.00 21.16  ?  140 SER D CA  1 
ATOM   2656 C  C   . SER B 1 145 ? 43.174 8.358   0.319   1.00 20.16  ?  140 SER D C   1 
ATOM   2657 O  O   . SER B 1 145 ? 43.329 7.606   -0.655  1.00 21.90  ?  140 SER D O   1 
ATOM   2658 C  CB  . SER B 1 145 ? 43.611 10.818  0.045   1.00 22.10  ?  140 SER D CB  1 
ATOM   2659 O  OG  . SER B 1 145 ? 44.671 10.380  -0.808  1.00 26.54  ?  140 SER D OG  1 
ATOM   2660 N  N   . ARG B 1 146 ? 43.557 8.013   1.532   1.00 18.92  ?  141 ARG D N   1 
ATOM   2661 C  CA  . ARG B 1 146 ? 44.308 6.771   1.811   1.00 21.76  ?  141 ARG D CA  1 
ATOM   2662 C  C   . ARG B 1 146 ? 43.393 5.583   2.087   1.00 19.92  ?  141 ARG D C   1 
ATOM   2663 O  O   . ARG B 1 146 ? 43.829 4.466   1.812   1.00 22.84  ?  141 ARG D O   1 
ATOM   2664 C  CB  . ARG B 1 146 ? 45.249 7.014   2.990   1.00 25.26  ?  141 ARG D CB  1 
ATOM   2665 C  CG  . ARG B 1 146 ? 46.532 6.221   2.909   1.00 31.75  ?  141 ARG D CG  1 
ATOM   2666 C  CD  . ARG B 1 146 ? 47.524 6.722   3.928   1.00 36.62  ?  141 ARG D CD  1 
ATOM   2667 N  NE  . ARG B 1 146 ? 48.878 6.543   3.418   1.00 44.32  ?  141 ARG D NE  1 
ATOM   2668 C  CZ  . ARG B 1 146 ? 49.606 7.509   2.886   1.00 44.61  ?  141 ARG D CZ  1 
ATOM   2669 N  NH1 . ARG B 1 146 ? 50.829 7.241   2.469   1.00 48.21  ?  141 ARG D NH1 1 
ATOM   2670 N  NH2 . ARG B 1 146 ? 49.127 8.744   2.812   1.00 44.62  ?  141 ARG D NH2 1 
ATOM   2671 N  N   . PHE B 1 147 ? 42.197 5.773   2.645   1.00 18.82  ?  142 PHE D N   1 
ATOM   2672 C  CA  . PHE B 1 147 ? 41.354 4.679   3.190   1.00 16.81  ?  142 PHE D CA  1 
ATOM   2673 C  C   . PHE B 1 147 ? 39.954 4.678   2.574   1.00 16.40  ?  142 PHE D C   1 
ATOM   2674 O  O   . PHE B 1 147 ? 39.147 3.746   2.848   1.00 17.08  ?  142 PHE D O   1 
ATOM   2675 C  CB  . PHE B 1 147 ? 41.270 4.842   4.709   1.00 18.26  ?  142 PHE D CB  1 
ATOM   2676 C  CG  . PHE B 1 147 ? 42.634 4.858   5.372   1.00 18.41  ?  142 PHE D CG  1 
ATOM   2677 C  CD1 . PHE B 1 147 ? 43.416 3.712   5.412   1.00 18.03  ?  142 PHE D CD1 1 
ATOM   2678 C  CD2 . PHE B 1 147 ? 43.138 6.034   5.901   1.00 17.45  ?  142 PHE D CD2 1 
ATOM   2679 C  CE1 . PHE B 1 147 ? 44.678 3.749   5.986   1.00 19.03  ?  142 PHE D CE1 1 
ATOM   2680 C  CE2 . PHE B 1 147 ? 44.411 6.088   6.456   1.00 16.58  ?  142 PHE D CE2 1 
ATOM   2681 C  CZ  . PHE B 1 147 ? 45.171 4.931   6.514   1.00 19.01  ?  142 PHE D CZ  1 
ATOM   2682 N  N   . GLY B 1 148 ? 39.619 5.722   1.823   1.00 16.91  ?  143 GLY D N   1 
ATOM   2683 C  CA  . GLY B 1 148 ? 38.204 5.950   1.474   1.00 16.95  ?  143 GLY D CA  1 
ATOM   2684 C  C   . GLY B 1 148 ? 37.893 5.559   0.021   1.00 18.82  ?  143 GLY D C   1 
ATOM   2685 O  O   . GLY B 1 148 ? 38.458 4.560   -0.517  1.00 17.25  ?  143 GLY D O   1 
ATOM   2686 N  N   . ALA B 1 149 ? 36.942 6.281   -0.556  1.00 19.41  ?  144 ALA D N   1 
ATOM   2687 C  CA  . ALA B 1 149 ? 36.292 5.947   -1.843  1.00 20.69  ?  144 ALA D CA  1 
ATOM   2688 C  C   . ALA B 1 149 ? 35.920 7.229   -2.587  1.00 20.29  ?  144 ALA D C   1 
ATOM   2689 O  O   . ALA B 1 149 ? 34.805 7.301   -3.144  1.00 22.85  ?  144 ALA D O   1 
ATOM   2690 C  CB  . ALA B 1 149 ? 35.089 5.081   -1.539  1.00 21.45  ?  144 ALA D CB  1 
ATOM   2691 N  N   . GLY B 1 150 ? 36.792 8.230   -2.541  1.00 18.08  ?  145 GLY D N   1 
ATOM   2692 C  CA  . GLY B 1 150 ? 36.652 9.437   -3.355  1.00 18.24  ?  145 GLY D CA  1 
ATOM   2693 C  C   . GLY B 1 150 ? 35.509 10.315  -2.896  1.00 20.66  ?  145 GLY D C   1 
ATOM   2694 O  O   . GLY B 1 150 ? 35.065 11.109  -3.706  1.00 19.54  ?  145 GLY D O   1 
ATOM   2695 N  N   . TRP B 1 151 ? 35.106 10.254  -1.633  1.00 17.87  ?  146 TRP D N   1 
ATOM   2696 C  CA  . TRP B 1 151 ? 33.992 11.088  -1.125  1.00 18.30  ?  146 TRP D CA  1 
ATOM   2697 C  C   . TRP B 1 151 ? 34.389 12.570  -1.106  1.00 19.21  ?  146 TRP D C   1 
ATOM   2698 O  O   . TRP B 1 151 ? 35.490 12.891  -0.668  1.00 19.11  ?  146 TRP D O   1 
ATOM   2699 C  CB  . TRP B 1 151 ? 33.513 10.622  0.234   1.00 17.77  ?  146 TRP D CB  1 
ATOM   2700 C  CG  . TRP B 1 151 ? 32.442 11.498  0.812   1.00 18.32  ?  146 TRP D CG  1 
ATOM   2701 C  CD1 . TRP B 1 151 ? 31.116 11.530  0.477   1.00 19.11  ?  146 TRP D CD1 1 
ATOM   2702 C  CD2 . TRP B 1 151 ? 32.612 12.441  1.880   1.00 17.47  ?  146 TRP D CD2 1 
ATOM   2703 N  NE1 . TRP B 1 151 ? 30.454 12.440  1.257   1.00 18.50  ?  146 TRP D NE1 1 
ATOM   2704 C  CE2 . TRP B 1 151 ? 31.347 13.019  2.120   1.00 18.09  ?  146 TRP D CE2 1 
ATOM   2705 C  CE3 . TRP B 1 151 ? 33.713 12.843  2.647   1.00 16.05  ?  146 TRP D CE3 1 
ATOM   2706 C  CZ2 . TRP B 1 151 ? 31.143 13.957  3.123   1.00 17.85  ?  146 TRP D CZ2 1 
ATOM   2707 C  CZ3 . TRP B 1 151 ? 33.518 13.811  3.604   1.00 17.63  ?  146 TRP D CZ3 1 
ATOM   2708 C  CH2 . TRP B 1 151 ? 32.249 14.336  3.852   1.00 18.76  ?  146 TRP D CH2 1 
ATOM   2709 N  N   . ASP B 1 152 ? 33.476 13.430  -1.564  1.00 20.36  ?  147 ASP D N   1 
ATOM   2710 C  CA  . ASP B 1 152 ? 33.712 14.884  -1.696  1.00 21.31  ?  147 ASP D CA  1 
ATOM   2711 C  C   . ASP B 1 152 ? 33.080 15.542  -0.471  1.00 19.87  ?  147 ASP D C   1 
ATOM   2712 O  O   . ASP B 1 152 ? 31.869 15.448  -0.327  1.00 18.85  ?  147 ASP D O   1 
ATOM   2713 C  CB  . ASP B 1 152 ? 33.113 15.385  -3.020  1.00 23.22  ?  147 ASP D CB  1 
ATOM   2714 C  CG  . ASP B 1 152 ? 33.266 16.882  -3.242  1.00 27.53  ?  147 ASP D CG  1 
ATOM   2715 O  OD1 . ASP B 1 152 ? 34.012 17.523  -2.465  1.00 27.19  ?  147 ASP D OD1 1 
ATOM   2716 O  OD2 . ASP B 1 152 ? 32.594 17.410  -4.175  1.00 33.97  -1 147 ASP D OD2 1 
ATOM   2717 N  N   . MET B 1 153 ? 33.868 16.176  0.405   1.00 18.48  ?  148 MET D N   1 
ATOM   2718 C  CA  . MET B 1 153 ? 33.313 16.822  1.633   1.00 20.11  ?  148 MET D CA  1 
ATOM   2719 C  C   . MET B 1 153 ? 32.546 18.121  1.312   1.00 20.33  ?  148 MET D C   1 
ATOM   2720 O  O   . MET B 1 153 ? 31.917 18.652  2.248   1.00 19.12  ?  148 MET D O   1 
ATOM   2721 C  CB  . MET B 1 153 ? 34.427 17.162  2.627   1.00 19.41  ?  148 MET D CB  1 
ATOM   2722 C  CG  . MET B 1 153 ? 35.238 18.356  2.282   1.00 20.67  ?  148 MET D CG  1 
ATOM   2723 S  SD  . MET B 1 153 ? 36.726 18.465  3.390   1.00 22.18  ?  148 MET D SD  1 
ATOM   2724 C  CE  . MET B 1 153 ? 38.014 17.763  2.360   1.00 23.70  ?  148 MET D CE  1 
ATOM   2725 N  N   . THR B 1 154 ? 32.601 18.623  0.072   1.00 23.39  ?  149 THR D N   1 
ATOM   2726 C  CA  . THR B 1 154 ? 32.212 20.023  -0.266  1.00 25.22  ?  149 THR D CA  1 
ATOM   2727 C  C   . THR B 1 154 ? 30.804 20.264  0.248   1.00 24.60  ?  149 THR D C   1 
ATOM   2728 O  O   . THR B 1 154 ? 30.607 21.268  0.957   1.00 27.96  ?  149 THR D O   1 
ATOM   2729 C  CB  . THR B 1 154 ? 32.255 20.308  -1.774  1.00 26.17  ?  149 THR D CB  1 
ATOM   2730 O  OG1 . THR B 1 154 ? 33.630 20.360  -2.129  1.00 27.19  ?  149 THR D OG1 1 
ATOM   2731 C  CG2 . THR B 1 154 ? 31.571 21.604  -2.166  1.00 27.11  ?  149 THR D CG2 1 
ATOM   2732 N  N   . GLY B 1 155 ? 29.886 19.363  -0.097  1.00 22.81  ?  150 GLY D N   1 
ATOM   2733 C  CA  . GLY B 1 155 ? 28.454 19.440  0.269   1.00 23.03  ?  150 GLY D CA  1 
ATOM   2734 C  C   . GLY B 1 155 ? 28.158 19.241  1.756   1.00 22.53  ?  150 GLY D C   1 
ATOM   2735 O  O   . GLY B 1 155 ? 26.961 19.396  2.164   1.00 25.47  ?  150 GLY D O   1 
ATOM   2736 N  N   . SER B 1 156 ? 29.166 18.927  2.574   1.00 20.51  ?  151 SER D N   1 
ATOM   2737 C  CA  . SER B 1 156 ? 28.999 18.694  4.029   1.00 20.79  ?  151 SER D CA  1 
ATOM   2738 C  C   . SER B 1 156 ? 29.722 19.766  4.849   1.00 21.70  ?  151 SER D C   1 
ATOM   2739 O  O   . SER B 1 156 ? 29.704 19.633  6.088   1.00 23.26  ?  151 SER D O   1 
ATOM   2740 C  CB  . SER B 1 156 ? 29.477 17.291  4.414   1.00 20.30  ?  151 SER D CB  1 
ATOM   2741 O  OG  . SER B 1 156 ? 28.725 16.315  3.718   1.00 21.75  ?  151 SER D OG  1 
ATOM   2742 N  N   . LEU B 1 157 ? 30.288 20.801  4.225   1.00 22.83  ?  152 LEU D N   1 
ATOM   2743 C  CA  . LEU B 1 157 ? 31.032 21.832  5.011   1.00 25.73  ?  152 LEU D CA  1 
ATOM   2744 C  C   . LEU B 1 157 ? 30.090 22.589  5.963   1.00 25.97  ?  152 LEU D C   1 
ATOM   2745 O  O   . LEU B 1 157 ? 30.507 22.816  7.107   1.00 25.48  ?  152 LEU D O   1 
ATOM   2746 C  CB  . LEU B 1 157 ? 31.787 22.756  4.069   1.00 24.53  ?  152 LEU D CB  1 
ATOM   2747 C  CG  . LEU B 1 157 ? 32.895 22.072  3.285   1.00 26.47  ?  152 LEU D CG  1 
ATOM   2748 C  CD1 . LEU B 1 157 ? 33.563 23.064  2.349   1.00 25.56  ?  152 LEU D CD1 1 
ATOM   2749 C  CD2 . LEU B 1 157 ? 33.906 21.436  4.233   1.00 25.58  ?  152 LEU D CD2 1 
ATOM   2750 N  N   . ASP B 1 158 ? 28.875 22.976  5.543   1.00 22.84  ?  153 ASP D N   1 
ATOM   2751 C  CA  . ASP B 1 158 ? 27.911 23.640  6.460   1.00 27.70  ?  153 ASP D CA  1 
ATOM   2752 C  C   . ASP B 1 158 ? 27.713 22.732  7.688   1.00 23.43  ?  153 ASP D C   1 
ATOM   2753 O  O   . ASP B 1 158 ? 27.770 23.241  8.830   1.00 19.62  ?  153 ASP D O   1 
ATOM   2754 C  CB  . ASP B 1 158 ? 26.591 23.974  5.750   1.00 30.68  ?  153 ASP D CB  1 
ATOM   2755 C  CG  . ASP B 1 158 ? 26.609 25.268  4.941   1.00 34.04  ?  153 ASP D CG  1 
ATOM   2756 O  OD1 . ASP B 1 158 ? 27.677 25.950  4.915   1.00 31.59  ?  153 ASP D OD1 1 
ATOM   2757 O  OD2 . ASP B 1 158 ? 25.542 25.610  4.379   1.00 38.46  -1 153 ASP D OD2 1 
ATOM   2758 N  N   . TYR B 1 159 ? 27.553 21.416  7.466   1.00 21.92  ?  154 TYR D N   1 
ATOM   2759 C  CA  . TYR B 1 159 ? 27.355 20.393  8.522   1.00 20.79  ?  154 TYR D CA  1 
ATOM   2760 C  C   . TYR B 1 159 ? 28.584 20.367  9.431   1.00 20.34  ?  154 TYR D C   1 
ATOM   2761 O  O   . TYR B 1 159 ? 28.405 20.346  10.668  1.00 21.61  ?  154 TYR D O   1 
ATOM   2762 C  CB  . TYR B 1 159 ? 27.096 19.008  7.931   1.00 21.66  ?  154 TYR D CB  1 
ATOM   2763 C  CG  . TYR B 1 159 ? 27.006 17.898  8.944   1.00 19.94  ?  154 TYR D CG  1 
ATOM   2764 C  CD1 . TYR B 1 159 ? 26.025 17.887  9.931   1.00 21.97  ?  154 TYR D CD1 1 
ATOM   2765 C  CD2 . TYR B 1 159 ? 27.898 16.838  8.901   1.00 20.90  ?  154 TYR D CD2 1 
ATOM   2766 C  CE1 . TYR B 1 159 ? 25.937 16.851  10.852  1.00 22.63  ?  154 TYR D CE1 1 
ATOM   2767 C  CE2 . TYR B 1 159 ? 27.825 15.803  9.822   1.00 21.84  ?  154 TYR D CE2 1 
ATOM   2768 C  CZ  . TYR B 1 159 ? 26.855 15.814  10.810  1.00 22.40  ?  154 TYR D CZ  1 
ATOM   2769 O  OH  . TYR B 1 159 ? 26.816 14.789  11.710  1.00 26.46  ?  154 TYR D OH  1 
ATOM   2770 N  N   . PHE B 1 160 ? 29.783 20.371  8.861   1.00 18.74  ?  155 PHE D N   1 
ATOM   2771 C  CA  . PHE B 1 160 ? 31.019 20.402  9.689   1.00 18.01  ?  155 PHE D CA  1 
ATOM   2772 C  C   . PHE B 1 160 ? 30.910 21.601  10.642  1.00 20.72  ?  155 PHE D C   1 
ATOM   2773 O  O   . PHE B 1 160 ? 31.211 21.501  11.849  1.00 20.73  ?  155 PHE D O   1 
ATOM   2774 C  CB  . PHE B 1 160 ? 32.288 20.481  8.838   1.00 16.26  ?  155 PHE D CB  1 
ATOM   2775 C  CG  . PHE B 1 160 ? 32.682 19.264  8.014   1.00 14.30  ?  155 PHE D CG  1 
ATOM   2776 C  CD1 . PHE B 1 160 ? 31.866 18.156  7.890   1.00 15.47  ?  155 PHE D CD1 1 
ATOM   2777 C  CD2 . PHE B 1 160 ? 33.891 19.263  7.316   1.00 13.37  ?  155 PHE D CD2 1 
ATOM   2778 C  CE1 . PHE B 1 160 ? 32.252 17.078  7.094   1.00 14.64  ?  155 PHE D CE1 1 
ATOM   2779 C  CE2 . PHE B 1 160 ? 34.256 18.228  6.495   1.00 13.39  ?  155 PHE D CE2 1 
ATOM   2780 C  CZ  . PHE B 1 160 ? 33.475 17.108  6.427   1.00 14.09  ?  155 PHE D CZ  1 
ATOM   2781 N  N   . ARG B 1 161 ? 30.526 22.744  10.096  1.00 21.88  ?  156 ARG D N   1 
ATOM   2782 C  CA  . ARG B 1 161 ? 30.498 24.011  10.868  1.00 23.05  ?  156 ARG D CA  1 
ATOM   2783 C  C   . ARG B 1 161 ? 29.456 23.881  11.970  1.00 21.86  ?  156 ARG D C   1 
ATOM   2784 O  O   . ARG B 1 161 ? 29.740 24.357  13.072  1.00 21.03  ?  156 ARG D O   1 
ATOM   2785 C  CB  . ARG B 1 161 ? 30.223 25.186  9.923   1.00 25.84  ?  156 ARG D CB  1 
ATOM   2786 C  CG  . ARG B 1 161 ? 31.446 25.601  9.119   1.00 27.98  ?  156 ARG D CG  1 
ATOM   2787 C  CD  . ARG B 1 161 ? 30.986 26.635  8.108   1.00 35.11  ?  156 ARG D CD  1 
ATOM   2788 N  NE  . ARG B 1 161 ? 32.057 27.513  7.692   1.00 38.35  ?  156 ARG D NE  1 
ATOM   2789 C  CZ  . ARG B 1 161 ? 32.762 27.426  6.564   1.00 46.36  ?  156 ARG D CZ  1 
ATOM   2790 N  NH1 . ARG B 1 161 ? 32.522 26.475  5.670   1.00 44.49  ?  156 ARG D NH1 1 
ATOM   2791 N  NH2 . ARG B 1 161 ? 33.717 28.317  6.333   1.00 47.13  ?  156 ARG D NH2 1 
ATOM   2792 N  N   . ARG B 1 162 ? 28.307 23.261  11.697  1.00 20.76  ?  157 ARG D N   1 
ATOM   2793 C  CA  . ARG B 1 162 ? 27.234 23.089  12.711  1.00 24.14  ?  157 ARG D CA  1 
ATOM   2794 C  C   . ARG B 1 162 ? 27.744 22.244  13.895  1.00 21.48  ?  157 ARG D C   1 
ATOM   2795 O  O   . ARG B 1 162 ? 27.359 22.539  15.027  1.00 21.23  ?  157 ARG D O   1 
ATOM   2796 C  CB  . ARG B 1 162 ? 25.968 22.435  12.141  1.00 28.83  ?  157 ARG D CB  1 
ATOM   2797 C  CG  . ARG B 1 162 ? 25.285 23.243  11.048  1.00 37.65  ?  157 ARG D CG  1 
ATOM   2798 C  CD  . ARG B 1 162 ? 23.802 22.939  10.897  1.00 39.57  ?  157 ARG D CD  1 
ATOM   2799 N  NE  . ARG B 1 162 ? 23.546 21.647  10.266  1.00 44.14  ?  157 ARG D NE  1 
ATOM   2800 C  CZ  . ARG B 1 162 ? 23.676 21.385  8.964   1.00 47.48  ?  157 ARG D CZ  1 
ATOM   2801 N  NH1 . ARG B 1 162 ? 24.090 22.320  8.118   1.00 49.48  ?  157 ARG D NH1 1 
ATOM   2802 N  NH2 . ARG B 1 162 ? 23.407 20.170  8.516   1.00 44.91  ?  157 ARG D NH2 1 
ATOM   2803 N  N   . ILE B 1 163 ? 28.592 21.239  13.684  1.00 22.21  ?  158 ILE D N   1 
ATOM   2804 C  CA  . ILE B 1 163 ? 28.974 20.312  14.793  1.00 20.34  ?  158 ILE D CA  1 
ATOM   2805 C  C   . ILE B 1 163 ? 30.355 20.694  15.370  1.00 20.01  ?  158 ILE D C   1 
ATOM   2806 O  O   . ILE B 1 163 ? 30.754 20.109  16.373  1.00 18.22  ?  158 ILE D O   1 
ATOM   2807 C  CB  . ILE B 1 163 ? 28.930 18.833  14.350  1.00 22.39  ?  158 ILE D CB  1 
ATOM   2808 C  CG1 . ILE B 1 163 ? 29.879 18.529  13.197  1.00 22.16  ?  158 ILE D CG1 1 
ATOM   2809 C  CG2 . ILE B 1 163 ? 27.516 18.396  14.026  1.00 24.03  ?  158 ILE D CG2 1 
ATOM   2810 C  CD1 . ILE B 1 163 ? 30.072 17.032  12.964  1.00 24.57  ?  158 ILE D CD1 1 
ATOM   2811 N  N   . LEU B 1 164 ? 31.035 21.650  14.768  1.00 20.09  ?  159 LEU D N   1 
ATOM   2812 C  CA  . LEU B 1 164 ? 32.407 22.073  15.124  1.00 20.43  ?  159 LEU D CA  1 
ATOM   2813 C  C   . LEU B 1 164 ? 32.580 22.444  16.604  1.00 19.65  ?  159 LEU D C   1 
ATOM   2814 O  O   . LEU B 1 164 ? 33.641 22.211  17.189  1.00 17.74  ?  159 LEU D O   1 
ATOM   2815 C  CB  . LEU B 1 164 ? 32.739 23.279  14.262  1.00 20.08  ?  159 LEU D CB  1 
ATOM   2816 C  CG  . LEU B 1 164 ? 34.225 23.556  14.109  1.00 18.04  ?  159 LEU D CG  1 
ATOM   2817 C  CD1 . LEU B 1 164 ? 34.912 22.393  13.419  1.00 19.14  ?  159 LEU D CD1 1 
ATOM   2818 C  CD2 . LEU B 1 164 ? 34.342 24.822  13.311  1.00 19.30  ?  159 LEU D CD2 1 
ATOM   2819 N  N   . PRO B 1 165 ? 31.607 23.066  17.286  1.00 20.08  ?  160 PRO D N   1 
ATOM   2820 C  CA  . PRO B 1 165 ? 31.824 23.404  18.698  1.00 19.32  ?  160 PRO D CA  1 
ATOM   2821 C  C   . PRO B 1 165 ? 32.311 22.235  19.573  1.00 18.95  ?  160 PRO D C   1 
ATOM   2822 O  O   . PRO B 1 165 ? 33.020 22.494  20.568  1.00 16.75  ?  160 PRO D O   1 
ATOM   2823 C  CB  . PRO B 1 165 ? 30.428 23.887  19.103  1.00 19.38  ?  160 PRO D CB  1 
ATOM   2824 C  CG  . PRO B 1 165 ? 29.950 24.583  17.844  1.00 20.94  ?  160 PRO D CG  1 
ATOM   2825 C  CD  . PRO B 1 165 ? 30.317 23.576  16.767  1.00 21.48  ?  160 PRO D CD  1 
ATOM   2826 N  N   . GLY B 1 166 ? 31.979 20.988  19.197  1.00 16.69  ?  161 GLY D N   1 
ATOM   2827 C  CA  . GLY B 1 166 ? 32.260 19.783  20.005  1.00 17.38  ?  161 GLY D CA  1 
ATOM   2828 C  C   . GLY B 1 166 ? 33.699 19.299  19.823  1.00 17.15  ?  161 GLY D C   1 
ATOM   2829 O  O   . GLY B 1 166 ? 34.181 18.466  20.614  1.00 18.03  ?  161 GLY D O   1 
ATOM   2830 N  N   . VAL B 1 167 ? 34.377 19.805  18.816  1.00 15.85  ?  162 VAL D N   1 
ATOM   2831 C  CA  . VAL B 1 167 ? 35.743 19.361  18.445  1.00 16.36  ?  162 VAL D CA  1 
ATOM   2832 C  C   . VAL B 1 167 ? 36.789 20.034  19.355  1.00 17.38  ?  162 VAL D C   1 
ATOM   2833 O  O   . VAL B 1 167 ? 36.788 21.298  19.438  1.00 18.06  ?  162 VAL D O   1 
ATOM   2834 C  CB  . VAL B 1 167 ? 36.027 19.671  16.973  1.00 15.32  ?  162 VAL D CB  1 
ATOM   2835 C  CG1 . VAL B 1 167 ? 37.450 19.290  16.610  1.00 15.23  ?  162 VAL D CG1 1 
ATOM   2836 C  CG2 . VAL B 1 167 ? 35.014 19.028  16.019  1.00 16.48  ?  162 VAL D CG2 1 
ATOM   2837 N  N   . GLY B 1 168 ? 37.639 19.215  19.982  1.00 14.69  ?  163 GLY D N   1 
ATOM   2838 C  CA  . GLY B 1 168 ? 38.874 19.647  20.627  1.00 14.35  ?  163 GLY D CA  1 
ATOM   2839 C  C   . GLY B 1 168 ? 40.070 19.314  19.745  1.00 13.96  ?  163 GLY D C   1 
ATOM   2840 O  O   . GLY B 1 168 ? 40.584 18.162  19.785  1.00 16.03  ?  163 GLY D O   1 
ATOM   2841 N  N   . ALA B 1 169 ? 40.475 20.271  18.934  1.00 13.12  ?  164 ALA D N   1 
ATOM   2842 C  CA  . ALA B 1 169 ? 41.527 20.091  17.931  1.00 13.80  ?  164 ALA D CA  1 
ATOM   2843 C  C   . ALA B 1 169 ? 42.835 20.384  18.624  1.00 12.94  ?  164 ALA D C   1 
ATOM   2844 O  O   . ALA B 1 169 ? 42.843 21.165  19.554  1.00 13.69  ?  164 ALA D O   1 
ATOM   2845 C  CB  . ALA B 1 169 ? 41.310 20.982  16.744  1.00 16.00  ?  164 ALA D CB  1 
ATOM   2846 N  N   . PHE B 1 170 ? 43.922 19.783  18.157  1.00 15.22  ?  165 PHE D N   1 
ATOM   2847 C  CA  . PHE B 1 170 ? 45.222 20.021  18.804  1.00 15.36  ?  165 PHE D CA  1 
ATOM   2848 C  C   . PHE B 1 170 ? 46.353 19.872  17.794  1.00 16.13  ?  165 PHE D C   1 
ATOM   2849 O  O   . PHE B 1 170 ? 46.129 19.352  16.665  1.00 15.04  ?  165 PHE D O   1 
ATOM   2850 C  CB  . PHE B 1 170 ? 45.374 19.137  20.031  1.00 16.93  ?  165 PHE D CB  1 
ATOM   2851 C  CG  . PHE B 1 170 ? 45.436 17.669  19.725  1.00 19.38  ?  165 PHE D CG  1 
ATOM   2852 C  CD1 . PHE B 1 170 ? 46.638 17.077  19.387  1.00 19.25  ?  165 PHE D CD1 1 
ATOM   2853 C  CD2 . PHE B 1 170 ? 44.294 16.882  19.836  1.00 19.34  ?  165 PHE D CD2 1 
ATOM   2854 C  CE1 . PHE B 1 170 ? 46.686 15.717  19.121  1.00 19.56  ?  165 PHE D CE1 1 
ATOM   2855 C  CE2 . PHE B 1 170 ? 44.345 15.523  19.567  1.00 20.38  ?  165 PHE D CE2 1 
ATOM   2856 C  CZ  . PHE B 1 170 ? 45.545 14.940  19.229  1.00 21.28  ?  165 PHE D CZ  1 
ATOM   2857 N  N   . ARG B 1 171 ? 47.507 20.295  18.292  1.00 16.11  ?  166 ARG D N   1 
ATOM   2858 C  CA  . ARG B 1 171 ? 48.818 20.353  17.603  1.00 18.35  ?  166 ARG D CA  1 
ATOM   2859 C  C   . ARG B 1 171 ? 49.858 19.722  18.516  1.00 19.68  ?  166 ARG D C   1 
ATOM   2860 O  O   . ARG B 1 171 ? 49.914 20.062  19.724  1.00 22.47  ?  166 ARG D O   1 
ATOM   2861 C  CB  . ARG B 1 171 ? 49.198 21.805  17.333  1.00 18.06  ?  166 ARG D CB  1 
ATOM   2862 C  CG  . ARG B 1 171 ? 48.188 22.550  16.478  1.00 18.57  ?  166 ARG D CG  1 
ATOM   2863 C  CD  . ARG B 1 171 ? 48.194 22.021  15.052  1.00 18.43  ?  166 ARG D CD  1 
ATOM   2864 N  NE  . ARG B 1 171 ? 47.257 22.705  14.195  1.00 20.73  ?  166 ARG D NE  1 
ATOM   2865 C  CZ  . ARG B 1 171 ? 45.995 22.330  13.950  1.00 17.99  ?  166 ARG D CZ  1 
ATOM   2866 N  NH1 . ARG B 1 171 ? 45.461 21.217  14.445  1.00 17.33  ?  166 ARG D NH1 1 
ATOM   2867 N  NH2 . ARG B 1 171 ? 45.275 23.100  13.173  1.00 18.64  ?  166 ARG D NH2 1 
ATOM   2868 N  N   . LEU B 1 172 ? 50.647 18.820  17.960  1.00 19.90  ?  167 LEU D N   1 
ATOM   2869 C  CA  . LEU B 1 172 ? 51.668 18.088  18.740  1.00 20.73  ?  167 LEU D CA  1 
ATOM   2870 C  C   . LEU B 1 172 ? 52.999 18.279  17.995  1.00 20.51  ?  167 LEU D C   1 
ATOM   2871 O  O   . LEU B 1 172 ? 53.232 17.670  16.938  1.00 16.81  ?  167 LEU D O   1 
ATOM   2872 C  CB  . LEU B 1 172 ? 51.261 16.620  18.916  1.00 22.84  ?  167 LEU D CB  1 
ATOM   2873 C  CG  . LEU B 1 172 ? 52.240 15.772  19.732  1.00 22.80  ?  167 LEU D CG  1 
ATOM   2874 C  CD1 . LEU B 1 172 ? 52.451 16.380  21.115  1.00 29.71  ?  167 LEU D CD1 1 
ATOM   2875 C  CD2 . LEU B 1 172 ? 51.734 14.351  19.854  1.00 22.37  ?  167 LEU D CD2 1 
ATOM   2876 N  N   . ARG B 1 173 ? 53.797 19.183  18.523  1.00 21.37  ?  168 ARG D N   1 
ATOM   2877 C  CA  . ARG B 1 173 ? 55.200 19.435  18.131  1.00 24.38  ?  168 ARG D CA  1 
ATOM   2878 C  C   . ARG B 1 173 ? 55.993 18.201  18.561  1.00 17.57  ?  168 ARG D C   1 
ATOM   2879 O  O   . ARG B 1 173 ? 56.057 17.989  19.720  1.00 17.35  ?  168 ARG D O   1 
ATOM   2880 C  CB  . ARG B 1 173 ? 55.634 20.725  18.858  1.00 28.79  ?  168 ARG D CB  1 
ATOM   2881 C  CG  . ARG B 1 173 ? 57.024 21.235  18.516  1.00 39.60  ?  168 ARG D CG  1 
ATOM   2882 C  CD  . ARG B 1 173 ? 57.423 21.071  17.064  1.00 43.49  ?  168 ARG D CD  1 
ATOM   2883 N  NE  . ARG B 1 173 ? 58.473 22.011  16.638  1.00 56.83  ?  168 ARG D NE  1 
ATOM   2884 C  CZ  . ARG B 1 173 ? 59.771 21.960  16.975  1.00 53.54  ?  168 ARG D CZ  1 
ATOM   2885 N  NH1 . ARG B 1 173 ? 60.606 22.865  16.498  1.00 58.12  ?  168 ARG D NH1 1 
ATOM   2886 N  NH2 . ARG B 1 173 ? 60.238 21.022  17.784  1.00 55.07  ?  168 ARG D NH2 1 
ATOM   2887 N  N   . VAL B 1 174 ? 56.463 17.390  17.623  1.00 20.78  ?  169 VAL D N   1 
ATOM   2888 C  CA  . VAL B 1 174 ? 57.238 16.145  17.895  1.00 20.19  ?  169 VAL D CA  1 
ATOM   2889 C  C   . VAL B 1 174 ? 58.662 16.517  18.345  1.00 18.01  ?  169 VAL D C   1 
ATOM   2890 O  O   . VAL B 1 174 ? 59.401 17.044  17.536  1.00 14.57  ?  169 VAL D O   1 
ATOM   2891 C  CB  . VAL B 1 174 ? 57.214 15.187  16.694  1.00 20.77  ?  169 VAL D CB  1 
ATOM   2892 C  CG1 . VAL B 1 174 ? 57.887 13.889  17.044  1.00 21.82  ?  169 VAL D CG1 1 
ATOM   2893 C  CG2 . VAL B 1 174 ? 55.772 14.911  16.246  1.00 19.73  ?  169 VAL D CG2 1 
ATOM   2894 N  N   . ALA B 1 175 ? 58.973 16.271  19.614  1.00 19.88  ?  170 ALA D N   1 
ATOM   2895 C  CA  . ALA B 1 175 ? 60.318 16.475  20.220  1.00 20.94  ?  170 ALA D CA  1 
ATOM   2896 C  C   . ALA B 1 175 ? 61.127 15.181  20.084  1.00 21.44  ?  170 ALA D C   1 
ATOM   2897 O  O   . ALA B 1 175 ? 62.334 15.234  19.920  1.00 21.98  ?  170 ALA D O   1 
ATOM   2898 C  CB  . ALA B 1 175 ? 60.161 16.838  21.677  1.00 19.93  ?  170 ALA D CB  1 
ATOM   2899 N  N   . GLU B 1 176 ? 60.459 14.036  20.213  1.00 21.99  ?  171 GLU D N   1 
ATOM   2900 C  CA  . GLU B 1 176 ? 61.100 12.701  20.184  1.00 23.56  ?  171 GLU D CA  1 
ATOM   2901 C  C   . GLU B 1 176 ? 60.237 11.749  19.362  1.00 20.03  ?  171 GLU D C   1 
ATOM   2902 O  O   . GLU B 1 176 ? 58.990 11.773  19.496  1.00 17.49  ?  171 GLU D O   1 
ATOM   2903 C  CB  . GLU B 1 176 ? 61.235 12.076  21.569  1.00 28.43  ?  171 GLU D CB  1 
ATOM   2904 C  CG  . GLU B 1 176 ? 62.017 12.907  22.556  1.00 35.39  ?  171 GLU D CG  1 
ATOM   2905 C  CD  . GLU B 1 176 ? 62.233 12.186  23.869  1.00 39.68  ?  171 GLU D CD  1 
ATOM   2906 O  OE1 . GLU B 1 176 ? 62.066 12.836  24.913  1.00 45.43  ?  171 GLU D OE1 1 
ATOM   2907 O  OE2 . GLU B 1 176 ? 62.561 10.972  23.833  1.00 48.55  -1 171 GLU D OE2 1 
ATOM   2908 N  N   . ALA B 1 177 ? 60.860 10.909  18.549  1.00 19.95  ?  172 ALA D N   1 
ATOM   2909 C  CA  . ALA B 1 177 ? 60.114 9.881   17.777  1.00 21.61  ?  172 ALA D CA  1 
ATOM   2910 C  C   . ALA B 1 177 ? 60.922 8.590   17.794  1.00 20.96  ?  172 ALA D C   1 
ATOM   2911 O  O   . ALA B 1 177 ? 62.147 8.642   17.591  1.00 22.06  ?  172 ALA D O   1 
ATOM   2912 C  CB  . ALA B 1 177 ? 59.784 10.377  16.390  1.00 19.43  ?  172 ALA D CB  1 
ATOM   2913 N  N   . ASP B 1 178 ? 60.268 7.486   18.128  1.00 21.41  ?  173 ASP D N   1 
ATOM   2914 C  CA  . ASP B 1 178 ? 60.875 6.131   18.265  1.00 20.97  ?  173 ASP D CA  1 
ATOM   2915 C  C   . ASP B 1 178 ? 59.965 5.148   17.505  1.00 19.65  ?  173 ASP D C   1 
ATOM   2916 O  O   . ASP B 1 178 ? 58.776 5.420   17.443  1.00 16.83  ?  173 ASP D O   1 
ATOM   2917 C  CB  . ASP B 1 178 ? 61.075 5.834   19.757  1.00 23.64  ?  173 ASP D CB  1 
ATOM   2918 C  CG  . ASP B 1 178 ? 62.058 6.753   20.507  1.00 31.60  ?  173 ASP D CG  1 
ATOM   2919 O  OD1 . ASP B 1 178 ? 63.264 6.631   20.215  1.00 38.96  ?  173 ASP D OD1 1 
ATOM   2920 O  OD2 . ASP B 1 178 ? 61.621 7.587   21.409  1.00 29.63  -1 173 ASP D OD2 1 
ATOM   2921 N  N   . GLY B 1 179 ? 60.537 4.136   16.867  1.00 18.62  ?  174 GLY D N   1 
ATOM   2922 C  CA  . GLY B 1 179 ? 59.835 3.114   16.071  1.00 18.03  ?  174 GLY D CA  1 
ATOM   2923 C  C   . GLY B 1 179 ? 60.338 1.720   16.385  1.00 17.81  ?  174 GLY D C   1 
ATOM   2924 O  O   . GLY B 1 179 ? 61.549 1.503   16.333  1.00 15.98  ?  174 GLY D O   1 
ATOM   2925 N  N   . MET B 1 180 ? 59.439 0.876   16.866  1.00 17.99  ?  175 MET D N   1 
ATOM   2926 C  CA  . MET B 1 180 ? 59.607 -0.577  17.043  1.00 17.00  ?  175 MET D CA  1 
ATOM   2927 C  C   . MET B 1 180 ? 59.258 -1.254  15.716  1.00 17.29  ?  175 MET D C   1 
ATOM   2928 O  O   . MET B 1 180 ? 58.048 -1.189  15.287  1.00 17.53  ?  175 MET D O   1 
ATOM   2929 C  CB  . MET B 1 180 ? 58.694 -1.081  18.173  1.00 17.08  ?  175 MET D CB  1 
ATOM   2930 C  CG  . MET B 1 180 ? 58.777 -2.556  18.433  1.00 20.00  ?  175 MET D CG  1 
ATOM   2931 S  SD  . MET B 1 180 ? 60.293 -3.048  19.305  1.00 23.26  ?  175 MET D SD  1 
ATOM   2932 C  CE  . MET B 1 180 ? 59.873 -2.417  20.924  1.00 21.13  ?  175 MET D CE  1 
ATOM   2933 N  N   . PHE B 1 181 ? 60.238 -1.870  15.053  1.00 16.07  ?  176 PHE D N   1 
ATOM   2934 C  CA  . PHE B 1 181 ? 59.921 -2.741  13.895  1.00 17.04  ?  176 PHE D CA  1 
ATOM   2935 C  C   . PHE B 1 181 ? 60.371 -4.159  14.228  1.00 19.62  ?  176 PHE D C   1 
ATOM   2936 O  O   . PHE B 1 181 ? 61.467 -4.598  13.851  1.00 17.05  ?  176 PHE D O   1 
ATOM   2937 C  CB  . PHE B 1 181 ? 60.496 -2.179  12.602  1.00 17.20  ?  176 PHE D CB  1 
ATOM   2938 C  CG  . PHE B 1 181 ? 59.815 -0.895  12.233  1.00 16.49  ?  176 PHE D CG  1 
ATOM   2939 C  CD1 . PHE B 1 181 ? 60.096 0.268   12.914  1.00 18.05  ?  176 PHE D CD1 1 
ATOM   2940 C  CD2 . PHE B 1 181 ? 58.807 -0.884  11.289  1.00 17.22  ?  176 PHE D CD2 1 
ATOM   2941 C  CE1 . PHE B 1 181 ? 59.421 1.445   12.610  1.00 18.83  ?  176 PHE D CE1 1 
ATOM   2942 C  CE2 . PHE B 1 181 ? 58.140 0.290   10.979  1.00 19.21  ?  176 PHE D CE2 1 
ATOM   2943 C  CZ  . PHE B 1 181 ? 58.464 1.456   11.631  1.00 18.10  ?  176 PHE D CZ  1 
ATOM   2944 N  N   . LYS B 1 182 ? 59.545 -4.813  15.032  1.00 19.68  ?  177 LYS D N   1 
ATOM   2945 C  CA  . LYS B 1 182 ? 59.891 -6.118  15.597  1.00 18.19  ?  177 LYS D CA  1 
ATOM   2946 C  C   . LYS B 1 182 ? 59.492 -7.157  14.551  1.00 16.71  ?  177 LYS D C   1 
ATOM   2947 O  O   . LYS B 1 182 ? 58.284 -7.507  14.441  1.00 15.28  ?  177 LYS D O   1 
ATOM   2948 C  CB  . LYS B 1 182 ? 59.170 -6.344  16.919  1.00 19.66  ?  177 LYS D CB  1 
ATOM   2949 C  CG  . LYS B 1 182 ? 59.520 -7.682  17.544  1.00 21.16  ?  177 LYS D CG  1 
ATOM   2950 C  CD  . LYS B 1 182 ? 59.243 -7.742  19.014  1.00 24.88  ?  177 LYS D CD  1 
ATOM   2951 C  CE  . LYS B 1 182 ? 58.990 -9.149  19.507  1.00 29.25  ?  177 LYS D CE  1 
ATOM   2952 N  NZ  . LYS B 1 182 ? 59.978 -10.116 18.990  1.00 31.76  ?  177 LYS D NZ  1 
ATOM   2953 N  N   . LEU B 1 183 ? 60.446 -7.595  13.760  1.00 14.29  ?  178 LEU D N   1 
ATOM   2954 C  CA  . LEU B 1 183 ? 60.113 -8.326  12.514  1.00 15.84  ?  178 LEU D CA  1 
ATOM   2955 C  C   . LEU B 1 183 ? 61.100 -9.494  12.337  1.00 15.29  ?  178 LEU D C   1 
ATOM   2956 O  O   . LEU B 1 183 ? 61.547 -9.713  11.196  1.00 16.76  ?  178 LEU D O   1 
ATOM   2957 C  CB  . LEU B 1 183 ? 60.177 -7.345  11.329  1.00 16.21  ?  178 LEU D CB  1 
ATOM   2958 C  CG  . LEU B 1 183 ? 59.115 -6.242  11.299  1.00 15.58  ?  178 LEU D CG  1 
ATOM   2959 C  CD1 . LEU B 1 183 ? 59.457 -5.171  10.276  1.00 16.61  ?  178 LEU D CD1 1 
ATOM   2960 C  CD2 . LEU B 1 183 ? 57.755 -6.857  11.007  1.00 16.15  ?  178 LEU D CD2 1 
ATOM   2961 N  N   . SER B 1 184 ? 61.425 -10.206 13.413  1.00 15.54  ?  179 SER D N   1 
ATOM   2962 C  CA  . SER B 1 184 ? 62.250 -11.450 13.394  1.00 17.50  ?  179 SER D CA  1 
ATOM   2963 C  C   . SER B 1 184 ? 63.720 -11.150 13.029  1.00 17.00  ?  179 SER D C   1 
ATOM   2964 O  O   . SER B 1 184 ? 64.472 -12.114 12.754  1.00 17.58  ?  179 SER D O   1 
ATOM   2965 C  CB  . SER B 1 184 ? 61.682 -12.478 12.489  1.00 16.97  ?  179 SER D CB  1 
ATOM   2966 O  OG  . SER B 1 184 ? 60.387 -12.871 12.897  1.00 15.63  ?  179 SER D OG  1 
ATOM   2967 N  N   . GLN B 1 185 ? 64.168 -9.902  13.102  1.00 17.59  ?  180 GLN D N   1 
ATOM   2968 C  CA  . GLN B 1 185 ? 65.592 -9.554  12.808  1.00 18.69  ?  180 GLN D CA  1 
ATOM   2969 C  C   . GLN B 1 185 ? 66.529 -10.277 13.805  1.00 21.63  ?  180 GLN D C   1 
ATOM   2970 O  O   . GLN B 1 185 ? 67.716 -10.390 13.443  1.00 24.56  ?  180 GLN D O   1 
ATOM   2971 C  CB  . GLN B 1 185 ? 65.857 -8.045  12.818  1.00 17.17  ?  180 GLN D CB  1 
ATOM   2972 C  CG  . GLN B 1 185 ? 65.054 -7.249  11.785  1.00 17.31  ?  180 GLN D CG  1 
ATOM   2973 C  CD  . GLN B 1 185 ? 63.783 -6.690  12.373  1.00 16.57  ?  180 GLN D CD  1 
ATOM   2974 O  OE1 . GLN B 1 185 ? 63.127 -7.368  13.129  1.00 16.36  ?  180 GLN D OE1 1 
ATOM   2975 N  NE2 . GLN B 1 185 ? 63.487 -5.414  12.137  1.00 16.89  ?  180 GLN D NE2 1 
ATOM   2976 N  N   . GLU B 1 186 ? 66.047 -10.737 14.974  1.00 23.51  ?  181 GLU D N   1 
ATOM   2977 C  CA  . GLU B 1 186 ? 66.819 -11.516 15.991  1.00 26.14  ?  181 GLU D CA  1 
ATOM   2978 C  C   . GLU B 1 186 ? 67.093 -12.932 15.471  1.00 27.07  ?  181 GLU D C   1 
ATOM   2979 O  O   . GLU B 1 186 ? 68.048 -13.547 15.983  1.00 28.87  ?  181 GLU D O   1 
ATOM   2980 C  CB  . GLU B 1 186 ? 66.158 -11.562 17.382  1.00 25.05  ?  181 GLU D CB  1 
ATOM   2981 C  CG  . GLU B 1 186 ? 65.083 -12.632 17.605  1.00 24.65  ?  181 GLU D CG  1 
ATOM   2982 C  CD  . GLU B 1 186 ? 63.750 -12.386 16.920  1.00 27.11  ?  181 GLU D CD  1 
ATOM   2983 O  OE1 . GLU B 1 186 ? 63.603 -11.257 16.333  1.00 23.62  ?  181 GLU D OE1 1 
ATOM   2984 O  OE2 . GLU B 1 186 ? 62.858 -13.302 16.977  1.00 22.13  -1 181 GLU D OE2 1 
ATOM   2985 N  N   . GLN B 1 187 ? 66.320 -13.443 14.505  1.00 25.32  ?  182 GLN D N   1 
ATOM   2986 C  CA  . GLN B 1 187 ? 66.502 -14.836 14.015  1.00 23.80  ?  182 GLN D CA  1 
ATOM   2987 C  C   . GLN B 1 187 ? 67.636 -14.860 12.977  1.00 23.80  ?  182 GLN D C   1 
ATOM   2988 O  O   . GLN B 1 187 ? 68.002 -13.791 12.426  1.00 22.17  ?  182 GLN D O   1 
ATOM   2989 C  CB  . GLN B 1 187 ? 65.193 -15.419 13.490  1.00 24.11  ?  182 GLN D CB  1 
ATOM   2990 C  CG  . GLN B 1 187 ? 64.093 -15.473 14.536  1.00 24.22  ?  182 GLN D CG  1 
ATOM   2991 C  CD  . GLN B 1 187 ? 64.434 -16.380 15.694  1.00 25.95  ?  182 GLN D CD  1 
ATOM   2992 O  OE1 . GLN B 1 187 ? 64.841 -17.533 15.526  1.00 25.22  ?  182 GLN D OE1 1 
ATOM   2993 N  NE2 . GLN B 1 187 ? 64.225 -15.873 16.893  1.00 27.51  ?  182 GLN D NE2 1 
ATOM   2994 N  N   . GLN B 1 188 ? 68.164 -16.050 12.721  1.00 25.04  ?  183 GLN D N   1 
ATOM   2995 C  CA  . GLN B 1 188 ? 69.116 -16.331 11.611  1.00 28.77  ?  183 GLN D CA  1 
ATOM   2996 C  C   . GLN B 1 188 ? 68.410 -16.131 10.266  1.00 28.26  ?  183 GLN D C   1 
ATOM   2997 O  O   . GLN B 1 188 ? 67.207 -16.365 10.159  1.00 24.97  ?  183 GLN D O   1 
ATOM   2998 C  CB  . GLN B 1 188 ? 69.646 -17.758 11.761  1.00 29.13  ?  183 GLN D CB  1 
ATOM   2999 C  CG  . GLN B 1 188 ? 70.499 -17.953 13.009  1.00 32.00  ?  183 GLN D CG  1 
ATOM   3000 C  CD  . GLN B 1 188 ? 71.836 -17.283 12.825  1.00 35.11  ?  183 GLN D CD  1 
ATOM   3001 O  OE1 . GLN B 1 188 ? 72.524 -17.505 11.826  1.00 36.65  ?  183 GLN D OE1 1 
ATOM   3002 N  NE2 . GLN B 1 188 ? 72.208 -16.452 13.784  1.00 40.29  ?  183 GLN D NE2 1 
ATOM   3003 N  N   . PRO B 1 189 ? 69.134 -15.747 9.186   1.00 32.38  ?  184 PRO D N   1 
ATOM   3004 C  CA  . PRO B 1 189 ? 68.520 -15.472 7.873   1.00 33.12  ?  184 PRO D CA  1 
ATOM   3005 C  C   . PRO B 1 189 ? 67.506 -16.486 7.333   1.00 32.01  ?  184 PRO D C   1 
ATOM   3006 O  O   . PRO B 1 189 ? 66.430 -16.055 6.924   1.00 33.50  ?  184 PRO D O   1 
ATOM   3007 C  CB  . PRO B 1 189 ? 69.726 -15.417 6.924   1.00 36.70  ?  184 PRO D CB  1 
ATOM   3008 C  CG  . PRO B 1 189 ? 70.841 -14.889 7.814   1.00 35.98  ?  184 PRO D CG  1 
ATOM   3009 C  CD  . PRO B 1 189 ? 70.596 -15.535 9.165   1.00 35.33  ?  184 PRO D CD  1 
ATOM   3010 N  N   . ALA B 1 190 ? 67.825 -17.781 7.367   1.00 29.17  ?  185 ALA D N   1 
ATOM   3011 C  CA  . ALA B 1 190 ? 66.939 -18.857 6.883   1.00 31.84  ?  185 ALA D CA  1 
ATOM   3012 C  C   . ALA B 1 190 ? 65.621 -18.839 7.657   1.00 32.05  ?  185 ALA D C   1 
ATOM   3013 O  O   . ALA B 1 190 ? 64.602 -19.096 7.044   1.00 31.58  ?  185 ALA D O   1 
ATOM   3014 C  CB  . ALA B 1 190 ? 67.610 -20.201 6.998   1.00 36.08  ?  185 ALA D CB  1 
ATOM   3015 N  N   . ILE B 1 191 ? 65.659 -18.593 8.968   1.00 28.13  ?  186 ILE D N   1 
ATOM   3016 C  CA  . ILE B 1 191 ? 64.443 -18.608 9.820   1.00 28.10  ?  186 ILE D CA  1 
ATOM   3017 C  C   . ILE B 1 191 ? 63.598 -17.363 9.487   1.00 25.21  ?  186 ILE D C   1 
ATOM   3018 O  O   . ILE B 1 191 ? 62.367 -17.503 9.378   1.00 24.11  ?  186 ILE D O   1 
ATOM   3019 C  CB  . ILE B 1 191 ? 64.824 -18.706 11.305  1.00 29.63  ?  186 ILE D CB  1 
ATOM   3020 C  CG1 . ILE B 1 191 ? 65.581 -20.003 11.610  1.00 36.32  ?  186 ILE D CG1 1 
ATOM   3021 C  CG2 . ILE B 1 191 ? 63.593 -18.561 12.171  1.00 28.07  ?  186 ILE D CG2 1 
ATOM   3022 C  CD1 . ILE B 1 191 ? 65.824 -20.236 13.088  1.00 37.99  ?  186 ILE D CD1 1 
ATOM   3023 N  N   . ARG B 1 192 ? 64.232 -16.203 9.299   1.00 24.38  ?  187 ARG D N   1 
ATOM   3024 C  CA  . ARG B 1 192 ? 63.528 -14.946 8.899   1.00 26.42  ?  187 ARG D CA  1 
ATOM   3025 C  C   . ARG B 1 192 ? 62.771 -15.219 7.592   1.00 25.66  ?  187 ARG D C   1 
ATOM   3026 O  O   . ARG B 1 192 ? 61.577 -14.853 7.507   1.00 21.37  ?  187 ARG D O   1 
ATOM   3027 C  CB  . ARG B 1 192 ? 64.474 -13.746 8.758   1.00 28.81  ?  187 ARG D CB  1 
ATOM   3028 C  CG  . ARG B 1 192 ? 65.242 -13.417 10.027  1.00 31.18  ?  187 ARG D CG  1 
ATOM   3029 C  CD  . ARG B 1 192 ? 65.979 -12.097 10.007  1.00 37.96  ?  187 ARG D CD  1 
ATOM   3030 N  NE  . ARG B 1 192 ? 66.702 -11.954 8.755   1.00 45.67  ?  187 ARG D NE  1 
ATOM   3031 C  CZ  . ARG B 1 192 ? 68.016 -12.135 8.581   1.00 49.58  ?  187 ARG D CZ  1 
ATOM   3032 N  NH1 . ARG B 1 192 ? 68.806 -12.472 9.592   1.00 49.35  ?  187 ARG D NH1 1 
ATOM   3033 N  NH2 . ARG B 1 192 ? 68.536 -11.974 7.374   1.00 50.01  ?  187 ARG D NH2 1 
ATOM   3034 N  N   . ARG B 1 193 ? 63.405 -15.915 6.644   1.00 25.41  ?  188 ARG D N   1 
ATOM   3035 C  CA  . ARG B 1 193 ? 62.768 -16.310 5.358   1.00 27.11  ?  188 ARG D CA  1 
ATOM   3036 C  C   . ARG B 1 193 ? 61.581 -17.242 5.594   1.00 25.24  ?  188 ARG D C   1 
ATOM   3037 O  O   . ARG B 1 193 ? 60.560 -17.065 4.876   1.00 22.37  ?  188 ARG D O   1 
ATOM   3038 C  CB  . ARG B 1 193 ? 63.735 -16.993 4.385   1.00 31.11  ?  188 ARG D CB  1 
ATOM   3039 C  CG  . ARG B 1 193 ? 64.809 -16.066 3.824   1.00 40.19  ?  188 ARG D CG  1 
ATOM   3040 C  CD  . ARG B 1 193 ? 65.655 -16.733 2.738   1.00 44.92  ?  188 ARG D CD  1 
ATOM   3041 N  NE  . ARG B 1 193 ? 67.077 -16.672 3.073   1.00 49.86  ?  188 ARG D NE  1 
ATOM   3042 C  CZ  . ARG B 1 193 ? 67.854 -17.709 3.389   1.00 51.41  ?  188 ARG D CZ  1 
ATOM   3043 N  NH1 . ARG B 1 193 ? 67.387 -18.952 3.399   1.00 53.97  ?  188 ARG D NH1 1 
ATOM   3044 N  NH2 . ARG B 1 193 ? 69.124 -17.492 3.672   1.00 56.39  ?  188 ARG D NH2 1 
ATOM   3045 N  N   . ARG B 1 194 ? 61.709 -18.219 6.502   1.00 21.58  ?  189 ARG D N   1 
ATOM   3046 C  CA  . ARG B 1 194 ? 60.604 -19.162 6.790   1.00 21.24  ?  189 ARG D CA  1 
ATOM   3047 C  C   . ARG B 1 194 ? 59.405 -18.370 7.328   1.00 19.90  ?  189 ARG D C   1 
ATOM   3048 O  O   . ARG B 1 194 ? 58.267 -18.691 6.940   1.00 19.90  ?  189 ARG D O   1 
ATOM   3049 C  CB  . ARG B 1 194 ? 61.034 -20.251 7.777   1.00 23.21  ?  189 ARG D CB  1 
ATOM   3050 C  CG  . ARG B 1 194 ? 61.949 -21.291 7.151   1.00 26.88  ?  189 ARG D CG  1 
ATOM   3051 C  CD  . ARG B 1 194 ? 62.446 -22.372 8.104   1.00 29.68  ?  189 ARG D CD  1 
ATOM   3052 N  NE  . ARG B 1 194 ? 63.534 -23.060 7.410   1.00 31.38  ?  189 ARG D NE  1 
ATOM   3053 C  CZ  . ARG B 1 194 ? 64.511 -23.755 7.985   1.00 35.25  ?  189 ARG D CZ  1 
ATOM   3054 N  NH1 . ARG B 1 194 ? 64.551 -23.932 9.293   1.00 35.13  ?  189 ARG D NH1 1 
ATOM   3055 N  NH2 . ARG B 1 194 ? 65.446 -24.301 7.230   1.00 36.88  ?  189 ARG D NH2 1 
ATOM   3056 N  N   . VAL B 1 195 ? 59.672 -17.438 8.250   1.00 20.58  ?  190 VAL D N   1 
ATOM   3057 C  CA  . VAL B 1 195 ? 58.645 -16.566 8.881   1.00 19.19  ?  190 VAL D CA  1 
ATOM   3058 C  C   . VAL B 1 195 ? 57.972 -15.742 7.770   1.00 19.56  ?  190 VAL D C   1 
ATOM   3059 O  O   . VAL B 1 195 ? 56.724 -15.773 7.678   1.00 18.43  ?  190 VAL D O   1 
ATOM   3060 C  CB  . VAL B 1 195 ? 59.221 -15.696 10.014  1.00 19.48  ?  190 VAL D CB  1 
ATOM   3061 C  CG1 . VAL B 1 195 ? 58.161 -14.715 10.502  1.00 19.54  ?  190 VAL D CG1 1 
ATOM   3062 C  CG2 . VAL B 1 195 ? 59.723 -16.556 11.190  1.00 20.60  ?  190 VAL D CG2 1 
ATOM   3063 N  N   . ARG B 1 196 ? 58.766 -15.029 6.966   1.00 19.26  ?  191 ARG D N   1 
ATOM   3064 C  CA  . ARG B 1 196 ? 58.252 -14.163 5.866   1.00 23.73  ?  191 ARG D CA  1 
ATOM   3065 C  C   . ARG B 1 196 ? 57.365 -15.023 4.970   1.00 24.68  ?  191 ARG D C   1 
ATOM   3066 O  O   . ARG B 1 196 ? 56.244 -14.580 4.595   1.00 24.81  ?  191 ARG D O   1 
ATOM   3067 C  CB  . ARG B 1 196 ? 59.405 -13.514 5.086   1.00 26.40  ?  191 ARG D CB  1 
ATOM   3068 C  CG  . ARG B 1 196 ? 58.969 -12.711 3.862   1.00 33.51  ?  191 ARG D CG  1 
ATOM   3069 C  CD  . ARG B 1 196 ? 60.135 -12.099 3.091   1.00 44.83  ?  191 ARG D CD  1 
ATOM   3070 N  NE  . ARG B 1 196 ? 61.363 -12.023 3.900   1.00 51.01  ?  191 ARG D NE  1 
ATOM   3071 C  CZ  . ARG B 1 196 ? 62.525 -12.629 3.629   1.00 54.21  ?  191 ARG D CZ  1 
ATOM   3072 N  NH1 . ARG B 1 196 ? 62.666 -13.347 2.525   1.00 58.20  ?  191 ARG D NH1 1 
ATOM   3073 N  NH2 . ARG B 1 196 ? 63.547 -12.513 4.474   1.00 52.01  ?  191 ARG D NH2 1 
ATOM   3074 N  N   . HIS B 1 197 ? 57.824 -16.237 4.656   1.00 23.58  ?  192 HIS D N   1 
ATOM   3075 C  CA  . HIS B 1 197 ? 57.116 -17.135 3.722   1.00 26.33  ?  192 HIS D CA  1 
ATOM   3076 C  C   . HIS B 1 197 ? 55.767 -17.546 4.330   1.00 25.77  ?  192 HIS D C   1 
ATOM   3077 O  O   . HIS B 1 197 ? 54.754 -17.520 3.581   1.00 24.10  ?  192 HIS D O   1 
ATOM   3078 C  CB  . HIS B 1 197 ? 57.963 -18.350 3.358   1.00 29.91  ?  192 HIS D CB  1 
ATOM   3079 C  CG  . HIS B 1 197 ? 57.204 -19.314 2.516   1.00 33.71  ?  192 HIS D CG  1 
ATOM   3080 N  ND1 . HIS B 1 197 ? 56.764 -18.991 1.242   1.00 37.17  ?  192 HIS D ND1 1 
ATOM   3081 C  CD2 . HIS B 1 197 ? 56.778 -20.568 2.765   1.00 37.05  ?  192 HIS D CD2 1 
ATOM   3082 C  CE1 . HIS B 1 197 ? 56.100 -20.011 0.748   1.00 37.96  ?  192 HIS D CE1 1 
ATOM   3083 N  NE2 . HIS B 1 197 ? 56.097 -20.991 1.664   1.00 37.36  ?  192 HIS D NE2 1 
ATOM   3084 N  N   . SER B 1 198 ? 55.745 -17.928 5.613   1.00 25.92  ?  193 SER D N   1 
ATOM   3085 C  CA  . SER B 1 198 ? 54.496 -18.348 6.310   1.00 25.05  ?  193 SER D CA  1 
ATOM   3086 C  C   . SER B 1 198 ? 53.492 -17.187 6.354   1.00 21.43  ?  193 SER D C   1 
ATOM   3087 O  O   . SER B 1 198 ? 52.302 -17.464 6.350   1.00 27.70  ?  193 SER D O   1 
ATOM   3088 C  CB  . SER B 1 198 ? 54.748 -18.861 7.696   1.00 25.94  ?  193 SER D CB  1 
ATOM   3089 O  OG  . SER B 1 198 ? 55.058 -17.781 8.582   1.00 34.73  ?  193 SER D OG  1 
ATOM   3090 N  N   . PHE B 1 199 ? 53.940 -15.943 6.442   1.00 22.06  ?  194 PHE D N   1 
ATOM   3091 C  CA  . PHE B 1 199 ? 53.039 -14.768 6.602   1.00 21.89  ?  194 PHE D CA  1 
ATOM   3092 C  C   . PHE B 1 199 ? 52.497 -14.341 5.228   1.00 25.67  ?  194 PHE D C   1 
ATOM   3093 O  O   . PHE B 1 199 ? 51.447 -13.652 5.190   1.00 22.45  ?  194 PHE D O   1 
ATOM   3094 C  CB  . PHE B 1 199 ? 53.738 -13.612 7.318   1.00 19.89  ?  194 PHE D CB  1 
ATOM   3095 C  CG  . PHE B 1 199 ? 53.928 -13.753 8.815   1.00 20.47  ?  194 PHE D CG  1 
ATOM   3096 C  CD1 . PHE B 1 199 ? 53.114 -14.559 9.597   1.00 21.77  ?  194 PHE D CD1 1 
ATOM   3097 C  CD2 . PHE B 1 199 ? 54.874 -12.978 9.465   1.00 20.52  ?  194 PHE D CD2 1 
ATOM   3098 C  CE1 . PHE B 1 199 ? 53.300 -14.646 10.972  1.00 19.99  ?  194 PHE D CE1 1 
ATOM   3099 C  CE2 . PHE B 1 199 ? 55.040 -13.057 10.839  1.00 19.25  ?  194 PHE D CE2 1 
ATOM   3100 C  CZ  . PHE B 1 199 ? 54.270 -13.897 11.588  1.00 19.15  ?  194 PHE D CZ  1 
ATOM   3101 N  N   . GLY B 1 200 ? 53.178 -14.741 4.144   1.00 23.55  ?  195 GLY D N   1 
ATOM   3102 C  CA  . GLY B 1 200 ? 52.775 -14.475 2.745   1.00 29.40  ?  195 GLY D CA  1 
ATOM   3103 C  C   . GLY B 1 200 ? 51.486 -15.187 2.353   1.00 32.08  ?  195 GLY D C   1 
ATOM   3104 O  O   . GLY B 1 200 ? 50.868 -14.750 1.370   1.00 38.48  ?  195 GLY D O   1 
ATOM   3105 N  N   . GLY B 1 201 ? 51.071 -16.204 3.114   1.00 35.25  ?  196 GLY D N   1 
ATOM   3106 C  CA  . GLY B 1 201 ? 50.005 -17.156 2.748   1.00 37.35  ?  196 GLY D CA  1 
ATOM   3107 C  C   . GLY B 1 201 ? 48.620 -16.787 3.272   1.00 37.88  ?  196 GLY D C   1 
ATOM   3108 O  O   . GLY B 1 201 ? 47.710 -17.613 3.065   1.00 40.61  ?  196 GLY D O   1 
ATOM   3109 N  N   . ALA B 1 202 ? 48.417 -15.616 3.892   1.00 35.02  ?  197 ALA D N   1 
ATOM   3110 C  CA  . ALA B 1 202 ? 47.100 -15.220 4.462   1.00 36.78  ?  197 ALA D CA  1 
ATOM   3111 C  C   . ALA B 1 202 ? 46.964 -13.703 4.593   1.00 36.37  ?  197 ALA D C   1 
ATOM   3112 O  O   . ALA B 1 202 ? 47.961 -13.039 4.931   1.00 36.97  ?  197 ALA D O   1 
ATOM   3113 C  CB  . ALA B 1 202 ? 46.902 -15.914 5.789   1.00 41.05  ?  197 ALA D CB  1 
ATOM   3114 N  N   . GLU B 1 203 ? 45.763 -13.159 4.367   1.00 34.55  ?  198 GLU D N   1 
ATOM   3115 C  CA  . GLU B 1 203 ? 45.539 -11.690 4.399   1.00 36.12  ?  198 GLU D CA  1 
ATOM   3116 C  C   . GLU B 1 203 ? 45.961 -11.097 5.753   1.00 35.08  ?  198 GLU D C   1 
ATOM   3117 O  O   . GLU B 1 203 ? 46.464 -9.958  5.759   1.00 35.04  ?  198 GLU D O   1 
ATOM   3118 C  CB  . GLU B 1 203 ? 44.077 -11.333 4.142   1.00 39.88  ?  198 GLU D CB  1 
ATOM   3119 C  CG  . GLU B 1 203 ? 43.827 -9.831  4.098   1.00 42.68  ?  198 GLU D CG  1 
ATOM   3120 C  CD  . GLU B 1 203 ? 43.518 -9.141  5.419   1.00 47.54  ?  198 GLU D CD  1 
ATOM   3121 O  OE1 . GLU B 1 203 ? 43.257 -9.855  6.434   1.00 54.01  ?  198 GLU D OE1 1 
ATOM   3122 O  OE2 . GLU B 1 203 ? 43.554 -7.884  5.444   1.00 51.77  -1 198 GLU D OE2 1 
ATOM   3123 N  N   . ALA B 1 204 ? 45.707 -11.801 6.863   1.00 32.71  ?  199 ALA D N   1 
ATOM   3124 C  CA  . ALA B 1 204 ? 45.921 -11.285 8.235   1.00 30.59  ?  199 ALA D CA  1 
ATOM   3125 C  C   . ALA B 1 204 ? 47.405 -10.939 8.460   1.00 27.64  ?  199 ALA D C   1 
ATOM   3126 O  O   . ALA B 1 204 ? 47.710 -10.120 9.368   1.00 28.37  ?  199 ALA D O   1 
ATOM   3127 C  CB  . ALA B 1 204 ? 45.438 -12.298 9.238   1.00 29.72  ?  199 ALA D CB  1 
ATOM   3128 N  N   . THR B 1 205 ? 48.311 -11.551 7.697   1.00 25.36  ?  200 THR D N   1 
ATOM   3129 C  CA  . THR B 1 205 ? 49.783 -11.496 7.956   1.00 24.52  ?  200 THR D CA  1 
ATOM   3130 C  C   . THR B 1 205 ? 50.586 -10.957 6.765   1.00 23.61  ?  200 THR D C   1 
ATOM   3131 O  O   . THR B 1 205 ? 51.801 -10.741 6.937   1.00 21.66  ?  200 THR D O   1 
ATOM   3132 C  CB  . THR B 1 205 ? 50.283 -12.893 8.339   1.00 27.78  ?  200 THR D CB  1 
ATOM   3133 O  OG1 . THR B 1 205 ? 50.014 -13.813 7.280   1.00 27.88  ?  200 THR D OG1 1 
ATOM   3134 C  CG2 . THR B 1 205 ? 49.643 -13.423 9.608   1.00 28.03  ?  200 THR D CG2 1 
ATOM   3135 N  N   . ARG B 1 206 ? 49.977 -10.749 5.586   1.00 23.11  ?  201 ARG D N   1 
ATOM   3136 C  CA  . ARG B 1 206 ? 50.704 -10.297 4.361   1.00 25.62  ?  201 ARG D CA  1 
ATOM   3137 C  C   . ARG B 1 206 ? 51.370 -8.931  4.568   1.00 23.83  ?  201 ARG D C   1 
ATOM   3138 O  O   . ARG B 1 206 ? 52.481 -8.719  4.013   1.00 21.87  ?  201 ARG D O   1 
ATOM   3139 C  CB  . ARG B 1 206 ? 49.771 -10.239 3.145   1.00 28.41  ?  201 ARG D CB  1 
ATOM   3140 C  CG  . ARG B 1 206 ? 49.818 -11.495 2.288   1.00 32.94  ?  201 ARG D CG  1 
ATOM   3141 C  CD  . ARG B 1 206 ? 48.784 -11.592 1.157   1.00 34.54  ?  201 ARG D CD  1 
ATOM   3142 N  NE  . ARG B 1 206 ? 48.688 -13.013 0.829   1.00 34.14  ?  201 ARG D NE  1 
ATOM   3143 C  CZ  . ARG B 1 206 ? 47.601 -13.782 0.922   1.00 36.57  ?  201 ARG D CZ  1 
ATOM   3144 N  NH1 . ARG B 1 206 ? 46.425 -13.272 1.262   1.00 35.89  ?  201 ARG D NH1 1 
ATOM   3145 N  NH2 . ARG B 1 206 ? 47.696 -15.070 0.600   1.00 36.40  ?  201 ARG D NH2 1 
ATOM   3146 N  N   . ALA B 1 207 ? 50.753 -8.021  5.334   1.00 22.75  ?  202 ALA D N   1 
ATOM   3147 C  CA  . ALA B 1 207 ? 51.304 -6.667  5.561   1.00 22.68  ?  202 ALA D CA  1 
ATOM   3148 C  C   . ALA B 1 207 ? 52.603 -6.774  6.377   1.00 21.15  ?  202 ALA D C   1 
ATOM   3149 O  O   . ALA B 1 207 ? 53.539 -6.006  6.131   1.00 21.36  ?  202 ALA D O   1 
ATOM   3150 C  CB  . ALA B 1 207 ? 50.271 -5.782  6.224   1.00 24.07  ?  202 ALA D CB  1 
ATOM   3151 N  N   . VAL B 1 208 ? 52.674 -7.716  7.315   1.00 20.34  ?  203 VAL D N   1 
ATOM   3152 C  CA  . VAL B 1 208 ? 53.931 -7.995  8.069   1.00 19.44  ?  203 VAL D CA  1 
ATOM   3153 C  C   . VAL B 1 208 ? 54.963 -8.571  7.087   1.00 18.02  ?  203 VAL D C   1 
ATOM   3154 O  O   . VAL B 1 208 ? 56.114 -8.145  7.122   1.00 19.39  ?  203 VAL D O   1 
ATOM   3155 C  CB  . VAL B 1 208 ? 53.699 -8.963  9.238   1.00 20.46  ?  203 VAL D CB  1 
ATOM   3156 C  CG1 . VAL B 1 208 ? 55.001 -9.278  9.961   1.00 18.74  ?  203 VAL D CG1 1 
ATOM   3157 C  CG2 . VAL B 1 208 ? 52.656 -8.440  10.204  1.00 21.85  ?  203 VAL D CG2 1 
ATOM   3158 N  N   . ALA B 1 209 ? 54.590 -9.558  6.287   1.00 17.10  ?  204 ALA D N   1 
ATOM   3159 C  CA  . ALA B 1 209 ? 55.482 -10.145 5.266   1.00 19.20  ?  204 ALA D CA  1 
ATOM   3160 C  C   . ALA B 1 209 ? 56.026 -9.025  4.360   1.00 20.09  ?  204 ALA D C   1 
ATOM   3161 O  O   . ALA B 1 209 ? 57.229 -9.029  4.063   1.00 21.98  ?  204 ALA D O   1 
ATOM   3162 C  CB  . ALA B 1 209 ? 54.760 -11.223 4.493   1.00 20.51  ?  204 ALA D CB  1 
ATOM   3163 N  N   . GLY B 1 210 ? 55.176 -8.074  3.965   1.00 21.72  ?  205 GLY D N   1 
ATOM   3164 C  CA  . GLY B 1 210 ? 55.554 -6.899  3.149   1.00 24.44  ?  205 GLY D CA  1 
ATOM   3165 C  C   . GLY B 1 210 ? 56.676 -6.092  3.778   1.00 24.36  ?  205 GLY D C   1 
ATOM   3166 O  O   . GLY B 1 210 ? 57.654 -5.705  3.056   1.00 22.12  ?  205 GLY D O   1 
ATOM   3167 N  N   . LEU B 1 211 ? 56.572 -5.815  5.079   1.00 21.24  ?  206 LEU D N   1 
ATOM   3168 C  CA  . LEU B 1 211 ? 57.651 -5.045  5.759   1.00 20.12  ?  206 LEU D CA  1 
ATOM   3169 C  C   . LEU B 1 211 ? 58.934 -5.895  5.885   1.00 18.98  ?  206 LEU D C   1 
ATOM   3170 O  O   . LEU B 1 211 ? 60.112 -5.381  5.654   1.00 18.89  ?  206 LEU D O   1 
ATOM   3171 C  CB  . LEU B 1 211 ? 57.122 -4.665  7.151   1.00 21.29  ?  206 LEU D CB  1 
ATOM   3172 C  CG  . LEU B 1 211 ? 56.133 -3.524  7.176   1.00 24.93  ?  206 LEU D CG  1 
ATOM   3173 C  CD1 . LEU B 1 211 ? 55.481 -3.461  8.530   1.00 26.64  ?  206 LEU D CD1 1 
ATOM   3174 C  CD2 . LEU B 1 211 ? 56.795 -2.193  6.809   1.00 28.94  ?  206 LEU D CD2 1 
ATOM   3175 N  N   . MET B 1 212 ? 58.772 -7.179  6.233   1.00 20.44  ?  207 MET D N   1 
ATOM   3176 C  CA  . MET B 1 212 ? 59.926 -8.114  6.363   1.00 20.81  ?  207 MET D CA  1 
ATOM   3177 C  C   . MET B 1 212 ? 60.695 -8.178  5.034   1.00 23.83  ?  207 MET D C   1 
ATOM   3178 O  O   . MET B 1 212 ? 61.941 -8.197  5.056   1.00 24.94  ?  207 MET D O   1 
ATOM   3179 C  CB  . MET B 1 212 ? 59.448 -9.517  6.753   1.00 23.84  ?  207 MET D CB  1 
ATOM   3180 C  CG  . MET B 1 212 ? 58.971 -9.618  8.200   1.00 22.27  ?  207 MET D CG  1 
ATOM   3181 S  SD  . MET B 1 212 ? 58.436 -11.280 8.675   1.00 20.96  ?  207 MET D SD  1 
ATOM   3182 C  CE  . MET B 1 212 ? 60.028 -12.020 9.072   1.00 22.57  ?  207 MET D CE  1 
ATOM   3183 N  N   . ASP B 1 213 ? 59.987 -8.190  3.906   1.00 26.00  ?  208 ASP D N   1 
ATOM   3184 C  CA  . ASP B 1 213 ? 60.584 -8.222  2.541   1.00 28.93  ?  208 ASP D CA  1 
ATOM   3185 C  C   . ASP B 1 213 ? 61.448 -6.971  2.271   1.00 31.55  ?  208 ASP D C   1 
ATOM   3186 O  O   . ASP B 1 213 ? 62.393 -7.069  1.463   1.00 30.44  ?  208 ASP D O   1 
ATOM   3187 C  CB  . ASP B 1 213 ? 59.482 -8.414  1.505   1.00 33.47  ?  208 ASP D CB  1 
ATOM   3188 C  CG  . ASP B 1 213 ? 59.786 -9.423  0.423   1.00 41.38  ?  208 ASP D CG  1 
ATOM   3189 O  OD1 . ASP B 1 213 ? 60.896 -10.029 0.465   1.00 47.22  ?  208 ASP D OD1 1 
ATOM   3190 O  OD2 . ASP B 1 213 ? 58.915 -9.575  -0.476  1.00 43.06  -1 208 ASP D OD2 1 
ATOM   3191 N  N   . ARG B 1 214 ? 61.195 -5.836  2.932   1.00 31.76  ?  209 ARG D N   1 
ATOM   3192 C  CA  . ARG B 1 214 ? 61.902 -4.560  2.653   1.00 31.46  ?  209 ARG D CA  1 
ATOM   3193 C  C   . ARG B 1 214 ? 63.084 -4.340  3.590   1.00 34.26  ?  209 ARG D C   1 
ATOM   3194 O  O   . ARG B 1 214 ? 63.756 -3.300  3.435   1.00 35.64  ?  209 ARG D O   1 
ATOM   3195 C  CB  . ARG B 1 214 ? 60.933 -3.397  2.771   1.00 33.92  ?  209 ARG D CB  1 
ATOM   3196 C  CG  . ARG B 1 214 ? 59.802 -3.502  1.770   1.00 37.32  ?  209 ARG D CG  1 
ATOM   3197 C  CD  . ARG B 1 214 ? 58.791 -2.434  2.066   1.00 37.73  ?  209 ARG D CD  1 
ATOM   3198 N  NE  . ARG B 1 214 ? 59.427 -1.123  2.065   1.00 39.63  ?  209 ARG D NE  1 
ATOM   3199 C  CZ  . ARG B 1 214 ? 59.011 -0.098  2.803   1.00 39.35  ?  209 ARG D CZ  1 
ATOM   3200 N  NH1 . ARG B 1 214 ? 57.967 -0.246  3.602   1.00 39.58  ?  209 ARG D NH1 1 
ATOM   3201 N  NH2 . ARG B 1 214 ? 59.631 1.068   2.732   1.00 40.08  ?  209 ARG D NH2 1 
ATOM   3202 N  N   . LEU B 1 215 ? 63.350 -5.259  4.516   1.00 28.55  ?  210 LEU D N   1 
ATOM   3203 C  CA  . LEU B 1 215 ? 64.506 -5.074  5.405   1.00 35.48  ?  210 LEU D CA  1 
ATOM   3204 C  C   . LEU B 1 215 ? 65.757 -5.292  4.554   1.00 37.77  ?  210 LEU D C   1 
ATOM   3205 O  O   . LEU B 1 215 ? 65.744 -6.091  3.629   1.00 41.69  ?  210 LEU D O   1 
ATOM   3206 C  CB  . LEU B 1 215 ? 64.364 -5.993  6.617   1.00 28.88  ?  210 LEU D CB  1 
ATOM   3207 C  CG  . LEU B 1 215 ? 63.214 -5.600  7.544   1.00 26.12  ?  210 LEU D CG  1 
ATOM   3208 C  CD1 . LEU B 1 215 ? 63.041 -6.630  8.643   1.00 23.91  ?  210 LEU D CD1 1 
ATOM   3209 C  CD2 . LEU B 1 215 ? 63.443 -4.233  8.159   1.00 27.67  ?  210 LEU D CD2 1 
ATOM   3210 N  N   . PRO B 1 216 ? 66.830 -4.503  4.763   1.00 49.79  ?  211 PRO D N   1 
ATOM   3211 C  CA  . PRO B 1 216 ? 68.030 -4.595  3.923   1.00 50.44  ?  211 PRO D CA  1 
ATOM   3212 C  C   . PRO B 1 216 ? 68.528 -6.032  3.703   1.00 49.33  ?  211 PRO D C   1 
ATOM   3213 O  O   . PRO B 1 216 ? 68.364 -6.822  4.619   1.00 48.81  ?  211 PRO D O   1 
ATOM   3214 C  CB  . PRO B 1 216 ? 69.070 -3.797  4.719   1.00 51.16  ?  211 PRO D CB  1 
ATOM   3215 C  CG  . PRO B 1 216 ? 68.251 -2.785  5.509   1.00 51.56  ?  211 PRO D CG  1 
ATOM   3216 C  CD  . PRO B 1 216 ? 66.930 -3.468  5.805   1.00 49.67  ?  211 PRO D CD  1 
ATOM   3217 N  N   . GLY C 1 4   ? 33.539 -13.813 -34.034 1.00 42.61  ?  -1  GLY A N   1 
ATOM   3218 C  CA  . GLY C 1 4   ? 34.699 -13.005 -34.560 1.00 36.65  ?  -1  GLY A CA  1 
ATOM   3219 C  C   . GLY C 1 4   ? 36.024 -13.377 -33.902 1.00 29.71  ?  -1  GLY A C   1 
ATOM   3220 O  O   . GLY C 1 4   ? 36.214 -14.548 -33.515 1.00 25.72  ?  -1  GLY A O   1 
ATOM   3221 N  N   . ALA C 1 5   ? 36.947 -12.417 -33.816 1.00 30.65  ?  0   ALA A N   1 
ATOM   3222 C  CA  . ALA C 1 5   ? 38.371 -12.658 -33.466 1.00 26.91  ?  0   ALA A CA  1 
ATOM   3223 C  C   . ALA C 1 5   ? 38.558 -12.652 -31.938 1.00 24.22  ?  0   ALA A C   1 
ATOM   3224 O  O   . ALA C 1 5   ? 39.608 -13.079 -31.462 1.00 23.99  ?  0   ALA A O   1 
ATOM   3225 C  CB  . ALA C 1 5   ? 39.238 -11.626 -34.138 1.00 27.36  ?  0   ALA A CB  1 
ATOM   3226 N  N   . MET C 1 6   ? 37.608 -12.080 -31.212 1.00 23.51  ?  1   MET A N   1 
ATOM   3227 C  CA  . MET C 1 6   ? 37.626 -12.032 -29.733 1.00 23.83  ?  1   MET A CA  1 
ATOM   3228 C  C   . MET C 1 6   ? 36.331 -12.642 -29.214 1.00 24.51  ?  1   MET A C   1 
ATOM   3229 O  O   . MET C 1 6   ? 35.248 -12.353 -29.757 1.00 27.27  ?  1   MET A O   1 
ATOM   3230 C  CB  . MET C 1 6   ? 37.786 -10.617 -29.206 1.00 23.37  ?  1   MET A CB  1 
ATOM   3231 C  CG  . MET C 1 6   ? 37.834 -10.542 -27.709 1.00 21.92  ?  1   MET A CG  1 
ATOM   3232 S  SD  . MET C 1 6   ? 37.766 -8.829  -27.280 1.00 24.07  ?  1   MET A SD  1 
ATOM   3233 C  CE  . MET C 1 6   ? 38.062 -8.913  -25.521 1.00 23.14  ?  1   MET A CE  1 
ATOM   3234 N  N   . PHE C 1 7   ? 36.454 -13.569 -28.283 1.00 23.18  ?  2   PHE A N   1 
ATOM   3235 C  CA  . PHE C 1 7   ? 35.281 -14.217 -27.687 1.00 21.84  ?  2   PHE A CA  1 
ATOM   3236 C  C   . PHE C 1 7   ? 34.688 -13.271 -26.631 1.00 21.70  ?  2   PHE A C   1 
ATOM   3237 O  O   . PHE C 1 7   ? 35.397 -12.884 -25.673 1.00 20.92  ?  2   PHE A O   1 
ATOM   3238 C  CB  . PHE C 1 7   ? 35.675 -15.575 -27.131 1.00 21.56  ?  2   PHE A CB  1 
ATOM   3239 C  CG  . PHE C 1 7   ? 34.502 -16.293 -26.506 1.00 22.92  ?  2   PHE A CG  1 
ATOM   3240 C  CD1 . PHE C 1 7   ? 33.434 -16.693 -27.296 1.00 25.90  ?  2   PHE A CD1 1 
ATOM   3241 C  CD2 . PHE C 1 7   ? 34.449 -16.537 -25.141 1.00 24.69  ?  2   PHE A CD2 1 
ATOM   3242 C  CE1 . PHE C 1 7   ? 32.355 -17.367 -26.757 1.00 26.54  ?  2   PHE A CE1 1 
ATOM   3243 C  CE2 . PHE C 1 7   ? 33.365 -17.208 -24.603 1.00 25.58  ?  2   PHE A CE2 1 
ATOM   3244 C  CZ  . PHE C 1 7   ? 32.336 -17.642 -25.411 1.00 27.74  ?  2   PHE A CZ  1 
ATOM   3245 N  N   . VAL C 1 8   ? 33.421 -12.872 -26.815 1.00 20.48  ?  3   VAL A N   1 
ATOM   3246 C  CA  . VAL C 1 8   ? 32.701 -11.988 -25.862 1.00 21.08  ?  3   VAL A CA  1 
ATOM   3247 C  C   . VAL C 1 8   ? 31.293 -12.546 -25.697 1.00 22.47  ?  3   VAL A C   1 
ATOM   3248 O  O   . VAL C 1 8   ? 30.487 -12.426 -26.612 1.00 22.21  ?  3   VAL A O   1 
ATOM   3249 C  CB  . VAL C 1 8   ? 32.687 -10.509 -26.286 1.00 19.71  ?  3   VAL A CB  1 
ATOM   3250 C  CG1 . VAL C 1 8   ? 32.091 -9.641  -25.204 1.00 20.74  ?  3   VAL A CG1 1 
ATOM   3251 C  CG2 . VAL C 1 8   ? 34.058 -9.980  -26.690 1.00 19.62  ?  3   VAL A CG2 1 
ATOM   3252 N  N   . PRO C 1 9   ? 30.984 -13.207 -24.557 1.00 24.46  ?  4   PRO A N   1 
ATOM   3253 C  CA  . PRO C 1 9   ? 29.625 -13.647 -24.272 1.00 26.57  ?  4   PRO A CA  1 
ATOM   3254 C  C   . PRO C 1 9   ? 28.647 -12.474 -24.342 1.00 26.17  ?  4   PRO A C   1 
ATOM   3255 O  O   . PRO C 1 9   ? 28.987 -11.341 -23.986 1.00 22.14  ?  4   PRO A O   1 
ATOM   3256 C  CB  . PRO C 1 9   ? 29.694 -14.213 -22.849 1.00 26.75  ?  4   PRO A CB  1 
ATOM   3257 C  CG  . PRO C 1 9   ? 31.146 -14.635 -22.699 1.00 27.49  ?  4   PRO A CG  1 
ATOM   3258 C  CD  . PRO C 1 9   ? 31.911 -13.589 -23.480 1.00 26.65  ?  4   PRO A CD  1 
ATOM   3259 N  N   . GLY C 1 10  ? 27.435 -12.784 -24.801 1.00 28.42  ?  5   GLY A N   1 
ATOM   3260 C  CA  . GLY C 1 10  ? 26.399 -11.781 -25.096 1.00 28.17  ?  5   GLY A CA  1 
ATOM   3261 C  C   . GLY C 1 10  ? 26.195 -10.796 -23.951 1.00 24.59  ?  5   GLY A C   1 
ATOM   3262 O  O   . GLY C 1 10  ? 26.031 -9.616  -24.209 1.00 25.18  ?  5   GLY A O   1 
ATOM   3263 N  N   . PRO C 1 11  ? 26.161 -11.241 -22.673 1.00 27.25  ?  6   PRO A N   1 
ATOM   3264 C  CA  . PRO C 1 11  ? 25.854 -10.349 -21.565 1.00 26.27  ?  6   PRO A CA  1 
ATOM   3265 C  C   . PRO C 1 11  ? 26.942 -9.289  -21.355 1.00 24.10  ?  6   PRO A C   1 
ATOM   3266 O  O   . PRO C 1 11  ? 26.639 -8.274  -20.737 1.00 22.64  ?  6   PRO A O   1 
ATOM   3267 C  CB  . PRO C 1 11  ? 25.728 -11.280 -20.342 1.00 27.42  ?  6   PRO A CB  1 
ATOM   3268 C  CG  . PRO C 1 11  ? 25.521 -12.662 -20.932 1.00 30.16  ?  6   PRO A CG  1 
ATOM   3269 C  CD  . PRO C 1 11  ? 26.311 -12.632 -22.221 1.00 28.88  ?  6   PRO A CD  1 
ATOM   3270 N  N   . TYR C 1 12  ? 28.146 -9.508  -21.893 1.00 22.75  ?  7   TYR A N   1 
ATOM   3271 C  CA  . TYR C 1 12  ? 29.329 -8.629  -21.664 1.00 21.97  ?  7   TYR A CA  1 
ATOM   3272 C  C   . TYR C 1 12  ? 29.637 -7.704  -22.852 1.00 21.36  ?  7   TYR A C   1 
ATOM   3273 O  O   . TYR C 1 12  ? 30.693 -7.089  -22.840 1.00 21.26  ?  7   TYR A O   1 
ATOM   3274 C  CB  . TYR C 1 12  ? 30.529 -9.499  -21.288 1.00 20.06  ?  7   TYR A CB  1 
ATOM   3275 C  CG  . TYR C 1 12  ? 30.247 -10.411 -20.122 1.00 21.75  ?  7   TYR A CG  1 
ATOM   3276 C  CD1 . TYR C 1 12  ? 29.436 -10.003 -19.073 1.00 22.60  ?  7   TYR A CD1 1 
ATOM   3277 C  CD2 . TYR C 1 12  ? 30.768 -11.689 -20.089 1.00 21.83  ?  7   TYR A CD2 1 
ATOM   3278 C  CE1 . TYR C 1 12  ? 29.151 -10.852 -18.022 1.00 22.30  ?  7   TYR A CE1 1 
ATOM   3279 C  CE2 . TYR C 1 12  ? 30.493 -12.555 -19.050 1.00 23.65  ?  7   TYR A CE2 1 
ATOM   3280 C  CZ  . TYR C 1 12  ? 29.661 -12.137 -18.027 1.00 24.24  ?  7   TYR A CZ  1 
ATOM   3281 O  OH  . TYR C 1 12  ? 29.425 -12.944 -16.974 1.00 28.01  ?  7   TYR A OH  1 
ATOM   3282 N  N   . HIS C 1 13  ? 28.726 -7.513  -23.804 1.00 23.34  ?  8   HIS A N   1 
ATOM   3283 C  CA  . HIS C 1 13  ? 28.893 -6.519  -24.897 1.00 24.87  ?  8   HIS A CA  1 
ATOM   3284 C  C   . HIS C 1 13  ? 28.722 -5.118  -24.303 1.00 24.92  ?  8   HIS A C   1 
ATOM   3285 O  O   . HIS C 1 13  ? 27.888 -4.948  -23.375 1.00 23.28  ?  8   HIS A O   1 
ATOM   3286 C  CB  . HIS C 1 13  ? 27.907 -6.789  -26.044 1.00 28.40  ?  8   HIS A CB  1 
ATOM   3287 C  CG  . HIS C 1 13  ? 28.201 -8.023  -26.820 1.00 33.64  ?  8   HIS A CG  1 
ATOM   3288 N  ND1 . HIS C 1 13  ? 27.847 -8.159  -28.154 1.00 43.19  ?  8   HIS A ND1 1 
ATOM   3289 C  CD2 . HIS C 1 13  ? 28.807 -9.174  -26.478 1.00 33.13  ?  8   HIS A CD2 1 
ATOM   3290 C  CE1 . HIS C 1 13  ? 28.226 -9.344  -28.587 1.00 38.27  ?  8   HIS A CE1 1 
ATOM   3291 N  NE2 . HIS C 1 13  ? 28.821 -9.975  -27.582 1.00 35.67  ?  8   HIS A NE2 1 
ATOM   3292 N  N   . ALA C 1 14  ? 29.467 -4.132  -24.808 1.00 26.37  ?  9   ALA A N   1 
ATOM   3293 C  CA  . ALA C 1 14  ? 29.237 -2.714  -24.429 1.00 26.60  ?  9   ALA A CA  1 
ATOM   3294 C  C   . ALA C 1 14  ? 27.792 -2.346  -24.775 1.00 27.30  ?  9   ALA A C   1 
ATOM   3295 O  O   . ALA C 1 14  ? 27.243 -2.879  -25.753 1.00 22.12  ?  9   ALA A O   1 
ATOM   3296 C  CB  . ALA C 1 14  ? 30.219 -1.809  -25.102 1.00 28.49  ?  9   ALA A CB  1 
ATOM   3297 N  N   . PRO C 1 15  ? 27.154 -1.467  -23.961 1.00 30.33  ?  10  PRO A N   1 
ATOM   3298 C  CA  . PRO C 1 15  ? 25.900 -0.806  -24.306 1.00 31.57  ?  10  PRO A CA  1 
ATOM   3299 C  C   . PRO C 1 15  ? 25.975 -0.050  -25.641 1.00 33.17  ?  10  PRO A C   1 
ATOM   3300 O  O   . PRO C 1 15  ? 25.025 -0.094  -26.376 1.00 31.80  ?  10  PRO A O   1 
ATOM   3301 C  CB  . PRO C 1 15  ? 25.710 0.222   -23.173 1.00 32.47  ?  10  PRO A CB  1 
ATOM   3302 C  CG  . PRO C 1 15  ? 26.365 -0.409  -22.013 1.00 33.55  ?  10  PRO A CG  1 
ATOM   3303 C  CD  . PRO C 1 15  ? 27.582 -1.096  -22.600 1.00 33.50  ?  10  PRO A CD  1 
ATOM   3304 N  N   . GLU C 1 16  ? 27.087 0.642   -25.894 1.00 30.07  ?  11  GLU A N   1 
ATOM   3305 C  CA  . GLU C 1 16  ? 27.269 1.576   -27.037 1.00 33.01  ?  11  GLU A CA  1 
ATOM   3306 C  C   . GLU C 1 16  ? 28.693 1.409   -27.583 1.00 29.33  ?  11  GLU A C   1 
ATOM   3307 O  O   . GLU C 1 16  ? 29.605 1.125   -26.776 1.00 23.42  ?  11  GLU A O   1 
ATOM   3308 C  CB  . GLU C 1 16  ? 27.041 3.032   -26.605 1.00 40.12  ?  11  GLU A CB  1 
ATOM   3309 C  CG  . GLU C 1 16  ? 25.742 3.300   -25.825 1.00 49.59  ?  11  GLU A CG  1 
ATOM   3310 C  CD  . GLU C 1 16  ? 24.430 3.410   -26.610 1.00 56.19  ?  11  GLU A CD  1 
ATOM   3311 O  OE1 . GLU C 1 16  ? 24.448 3.216   -27.851 1.00 61.05  ?  11  GLU A OE1 1 
ATOM   3312 O  OE2 . GLU C 1 16  ? 23.370 3.685   -25.978 1.00 59.30  -1 11  GLU A OE2 1 
ATOM   3313 N  N   . ASP C 1 17  ? 28.891 1.627   -28.885 1.00 25.86  ?  12  ASP A N   1 
ATOM   3314 C  CA  . ASP C 1 17  ? 30.240 1.535   -29.505 1.00 27.93  ?  12  ASP A CA  1 
ATOM   3315 C  C   . ASP C 1 17  ? 31.182 2.533   -28.824 1.00 25.91  ?  12  ASP A C   1 
ATOM   3316 O  O   . ASP C 1 17  ? 32.373 2.270   -28.800 1.00 20.99  ?  12  ASP A O   1 
ATOM   3317 C  CB  . ASP C 1 17  ? 30.202 1.789   -31.011 1.00 30.10  ?  12  ASP A CB  1 
ATOM   3318 C  CG  . ASP C 1 17  ? 29.520 0.681   -31.792 1.00 35.00  ?  12  ASP A CG  1 
ATOM   3319 O  OD1 . ASP C 1 17  ? 29.822 -0.508  -31.531 1.00 33.30  ?  12  ASP A OD1 1 
ATOM   3320 O  OD2 . ASP C 1 17  ? 28.691 1.020   -32.660 1.00 38.19  -1 12  ASP A OD2 1 
ATOM   3321 N  N   . ARG C 1 18  ? 30.658 3.649   -28.309 1.00 23.49  ?  13  ARG A N   1 
ATOM   3322 C  CA  . ARG C 1 18  ? 31.491 4.719   -27.703 1.00 24.43  ?  13  ARG A CA  1 
ATOM   3323 C  C   . ARG C 1 18  ? 32.280 4.190   -26.491 1.00 22.76  ?  13  ARG A C   1 
ATOM   3324 O  O   . ARG C 1 18  ? 33.375 4.789   -26.167 1.00 20.15  ?  13  ARG A O   1 
ATOM   3325 C  CB  . ARG C 1 18  ? 30.605 5.895   -27.300 1.00 26.45  ?  13  ARG A CB  1 
ATOM   3326 C  CG  . ARG C 1 18  ? 31.309 6.934   -26.442 1.00 29.24  ?  13  ARG A CG  1 
ATOM   3327 C  CD  . ARG C 1 18  ? 32.280 7.789   -27.194 1.00 34.14  ?  13  ARG A CD  1 
ATOM   3328 N  NE  . ARG C 1 18  ? 31.534 8.800   -27.927 1.00 47.32  ?  13  ARG A NE  1 
ATOM   3329 C  CZ  . ARG C 1 18  ? 31.763 10.113  -27.914 1.00 50.39  ?  13  ARG A CZ  1 
ATOM   3330 N  NH1 . ARG C 1 18  ? 32.765 10.632  -27.221 1.00 49.98  ?  13  ARG A NH1 1 
ATOM   3331 N  NH2 . ARG C 1 18  ? 30.987 10.905  -28.640 1.00 56.75  ?  13  ARG A NH2 1 
ATOM   3332 N  N   . TRP C 1 19  ? 31.748 3.180   -25.795 1.00 20.06  ?  14  TRP A N   1 
ATOM   3333 C  CA  . TRP C 1 19  ? 32.417 2.607   -24.609 1.00 19.77  ?  14  TRP A CA  1 
ATOM   3334 C  C   . TRP C 1 19  ? 33.787 2.068   -25.029 1.00 19.23  ?  14  TRP A C   1 
ATOM   3335 O  O   . TRP C 1 19  ? 34.695 2.117   -24.192 1.00 17.49  ?  14  TRP A O   1 
ATOM   3336 C  CB  . TRP C 1 19  ? 31.592 1.536   -23.923 1.00 21.56  ?  14  TRP A CB  1 
ATOM   3337 C  CG  . TRP C 1 19  ? 30.442 2.039   -23.103 1.00 23.41  ?  14  TRP A CG  1 
ATOM   3338 C  CD1 . TRP C 1 19  ? 29.494 2.960   -23.460 1.00 25.59  ?  14  TRP A CD1 1 
ATOM   3339 C  CD2 . TRP C 1 19  ? 30.113 1.613   -21.768 1.00 24.10  ?  14  TRP A CD2 1 
ATOM   3340 N  NE1 . TRP C 1 19  ? 28.587 3.115   -22.443 1.00 26.03  ?  14  TRP A NE1 1 
ATOM   3341 C  CE2 . TRP C 1 19  ? 28.941 2.298   -21.397 1.00 25.90  ?  14  TRP A CE2 1 
ATOM   3342 C  CE3 . TRP C 1 19  ? 30.665 0.681   -20.875 1.00 23.02  ?  14  TRP A CE3 1 
ATOM   3343 C  CZ2 . TRP C 1 19  ? 28.350 2.100   -20.148 1.00 27.12  ?  14  TRP A CZ2 1 
ATOM   3344 C  CZ3 . TRP C 1 19  ? 30.077 0.483   -19.652 1.00 24.64  ?  14  TRP A CZ3 1 
ATOM   3345 C  CH2 . TRP C 1 19  ? 28.941 1.198   -19.286 1.00 22.96  ?  14  TRP A CH2 1 
ATOM   3346 N  N   . LEU C 1 20  ? 33.931 1.569   -26.256 1.00 17.63  ?  15  LEU A N   1 
ATOM   3347 C  CA  . LEU C 1 20  ? 35.239 0.980   -26.642 1.00 18.90  ?  15  LEU A CA  1 
ATOM   3348 C  C   . LEU C 1 20  ? 36.228 2.123   -26.870 1.00 20.50  ?  15  LEU A C   1 
ATOM   3349 O  O   . LEU C 1 20  ? 37.404 1.986   -26.505 1.00 18.67  ?  15  LEU A O   1 
ATOM   3350 C  CB  . LEU C 1 20  ? 35.086 0.108   -27.880 1.00 17.99  ?  15  LEU A CB  1 
ATOM   3351 C  CG  . LEU C 1 20  ? 34.456 -1.259  -27.623 1.00 17.90  ?  15  LEU A CG  1 
ATOM   3352 C  CD1 . LEU C 1 20  ? 32.961 -1.149  -27.526 1.00 19.15  ?  15  LEU A CD1 1 
ATOM   3353 C  CD2 . LEU C 1 20  ? 34.852 -2.235  -28.702 1.00 18.08  ?  15  LEU A CD2 1 
ATOM   3354 N  N   . VAL C 1 21  ? 35.764 3.205   -27.510 1.00 19.25  ?  16  VAL A N   1 
ATOM   3355 C  CA  . VAL C 1 21  ? 36.614 4.408   -27.753 1.00 18.67  ?  16  VAL A CA  1 
ATOM   3356 C  C   . VAL C 1 21  ? 37.019 4.970   -26.394 1.00 17.01  ?  16  VAL A C   1 
ATOM   3357 O  O   . VAL C 1 21  ? 38.227 5.286   -26.203 1.00 16.87  ?  16  VAL A O   1 
ATOM   3358 C  CB  . VAL C 1 21  ? 35.934 5.483   -28.620 1.00 17.18  ?  16  VAL A CB  1 
ATOM   3359 C  CG1 . VAL C 1 21  ? 36.801 6.719   -28.696 1.00 15.92  ?  16  VAL A CG1 1 
ATOM   3360 C  CG2 . VAL C 1 21  ? 35.626 4.946   -30.014 1.00 19.08  ?  16  VAL A CG2 1 
ATOM   3361 N  N   . ASP C 1 22  ? 36.069 5.041   -25.468 1.00 17.39  ?  17  ASP A N   1 
ATOM   3362 C  CA  . ASP C 1 22  ? 36.310 5.603   -24.119 1.00 20.02  ?  17  ASP A CA  1 
ATOM   3363 C  C   . ASP C 1 22  ? 37.435 4.808   -23.422 1.00 17.52  ?  17  ASP A C   1 
ATOM   3364 O  O   . ASP C 1 22  ? 38.326 5.409   -22.788 1.00 19.94  ?  17  ASP A O   1 
ATOM   3365 C  CB  . ASP C 1 22  ? 35.018 5.558   -23.318 1.00 22.18  ?  17  ASP A CB  1 
ATOM   3366 C  CG  . ASP C 1 22  ? 33.977 6.599   -23.697 1.00 27.46  ?  17  ASP A CG  1 
ATOM   3367 O  OD1 . ASP C 1 22  ? 34.265 7.524   -24.522 1.00 24.74  ?  17  ASP A OD1 1 
ATOM   3368 O  OD2 . ASP C 1 22  ? 32.858 6.469   -23.148 1.00 28.64  -1 17  ASP A OD2 1 
ATOM   3369 N  N   . LEU C 1 23  ? 37.432 3.482   -23.538 1.00 17.79  ?  18  LEU A N   1 
ATOM   3370 C  CA  . LEU C 1 23  ? 38.442 2.632   -22.854 1.00 17.03  ?  18  LEU A CA  1 
ATOM   3371 C  C   . LEU C 1 23  ? 39.829 2.841   -23.495 1.00 16.51  ?  18  LEU A C   1 
ATOM   3372 O  O   . LEU C 1 23  ? 40.836 2.968   -22.779 1.00 17.19  ?  18  LEU A O   1 
ATOM   3373 C  CB  . LEU C 1 23  ? 37.975 1.174   -22.908 1.00 20.09  ?  18  LEU A CB  1 
ATOM   3374 C  CG  . LEU C 1 23  ? 38.701 0.242   -21.926 1.00 21.69  ?  18  LEU A CG  1 
ATOM   3375 C  CD1 . LEU C 1 23  ? 37.876 -0.973  -21.515 1.00 24.94  ?  18  LEU A CD1 1 
ATOM   3376 C  CD2 . LEU C 1 23  ? 39.997 -0.235  -22.517 1.00 24.31  ?  18  LEU A CD2 1 
ATOM   3377 N  N   . VAL C 1 24  ? 39.888 2.932   -24.814 1.00 16.67  ?  19  VAL A N   1 
ATOM   3378 C  CA  . VAL C 1 24  ? 41.161 3.190   -25.544 1.00 16.41  ?  19  VAL A CA  1 
ATOM   3379 C  C   . VAL C 1 24  ? 41.741 4.522   -25.053 1.00 17.01  ?  19  VAL A C   1 
ATOM   3380 O  O   . VAL C 1 24  ? 42.990 4.576   -24.796 1.00 16.06  ?  19  VAL A O   1 
ATOM   3381 C  CB  . VAL C 1 24  ? 40.964 3.174   -27.065 1.00 15.66  ?  19  VAL A CB  1 
ATOM   3382 C  CG1 . VAL C 1 24  ? 41.910 4.073   -27.746 1.00 15.63  ?  19  VAL A CG1 1 
ATOM   3383 C  CG2 . VAL C 1 24  ? 41.013 1.798   -27.661 1.00 16.88  ?  19  VAL A CG2 1 
ATOM   3384 N  N   . ARG C 1 25  ? 40.888 5.559   -24.926 1.00 17.20  ?  20  ARG A N   1 
ATOM   3385 C  CA  . ARG C 1 25  ? 41.284 6.925   -24.495 1.00 17.41  ?  20  ARG A CA  1 
ATOM   3386 C  C   . ARG C 1 25  ? 41.775 6.850   -23.054 1.00 17.63  ?  20  ARG A C   1 
ATOM   3387 O  O   . ARG C 1 25  ? 42.771 7.495   -22.747 1.00 20.28  ?  20  ARG A O   1 
ATOM   3388 C  CB  . ARG C 1 25  ? 40.123 7.930   -24.656 1.00 17.16  ?  20  ARG A CB  1 
ATOM   3389 C  CG  . ARG C 1 25  ? 39.807 8.230   -26.113 1.00 21.11  ?  20  ARG A CG  1 
ATOM   3390 C  CD  . ARG C 1 25  ? 39.144 9.563   -26.221 1.00 21.02  ?  20  ARG A CD  1 
ATOM   3391 N  NE  . ARG C 1 25  ? 38.448 9.762   -27.465 1.00 26.45  ?  20  ARG A NE  1 
ATOM   3392 C  CZ  . ARG C 1 25  ? 38.916 10.360  -28.521 1.00 26.06  ?  20  ARG A CZ  1 
ATOM   3393 N  NH1 . ARG C 1 25  ? 40.154 10.800  -28.550 1.00 28.89  ?  20  ARG A NH1 1 
ATOM   3394 N  NH2 . ARG C 1 25  ? 38.134 10.492  -29.577 1.00 31.39  ?  20  ARG A NH2 1 
ATOM   3395 N  N   . GLY C 1 26  ? 41.111 6.049   -22.217 1.00 17.94  ?  21  GLY A N   1 
ATOM   3396 C  CA  . GLY C 1 26  ? 41.374 5.993   -20.761 1.00 16.44  ?  21  GLY A CA  1 
ATOM   3397 C  C   . GLY C 1 26  ? 42.620 5.183   -20.416 1.00 15.32  ?  21  GLY A C   1 
ATOM   3398 O  O   . GLY C 1 26  ? 43.126 5.383   -19.321 1.00 15.62  ?  21  GLY A O   1 
ATOM   3399 N  N   . HIS C 1 27  ? 43.035 4.244   -21.272 1.00 13.98  ?  22  HIS A N   1 
ATOM   3400 C  CA  . HIS C 1 27  ? 44.042 3.182   -20.993 1.00 15.65  ?  22  HIS A CA  1 
ATOM   3401 C  C   . HIS C 1 27  ? 44.971 2.997   -22.183 1.00 14.64  ?  22  HIS A C   1 
ATOM   3402 O  O   . HIS C 1 27  ? 44.989 1.964   -22.847 1.00 17.31  ?  22  HIS A O   1 
ATOM   3403 C  CB  . HIS C 1 27  ? 43.299 1.900   -20.583 1.00 17.21  ?  22  HIS A CB  1 
ATOM   3404 C  CG  . HIS C 1 27  ? 42.354 2.182   -19.499 1.00 16.82  ?  22  HIS A CG  1 
ATOM   3405 N  ND1 . HIS C 1 27  ? 42.736 2.129   -18.165 1.00 17.25  ?  22  HIS A ND1 1 
ATOM   3406 C  CD2 . HIS C 1 27  ? 41.052 2.530   -19.505 1.00 19.08  ?  22  HIS A CD2 1 
ATOM   3407 C  CE1 . HIS C 1 27  ? 41.708 2.487   -17.416 1.00 19.11  ?  22  HIS A CE1 1 
ATOM   3408 N  NE2 . HIS C 1 27  ? 40.677 2.726   -18.209 1.00 18.26  ?  22  HIS A NE2 1 
ATOM   3409 N  N   . PRO C 1 28  ? 45.753 4.038   -22.538 1.00 13.02  ?  23  PRO A N   1 
ATOM   3410 C  CA  . PRO C 1 28  ? 46.519 4.038   -23.781 1.00 13.27  ?  23  PRO A CA  1 
ATOM   3411 C  C   . PRO C 1 28  ? 47.734 3.116   -23.876 1.00 14.14  ?  23  PRO A C   1 
ATOM   3412 O  O   . PRO C 1 28  ? 48.230 2.898   -24.996 1.00 11.78  ?  23  PRO A O   1 
ATOM   3413 C  CB  . PRO C 1 28  ? 47.098 5.445   -23.868 1.00 13.46  ?  23  PRO A CB  1 
ATOM   3414 C  CG  . PRO C 1 28  ? 47.038 5.958   -22.476 1.00 12.77  ?  23  PRO A CG  1 
ATOM   3415 C  CD  . PRO C 1 28  ? 45.826 5.303   -21.830 1.00 12.07  ?  23  PRO A CD  1 
ATOM   3416 N  N   . LEU C 1 29  ? 48.195 2.605   -22.736 1.00 13.44  ?  24  LEU A N   1 
ATOM   3417 C  CA  . LEU C 1 29  ? 49.346 1.682   -22.722 1.00 14.71  ?  24  LEU A CA  1 
ATOM   3418 C  C   . LEU C 1 29  ? 48.802 0.283   -23.041 1.00 15.68  ?  24  LEU A C   1 
ATOM   3419 O  O   . LEU C 1 29  ? 48.365 -0.501  -22.124 1.00 13.99  ?  24  LEU A O   1 
ATOM   3420 C  CB  . LEU C 1 29  ? 50.080 1.695   -21.393 1.00 14.96  ?  24  LEU A CB  1 
ATOM   3421 C  CG  . LEU C 1 29  ? 51.438 1.013   -21.472 1.00 14.87  ?  24  LEU A CG  1 
ATOM   3422 C  CD1 . LEU C 1 29  ? 52.379 1.845   -22.338 1.00 16.67  ?  24  LEU A CD1 1 
ATOM   3423 C  CD2 . LEU C 1 29  ? 51.923 0.773   -20.059 1.00 15.97  ?  24  LEU A CD2 1 
ATOM   3424 N  N   . ALA C 1 30  ? 48.812 -0.014  -24.336 1.00 15.35  ?  25  ALA A N   1 
ATOM   3425 C  CA  . ALA C 1 30  ? 48.130 -1.186  -24.897 1.00 15.42  ?  25  ALA A CA  1 
ATOM   3426 C  C   . ALA C 1 30  ? 49.136 -2.330  -24.950 1.00 15.80  ?  25  ALA A C   1 
ATOM   3427 O  O   . ALA C 1 30  ? 50.390 -2.015  -24.980 1.00 15.28  ?  25  ALA A O   1 
ATOM   3428 C  CB  . ALA C 1 30  ? 47.601 -0.845  -26.254 1.00 17.14  ?  25  ALA A CB  1 
ATOM   3429 N  N   . GLN C 1 31  ? 48.660 -3.573  -25.022 1.00 13.03  ?  26  GLN A N   1 
ATOM   3430 C  CA  . GLN C 1 31  ? 49.594 -4.706  -25.311 1.00 15.35  ?  26  GLN A CA  1 
ATOM   3431 C  C   . GLN C 1 31  ? 49.517 -5.009  -26.806 1.00 13.60  ?  26  GLN A C   1 
ATOM   3432 O  O   . GLN C 1 31  ? 48.428 -5.294  -27.335 1.00 15.86  ?  26  GLN A O   1 
ATOM   3433 C  CB  . GLN C 1 31  ? 49.307 -5.932  -24.452 1.00 15.07  ?  26  GLN A CB  1 
ATOM   3434 C  CG  . GLN C 1 31  ? 49.471 -5.677  -22.958 1.00 16.55  ?  26  GLN A CG  1 
ATOM   3435 C  CD  . GLN C 1 31  ? 49.332 -6.961  -22.158 1.00 16.51  ?  26  GLN A CD  1 
ATOM   3436 O  OE1 . GLN C 1 31  ? 49.609 -8.061  -22.659 1.00 19.34  ?  26  GLN A OE1 1 
ATOM   3437 N  NE2 . GLN C 1 31  ? 48.912 -6.829  -20.912 1.00 17.28  ?  26  GLN A NE2 1 
ATOM   3438 N  N   . LEU C 1 32  ? 50.587 -4.743  -27.521 1.00 15.61  ?  27  LEU A N   1 
ATOM   3439 C  CA  . LEU C 1 32  ? 50.673 -5.020  -28.982 1.00 16.17  ?  27  LEU A CA  1 
ATOM   3440 C  C   . LEU C 1 32  ? 51.201 -6.442  -29.189 1.00 16.08  ?  27  LEU A C   1 
ATOM   3441 O  O   . LEU C 1 32  ? 52.298 -6.748  -28.692 1.00 18.19  ?  27  LEU A O   1 
ATOM   3442 C  CB  . LEU C 1 32  ? 51.596 -4.008  -29.675 1.00 15.50  ?  27  LEU A CB  1 
ATOM   3443 C  CG  . LEU C 1 32  ? 51.707 -4.171  -31.188 1.00 16.67  ?  27  LEU A CG  1 
ATOM   3444 C  CD1 . LEU C 1 32  ? 50.395 -3.823  -31.865 1.00 18.19  ?  27  LEU A CD1 1 
ATOM   3445 C  CD2 . LEU C 1 32  ? 52.839 -3.323  -31.751 1.00 18.21  ?  27  LEU A CD2 1 
ATOM   3446 N  N   . ALA C 1 33  ? 50.446 -7.253  -29.922 1.00 15.89  ?  28  ALA A N   1 
ATOM   3447 C  CA  . ALA C 1 33  ? 50.764 -8.679  -30.173 1.00 15.63  ?  28  ALA A CA  1 
ATOM   3448 C  C   . ALA C 1 33  ? 50.794 -8.965  -31.669 1.00 15.28  ?  28  ALA A C   1 
ATOM   3449 O  O   . ALA C 1 33  ? 49.870 -8.527  -32.429 1.00 17.02  ?  28  ALA A O   1 
ATOM   3450 C  CB  . ALA C 1 33  ? 49.769 -9.568  -29.469 1.00 15.69  ?  28  ALA A CB  1 
ATOM   3451 N  N   . SER C 1 34  ? 51.796 -9.721  -32.078 1.00 16.54  ?  29  SER A N   1 
ATOM   3452 C  CA  . SER C 1 34  ? 51.924 -10.250 -33.458 1.00 17.60  ?  29  SER A CA  1 
ATOM   3453 C  C   . SER C 1 34  ? 52.563 -11.652 -33.392 1.00 18.36  ?  29  SER A C   1 
ATOM   3454 O  O   . SER C 1 34  ? 53.154 -12.028 -32.353 1.00 19.09  ?  29  SER A O   1 
ATOM   3455 C  CB  . SER C 1 34  ? 52.708 -9.280  -34.309 1.00 18.38  ?  29  SER A CB  1 
ATOM   3456 O  OG  . SER C 1 34  ? 54.072 -9.223  -33.876 1.00 17.95  ?  29  SER A OG  1 
ATOM   3457 N  N   . ASN C 1 35  ? 52.368 -12.438 -34.437 1.00 18.97  ?  30  ASN A N   1 
ATOM   3458 C  CA  . ASN C 1 35  ? 52.732 -13.870 -34.456 1.00 19.62  ?  30  ASN A CA  1 
ATOM   3459 C  C   . ASN C 1 35  ? 54.245 -14.025 -34.266 1.00 21.65  ?  30  ASN A C   1 
ATOM   3460 O  O   . ASN C 1 35  ? 55.016 -13.211 -34.808 1.00 20.84  ?  30  ASN A O   1 
ATOM   3461 C  CB  . ASN C 1 35  ? 52.294 -14.540 -35.744 1.00 19.09  ?  30  ASN A CB  1 
ATOM   3462 C  CG  . ASN C 1 35  ? 50.809 -14.793 -35.817 1.00 20.79  ?  30  ASN A CG  1 
ATOM   3463 O  OD1 . ASN C 1 35  ? 50.084 -14.679 -34.817 1.00 19.26  ?  30  ASN A OD1 1 
ATOM   3464 N  ND2 . ASN C 1 35  ? 50.354 -15.166 -37.009 1.00 21.31  ?  30  ASN A ND2 1 
ATOM   3465 N  N   . GLY C 1 36  ? 54.644 -15.014 -33.476 1.00 21.67  ?  31  GLY A N   1 
ATOM   3466 C  CA  . GLY C 1 36  ? 56.043 -15.468 -33.417 1.00 22.46  ?  31  GLY A CA  1 
ATOM   3467 C  C   . GLY C 1 36  ? 56.371 -16.278 -34.671 1.00 24.79  ?  31  GLY A C   1 
ATOM   3468 O  O   . GLY C 1 36  ? 55.474 -16.881 -35.239 1.00 26.74  ?  31  GLY A O   1 
ATOM   3469 N  N   . ALA C 1 37  ? 57.610 -16.241 -35.133 1.00 27.81  ?  32  ALA A N   1 
ATOM   3470 C  CA  . ALA C 1 37  ? 58.025 -16.990 -36.347 1.00 29.98  ?  32  ALA A CA  1 
ATOM   3471 C  C   . ALA C 1 37  ? 58.178 -18.470 -35.982 1.00 30.81  ?  32  ALA A C   1 
ATOM   3472 O  O   . ALA C 1 37  ? 58.651 -18.775 -34.828 1.00 29.84  ?  32  ALA A O   1 
ATOM   3473 C  CB  . ALA C 1 37  ? 59.303 -16.403 -36.909 1.00 28.90  ?  32  ALA A CB  1 
ATOM   3474 N  N   . GLY C 1 38  ? 57.785 -19.344 -36.918 1.00 31.74  ?  33  GLY A N   1 
ATOM   3475 C  CA  . GLY C 1 38  ? 57.971 -20.806 -36.859 1.00 34.76  ?  33  GLY A CA  1 
ATOM   3476 C  C   . GLY C 1 38  ? 57.329 -21.396 -35.619 1.00 37.64  ?  33  GLY A C   1 
ATOM   3477 O  O   . GLY C 1 38  ? 58.017 -22.122 -34.883 1.00 40.97  ?  33  GLY A O   1 
ATOM   3478 N  N   . GLY C 1 39  ? 56.082 -21.012 -35.340 1.00 38.46  ?  34  GLY A N   1 
ATOM   3479 C  CA  . GLY C 1 39  ? 55.265 -21.589 -34.255 1.00 39.31  ?  34  GLY A CA  1 
ATOM   3480 C  C   . GLY C 1 39  ? 55.665 -21.113 -32.861 1.00 41.24  ?  34  GLY A C   1 
ATOM   3481 O  O   . GLY C 1 39  ? 55.071 -21.654 -31.894 1.00 42.46  ?  34  GLY A O   1 
ATOM   3482 N  N   . ALA C 1 40  ? 56.599 -20.151 -32.733 1.00 35.56  ?  35  ALA A N   1 
ATOM   3483 C  CA  . ALA C 1 40  ? 57.012 -19.546 -31.438 1.00 31.50  ?  35  ALA A CA  1 
ATOM   3484 C  C   . ALA C 1 40  ? 55.841 -18.740 -30.889 1.00 27.21  ?  35  ALA A C   1 
ATOM   3485 O  O   . ALA C 1 40  ? 54.939 -18.405 -31.673 1.00 25.16  ?  35  ALA A O   1 
ATOM   3486 C  CB  . ALA C 1 40  ? 58.222 -18.665 -31.547 1.00 29.99  ?  35  ALA A CB  1 
ATOM   3487 N  N   . ALA C 1 41  ? 55.844 -18.468 -29.585 1.00 24.87  ?  36  ALA A N   1 
ATOM   3488 C  CA  . ALA C 1 41  ? 54.776 -17.661 -28.941 1.00 21.67  ?  36  ALA A CA  1 
ATOM   3489 C  C   . ALA C 1 41  ? 54.778 -16.275 -29.577 1.00 20.05  ?  36  ALA A C   1 
ATOM   3490 O  O   . ALA C 1 41  ? 55.820 -15.784 -30.019 1.00 21.87  ?  36  ALA A O   1 
ATOM   3491 C  CB  . ALA C 1 41  ? 54.963 -17.566 -27.443 1.00 20.92  ?  36  ALA A CB  1 
ATOM   3492 N  N   . PRO C 1 42  ? 53.617 -15.598 -29.627 1.00 19.25  ?  37  PRO A N   1 
ATOM   3493 C  CA  . PRO C 1 42  ? 53.562 -14.211 -30.072 1.00 18.21  ?  37  PRO A CA  1 
ATOM   3494 C  C   . PRO C 1 42  ? 54.569 -13.279 -29.370 1.00 18.66  ?  37  PRO A C   1 
ATOM   3495 O  O   . PRO C 1 42  ? 54.937 -13.471 -28.217 1.00 17.54  ?  37  PRO A O   1 
ATOM   3496 C  CB  . PRO C 1 42  ? 52.117 -13.816 -29.742 1.00 19.12  ?  37  PRO A CB  1 
ATOM   3497 C  CG  . PRO C 1 42  ? 51.372 -15.108 -29.875 1.00 17.14  ?  37  PRO A CG  1 
ATOM   3498 C  CD  . PRO C 1 42  ? 52.288 -16.142 -29.284 1.00 17.81  ?  37  PRO A CD  1 
ATOM   3499 N  N   . HIS C 1 43  ? 54.990 -12.243 -30.097 1.00 18.58  ?  38  HIS A N   1 
ATOM   3500 C  CA  . HIS C 1 43  ? 55.717 -11.073 -29.554 1.00 18.47  ?  38  HIS A CA  1 
ATOM   3501 C  C   . HIS C 1 43  ? 54.689 -10.193 -28.831 1.00 15.57  ?  38  HIS A C   1 
ATOM   3502 O  O   . HIS C 1 43  ? 53.613 -10.039 -29.368 1.00 17.12  ?  38  HIS A O   1 
ATOM   3503 C  CB  . HIS C 1 43  ? 56.376 -10.254 -30.683 1.00 21.96  ?  38  HIS A CB  1 
ATOM   3504 C  CG  . HIS C 1 43  ? 57.331 -11.021 -31.530 1.00 24.17  ?  38  HIS A CG  1 
ATOM   3505 N  ND1 . HIS C 1 43  ? 58.663 -11.154 -31.206 1.00 29.45  ?  38  HIS A ND1 1 
ATOM   3506 C  CD2 . HIS C 1 43  ? 57.163 -11.652 -32.711 1.00 26.10  ?  38  HIS A CD2 1 
ATOM   3507 C  CE1 . HIS C 1 43  ? 59.266 -11.874 -32.126 1.00 26.88  ?  38  HIS A CE1 1 
ATOM   3508 N  NE2 . HIS C 1 43  ? 58.370 -12.196 -33.048 1.00 26.92  ?  38  HIS A NE2 1 
ATOM   3509 N  N   . ILE C 1 44  ? 54.994 -9.687  -27.647 1.00 15.34  ?  39  ILE A N   1 
ATOM   3510 C  CA  . ILE C 1 44  ? 54.081 -8.765  -26.894 1.00 17.27  ?  39  ILE A CA  1 
ATOM   3511 C  C   . ILE C 1 44  ? 54.928 -7.575  -26.455 1.00 15.87  ?  39  ILE A C   1 
ATOM   3512 O  O   . ILE C 1 44  ? 55.942 -7.783  -25.713 1.00 15.10  ?  39  ILE A O   1 
ATOM   3513 C  CB  . ILE C 1 44  ? 53.436 -9.428  -25.657 1.00 18.00  ?  39  ILE A CB  1 
ATOM   3514 C  CG1 . ILE C 1 44  ? 52.822 -10.800 -25.917 1.00 18.67  ?  39  ILE A CG1 1 
ATOM   3515 C  CG2 . ILE C 1 44  ? 52.438 -8.486  -25.031 1.00 19.64  ?  39  ILE A CG2 1 
ATOM   3516 C  CD1 . ILE C 1 44  ? 51.510 -10.759 -26.662 1.00 18.28  ?  39  ILE A CD1 1 
ATOM   3517 N  N   . THR C 1 45  ? 54.522 -6.373  -26.833 1.00 14.52  ?  40  THR A N   1 
ATOM   3518 C  CA  . THR C 1 45  ? 55.154 -5.131  -26.342 1.00 15.93  ?  40  THR A CA  1 
ATOM   3519 C  C   . THR C 1 45  ? 54.087 -4.184  -25.803 1.00 14.06  ?  40  THR A C   1 
ATOM   3520 O  O   . THR C 1 45  ? 53.051 -4.035  -26.501 1.00 16.40  ?  40  THR A O   1 
ATOM   3521 C  CB  . THR C 1 45  ? 55.981 -4.467  -27.437 1.00 16.05  ?  40  THR A CB  1 
ATOM   3522 O  OG1 . THR C 1 45  ? 56.909 -5.427  -27.939 1.00 16.71  ?  40  THR A OG1 1 
ATOM   3523 C  CG2 . THR C 1 45  ? 56.710 -3.252  -26.904 1.00 16.27  ?  40  THR A CG2 1 
ATOM   3524 N  N   . HIS C 1 46  ? 54.319 -3.597  -24.621 1.00 14.08  ?  41  HIS A N   1 
ATOM   3525 C  CA  . HIS C 1 46  ? 53.490 -2.494  -24.076 1.00 13.81  ?  41  HIS A CA  1 
ATOM   3526 C  C   . HIS C 1 46  ? 53.858 -1.166  -24.783 1.00 15.09  ?  41  HIS A C   1 
ATOM   3527 O  O   . HIS C 1 46  ? 54.996 -0.711  -24.682 1.00 15.03  ?  41  HIS A O   1 
ATOM   3528 C  CB  . HIS C 1 46  ? 53.537 -2.410  -22.552 1.00 14.86  ?  41  HIS A CB  1 
ATOM   3529 C  CG  . HIS C 1 46  ? 52.588 -3.297  -21.770 1.00 17.26  ?  41  HIS A CG  1 
ATOM   3530 N  ND1 . HIS C 1 46  ? 52.952 -4.558  -21.360 1.00 24.04  ?  41  HIS A ND1 1 
ATOM   3531 C  CD2 . HIS C 1 46  ? 51.419 -3.027  -21.137 1.00 22.86  ?  41  HIS A CD2 1 
ATOM   3532 C  CE1 . HIS C 1 46  ? 52.000 -5.077  -20.614 1.00 23.99  ?  41  HIS A CE1 1 
ATOM   3533 N  NE2 . HIS C 1 46  ? 51.033 -4.134  -20.437 1.00 21.75  ?  41  HIS A NE2 1 
ATOM   3534 N  N   . VAL C 1 47  ? 52.883 -0.530  -25.425 1.00 14.71  ?  42  VAL A N   1 
ATOM   3535 C  CA  . VAL C 1 47  ? 53.138 0.610   -26.358 1.00 14.81  ?  42  VAL A CA  1 
ATOM   3536 C  C   . VAL C 1 47  ? 52.028 1.618   -26.196 1.00 15.15  ?  42  VAL A C   1 
ATOM   3537 O  O   . VAL C 1 47  ? 50.870 1.234   -26.065 1.00 15.26  ?  42  VAL A O   1 
ATOM   3538 C  CB  . VAL C 1 47  ? 53.273 0.154   -27.829 1.00 14.22  ?  42  VAL A CB  1 
ATOM   3539 C  CG1 . VAL C 1 47  ? 54.475 -0.750  -28.082 1.00 15.98  ?  42  VAL A CG1 1 
ATOM   3540 C  CG2 . VAL C 1 47  ? 52.025 -0.542  -28.344 1.00 14.80  ?  42  VAL A CG2 1 
ATOM   3541 N  N   . PRO C 1 48  ? 52.372 2.928   -26.189 1.00 16.82  ?  43  PRO A N   1 
ATOM   3542 C  CA  . PRO C 1 48  ? 51.381 3.986   -26.101 1.00 17.35  ?  43  PRO A CA  1 
ATOM   3543 C  C   . PRO C 1 48  ? 50.702 4.222   -27.452 1.00 16.31  ?  43  PRO A C   1 
ATOM   3544 O  O   . PRO C 1 48  ? 51.412 4.614   -28.433 1.00 17.06  ?  43  PRO A O   1 
ATOM   3545 C  CB  . PRO C 1 48  ? 52.214 5.221   -25.721 1.00 16.71  ?  43  PRO A CB  1 
ATOM   3546 C  CG  . PRO C 1 48  ? 53.598 4.953   -26.315 1.00 16.64  ?  43  PRO A CG  1 
ATOM   3547 C  CD  . PRO C 1 48  ? 53.735 3.443   -26.416 1.00 15.58  ?  43  PRO A CD  1 
ATOM   3548 N  N   . ILE C 1 49  ? 49.374 4.069   -27.456 1.00 17.90  ?  44  ILE A N   1 
ATOM   3549 C  CA  . ILE C 1 49  ? 48.525 4.190   -28.671 1.00 17.26  ?  44  ILE A CA  1 
ATOM   3550 C  C   . ILE C 1 49  ? 47.403 5.197   -28.416 1.00 18.34  ?  44  ILE A C   1 
ATOM   3551 O  O   . ILE C 1 49  ? 46.768 5.144   -27.370 1.00 16.86  ?  44  ILE A O   1 
ATOM   3552 C  CB  . ILE C 1 49  ? 47.968 2.832   -29.151 1.00 15.49  ?  44  ILE A CB  1 
ATOM   3553 C  CG1 . ILE C 1 49  ? 49.116 1.883   -29.515 1.00 15.65  ?  44  ILE A CG1 1 
ATOM   3554 C  CG2 . ILE C 1 49  ? 47.005 2.968   -30.323 1.00 15.60  ?  44  ILE A CG2 1 
ATOM   3555 C  CD1 . ILE C 1 49  ? 48.633 0.470   -29.814 1.00 15.39  ?  44  ILE A CD1 1 
ATOM   3556 N  N   . ILE C 1 50  ? 47.201 6.086   -29.385 1.00 18.25  ?  45  ILE A N   1 
ATOM   3557 C  CA  . ILE C 1 50  ? 46.170 7.140   -29.315 1.00 17.68  ?  45  ILE A CA  1 
ATOM   3558 C  C   . ILE C 1 50  ? 45.325 7.073   -30.565 1.00 19.11  ?  45  ILE A C   1 
ATOM   3559 O  O   . ILE C 1 50  ? 45.817 6.631   -31.570 1.00 17.01  ?  45  ILE A O   1 
ATOM   3560 C  CB  . ILE C 1 50  ? 46.787 8.532   -29.148 1.00 18.80  ?  45  ILE A CB  1 
ATOM   3561 C  CG1 . ILE C 1 50  ? 47.650 8.941   -30.331 1.00 19.83  ?  45  ILE A CG1 1 
ATOM   3562 C  CG2 . ILE C 1 50  ? 47.530 8.624   -27.813 1.00 18.85  ?  45  ILE A CG2 1 
ATOM   3563 C  CD1 . ILE C 1 50  ? 47.892 10.437  -30.388 1.00 20.77  ?  45  ILE A CD1 1 
ATOM   3564 N  N   . VAL C 1 51  ? 44.111 7.592   -30.468 1.00 21.75  ?  46  VAL A N   1 
ATOM   3565 C  CA  . VAL C 1 51  ? 43.240 7.802   -31.658 1.00 21.38  ?  46  VAL A CA  1 
ATOM   3566 C  C   . VAL C 1 51  ? 43.861 8.903   -32.522 1.00 21.54  ?  46  VAL A C   1 
ATOM   3567 O  O   . VAL C 1 51  ? 44.332 9.913   -31.978 1.00 19.21  ?  46  VAL A O   1 
ATOM   3568 C  CB  . VAL C 1 51  ? 41.822 8.162   -31.189 1.00 20.19  ?  46  VAL A CB  1 
ATOM   3569 C  CG1 . VAL C 1 51  ? 40.976 8.700   -32.318 1.00 22.73  ?  46  VAL A CG1 1 
ATOM   3570 C  CG2 . VAL C 1 51  ? 41.145 6.997   -30.498 1.00 21.23  ?  46  VAL A CG2 1 
ATOM   3571 N  N   . ASP C 1 52  ? 43.803 8.723   -33.843 1.00 20.56  ?  47  ASP A N   1 
ATOM   3572 C  CA  . ASP C 1 52  ? 44.154 9.733   -34.862 1.00 21.34  ?  47  ASP A CA  1 
ATOM   3573 C  C   . ASP C 1 52  ? 43.814 11.113  -34.311 1.00 19.01  ?  47  ASP A C   1 
ATOM   3574 O  O   . ASP C 1 52  ? 42.635 11.427  -34.119 1.00 21.83  ?  47  ASP A O   1 
ATOM   3575 C  CB  . ASP C 1 52  ? 43.421 9.474   -36.182 1.00 24.70  ?  47  ASP A CB  1 
ATOM   3576 C  CG  . ASP C 1 52  ? 43.733 10.465  -37.305 1.00 26.73  ?  47  ASP A CG  1 
ATOM   3577 O  OD1 . ASP C 1 52  ? 44.542 11.405  -37.083 1.00 24.26  ?  47  ASP A OD1 1 
ATOM   3578 O  OD2 . ASP C 1 52  ? 43.239 10.242  -38.426 1.00 25.93  -1 47  ASP A OD2 1 
ATOM   3579 N  N   . PRO C 1 53  ? 44.822 11.968  -34.063 1.00 20.81  ?  48  PRO A N   1 
ATOM   3580 C  CA  . PRO C 1 53  ? 44.586 13.309  -33.518 1.00 23.31  ?  48  PRO A CA  1 
ATOM   3581 C  C   . PRO C 1 53  ? 43.964 14.269  -34.540 1.00 24.64  ?  48  PRO A C   1 
ATOM   3582 O  O   . PRO C 1 53  ? 43.534 15.326  -34.144 1.00 25.22  ?  48  PRO A O   1 
ATOM   3583 C  CB  . PRO C 1 53  ? 46.002 13.777  -33.189 1.00 23.60  ?  48  PRO A CB  1 
ATOM   3584 C  CG  . PRO C 1 53  ? 46.845 13.102  -34.230 1.00 23.11  ?  48  PRO A CG  1 
ATOM   3585 C  CD  . PRO C 1 53  ? 46.260 11.700  -34.289 1.00 23.04  ?  48  PRO A CD  1 
ATOM   3586 N  N   . GLU C 1 54  ? 43.959 13.888  -35.823 1.00 26.97  ?  49  GLU A N   1 
ATOM   3587 C  CA  . GLU C 1 54  ? 43.383 14.723  -36.912 1.00 26.76  ?  49  GLU A CA  1 
ATOM   3588 C  C   . GLU C 1 54  ? 41.859 14.534  -37.002 1.00 26.36  ?  49  GLU A C   1 
ATOM   3589 O  O   . GLU C 1 54  ? 41.301 15.285  -37.757 1.00 22.87  ?  49  GLU A O   1 
ATOM   3590 C  CB  . GLU C 1 54  ? 44.097 14.470  -38.241 1.00 27.37  ?  49  GLU A CB  1 
ATOM   3591 C  CG  . GLU C 1 54  ? 45.609 14.713  -38.182 1.00 27.94  ?  49  GLU A CG  1 
ATOM   3592 C  CD  . GLU C 1 54  ? 46.064 16.107  -37.756 1.00 32.19  ?  49  GLU A CD  1 
ATOM   3593 O  OE1 . GLU C 1 54  ? 45.451 17.122  -38.227 1.00 36.46  ?  49  GLU A OE1 1 
ATOM   3594 O  OE2 . GLU C 1 54  ? 47.033 16.200  -36.943 1.00 34.30  -1 49  GLU A OE2 1 
ATOM   3595 N  N   . LEU C 1 55  ? 41.213 13.623  -36.246 1.00 26.72  ?  50  LEU A N   1 
ATOM   3596 C  CA  . LEU C 1 55  ? 39.748 13.369  -36.368 1.00 31.37  ?  50  LEU A CA  1 
ATOM   3597 C  C   . LEU C 1 55  ? 38.965 14.497  -35.703 1.00 35.44  ?  50  LEU A C   1 
ATOM   3598 O  O   . LEU C 1 55  ? 39.319 14.889  -34.584 1.00 40.25  ?  50  LEU A O   1 
ATOM   3599 C  CB  . LEU C 1 55  ? 39.381 12.019  -35.744 1.00 33.75  ?  50  LEU A CB  1 
ATOM   3600 C  CG  . LEU C 1 55  ? 39.977 10.809  -36.448 1.00 34.42  ?  50  LEU A CG  1 
ATOM   3601 C  CD1 . LEU C 1 55  ? 39.529 9.527   -35.770 1.00 34.95  ?  50  LEU A CD1 1 
ATOM   3602 C  CD2 . LEU C 1 55  ? 39.629 10.787  -37.936 1.00 34.89  ?  50  LEU A CD2 1 
ATOM   3603 N  N   . ASP C 1 56  ? 37.969 15.028  -36.402 1.00 41.24  ?  51  ASP A N   1 
ATOM   3604 C  CA  . ASP C 1 56  ? 37.120 16.148  -35.916 1.00 48.73  ?  51  ASP A CA  1 
ATOM   3605 C  C   . ASP C 1 56  ? 35.763 15.572  -35.522 1.00 50.93  ?  51  ASP A C   1 
ATOM   3606 O  O   . ASP C 1 56  ? 35.340 14.592  -36.176 1.00 52.24  ?  51  ASP A O   1 
ATOM   3607 C  CB  . ASP C 1 56  ? 36.998 17.260  -36.963 1.00 49.62  ?  51  ASP A CB  1 
ATOM   3608 C  CG  . ASP C 1 56  ? 38.227 18.154  -37.024 1.00 53.34  ?  51  ASP A CG  1 
ATOM   3609 O  OD1 . ASP C 1 56  ? 38.347 19.043  -36.156 1.00 55.80  ?  51  ASP A OD1 1 
ATOM   3610 O  OD2 . ASP C 1 56  ? 39.072 17.937  -37.927 1.00 56.65  -1 51  ASP A OD2 1 
ATOM   3611 N  N   . GLY C 1 57  ? 35.143 16.141  -34.482 1.00 51.71  ?  52  GLY A N   1 
ATOM   3612 C  CA  . GLY C 1 57  ? 33.762 15.819  -34.064 1.00 55.33  ?  52  GLY A CA  1 
ATOM   3613 C  C   . GLY C 1 57  ? 33.724 14.477  -33.346 1.00 58.19  ?  52  GLY A C   1 
ATOM   3614 O  O   . GLY C 1 57  ? 34.789 13.895  -33.113 1.00 60.97  ?  52  GLY A O   1 
ATOM   3615 N  N   . PRO C 1 58  ? 32.521 13.936  -33.021 1.00 49.62  ?  53  PRO A N   1 
ATOM   3616 C  CA  . PRO C 1 58  ? 32.400 12.817  -32.087 1.00 48.48  ?  53  PRO A CA  1 
ATOM   3617 C  C   . PRO C 1 58  ? 32.955 11.530  -32.705 1.00 40.19  ?  53  PRO A C   1 
ATOM   3618 O  O   . PRO C 1 58  ? 32.660 11.253  -33.840 1.00 41.40  ?  53  PRO A O   1 
ATOM   3619 C  CB  . PRO C 1 58  ? 30.883 12.707  -31.821 1.00 53.24  ?  53  PRO A CB  1 
ATOM   3620 C  CG  . PRO C 1 58  ? 30.240 13.282  -33.067 1.00 52.56  ?  53  PRO A CG  1 
ATOM   3621 C  CD  . PRO C 1 58  ? 31.215 14.335  -33.572 1.00 51.80  ?  53  PRO A CD  1 
ATOM   3622 N  N   . VAL C 1 59  ? 33.803 10.816  -31.971 1.00 37.12  ?  54  VAL A N   1 
ATOM   3623 C  CA  . VAL C 1 59  ? 34.345 9.493   -32.405 1.00 34.54  ?  54  VAL A CA  1 
ATOM   3624 C  C   . VAL C 1 59  ? 33.544 8.450   -31.629 1.00 28.83  ?  54  VAL A C   1 
ATOM   3625 O  O   . VAL C 1 59  ? 33.770 8.316   -30.431 1.00 24.76  ?  54  VAL A O   1 
ATOM   3626 C  CB  . VAL C 1 59  ? 35.870 9.363   -32.176 1.00 34.97  ?  54  VAL A CB  1 
ATOM   3627 C  CG1 . VAL C 1 59  ? 36.398 8.013   -32.647 1.00 35.29  ?  54  VAL A CG1 1 
ATOM   3628 C  CG2 . VAL C 1 59  ? 36.630 10.485  -32.861 1.00 39.23  ?  54  VAL A CG2 1 
ATOM   3629 N  N   . ASP C 1 60  ? 32.600 7.786   -32.283 1.00 27.33  ?  55  ASP A N   1 
ATOM   3630 C  CA  . ASP C 1 60  ? 31.688 6.830   -31.611 1.00 30.75  ?  55  ASP A CA  1 
ATOM   3631 C  C   . ASP C 1 60  ? 32.156 5.400   -31.892 1.00 28.29  ?  55  ASP A C   1 
ATOM   3632 O  O   . ASP C 1 60  ? 31.876 4.524   -31.056 1.00 30.58  ?  55  ASP A O   1 
ATOM   3633 C  CB  . ASP C 1 60  ? 30.242 7.171   -31.992 1.00 35.57  ?  55  ASP A CB  1 
ATOM   3634 C  CG  . ASP C 1 60  ? 29.844 8.544   -31.458 1.00 39.99  ?  55  ASP A CG  1 
ATOM   3635 O  OD1 . ASP C 1 60  ? 30.134 8.825   -30.264 1.00 39.62  ?  55  ASP A OD1 1 
ATOM   3636 O  OD2 . ASP C 1 60  ? 29.319 9.362   -32.249 1.00 45.21  -1 55  ASP A OD2 1 
ATOM   3637 N  N   . ARG C 1 61  ? 32.903 5.172   -32.976 1.00 29.33  ?  56  ARG A N   1 
ATOM   3638 C  CA  . ARG C 1 61  ? 33.249 3.803   -33.446 1.00 30.16  ?  56  ARG A CA  1 
ATOM   3639 C  C   . ARG C 1 61  ? 34.755 3.717   -33.665 1.00 25.81  ?  56  ARG A C   1 
ATOM   3640 O  O   . ARG C 1 61  ? 35.305 4.632   -34.282 1.00 28.59  ?  56  ARG A O   1 
ATOM   3641 C  CB  . ARG C 1 61  ? 32.505 3.466   -34.743 1.00 35.43  ?  56  ARG A CB  1 
ATOM   3642 C  CG  . ARG C 1 61  ? 30.987 3.377   -34.616 1.00 41.85  ?  56  ARG A CG  1 
ATOM   3643 C  CD  . ARG C 1 61  ? 30.360 2.793   -35.871 1.00 47.31  ?  56  ARG A CD  1 
ATOM   3644 N  NE  . ARG C 1 61  ? 31.122 1.606   -36.282 1.00 60.71  ?  56  ARG A NE  1 
ATOM   3645 C  CZ  . ARG C 1 61  ? 30.872 0.334   -35.929 1.00 63.61  ?  56  ARG A CZ  1 
ATOM   3646 N  NH1 . ARG C 1 61  ? 31.668 -0.640  -36.354 1.00 57.59  ?  56  ARG A NH1 1 
ATOM   3647 N  NH2 . ARG C 1 61  ? 29.833 0.034   -35.164 1.00 65.79  ?  56  ARG A NH2 1 
ATOM   3648 N  N   . LEU C 1 62  ? 35.398 2.633   -33.220 1.00 24.90  ?  57  LEU A N   1 
ATOM   3649 C  CA  . LEU C 1 62  ? 36.842 2.393   -33.517 1.00 22.48  ?  57  LEU A CA  1 
ATOM   3650 C  C   . LEU C 1 62  ? 37.002 1.872   -34.953 1.00 22.15  ?  57  LEU A C   1 
ATOM   3651 O  O   . LEU C 1 62  ? 38.038 2.186   -35.605 1.00 23.36  ?  57  LEU A O   1 
ATOM   3652 C  CB  . LEU C 1 62  ? 37.434 1.398   -32.511 1.00 22.00  ?  57  LEU A CB  1 
ATOM   3653 C  CG  . LEU C 1 62  ? 37.600 1.916   -31.090 1.00 19.61  ?  57  LEU A CG  1 
ATOM   3654 C  CD1 . LEU C 1 62  ? 37.944 0.780   -30.123 1.00 18.30  ?  57  LEU A CD1 1 
ATOM   3655 C  CD2 . LEU C 1 62  ? 38.675 2.982   -31.063 1.00 19.61  ?  57  LEU A CD2 1 
ATOM   3656 N  N   . VAL C 1 63  ? 36.071 1.070   -35.458 1.00 24.10  ?  58  VAL A N   1 
ATOM   3657 C  CA  . VAL C 1 63  ? 36.315 0.376   -36.758 1.00 24.84  ?  58  VAL A CA  1 
ATOM   3658 C  C   . VAL C 1 63  ? 36.421 1.459   -37.831 1.00 23.22  ?  58  VAL A C   1 
ATOM   3659 O  O   . VAL C 1 63  ? 35.543 2.303   -37.888 1.00 24.11  ?  58  VAL A O   1 
ATOM   3660 C  CB  . VAL C 1 63  ? 35.262 -0.682  -37.122 1.00 25.21  ?  58  VAL A CB  1 
ATOM   3661 C  CG1 . VAL C 1 63  ? 35.420 -1.157  -38.562 1.00 24.81  ?  58  VAL A CG1 1 
ATOM   3662 C  CG2 . VAL C 1 63  ? 35.288 -1.875  -36.177 1.00 26.91  ?  58  VAL A CG2 1 
ATOM   3663 N  N   . GLY C 1 64  ? 37.498 1.460   -38.608 1.00 24.05  ?  59  GLY A N   1 
ATOM   3664 C  CA  . GLY C 1 64  ? 37.667 2.441   -39.688 1.00 28.26  ?  59  GLY A CA  1 
ATOM   3665 C  C   . GLY C 1 64  ? 38.554 3.610   -39.295 1.00 29.76  ?  59  GLY A C   1 
ATOM   3666 O  O   . GLY C 1 64  ? 39.015 4.293   -40.218 1.00 31.18  ?  59  GLY A O   1 
ATOM   3667 N  N   . ILE C 1 65  ? 38.816 3.860   -38.003 1.00 27.04  ?  60  ILE A N   1 
ATOM   3668 C  CA  . ILE C 1 65  ? 39.773 4.949   -37.638 1.00 25.12  ?  60  ILE A CA  1 
ATOM   3669 C  C   . ILE C 1 65  ? 41.196 4.386   -37.634 1.00 22.98  ?  60  ILE A C   1 
ATOM   3670 O  O   . ILE C 1 65  ? 41.384 3.133   -37.596 1.00 23.70  ?  60  ILE A O   1 
ATOM   3671 C  CB  . ILE C 1 65  ? 39.423 5.664   -36.320 1.00 28.00  ?  60  ILE A CB  1 
ATOM   3672 C  CG1 . ILE C 1 65  ? 39.753 4.821   -35.094 1.00 26.91  ?  60  ILE A CG1 1 
ATOM   3673 C  CG2 . ILE C 1 65  ? 37.989 6.171   -36.307 1.00 27.14  ?  60  ILE A CG2 1 
ATOM   3674 C  CD1 . ILE C 1 65  ? 39.411 5.489   -33.790 1.00 31.55  ?  60  ILE A CD1 1 
ATOM   3675 N  N   . THR C 1 66  ? 42.169 5.276   -37.745 1.00 19.90  ?  61  THR A N   1 
ATOM   3676 C  CA  . THR C 1 66  ? 43.610 4.938   -37.690 1.00 21.35  ?  61  THR A CA  1 
ATOM   3677 C  C   . THR C 1 66  ? 44.083 5.284   -36.283 1.00 21.73  ?  61  THR A C   1 
ATOM   3678 O  O   . THR C 1 66  ? 43.776 6.403   -35.799 1.00 21.72  ?  61  THR A O   1 
ATOM   3679 C  CB  . THR C 1 66  ? 44.438 5.633   -38.773 1.00 23.51  ?  61  THR A CB  1 
ATOM   3680 O  OG1 . THR C 1 66  ? 44.007 5.161   -40.048 1.00 27.01  ?  61  THR A OG1 1 
ATOM   3681 C  CG2 . THR C 1 66  ? 45.920 5.357   -38.637 1.00 23.81  ?  61  THR A CG2 1 
ATOM   3682 N  N   . LEU C 1 67  ? 44.771 4.336   -35.655 1.00 20.05  ?  62  LEU A N   1 
ATOM   3683 C  CA  . LEU C 1 67  ? 45.433 4.555   -34.357 1.00 20.52  ?  62  LEU A CA  1 
ATOM   3684 C  C   . LEU C 1 67  ? 46.910 4.854   -34.599 1.00 16.78  ?  62  LEU A C   1 
ATOM   3685 O  O   . LEU C 1 67  ? 47.551 4.340   -35.553 1.00 18.88  ?  62  LEU A O   1 
ATOM   3686 C  CB  . LEU C 1 67  ? 45.201 3.358   -33.415 1.00 18.72  ?  62  LEU A CB  1 
ATOM   3687 C  CG  . LEU C 1 67  ? 43.756 2.943   -33.183 1.00 21.16  ?  62  LEU A CG  1 
ATOM   3688 C  CD1 . LEU C 1 67  ? 43.708 1.709   -32.267 1.00 22.07  ?  62  LEU A CD1 1 
ATOM   3689 C  CD2 . LEU C 1 67  ? 42.898 4.069   -32.613 1.00 20.05  ?  62  LEU A CD2 1 
ATOM   3690 N  N   . TRP C 1 68  ? 47.446 5.710   -33.757 1.00 15.89  ?  63  TRP A N   1 
ATOM   3691 C  CA  . TRP C 1 68  ? 48.877 6.128   -33.831 1.00 16.72  ?  63  TRP A CA  1 
ATOM   3692 C  C   . TRP C 1 68  ? 49.607 5.548   -32.628 1.00 16.09  ?  63  TRP A C   1 
ATOM   3693 O  O   . TRP C 1 68  ? 49.078 5.629   -31.534 1.00 17.03  ?  63  TRP A O   1 
ATOM   3694 C  CB  . TRP C 1 68  ? 48.994 7.646   -33.797 1.00 18.12  ?  63  TRP A CB  1 
ATOM   3695 C  CG  . TRP C 1 68  ? 48.524 8.378   -35.014 1.00 18.76  ?  63  TRP A CG  1 
ATOM   3696 C  CD1 . TRP C 1 68  ? 47.587 8.025   -35.943 1.00 19.81  ?  63  TRP A CD1 1 
ATOM   3697 C  CD2 . TRP C 1 68  ? 48.966 9.698   -35.368 1.00 18.21  ?  63  TRP A CD2 1 
ATOM   3698 N  NE1 . TRP C 1 68  ? 47.445 9.028   -36.871 1.00 19.05  ?  63  TRP A NE1 1 
ATOM   3699 C  CE2 . TRP C 1 68  ? 48.263 10.070  -36.539 1.00 19.54  ?  63  TRP A CE2 1 
ATOM   3700 C  CE3 . TRP C 1 68  ? 49.850 10.605  -34.776 1.00 18.07  ?  63  TRP A CE3 1 
ATOM   3701 C  CZ2 . TRP C 1 68  ? 48.460 11.314  -37.150 1.00 21.02  ?  63  TRP A CZ2 1 
ATOM   3702 C  CZ3 . TRP C 1 68  ? 50.060 11.826  -35.390 1.00 19.85  ?  63  TRP A CZ3 1 
ATOM   3703 C  CH2 . TRP C 1 68  ? 49.384 12.158  -36.568 1.00 21.57  ?  63  TRP A CH2 1 
ATOM   3704 N  N   . GLY C 1 69  ? 50.825 5.049   -32.798 1.00 15.56  ?  64  GLY A N   1 
ATOM   3705 C  CA  . GLY C 1 69  ? 51.543 4.504   -31.639 1.00 15.71  ?  64  GLY A CA  1 
ATOM   3706 C  C   . GLY C 1 69  ? 53.011 4.476   -31.911 1.00 15.37  ?  64  GLY A C   1 
ATOM   3707 O  O   . GLY C 1 69  ? 53.401 4.864   -33.033 1.00 16.25  ?  64  GLY A O   1 
ATOM   3708 N  N   . HIS C 1 70  ? 53.813 4.205   -30.898 1.00 15.51  ?  65  HIS A N   1 
ATOM   3709 C  CA  . HIS C 1 70  ? 55.272 4.024   -31.109 1.00 16.65  ?  65  HIS A CA  1 
ATOM   3710 C  C   . HIS C 1 70  ? 55.782 2.957   -30.143 1.00 17.15  ?  65  HIS A C   1 
ATOM   3711 O  O   . HIS C 1 70  ? 55.064 2.588   -29.170 1.00 16.83  ?  65  HIS A O   1 
ATOM   3712 C  CB  . HIS C 1 70  ? 56.072 5.322   -30.973 1.00 17.26  ?  65  HIS A CB  1 
ATOM   3713 C  CG  . HIS C 1 70  ? 56.242 5.888   -29.596 1.00 15.44  ?  65  HIS A CG  1 
ATOM   3714 N  ND1 . HIS C 1 70  ? 55.281 6.683   -28.990 1.00 16.14  ?  65  HIS A ND1 1 
ATOM   3715 C  CD2 . HIS C 1 70  ? 57.301 5.907   -28.759 1.00 17.05  ?  65  HIS A CD2 1 
ATOM   3716 C  CE1 . HIS C 1 70  ? 55.753 7.121   -27.822 1.00 16.53  ?  65  HIS A CE1 1 
ATOM   3717 N  NE2 . HIS C 1 70  ? 57.000 6.633   -27.632 1.00 13.69  ?  65  HIS A NE2 1 
ATOM   3718 N  N   . MET C 1 71  ? 56.946 2.437   -30.491 1.00 18.26  ?  66  MET A N   1 
ATOM   3719 C  CA  . MET C 1 71  ? 57.741 1.501   -29.696 1.00 19.88  ?  66  MET A CA  1 
ATOM   3720 C  C   . MET C 1 71  ? 59.223 1.794   -29.945 1.00 21.33  ?  66  MET A C   1 
ATOM   3721 O  O   . MET C 1 71  ? 59.544 2.770   -30.668 1.00 19.95  ?  66  MET A O   1 
ATOM   3722 C  CB  . MET C 1 71  ? 57.414 0.048   -30.055 1.00 23.71  ?  66  MET A CB  1 
ATOM   3723 C  CG  . MET C 1 71  ? 58.021 -0.409  -31.355 1.00 24.27  ?  66  MET A CG  1 
ATOM   3724 S  SD  . MET C 1 71  ? 57.886 -2.212  -31.532 1.00 28.82  ?  66  MET A SD  1 
ATOM   3725 C  CE  . MET C 1 71  ? 56.174 -2.217  -32.019 1.00 26.96  ?  66  MET A CE  1 
ATOM   3726 N  N   . ASN C 1 72  ? 60.087 1.076   -29.232 1.00 18.20  ?  67  ASN A N   1 
ATOM   3727 C  CA  . ASN C 1 72  ? 61.560 1.178   -29.373 1.00 19.98  ?  67  ASN A CA  1 
ATOM   3728 C  C   . ASN C 1 72  ? 61.968 0.466   -30.671 1.00 21.39  ?  67  ASN A C   1 
ATOM   3729 O  O   . ASN C 1 72  ? 61.656 -0.710  -30.863 1.00 21.29  ?  67  ASN A O   1 
ATOM   3730 C  CB  . ASN C 1 72  ? 62.242 0.652   -28.108 1.00 19.05  ?  67  ASN A CB  1 
ATOM   3731 C  CG  . ASN C 1 72  ? 63.733 0.869   -28.089 1.00 21.20  ?  67  ASN A CG  1 
ATOM   3732 O  OD1 . ASN C 1 72  ? 64.317 1.255   -29.100 1.00 21.69  ?  67  ASN A OD1 1 
ATOM   3733 N  ND2 . ASN C 1 72  ? 64.333 0.681   -26.929 1.00 20.13  ?  67  ASN A ND2 1 
ATOM   3734 N  N   . ARG C 1 73  ? 62.626 1.179   -31.577 1.00 24.49  ?  68  ARG A N   1 
ATOM   3735 C  CA  . ARG C 1 73  ? 63.102 0.593   -32.856 1.00 28.14  ?  68  ARG A CA  1 
ATOM   3736 C  C   . ARG C 1 73  ? 64.067 -0.550  -32.570 1.00 28.00  ?  68  ARG A C   1 
ATOM   3737 O  O   . ARG C 1 73  ? 64.166 -1.461  -33.431 1.00 30.71  ?  68  ARG A O   1 
ATOM   3738 C  CB  . ARG C 1 73  ? 63.813 1.647   -33.700 1.00 30.91  ?  68  ARG A CB  1 
ATOM   3739 C  CG  . ARG C 1 73  ? 63.109 1.985   -34.987 1.00 30.82  ?  68  ARG A CG  1 
ATOM   3740 C  CD  . ARG C 1 73  ? 63.668 3.274   -35.511 1.00 33.92  ?  68  ARG A CD  1 
ATOM   3741 N  NE  . ARG C 1 73  ? 62.633 3.834   -36.323 1.00 34.98  ?  68  ARG A NE  1 
ATOM   3742 C  CZ  . ARG C 1 73  ? 62.445 3.553   -37.587 1.00 38.40  ?  68  ARG A CZ  1 
ATOM   3743 N  NH1 . ARG C 1 73  ? 63.291 2.741   -38.196 1.00 40.64  ?  68  ARG A NH1 1 
ATOM   3744 N  NH2 . ARG C 1 73  ? 61.438 4.123   -38.237 1.00 35.34  ?  68  ARG A NH2 1 
ATOM   3745 N  N   . ALA C 1 74  ? 64.762 -0.498  -31.428 1.00 27.42  ?  69  ALA A N   1 
ATOM   3746 C  CA  . ALA C 1 74  ? 65.771 -1.503  -31.022 1.00 29.15  ?  69  ALA A CA  1 
ATOM   3747 C  C   . ALA C 1 74  ? 65.080 -2.756  -30.491 1.00 30.32  ?  69  ALA A C   1 
ATOM   3748 O  O   . ALA C 1 74  ? 65.778 -3.750  -30.249 1.00 28.84  ?  69  ALA A O   1 
ATOM   3749 C  CB  . ALA C 1 74  ? 66.703 -0.941  -29.982 1.00 31.99  ?  69  ALA A CB  1 
ATOM   3750 N  N   . ASN C 1 75  ? 63.773 -2.669  -30.209 1.00 26.51  ?  70  ASN A N   1 
ATOM   3751 C  CA  . ASN C 1 75  ? 62.970 -3.825  -29.746 1.00 23.68  ?  70  ASN A CA  1 
ATOM   3752 C  C   . ASN C 1 75  ? 62.947 -4.819  -30.909 1.00 21.26  ?  70  ASN A C   1 
ATOM   3753 O  O   . ASN C 1 75  ? 62.507 -4.476  -32.002 1.00 18.20  ?  70  ASN A O   1 
ATOM   3754 C  CB  . ASN C 1 75  ? 61.585 -3.358  -29.286 1.00 25.48  ?  70  ASN A CB  1 
ATOM   3755 C  CG  . ASN C 1 75  ? 60.745 -4.473  -28.710 1.00 25.54  ?  70  ASN A CG  1 
ATOM   3756 O  OD1 . ASN C 1 75  ? 61.033 -5.647  -28.923 1.00 23.83  ?  70  ASN A OD1 1 
ATOM   3757 N  ND2 . ASN C 1 75  ? 59.709 -4.119  -27.977 1.00 24.18  ?  70  ASN A ND2 1 
ATOM   3758 N  N   . PRO C 1 76  ? 63.392 -6.083  -30.721 1.00 19.94  ?  71  PRO A N   1 
ATOM   3759 C  CA  . PRO C 1 76  ? 63.287 -7.109  -31.768 1.00 20.14  ?  71  PRO A CA  1 
ATOM   3760 C  C   . PRO C 1 76  ? 61.890 -7.243  -32.373 1.00 18.46  ?  71  PRO A C   1 
ATOM   3761 O  O   . PRO C 1 76  ? 61.738 -7.645  -33.490 1.00 17.97  ?  71  PRO A O   1 
ATOM   3762 C  CB  . PRO C 1 76  ? 63.652 -8.428  -31.055 1.00 20.32  ?  71  PRO A CB  1 
ATOM   3763 C  CG  . PRO C 1 76  ? 64.503 -7.990  -29.909 1.00 22.80  ?  71  PRO A CG  1 
ATOM   3764 C  CD  . PRO C 1 76  ? 64.016 -6.605  -29.508 1.00 21.11  ?  71  PRO A CD  1 
ATOM   3765 N  N   . HIS C 1 77  ? 60.858 -6.875  -31.619 1.00 18.17  ?  72  HIS A N   1 
ATOM   3766 C  CA  . HIS C 1 77  ? 59.465 -6.899  -32.130 1.00 16.94  ?  72  HIS A CA  1 
ATOM   3767 C  C   . HIS C 1 77  ? 59.340 -6.019  -33.382 1.00 17.43  ?  72  HIS A C   1 
ATOM   3768 O  O   . HIS C 1 77  ? 58.684 -6.455  -34.380 1.00 18.25  ?  72  HIS A O   1 
ATOM   3769 C  CB  . HIS C 1 77  ? 58.542 -6.501  -30.978 1.00 15.51  ?  72  HIS A CB  1 
ATOM   3770 C  CG  . HIS C 1 77  ? 57.120 -6.780  -31.270 1.00 16.23  ?  72  HIS A CG  1 
ATOM   3771 N  ND1 . HIS C 1 77  ? 56.144 -6.583  -30.316 1.00 15.81  ?  72  HIS A ND1 1 
ATOM   3772 C  CD2 . HIS C 1 77  ? 56.505 -7.258  -32.362 1.00 16.85  ?  72  HIS A CD2 1 
ATOM   3773 C  CE1 . HIS C 1 77  ? 54.985 -6.834  -30.856 1.00 16.96  ?  72  HIS A CE1 1 
ATOM   3774 N  NE2 . HIS C 1 77  ? 55.178 -7.276  -32.078 1.00 16.57  ?  72  HIS A NE2 1 
ATOM   3775 N  N   . TRP C 1 78  ? 60.000 -4.848  -33.366 1.00 18.28  ?  73  TRP A N   1 
ATOM   3776 C  CA  . TRP C 1 78  ? 59.983 -3.897  -34.511 1.00 20.54  ?  73  TRP A CA  1 
ATOM   3777 C  C   . TRP C 1 78  ? 60.390 -4.614  -35.810 1.00 20.04  ?  73  TRP A C   1 
ATOM   3778 O  O   . TRP C 1 78  ? 59.612 -4.573  -36.739 1.00 18.67  ?  73  TRP A O   1 
ATOM   3779 C  CB  . TRP C 1 78  ? 60.859 -2.683  -34.211 1.00 21.04  ?  73  TRP A CB  1 
ATOM   3780 C  CG  . TRP C 1 78  ? 60.900 -1.687  -35.324 1.00 24.93  ?  73  TRP A CG  1 
ATOM   3781 C  CD1 . TRP C 1 78  ? 61.948 -1.462  -36.177 1.00 26.18  ?  73  TRP A CD1 1 
ATOM   3782 C  CD2 . TRP C 1 78  ? 59.858 -0.775  -35.708 1.00 23.66  ?  73  TRP A CD2 1 
ATOM   3783 N  NE1 . TRP C 1 78  ? 61.621 -0.483  -37.071 1.00 26.09  ?  73  TRP A NE1 1 
ATOM   3784 C  CE2 . TRP C 1 78  ? 60.362 -0.024  -36.797 1.00 23.62  ?  73  TRP A CE2 1 
ATOM   3785 C  CE3 . TRP C 1 78  ? 58.570 -0.502  -35.237 1.00 23.28  ?  73  TRP A CE3 1 
ATOM   3786 C  CZ2 . TRP C 1 78  ? 59.622 0.973   -37.413 1.00 24.65  ?  73  TRP A CZ2 1 
ATOM   3787 C  CZ3 . TRP C 1 78  ? 57.849 0.507   -35.833 1.00 24.78  ?  73  TRP A CZ3 1 
ATOM   3788 C  CH2 . TRP C 1 78  ? 58.353 1.210   -36.931 1.00 23.40  ?  73  TRP A CH2 1 
ATOM   3789 N  N   . ALA C 1 79  ? 61.571 -5.254  -35.850 1.00 24.34  ?  74  ALA A N   1 
ATOM   3790 C  CA  . ALA C 1 79  ? 62.070 -6.029  -37.017 1.00 25.38  ?  74  ALA A CA  1 
ATOM   3791 C  C   . ALA C 1 79  ? 61.131 -7.197  -37.314 1.00 26.76  ?  74  ALA A C   1 
ATOM   3792 O  O   . ALA C 1 79  ? 60.898 -7.456  -38.510 1.00 28.33  ?  74  ALA A O   1 
ATOM   3793 C  CB  . ALA C 1 79  ? 63.505 -6.480  -36.786 1.00 26.11  ?  74  ALA A CB  1 
ATOM   3794 N  N   . ALA C 1 80  ? 60.534 -7.825  -36.286 1.00 24.16  ?  75  ALA A N   1 
ATOM   3795 C  CA  . ALA C 1 80  ? 59.658 -9.002  -36.450 1.00 25.47  ?  75  ALA A CA  1 
ATOM   3796 C  C   . ALA C 1 80  ? 58.356 -8.583  -37.135 1.00 23.84  ?  75  ALA A C   1 
ATOM   3797 O  O   . ALA C 1 80  ? 57.722 -9.443  -37.769 1.00 29.92  ?  75  ALA A O   1 
ATOM   3798 C  CB  . ALA C 1 80  ? 59.399 -9.695  -35.124 1.00 25.17  ?  75  ALA A CB  1 
ATOM   3799 N  N   . LEU C 1 81  ? 57.959 -7.323  -37.034 1.00 24.55  ?  76  LEU A N   1 
ATOM   3800 C  CA  . LEU C 1 81  ? 56.669 -6.861  -37.621 1.00 28.45  ?  76  LEU A CA  1 
ATOM   3801 C  C   . LEU C 1 81  ? 56.801 -6.797  -39.150 1.00 35.48  ?  76  LEU A C   1 
ATOM   3802 O  O   . LEU C 1 81  ? 55.776 -6.972  -39.825 1.00 37.78  ?  76  LEU A O   1 
ATOM   3803 C  CB  . LEU C 1 81  ? 56.283 -5.497  -37.040 1.00 28.98  ?  76  LEU A CB  1 
ATOM   3804 C  CG  . LEU C 1 81  ? 55.724 -5.558  -35.615 1.00 24.06  ?  76  LEU A CG  1 
ATOM   3805 C  CD1 . LEU C 1 81  ? 55.830 -4.231  -34.941 1.00 24.14  ?  76  LEU A CD1 1 
ATOM   3806 C  CD2 . LEU C 1 81  ? 54.293 -6.087  -35.597 1.00 26.83  ?  76  LEU A CD2 1 
ATOM   3807 N  N   . GLY C 1 82  ? 58.018 -6.580  -39.654 1.00 35.89  ?  77  GLY A N   1 
ATOM   3808 C  CA  . GLY C 1 82  ? 58.290 -6.418  -41.093 1.00 43.55  ?  77  GLY A CA  1 
ATOM   3809 C  C   . GLY C 1 82  ? 57.380 -5.359  -41.682 1.00 48.23  ?  77  GLY A C   1 
ATOM   3810 O  O   . GLY C 1 82  ? 57.279 -4.269  -41.067 1.00 52.89  ?  77  GLY A O   1 
ATOM   3811 N  N   . GLY C 1 83  ? 56.699 -5.683  -42.787 1.00 49.38  ?  78  GLY A N   1 
ATOM   3812 C  CA  . GLY C 1 83  ? 55.907 -4.727  -43.584 1.00 51.05  ?  78  GLY A CA  1 
ATOM   3813 C  C   . GLY C 1 83  ? 54.491 -4.553  -43.058 1.00 52.90  ?  78  GLY A C   1 
ATOM   3814 O  O   . GLY C 1 83  ? 54.264 -3.609  -42.275 1.00 68.78  ?  78  GLY A O   1 
ATOM   3815 N  N   . ALA C 1 84  ? 53.570 -5.430  -43.465 1.00 52.17  ?  79  ALA A N   1 
ATOM   3816 C  CA  . ALA C 1 84  ? 52.105 -5.277  -43.296 1.00 47.89  ?  79  ALA A CA  1 
ATOM   3817 C  C   . ALA C 1 84  ? 51.570 -6.316  -42.296 1.00 43.66  ?  79  ALA A C   1 
ATOM   3818 O  O   . ALA C 1 84  ? 50.537 -6.983  -42.608 1.00 41.63  ?  79  ALA A O   1 
ATOM   3819 C  CB  . ALA C 1 84  ? 51.440 -5.412  -44.644 1.00 52.15  ?  79  ALA A CB  1 
ATOM   3820 N  N   . ALA C 1 85  ? 52.215 -6.414  -41.130 1.00 34.36  ?  80  ALA A N   1 
ATOM   3821 C  CA  . ALA C 1 85  ? 51.898 -7.391  -40.059 1.00 30.65  ?  80  ALA A CA  1 
ATOM   3822 C  C   . ALA C 1 85  ? 50.445 -7.247  -39.593 1.00 26.87  ?  80  ALA A C   1 
ATOM   3823 O  O   . ALA C 1 85  ? 50.033 -6.111  -39.274 1.00 23.58  ?  80  ALA A O   1 
ATOM   3824 C  CB  . ALA C 1 85  ? 52.832 -7.219  -38.897 1.00 31.64  ?  80  ALA A CB  1 
ATOM   3825 N  N   . ASN C 1 86  ? 49.730 -8.372  -39.493 1.00 23.03  ?  81  ASN A N   1 
ATOM   3826 C  CA  . ASN C 1 86  ? 48.395 -8.410  -38.847 1.00 25.47  ?  81  ASN A CA  1 
ATOM   3827 C  C   . ASN C 1 86  ? 48.605 -8.472  -37.336 1.00 23.90  ?  81  ASN A C   1 
ATOM   3828 O  O   . ASN C 1 86  ? 49.277 -9.406  -36.850 1.00 23.86  ?  81  ASN A O   1 
ATOM   3829 C  CB  . ASN C 1 86  ? 47.545 -9.563  -39.366 1.00 26.83  ?  81  ASN A CB  1 
ATOM   3830 C  CG  . ASN C 1 86  ? 47.183 -9.354  -40.816 1.00 30.12  ?  81  ASN A CG  1 
ATOM   3831 O  OD1 . ASN C 1 86  ? 46.827 -8.239  -41.210 1.00 30.48  ?  81  ASN A OD1 1 
ATOM   3832 N  ND2 . ASN C 1 86  ? 47.293 -10.410 -41.608 1.00 27.85  ?  81  ASN A ND2 1 
ATOM   3833 N  N   . VAL C 1 87  ? 48.083 -7.481  -36.622 1.00 21.23  ?  82  VAL A N   1 
ATOM   3834 C  CA  . VAL C 1 87  ? 48.385 -7.323  -35.175 1.00 19.08  ?  82  VAL A CA  1 
ATOM   3835 C  C   . VAL C 1 87  ? 47.080 -7.218  -34.404 1.00 17.99  ?  82  VAL A C   1 
ATOM   3836 O  O   . VAL C 1 87  ? 45.987 -7.024  -35.004 1.00 16.47  ?  82  VAL A O   1 
ATOM   3837 C  CB  . VAL C 1 87  ? 49.254 -6.103  -34.863 1.00 18.76  ?  82  VAL A CB  1 
ATOM   3838 C  CG1 . VAL C 1 87  ? 50.566 -6.130  -35.594 1.00 21.64  ?  82  VAL A CG1 1 
ATOM   3839 C  CG2 . VAL C 1 87  ? 48.501 -4.798  -35.054 1.00 17.77  ?  82  VAL A CG2 1 
ATOM   3840 N  N   . VAL C 1 88  ? 47.208 -7.369  -33.111 1.00 17.50  ?  83  VAL A N   1 
ATOM   3841 C  CA  . VAL C 1 88  ? 46.096 -7.071  -32.165 1.00 16.94  ?  83  VAL A CA  1 
ATOM   3842 C  C   . VAL C 1 88  ? 46.694 -6.161  -31.111 1.00 16.52  ?  83  VAL A C   1 
ATOM   3843 O  O   . VAL C 1 88  ? 47.838 -6.434  -30.676 1.00 15.88  ?  83  VAL A O   1 
ATOM   3844 C  CB  . VAL C 1 88  ? 45.481 -8.333  -31.557 1.00 18.16  ?  83  VAL A CB  1 
ATOM   3845 C  CG1 . VAL C 1 88  ? 46.540 -9.218  -30.930 1.00 16.18  ?  83  VAL A CG1 1 
ATOM   3846 C  CG2 . VAL C 1 88  ? 44.383 -7.969  -30.557 1.00 17.32  ?  83  VAL A CG2 1 
ATOM   3847 N  N   . ALA C 1 89  ? 45.990 -5.092  -30.759 1.00 17.30  ?  84  ALA A N   1 
ATOM   3848 C  CA  . ALA C 1 89  ? 46.374 -4.218  -29.634 1.00 16.19  ?  84  ALA A CA  1 
ATOM   3849 C  C   . ALA C 1 89  ? 45.237 -4.286  -28.624 1.00 16.47  ?  84  ALA A C   1 
ATOM   3850 O  O   . ALA C 1 89  ? 44.033 -4.176  -29.054 1.00 16.05  ?  84  ALA A O   1 
ATOM   3851 C  CB  . ALA C 1 89  ? 46.688 -2.825  -30.112 1.00 16.46  ?  84  ALA A CB  1 
ATOM   3852 N  N   . THR C 1 90  ? 45.573 -4.721  -27.417 1.00 15.79  ?  85  THR A N   1 
ATOM   3853 C  CA  . THR C 1 90  ? 44.609 -4.981  -26.335 1.00 15.35  ?  85  THR A CA  1 
ATOM   3854 C  C   . THR C 1 90  ? 44.777 -3.860  -25.314 1.00 15.97  ?  85  THR A C   1 
ATOM   3855 O  O   . THR C 1 90  ? 45.934 -3.566  -24.851 1.00 12.11  ?  85  THR A O   1 
ATOM   3856 C  CB  . THR C 1 90  ? 44.794 -6.376  -25.723 1.00 15.15  ?  85  THR A CB  1 
ATOM   3857 O  OG1 . THR C 1 90  ? 44.709 -7.332  -26.795 1.00 16.29  ?  85  THR A OG1 1 
ATOM   3858 C  CG2 . THR C 1 90  ? 43.800 -6.638  -24.604 1.00 15.68  ?  85  THR A CG2 1 
ATOM   3859 N  N   . PHE C 1 91  ? 43.659 -3.237  -24.977 1.00 14.03  ?  86  PHE A N   1 
ATOM   3860 C  CA  . PHE C 1 91  ? 43.571 -2.116  -24.031 1.00 14.90  ?  86  PHE A CA  1 
ATOM   3861 C  C   . PHE C 1 91  ? 42.800 -2.628  -22.828 1.00 15.07  ?  86  PHE A C   1 
ATOM   3862 O  O   . PHE C 1 91  ? 41.756 -3.253  -23.081 1.00 17.37  ?  86  PHE A O   1 
ATOM   3863 C  CB  . PHE C 1 91  ? 42.888 -0.911  -24.649 1.00 14.46  ?  86  PHE A CB  1 
ATOM   3864 C  CG  . PHE C 1 91  ? 43.547 -0.359  -25.872 1.00 15.16  ?  86  PHE A CG  1 
ATOM   3865 C  CD1 . PHE C 1 91  ? 43.409 -1.013  -27.080 1.00 16.44  ?  86  PHE A CD1 1 
ATOM   3866 C  CD2 . PHE C 1 91  ? 44.255 0.840   -25.818 1.00 13.24  ?  86  PHE A CD2 1 
ATOM   3867 C  CE1 . PHE C 1 91  ? 43.974 -0.498  -28.218 1.00 15.84  ?  86  PHE A CE1 1 
ATOM   3868 C  CE2 . PHE C 1 91  ? 44.794 1.367   -26.969 1.00 13.80  ?  86  PHE A CE2 1 
ATOM   3869 C  CZ  . PHE C 1 91  ? 44.677 0.687   -28.157 1.00 15.27  ?  86  PHE A CZ  1 
ATOM   3870 N  N   . ALA C 1 92  ? 43.387 -2.567  -21.633 1.00 13.54  ?  87  ALA A N   1 
ATOM   3871 C  CA  . ALA C 1 92  ? 42.829 -3.153  -20.384 1.00 16.01  ?  87  ALA A CA  1 
ATOM   3872 C  C   . ALA C 1 92  ? 42.334 -2.045  -19.460 1.00 16.90  ?  87  ALA A C   1 
ATOM   3873 O  O   . ALA C 1 92  ? 43.165 -1.191  -19.035 1.00 20.97  ?  87  ALA A O   1 
ATOM   3874 C  CB  . ALA C 1 92  ? 43.836 -4.068  -19.682 1.00 16.07  ?  87  ALA A CB  1 
ATOM   3875 N  N   . GLY C 1 93  ? 41.026 -2.023  -19.176 1.00 15.32  ?  88  GLY A N   1 
ATOM   3876 C  CA  . GLY C 1 93  ? 40.466 -0.974  -18.297 1.00 16.51  ?  88  GLY A CA  1 
ATOM   3877 C  C   . GLY C 1 93  ? 40.274 -1.368  -16.819 1.00 16.08  ?  88  GLY A C   1 
ATOM   3878 O  O   . GLY C 1 93  ? 40.874 -2.301  -16.293 1.00 16.35  ?  88  GLY A O   1 
ATOM   3879 N  N   . PRO C 1 94  ? 39.326 -0.702  -16.122 1.00 16.98  ?  89  PRO A N   1 
ATOM   3880 C  CA  . PRO C 1 94  ? 38.985 -1.038  -14.740 1.00 17.48  ?  89  PRO A CA  1 
ATOM   3881 C  C   . PRO C 1 94  ? 38.634 -2.513  -14.587 1.00 15.56  ?  89  PRO A C   1 
ATOM   3882 O  O   . PRO C 1 94  ? 38.031 -3.066  -15.486 1.00 15.55  ?  89  PRO A O   1 
ATOM   3883 C  CB  . PRO C 1 94  ? 37.730 -0.207  -14.472 1.00 17.45  ?  89  PRO A CB  1 
ATOM   3884 C  CG  . PRO C 1 94  ? 37.909 0.984   -15.393 1.00 16.61  ?  89  PRO A CG  1 
ATOM   3885 C  CD  . PRO C 1 94  ? 38.476 0.370   -16.657 1.00 17.49  ?  89  PRO A CD  1 
ATOM   3886 N  N   . ASN C 1 95  ? 38.987 -3.089  -13.441 1.00 15.83  ?  90  ASN A N   1 
ATOM   3887 C  CA  . ASN C 1 95  ? 38.745 -4.520  -13.189 1.00 15.97  ?  90  ASN A CA  1 
ATOM   3888 C  C   . ASN C 1 95  ? 38.738 -4.713  -11.692 1.00 15.23  ?  90  ASN A C   1 
ATOM   3889 O  O   . ASN C 1 95  ? 39.503 -3.971  -11.022 1.00 16.39  ?  90  ASN A O   1 
ATOM   3890 C  CB  . ASN C 1 95  ? 39.798 -5.388  -13.903 1.00 14.99  ?  90  ASN A CB  1 
ATOM   3891 C  CG  . ASN C 1 95  ? 41.202 -5.221  -13.337 1.00 15.79  ?  90  ASN A CG  1 
ATOM   3892 O  OD1 . ASN C 1 95  ? 41.605 -5.955  -12.436 1.00 15.52  ?  90  ASN A OD1 1 
ATOM   3893 N  ND2 . ASN C 1 95  ? 41.948 -4.297  -13.890 1.00 14.27  ?  90  ASN A ND2 1 
ATOM   3894 N  N   . ALA C 1 96  ? 38.040 -5.723  -11.188 1.00 13.93  ?  91  ALA A N   1 
ATOM   3895 C  CA  . ALA C 1 96  ? 38.117 -6.107  -9.760  1.00 13.18  ?  91  ALA A CA  1 
ATOM   3896 C  C   . ALA C 1 96  ? 37.634 -7.536  -9.568  1.00 13.34  ?  91  ALA A C   1 
ATOM   3897 O  O   . ALA C 1 96  ? 36.636 -7.975  -10.239 1.00 14.17  ?  91  ALA A O   1 
ATOM   3898 C  CB  . ALA C 1 96  ? 37.317 -5.166  -8.935  1.00 14.57  ?  91  ALA A CB  1 
ATOM   3899 N  N   . TYR C 1 97  ? 38.311 -8.244  -8.677  1.00 14.87  ?  92  TYR A N   1 
ATOM   3900 C  CA  . TYR C 1 97  ? 37.893 -9.592  -8.235  1.00 14.34  ?  92  TYR A CA  1 
ATOM   3901 C  C   . TYR C 1 97  ? 36.545 -9.478  -7.533  1.00 14.33  ?  92  TYR A C   1 
ATOM   3902 O  O   . TYR C 1 97  ? 36.352 -8.537  -6.741  1.00 12.80  ?  92  TYR A O   1 
ATOM   3903 C  CB  . TYR C 1 97  ? 38.934 -10.201 -7.319  1.00 14.79  ?  92  TYR A CB  1 
ATOM   3904 C  CG  . TYR C 1 97  ? 38.518 -11.517 -6.724  1.00 15.54  ?  92  TYR A CG  1 
ATOM   3905 C  CD1 . TYR C 1 97  ? 38.688 -12.693 -7.448  1.00 15.00  ?  92  TYR A CD1 1 
ATOM   3906 C  CD2 . TYR C 1 97  ? 38.058 -11.606 -5.416  1.00 14.82  ?  92  TYR A CD2 1 
ATOM   3907 C  CE1 . TYR C 1 97  ? 38.370 -13.925 -6.914  1.00 15.56  ?  92  TYR A CE1 1 
ATOM   3908 C  CE2 . TYR C 1 97  ? 37.787 -12.850 -4.853  1.00 16.04  ?  92  TYR A CE2 1 
ATOM   3909 C  CZ  . TYR C 1 97  ? 37.906 -14.019 -5.615  1.00 16.21  ?  92  TYR A CZ  1 
ATOM   3910 O  OH  . TYR C 1 97  ? 37.608 -15.272 -5.136  1.00 17.45  ?  92  TYR A OH  1 
ATOM   3911 N  N   . VAL C 1 98  ? 35.671 -10.442 -7.790  1.00 14.73  ?  93  VAL A N   1 
ATOM   3912 C  CA  . VAL C 1 98  ? 34.307 -10.555 -7.194  1.00 15.40  ?  93  VAL A CA  1 
ATOM   3913 C  C   . VAL C 1 98  ? 34.227 -11.794 -6.297  1.00 14.24  ?  93  VAL A C   1 
ATOM   3914 O  O   . VAL C 1 98  ? 34.187 -12.956 -6.815  1.00 12.90  ?  93  VAL A O   1 
ATOM   3915 C  CB  . VAL C 1 98  ? 33.220 -10.657 -8.262  1.00 15.38  ?  93  VAL A CB  1 
ATOM   3916 C  CG1 . VAL C 1 98  ? 31.874 -10.732 -7.561  1.00 15.77  ?  93  VAL A CG1 1 
ATOM   3917 C  CG2 . VAL C 1 98  ? 33.277 -9.527  -9.268  1.00 15.16  ?  93  VAL A CG2 1 
ATOM   3918 N  N   . SER C 1 99  ? 34.245 -11.549 -4.987  1.00 15.45  ?  94  SER A N   1 
ATOM   3919 C  CA  . SER C 1 99  ? 34.036 -12.562 -3.930  1.00 15.18  ?  94  SER A CA  1 
ATOM   3920 C  C   . SER C 1 99  ? 32.552 -12.903 -3.890  1.00 17.08  ?  94  SER A C   1 
ATOM   3921 O  O   . SER C 1 99  ? 31.770 -11.977 -3.811  1.00 16.53  ?  94  SER A O   1 
ATOM   3922 C  CB  . SER C 1 99  ? 34.458 -12.050 -2.568  1.00 14.32  ?  94  SER A CB  1 
ATOM   3923 O  OG  . SER C 1 99  ? 34.272 -13.099 -1.634  1.00 16.43  ?  94  SER A OG  1 
ATOM   3924 N  N   . PRO C 1 100 ? 32.121 -14.185 -3.837  1.00 18.73  ?  95  PRO A N   1 
ATOM   3925 C  CA  . PRO C 1 100 ? 30.706 -14.500 -3.587  1.00 17.02  ?  95  PRO A CA  1 
ATOM   3926 C  C   . PRO C 1 100 ? 30.168 -14.057 -2.208  1.00 19.43  ?  95  PRO A C   1 
ATOM   3927 O  O   . PRO C 1 100 ? 28.957 -13.907 -2.079  1.00 19.22  ?  95  PRO A O   1 
ATOM   3928 C  CB  . PRO C 1 100 ? 30.653 -16.019 -3.703  1.00 16.87  ?  95  PRO A CB  1 
ATOM   3929 C  CG  . PRO C 1 100 ? 31.856 -16.380 -4.539  1.00 17.12  ?  95  PRO A CG  1 
ATOM   3930 C  CD  . PRO C 1 100 ? 32.922 -15.408 -4.070  1.00 18.79  ?  95  PRO A CD  1 
ATOM   3931 N  N   . ALA C 1 101 ? 31.043 -13.709 -1.266  1.00 19.60  ?  96  ALA A N   1 
ATOM   3932 C  CA  . ALA C 1 101 ? 30.700 -12.974 -0.026  1.00 21.03  ?  96  ALA A CA  1 
ATOM   3933 C  C   . ALA C 1 101 ? 29.869 -11.728 -0.351  1.00 20.83  ?  96  ALA A C   1 
ATOM   3934 O  O   . ALA C 1 101 ? 28.968 -11.396 0.437   1.00 25.00  ?  96  ALA A O   1 
ATOM   3935 C  CB  . ALA C 1 101 ? 31.975 -12.585 0.704   1.00 20.96  ?  96  ALA A CB  1 
ATOM   3936 N  N   . VAL C 1 102 ? 30.155 -11.038 -1.447  1.00 17.58  ?  97  VAL A N   1 
ATOM   3937 C  CA  . VAL C 1 102 ? 29.495 -9.767  -1.826  1.00 18.47  ?  97  VAL A CA  1 
ATOM   3938 C  C   . VAL C 1 102 ? 28.101 -10.148 -2.311  1.00 20.74  ?  97  VAL A C   1 
ATOM   3939 O  O   . VAL C 1 102 ? 27.133 -9.434  -2.000  1.00 21.19  ?  97  VAL A O   1 
ATOM   3940 C  CB  . VAL C 1 102 ? 30.319 -9.023  -2.900  1.00 20.17  ?  97  VAL A CB  1 
ATOM   3941 C  CG1 . VAL C 1 102 ? 29.544 -7.899  -3.559  1.00 21.28  ?  97  VAL A CG1 1 
ATOM   3942 C  CG2 . VAL C 1 102 ? 31.639 -8.518  -2.346  1.00 20.71  ?  97  VAL A CG2 1 
ATOM   3943 N  N   . TYR C 1 103 ? 27.955 -11.275 -3.016  1.00 21.16  ?  98  TYR A N   1 
ATOM   3944 C  CA  . TYR C 1 103 ? 26.620 -11.709 -3.524  1.00 20.04  ?  98  TYR A CA  1 
ATOM   3945 C  C   . TYR C 1 103 ? 25.666 -11.983 -2.355  1.00 22.00  ?  98  TYR A C   1 
ATOM   3946 O  O   . TYR C 1 103 ? 24.448 -11.717 -2.505  1.00 22.54  ?  98  TYR A O   1 
ATOM   3947 C  CB  . TYR C 1 103 ? 26.686 -12.983 -4.378  1.00 20.83  ?  98  TYR A CB  1 
ATOM   3948 C  CG  . TYR C 1 103 ? 27.552 -12.949 -5.607  1.00 20.80  ?  98  TYR A CG  1 
ATOM   3949 C  CD1 . TYR C 1 103 ? 27.763 -11.797 -6.339  1.00 21.34  ?  98  TYR A CD1 1 
ATOM   3950 C  CD2 . TYR C 1 103 ? 28.052 -14.140 -6.132  1.00 23.53  ?  98  TYR A CD2 1 
ATOM   3951 C  CE1 . TYR C 1 103 ? 28.527 -11.815 -7.497  1.00 21.43  ?  98  TYR A CE1 1 
ATOM   3952 C  CE2 . TYR C 1 103 ? 28.827 -14.167 -7.276  1.00 24.01  ?  98  TYR A CE2 1 
ATOM   3953 C  CZ  . TYR C 1 103 ? 29.057 -13.005 -7.972  1.00 21.37  ?  98  TYR A CZ  1 
ATOM   3954 O  OH  . TYR C 1 103 ? 29.789 -13.058 -9.125  1.00 19.67  ?  98  TYR A OH  1 
ATOM   3955 N  N   . ARG C 1 104 ? 26.169 -12.634 -1.299  1.00 25.00  ?  99  ARG A N   1 
ATOM   3956 C  CA  . ARG C 1 104 ? 25.388 -13.135 -0.134  1.00 27.15  ?  99  ARG A CA  1 
ATOM   3957 C  C   . ARG C 1 104 ? 24.385 -14.206 -0.582  1.00 29.76  ?  99  ARG A C   1 
ATOM   3958 O  O   . ARG C 1 104 ? 23.302 -14.318 0.052   1.00 35.41  ?  99  ARG A O   1 
ATOM   3959 C  CB  . ARG C 1 104 ? 24.654 -11.986 0.578   1.00 28.14  ?  99  ARG A CB  1 
ATOM   3960 C  CG  . ARG C 1 104 ? 25.517 -10.753 0.780   1.00 25.82  ?  99  ARG A CG  1 
ATOM   3961 C  CD  . ARG C 1 104 ? 25.041 -9.903  1.935   1.00 27.09  ?  99  ARG A CD  1 
ATOM   3962 N  NE  . ARG C 1 104 ? 23.658 -9.422  1.844   1.00 28.09  ?  99  ARG A NE  1 
ATOM   3963 C  CZ  . ARG C 1 104 ? 23.267 -8.273  1.293   1.00 28.95  ?  99  ARG A CZ  1 
ATOM   3964 N  NH1 . ARG C 1 104 ? 24.133 -7.483  0.684   1.00 28.80  ?  99  ARG A NH1 1 
ATOM   3965 N  NH2 . ARG C 1 104 ? 21.985 -7.930  1.323   1.00 31.65  ?  99  ARG A NH2 1 
ATOM   3966 N  N   . THR C 1 105 ? 24.717 -14.972 -1.616  1.00 26.02  ?  100 THR A N   1 
ATOM   3967 C  CA  . THR C 1 105 ? 23.864 -16.050 -2.173  1.00 29.56  ?  100 THR A CA  1 
ATOM   3968 C  C   . THR C 1 105 ? 24.685 -17.333 -2.161  1.00 28.31  ?  100 THR A C   1 
ATOM   3969 O  O   . THR C 1 105 ? 25.914 -17.246 -2.019  1.00 25.83  ?  100 THR A O   1 
ATOM   3970 C  CB  . THR C 1 105 ? 23.368 -15.705 -3.582  1.00 30.02  ?  100 THR A CB  1 
ATOM   3971 O  OG1 . THR C 1 105 ? 24.500 -15.602 -4.439  1.00 31.57  ?  100 THR A OG1 1 
ATOM   3972 C  CG2 . THR C 1 105 ? 22.599 -14.409 -3.649  1.00 33.38  ?  100 THR A CG2 1 
ATOM   3973 N  N   . ALA C 1 106 ? 24.013 -18.467 -2.298  1.00 28.22  ?  101 ALA A N   1 
ATOM   3974 C  CA  . ALA C 1 106 ? 24.616 -19.816 -2.335  1.00 29.52  ?  101 ALA A CA  1 
ATOM   3975 C  C   . ALA C 1 106 ? 23.742 -20.686 -3.229  1.00 28.63  ?  101 ALA A C   1 
ATOM   3976 O  O   . ALA C 1 106 ? 22.524 -20.544 -3.208  1.00 25.49  ?  101 ALA A O   1 
ATOM   3977 C  CB  . ALA C 1 106 ? 24.737 -20.398 -0.944  1.00 28.99  ?  101 ALA A CB  1 
ATOM   3978 N  N   . PRO C 1 107 ? 24.322 -21.525 -4.117  1.00 27.84  ?  102 PRO A N   1 
ATOM   3979 C  CA  . PRO C 1 107 ? 25.768 -21.640 -4.281  1.00 24.49  ?  102 PRO A CA  1 
ATOM   3980 C  C   . PRO C 1 107 ? 26.265 -20.526 -5.222  1.00 22.31  ?  102 PRO A C   1 
ATOM   3981 O  O   . PRO C 1 107 ? 25.477 -19.768 -5.775  1.00 23.92  ?  102 PRO A O   1 
ATOM   3982 C  CB  . PRO C 1 107 ? 25.875 -23.069 -4.858  1.00 24.96  ?  102 PRO A CB  1 
ATOM   3983 C  CG  . PRO C 1 107 ? 24.685 -23.156 -5.777  1.00 29.77  ?  102 PRO A CG  1 
ATOM   3984 C  CD  . PRO C 1 107 ? 23.594 -22.332 -5.109  1.00 29.33  ?  102 PRO A CD  1 
ATOM   3985 N  N   . ALA C 1 108 ? 27.574 -20.410 -5.418  1.00 20.60  ?  103 ALA A N   1 
ATOM   3986 C  CA  . ALA C 1 108 ? 28.134 -19.367 -6.305  1.00 20.95  ?  103 ALA A CA  1 
ATOM   3987 C  C   . ALA C 1 108 ? 29.550 -19.775 -6.671  1.00 19.08  ?  103 ALA A C   1 
ATOM   3988 O  O   . ALA C 1 108 ? 30.025 -20.734 -6.083  1.00 19.31  ?  103 ALA A O   1 
ATOM   3989 C  CB  . ALA C 1 108 ? 28.147 -18.011 -5.611  1.00 22.72  ?  103 ALA A CB  1 
ATOM   3990 N  N   . ALA C 1 109 ? 30.150 -19.044 -7.598  1.00 20.27  ?  104 ALA A N   1 
ATOM   3991 C  CA  . ALA C 1 109 ? 31.587 -19.130 -7.925  1.00 20.74  ?  104 ALA A CA  1 
ATOM   3992 C  C   . ALA C 1 109 ? 32.125 -17.704 -7.954  1.00 19.26  ?  104 ALA A C   1 
ATOM   3993 O  O   . ALA C 1 109 ? 31.394 -16.770 -8.289  1.00 20.84  ?  104 ALA A O   1 
ATOM   3994 C  CB  . ALA C 1 109 ? 31.778 -19.845 -9.243  1.00 19.52  ?  104 ALA A CB  1 
ATOM   3995 N  N   . PRO C 1 110 ? 33.400 -17.476 -7.572  1.00 17.39  ?  105 PRO A N   1 
ATOM   3996 C  CA  . PRO C 1 110 ? 33.981 -16.152 -7.690  1.00 16.21  ?  105 PRO A CA  1 
ATOM   3997 C  C   . PRO C 1 110 ? 34.111 -15.859 -9.188  1.00 15.69  ?  105 PRO A C   1 
ATOM   3998 O  O   . PRO C 1 110 ? 33.985 -16.788 -10.028 1.00 18.49  ?  105 PRO A O   1 
ATOM   3999 C  CB  . PRO C 1 110 ? 35.346 -16.267 -6.993  1.00 15.59  ?  105 PRO A CB  1 
ATOM   4000 C  CG  . PRO C 1 110 ? 35.249 -17.549 -6.193  1.00 16.89  ?  105 PRO A CG  1 
ATOM   4001 C  CD  . PRO C 1 110 ? 34.337 -18.443 -7.001  1.00 17.75  ?  105 PRO A CD  1 
ATOM   4002 N  N   . THR C 1 111 ? 34.402 -14.607 -9.543  1.00 16.69  ?  106 THR A N   1 
ATOM   4003 C  CA  . THR C 1 111 ? 34.730 -14.237 -10.928 1.00 16.11  ?  106 THR A CA  1 
ATOM   4004 C  C   . THR C 1 111 ? 35.668 -13.032 -10.855 1.00 15.90  ?  106 THR A C   1 
ATOM   4005 O  O   . THR C 1 111 ? 35.983 -12.555 -9.718  1.00 14.91  ?  106 THR A O   1 
ATOM   4006 C  CB  . THR C 1 111 ? 33.468 -14.032 -11.796 1.00 18.73  ?  106 THR A CB  1 
ATOM   4007 O  OG1 . THR C 1 111 ? 33.930 -14.136 -13.144 1.00 18.60  ?  106 THR A OG1 1 
ATOM   4008 C  CG2 . THR C 1 111 ? 32.788 -12.696 -11.585 1.00 17.73  ?  106 THR A CG2 1 
ATOM   4009 N  N   . TRP C 1 112 ? 36.050 -12.513 -12.006 1.00 15.32  ?  107 TRP A N   1 
ATOM   4010 C  CA  . TRP C 1 112 ? 36.802 -11.233 -12.060 1.00 14.72  ?  107 TRP A CA  1 
ATOM   4011 C  C   . TRP C 1 112 ? 36.044 -10.305 -13.000 1.00 16.35  ?  107 TRP A C   1 
ATOM   4012 O  O   . TRP C 1 112 ? 35.873 -10.708 -14.178 1.00 17.22  ?  107 TRP A O   1 
ATOM   4013 C  CB  . TRP C 1 112 ? 38.229 -11.507 -12.542 1.00 15.26  ?  107 TRP A CB  1 
ATOM   4014 C  CG  . TRP C 1 112 ? 39.200 -10.486 -12.039 1.00 13.58  ?  107 TRP A CG  1 
ATOM   4015 C  CD1 . TRP C 1 112 ? 39.246 -9.177  -12.400 1.00 14.10  ?  107 TRP A CD1 1 
ATOM   4016 C  CD2 . TRP C 1 112 ? 40.237 -10.672 -11.062 1.00 13.09  ?  107 TRP A CD2 1 
ATOM   4017 N  NE1 . TRP C 1 112 ? 40.259 -8.534  -11.743 1.00 13.31  ?  107 TRP A NE1 1 
ATOM   4018 C  CE2 . TRP C 1 112 ? 40.875 -9.419  -10.905 1.00 14.31  ?  107 TRP A CE2 1 
ATOM   4019 C  CE3 . TRP C 1 112 ? 40.747 -11.772 -10.377 1.00 14.52  ?  107 TRP A CE3 1 
ATOM   4020 C  CZ2 . TRP C 1 112 ? 41.931 -9.234  -10.039 1.00 14.76  ?  107 TRP A CZ2 1 
ATOM   4021 C  CZ3 . TRP C 1 112 ? 41.762 -11.578 -9.489  1.00 14.37  ?  107 TRP A CZ3 1 
ATOM   4022 C  CH2 . TRP C 1 112 ? 42.333 -10.320 -9.304  1.00 16.01  ?  107 TRP A CH2 1 
ATOM   4023 N  N   . ASN C 1 113 ? 35.512 -9.181  -12.508 1.00 12.26  ?  108 ASN A N   1 
ATOM   4024 C  CA  . ASN C 1 113 ? 34.922 -8.211  -13.407 1.00 11.76  ?  108 ASN A CA  1 
ATOM   4025 C  C   . ASN C 1 113 ? 36.058 -7.488  -14.089 1.00 8.20   ?  108 ASN A C   1 
ATOM   4026 O  O   . ASN C 1 113 ? 36.966 -6.915  -13.375 1.00 13.33  ?  108 ASN A O   1 
ATOM   4027 C  CB  . ASN C 1 113 ? 33.989 -7.248  -12.705 1.00 12.86  ?  108 ASN A CB  1 
ATOM   4028 C  CG  . ASN C 1 113 ? 32.632 -7.868  -12.474 1.00 14.44  ?  108 ASN A CG  1 
ATOM   4029 O  OD1 . ASN C 1 113 ? 32.421 -9.032  -12.798 1.00 17.11  ?  108 ASN A OD1 1 
ATOM   4030 N  ND2 . ASN C 1 113 ? 31.713 -7.106  -11.914 1.00 16.55  ?  108 ASN A ND2 1 
ATOM   4031 N  N   . PHE C 1 114 ? 35.956 -7.291  -15.311 1.00 9.48   ?  109 PHE A N   1 
ATOM   4032 C  CA  . PHE C 1 114 ? 36.975 -6.578  -16.105 1.00 11.46  ?  109 PHE A CA  1 
ATOM   4033 C  C   . PHE C 1 114 ? 36.422 -6.003  -17.391 1.00 13.77  ?  109 PHE A C   1 
ATOM   4034 O  O   . PHE C 1 114 ? 35.406 -6.471  -17.893 1.00 15.33  ?  109 PHE A O   1 
ATOM   4035 C  CB  . PHE C 1 114 ? 38.219 -7.468  -16.361 1.00 12.45  ?  109 PHE A CB  1 
ATOM   4036 C  CG  . PHE C 1 114 ? 38.128 -8.519  -17.470 1.00 13.82  ?  109 PHE A CG  1 
ATOM   4037 C  CD1 . PHE C 1 114 ? 37.515 -9.744  -17.252 1.00 15.69  ?  109 PHE A CD1 1 
ATOM   4038 C  CD2 . PHE C 1 114 ? 38.555 -8.244  -18.770 1.00 15.40  ?  109 PHE A CD2 1 
ATOM   4039 C  CE1 . PHE C 1 114 ? 37.410 -10.695 -18.272 1.00 15.82  ?  109 PHE A CE1 1 
ATOM   4040 C  CE2 . PHE C 1 114 ? 38.491 -9.209  -19.774 1.00 16.95  ?  109 PHE A CE2 1 
ATOM   4041 C  CZ  . PHE C 1 114 ? 37.855 -10.408 -19.549 1.00 15.51  ?  109 PHE A CZ  1 
ATOM   4042 N  N   . THR C 1 115 ? 37.237 -5.110  -17.961 1.00 15.09  ?  110 THR A N   1 
ATOM   4043 C  CA  . THR C 1 115 ? 37.000 -4.442  -19.266 1.00 14.71  ?  110 THR A CA  1 
ATOM   4044 C  C   . THR C 1 115 ? 38.208 -4.615  -20.184 1.00 16.18  ?  110 THR A C   1 
ATOM   4045 O  O   . THR C 1 115 ? 39.368 -4.409  -19.723 1.00 15.97  ?  110 THR A O   1 
ATOM   4046 C  CB  . THR C 1 115 ? 36.690 -2.979  -18.987 1.00 16.16  ?  110 THR A CB  1 
ATOM   4047 O  OG1 . THR C 1 115 ? 37.797 -2.477  -18.247 1.00 17.35  ?  110 THR A OG1 1 
ATOM   4048 C  CG2 . THR C 1 115 ? 35.409 -2.816  -18.209 1.00 16.32  ?  110 THR A CG2 1 
ATOM   4049 N  N   . SER C 1 116 ? 37.965 -4.941  -21.458 1.00 16.69  ?  111 SER A N   1 
ATOM   4050 C  CA  . SER C 1 116 ? 39.085 -5.112  -22.416 1.00 18.06  ?  111 SER A CA  1 
ATOM   4051 C  C   . SER C 1 116 ? 38.589 -4.650  -23.786 1.00 16.87  ?  111 SER A C   1 
ATOM   4052 O  O   . SER C 1 116 ? 37.443 -4.915  -24.099 1.00 15.05  ?  111 SER A O   1 
ATOM   4053 C  CB  . SER C 1 116 ? 39.517 -6.572  -22.446 1.00 20.87  ?  111 SER A CB  1 
ATOM   4054 O  OG  . SER C 1 116 ? 40.375 -6.791  -23.533 1.00 30.28  ?  111 SER A OG  1 
ATOM   4055 N  N   . VAL C 1 117 ? 39.432 -3.992  -24.547 1.00 15.50  ?  112 VAL A N   1 
ATOM   4056 C  CA  . VAL C 1 117 ? 39.182 -3.729  -25.990 1.00 14.75  ?  112 VAL A CA  1 
ATOM   4057 C  C   . VAL C 1 117 ? 40.341 -4.323  -26.772 1.00 14.06  ?  112 VAL A C   1 
ATOM   4058 O  O   . VAL C 1 117 ? 41.480 -4.064  -26.382 1.00 14.36  ?  112 VAL A O   1 
ATOM   4059 C  CB  . VAL C 1 117 ? 39.028 -2.217  -26.195 1.00 13.85  ?  112 VAL A CB  1 
ATOM   4060 C  CG1 . VAL C 1 117 ? 39.074 -1.823  -27.635 1.00 14.05  ?  112 VAL A CG1 1 
ATOM   4061 C  CG2 . VAL C 1 117 ? 37.752 -1.731  -25.499 1.00 14.52  ?  112 VAL A CG2 1 
ATOM   4062 N  N   . GLN C 1 118 ? 40.023 -5.123  -27.783 1.00 14.83  ?  113 GLN A N   1 
ATOM   4063 C  CA  . GLN C 1 118 ? 40.988 -5.743  -28.717 1.00 15.23  ?  113 GLN A CA  1 
ATOM   4064 C  C   . GLN C 1 118 ? 40.721 -5.170  -30.113 1.00 16.01  ?  113 GLN A C   1 
ATOM   4065 O  O   . GLN C 1 118 ? 39.604 -5.342  -30.676 1.00 16.94  ?  113 GLN A O   1 
ATOM   4066 C  CB  . GLN C 1 118 ? 40.833 -7.256  -28.705 1.00 16.57  ?  113 GLN A CB  1 
ATOM   4067 C  CG  . GLN C 1 118 ? 41.336 -7.853  -27.404 1.00 17.00  ?  113 GLN A CG  1 
ATOM   4068 C  CD  . GLN C 1 118 ? 41.187 -9.345  -27.474 1.00 18.78  ?  113 GLN A CD  1 
ATOM   4069 O  OE1 . GLN C 1 118 ? 41.189 -9.917  -28.546 1.00 17.83  ?  113 GLN A OE1 1 
ATOM   4070 N  NE2 . GLN C 1 118 ? 41.155 -9.988  -26.320 1.00 19.91  ?  113 GLN A NE2 1 
ATOM   4071 N  N   . VAL C 1 119 ? 41.659 -4.396  -30.613 1.00 18.04  ?  114 VAL A N   1 
ATOM   4072 C  CA  . VAL C 1 119 ? 41.592 -3.934  -32.028 1.00 18.45  ?  114 VAL A CA  1 
ATOM   4073 C  C   . VAL C 1 119 ? 42.557 -4.763  -32.855 1.00 17.62  ?  114 VAL A C   1 
ATOM   4074 O  O   . VAL C 1 119 ? 43.671 -5.073  -32.403 1.00 17.39  ?  114 VAL A O   1 
ATOM   4075 C  CB  . VAL C 1 119 ? 41.792 -2.422  -32.207 1.00 18.52  ?  114 VAL A CB  1 
ATOM   4076 C  CG1 . VAL C 1 119 ? 40.706 -1.659  -31.457 1.00 20.23  ?  114 VAL A CG1 1 
ATOM   4077 C  CG2 . VAL C 1 119 ? 43.165 -1.985  -31.751 1.00 20.43  ?  114 VAL A CG2 1 
ATOM   4078 N  N   . ARG C 1 120 ? 42.113 -5.046  -34.064 1.00 18.57  ?  115 ARG A N   1 
ATOM   4079 C  CA  . ARG C 1 120 ? 42.863 -5.784  -35.086 1.00 19.61  ?  115 ARG A CA  1 
ATOM   4080 C  C   . ARG C 1 120 ? 42.897 -4.962  -36.371 1.00 19.90  ?  115 ARG A C   1 
ATOM   4081 O  O   . ARG C 1 120 ? 41.863 -4.305  -36.779 1.00 20.01  ?  115 ARG A O   1 
ATOM   4082 C  CB  . ARG C 1 120 ? 42.255 -7.174  -35.273 1.00 19.54  ?  115 ARG A CB  1 
ATOM   4083 C  CG  . ARG C 1 120 ? 42.659 -8.149  -34.176 1.00 19.87  ?  115 ARG A CG  1 
ATOM   4084 C  CD  . ARG C 1 120 ? 41.916 -9.474  -34.207 1.00 20.54  ?  115 ARG A CD  1 
ATOM   4085 N  NE  . ARG C 1 120 ? 42.403 -10.370 -33.165 1.00 19.46  ?  115 ARG A NE  1 
ATOM   4086 C  CZ  . ARG C 1 120 ? 42.031 -10.371 -31.885 1.00 19.26  ?  115 ARG A CZ  1 
ATOM   4087 N  NH1 . ARG C 1 120 ? 41.093 -9.563  -31.391 1.00 20.70  ?  115 ARG A NH1 1 
ATOM   4088 N  NH2 . ARG C 1 120 ? 42.589 -11.244 -31.097 1.00 19.23  ?  115 ARG A NH2 1 
ATOM   4089 N  N   . GLY C 1 121 ? 44.056 -5.029  -36.984 1.00 19.65  ?  116 GLY A N   1 
ATOM   4090 C  CA  . GLY C 1 121 ? 44.269 -4.625  -38.384 1.00 22.36  ?  116 GLY A CA  1 
ATOM   4091 C  C   . GLY C 1 121 ? 45.729 -4.766  -38.746 1.00 23.23  ?  116 GLY A C   1 
ATOM   4092 O  O   . GLY C 1 121 ? 46.471 -5.487  -38.031 1.00 22.47  ?  116 GLY A O   1 
ATOM   4093 N  N   . GLU C 1 122 ? 46.110 -4.111  -39.830 1.00 23.44  ?  117 GLU A N   1 
ATOM   4094 C  CA  . GLU C 1 122 ? 47.462 -4.164  -40.423 1.00 28.04  ?  117 GLU A CA  1 
ATOM   4095 C  C   . GLU C 1 122 ? 48.270 -3.010  -39.824 1.00 26.35  ?  117 GLU A C   1 
ATOM   4096 O  O   . GLU C 1 122 ? 47.812 -1.872  -39.844 1.00 26.77  ?  117 GLU A O   1 
ATOM   4097 C  CB  . GLU C 1 122 ? 47.277 -4.144  -41.942 1.00 32.39  ?  117 GLU A CB  1 
ATOM   4098 C  CG  . GLU C 1 122 ? 48.544 -4.280  -42.734 1.00 39.96  ?  117 GLU A CG  1 
ATOM   4099 C  CD  . GLU C 1 122 ? 48.302 -4.061  -44.222 1.00 49.29  ?  117 GLU A CD  1 
ATOM   4100 O  OE1 . GLU C 1 122 ? 47.276 -4.594  -44.735 1.00 52.00  ?  117 GLU A OE1 1 
ATOM   4101 O  OE2 . GLU C 1 122 ? 49.111 -3.339  -44.855 1.00 52.72  -1 117 GLU A OE2 1 
ATOM   4102 N  N   . LEU C 1 123 ? 49.425 -3.304  -39.241 1.00 26.27  ?  118 LEU A N   1 
ATOM   4103 C  CA  . LEU C 1 123 ? 50.310 -2.268  -38.657 1.00 26.73  ?  118 LEU A CA  1 
ATOM   4104 C  C   . LEU C 1 123 ? 51.233 -1.764  -39.777 1.00 27.09  ?  118 LEU A C   1 
ATOM   4105 O  O   . LEU C 1 123 ? 51.865 -2.591  -40.436 1.00 27.91  ?  118 LEU A O   1 
ATOM   4106 C  CB  . LEU C 1 123 ? 51.063 -2.880  -37.469 1.00 24.35  ?  118 LEU A CB  1 
ATOM   4107 C  CG  . LEU C 1 123 ? 52.015 -1.936  -36.729 1.00 23.83  ?  118 LEU A CG  1 
ATOM   4108 C  CD1 . LEU C 1 123 ? 52.238 -2.407  -35.315 1.00 23.59  ?  118 LEU A CD1 1 
ATOM   4109 C  CD2 . LEU C 1 123 ? 53.363 -1.807  -37.435 1.00 24.18  ?  118 LEU A CD2 1 
ATOM   4110 N  N   . ARG C 1 124 ? 51.210 -0.468  -40.061 1.00 26.09  ?  119 ARG A N   1 
ATOM   4111 C  CA  . ARG C 1 124 ? 52.046 0.153   -41.111 1.00 27.62  ?  119 ARG A CA  1 
ATOM   4112 C  C   . ARG C 1 124 ? 53.094 0.977   -40.378 1.00 24.88  ?  119 ARG A C   1 
ATOM   4113 O  O   . ARG C 1 124 ? 52.703 1.812   -39.587 1.00 22.81  ?  119 ARG A O   1 
ATOM   4114 C  CB  . ARG C 1 124 ? 51.177 0.984   -42.060 1.00 34.54  ?  119 ARG A CB  1 
ATOM   4115 C  CG  . ARG C 1 124 ? 50.730 0.235   -43.311 1.00 43.11  ?  119 ARG A CG  1 
ATOM   4116 C  CD  . ARG C 1 124 ? 49.347 0.633   -43.803 1.00 50.49  ?  119 ARG A CD  1 
ATOM   4117 N  NE  . ARG C 1 124 ? 48.346 0.088   -42.888 1.00 59.87  ?  119 ARG A NE  1 
ATOM   4118 C  CZ  . ARG C 1 124 ? 47.668 0.768   -41.942 1.00 60.88  ?  119 ARG A CZ  1 
ATOM   4119 N  NH1 . ARG C 1 124 ? 46.829 0.102   -41.156 1.00 47.17  ?  119 ARG A NH1 1 
ATOM   4120 N  NH2 . ARG C 1 124 ? 47.811 2.085   -41.780 1.00 53.15  ?  119 ARG A NH2 1 
ATOM   4121 N  N   . LYS C 1 125 ? 54.366 0.700   -40.596 1.00 22.98  ?  120 LYS A N   1 
ATOM   4122 C  CA  . LYS C 1 125 ? 55.465 1.504   -40.040 1.00 25.38  ?  120 LYS A CA  1 
ATOM   4123 C  C   . LYS C 1 125 ? 55.511 2.877   -40.720 1.00 25.35  ?  120 LYS A C   1 
ATOM   4124 O  O   . LYS C 1 125 ? 55.238 2.971   -41.927 1.00 24.50  ?  120 LYS A O   1 
ATOM   4125 C  CB  . LYS C 1 125 ? 56.791 0.755   -40.191 1.00 26.26  ?  120 LYS A CB  1 
ATOM   4126 C  CG  . LYS C 1 125 ? 56.859 -0.563  -39.444 1.00 26.94  ?  120 LYS A CG  1 
ATOM   4127 C  CD  . LYS C 1 125 ? 58.177 -1.218  -39.618 1.00 30.08  ?  120 LYS A CD  1 
ATOM   4128 C  CE  . LYS C 1 125 ? 58.319 -2.449  -38.760 1.00 31.49  ?  120 LYS A CE  1 
ATOM   4129 N  NZ  . LYS C 1 125 ? 59.554 -3.174  -39.109 1.00 32.94  ?  120 LYS A NZ  1 
ATOM   4130 N  N   . VAL C 1 126 ? 55.781 3.900   -39.918 1.00 24.79  ?  121 VAL A N   1 
ATOM   4131 C  CA  . VAL C 1 126 ? 56.185 5.262   -40.325 1.00 29.96  ?  121 VAL A CA  1 
ATOM   4132 C  C   . VAL C 1 126 ? 57.709 5.239   -40.393 1.00 34.98  ?  121 VAL A C   1 
ATOM   4133 O  O   . VAL C 1 126 ? 58.322 5.053   -39.341 1.00 41.48  ?  121 VAL A O   1 
ATOM   4134 C  CB  . VAL C 1 126 ? 55.743 6.288   -39.272 1.00 34.94  ?  121 VAL A CB  1 
ATOM   4135 C  CG1 . VAL C 1 126 ? 56.419 7.624   -39.494 1.00 38.81  ?  121 VAL A CG1 1 
ATOM   4136 C  CG2 . VAL C 1 126 ? 54.248 6.421   -39.167 1.00 33.76  ?  121 VAL A CG2 1 
ATOM   4137 N  N   . GLU C 1 127 ? 58.322 5.468   -41.542 1.00 39.72  ?  122 GLU A N   1 
ATOM   4138 C  CA  . GLU C 1 127 ? 59.812 5.536   -41.572 1.00 45.38  ?  122 GLU A CA  1 
ATOM   4139 C  C   . GLU C 1 127 ? 60.272 6.999   -41.407 1.00 48.11  ?  122 GLU A C   1 
ATOM   4140 O  O   . GLU C 1 127 ? 61.281 7.256   -40.653 1.00 39.87  ?  122 GLU A O   1 
ATOM   4141 C  CB  . GLU C 1 127 ? 60.315 4.805   -42.818 1.00 47.99  ?  122 GLU A CB  1 
ATOM   4142 C  CG  . GLU C 1 127 ? 59.911 3.327   -42.841 1.00 49.46  ?  122 GLU A CG  1 
ATOM   4143 C  CD  . GLU C 1 127 ? 60.400 2.449   -41.687 1.00 49.59  ?  122 GLU A CD  1 
ATOM   4144 O  OE1 . GLU C 1 127 ? 59.930 1.295   -41.581 1.00 53.88  ?  122 GLU A OE1 1 
ATOM   4145 O  OE2 . GLU C 1 127 ? 61.256 2.896   -40.901 1.00 44.22  -1 122 GLU A OE2 1 
ATOM   4146 N  N   . SER C 1 128 ? 59.531 7.928   -42.016 1.00 39.79  ?  123 SER A N   1 
ATOM   4147 C  CA  . SER C 1 128 ? 59.916 9.354   -42.158 1.00 37.99  ?  123 SER A CA  1 
ATOM   4148 C  C   . SER C 1 128 ? 60.003 10.022  -40.786 1.00 31.93  ?  123 SER A C   1 
ATOM   4149 O  O   . SER C 1 128 ? 59.046 9.897   -39.990 1.00 34.36  ?  123 SER A O   1 
ATOM   4150 C  CB  . SER C 1 128 ? 58.929 10.043  -43.039 1.00 43.23  ?  123 SER A CB  1 
ATOM   4151 O  OG  . SER C 1 128 ? 58.477 9.154   -44.045 1.00 54.07  ?  123 SER A OG  1 
ATOM   4152 N  N   . ALA C 1 129 ? 61.123 10.687  -40.520 1.00 27.49  ?  124 ALA A N   1 
ATOM   4153 C  CA  . ALA C 1 129 ? 61.368 11.534  -39.335 1.00 30.05  ?  124 ALA A CA  1 
ATOM   4154 C  C   . ALA C 1 129 ? 60.186 12.490  -39.084 1.00 30.85  ?  124 ALA A C   1 
ATOM   4155 O  O   . ALA C 1 129 ? 59.854 12.700  -37.902 1.00 28.08  ?  124 ALA A O   1 
ATOM   4156 C  CB  . ALA C 1 129 ? 62.665 12.280  -39.493 1.00 28.63  ?  124 ALA A CB  1 
ATOM   4157 N  N   . ASP C 1 130 ? 59.594 13.061  -40.140 1.00 31.65  ?  125 ASP A N   1 
ATOM   4158 C  CA  . ASP C 1 130 ? 58.479 14.052  -40.034 1.00 31.57  ?  125 ASP A CA  1 
ATOM   4159 C  C   . ASP C 1 130 ? 57.287 13.393  -39.322 1.00 26.46  ?  125 ASP A C   1 
ATOM   4160 O  O   . ASP C 1 130 ? 56.666 14.022  -38.412 1.00 25.51  ?  125 ASP A O   1 
ATOM   4161 C  CB  . ASP C 1 130 ? 58.063 14.606  -41.410 1.00 35.17  ?  125 ASP A CB  1 
ATOM   4162 C  CG  . ASP C 1 130 ? 57.663 13.582  -42.487 1.00 43.94  ?  125 ASP A CG  1 
ATOM   4163 O  OD1 . ASP C 1 130 ? 57.377 14.010  -43.642 1.00 48.39  ?  125 ASP A OD1 1 
ATOM   4164 O  OD2 . ASP C 1 130 ? 57.648 12.353  -42.197 1.00 49.92  -1 125 ASP A OD2 1 
ATOM   4165 N  N   . ASP C 1 131 ? 56.985 12.175  -39.715 1.00 21.53  ?  126 ASP A N   1 
ATOM   4166 C  CA  . ASP C 1 131 ? 55.764 11.452  -39.277 1.00 27.41  ?  126 ASP A CA  1 
ATOM   4167 C  C   . ASP C 1 131 ? 56.033 10.813  -37.904 1.00 23.33  ?  126 ASP A C   1 
ATOM   4168 O  O   . ASP C 1 131 ? 55.043 10.628  -37.115 1.00 23.45  ?  126 ASP A O   1 
ATOM   4169 C  CB  . ASP C 1 131 ? 55.342 10.429  -40.330 1.00 28.91  ?  126 ASP A CB  1 
ATOM   4170 C  CG  . ASP C 1 131 ? 54.910 11.066  -41.633 1.00 36.81  ?  126 ASP A CG  1 
ATOM   4171 O  OD1 . ASP C 1 131 ? 54.399 12.217  -41.585 1.00 38.35  ?  126 ASP A OD1 1 
ATOM   4172 O  OD2 . ASP C 1 131 ? 55.097 10.409  -42.677 1.00 39.38  -1 126 ASP A OD2 1 
ATOM   4173 N  N   . THR C 1 132 ? 57.296 10.496  -37.637 1.00 22.90  ?  127 THR A N   1 
ATOM   4174 C  CA  . THR C 1 132 ? 57.803 9.991   -36.336 1.00 21.85  ?  127 THR A CA  1 
ATOM   4175 C  C   . THR C 1 132 ? 57.673 11.104  -35.283 1.00 21.73  ?  127 THR A C   1 
ATOM   4176 O  O   . THR C 1 132 ? 57.043 10.871  -34.189 1.00 19.35  ?  127 THR A O   1 
ATOM   4177 C  CB  . THR C 1 132 ? 59.220 9.429   -36.522 1.00 23.25  ?  127 THR A CB  1 
ATOM   4178 O  OG1 . THR C 1 132 ? 59.097 8.358   -37.455 1.00 23.73  ?  127 THR A OG1 1 
ATOM   4179 C  CG2 . THR C 1 132 ? 59.784 8.908   -35.236 1.00 24.08  ?  127 THR A CG2 1 
ATOM   4180 N  N   . LEU C 1 133 ? 58.149 12.306  -35.616 1.00 17.37  ?  128 LEU A N   1 
ATOM   4181 C  CA  . LEU C 1 133 ? 58.003 13.478  -34.743 1.00 18.88  ?  128 LEU A CA  1 
ATOM   4182 C  C   . LEU C 1 133 ? 56.518 13.760  -34.488 1.00 17.66  ?  128 LEU A C   1 
ATOM   4183 O  O   . LEU C 1 133 ? 56.161 13.962  -33.310 1.00 20.08  ?  128 LEU A O   1 
ATOM   4184 C  CB  . LEU C 1 133 ? 58.682 14.696  -35.372 1.00 20.76  ?  128 LEU A CB  1 
ATOM   4185 C  CG  . LEU C 1 133 ? 58.672 15.942  -34.487 1.00 18.63  ?  128 LEU A CG  1 
ATOM   4186 C  CD1 . LEU C 1 133 ? 59.611 15.768  -33.277 1.00 19.23  ?  128 LEU A CD1 1 
ATOM   4187 C  CD2 . LEU C 1 133 ? 59.099 17.164  -35.294 1.00 20.72  ?  128 LEU A CD2 1 
ATOM   4188 N  N   . ALA C 1 134 ? 55.694 13.802  -35.520 1.00 17.41  ?  129 ALA A N   1 
ATOM   4189 C  CA  . ALA C 1 134 ? 54.228 14.052  -35.377 1.00 17.13  ?  129 ALA A CA  1 
ATOM   4190 C  C   . ALA C 1 134 ? 53.637 13.054  -34.374 1.00 18.79  ?  129 ALA A C   1 
ATOM   4191 O  O   . ALA C 1 134 ? 52.768 13.459  -33.575 1.00 20.24  ?  129 ALA A O   1 
ATOM   4192 C  CB  . ALA C 1 134 ? 53.534 13.968  -36.662 1.00 17.81  ?  129 ALA A CB  1 
ATOM   4193 N  N   . THR C 1 135 ? 54.052 11.773  -34.452 1.00 18.06  ?  130 THR A N   1 
ATOM   4194 C  CA  . THR C 1 135 ? 53.520 10.694  -33.597 1.00 16.83  ?  130 THR A CA  1 
ATOM   4195 C  C   . THR C 1 135 ? 53.801 11.033  -32.133 1.00 17.07  ?  130 THR A C   1 
ATOM   4196 O  O   . THR C 1 135 ? 52.831 10.988  -31.326 1.00 16.86  ?  130 THR A O   1 
ATOM   4197 C  CB  . THR C 1 135 ? 54.054 9.303   -33.949 1.00 16.24  ?  130 THR A CB  1 
ATOM   4198 O  OG1 . THR C 1 135 ? 53.798 9.070   -35.324 1.00 16.05  ?  130 THR A OG1 1 
ATOM   4199 C  CG2 . THR C 1 135 ? 53.343 8.238   -33.148 1.00 17.23  ?  130 THR A CG2 1 
ATOM   4200 N  N   . VAL C 1 136 ? 55.035 11.346  -31.777 1.00 17.03  ?  131 VAL A N   1 
ATOM   4201 C  CA  . VAL C 1 136 ? 55.412 11.557  -30.343 1.00 17.16  ?  131 VAL A CA  1 
ATOM   4202 C  C   . VAL C 1 136 ? 54.792 12.871  -29.823 1.00 17.19  ?  131 VAL A C   1 
ATOM   4203 O  O   . VAL C 1 136 ? 54.246 12.883  -28.678 1.00 16.91  ?  131 VAL A O   1 
ATOM   4204 C  CB  . VAL C 1 136 ? 56.933 11.401  -30.065 1.00 18.42  ?  131 VAL A CB  1 
ATOM   4205 C  CG1 . VAL C 1 136 ? 57.470 10.029  -30.514 1.00 19.57  ?  131 VAL A CG1 1 
ATOM   4206 C  CG2 . VAL C 1 136 ? 57.773 12.508  -30.654 1.00 17.52  ?  131 VAL A CG2 1 
ATOM   4207 N  N   . ARG C 1 137 ? 54.727 13.934  -30.634 1.00 17.37  ?  132 ARG A N   1 
ATOM   4208 C  CA  . ARG C 1 137 ? 54.156 15.220  -30.122 1.00 17.07  ?  132 ARG A CA  1 
ATOM   4209 C  C   . ARG C 1 137 ? 52.643 15.040  -29.946 1.00 16.51  ?  132 ARG A C   1 
ATOM   4210 O  O   . ARG C 1 137 ? 52.055 15.666  -29.010 1.00 16.99  ?  132 ARG A O   1 
ATOM   4211 C  CB  . ARG C 1 137 ? 54.471 16.371  -31.061 1.00 15.96  ?  132 ARG A CB  1 
ATOM   4212 C  CG  . ARG C 1 137 ? 55.976 16.595  -31.192 1.00 16.24  ?  132 ARG A CG  1 
ATOM   4213 C  CD  . ARG C 1 137 ? 56.375 17.898  -31.843 1.00 16.91  ?  132 ARG A CD  1 
ATOM   4214 N  NE  . ARG C 1 137 ? 55.816 18.071  -33.173 1.00 17.44  ?  132 ARG A NE  1 
ATOM   4215 C  CZ  . ARG C 1 137 ? 56.134 19.029  -34.055 1.00 19.25  ?  132 ARG A CZ  1 
ATOM   4216 N  NH1 . ARG C 1 137 ? 57.060 19.935  -33.788 1.00 20.36  ?  132 ARG A NH1 1 
ATOM   4217 N  NH2 . ARG C 1 137 ? 55.513 19.076  -35.210 1.00 18.45  ?  132 ARG A NH2 1 
ATOM   4218 N  N   . ALA C 1 138 ? 51.996 14.290  -30.835 1.00 16.69  ?  133 ALA A N   1 
ATOM   4219 C  CA  . ALA C 1 138 ? 50.528 14.097  -30.729 1.00 15.52  ?  133 ALA A CA  1 
ATOM   4220 C  C   . ALA C 1 138 ? 50.290 13.260  -29.482 1.00 16.48  ?  133 ALA A C   1 
ATOM   4221 O  O   . ALA C 1 138 ? 49.229 13.463  -28.865 1.00 14.84  ?  133 ALA A O   1 
ATOM   4222 C  CB  . ALA C 1 138 ? 49.898 13.429  -31.912 1.00 16.20  ?  133 ALA A CB  1 
ATOM   4223 N  N   . THR C 1 139 ? 51.236 12.359  -29.167 1.00 14.83  ?  134 THR A N   1 
ATOM   4224 C  CA  . THR C 1 139 ? 51.103 11.476  -27.975 1.00 15.18  ?  134 THR A CA  1 
ATOM   4225 C  C   . THR C 1 139 ? 51.229 12.336  -26.699 1.00 14.68  ?  134 THR A C   1 
ATOM   4226 O  O   . THR C 1 139 ? 50.435 12.163  -25.764 1.00 13.87  ?  134 THR A O   1 
ATOM   4227 C  CB  . THR C 1 139 ? 52.041 10.272  -28.065 1.00 14.08  ?  134 THR A CB  1 
ATOM   4228 O  OG1 . THR C 1 139 ? 51.782 9.496   -29.254 1.00 15.06  ?  134 THR A OG1 1 
ATOM   4229 C  CG2 . THR C 1 139 ? 51.862 9.382   -26.854 1.00 14.10  ?  134 THR A CG2 1 
ATOM   4230 N  N   . VAL C 1 140 ? 52.184 13.244  -26.657 1.00 14.74  ?  135 VAL A N   1 
ATOM   4231 C  CA  . VAL C 1 140 ? 52.362 14.165  -25.518 1.00 16.07  ?  135 VAL A CA  1 
ATOM   4232 C  C   . VAL C 1 140 ? 51.072 14.963  -25.366 1.00 18.54  ?  135 VAL A C   1 
ATOM   4233 O  O   . VAL C 1 140 ? 50.554 15.027  -24.188 1.00 17.80  ?  135 VAL A O   1 
ATOM   4234 C  CB  . VAL C 1 140 ? 53.597 15.063  -25.690 1.00 16.36  ?  135 VAL A CB  1 
ATOM   4235 C  CG1 . VAL C 1 140 ? 53.687 16.074  -24.559 1.00 19.85  ?  135 VAL A CG1 1 
ATOM   4236 C  CG2 . VAL C 1 140 ? 54.863 14.232  -25.699 1.00 17.36  ?  135 VAL A CG2 1 
ATOM   4237 N  N   . ALA C 1 141 ? 50.580 15.567  -26.447 1.00 17.61  ?  136 ALA A N   1 
ATOM   4238 C  CA  . ALA C 1 141 ? 49.371 16.422  -26.351 1.00 17.99  ?  136 ALA A CA  1 
ATOM   4239 C  C   . ALA C 1 141 ? 48.231 15.620  -25.685 1.00 19.45  ?  136 ALA A C   1 
ATOM   4240 O  O   . ALA C 1 141 ? 47.558 16.124  -24.716 1.00 23.29  ?  136 ALA A O   1 
ATOM   4241 C  CB  . ALA C 1 141 ? 49.010 16.951  -27.699 1.00 20.74  ?  136 ALA A CB  1 
ATOM   4242 N  N   . ALA C 1 142 ? 47.958 14.440  -26.220 1.00 18.06  ?  137 ALA A N   1 
ATOM   4243 C  CA  . ALA C 1 142 ? 46.842 13.577  -25.795 1.00 17.91  ?  137 ALA A CA  1 
ATOM   4244 C  C   . ALA C 1 142 ? 47.049 13.117  -24.347 1.00 16.13  ?  137 ALA A C   1 
ATOM   4245 O  O   . ALA C 1 142 ? 46.046 13.259  -23.591 1.00 17.76  ?  137 ALA A O   1 
ATOM   4246 C  CB  . ALA C 1 142 ? 46.678 12.416  -26.728 1.00 18.68  ?  137 ALA A CB  1 
ATOM   4247 N  N   . LEU C 1 143 ? 48.243 12.591  -23.981 1.00 14.29  ?  138 LEU A N   1 
ATOM   4248 C  CA  . LEU C 1 143 ? 48.409 11.960  -22.648 1.00 14.89  ?  138 LEU A CA  1 
ATOM   4249 C  C   . LEU C 1 143 ? 48.645 13.030  -21.593 1.00 17.34  ?  138 LEU A C   1 
ATOM   4250 O  O   . LEU C 1 143 ? 48.077 12.868  -20.484 1.00 16.77  ?  138 LEU A O   1 
ATOM   4251 C  CB  . LEU C 1 143 ? 49.501 10.901  -22.601 1.00 16.02  ?  138 LEU A CB  1 
ATOM   4252 C  CG  . LEU C 1 143 ? 49.514 9.740   -23.604 1.00 19.22  ?  138 LEU A CG  1 
ATOM   4253 C  CD1 . LEU C 1 143 ? 50.125 8.514   -22.987 1.00 17.71  ?  138 LEU A CD1 1 
ATOM   4254 C  CD2 . LEU C 1 143 ? 48.182 9.405   -24.211 1.00 19.29  ?  138 LEU A CD2 1 
ATOM   4255 N  N   . GLU C 1 144 ? 49.440 14.071  -21.881 1.00 16.45  ?  139 GLU A N   1 
ATOM   4256 C  CA  . GLU C 1 144 ? 49.755 15.070  -20.818 1.00 16.46  ?  139 GLU A CA  1 
ATOM   4257 C  C   . GLU C 1 144 ? 48.436 15.724  -20.362 1.00 19.07  ?  139 GLU A C   1 
ATOM   4258 O  O   . GLU C 1 144 ? 48.265 15.922  -19.157 1.00 19.85  ?  139 GLU A O   1 
ATOM   4259 C  CB  . GLU C 1 144 ? 50.795 16.113  -21.202 1.00 17.03  ?  139 GLU A CB  1 
ATOM   4260 C  CG  . GLU C 1 144 ? 51.156 17.041  -20.030 1.00 15.66  ?  139 GLU A CG  1 
ATOM   4261 C  CD  . GLU C 1 144 ? 51.942 16.417  -18.872 1.00 15.31  ?  139 GLU A CD  1 
ATOM   4262 O  OE1 . GLU C 1 144 ? 52.471 15.330  -18.999 1.00 16.56  ?  139 GLU A OE1 1 
ATOM   4263 O  OE2 . GLU C 1 144 ? 52.006 17.049  -17.813 1.00 20.21  -1 139 GLU A OE2 1 
ATOM   4264 N  N   . SER C 1 145 ? 47.510 15.989  -21.272 1.00 20.48  ?  140 SER A N   1 
ATOM   4265 C  CA  . SER C 1 145 ? 46.230 16.682  -20.963 1.00 22.36  ?  140 SER A CA  1 
ATOM   4266 C  C   . SER C 1 145 ? 45.346 15.756  -20.112 1.00 24.43  ?  140 SER A C   1 
ATOM   4267 O  O   . SER C 1 145 ? 44.828 16.204  -19.093 1.00 27.53  ?  140 SER A O   1 
ATOM   4268 C  CB  . SER C 1 145 ? 45.556 17.089  -22.192 1.00 20.16  ?  140 SER A CB  1 
ATOM   4269 O  OG  . SER C 1 145 ? 45.455 15.962  -23.001 1.00 28.94  ?  140 SER A OG  1 
ATOM   4270 N  N   . ARG C 1 146 ? 45.280 14.471  -20.449 1.00 25.70  ?  141 ARG A N   1 
ATOM   4271 C  CA  . ARG C 1 146 ? 44.404 13.497  -19.746 1.00 23.17  ?  141 ARG A CA  1 
ATOM   4272 C  C   . ARG C 1 146 ? 45.023 12.987  -18.432 1.00 20.68  ?  141 ARG A C   1 
ATOM   4273 O  O   . ARG C 1 146 ? 44.249 12.809  -17.479 1.00 19.92  ?  141 ARG A O   1 
ATOM   4274 C  CB  . ARG C 1 146 ? 44.006 12.387  -20.721 1.00 23.91  ?  141 ARG A CB  1 
ATOM   4275 C  CG  . ARG C 1 146 ? 43.036 11.360  -20.147 1.00 27.11  ?  141 ARG A CG  1 
ATOM   4276 C  CD  . ARG C 1 146 ? 42.727 10.346  -21.232 1.00 31.10  ?  141 ARG A CD  1 
ATOM   4277 N  NE  . ARG C 1 146 ? 41.996 10.997  -22.301 1.00 37.76  ?  141 ARG A NE  1 
ATOM   4278 C  CZ  . ARG C 1 146 ? 40.667 11.036  -22.397 1.00 41.05  ?  141 ARG A CZ  1 
ATOM   4279 N  NH1 . ARG C 1 146 ? 39.899 10.424  -21.498 1.00 43.03  ?  141 ARG A NH1 1 
ATOM   4280 N  NH2 . ARG C 1 146 ? 40.121 11.683  -23.408 1.00 37.84  ?  141 ARG A NH2 1 
ATOM   4281 N  N   . PHE C 1 147 ? 46.329 12.719  -18.335 1.00 17.01  ?  142 PHE A N   1 
ATOM   4282 C  CA  . PHE C 1 147 ? 46.946 12.005  -17.184 1.00 17.99  ?  142 PHE A CA  1 
ATOM   4283 C  C   . PHE C 1 147 ? 48.021 12.854  -16.490 1.00 17.70  ?  142 PHE A C   1 
ATOM   4284 O  O   . PHE C 1 147 ? 48.545 12.433  -15.441 1.00 17.93  ?  142 PHE A O   1 
ATOM   4285 C  CB  . PHE C 1 147 ? 47.539 10.666  -17.639 1.00 17.22  ?  142 PHE A CB  1 
ATOM   4286 C  CG  . PHE C 1 147 ? 46.593 9.792   -18.416 1.00 17.69  ?  142 PHE A CG  1 
ATOM   4287 C  CD1 . PHE C 1 147 ? 45.598 9.076   -17.758 1.00 19.21  ?  142 PHE A CD1 1 
ATOM   4288 C  CD2 . PHE C 1 147 ? 46.654 9.717   -19.802 1.00 16.91  ?  142 PHE A CD2 1 
ATOM   4289 C  CE1 . PHE C 1 147 ? 44.699 8.298   -18.468 1.00 19.42  ?  142 PHE A CE1 1 
ATOM   4290 C  CE2 . PHE C 1 147 ? 45.744 8.945   -20.511 1.00 18.88  ?  142 PHE A CE2 1 
ATOM   4291 C  CZ  . PHE C 1 147 ? 44.761 8.243   -19.842 1.00 17.99  ?  142 PHE A CZ  1 
ATOM   4292 N  N   . GLY C 1 148 ? 48.342 14.025  -17.046 1.00 19.46  ?  143 GLY A N   1 
ATOM   4293 C  CA  . GLY C 1 148 ? 49.552 14.744  -16.630 1.00 19.30  ?  143 GLY A CA  1 
ATOM   4294 C  C   . GLY C 1 148 ? 49.252 15.856  -15.654 1.00 20.70  ?  143 GLY A C   1 
ATOM   4295 O  O   . GLY C 1 148 ? 48.186 15.843  -14.968 1.00 19.66  ?  143 GLY A O   1 
ATOM   4296 N  N   . ALA C 1 149 ? 50.216 16.765  -15.561 1.00 22.86  ?  144 ALA A N   1 
ATOM   4297 C  CA  . ALA C 1 149 ? 50.309 17.789  -14.501 1.00 23.05  ?  144 ALA A CA  1 
ATOM   4298 C  C   . ALA C 1 149 ? 50.768 19.103  -15.124 1.00 22.61  ?  144 ALA A C   1 
ATOM   4299 O  O   . ALA C 1 149 ? 51.467 19.834  -14.472 1.00 29.51  ?  144 ALA A O   1 
ATOM   4300 C  CB  . ALA C 1 149 ? 51.202 17.292  -13.396 1.00 22.07  ?  144 ALA A CB  1 
ATOM   4301 N  N   . GLY C 1 150 ? 50.280 19.406  -16.325 1.00 24.52  ?  145 GLY A N   1 
ATOM   4302 C  CA  . GLY C 1 150 ? 50.361 20.716  -16.981 1.00 22.23  ?  145 GLY A CA  1 
ATOM   4303 C  C   . GLY C 1 150 ? 51.705 20.950  -17.645 1.00 25.07  ?  145 GLY A C   1 
ATOM   4304 O  O   . GLY C 1 150 ? 52.025 22.121  -17.874 1.00 23.69  ?  145 GLY A O   1 
ATOM   4305 N  N   . TRP C 1 151 ? 52.492 19.898  -17.935 1.00 21.95  ?  146 TRP A N   1 
ATOM   4306 C  CA  . TRP C 1 151 ? 53.860 20.074  -18.521 1.00 21.41  ?  146 TRP A CA  1 
ATOM   4307 C  C   . TRP C 1 151 ? 53.740 20.654  -19.937 1.00 21.97  ?  146 TRP A C   1 
ATOM   4308 O  O   . TRP C 1 151 ? 52.856 20.248  -20.720 1.00 19.57  ?  146 TRP A O   1 
ATOM   4309 C  CB  . TRP C 1 151 ? 54.629 18.754  -18.508 1.00 20.69  ?  146 TRP A CB  1 
ATOM   4310 C  CG  . TRP C 1 151 ? 56.004 18.846  -19.071 1.00 16.09  ?  146 TRP A CG  1 
ATOM   4311 C  CD1 . TRP C 1 151 ? 57.099 19.418  -18.479 1.00 20.56  ?  146 TRP A CD1 1 
ATOM   4312 C  CD2 . TRP C 1 151 ? 56.476 18.270  -20.294 1.00 18.36  ?  146 TRP A CD2 1 
ATOM   4313 N  NE1 . TRP C 1 151 ? 58.213 19.310  -19.287 1.00 15.76  ?  146 TRP A NE1 1 
ATOM   4314 C  CE2 . TRP C 1 151 ? 57.878 18.555  -20.373 1.00 15.16  ?  146 TRP A CE2 1 
ATOM   4315 C  CE3 . TRP C 1 151 ? 55.885 17.523  -21.321 1.00 15.73  ?  146 TRP A CE3 1 
ATOM   4316 C  CZ2 . TRP C 1 151 ? 58.633 18.150  -21.456 1.00 16.77  ?  146 TRP A CZ2 1 
ATOM   4317 C  CZ3 . TRP C 1 151 ? 56.648 17.119  -22.391 1.00 16.84  ?  146 TRP A CZ3 1 
ATOM   4318 C  CH2 . TRP C 1 151 ? 58.014 17.433  -22.453 1.00 16.25  ?  146 TRP A CH2 1 
ATOM   4319 N  N   . ASP C 1 152 ? 54.622 21.590  -20.245 1.00 21.16  ?  147 ASP A N   1 
ATOM   4320 C  CA  . ASP C 1 152 ? 54.756 22.228  -21.566 1.00 21.38  ?  147 ASP A CA  1 
ATOM   4321 C  C   . ASP C 1 152 ? 55.959 21.602  -22.268 1.00 20.93  ?  147 ASP A C   1 
ATOM   4322 O  O   . ASP C 1 152 ? 57.119 21.786  -21.781 1.00 21.08  ?  147 ASP A O   1 
ATOM   4323 C  CB  . ASP C 1 152 ? 54.900 23.732  -21.332 1.00 23.91  ?  147 ASP A CB  1 
ATOM   4324 C  CG  . ASP C 1 152 ? 55.005 24.561  -22.582 1.00 26.70  ?  147 ASP A CG  1 
ATOM   4325 O  OD1 . ASP C 1 152 ? 54.906 23.976  -23.702 1.00 25.80  ?  147 ASP A OD1 1 
ATOM   4326 O  OD2 . ASP C 1 152 ? 55.200 25.792  -22.423 1.00 33.39  -1 147 ASP A OD2 1 
ATOM   4327 N  N   . MET C 1 153 ? 55.707 20.976  -23.417 1.00 18.98  ?  148 MET A N   1 
ATOM   4328 C  CA  . MET C 1 153 ? 56.754 20.264  -24.197 1.00 18.84  ?  148 MET A CA  1 
ATOM   4329 C  C   . MET C 1 153 ? 57.620 21.243  -25.026 1.00 20.88  ?  148 MET A C   1 
ATOM   4330 O  O   . MET C 1 153 ? 58.622 20.789  -25.688 1.00 17.03  ?  148 MET A O   1 
ATOM   4331 C  CB  . MET C 1 153 ? 56.069 19.253  -25.088 1.00 19.82  ?  148 MET A CB  1 
ATOM   4332 C  CG  . MET C 1 153 ? 55.443 19.915  -26.329 1.00 21.44  ?  148 MET A CG  1 
ATOM   4333 S  SD  . MET C 1 153 ? 54.884 18.717  -27.544 1.00 24.82  ?  148 MET A SD  1 
ATOM   4334 C  CE  . MET C 1 153 ? 53.148 18.544  -27.123 1.00 26.04  ?  148 MET A CE  1 
ATOM   4335 N  N   . THR C 1 154 ? 57.257 22.519  -25.069 1.00 20.00  ?  149 THR A N   1 
ATOM   4336 C  CA  . THR C 1 154 ? 57.884 23.490  -26.017 1.00 21.13  ?  149 THR A CA  1 
ATOM   4337 C  C   . THR C 1 154 ? 59.412 23.437  -25.912 1.00 21.74  ?  149 THR A C   1 
ATOM   4338 O  O   . THR C 1 154 ? 60.077 23.304  -26.949 1.00 23.77  ?  149 THR A O   1 
ATOM   4339 C  CB  . THR C 1 154 ? 57.405 24.916  -25.744 1.00 21.87  ?  149 THR A CB  1 
ATOM   4340 O  OG1 . THR C 1 154 ? 55.969 24.919  -25.816 1.00 28.52  ?  149 THR A OG1 1 
ATOM   4341 C  CG2 . THR C 1 154 ? 58.034 25.911  -26.697 1.00 21.98  ?  149 THR A CG2 1 
ATOM   4342 N  N   . GLY C 1 155 ? 59.937 23.522  -24.698 1.00 23.13  ?  150 GLY A N   1 
ATOM   4343 C  CA  . GLY C 1 155 ? 61.386 23.589  -24.419 1.00 24.76  ?  150 GLY A CA  1 
ATOM   4344 C  C   . GLY C 1 155 ? 62.108 22.284  -24.702 1.00 23.93  ?  150 GLY A C   1 
ATOM   4345 O  O   . GLY C 1 155 ? 63.351 22.252  -24.582 1.00 25.58  ?  150 GLY A O   1 
ATOM   4346 N  N   . SER C 1 156 ? 61.371 21.224  -25.036 1.00 21.57  ?  151 SER A N   1 
ATOM   4347 C  CA  . SER C 1 156 ? 61.915 19.870  -25.319 1.00 18.33  ?  151 SER A CA  1 
ATOM   4348 C  C   . SER C 1 156 ? 61.686 19.438  -26.766 1.00 16.53  ?  151 SER A C   1 
ATOM   4349 O  O   . SER C 1 156 ? 62.109 18.320  -27.135 1.00 15.53  ?  151 SER A O   1 
ATOM   4350 C  CB  . SER C 1 156 ? 61.371 18.880  -24.294 1.00 18.97  ?  151 SER A CB  1 
ATOM   4351 O  OG  . SER C 1 156 ? 61.697 19.317  -22.983 1.00 19.35  ?  151 SER A OG  1 
ATOM   4352 N  N   . LEU C 1 157 ? 61.172 20.329  -27.615 1.00 19.01  ?  152 LEU A N   1 
ATOM   4353 C  CA  . LEU C 1 157 ? 60.961 20.012  -29.061 1.00 21.51  ?  152 LEU A CA  1 
ATOM   4354 C  C   . LEU C 1 157 ? 62.278 19.635  -29.749 1.00 20.39  ?  152 LEU A C   1 
ATOM   4355 O  O   . LEU C 1 157 ? 62.315 18.639  -30.479 1.00 21.96  ?  152 LEU A O   1 
ATOM   4356 C  CB  . LEU C 1 157 ? 60.209 21.170  -29.736 1.00 25.37  ?  152 LEU A CB  1 
ATOM   4357 C  CG  . LEU C 1 157 ? 58.747 21.382  -29.269 1.00 30.11  ?  152 LEU A CG  1 
ATOM   4358 C  CD1 . LEU C 1 157 ? 58.087 22.617  -29.898 1.00 31.09  ?  152 LEU A CD1 1 
ATOM   4359 C  CD2 . LEU C 1 157 ? 57.891 20.175  -29.579 1.00 30.15  ?  152 LEU A CD2 1 
ATOM   4360 N  N   . ASP C 1 158 ? 63.396 20.289  -29.430 1.00 21.34  ?  153 ASP A N   1 
ATOM   4361 C  CA  . ASP C 1 158 ? 64.704 19.933  -30.044 1.00 21.49  ?  153 ASP A CA  1 
ATOM   4362 C  C   . ASP C 1 158 ? 65.203 18.588  -29.504 1.00 21.65  ?  153 ASP A C   1 
ATOM   4363 O  O   . ASP C 1 158 ? 65.766 17.791  -30.272 1.00 19.99  ?  153 ASP A O   1 
ATOM   4364 C  CB  . ASP C 1 158 ? 65.694 21.064  -29.816 1.00 23.33  ?  153 ASP A CB  1 
ATOM   4365 C  CG  . ASP C 1 158 ? 65.426 22.258  -30.703 1.00 27.36  ?  153 ASP A CG  1 
ATOM   4366 O  OD1 . ASP C 1 158 ? 64.894 22.051  -31.836 1.00 25.06  ?  153 ASP A OD1 1 
ATOM   4367 O  OD2 . ASP C 1 158 ? 65.753 23.369  -30.253 1.00 27.17  -1 153 ASP A OD2 1 
ATOM   4368 N  N   . TYR C 1 159 ? 64.920 18.310  -28.236 1.00 22.50  ?  154 TYR A N   1 
ATOM   4369 C  CA  . TYR C 1 159 ? 65.274 17.023  -27.584 1.00 21.36  ?  154 TYR A CA  1 
ATOM   4370 C  C   . TYR C 1 159 ? 64.557 15.887  -28.322 1.00 20.44  ?  154 TYR A C   1 
ATOM   4371 O  O   . TYR C 1 159 ? 65.220 14.887  -28.678 1.00 23.42  ?  154 TYR A O   1 
ATOM   4372 C  CB  . TYR C 1 159 ? 64.956 17.086  -26.088 1.00 20.77  ?  154 TYR A CB  1 
ATOM   4373 C  CG  . TYR C 1 159 ? 65.056 15.735  -25.433 1.00 25.25  ?  154 TYR A CG  1 
ATOM   4374 C  CD1 . TYR C 1 159 ? 66.202 14.955  -25.569 1.00 26.40  ?  154 TYR A CD1 1 
ATOM   4375 C  CD2 . TYR C 1 159 ? 64.038 15.249  -24.638 1.00 24.85  ?  154 TYR A CD2 1 
ATOM   4376 C  CE1 . TYR C 1 159 ? 66.330 13.725  -24.938 1.00 26.46  ?  154 TYR A CE1 1 
ATOM   4377 C  CE2 . TYR C 1 159 ? 64.160 14.034  -23.982 1.00 23.34  ?  154 TYR A CE2 1 
ATOM   4378 C  CZ  . TYR C 1 159 ? 65.305 13.273  -24.130 1.00 25.87  ?  154 TYR A CZ  1 
ATOM   4379 O  OH  . TYR C 1 159 ? 65.388 12.049  -23.527 1.00 26.72  ?  154 TYR A OH  1 
ATOM   4380 N  N   . PHE C 1 160 ? 63.237 16.026  -28.547 1.00 18.80  ?  155 PHE A N   1 
ATOM   4381 C  CA  . PHE C 1 160 ? 62.400 15.030  -29.251 1.00 16.97  ?  155 PHE A CA  1 
ATOM   4382 C  C   . PHE C 1 160 ? 63.074 14.708  -30.605 1.00 18.69  ?  155 PHE A C   1 
ATOM   4383 O  O   . PHE C 1 160 ? 63.137 13.509  -31.041 1.00 18.26  ?  155 PHE A O   1 
ATOM   4384 C  CB  . PHE C 1 160 ? 60.963 15.542  -29.476 1.00 16.62  ?  155 PHE A CB  1 
ATOM   4385 C  CG  . PHE C 1 160 ? 60.073 15.726  -28.256 1.00 17.28  ?  155 PHE A CG  1 
ATOM   4386 C  CD1 . PHE C 1 160 ? 60.546 15.586  -26.955 1.00 16.16  ?  155 PHE A CD1 1 
ATOM   4387 C  CD2 . PHE C 1 160 ? 58.745 16.114  -28.418 1.00 18.89  ?  155 PHE A CD2 1 
ATOM   4388 C  CE1 . PHE C 1 160 ? 59.731 15.777  -25.857 1.00 16.54  ?  155 PHE A CE1 1 
ATOM   4389 C  CE2 . PHE C 1 160 ? 57.915 16.281  -27.311 1.00 17.84  ?  155 PHE A CE2 1 
ATOM   4390 C  CZ  . PHE C 1 160 ? 58.411 16.098  -26.031 1.00 17.50  ?  155 PHE A CZ  1 
ATOM   4391 N  N   . ARG C 1 161 ? 63.476 15.769  -31.319 1.00 17.59  ?  156 ARG A N   1 
ATOM   4392 C  CA  . ARG C 1 161 ? 63.960 15.630  -32.708 1.00 21.89  ?  156 ARG A CA  1 
ATOM   4393 C  C   . ARG C 1 161 ? 65.256 14.811  -32.668 1.00 22.10  ?  156 ARG A C   1 
ATOM   4394 O  O   . ARG C 1 161 ? 65.456 13.974  -33.553 1.00 26.26  ?  156 ARG A O   1 
ATOM   4395 C  CB  . ARG C 1 161 ? 64.133 17.005  -33.358 1.00 22.70  ?  156 ARG A CB  1 
ATOM   4396 C  CG  . ARG C 1 161 ? 62.822 17.772  -33.558 1.00 27.08  ?  156 ARG A CG  1 
ATOM   4397 C  CD  . ARG C 1 161 ? 63.038 19.079  -34.338 1.00 25.49  ?  156 ARG A CD  1 
ATOM   4398 N  NE  . ARG C 1 161 ? 63.602 18.700  -35.599 1.00 26.25  ?  156 ARG A NE  1 
ATOM   4399 C  CZ  . ARG C 1 161 ? 64.120 19.519  -36.504 1.00 33.93  ?  156 ARG A CZ  1 
ATOM   4400 N  NH1 . ARG C 1 161 ? 64.077 20.829  -36.331 1.00 30.60  ?  156 ARG A NH1 1 
ATOM   4401 N  NH2 . ARG C 1 161 ? 64.622 19.011  -37.620 1.00 35.33  ?  156 ARG A NH2 1 
ATOM   4402 N  N   . ARG C 1 162 ? 66.058 15.009  -31.647 1.00 20.21  ?  157 ARG A N   1 
ATOM   4403 C  CA  . ARG C 1 162 ? 67.356 14.319  -31.545 1.00 22.67  ?  157 ARG A CA  1 
ATOM   4404 C  C   . ARG C 1 162 ? 67.134 12.829  -31.261 1.00 25.06  ?  157 ARG A C   1 
ATOM   4405 O  O   . ARG C 1 162 ? 67.951 12.036  -31.785 1.00 25.31  ?  157 ARG A O   1 
ATOM   4406 C  CB  . ARG C 1 162 ? 68.220 14.936  -30.454 1.00 21.73  ?  157 ARG A CB  1 
ATOM   4407 C  CG  . ARG C 1 162 ? 69.619 14.324  -30.413 1.00 23.46  ?  157 ARG A CG  1 
ATOM   4408 C  CD  . ARG C 1 162 ? 70.566 14.805  -31.502 1.00 24.43  ?  157 ARG A CD  1 
ATOM   4409 N  NE  . ARG C 1 162 ? 71.823 14.034  -31.513 1.00 22.50  ?  157 ARG A NE  1 
ATOM   4410 C  CZ  . ARG C 1 162 ? 73.015 14.478  -31.903 1.00 22.55  ?  157 ARG A CZ  1 
ATOM   4411 N  NH1 . ARG C 1 162 ? 73.158 15.730  -32.285 1.00 21.14  ?  157 ARG A NH1 1 
ATOM   4412 N  NH2 . ARG C 1 162 ? 74.077 13.665  -31.849 1.00 22.77  ?  157 ARG A NH2 1 
ATOM   4413 N  N   . ILE C 1 163 ? 66.116 12.448  -30.464 1.00 23.48  ?  158 ILE A N   1 
ATOM   4414 C  CA  . ILE C 1 163 ? 65.994 11.039  -30.001 1.00 22.56  ?  158 ILE A CA  1 
ATOM   4415 C  C   . ILE C 1 163 ? 65.141 10.276  -30.995 1.00 23.51  ?  158 ILE A C   1 
ATOM   4416 O  O   . ILE C 1 163 ? 65.041 9.045   -30.848 1.00 26.98  ?  158 ILE A O   1 
ATOM   4417 C  CB  . ILE C 1 163 ? 65.517 10.909  -28.551 1.00 24.39  ?  158 ILE A CB  1 
ATOM   4418 C  CG1 . ILE C 1 163 ? 64.138 11.524  -28.289 1.00 26.53  ?  158 ILE A CG1 1 
ATOM   4419 C  CG2 . ILE C 1 163 ? 66.555 11.523  -27.643 1.00 23.95  ?  158 ILE A CG2 1 
ATOM   4420 C  CD1 . ILE C 1 163 ? 63.672 11.354  -26.859 1.00 23.56  ?  158 ILE A CD1 1 
ATOM   4421 N  N   . LEU C 1 164 ? 64.651 10.970  -31.993 1.00 18.34  ?  159 LEU A N   1 
ATOM   4422 C  CA  . LEU C 1 164 ? 63.697 10.421  -32.954 1.00 25.26  ?  159 LEU A CA  1 
ATOM   4423 C  C   . LEU C 1 164 ? 64.228 9.150   -33.629 1.00 25.97  ?  159 LEU A C   1 
ATOM   4424 O  O   . LEU C 1 164 ? 63.437 8.250   -33.918 1.00 27.16  ?  159 LEU A O   1 
ATOM   4425 C  CB  . LEU C 1 164 ? 63.351 11.519  -33.946 1.00 24.88  ?  159 LEU A CB  1 
ATOM   4426 C  CG  . LEU C 1 164 ? 61.967 11.374  -34.517 1.00 27.93  ?  159 LEU A CG  1 
ATOM   4427 C  CD1 . LEU C 1 164 ? 60.935 11.723  -33.456 1.00 25.47  ?  159 LEU A CD1 1 
ATOM   4428 C  CD2 . LEU C 1 164 ? 61.828 12.237  -35.761 1.00 30.60  ?  159 LEU A CD2 1 
ATOM   4429 N  N   . PRO C 1 165 ? 65.543 9.013   -33.952 1.00 27.42  ?  160 PRO A N   1 
ATOM   4430 C  CA  . PRO C 1 165 ? 66.057 7.775   -34.543 1.00 25.39  ?  160 PRO A CA  1 
ATOM   4431 C  C   . PRO C 1 165 ? 65.685 6.494   -33.758 1.00 24.65  ?  160 PRO A C   1 
ATOM   4432 O  O   . PRO C 1 165 ? 65.623 5.468   -34.379 1.00 23.45  ?  160 PRO A O   1 
ATOM   4433 C  CB  . PRO C 1 165 ? 67.589 7.973   -34.547 1.00 26.62  ?  160 PRO A CB  1 
ATOM   4434 C  CG  . PRO C 1 165 ? 67.771 9.470   -34.604 1.00 28.13  ?  160 PRO A CG  1 
ATOM   4435 C  CD  . PRO C 1 165 ? 66.602 10.026  -33.811 1.00 30.99  ?  160 PRO A CD  1 
ATOM   4436 N  N   . GLY C 1 166 ? 65.499 6.576   -32.433 1.00 19.98  ?  161 GLY A N   1 
ATOM   4437 C  CA  . GLY C 1 166 ? 65.188 5.421   -31.563 1.00 21.41  ?  161 GLY A CA  1 
ATOM   4438 C  C   . GLY C 1 166 ? 63.707 5.081   -31.575 1.00 17.92  ?  161 GLY A C   1 
ATOM   4439 O  O   . GLY C 1 166 ? 63.352 3.993   -31.140 1.00 17.01  ?  161 GLY A O   1 
ATOM   4440 N  N   . VAL C 1 167 ? 62.857 5.923   -32.161 1.00 20.10  ?  162 VAL A N   1 
ATOM   4441 C  CA  . VAL C 1 167 ? 61.395 5.625   -32.159 1.00 19.32  ?  162 VAL A CA  1 
ATOM   4442 C  C   . VAL C 1 167 ? 60.996 4.828   -33.399 1.00 22.36  ?  162 VAL A C   1 
ATOM   4443 O  O   . VAL C 1 167 ? 61.330 5.247   -34.538 1.00 20.86  ?  162 VAL A O   1 
ATOM   4444 C  CB  . VAL C 1 167 ? 60.534 6.891   -32.000 1.00 20.70  ?  162 VAL A CB  1 
ATOM   4445 C  CG1 . VAL C 1 167 ? 61.095 7.912   -31.030 1.00 20.46  ?  162 VAL A CG1 1 
ATOM   4446 C  CG2 . VAL C 1 167 ? 60.266 7.535   -33.285 1.00 22.95  ?  162 VAL A CG2 1 
ATOM   4447 N  N   . GLY C 1 168 ? 60.141 3.808   -33.188 1.00 20.59  ?  163 GLY A N   1 
ATOM   4448 C  CA  . GLY C 1 168 ? 59.455 3.058   -34.247 1.00 19.22  ?  163 GLY A CA  1 
ATOM   4449 C  C   . GLY C 1 168 ? 58.002 3.457   -34.212 1.00 19.61  ?  163 GLY A C   1 
ATOM   4450 O  O   . GLY C 1 168 ? 57.238 2.882   -33.401 1.00 17.80  ?  163 GLY A O   1 
ATOM   4451 N  N   . ALA C 1 169 ? 57.640 4.472   -34.998 1.00 19.13  ?  164 ALA A N   1 
ATOM   4452 C  CA  . ALA C 1 169 ? 56.248 4.966   -35.060 1.00 18.30  ?  164 ALA A CA  1 
ATOM   4453 C  C   . ALA C 1 169 ? 55.443 4.122   -36.049 1.00 18.54  ?  164 ALA A C   1 
ATOM   4454 O  O   . ALA C 1 169 ? 55.998 3.667   -37.106 1.00 20.13  ?  164 ALA A O   1 
ATOM   4455 C  CB  . ALA C 1 169 ? 56.243 6.443   -35.388 1.00 17.58  ?  164 ALA A CB  1 
ATOM   4456 N  N   . PHE C 1 170 ? 54.139 4.007   -35.801 1.00 17.89  ?  165 PHE A N   1 
ATOM   4457 C  CA  . PHE C 1 170 ? 53.276 3.135   -36.600 1.00 19.22  ?  165 PHE A CA  1 
ATOM   4458 C  C   . PHE C 1 170 ? 51.861 3.677   -36.628 1.00 18.20  ?  165 PHE A C   1 
ATOM   4459 O  O   . PHE C 1 170 ? 51.465 4.568   -35.838 1.00 18.80  ?  165 PHE A O   1 
ATOM   4460 C  CB  . PHE C 1 170 ? 53.368 1.686   -36.116 1.00 19.71  ?  165 PHE A CB  1 
ATOM   4461 C  CG  . PHE C 1 170 ? 52.912 1.437   -34.710 1.00 21.14  ?  165 PHE A CG  1 
ATOM   4462 C  CD1 . PHE C 1 170 ? 51.566 1.346   -34.431 1.00 21.73  ?  165 PHE A CD1 1 
ATOM   4463 C  CD2 . PHE C 1 170 ? 53.825 1.231   -33.696 1.00 21.76  ?  165 PHE A CD2 1 
ATOM   4464 C  CE1 . PHE C 1 170 ? 51.151 1.103   -33.141 1.00 22.69  ?  165 PHE A CE1 1 
ATOM   4465 C  CE2 . PHE C 1 170 ? 53.396 0.928   -32.417 1.00 22.12  ?  165 PHE A CE2 1 
ATOM   4466 C  CZ  . PHE C 1 170 ? 52.064 0.942   -32.137 1.00 22.28  ?  165 PHE A CZ  1 
ATOM   4467 N  N   . ARG C 1 171 ? 51.128 3.134   -37.577 1.00 19.08  ?  166 ARG A N   1 
ATOM   4468 C  CA  . ARG C 1 171 ? 49.706 3.440   -37.829 1.00 19.45  ?  166 ARG A CA  1 
ATOM   4469 C  C   . ARG C 1 171 ? 48.938 2.127   -37.839 1.00 23.68  ?  166 ARG A C   1 
ATOM   4470 O  O   . ARG C 1 171 ? 49.423 1.135   -38.423 1.00 22.10  ?  166 ARG A O   1 
ATOM   4471 C  CB  . ARG C 1 171 ? 49.649 4.190   -39.162 1.00 19.59  ?  166 ARG A CB  1 
ATOM   4472 C  CG  . ARG C 1 171 ? 50.391 5.530   -39.172 1.00 18.80  ?  166 ARG A CG  1 
ATOM   4473 C  CD  . ARG C 1 171 ? 49.656 6.560   -38.335 1.00 19.94  ?  166 ARG A CD  1 
ATOM   4474 N  NE  . ARG C 1 171 ? 50.223 7.914   -38.344 1.00 20.39  ?  166 ARG A NE  1 
ATOM   4475 C  CZ  . ARG C 1 171 ? 51.178 8.349   -37.513 1.00 21.01  ?  166 ARG A CZ  1 
ATOM   4476 N  NH1 . ARG C 1 171 ? 51.683 7.565   -36.575 1.00 21.67  ?  166 ARG A NH1 1 
ATOM   4477 N  NH2 . ARG C 1 171 ? 51.642 9.581   -37.615 1.00 21.31  ?  166 ARG A NH2 1 
ATOM   4478 N  N   . LEU C 1 172 ? 47.756 2.107   -37.236 1.00 24.77  ?  167 LEU A N   1 
ATOM   4479 C  CA  . LEU C 1 172 ? 46.948 0.875   -37.162 1.00 23.08  ?  167 LEU A CA  1 
ATOM   4480 C  C   . LEU C 1 172 ? 45.526 1.246   -37.534 1.00 23.34  ?  167 LEU A C   1 
ATOM   4481 O  O   . LEU C 1 172 ? 44.825 1.872   -36.719 1.00 23.82  ?  167 LEU A O   1 
ATOM   4482 C  CB  . LEU C 1 172 ? 47.059 0.313   -35.748 1.00 21.45  ?  167 LEU A CB  1 
ATOM   4483 C  CG  . LEU C 1 172 ? 46.310 -0.978  -35.471 1.00 22.56  ?  167 LEU A CG  1 
ATOM   4484 C  CD1 . LEU C 1 172 ? 46.690 -2.054  -36.497 1.00 25.26  ?  167 LEU A CD1 1 
ATOM   4485 C  CD2 . LEU C 1 172 ? 46.642 -1.411  -34.057 1.00 22.46  ?  167 LEU A CD2 1 
ATOM   4486 N  N   . ARG C 1 173 ? 45.144 0.918   -38.760 1.00 21.45  ?  168 ARG A N   1 
ATOM   4487 C  CA  . ARG C 1 173 ? 43.771 1.120   -39.221 1.00 24.25  ?  168 ARG A CA  1 
ATOM   4488 C  C   . ARG C 1 173 ? 43.006 -0.036  -38.612 1.00 20.93  ?  168 ARG A C   1 
ATOM   4489 O  O   . ARG C 1 173 ? 43.337 -1.200  -38.911 1.00 23.89  ?  168 ARG A O   1 
ATOM   4490 C  CB  . ARG C 1 173 ? 43.643 1.207   -40.750 1.00 29.61  ?  168 ARG A CB  1 
ATOM   4491 C  CG  . ARG C 1 173 ? 42.187 1.274   -41.202 1.00 34.44  ?  168 ARG A CG  1 
ATOM   4492 C  CD  . ARG C 1 173 ? 41.825 2.400   -42.140 1.00 44.25  ?  168 ARG A CD  1 
ATOM   4493 N  NE  . ARG C 1 173 ? 41.746 3.659   -41.405 1.00 54.42  ?  168 ARG A NE  1 
ATOM   4494 C  CZ  . ARG C 1 173 ? 41.344 4.824   -41.909 1.00 56.66  ?  168 ARG A CZ  1 
ATOM   4495 N  NH1 . ARG C 1 173 ? 41.333 5.904   -41.140 1.00 53.65  ?  168 ARG A NH1 1 
ATOM   4496 N  NH2 . ARG C 1 173 ? 40.963 4.910   -43.175 1.00 63.09  ?  168 ARG A NH2 1 
ATOM   4497 N  N   . VAL C 1 174 ? 42.040 0.285   -37.775 1.00 20.84  ?  169 VAL A N   1 
ATOM   4498 C  CA  . VAL C 1 174 ? 41.209 -0.725  -37.085 1.00 21.55  ?  169 VAL A CA  1 
ATOM   4499 C  C   . VAL C 1 174 ? 40.284 -1.376  -38.118 1.00 22.51  ?  169 VAL A C   1 
ATOM   4500 O  O   . VAL C 1 174 ? 39.427 -0.674  -38.635 1.00 22.94  ?  169 VAL A O   1 
ATOM   4501 C  CB  . VAL C 1 174 ? 40.434 -0.066  -35.934 1.00 23.84  ?  169 VAL A CB  1 
ATOM   4502 C  CG1 . VAL C 1 174 ? 39.524 -1.060  -35.241 1.00 22.63  ?  169 VAL A CG1 1 
ATOM   4503 C  CG2 . VAL C 1 174 ? 41.389 0.593   -34.952 1.00 22.61  ?  169 VAL A CG2 1 
ATOM   4504 N  N   . ALA C 1 175 ? 40.450 -2.677  -38.368 1.00 22.00  ?  170 ALA A N   1 
ATOM   4505 C  CA  . ALA C 1 175 ? 39.590 -3.506  -39.249 1.00 24.05  ?  170 ALA A CA  1 
ATOM   4506 C  C   . ALA C 1 175 ? 38.493 -4.174  -38.421 1.00 25.20  ?  170 ALA A C   1 
ATOM   4507 O  O   . ALA C 1 175 ? 37.363 -4.269  -38.911 1.00 26.44  ?  170 ALA A O   1 
ATOM   4508 C  CB  . ALA C 1 175 ? 40.423 -4.519  -39.993 1.00 25.29  ?  170 ALA A CB  1 
ATOM   4509 N  N   . GLU C 1 176 ? 38.811 -4.577  -37.187 1.00 23.63  ?  171 GLU A N   1 
ATOM   4510 C  CA  . GLU C 1 176 ? 37.886 -5.225  -36.240 1.00 25.13  ?  171 GLU A CA  1 
ATOM   4511 C  C   . GLU C 1 176 ? 38.142 -4.658  -34.833 1.00 23.22  ?  171 GLU A C   1 
ATOM   4512 O  O   . GLU C 1 176 ? 39.318 -4.402  -34.441 1.00 17.83  ?  171 GLU A O   1 
ATOM   4513 C  CB  . GLU C 1 176 ? 38.091 -6.750  -36.192 1.00 30.65  ?  171 GLU A CB  1 
ATOM   4514 C  CG  . GLU C 1 176 ? 37.972 -7.466  -37.527 1.00 35.52  ?  171 GLU A CG  1 
ATOM   4515 C  CD  . GLU C 1 176 ? 37.737 -8.964  -37.363 1.00 46.00  ?  171 GLU A CD  1 
ATOM   4516 O  OE1 . GLU C 1 176 ? 38.704 -9.670  -37.010 1.00 47.26  ?  171 GLU A OE1 1 
ATOM   4517 O  OE2 . GLU C 1 176 ? 36.574 -9.424  -37.553 1.00 55.31  -1 171 GLU A OE2 1 
ATOM   4518 N  N   . ALA C 1 177 ? 37.068 -4.439  -34.098 1.00 20.87  ?  172 ALA A N   1 
ATOM   4519 C  CA  . ALA C 1 177 ? 37.166 -3.960  -32.706 1.00 22.32  ?  172 ALA A CA  1 
ATOM   4520 C  C   . ALA C 1 177 ? 36.196 -4.781  -31.872 1.00 24.45  ?  172 ALA A C   1 
ATOM   4521 O  O   . ALA C 1 177 ? 35.017 -4.943  -32.295 1.00 25.74  ?  172 ALA A O   1 
ATOM   4522 C  CB  . ALA C 1 177 ? 36.861 -2.496  -32.631 1.00 22.28  ?  172 ALA A CB  1 
ATOM   4523 N  N   . ASP C 1 178 ? 36.671 -5.294  -30.746 1.00 21.72  ?  173 ASP A N   1 
ATOM   4524 C  CA  . ASP C 1 178 ? 35.849 -6.145  -29.854 1.00 21.29  ?  173 ASP A CA  1 
ATOM   4525 C  C   . ASP C 1 178 ? 36.023 -5.616  -28.445 1.00 19.71  ?  173 ASP A C   1 
ATOM   4526 O  O   . ASP C 1 178 ? 37.163 -5.240  -28.096 1.00 18.03  ?  173 ASP A O   1 
ATOM   4527 C  CB  . ASP C 1 178 ? 36.291 -7.593  -29.925 1.00 22.93  ?  173 ASP A CB  1 
ATOM   4528 C  CG  . ASP C 1 178 ? 35.924 -8.159  -31.284 1.00 30.89  ?  173 ASP A CG  1 
ATOM   4529 O  OD1 . ASP C 1 178 ? 36.866 -8.384  -32.116 1.00 29.36  ?  173 ASP A OD1 1 
ATOM   4530 O  OD2 . ASP C 1 178 ? 34.677 -8.331  -31.503 1.00 27.60  -1 173 ASP A OD2 1 
ATOM   4531 N  N   . GLY C 1 179 ? 34.947 -5.648  -27.673 1.00 19.53  ?  174 GLY A N   1 
ATOM   4532 C  CA  . GLY C 1 179 ? 34.946 -5.075  -26.311 1.00 21.42  ?  174 GLY A CA  1 
ATOM   4533 C  C   . GLY C 1 179 ? 34.348 -6.062  -25.341 1.00 21.40  ?  174 GLY A C   1 
ATOM   4534 O  O   . GLY C 1 179 ? 33.151 -6.439  -25.558 1.00 21.00  ?  174 GLY A O   1 
ATOM   4535 N  N   . MET C 1 180 ? 35.122 -6.453  -24.325 1.00 19.10  ?  175 MET A N   1 
ATOM   4536 C  CA  . MET C 1 180 ? 34.634 -7.244  -23.167 1.00 18.08  ?  175 MET A CA  1 
ATOM   4537 C  C   . MET C 1 180 ? 34.314 -6.304  -22.006 1.00 18.68  ?  175 MET A C   1 
ATOM   4538 O  O   . MET C 1 180 ? 35.238 -5.704  -21.449 1.00 17.73  ?  175 MET A O   1 
ATOM   4539 C  CB  . MET C 1 180 ? 35.656 -8.281  -22.711 1.00 18.43  ?  175 MET A CB  1 
ATOM   4540 C  CG  . MET C 1 180 ? 35.235 -9.043  -21.484 1.00 19.74  ?  175 MET A CG  1 
ATOM   4541 S  SD  . MET C 1 180 ? 34.194 -10.470 -21.806 1.00 23.44  ?  175 MET A SD  1 
ATOM   4542 C  CE  . MET C 1 180 ? 35.397 -11.550 -22.612 1.00 18.37  ?  175 MET A CE  1 
ATOM   4543 N  N   . PHE C 1 181 ? 33.024 -6.151  -21.656 1.00 16.77  ?  176 PHE A N   1 
ATOM   4544 C  CA  . PHE C 1 181 ? 32.614 -5.361  -20.488 1.00 18.46  ?  176 PHE A CA  1 
ATOM   4545 C  C   . PHE C 1 181 ? 31.954 -6.310  -19.479 1.00 19.46  ?  176 PHE A C   1 
ATOM   4546 O  O   . PHE C 1 181 ? 30.710 -6.426  -19.436 1.00 19.11  ?  176 PHE A O   1 
ATOM   4547 C  CB  . PHE C 1 181 ? 31.757 -4.182  -20.939 1.00 21.05  ?  176 PHE A CB  1 
ATOM   4548 C  CG  . PHE C 1 181 ? 32.559 -3.179  -21.710 1.00 22.22  ?  176 PHE A CG  1 
ATOM   4549 C  CD1 . PHE C 1 181 ? 32.869 -3.404  -23.042 1.00 22.67  ?  176 PHE A CD1 1 
ATOM   4550 C  CD2 . PHE C 1 181 ? 33.082 -2.058  -21.076 1.00 24.20  ?  176 PHE A CD2 1 
ATOM   4551 C  CE1 . PHE C 1 181 ? 33.641 -2.492  -23.742 1.00 22.62  ?  176 PHE A CE1 1 
ATOM   4552 C  CE2 . PHE C 1 181 ? 33.864 -1.155  -21.781 1.00 21.63  ?  176 PHE A CE2 1 
ATOM   4553 C  CZ  . PHE C 1 181 ? 34.140 -1.373  -23.108 1.00 22.51  ?  176 PHE A CZ  1 
ATOM   4554 N  N   . LYS C 1 182 ? 32.788 -7.015  -18.728 1.00 17.42  ?  177 LYS A N   1 
ATOM   4555 C  CA  . LYS C 1 182 ? 32.349 -8.067  -17.773 1.00 16.37  ?  177 LYS A CA  1 
ATOM   4556 C  C   . LYS C 1 182 ? 32.082 -7.413  -16.410 1.00 15.70  ?  177 LYS A C   1 
ATOM   4557 O  O   . LYS C 1 182 ? 33.039 -7.129  -15.680 1.00 13.00  ?  177 LYS A O   1 
ATOM   4558 C  CB  . LYS C 1 182 ? 33.365 -9.191  -17.758 1.00 17.44  ?  177 LYS A CB  1 
ATOM   4559 C  CG  . LYS C 1 182 ? 33.002 -10.346 -16.864 1.00 18.25  ?  177 LYS A CG  1 
ATOM   4560 C  CD  . LYS C 1 182 ? 33.882 -11.564 -17.109 1.00 21.66  ?  177 LYS A CD  1 
ATOM   4561 C  CE  . LYS C 1 182 ? 33.830 -12.582 -15.993 1.00 24.60  ?  177 LYS A CE  1 
ATOM   4562 N  NZ  . LYS C 1 182 ? 32.524 -12.593 -15.297 1.00 28.39  ?  177 LYS A NZ  1 
ATOM   4563 N  N   . LEU C 1 183 ? 30.806 -7.092  -16.157 1.00 15.64  ?  178 LEU A N   1 
ATOM   4564 C  CA  . LEU C 1 183 ? 30.366 -6.154  -15.088 1.00 16.15  ?  178 LEU A CA  1 
ATOM   4565 C  C   . LEU C 1 183 ? 29.117 -6.714  -14.385 1.00 15.90  ?  178 LEU A C   1 
ATOM   4566 O  O   . LEU C 1 183 ? 28.253 -5.902  -14.015 1.00 16.23  ?  178 LEU A O   1 
ATOM   4567 C  CB  . LEU C 1 183 ? 30.097 -4.793  -15.722 1.00 16.48  ?  178 LEU A CB  1 
ATOM   4568 C  CG  . LEU C 1 183 ? 31.298 -4.078  -16.333 1.00 17.85  ?  178 LEU A CG  1 
ATOM   4569 C  CD1 . LEU C 1 183 ? 30.832 -2.837  -17.080 1.00 17.39  ?  178 LEU A CD1 1 
ATOM   4570 C  CD2 . LEU C 1 183 ? 32.316 -3.690  -15.265 1.00 17.98  ?  178 LEU A CD2 1 
ATOM   4571 N  N   . SER C 1 184 ? 29.098 -8.032  -14.187 1.00 16.00  ?  179 SER A N   1 
ATOM   4572 C  CA  . SER C 1 184 ? 28.115 -8.820  -13.399 1.00 18.32  ?  179 SER A CA  1 
ATOM   4573 C  C   . SER C 1 184 ? 26.749 -8.811  -14.103 1.00 19.21  ?  179 SER A C   1 
ATOM   4574 O  O   . SER C 1 184 ? 25.732 -9.043  -13.419 1.00 19.88  ?  179 SER A O   1 
ATOM   4575 C  CB  . SER C 1 184 ? 27.984 -8.301  -11.976 1.00 19.84  ?  179 SER A CB  1 
ATOM   4576 O  OG  . SER C 1 184 ? 29.215 -8.442  -11.247 1.00 18.64  ?  179 SER A OG  1 
ATOM   4577 N  N   . GLN C 1 185 ? 26.712 -8.604  -15.414 1.00 19.69  ?  180 GLN A N   1 
ATOM   4578 C  CA  . GLN C 1 185 ? 25.431 -8.628  -16.183 1.00 22.90  ?  180 GLN A CA  1 
ATOM   4579 C  C   . GLN C 1 185 ? 24.756 -9.996  -16.046 1.00 25.41  ?  180 GLN A C   1 
ATOM   4580 O  O   . GLN C 1 185 ? 23.503 -10.070 -16.166 1.00 25.70  ?  180 GLN A O   1 
ATOM   4581 C  CB  . GLN C 1 185 ? 25.643 -8.249  -17.644 1.00 21.44  ?  180 GLN A CB  1 
ATOM   4582 C  CG  . GLN C 1 185 ? 26.100 -6.814  -17.869 1.00 20.10  ?  180 GLN A CG  1 
ATOM   4583 C  CD  . GLN C 1 185 ? 27.607 -6.748  -18.017 1.00 19.74  ?  180 GLN A CD  1 
ATOM   4584 O  OE1 . GLN C 1 185 ? 28.332 -7.414  -17.281 1.00 18.88  ?  180 GLN A OE1 1 
ATOM   4585 N  NE2 . GLN C 1 185 ? 28.074 -5.964  -18.976 1.00 19.65  ?  180 GLN A NE2 1 
ATOM   4586 N  N   . GLU C 1 186 ? 25.524 -11.051 -15.769 1.00 23.26  ?  181 GLU A N   1 
ATOM   4587 C  CA  . GLU C 1 186 ? 25.004 -12.436 -15.747 1.00 25.51  ?  181 GLU A CA  1 
ATOM   4588 C  C   . GLU C 1 186 ? 24.216 -12.660 -14.450 1.00 24.59  ?  181 GLU A C   1 
ATOM   4589 O  O   . GLU C 1 186 ? 23.535 -13.680 -14.356 1.00 24.69  ?  181 GLU A O   1 
ATOM   4590 C  CB  . GLU C 1 186 ? 26.160 -13.434 -15.860 1.00 26.57  ?  181 GLU A CB  1 
ATOM   4591 C  CG  . GLU C 1 186 ? 26.901 -13.708 -14.543 1.00 28.30  ?  181 GLU A CG  1 
ATOM   4592 C  CD  . GLU C 1 186 ? 27.919 -12.669 -14.090 1.00 26.49  ?  181 GLU A CD  1 
ATOM   4593 O  OE1 . GLU C 1 186 ? 28.094 -11.667 -14.824 1.00 24.16  ?  181 GLU A OE1 1 
ATOM   4594 O  OE2 . GLU C 1 186 ? 28.561 -12.889 -13.024 1.00 26.98  -1 181 GLU A OE2 1 
ATOM   4595 N  N   . GLN C 1 187 ? 24.405 -11.808 -13.443 1.00 23.51  ?  182 GLN A N   1 
ATOM   4596 C  CA  . GLN C 1 187 ? 23.798 -11.970 -12.093 1.00 22.58  ?  182 GLN A CA  1 
ATOM   4597 C  C   . GLN C 1 187 ? 22.359 -11.445 -12.135 1.00 23.29  ?  182 GLN A C   1 
ATOM   4598 O  O   . GLN C 1 187 ? 22.084 -10.577 -12.980 1.00 22.08  ?  182 GLN A O   1 
ATOM   4599 C  CB  . GLN C 1 187 ? 24.609 -11.188 -11.043 1.00 22.66  ?  182 GLN A CB  1 
ATOM   4600 C  CG  . GLN C 1 187 ? 25.979 -11.765 -10.705 1.00 22.31  ?  182 GLN A CG  1 
ATOM   4601 C  CD  . GLN C 1 187 ? 25.932 -13.240 -10.390 1.00 24.39  ?  182 GLN A CD  1 
ATOM   4602 O  OE1 . GLN C 1 187 ? 25.230 -13.682 -9.475  1.00 27.31  ?  182 GLN A OE1 1 
ATOM   4603 N  NE2 . GLN C 1 187 ? 26.651 -14.043 -11.162 1.00 26.46  ?  182 GLN A NE2 1 
ATOM   4604 N  N   . GLN C 1 188 ? 21.512 -11.862 -11.188 1.00 25.49  ?  183 GLN A N   1 
ATOM   4605 C  CA  . GLN C 1 188 ? 20.167 -11.248 -10.985 1.00 28.41  ?  183 GLN A CA  1 
ATOM   4606 C  C   . GLN C 1 188 ? 20.351 -9.774  -10.606 1.00 29.28  ?  183 GLN A C   1 
ATOM   4607 O  O   . GLN C 1 188 ? 21.361 -9.417  -9.996  1.00 27.44  ?  183 GLN A O   1 
ATOM   4608 C  CB  . GLN C 1 188 ? 19.373 -12.042 -9.944  1.00 30.18  ?  183 GLN A CB  1 
ATOM   4609 C  CG  . GLN C 1 188 ? 18.913 -13.403 -10.429 1.00 35.27  ?  183 GLN A CG  1 
ATOM   4610 C  CD  . GLN C 1 188 ? 17.969 -13.282 -11.606 1.00 38.46  ?  183 GLN A CD  1 
ATOM   4611 O  OE1 . GLN C 1 188 ? 18.282 -13.689 -12.724 1.00 44.59  ?  183 GLN A OE1 1 
ATOM   4612 N  NE2 . GLN C 1 188 ? 16.828 -12.648 -11.389 1.00 42.09  ?  183 GLN A NE2 1 
ATOM   4613 N  N   . PRO C 1 189 ? 19.402 -8.868  -10.956 1.00 28.47  ?  184 PRO A N   1 
ATOM   4614 C  CA  . PRO C 1 189 ? 19.562 -7.429  -10.709 1.00 30.40  ?  184 PRO A CA  1 
ATOM   4615 C  C   . PRO C 1 189 ? 19.853 -7.013  -9.254  1.00 31.37  ?  184 PRO A C   1 
ATOM   4616 O  O   . PRO C 1 189 ? 20.684 -6.127  -9.049  1.00 33.74  ?  184 PRO A O   1 
ATOM   4617 C  CB  . PRO C 1 189 ? 18.211 -6.834  -11.155 1.00 30.36  ?  184 PRO A CB  1 
ATOM   4618 C  CG  . PRO C 1 189 ? 17.696 -7.829  -12.164 1.00 30.08  ?  184 PRO A CG  1 
ATOM   4619 C  CD  . PRO C 1 189 ? 18.101 -9.172  -11.598 1.00 31.69  ?  184 PRO A CD  1 
ATOM   4620 N  N   . ALA C 1 190 ? 19.205 -7.641  -8.268  1.00 31.47  ?  185 ALA A N   1 
ATOM   4621 C  CA  . ALA C 1 190 ? 19.485 -7.413  -6.831  1.00 29.77  ?  185 ALA A CA  1 
ATOM   4622 C  C   . ALA C 1 190 ? 20.961 -7.736  -6.495  1.00 27.08  ?  185 ALA A C   1 
ATOM   4623 O  O   . ALA C 1 190 ? 21.551 -7.031  -5.650  1.00 25.38  ?  185 ALA A O   1 
ATOM   4624 C  CB  . ALA C 1 190 ? 18.532 -8.224  -6.001  1.00 32.19  ?  185 ALA A CB  1 
ATOM   4625 N  N   . ILE C 1 191 ? 21.542 -8.761  -7.107  1.00 23.74  ?  186 ILE A N   1 
ATOM   4626 C  CA  . ILE C 1 191 ? 22.948 -9.198  -6.828  1.00 25.55  ?  186 ILE A CA  1 
ATOM   4627 C  C   . ILE C 1 191 ? 23.909 -8.205  -7.504  1.00 24.44  ?  186 ILE A C   1 
ATOM   4628 O  O   . ILE C 1 191 ? 24.932 -7.833  -6.860  1.00 20.87  ?  186 ILE A O   1 
ATOM   4629 C  CB  . ILE C 1 191 ? 23.212 -10.648 -7.292  1.00 27.86  ?  186 ILE A CB  1 
ATOM   4630 C  CG1 . ILE C 1 191 ? 22.108 -11.625 -6.873  1.00 30.11  ?  186 ILE A CG1 1 
ATOM   4631 C  CG2 . ILE C 1 191 ? 24.586 -11.115 -6.836  1.00 24.90  ?  186 ILE A CG2 1 
ATOM   4632 C  CD1 . ILE C 1 191 ? 21.839 -11.632 -5.401  1.00 31.60  ?  186 ILE A CD1 1 
ATOM   4633 N  N   . ARG C 1 192 ? 23.589 -7.767  -8.729  1.00 21.70  ?  187 ARG A N   1 
ATOM   4634 C  CA  . ARG C 1 192 ? 24.383 -6.761  -9.488  1.00 23.52  ?  187 ARG A CA  1 
ATOM   4635 C  C   . ARG C 1 192 ? 24.452 -5.480  -8.665  1.00 23.40  ?  187 ARG A C   1 
ATOM   4636 O  O   . ARG C 1 192 ? 25.531 -4.819  -8.579  1.00 19.03  ?  187 ARG A O   1 
ATOM   4637 C  CB  . ARG C 1 192 ? 23.756 -6.366  -10.825 1.00 26.81  ?  187 ARG A CB  1 
ATOM   4638 C  CG  . ARG C 1 192 ? 23.554 -7.504  -11.809 1.00 32.01  ?  187 ARG A CG  1 
ATOM   4639 C  CD  . ARG C 1 192 ? 23.226 -6.922  -13.184 1.00 37.33  ?  187 ARG A CD  1 
ATOM   4640 N  NE  . ARG C 1 192 ? 22.264 -7.768  -13.862 1.00 47.08  ?  187 ARG A NE  1 
ATOM   4641 C  CZ  . ARG C 1 192 ? 21.099 -7.369  -14.374 1.00 53.70  ?  187 ARG A CZ  1 
ATOM   4642 N  NH1 . ARG C 1 192 ? 20.736 -6.095  -14.336 1.00 52.51  ?  187 ARG A NH1 1 
ATOM   4643 N  NH2 . ARG C 1 192 ? 20.306 -8.261  -14.945 1.00 54.70  ?  187 ARG A NH2 1 
ATOM   4644 N  N   . ARG C 1 193 ? 23.325 -5.122  -8.061  1.00 22.28  ?  188 ARG A N   1 
ATOM   4645 C  CA  . ARG C 1 193 ? 23.258 -3.938  -7.170  1.00 23.44  ?  188 ARG A CA  1 
ATOM   4646 C  C   . ARG C 1 193 ? 24.147 -4.168  -5.937  1.00 19.86  ?  188 ARG A C   1 
ATOM   4647 O  O   . ARG C 1 193 ? 24.798 -3.193  -5.531  1.00 19.70  ?  188 ARG A O   1 
ATOM   4648 C  CB  . ARG C 1 193 ? 21.795 -3.698  -6.801  1.00 27.27  ?  188 ARG A CB  1 
ATOM   4649 C  CG  . ARG C 1 193 ? 21.498 -2.322  -6.239  1.00 33.58  ?  188 ARG A CG  1 
ATOM   4650 C  CD  . ARG C 1 193 ? 20.042 -2.275  -5.769  1.00 39.18  ?  188 ARG A CD  1 
ATOM   4651 N  NE  . ARG C 1 193 ? 19.726 -1.069  -5.005  1.00 42.93  ?  188 ARG A NE  1 
ATOM   4652 C  CZ  . ARG C 1 193 ? 19.538 -0.996  -3.683  1.00 48.86  ?  188 ARG A CZ  1 
ATOM   4653 N  NH1 . ARG C 1 193 ? 19.636 -2.067  -2.909  1.00 52.04  ?  188 ARG A NH1 1 
ATOM   4654 N  NH2 . ARG C 1 193 ? 19.258 0.176   -3.134  1.00 49.94  ?  188 ARG A NH2 1 
ATOM   4655 N  N   . ARG C 1 194 ? 24.171 -5.369  -5.335  1.00 19.30  ?  189 ARG A N   1 
ATOM   4656 C  CA  . ARG C 1 194 ? 25.066 -5.620  -4.174  1.00 19.88  ?  189 ARG A CA  1 
ATOM   4657 C  C   . ARG C 1 194 ? 26.541 -5.457  -4.595  1.00 19.17  ?  189 ARG A C   1 
ATOM   4658 O  O   . ARG C 1 194 ? 27.335 -4.887  -3.817  1.00 20.64  ?  189 ARG A O   1 
ATOM   4659 C  CB  . ARG C 1 194 ? 24.851 -6.996  -3.547  1.00 22.03  ?  189 ARG A CB  1 
ATOM   4660 C  CG  . ARG C 1 194 ? 23.530 -7.139  -2.830  1.00 23.40  ?  189 ARG A CG  1 
ATOM   4661 C  CD  . ARG C 1 194 ? 23.203 -8.603  -2.624  1.00 25.39  ?  189 ARG A CD  1 
ATOM   4662 N  NE  . ARG C 1 194 ? 21.873 -8.658  -2.049  1.00 26.20  ?  189 ARG A NE  1 
ATOM   4663 C  CZ  . ARG C 1 194 ? 21.228 -9.747  -1.661  1.00 30.91  ?  189 ARG A CZ  1 
ATOM   4664 N  NH1 . ARG C 1 194 ? 21.781 -10.947 -1.744  1.00 30.78  ?  189 ARG A NH1 1 
ATOM   4665 N  NH2 . ARG C 1 194 ? 19.997 -9.623  -1.189  1.00 34.54  ?  189 ARG A NH2 1 
ATOM   4666 N  N   . VAL C 1 195 ? 26.916 -5.907  -5.781  1.00 18.44  ?  190 VAL A N   1 
ATOM   4667 C  CA  . VAL C 1 195 ? 28.322 -5.815  -6.260  1.00 17.63  ?  190 VAL A CA  1 
ATOM   4668 C  C   . VAL C 1 195 ? 28.661 -4.334  -6.522  1.00 18.61  ?  190 VAL A C   1 
ATOM   4669 O  O   . VAL C 1 195 ? 29.742 -3.866  -6.117  1.00 16.57  ?  190 VAL A O   1 
ATOM   4670 C  CB  . VAL C 1 195 ? 28.529 -6.685  -7.518  1.00 19.87  ?  190 VAL A CB  1 
ATOM   4671 C  CG1 . VAL C 1 195 ? 29.889 -6.466  -8.134  1.00 18.28  ?  190 VAL A CG1 1 
ATOM   4672 C  CG2 . VAL C 1 195 ? 28.301 -8.151  -7.256  1.00 20.40  ?  190 VAL A CG2 1 
ATOM   4673 N  N   . ARG C 1 196 ? 27.753 -3.572  -7.138  1.00 17.78  ?  191 ARG A N   1 
ATOM   4674 C  CA  . ARG C 1 196 ? 27.966 -2.129  -7.435  1.00 19.10  ?  191 ARG A CA  1 
ATOM   4675 C  C   . ARG C 1 196 ? 28.100 -1.330  -6.138  1.00 18.43  ?  191 ARG A C   1 
ATOM   4676 O  O   . ARG C 1 196 ? 29.095 -0.573  -6.041  1.00 21.10  ?  191 ARG A O   1 
ATOM   4677 C  CB  . ARG C 1 196 ? 26.827 -1.572  -8.310  1.00 20.17  ?  191 ARG A CB  1 
ATOM   4678 C  CG  . ARG C 1 196 ? 26.917 -0.086  -8.620  1.00 22.71  ?  191 ARG A CG  1 
ATOM   4679 C  CD  . ARG C 1 196 ? 25.828 0.321   -9.602  1.00 26.70  ?  191 ARG A CD  1 
ATOM   4680 N  NE  . ARG C 1 196 ? 24.460 0.065   -9.104  1.00 31.12  ?  191 ARG A NE  1 
ATOM   4681 C  CZ  . ARG C 1 196 ? 23.732 0.878   -8.312  1.00 33.20  ?  191 ARG A CZ  1 
ATOM   4682 N  NH1 . ARG C 1 196 ? 24.217 2.018   -7.866  1.00 32.95  ?  191 ARG A NH1 1 
ATOM   4683 N  NH2 . ARG C 1 196 ? 22.503 0.543   -7.964  1.00 34.39  ?  191 ARG A NH2 1 
ATOM   4684 N  N   . HIS C 1 197 ? 27.194 -1.475  -5.163  1.00 19.96  ?  192 HIS A N   1 
ATOM   4685 C  CA  . HIS C 1 197 ? 27.333 -0.835  -3.821  1.00 21.17  ?  192 HIS A CA  1 
ATOM   4686 C  C   . HIS C 1 197 ? 28.650 -1.237  -3.132  1.00 19.14  ?  192 HIS A C   1 
ATOM   4687 O  O   . HIS C 1 197 ? 29.365 -0.338  -2.706  1.00 22.60  ?  192 HIS A O   1 
ATOM   4688 C  CB  . HIS C 1 197 ? 26.113 -1.054  -2.925  1.00 23.47  ?  192 HIS A CB  1 
ATOM   4689 C  CG  . HIS C 1 197 ? 24.948 -0.280  -3.413  1.00 22.83  ?  192 HIS A CG  1 
ATOM   4690 N  ND1 . HIS C 1 197 ? 25.094 0.956   -3.979  1.00 27.02  ?  192 HIS A ND1 1 
ATOM   4691 C  CD2 . HIS C 1 197 ? 23.639 -0.589  -3.516  1.00 25.08  ?  192 HIS A CD2 1 
ATOM   4692 C  CE1 . HIS C 1 197 ? 23.921 1.394   -4.406  1.00 27.37  ?  192 HIS A CE1 1 
ATOM   4693 N  NE2 . HIS C 1 197 ? 23.024 0.473   -4.154  1.00 26.01  ?  192 HIS A NE2 1 
ATOM   4694 N  N   . SER C 1 198 ? 28.985 -2.505  -3.056  1.00 19.94  ?  193 SER A N   1 
ATOM   4695 C  CA  . SER C 1 198 ? 30.296 -2.993  -2.543  1.00 21.07  ?  193 SER A CA  1 
ATOM   4696 C  C   . SER C 1 198 ? 31.449 -2.250  -3.216  1.00 22.45  ?  193 SER A C   1 
ATOM   4697 O  O   . SER C 1 198 ? 32.251 -1.623  -2.504  1.00 22.67  ?  193 SER A O   1 
ATOM   4698 C  CB  . SER C 1 198 ? 30.472 -4.460  -2.727  1.00 22.41  ?  193 SER A CB  1 
ATOM   4699 O  OG  . SER C 1 198 ? 31.584 -4.908  -1.960  1.00 25.56  ?  193 SER A OG  1 
ATOM   4700 N  N   . PHE C 1 199 ? 31.547 -2.310  -4.527  1.00 18.57  ?  194 PHE A N   1 
ATOM   4701 C  CA  . PHE C 1 199 ? 32.711 -1.748  -5.254  1.00 18.66  ?  194 PHE A CA  1 
ATOM   4702 C  C   . PHE C 1 199 ? 32.741 -0.231  -5.061  1.00 18.33  ?  194 PHE A C   1 
ATOM   4703 O  O   . PHE C 1 199 ? 33.823 0.385   -5.203  1.00 13.89  ?  194 PHE A O   1 
ATOM   4704 C  CB  . PHE C 1 199 ? 32.728 -2.172  -6.727  1.00 18.01  ?  194 PHE A CB  1 
ATOM   4705 C  CG  . PHE C 1 199 ? 33.139 -3.601  -6.989  1.00 18.42  ?  194 PHE A CG  1 
ATOM   4706 C  CD1 . PHE C 1 199 ? 33.834 -4.342  -6.041  1.00 21.47  ?  194 PHE A CD1 1 
ATOM   4707 C  CD2 . PHE C 1 199 ? 32.915 -4.190  -8.213  1.00 20.33  ?  194 PHE A CD2 1 
ATOM   4708 C  CE1 . PHE C 1 199 ? 34.271 -5.637  -6.309  1.00 20.89  ?  194 PHE A CE1 1 
ATOM   4709 C  CE2 . PHE C 1 199 ? 33.302 -5.507  -8.452  1.00 18.20  ?  194 PHE A CE2 1 
ATOM   4710 C  CZ  . PHE C 1 199 ? 33.977 -6.227  -7.503  1.00 17.12  ?  194 PHE A CZ  1 
ATOM   4711 N  N   . GLY C 1 200 ? 31.597 0.363   -4.692  1.00 17.16  ?  195 GLY A N   1 
ATOM   4712 C  CA  . GLY C 1 200 ? 31.493 1.819   -4.488  1.00 18.65  ?  195 GLY A CA  1 
ATOM   4713 C  C   . GLY C 1 200 ? 32.117 2.308   -3.187  1.00 19.29  ?  195 GLY A C   1 
ATOM   4714 O  O   . GLY C 1 200 ? 32.273 3.530   -3.047  1.00 19.43  ?  195 GLY A O   1 
ATOM   4715 N  N   . GLY C 1 201 ? 32.498 1.400   -2.296  1.00 20.38  ?  196 GLY A N   1 
ATOM   4716 C  CA  . GLY C 1 201 ? 32.947 1.688   -0.921  1.00 20.82  ?  196 GLY A CA  1 
ATOM   4717 C  C   . GLY C 1 201 ? 34.459 1.709   -0.769  1.00 21.47  ?  196 GLY A C   1 
ATOM   4718 O  O   . GLY C 1 201 ? 34.913 1.875   0.386   1.00 24.21  ?  196 GLY A O   1 
ATOM   4719 N  N   . ALA C 1 202 ? 35.215 1.523   -1.859  1.00 18.98  ?  197 ALA A N   1 
ATOM   4720 C  CA  . ALA C 1 202 ? 36.692 1.639   -1.883  1.00 20.02  ?  197 ALA A CA  1 
ATOM   4721 C  C   . ALA C 1 202 ? 37.185 2.261   -3.189  1.00 21.10  ?  197 ALA A C   1 
ATOM   4722 O  O   . ALA C 1 202 ? 36.679 1.930   -4.284  1.00 19.00  ?  197 ALA A O   1 
ATOM   4723 C  CB  . ALA C 1 202 ? 37.331 0.279   -1.714  1.00 22.57  ?  197 ALA A CB  1 
ATOM   4724 N  N   . GLU C 1 203 ? 38.243 3.069   -3.102  1.00 20.90  ?  198 GLU A N   1 
ATOM   4725 C  CA  . GLU C 1 203 ? 38.767 3.803   -4.272  1.00 22.26  ?  198 GLU A CA  1 
ATOM   4726 C  C   . GLU C 1 203 ? 39.241 2.788   -5.328  1.00 19.57  ?  198 GLU A C   1 
ATOM   4727 O  O   . GLU C 1 203 ? 39.016 3.049   -6.486  1.00 18.26  ?  198 GLU A O   1 
ATOM   4728 C  CB  . GLU C 1 203 ? 39.875 4.760   -3.850  1.00 21.25  ?  198 GLU A CB  1 
ATOM   4729 C  CG  . GLU C 1 203 ? 40.325 5.680   -4.962  1.00 25.06  ?  198 GLU A CG  1 
ATOM   4730 C  CD  . GLU C 1 203 ? 39.260 6.546   -5.621  1.00 29.89  ?  198 GLU A CD  1 
ATOM   4731 O  OE1 . GLU C 1 203 ? 38.085 6.568   -5.143  1.00 27.44  ?  198 GLU A OE1 1 
ATOM   4732 O  OE2 . GLU C 1 203 ? 39.599 7.163   -6.643  1.00 28.75  -1 198 GLU A OE2 1 
ATOM   4733 N  N   . ALA C 1 204 ? 39.848 1.685   -4.912  1.00 19.44  ?  199 ALA A N   1 
ATOM   4734 C  CA  . ALA C 1 204 ? 40.395 0.609   -5.773  1.00 20.90  ?  199 ALA A CA  1 
ATOM   4735 C  C   . ALA C 1 204 ? 39.336 0.099   -6.773  1.00 21.69  ?  199 ALA A C   1 
ATOM   4736 O  O   . ALA C 1 204 ? 39.683 -0.312  -7.876  1.00 24.88  ?  199 ALA A O   1 
ATOM   4737 C  CB  . ALA C 1 204 ? 40.875 -0.514  -4.904  1.00 22.44  ?  199 ALA A CB  1 
ATOM   4738 N  N   . THR C 1 205 ? 38.082 0.080   -6.368  1.00 18.67  ?  200 THR A N   1 
ATOM   4739 C  CA  . THR C 1 205 ? 37.007 -0.615  -7.129  1.00 19.51  ?  200 THR A CA  1 
ATOM   4740 C  C   . THR C 1 205 ? 35.989 0.399   -7.655  1.00 16.51  ?  200 THR A C   1 
ATOM   4741 O  O   . THR C 1 205 ? 35.055 -0.033  -8.334  1.00 18.37  ?  200 THR A O   1 
ATOM   4742 C  CB  . THR C 1 205 ? 36.410 -1.722  -6.251  1.00 17.18  ?  200 THR A CB  1 
ATOM   4743 O  OG1 . THR C 1 205 ? 35.950 -1.115  -5.052  1.00 18.16  ?  200 THR A OG1 1 
ATOM   4744 C  CG2 . THR C 1 205 ? 37.389 -2.834  -5.902  1.00 16.28  ?  200 THR A CG2 1 
ATOM   4745 N  N   . ARG C 1 206 ? 36.176 1.684   -7.375  1.00 18.12  ?  201 ARG A N   1 
ATOM   4746 C  CA  . ARG C 1 206 ? 35.190 2.728   -7.666  1.00 21.19  ?  201 ARG A CA  1 
ATOM   4747 C  C   . ARG C 1 206 ? 34.957 2.836   -9.183  1.00 19.15  ?  201 ARG A C   1 
ATOM   4748 O  O   . ARG C 1 206 ? 33.762 2.977   -9.585  1.00 16.12  ?  201 ARG A O   1 
ATOM   4749 C  CB  . ARG C 1 206 ? 35.586 4.069   -7.044  1.00 20.13  ?  201 ARG A CB  1 
ATOM   4750 C  CG  . ARG C 1 206 ? 34.479 5.094   -7.289  1.00 23.15  ?  201 ARG A CG  1 
ATOM   4751 C  CD  . ARG C 1 206 ? 34.453 6.281   -6.368  1.00 24.86  ?  201 ARG A CD  1 
ATOM   4752 N  NE  . ARG C 1 206 ? 35.667 7.055   -6.525  1.00 28.85  ?  201 ARG A NE  1 
ATOM   4753 C  CZ  . ARG C 1 206 ? 35.868 7.998   -7.446  1.00 35.38  ?  201 ARG A CZ  1 
ATOM   4754 N  NH1 . ARG C 1 206 ? 34.939 8.268   -8.352  1.00 37.08  ?  201 ARG A NH1 1 
ATOM   4755 N  NH2 . ARG C 1 206 ? 37.018 8.659   -7.472  1.00 39.93  ?  201 ARG A NH2 1 
ATOM   4756 N  N   . ALA C 1 207 ? 36.011 2.749   -10.005 1.00 17.49  ?  202 ALA A N   1 
ATOM   4757 C  CA  . ALA C 1 207 ? 35.897 2.859   -11.482 1.00 20.48  ?  202 ALA A CA  1 
ATOM   4758 C  C   . ALA C 1 207 ? 35.050 1.698   -12.004 1.00 19.26  ?  202 ALA A C   1 
ATOM   4759 O  O   . ALA C 1 207 ? 34.265 1.924   -12.927 1.00 19.64  ?  202 ALA A O   1 
ATOM   4760 C  CB  . ALA C 1 207 ? 37.258 2.911   -12.116 1.00 20.11  ?  202 ALA A CB  1 
ATOM   4761 N  N   . VAL C 1 208 ? 35.177 0.493   -11.430 1.00 19.88  ?  203 VAL A N   1 
ATOM   4762 C  CA  . VAL C 1 208 ? 34.304 -0.651  -11.816 1.00 21.56  ?  203 VAL A CA  1 
ATOM   4763 C  C   . VAL C 1 208 ? 32.856 -0.288  -11.459 1.00 17.32  ?  203 VAL A C   1 
ATOM   4764 O  O   . VAL C 1 208 ? 31.982 -0.515  -12.263 1.00 16.84  ?  203 VAL A O   1 
ATOM   4765 C  CB  . VAL C 1 208 ? 34.720 -1.996  -11.191 1.00 18.41  ?  203 VAL A CB  1 
ATOM   4766 C  CG1 . VAL C 1 208 ? 33.685 -3.046  -11.566 1.00 20.75  ?  203 VAL A CG1 1 
ATOM   4767 C  CG2 . VAL C 1 208 ? 36.102 -2.395  -11.687 1.00 19.98  ?  203 VAL A CG2 1 
ATOM   4768 N  N   . ALA C 1 209 ? 32.619 0.246   -10.269 1.00 17.63  ?  204 ALA A N   1 
ATOM   4769 C  CA  . ALA C 1 209 ? 31.247 0.617   -9.824  1.00 17.68  ?  204 ALA A CA  1 
ATOM   4770 C  C   . ALA C 1 209 ? 30.672 1.659   -10.792 1.00 19.14  ?  204 ALA A C   1 
ATOM   4771 O  O   . ALA C 1 209 ? 29.473 1.514   -11.156 1.00 19.25  ?  204 ALA A O   1 
ATOM   4772 C  CB  . ALA C 1 209 ? 31.259 1.097   -8.382  1.00 18.25  ?  204 ALA A CB  1 
ATOM   4773 N  N   . GLY C 1 210 ? 31.490 2.627   -11.242 1.00 20.69  ?  205 GLY A N   1 
ATOM   4774 C  CA  . GLY C 1 210 ? 31.087 3.709   -12.179 1.00 22.38  ?  205 GLY A CA  1 
ATOM   4775 C  C   . GLY C 1 210 ? 30.504 3.148   -13.486 1.00 22.43  ?  205 GLY A C   1 
ATOM   4776 O  O   . GLY C 1 210 ? 29.366 3.590   -14.010 1.00 19.35  ?  205 GLY A O   1 
ATOM   4777 N  N   . LEU C 1 211 ? 31.222 2.169   -14.038 1.00 21.66  ?  206 LEU A N   1 
ATOM   4778 C  CA  . LEU C 1 211 ? 30.814 1.497   -15.288 1.00 19.43  ?  206 LEU A CA  1 
ATOM   4779 C  C   . LEU C 1 211 ? 29.539 0.729   -15.001 1.00 21.06  ?  206 LEU A C   1 
ATOM   4780 O  O   . LEU C 1 211 ? 28.596 0.838   -15.804 1.00 20.05  ?  206 LEU A O   1 
ATOM   4781 C  CB  . LEU C 1 211 ? 31.945 0.602   -15.816 1.00 20.22  ?  206 LEU A CB  1 
ATOM   4782 C  CG  . LEU C 1 211 ? 33.174 1.343   -16.362 1.00 20.01  ?  206 LEU A CG  1 
ATOM   4783 C  CD1 . LEU C 1 211 ? 34.257 0.343   -16.681 1.00 22.45  ?  206 LEU A CD1 1 
ATOM   4784 C  CD2 . LEU C 1 211 ? 32.861 2.139   -17.604 1.00 22.52  ?  206 LEU A CD2 1 
ATOM   4785 N  N   . MET C 1 212 ? 29.470 0.018   -13.873 1.00 18.47  ?  207 MET A N   1 
ATOM   4786 C  CA  . MET C 1 212 ? 28.261 -0.748  -13.546 1.00 17.86  ?  207 MET A CA  1 
ATOM   4787 C  C   . MET C 1 212 ? 27.064 0.208   -13.407 1.00 20.36  ?  207 MET A C   1 
ATOM   4788 O  O   . MET C 1 212 ? 25.925 -0.177  -13.770 1.00 20.09  ?  207 MET A O   1 
ATOM   4789 C  CB  . MET C 1 212 ? 28.455 -1.552  -12.271 1.00 18.26  ?  207 MET A CB  1 
ATOM   4790 C  CG  . MET C 1 212 ? 29.453 -2.697  -12.397 1.00 17.52  ?  207 MET A CG  1 
ATOM   4791 S  SD  . MET C 1 212 ? 29.770 -3.569  -10.847 1.00 18.36  ?  207 MET A SD  1 
ATOM   4792 C  CE  . MET C 1 212 ? 28.329 -4.633  -10.799 1.00 19.12  ?  207 MET A CE  1 
ATOM   4793 N  N   . ASP C 1 213 ? 27.296 1.409   -12.897 1.00 22.57  ?  208 ASP A N   1 
ATOM   4794 C  CA  . ASP C 1 213 ? 26.236 2.422   -12.679 1.00 26.26  ?  208 ASP A CA  1 
ATOM   4795 C  C   . ASP C 1 213 ? 25.783 2.980   -14.032 1.00 25.32  ?  208 ASP A C   1 
ATOM   4796 O  O   . ASP C 1 213 ? 24.656 3.456   -14.077 1.00 27.50  ?  208 ASP A O   1 
ATOM   4797 C  CB  . ASP C 1 213 ? 26.697 3.522   -11.706 1.00 30.21  ?  208 ASP A CB  1 
ATOM   4798 C  CG  . ASP C 1 213 ? 25.533 4.300   -11.095 1.00 39.06  ?  208 ASP A CG  1 
ATOM   4799 O  OD1 . ASP C 1 213 ? 24.539 3.648   -10.694 1.00 40.03  ?  208 ASP A OD1 1 
ATOM   4800 O  OD2 . ASP C 1 213 ? 25.618 5.558   -11.022 1.00 48.49  -1 208 ASP A OD2 1 
ATOM   4801 N  N   . ARG C 1 214 ? 26.628 2.991   -15.062 1.00 22.68  ?  209 ARG A N   1 
ATOM   4802 C  CA  . ARG C 1 214 ? 26.335 3.586   -16.381 1.00 26.36  ?  209 ARG A CA  1 
ATOM   4803 C  C   . ARG C 1 214 ? 25.617 2.544   -17.244 1.00 28.06  ?  209 ARG A C   1 
ATOM   4804 O  O   . ARG C 1 214 ? 25.251 2.920   -18.368 1.00 33.61  ?  209 ARG A O   1 
ATOM   4805 C  CB  . ARG C 1 214 ? 27.615 4.151   -17.027 1.00 29.34  ?  209 ARG A CB  1 
ATOM   4806 C  CG  . ARG C 1 214 ? 28.098 5.429   -16.366 1.00 30.92  ?  209 ARG A CG  1 
ATOM   4807 C  CD  . ARG C 1 214 ? 29.226 6.231   -17.001 1.00 37.27  ?  209 ARG A CD  1 
ATOM   4808 N  NE  . ARG C 1 214 ? 30.564 5.614   -16.989 1.00 42.08  ?  209 ARG A NE  1 
ATOM   4809 C  CZ  . ARG C 1 214 ? 31.407 5.565   -15.951 1.00 42.35  ?  209 ARG A CZ  1 
ATOM   4810 N  NH1 . ARG C 1 214 ? 31.070 6.091   -14.784 1.00 43.05  ?  209 ARG A NH1 1 
ATOM   4811 N  NH2 . ARG C 1 214 ? 32.601 4.994   -16.079 1.00 35.94  ?  209 ARG A NH2 1 
ATOM   4812 N  N   . LEU C 1 215 ? 25.449 1.290   -16.778 1.00 27.15  ?  210 LEU A N   1 
ATOM   4813 C  CA  . LEU C 1 215 ? 24.825 0.189   -17.561 1.00 29.99  ?  210 LEU A CA  1 
ATOM   4814 C  C   . LEU C 1 215 ? 23.318 0.416   -17.640 1.00 34.77  ?  210 LEU A C   1 
ATOM   4815 O  O   . LEU C 1 215 ? 22.693 0.713   -16.635 1.00 32.19  ?  210 LEU A O   1 
ATOM   4816 C  CB  . LEU C 1 215 ? 25.083 -1.172  -16.914 1.00 30.15  ?  210 LEU A CB  1 
ATOM   4817 C  CG  . LEU C 1 215 ? 26.481 -1.760  -17.084 1.00 28.63  ?  210 LEU A CG  1 
ATOM   4818 C  CD1 . LEU C 1 215 ? 26.582 -3.058  -16.304 1.00 29.06  ?  210 LEU A CD1 1 
ATOM   4819 C  CD2 . LEU C 1 215 ? 26.832 -1.985  -18.549 1.00 30.93  ?  210 LEU A CD2 1 
ATOM   4820 N  N   . PRO C 1 216 ? 22.671 0.160   -18.796 1.00 37.49  ?  211 PRO A N   1 
ATOM   4821 C  CA  . PRO C 1 216 ? 21.280 0.588   -19.011 1.00 40.94  ?  211 PRO A CA  1 
ATOM   4822 C  C   . PRO C 1 216 ? 20.291 0.125   -17.923 1.00 37.63  ?  211 PRO A C   1 
ATOM   4823 O  O   . PRO C 1 216 ? 20.382 -1.025  -17.506 1.00 39.89  ?  211 PRO A O   1 
ATOM   4824 C  CB  . PRO C 1 216 ? 20.917 -0.042  -20.371 1.00 39.31  ?  211 PRO A CB  1 
ATOM   4825 C  CG  . PRO C 1 216 ? 21.947 -1.151  -20.577 1.00 39.78  ?  211 PRO A CG  1 
ATOM   4826 C  CD  . PRO C 1 216 ? 23.203 -0.639  -19.907 1.00 39.29  ?  211 PRO A CD  1 
ATOM   4827 N  N   . ALA D 1 5   ? 62.941 -13.351 -25.583 1.00 27.95  ?  0   ALA C N   1 
ATOM   4828 C  CA  . ALA D 1 5   ? 61.589 -13.311 -26.246 1.00 28.25  ?  0   ALA C CA  1 
ATOM   4829 C  C   . ALA D 1 5   ? 60.798 -12.083 -25.789 1.00 27.63  ?  0   ALA C C   1 
ATOM   4830 O  O   . ALA D 1 5   ? 59.834 -11.746 -26.464 1.00 29.68  ?  0   ALA C O   1 
ATOM   4831 C  CB  . ALA D 1 5   ? 60.830 -14.582 -25.981 1.00 28.78  ?  0   ALA C CB  1 
ATOM   4832 N  N   . MET D 1 6   ? 61.186 -11.450 -24.682 1.00 27.01  ?  1   MET C N   1 
ATOM   4833 C  CA  . MET D 1 6   ? 60.650 -10.134 -24.259 1.00 27.80  ?  1   MET C CA  1 
ATOM   4834 C  C   . MET D 1 6   ? 61.805 -9.140  -24.238 1.00 25.08  ?  1   MET C C   1 
ATOM   4835 O  O   . MET D 1 6   ? 62.849 -9.486  -23.681 1.00 25.83  ?  1   MET C O   1 
ATOM   4836 C  CB  . MET D 1 6   ? 60.038 -10.206 -22.860 1.00 28.18  ?  1   MET C CB  1 
ATOM   4837 C  CG  . MET D 1 6   ? 59.381 -8.906  -22.453 1.00 28.97  ?  1   MET C CG  1 
ATOM   4838 S  SD  . MET D 1 6   ? 58.614 -9.106  -20.830 1.00 28.81  ?  1   MET C SD  1 
ATOM   4839 C  CE  . MET D 1 6   ? 57.866 -7.496  -20.669 1.00 28.23  ?  1   MET C CE  1 
ATOM   4840 N  N   . PHE D 1 7   ? 61.601 -7.946  -24.788 1.00 24.74  ?  2   PHE C N   1 
ATOM   4841 C  CA  . PHE D 1 7   ? 62.598 -6.856  -24.782 1.00 26.01  ?  2   PHE C CA  1 
ATOM   4842 C  C   . PHE D 1 7   ? 62.483 -6.122  -23.453 1.00 25.12  ?  2   PHE C C   1 
ATOM   4843 O  O   . PHE D 1 7   ? 61.450 -5.523  -23.210 1.00 23.73  ?  2   PHE C O   1 
ATOM   4844 C  CB  . PHE D 1 7   ? 62.377 -5.885  -25.934 1.00 26.94  ?  2   PHE C CB  1 
ATOM   4845 C  CG  . PHE D 1 7   ? 63.360 -4.742  -25.982 1.00 28.53  ?  2   PHE C CG  1 
ATOM   4846 C  CD1 . PHE D 1 7   ? 64.708 -4.973  -26.217 1.00 30.85  ?  2   PHE C CD1 1 
ATOM   4847 C  CD2 . PHE D 1 7   ? 62.932 -3.438  -25.816 1.00 30.34  ?  2   PHE C CD2 1 
ATOM   4848 C  CE1 . PHE D 1 7   ? 65.606 -3.922  -26.271 1.00 31.37  ?  2   PHE C CE1 1 
ATOM   4849 C  CE2 . PHE D 1 7   ? 63.829 -2.383  -25.869 1.00 31.70  ?  2   PHE C CE2 1 
ATOM   4850 C  CZ  . PHE D 1 7   ? 65.169 -2.630  -26.085 1.00 31.93  ?  2   PHE C CZ  1 
ATOM   4851 N  N   . VAL D 1 8   ? 63.515 -6.205  -22.619 1.00 24.32  ?  3   VAL C N   1 
ATOM   4852 C  CA  . VAL D 1 8   ? 63.574 -5.464  -21.331 1.00 21.05  ?  3   VAL C CA  1 
ATOM   4853 C  C   . VAL D 1 8   ? 64.925 -4.791  -21.220 1.00 22.12  ?  3   VAL C C   1 
ATOM   4854 O  O   . VAL D 1 8   ? 65.924 -5.476  -20.986 1.00 21.24  ?  3   VAL C O   1 
ATOM   4855 C  CB  . VAL D 1 8   ? 63.359 -6.360  -20.110 1.00 20.21  ?  3   VAL C CB  1 
ATOM   4856 C  CG1 . VAL D 1 8   ? 63.410 -5.489  -18.861 1.00 17.83  ?  3   VAL C CG1 1 
ATOM   4857 C  CG2 . VAL D 1 8   ? 62.059 -7.149  -20.205 1.00 20.80  ?  3   VAL C CG2 1 
ATOM   4858 N  N   . PRO D 1 9   ? 64.971 -3.457  -21.359 1.00 23.49  ?  4   PRO C N   1 
ATOM   4859 C  CA  . PRO D 1 9   ? 66.222 -2.714  -21.180 1.00 24.44  ?  4   PRO C CA  1 
ATOM   4860 C  C   . PRO D 1 9   ? 66.822 -3.006  -19.801 1.00 24.38  ?  4   PRO C C   1 
ATOM   4861 O  O   . PRO D 1 9   ? 66.087 -3.193  -18.854 1.00 22.72  ?  4   PRO C O   1 
ATOM   4862 C  CB  . PRO D 1 9   ? 65.806 -1.249  -21.388 1.00 24.11  ?  4   PRO C CB  1 
ATOM   4863 C  CG  . PRO D 1 9   ? 64.528 -1.310  -22.217 1.00 24.28  ?  4   PRO C CG  1 
ATOM   4864 C  CD  . PRO D 1 9   ? 63.853 -2.589  -21.756 1.00 23.17  ?  4   PRO C CD  1 
ATOM   4865 N  N   . GLY D 1 10  ? 68.157 -3.067  -19.724 1.00 26.20  ?  5   GLY C N   1 
ATOM   4866 C  CA  . GLY D 1 10  ? 68.921 -3.462  -18.523 1.00 27.23  ?  5   GLY C CA  1 
ATOM   4867 C  C   . GLY D 1 10  ? 68.395 -2.811  -17.239 1.00 23.82  ?  5   GLY C C   1 
ATOM   4868 O  O   . GLY D 1 10  ? 68.136 -3.528  -16.267 1.00 20.76  ?  5   GLY C O   1 
ATOM   4869 N  N   . PRO D 1 11  ? 68.148 -1.473  -17.246 1.00 23.06  ?  6   PRO C N   1 
ATOM   4870 C  CA  . PRO D 1 11  ? 67.734 -0.724  -16.058 1.00 23.26  ?  6   PRO C CA  1 
ATOM   4871 C  C   . PRO D 1 11  ? 66.352 -1.110  -15.503 1.00 21.36  ?  6   PRO C C   1 
ATOM   4872 O  O   . PRO D 1 11  ? 66.077 -0.826  -14.354 1.00 20.80  ?  6   PRO C O   1 
ATOM   4873 C  CB  . PRO D 1 11  ? 67.721 0.731   -16.553 1.00 25.48  ?  6   PRO C CB  1 
ATOM   4874 C  CG  . PRO D 1 11  ? 68.690 0.726   -17.706 1.00 27.34  ?  6   PRO C CG  1 
ATOM   4875 C  CD  . PRO D 1 11  ? 68.356 -0.576  -18.400 1.00 27.13  ?  6   PRO C CD  1 
ATOM   4876 N  N   . TYR D 1 12  ? 65.557 -1.823  -16.295 1.00 21.64  ?  7   TYR C N   1 
ATOM   4877 C  CA  . TYR D 1 12  ? 64.157 -2.205  -15.947 1.00 19.58  ?  7   TYR C CA  1 
ATOM   4878 C  C   . TYR D 1 12  ? 64.039 -3.686  -15.548 1.00 20.65  ?  7   TYR C C   1 
ATOM   4879 O  O   . TYR D 1 12  ? 62.882 -4.177  -15.391 1.00 17.43  ?  7   TYR C O   1 
ATOM   4880 C  CB  . TYR D 1 12  ? 63.237 -1.827  -17.096 1.00 18.77  ?  7   TYR C CB  1 
ATOM   4881 C  CG  . TYR D 1 12  ? 63.266 -0.371  -17.501 1.00 18.33  ?  7   TYR C CG  1 
ATOM   4882 C  CD1 . TYR D 1 12  ? 63.425 0.630   -16.563 1.00 18.43  ?  7   TYR C CD1 1 
ATOM   4883 C  CD2 . TYR D 1 12  ? 63.100 0.019   -18.818 1.00 20.24  ?  7   TYR C CD2 1 
ATOM   4884 C  CE1 . TYR D 1 12  ? 63.461 1.961   -16.913 1.00 16.66  ?  7   TYR C CE1 1 
ATOM   4885 C  CE2 . TYR D 1 12  ? 63.141 1.362   -19.194 1.00 19.89  ?  7   TYR C CE2 1 
ATOM   4886 C  CZ  . TYR D 1 12  ? 63.293 2.336   -18.221 1.00 19.83  ?  7   TYR C CZ  1 
ATOM   4887 O  OH  . TYR D 1 12  ? 63.380 3.671   -18.509 1.00 21.77  ?  7   TYR C OH  1 
ATOM   4888 N  N   . HIS D 1 13  ? 65.157 -4.412  -15.453 1.00 19.33  ?  8   HIS C N   1 
ATOM   4889 C  CA  . HIS D 1 13  ? 65.235 -5.783  -14.878 1.00 23.31  ?  8   HIS C CA  1 
ATOM   4890 C  C   . HIS D 1 13  ? 64.870 -5.765  -13.390 1.00 22.72  ?  8   HIS C C   1 
ATOM   4891 O  O   . HIS D 1 13  ? 65.270 -4.812  -12.678 1.00 23.31  ?  8   HIS C O   1 
ATOM   4892 C  CB  . HIS D 1 13  ? 66.628 -6.379  -15.106 1.00 26.08  ?  8   HIS C CB  1 
ATOM   4893 C  CG  . HIS D 1 13  ? 66.838 -6.819  -16.514 1.00 30.72  ?  8   HIS C CG  1 
ATOM   4894 N  ND1 . HIS D 1 13  ? 67.318 -8.066  -16.831 1.00 38.72  ?  8   HIS C ND1 1 
ATOM   4895 C  CD2 . HIS D 1 13  ? 66.596 -6.205  -17.687 1.00 32.74  ?  8   HIS C CD2 1 
ATOM   4896 C  CE1 . HIS D 1 13  ? 67.362 -8.198  -18.141 1.00 39.09  ?  8   HIS C CE1 1 
ATOM   4897 N  NE2 . HIS D 1 13  ? 66.931 -7.067  -18.686 1.00 34.78  ?  8   HIS C NE2 1 
ATOM   4898 N  N   . ALA D 1 14  ? 64.119 -6.768  -12.928 1.00 24.60  ?  9   ALA C N   1 
ATOM   4899 C  CA  . ALA D 1 14  ? 63.768 -6.901  -11.495 1.00 26.58  ?  9   ALA C CA  1 
ATOM   4900 C  C   . ALA D 1 14  ? 65.062 -7.036  -10.705 1.00 27.51  ?  9   ALA C C   1 
ATOM   4901 O  O   . ALA D 1 14  ? 66.008 -7.621  -11.203 1.00 25.98  ?  9   ALA C O   1 
ATOM   4902 C  CB  . ALA D 1 14  ? 62.871 -8.071  -11.255 1.00 28.23  ?  9   ALA C CB  1 
ATOM   4903 N  N   . PRO D 1 15  ? 65.130 -6.483  -9.484  1.00 28.44  ?  10  PRO C N   1 
ATOM   4904 C  CA  . PRO D 1 15  ? 66.278 -6.688  -8.608  1.00 29.64  ?  10  PRO C CA  1 
ATOM   4905 C  C   . PRO D 1 15  ? 66.506 -8.168  -8.292  1.00 28.40  ?  10  PRO C C   1 
ATOM   4906 O  O   . PRO D 1 15  ? 67.641 -8.541  -8.012  1.00 30.09  ?  10  PRO C O   1 
ATOM   4907 C  CB  . PRO D 1 15  ? 65.913 -5.995  -7.287  1.00 31.08  ?  10  PRO C CB  1 
ATOM   4908 C  CG  . PRO D 1 15  ? 64.760 -5.072  -7.642  1.00 32.73  ?  10  PRO C CG  1 
ATOM   4909 C  CD  . PRO D 1 15  ? 64.097 -5.649  -8.872  1.00 29.16  ?  10  PRO C CD  1 
ATOM   4910 N  N   . GLU D 1 16  ? 65.445 -8.967  -8.280  1.00 24.63  ?  11  GLU C N   1 
ATOM   4911 C  CA  . GLU D 1 16  ? 65.471 -10.394 -7.880  1.00 25.84  ?  11  GLU C CA  1 
ATOM   4912 C  C   . GLU D 1 16  ? 64.418 -11.168 -8.671  1.00 25.38  ?  11  GLU C C   1 
ATOM   4913 O  O   . GLU D 1 16  ? 63.384 -10.569 -9.001  1.00 21.59  ?  11  GLU C O   1 
ATOM   4914 C  CB  . GLU D 1 16  ? 65.087 -10.583 -6.402  1.00 31.90  ?  11  GLU C CB  1 
ATOM   4915 C  CG  . GLU D 1 16  ? 65.957 -9.843  -5.395  1.00 39.63  ?  11  GLU C CG  1 
ATOM   4916 C  CD  . GLU D 1 16  ? 67.400 -10.313 -5.255  1.00 47.95  ?  11  GLU C CD  1 
ATOM   4917 O  OE1 . GLU D 1 16  ? 68.205 -9.534  -4.686  1.00 51.39  ?  11  GLU C OE1 1 
ATOM   4918 O  OE2 . GLU D 1 16  ? 67.723 -11.450 -5.701  1.00 53.96  -1 11  GLU C OE2 1 
ATOM   4919 N  N   . ASP D 1 17  ? 64.616 -12.469 -8.871  1.00 23.93  ?  12  ASP C N   1 
ATOM   4920 C  CA  . ASP D 1 17  ? 63.659 -13.320 -9.629  1.00 23.78  ?  12  ASP C CA  1 
ATOM   4921 C  C   . ASP D 1 17  ? 62.290 -13.360 -8.937  1.00 23.56  ?  12  ASP C C   1 
ATOM   4922 O  O   . ASP D 1 17  ? 61.250 -13.474 -9.661  1.00 19.84  ?  12  ASP C O   1 
ATOM   4923 C  CB  . ASP D 1 17  ? 64.152 -14.756 -9.762  1.00 26.09  ?  12  ASP C CB  1 
ATOM   4924 C  CG  . ASP D 1 17  ? 65.404 -14.887 -10.602 1.00 31.02  ?  12  ASP C CG  1 
ATOM   4925 O  OD1 . ASP D 1 17  ? 65.471 -14.194 -11.612 1.00 31.69  ?  12  ASP C OD1 1 
ATOM   4926 O  OD2 . ASP D 1 17  ? 66.289 -15.686 -10.227 1.00 35.22  -1 12  ASP C OD2 1 
ATOM   4927 N  N   . ARG D 1 18  ? 62.288 -13.245 -7.608  1.00 22.77  ?  13  ARG C N   1 
ATOM   4928 C  CA  . ARG D 1 18  ? 61.075 -13.325 -6.772  1.00 24.18  ?  13  ARG C CA  1 
ATOM   4929 C  C   . ARG D 1 18  ? 60.093 -12.207 -7.162  1.00 20.32  ?  13  ARG C C   1 
ATOM   4930 O  O   . ARG D 1 18  ? 58.916 -12.399 -6.916  1.00 19.95  ?  13  ARG C O   1 
ATOM   4931 C  CB  . ARG D 1 18  ? 61.449 -13.294 -5.289  1.00 29.91  ?  13  ARG C CB  1 
ATOM   4932 C  CG  . ARG D 1 18  ? 60.273 -13.311 -4.327  1.00 37.79  ?  13  ARG C CG  1 
ATOM   4933 C  CD  . ARG D 1 18  ? 59.401 -14.536 -4.459  1.00 45.78  ?  13  ARG C CD  1 
ATOM   4934 N  NE  . ARG D 1 18  ? 58.271 -14.497 -3.534  1.00 53.32  ?  13  ARG C NE  1 
ATOM   4935 C  CZ  . ARG D 1 18  ? 58.130 -15.268 -2.457  1.00 58.70  ?  13  ARG C CZ  1 
ATOM   4936 N  NH1 . ARG D 1 18  ? 59.047 -16.173 -2.141  1.00 61.48  ?  13  ARG C NH1 1 
ATOM   4937 N  NH2 . ARG D 1 18  ? 57.063 -15.120 -1.691  1.00 58.07  ?  13  ARG C NH2 1 
ATOM   4938 N  N   . TRP D 1 19  ? 60.546 -11.103 -7.766  1.00 20.32  ?  14  TRP C N   1 
ATOM   4939 C  CA  . TRP D 1 19  ? 59.663 -9.964  -8.097  1.00 22.00  ?  14  TRP C CA  1 
ATOM   4940 C  C   . TRP D 1 19  ? 58.648 -10.408 -9.163  1.00 19.45  ?  14  TRP C C   1 
ATOM   4941 O  O   . TRP D 1 19  ? 57.508 -9.886  -9.149  1.00 18.96  ?  14  TRP C O   1 
ATOM   4942 C  CB  . TRP D 1 19  ? 60.470 -8.751  -8.551  1.00 22.98  ?  14  TRP C CB  1 
ATOM   4943 C  CG  . TRP D 1 19  ? 61.014 -7.901  -7.441  1.00 23.16  ?  14  TRP C CG  1 
ATOM   4944 C  CD1 . TRP D 1 19  ? 61.660 -8.311  -6.309  1.00 23.37  ?  14  TRP C CD1 1 
ATOM   4945 C  CD2 . TRP D 1 19  ? 60.969 -6.470  -7.383  1.00 21.09  ?  14  TRP C CD2 1 
ATOM   4946 N  NE1 . TRP D 1 19  ? 62.001 -7.219  -5.546  1.00 26.39  ?  14  TRP C NE1 1 
ATOM   4947 C  CE2 . TRP D 1 19  ? 61.589 -6.079  -6.181  1.00 22.61  ?  14  TRP C CE2 1 
ATOM   4948 C  CE3 . TRP D 1 19  ? 60.421 -5.489  -8.202  1.00 24.08  ?  14  TRP C CE3 1 
ATOM   4949 C  CZ2 . TRP D 1 19  ? 61.705 -4.747  -5.795  1.00 24.14  ?  14  TRP C CZ2 1 
ATOM   4950 C  CZ3 . TRP D 1 19  ? 60.558 -4.166  -7.836  1.00 27.37  ?  14  TRP C CZ3 1 
ATOM   4951 C  CH2 . TRP D 1 19  ? 61.199 -3.802  -6.647  1.00 25.47  ?  14  TRP C CH2 1 
ATOM   4952 N  N   . LEU D 1 20  ? 59.070 -11.283 -10.078 1.00 19.28  ?  15  LEU C N   1 
ATOM   4953 C  CA  . LEU D 1 20  ? 58.259 -11.808 -11.189 1.00 18.03  ?  15  LEU C CA  1 
ATOM   4954 C  C   . LEU D 1 20  ? 57.179 -12.704 -10.585 1.00 17.76  ?  15  LEU C C   1 
ATOM   4955 O  O   . LEU D 1 20  ? 56.027 -12.535 -10.907 1.00 17.29  ?  15  LEU C O   1 
ATOM   4956 C  CB  . LEU D 1 20  ? 59.156 -12.540 -12.193 1.00 18.87  ?  15  LEU C CB  1 
ATOM   4957 C  CG  . LEU D 1 20  ? 59.963 -11.686 -13.192 1.00 20.36  ?  15  LEU C CG  1 
ATOM   4958 C  CD1 . LEU D 1 20  ? 61.214 -11.047 -12.554 1.00 19.79  ?  15  LEU C CD1 1 
ATOM   4959 C  CD2 . LEU D 1 20  ? 60.407 -12.490 -14.411 1.00 18.83  ?  15  LEU C CD2 1 
ATOM   4960 N  N   . VAL D 1 21  ? 57.528 -13.556 -9.621  1.00 17.83  ?  16  VAL C N   1 
ATOM   4961 C  CA  . VAL D 1 21  ? 56.539 -14.448 -8.944  1.00 19.43  ?  16  VAL C CA  1 
ATOM   4962 C  C   . VAL D 1 21  ? 55.508 -13.589 -8.206  1.00 18.09  ?  16  VAL C C   1 
ATOM   4963 O  O   . VAL D 1 21  ? 54.272 -13.883 -8.289  1.00 18.58  ?  16  VAL C O   1 
ATOM   4964 C  CB  . VAL D 1 21  ? 57.216 -15.431 -7.970  1.00 19.62  ?  16  VAL C CB  1 
ATOM   4965 C  CG1 . VAL D 1 21  ? 56.175 -16.301 -7.284  1.00 21.17  ?  16  VAL C CG1 1 
ATOM   4966 C  CG2 . VAL D 1 21  ? 58.259 -16.277 -8.681  1.00 20.59  ?  16  VAL C CG2 1 
ATOM   4967 N  N   . ASP D 1 22  ? 55.987 -12.575 -7.492  1.00 18.35  ?  17  ASP C N   1 
ATOM   4968 C  CA  . ASP D 1 22  ? 55.116 -11.635 -6.741  1.00 21.61  ?  17  ASP C CA  1 
ATOM   4969 C  C   . ASP D 1 22  ? 54.101 -10.994 -7.688  1.00 19.38  ?  17  ASP C C   1 
ATOM   4970 O  O   . ASP D 1 22  ? 52.914 -10.868 -7.300  1.00 18.23  ?  17  ASP C O   1 
ATOM   4971 C  CB  . ASP D 1 22  ? 55.921 -10.534 -6.046  1.00 25.18  ?  17  ASP C CB  1 
ATOM   4972 C  CG  . ASP D 1 22  ? 56.762 -10.981 -4.860  1.00 31.34  ?  17  ASP C CG  1 
ATOM   4973 O  OD1 . ASP D 1 22  ? 56.567 -12.131 -4.369  1.00 31.26  ?  17  ASP C OD1 1 
ATOM   4974 O  OD2 . ASP D 1 22  ? 57.588 -10.162 -4.427  1.00 33.99  -1 17  ASP C OD2 1 
ATOM   4975 N  N   . LEU D 1 23  ? 54.541 -10.527 -8.859  1.00 19.14  ?  18  LEU C N   1 
ATOM   4976 C  CA  . LEU D 1 23  ? 53.605 -9.878  -9.819  1.00 19.91  ?  18  LEU C CA  1 
ATOM   4977 C  C   . LEU D 1 23  ? 52.586 -10.919 -10.276 1.00 17.94  ?  18  LEU C C   1 
ATOM   4978 O  O   . LEU D 1 23  ? 51.368 -10.583 -10.273 1.00 18.02  ?  18  LEU C O   1 
ATOM   4979 C  CB  . LEU D 1 23  ? 54.369 -9.239  -10.988 1.00 22.56  ?  18  LEU C CB  1 
ATOM   4980 C  CG  . LEU D 1 23  ? 53.549 -8.239  -11.816 1.00 24.73  ?  18  LEU C CG  1 
ATOM   4981 C  CD1 . LEU D 1 23  ? 54.413 -7.225  -12.520 1.00 27.18  ?  18  LEU C CD1 1 
ATOM   4982 C  CD2 . LEU D 1 23  ? 52.725 -8.941  -12.859 1.00 25.36  ?  18  LEU C CD2 1 
ATOM   4983 N  N   . VAL D 1 24  ? 53.023 -12.144 -10.597 1.00 18.17  ?  19  VAL C N   1 
ATOM   4984 C  CA  . VAL D 1 24  ? 52.065 -13.184 -11.078 1.00 19.15  ?  19  VAL C CA  1 
ATOM   4985 C  C   . VAL D 1 24  ? 51.007 -13.376 -9.989  1.00 18.12  ?  19  VAL C C   1 
ATOM   4986 O  O   . VAL D 1 24  ? 49.818 -13.418 -10.305 1.00 16.86  ?  19  VAL C O   1 
ATOM   4987 C  CB  . VAL D 1 24  ? 52.758 -14.517 -11.451 1.00 20.67  ?  19  VAL C CB  1 
ATOM   4988 C  CG1 . VAL D 1 24  ? 51.746 -15.664 -11.524 1.00 21.62  ?  19  VAL C CG1 1 
ATOM   4989 C  CG2 . VAL D 1 24  ? 53.521 -14.395 -12.759 1.00 20.15  ?  19  VAL C CG2 1 
ATOM   4990 N  N   . ARG D 1 25  ? 51.431 -13.555 -8.754  1.00 18.21  ?  20  ARG C N   1 
ATOM   4991 C  CA  . ARG D 1 25  ? 50.491 -13.790 -7.623  1.00 21.50  ?  20  ARG C CA  1 
ATOM   4992 C  C   . ARG D 1 25  ? 49.574 -12.597 -7.427  1.00 21.06  ?  20  ARG C C   1 
ATOM   4993 O  O   . ARG D 1 25  ? 48.410 -12.844 -7.119  1.00 21.90  ?  20  ARG C O   1 
ATOM   4994 C  CB  . ARG D 1 25  ? 51.228 -14.100 -6.321  1.00 23.67  ?  20  ARG C CB  1 
ATOM   4995 C  CG  . ARG D 1 25  ? 51.860 -15.472 -6.256  1.00 25.76  ?  20  ARG C CG  1 
ATOM   4996 C  CD  . ARG D 1 25  ? 52.366 -15.716 -4.835  1.00 27.93  ?  20  ARG C CD  1 
ATOM   4997 N  NE  . ARG D 1 25  ? 53.302 -16.820 -4.697  1.00 30.27  ?  20  ARG C NE  1 
ATOM   4998 C  CZ  . ARG D 1 25  ? 53.017 -18.114 -4.859  1.00 36.74  ?  20  ARG C CZ  1 
ATOM   4999 N  NH1 . ARG D 1 25  ? 51.790 -18.523 -5.169  1.00 34.86  ?  20  ARG C NH1 1 
ATOM   5000 N  NH2 . ARG D 1 25  ? 53.982 -19.005 -4.690  1.00 37.67  ?  20  ARG C NH2 1 
ATOM   5001 N  N   . GLY D 1 26  ? 50.065 -11.373 -7.682  1.00 19.24  ?  21  GLY C N   1 
ATOM   5002 C  CA  . GLY D 1 26  ? 49.370 -10.107 -7.412  1.00 17.46  ?  21  GLY C CA  1 
ATOM   5003 C  C   . GLY D 1 26  ? 48.375 -9.760  -8.493  1.00 16.43  ?  21  GLY C C   1 
ATOM   5004 O  O   . GLY D 1 26  ? 47.510 -8.936  -8.233  1.00 15.83  ?  21  GLY C O   1 
ATOM   5005 N  N   . HIS D 1 27  ? 48.490 -10.386 -9.673  1.00 14.66  ?  22  HIS C N   1 
ATOM   5006 C  CA  . HIS D 1 27  ? 47.828 -9.937  -10.919 1.00 15.29  ?  22  HIS C CA  1 
ATOM   5007 C  C   . HIS D 1 27  ? 47.453 -11.143 -11.781 1.00 17.01  ?  22  HIS C C   1 
ATOM   5008 O  O   . HIS D 1 27  ? 47.918 -11.339 -12.917 1.00 15.95  ?  22  HIS C O   1 
ATOM   5009 C  CB  . HIS D 1 27  ? 48.809 -8.931  -11.534 1.00 13.19  ?  22  HIS C CB  1 
ATOM   5010 C  CG  . HIS D 1 27  ? 49.078 -7.796  -10.622 1.00 13.57  ?  22  HIS C CG  1 
ATOM   5011 N  ND1 . HIS D 1 27  ? 48.202 -6.730  -10.514 1.00 13.04  ?  22  HIS C ND1 1 
ATOM   5012 C  CD2 . HIS D 1 27  ? 50.108 -7.505  -9.809  1.00 14.29  ?  22  HIS C CD2 1 
ATOM   5013 C  CE1 . HIS D 1 27  ? 48.702 -5.837  -9.691  1.00 15.44  ?  22  HIS C CE1 1 
ATOM   5014 N  NE2 . HIS D 1 27  ? 49.839 -6.316  -9.172  1.00 14.17  ?  22  HIS C NE2 1 
ATOM   5015 N  N   . PRO D 1 28  ? 46.627 -12.057 -11.239 1.00 16.07  ?  23  PRO C N   1 
ATOM   5016 C  CA  . PRO D 1 28  ? 46.452 -13.360 -11.878 1.00 15.66  ?  23  PRO C CA  1 
ATOM   5017 C  C   . PRO D 1 28  ? 45.616 -13.346 -13.167 1.00 15.03  ?  23  PRO C C   1 
ATOM   5018 O  O   . PRO D 1 28  ? 45.603 -14.358 -13.889 1.00 13.69  ?  23  PRO C O   1 
ATOM   5019 C  CB  . PRO D 1 28  ? 45.717 -14.174 -10.783 1.00 15.31  ?  23  PRO C CB  1 
ATOM   5020 C  CG  . PRO D 1 28  ? 44.913 -13.108 -10.059 1.00 16.70  ?  23  PRO C CG  1 
ATOM   5021 C  CD  . PRO D 1 28  ? 45.889 -11.945 -9.961  1.00 16.63  ?  23  PRO C CD  1 
ATOM   5022 N  N   . LEU D 1 29  ? 44.888 -12.264 -13.432 1.00 14.80  ?  24  LEU C N   1 
ATOM   5023 C  CA  . LEU D 1 29  ? 44.104 -12.230 -14.673 1.00 15.65  ?  24  LEU C CA  1 
ATOM   5024 C  C   . LEU D 1 29  ? 45.084 -11.845 -15.772 1.00 14.71  ?  24  LEU C C   1 
ATOM   5025 O  O   . LEU D 1 29  ? 45.323 -10.611 -15.936 1.00 13.40  ?  24  LEU C O   1 
ATOM   5026 C  CB  . LEU D 1 29  ? 42.900 -11.291 -14.589 1.00 17.15  ?  24  LEU C CB  1 
ATOM   5027 C  CG  . LEU D 1 29  ? 41.877 -11.520 -15.712 1.00 21.28  ?  24  LEU C CG  1 
ATOM   5028 C  CD1 . LEU D 1 29  ? 41.189 -12.849 -15.547 1.00 19.49  ?  24  LEU C CD1 1 
ATOM   5029 C  CD2 . LEU D 1 29  ? 40.829 -10.415 -15.817 1.00 22.10  ?  24  LEU C CD2 1 
ATOM   5030 N  N   . ALA D 1 30  ? 45.637 -12.865 -16.434 1.00 13.17  ?  25  ALA C N   1 
ATOM   5031 C  CA  . ALA D 1 30  ? 46.656 -12.757 -17.496 1.00 14.11  ?  25  ALA C CA  1 
ATOM   5032 C  C   . ALA D 1 30  ? 45.993 -12.564 -18.853 1.00 14.75  ?  25  ALA C C   1 
ATOM   5033 O  O   . ALA D 1 30  ? 44.884 -13.035 -19.023 1.00 14.87  ?  25  ALA C O   1 
ATOM   5034 C  CB  . ALA D 1 30  ? 47.515 -13.996 -17.514 1.00 16.70  ?  25  ALA C CB  1 
ATOM   5035 N  N   . GLN D 1 31  ? 46.725 -11.992 -19.807 1.00 15.42  ?  26  GLN C N   1 
ATOM   5036 C  CA  . GLN D 1 31  ? 46.373 -12.081 -21.243 1.00 14.89  ?  26  GLN C CA  1 
ATOM   5037 C  C   . GLN D 1 31  ? 47.133 -13.270 -21.836 1.00 15.95  ?  26  GLN C C   1 
ATOM   5038 O  O   . GLN D 1 31  ? 48.362 -13.167 -21.950 1.00 14.06  ?  26  GLN C O   1 
ATOM   5039 C  CB  . GLN D 1 31  ? 46.693 -10.771 -21.956 1.00 15.34  ?  26  GLN C CB  1 
ATOM   5040 C  CG  . GLN D 1 31  ? 45.815 -9.650  -21.455 1.00 14.89  ?  26  GLN C CG  1 
ATOM   5041 C  CD  . GLN D 1 31  ? 45.959 -8.356  -22.220 1.00 15.10  ?  26  GLN C CD  1 
ATOM   5042 O  OE1 . GLN D 1 31  ? 46.249 -8.379  -23.408 1.00 18.20  ?  26  GLN C OE1 1 
ATOM   5043 N  NE2 . GLN D 1 31  ? 45.777 -7.241  -21.532 1.00 16.60  ?  26  GLN C NE2 1 
ATOM   5044 N  N   . LEU D 1 32  ? 46.418 -14.320 -22.217 1.00 14.75  ?  27  LEU C N   1 
ATOM   5045 C  CA  . LEU D 1 32  ? 47.014 -15.515 -22.888 1.00 14.98  ?  27  LEU C CA  1 
ATOM   5046 C  C   . LEU D 1 32  ? 47.026 -15.288 -24.388 1.00 15.70  ?  27  LEU C C   1 
ATOM   5047 O  O   . LEU D 1 32  ? 45.914 -15.076 -24.949 1.00 13.27  ?  27  LEU C O   1 
ATOM   5048 C  CB  . LEU D 1 32  ? 46.199 -16.749 -22.530 1.00 14.14  ?  27  LEU C CB  1 
ATOM   5049 C  CG  . LEU D 1 32  ? 46.668 -18.112 -23.037 1.00 15.17  ?  27  LEU C CG  1 
ATOM   5050 C  CD1 . LEU D 1 32  ? 48.074 -18.476 -22.571 1.00 17.28  ?  27  LEU C CD1 1 
ATOM   5051 C  CD2 . LEU D 1 32  ? 45.671 -19.160 -22.548 1.00 16.75  ?  27  LEU C CD2 1 
ATOM   5052 N  N   . ALA D 1 33  ? 48.213 -15.355 -25.031 1.00 14.57  ?  28  ALA C N   1 
ATOM   5053 C  CA  . ALA D 1 33  ? 48.307 -15.122 -26.490 1.00 14.94  ?  28  ALA C CA  1 
ATOM   5054 C  C   . ALA D 1 33  ? 48.859 -16.383 -27.159 1.00 14.95  ?  28  ALA C C   1 
ATOM   5055 O  O   . ALA D 1 33  ? 49.800 -16.999 -26.649 1.00 14.82  ?  28  ALA C O   1 
ATOM   5056 C  CB  . ALA D 1 33  ? 49.124 -13.893 -26.814 1.00 14.10  ?  28  ALA C CB  1 
ATOM   5057 N  N   . SER D 1 34  ? 48.271 -16.735 -28.286 1.00 15.39  ?  29  SER C N   1 
ATOM   5058 C  CA  . SER D 1 34  ? 48.821 -17.762 -29.187 1.00 17.76  ?  29  SER C CA  1 
ATOM   5059 C  C   . SER D 1 34  ? 48.687 -17.252 -30.613 1.00 19.79  ?  29  SER C C   1 
ATOM   5060 O  O   . SER D 1 34  ? 47.841 -16.351 -30.845 1.00 19.18  ?  29  SER C O   1 
ATOM   5061 C  CB  . SER D 1 34  ? 48.185 -19.091 -28.961 1.00 17.49  ?  29  SER C CB  1 
ATOM   5062 O  OG  . SER D 1 34  ? 46.795 -19.005 -29.161 1.00 18.72  ?  29  SER C OG  1 
ATOM   5063 N  N   . ASN D 1 35  ? 49.543 -17.757 -31.500 1.00 18.88  ?  30  ASN C N   1 
ATOM   5064 C  CA  . ASN D 1 35  ? 49.580 -17.316 -32.912 1.00 20.09  ?  30  ASN C CA  1 
ATOM   5065 C  C   . ASN D 1 35  ? 48.231 -17.524 -33.585 1.00 19.39  ?  30  ASN C C   1 
ATOM   5066 O  O   . ASN D 1 35  ? 47.576 -18.545 -33.310 1.00 19.17  ?  30  ASN C O   1 
ATOM   5067 C  CB  . ASN D 1 35  ? 50.630 -18.065 -33.719 1.00 19.95  ?  30  ASN C CB  1 
ATOM   5068 C  CG  . ASN D 1 35  ? 52.031 -17.651 -33.370 1.00 21.06  ?  30  ASN C CG  1 
ATOM   5069 O  OD1 . ASN D 1 35  ? 52.263 -16.612 -32.737 1.00 19.45  ?  30  ASN C OD1 1 
ATOM   5070 N  ND2 . ASN D 1 35  ? 52.976 -18.486 -33.787 1.00 24.26  ?  30  ASN C ND2 1 
ATOM   5071 N  N   . GLY D 1 36  ? 47.880 -16.595 -34.483 1.00 19.96  ?  31  GLY C N   1 
ATOM   5072 C  CA  . GLY D 1 36  ? 46.720 -16.703 -35.375 1.00 23.48  ?  31  GLY C CA  1 
ATOM   5073 C  C   . GLY D 1 36  ? 47.117 -17.547 -36.569 1.00 25.50  ?  31  GLY C C   1 
ATOM   5074 O  O   . GLY D 1 36  ? 48.281 -17.470 -36.977 1.00 29.01  ?  31  GLY C O   1 
ATOM   5075 N  N   . ALA D 1 37  ? 46.227 -18.391 -37.049 1.00 28.15  ?  32  ALA C N   1 
ATOM   5076 C  CA  . ALA D 1 37  ? 46.529 -19.266 -38.202 1.00 31.15  ?  32  ALA C CA  1 
ATOM   5077 C  C   . ALA D 1 37  ? 46.533 -18.399 -39.458 1.00 32.19  ?  32  ALA C C   1 
ATOM   5078 O  O   . ALA D 1 37  ? 45.744 -17.417 -39.514 1.00 28.65  ?  32  ALA C O   1 
ATOM   5079 C  CB  . ALA D 1 37  ? 45.538 -20.385 -38.280 1.00 31.56  ?  32  ALA C CB  1 
ATOM   5080 N  N   . GLY D 1 38  ? 47.416 -18.732 -40.407 1.00 38.01  ?  33  GLY C N   1 
ATOM   5081 C  CA  . GLY D 1 38  ? 47.461 -18.149 -41.763 1.00 38.96  ?  33  GLY C CA  1 
ATOM   5082 C  C   . GLY D 1 38  ? 47.771 -16.663 -41.734 1.00 37.99  ?  33  GLY C C   1 
ATOM   5083 O  O   . GLY D 1 38  ? 47.090 -15.918 -42.445 1.00 39.68  ?  33  GLY C O   1 
ATOM   5084 N  N   . GLY D 1 39  ? 48.731 -16.258 -40.899 1.00 35.12  ?  34  GLY C N   1 
ATOM   5085 C  CA  . GLY D 1 39  ? 49.250 -14.881 -40.814 1.00 35.00  ?  34  GLY C CA  1 
ATOM   5086 C  C   . GLY D 1 39  ? 48.310 -13.931 -40.085 1.00 33.31  ?  34  GLY C C   1 
ATOM   5087 O  O   . GLY D 1 39  ? 48.631 -12.741 -40.065 1.00 36.48  ?  34  GLY C O   1 
ATOM   5088 N  N   . ALA D 1 40  ? 47.191 -14.418 -39.531 1.00 30.32  ?  35  ALA C N   1 
ATOM   5089 C  CA  . ALA D 1 40  ? 46.199 -13.600 -38.793 1.00 27.53  ?  35  ALA C CA  1 
ATOM   5090 C  C   . ALA D 1 40  ? 46.827 -13.142 -37.474 1.00 24.99  ?  35  ALA C C   1 
ATOM   5091 O  O   . ALA D 1 40  ? 47.818 -13.739 -37.027 1.00 27.57  ?  35  ALA C O   1 
ATOM   5092 C  CB  . ALA D 1 40  ? 44.912 -14.356 -38.583 1.00 26.94  ?  35  ALA C CB  1 
ATOM   5093 N  N   . ALA D 1 41  ? 46.308 -12.052 -36.911 1.00 23.64  ?  36  ALA C N   1 
ATOM   5094 C  CA  . ALA D 1 41  ? 46.664 -11.566 -35.559 1.00 21.14  ?  36  ALA C CA  1 
ATOM   5095 C  C   . ALA D 1 41  ? 46.519 -12.699 -34.531 1.00 19.75  ?  36  ALA C C   1 
ATOM   5096 O  O   . ALA D 1 41  ? 45.654 -13.590 -34.628 1.00 17.70  ?  36  ALA C O   1 
ATOM   5097 C  CB  . ALA D 1 41  ? 45.783 -10.387 -35.184 1.00 18.36  ?  36  ALA C CB  1 
ATOM   5098 N  N   . PRO D 1 42  ? 47.331 -12.655 -33.457 1.00 17.93  ?  37  PRO C N   1 
ATOM   5099 C  CA  . PRO D 1 42  ? 47.154 -13.569 -32.330 1.00 17.58  ?  37  PRO C CA  1 
ATOM   5100 C  C   . PRO D 1 42  ? 45.755 -13.549 -31.710 1.00 16.97  ?  37  PRO C C   1 
ATOM   5101 O  O   . PRO D 1 42  ? 45.110 -12.495 -31.765 1.00 15.73  ?  37  PRO C O   1 
ATOM   5102 C  CB  . PRO D 1 42  ? 48.184 -13.069 -31.321 1.00 17.07  ?  37  PRO C CB  1 
ATOM   5103 C  CG  . PRO D 1 42  ? 49.284 -12.519 -32.196 1.00 17.76  ?  37  PRO C CG  1 
ATOM   5104 C  CD  . PRO D 1 42  ? 48.525 -11.794 -33.298 1.00 17.93  ?  37  PRO C CD  1 
ATOM   5105 N  N   . HIS D 1 43  ? 45.365 -14.708 -31.177 1.00 15.76  ?  38  HIS C N   1 
ATOM   5106 C  CA  . HIS D 1 43  ? 44.269 -14.879 -30.187 1.00 16.92  ?  38  HIS C CA  1 
ATOM   5107 C  C   . HIS D 1 43  ? 44.765 -14.327 -28.854 1.00 14.86  ?  38  HIS C C   1 
ATOM   5108 O  O   . HIS D 1 43  ? 45.915 -14.632 -28.458 1.00 14.25  ?  38  HIS C O   1 
ATOM   5109 C  CB  . HIS D 1 43  ? 43.835 -16.340 -30.027 1.00 18.40  ?  38  HIS C CB  1 
ATOM   5110 C  CG  . HIS D 1 43  ? 43.582 -17.023 -31.329 1.00 21.11  ?  38  HIS C CG  1 
ATOM   5111 N  ND1 . HIS D 1 43  ? 42.376 -16.944 -31.977 1.00 25.11  ?  38  HIS C ND1 1 
ATOM   5112 C  CD2 . HIS D 1 43  ? 44.387 -17.775 -32.106 1.00 23.42  ?  38  HIS C CD2 1 
ATOM   5113 C  CE1 . HIS D 1 43  ? 42.443 -17.629 -33.106 1.00 25.56  ?  38  HIS C CE1 1 
ATOM   5114 N  NE2 . HIS D 1 43  ? 43.677 -18.130 -33.205 1.00 23.17  ?  38  HIS C NE2 1 
ATOM   5115 N  N   . ILE D 1 44  ? 43.886 -13.607 -28.175 1.00 14.03  ?  39  ILE C N   1 
ATOM   5116 C  CA  . ILE D 1 44  ? 44.108 -12.975 -26.842 1.00 14.44  ?  39  ILE C CA  1 
ATOM   5117 C  C   . ILE D 1 44  ? 42.888 -13.318 -25.976 1.00 15.46  ?  39  ILE C C   1 
ATOM   5118 O  O   . ILE D 1 44  ? 41.768 -12.966 -26.395 1.00 15.59  ?  39  ILE C O   1 
ATOM   5119 C  CB  . ILE D 1 44  ? 44.277 -11.455 -26.948 1.00 15.03  ?  39  ILE C CB  1 
ATOM   5120 C  CG1 . ILE D 1 44  ? 45.331 -11.044 -27.978 1.00 14.17  ?  39  ILE C CG1 1 
ATOM   5121 C  CG2 . ILE D 1 44  ? 44.514 -10.826 -25.588 1.00 14.22  ?  39  ILE C CG2 1 
ATOM   5122 C  CD1 . ILE D 1 44  ? 46.740 -11.347 -27.555 1.00 16.96  ?  39  ILE C CD1 1 
ATOM   5123 N  N   . THR D 1 45  ? 43.099 -14.009 -24.850 1.00 14.04  ?  40  THR C N   1 
ATOM   5124 C  CA  . THR D 1 45  ? 42.043 -14.257 -23.844 1.00 15.90  ?  40  THR C CA  1 
ATOM   5125 C  C   . THR D 1 45  ? 42.528 -13.883 -22.451 1.00 15.13  ?  40  THR C C   1 
ATOM   5126 O  O   . THR D 1 45  ? 43.697 -14.207 -22.067 1.00 13.53  ?  40  THR C O   1 
ATOM   5127 C  CB  . THR D 1 45  ? 41.560 -15.713 -23.861 1.00 16.95  ?  40  THR C CB  1 
ATOM   5128 O  OG1 . THR D 1 45  ? 41.196 -15.975 -25.216 1.00 16.79  ?  40  THR C OG1 1 
ATOM   5129 C  CG2 . THR D 1 45  ? 40.418 -15.931 -22.901 1.00 17.95  ?  40  THR C CG2 1 
ATOM   5130 N  N   . HIS D 1 46  ? 41.711 -13.117 -21.748 1.00 15.32  ?  41  HIS C N   1 
ATOM   5131 C  CA  . HIS D 1 46  ? 41.922 -12.817 -20.315 1.00 16.64  ?  41  HIS C CA  1 
ATOM   5132 C  C   . HIS D 1 46  ? 41.576 -14.060 -19.499 1.00 18.08  ?  41  HIS C C   1 
ATOM   5133 O  O   . HIS D 1 46  ? 40.378 -14.405 -19.467 1.00 13.18  ?  41  HIS C O   1 
ATOM   5134 C  CB  . HIS D 1 46  ? 41.083 -11.647 -19.830 1.00 17.31  ?  41  HIS C CB  1 
ATOM   5135 C  CG  . HIS D 1 46  ? 41.680 -10.353 -20.254 1.00 21.03  ?  41  HIS C CG  1 
ATOM   5136 N  ND1 . HIS D 1 46  ? 41.428 -9.805  -21.482 1.00 27.45  ?  41  HIS C ND1 1 
ATOM   5137 C  CD2 . HIS D 1 46  ? 42.532 -9.522  -19.626 1.00 24.80  ?  41  HIS C CD2 1 
ATOM   5138 C  CE1 . HIS D 1 46  ? 42.087 -8.665  -21.581 1.00 25.49  ?  41  HIS C CE1 1 
ATOM   5139 N  NE2 . HIS D 1 46  ? 42.732 -8.459  -20.443 1.00 27.06  ?  41  HIS C NE2 1 
ATOM   5140 N  N   . VAL D 1 47  ? 42.584 -14.663 -18.867 1.00 15.04  ?  42  VAL C N   1 
ATOM   5141 C  CA  . VAL D 1 47  ? 42.373 -15.921 -18.098 1.00 17.54  ?  42  VAL C CA  1 
ATOM   5142 C  C   . VAL D 1 47  ? 43.028 -15.858 -16.718 1.00 16.73  ?  42  VAL C C   1 
ATOM   5143 O  O   . VAL D 1 47  ? 44.118 -15.295 -16.574 1.00 16.39  ?  42  VAL C O   1 
ATOM   5144 C  CB  . VAL D 1 47  ? 42.886 -17.119 -18.907 1.00 17.43  ?  42  VAL C CB  1 
ATOM   5145 C  CG1 . VAL D 1 47  ? 42.011 -17.333 -20.123 1.00 19.13  ?  42  VAL C CG1 1 
ATOM   5146 C  CG2 . VAL D 1 47  ? 44.343 -16.946 -19.315 1.00 17.26  ?  42  VAL C CG2 1 
ATOM   5147 N  N   . PRO D 1 48  ? 42.408 -16.477 -15.686 1.00 15.58  ?  43  PRO C N   1 
ATOM   5148 C  CA  . PRO D 1 48  ? 42.970 -16.572 -14.344 1.00 16.47  ?  43  PRO C CA  1 
ATOM   5149 C  C   . PRO D 1 48  ? 44.052 -17.641 -14.283 1.00 16.13  ?  43  PRO C C   1 
ATOM   5150 O  O   . PRO D 1 48  ? 43.761 -18.804 -14.589 1.00 16.66  ?  43  PRO C O   1 
ATOM   5151 C  CB  . PRO D 1 48  ? 41.792 -17.006 -13.424 1.00 16.80  ?  43  PRO C CB  1 
ATOM   5152 C  CG  . PRO D 1 48  ? 40.835 -17.709 -14.383 1.00 17.51  ?  43  PRO C CG  1 
ATOM   5153 C  CD  . PRO D 1 48  ? 41.060 -17.062 -15.732 1.00 17.34  ?  43  PRO C CD  1 
ATOM   5154 N  N   . ILE D 1 49  ? 45.262 -17.229 -13.894 1.00 15.73  ?  44  ILE C N   1 
ATOM   5155 C  CA  . ILE D 1 49  ? 46.421 -18.141 -13.877 1.00 16.27  ?  44  ILE C CA  1 
ATOM   5156 C  C   . ILE D 1 49  ? 47.058 -18.052 -12.492 1.00 16.78  ?  44  ILE C C   1 
ATOM   5157 O  O   . ILE D 1 49  ? 47.305 -16.920 -12.002 1.00 16.82  ?  44  ILE C O   1 
ATOM   5158 C  CB  . ILE D 1 49  ? 47.421 -17.835 -14.995 1.00 16.26  ?  44  ILE C CB  1 
ATOM   5159 C  CG1 . ILE D 1 49  ? 46.803 -18.028 -16.384 1.00 16.46  ?  44  ILE C CG1 1 
ATOM   5160 C  CG2 . ILE D 1 49  ? 48.640 -18.722 -14.820 1.00 15.06  ?  44  ILE C CG2 1 
ATOM   5161 C  CD1 . ILE D 1 49  ? 47.741 -17.650 -17.518 1.00 16.29  ?  44  ILE C CD1 1 
ATOM   5162 N  N   . ILE D 1 50  ? 47.338 -19.207 -11.909 1.00 14.83  ?  45  ILE C N   1 
ATOM   5163 C  CA  . ILE D 1 50  ? 48.029 -19.320 -10.586 1.00 16.83  ?  45  ILE C CA  1 
ATOM   5164 C  C   . ILE D 1 50  ? 49.267 -20.213 -10.696 1.00 15.70  ?  45  ILE C C   1 
ATOM   5165 O  O   . ILE D 1 50  ? 49.360 -21.086 -11.595 1.00 14.30  ?  45  ILE C O   1 
ATOM   5166 C  CB  . ILE D 1 50  ? 47.059 -19.886 -9.524  1.00 16.29  ?  45  ILE C CB  1 
ATOM   5167 C  CG1 . ILE D 1 50  ? 46.562 -21.294 -9.904  1.00 17.23  ?  45  ILE C CG1 1 
ATOM   5168 C  CG2 . ILE D 1 50  ? 45.901 -18.921 -9.311  1.00 16.54  ?  45  ILE C CG2 1 
ATOM   5169 C  CD1 . ILE D 1 50  ? 45.932 -22.050 -8.745  1.00 19.86  ?  45  ILE C CD1 1 
ATOM   5170 N  N   . VAL D 1 51  ? 50.183 -20.007 -9.762  1.00 18.17  ?  46  VAL C N   1 
ATOM   5171 C  CA  . VAL D 1 51  ? 51.345 -20.903 -9.525  1.00 19.02  ?  46  VAL C CA  1 
ATOM   5172 C  C   . VAL D 1 51  ? 50.826 -22.259 -9.002  1.00 19.27  ?  46  VAL C C   1 
ATOM   5173 O  O   . VAL D 1 51  ? 49.846 -22.300 -8.199  1.00 18.02  ?  46  VAL C O   1 
ATOM   5174 C  CB  . VAL D 1 51  ? 52.355 -20.240 -8.568  1.00 20.88  ?  46  VAL C CB  1 
ATOM   5175 C  CG1 . VAL D 1 51  ? 53.394 -21.231 -8.087  1.00 23.45  ?  46  VAL C CG1 1 
ATOM   5176 C  CG2 . VAL D 1 51  ? 53.023 -19.029 -9.213  1.00 22.42  ?  46  VAL C CG2 1 
ATOM   5177 N  N   . ASP D 1 52  ? 51.356 -23.346 -9.563  1.00 20.59  ?  47  ASP C N   1 
ATOM   5178 C  CA  . ASP D 1 52  ? 51.161 -24.745 -9.096  1.00 20.87  ?  47  ASP C CA  1 
ATOM   5179 C  C   . ASP D 1 52  ? 50.871 -24.720 -7.596  1.00 19.96  ?  47  ASP C C   1 
ATOM   5180 O  O   . ASP D 1 52  ? 51.747 -24.393 -6.806  1.00 20.16  ?  47  ASP C O   1 
ATOM   5181 C  CB  . ASP D 1 52  ? 52.417 -25.561 -9.407  1.00 22.25  ?  47  ASP C CB  1 
ATOM   5182 C  CG  . ASP D 1 52  ? 52.358 -27.035 -9.030  1.00 23.35  ?  47  ASP C CG  1 
ATOM   5183 O  OD1 . ASP D 1 52  ? 51.360 -27.474 -8.411  1.00 24.59  ?  47  ASP C OD1 1 
ATOM   5184 O  OD2 . ASP D 1 52  ? 53.350 -27.719 -9.335  1.00 22.63  -1 47  ASP C OD2 1 
ATOM   5185 N  N   . PRO D 1 53  ? 49.632 -25.003 -7.152  1.00 21.37  ?  48  PRO C N   1 
ATOM   5186 C  CA  . PRO D 1 53  ? 49.314 -24.956 -5.730  1.00 24.75  ?  48  PRO C CA  1 
ATOM   5187 C  C   . PRO D 1 53  ? 50.030 -26.028 -4.903  1.00 27.97  ?  48  PRO C C   1 
ATOM   5188 O  O   . PRO D 1 53  ? 50.033 -25.917 -3.680  1.00 26.98  ?  48  PRO C O   1 
ATOM   5189 C  CB  . PRO D 1 53  ? 47.824 -25.270 -5.677  1.00 25.31  ?  48  PRO C CB  1 
ATOM   5190 C  CG  . PRO D 1 53  ? 47.554 -26.011 -6.974  1.00 23.31  ?  48  PRO C CG  1 
ATOM   5191 C  CD  . PRO D 1 53  ? 48.472 -25.363 -7.985  1.00 22.22  ?  48  PRO C CD  1 
ATOM   5192 N  N   . GLU D 1 54  ? 50.589 -27.038 -5.572  1.00 29.13  ?  49  GLU C N   1 
ATOM   5193 C  CA  . GLU D 1 54  ? 51.233 -28.186 -4.887  1.00 33.10  ?  49  GLU C CA  1 
ATOM   5194 C  C   . GLU D 1 54  ? 52.641 -27.773 -4.473  1.00 33.99  ?  49  GLU C C   1 
ATOM   5195 O  O   . GLU D 1 54  ? 53.243 -28.515 -3.702  1.00 32.87  ?  49  GLU C O   1 
ATOM   5196 C  CB  . GLU D 1 54  ? 51.249 -29.429 -5.773  1.00 38.28  ?  49  GLU C CB  1 
ATOM   5197 C  CG  . GLU D 1 54  ? 49.874 -29.875 -6.238  1.00 43.88  ?  49  GLU C CG  1 
ATOM   5198 C  CD  . GLU D 1 54  ? 49.228 -30.974 -5.408  1.00 55.11  ?  49  GLU C CD  1 
ATOM   5199 O  OE1 . GLU D 1 54  ? 49.726 -31.247 -4.286  1.00 60.76  ?  49  GLU C OE1 1 
ATOM   5200 O  OE2 . GLU D 1 54  ? 48.226 -31.564 -5.887  1.00 63.10  -1 49  GLU C OE2 1 
ATOM   5201 N  N   . LEU D 1 55  ? 53.145 -26.634 -4.955  1.00 35.20  ?  50  LEU C N   1 
ATOM   5202 C  CA  . LEU D 1 55  ? 54.488 -26.144 -4.546  1.00 38.99  ?  50  LEU C CA  1 
ATOM   5203 C  C   . LEU D 1 55  ? 54.370 -25.612 -3.112  1.00 44.64  ?  50  LEU C C   1 
ATOM   5204 O  O   . LEU D 1 55  ? 53.769 -24.541 -2.917  1.00 46.53  ?  50  LEU C O   1 
ATOM   5205 C  CB  . LEU D 1 55  ? 55.000 -25.081 -5.524  1.00 36.33  ?  50  LEU C CB  1 
ATOM   5206 C  CG  . LEU D 1 55  ? 55.326 -25.571 -6.940  1.00 33.04  ?  50  LEU C CG  1 
ATOM   5207 C  CD1 . LEU D 1 55  ? 55.818 -24.399 -7.785  1.00 31.46  ?  50  LEU C CD1 1 
ATOM   5208 C  CD2 . LEU D 1 55  ? 56.375 -26.678 -6.936  1.00 35.60  ?  50  LEU C CD2 1 
ATOM   5209 N  N   . ASP D 1 56  ? 54.857 -26.406 -2.157  1.00 51.49  ?  51  ASP C N   1 
ATOM   5210 C  CA  . ASP D 1 56  ? 55.133 -26.006 -0.755  1.00 59.48  ?  51  ASP C CA  1 
ATOM   5211 C  C   . ASP D 1 56  ? 56.500 -25.314 -0.737  1.00 60.06  ?  51  ASP C C   1 
ATOM   5212 O  O   . ASP D 1 56  ? 57.412 -25.730 -1.503  1.00 63.44  ?  51  ASP C O   1 
ATOM   5213 C  CB  . ASP D 1 56  ? 55.085 -27.207 0.200   1.00 67.20  ?  51  ASP C CB  1 
ATOM   5214 C  CG  . ASP D 1 56  ? 53.686 -27.746 0.475   1.00 74.25  ?  51  ASP C CG  1 
ATOM   5215 O  OD1 . ASP D 1 56  ? 53.350 -28.821 -0.081  1.00 78.51  ?  51  ASP C OD1 1 
ATOM   5216 O  OD2 . ASP D 1 56  ? 52.944 -27.101 1.261   1.00 75.75  -1 51  ASP C OD2 1 
ATOM   5217 N  N   . GLY D 1 57  ? 56.625 -24.275 0.082   1.00 54.26  ?  52  GLY C N   1 
ATOM   5218 C  CA  . GLY D 1 57  ? 57.890 -23.552 0.277   1.00 47.90  ?  52  GLY C CA  1 
ATOM   5219 C  C   . GLY D 1 57  ? 58.003 -22.372 -0.678  1.00 42.28  ?  52  GLY C C   1 
ATOM   5220 O  O   . GLY D 1 57  ? 57.235 -22.241 -1.636  1.00 35.31  ?  52  GLY C O   1 
ATOM   5221 N  N   . PRO D 1 58  ? 58.977 -21.476 -0.427  1.00 39.61  ?  53  PRO C N   1 
ATOM   5222 C  CA  . PRO D 1 58  ? 59.116 -20.258 -1.219  1.00 35.64  ?  53  PRO C CA  1 
ATOM   5223 C  C   . PRO D 1 58  ? 59.348 -20.625 -2.693  1.00 34.04  ?  53  PRO C C   1 
ATOM   5224 O  O   . PRO D 1 58  ? 60.118 -21.523 -2.986  1.00 32.52  ?  53  PRO C O   1 
ATOM   5225 C  CB  . PRO D 1 58  ? 60.321 -19.528 -0.597  1.00 37.71  ?  53  PRO C CB  1 
ATOM   5226 C  CG  . PRO D 1 58  ? 60.490 -20.172 0.777   1.00 38.75  ?  53  PRO C CG  1 
ATOM   5227 C  CD  . PRO D 1 58  ? 60.007 -21.599 0.621   1.00 40.37  ?  53  PRO C CD  1 
ATOM   5228 N  N   . VAL D 1 59  ? 58.615 -19.961 -3.581  1.00 30.54  ?  54  VAL C N   1 
ATOM   5229 C  CA  . VAL D 1 59  ? 58.818 -20.015 -5.055  1.00 30.66  ?  54  VAL C CA  1 
ATOM   5230 C  C   . VAL D 1 59  ? 59.537 -18.722 -5.412  1.00 30.06  ?  54  VAL C C   1 
ATOM   5231 O  O   . VAL D 1 59  ? 58.893 -17.675 -5.344  1.00 31.35  ?  54  VAL C O   1 
ATOM   5232 C  CB  . VAL D 1 59  ? 57.464 -20.147 -5.780  1.00 28.85  ?  54  VAL C CB  1 
ATOM   5233 C  CG1 . VAL D 1 59  ? 57.626 -20.284 -7.281  1.00 30.46  ?  54  VAL C CG1 1 
ATOM   5234 C  CG2 . VAL D 1 59  ? 56.648 -21.296 -5.222  1.00 30.89  ?  54  VAL C CG2 1 
ATOM   5235 N  N   . ASP D 1 60  ? 60.817 -18.802 -5.747  1.00 34.05  ?  55  ASP C N   1 
ATOM   5236 C  CA  . ASP D 1 60  ? 61.680 -17.622 -6.017  1.00 35.21  ?  55  ASP C CA  1 
ATOM   5237 C  C   . ASP D 1 60  ? 61.834 -17.389 -7.527  1.00 33.01  ?  55  ASP C C   1 
ATOM   5238 O  O   . ASP D 1 60  ? 62.188 -16.251 -7.890  1.00 35.57  ?  55  ASP C O   1 
ATOM   5239 C  CB  . ASP D 1 60  ? 63.020 -17.788 -5.292  1.00 38.77  ?  55  ASP C CB  1 
ATOM   5240 C  CG  . ASP D 1 60  ? 62.848 -17.721 -3.776  1.00 41.83  ?  55  ASP C CG  1 
ATOM   5241 O  OD1 . ASP D 1 60  ? 63.365 -18.619 -3.069  1.00 46.43  ?  55  ASP C OD1 1 
ATOM   5242 O  OD2 . ASP D 1 60  ? 62.171 -16.786 -3.313  1.00 42.55  -1 55  ASP C OD2 1 
ATOM   5243 N  N   . ARG D 1 61  ? 61.574 -18.404 -8.360  1.00 29.12  ?  56  ARG C N   1 
ATOM   5244 C  CA  . ARG D 1 61  ? 61.785 -18.358 -9.836  1.00 31.19  ?  56  ARG C CA  1 
ATOM   5245 C  C   . ARG D 1 61  ? 60.569 -18.944 -10.557 1.00 25.36  ?  56  ARG C C   1 
ATOM   5246 O  O   . ARG D 1 61  ? 60.036 -19.983 -10.114 1.00 24.62  ?  56  ARG C O   1 
ATOM   5247 C  CB  . ARG D 1 61  ? 63.016 -19.167 -10.268 1.00 35.18  ?  56  ARG C CB  1 
ATOM   5248 C  CG  . ARG D 1 61  ? 64.342 -18.464 -10.021 1.00 41.39  ?  56  ARG C CG  1 
ATOM   5249 C  CD  . ARG D 1 61  ? 65.526 -19.317 -10.440 1.00 43.59  ?  56  ARG C CD  1 
ATOM   5250 N  NE  . ARG D 1 61  ? 65.415 -20.601 -9.761  1.00 51.08  ?  56  ARG C NE  1 
ATOM   5251 C  CZ  . ARG D 1 61  ? 65.741 -20.830 -8.489  1.00 51.13  ?  56  ARG C CZ  1 
ATOM   5252 N  NH1 . ARG D 1 61  ? 66.249 -19.864 -7.738  1.00 49.37  ?  56  ARG C NH1 1 
ATOM   5253 N  NH2 . ARG D 1 61  ? 65.569 -22.040 -7.978  1.00 53.12  ?  56  ARG C NH2 1 
ATOM   5254 N  N   . LEU D 1 62  ? 60.168 -18.329 -11.662 1.00 24.75  ?  57  LEU C N   1 
ATOM   5255 C  CA  . LEU D 1 62  ? 59.078 -18.855 -12.519 1.00 21.90  ?  57  LEU C CA  1 
ATOM   5256 C  C   . LEU D 1 62  ? 59.599 -19.932 -13.495 1.00 23.10  ?  57  LEU C C   1 
ATOM   5257 O  O   . LEU D 1 62  ? 58.869 -20.919 -13.713 1.00 22.07  ?  57  LEU C O   1 
ATOM   5258 C  CB  . LEU D 1 62  ? 58.449 -17.684 -13.265 1.00 21.73  ?  57  LEU C CB  1 
ATOM   5259 C  CG  . LEU D 1 62  ? 57.513 -16.804 -12.443 1.00 21.32  ?  57  LEU C CG  1 
ATOM   5260 C  CD1 . LEU D 1 62  ? 57.023 -15.665 -13.306 1.00 20.92  ?  57  LEU C CD1 1 
ATOM   5261 C  CD2 . LEU D 1 62  ? 56.349 -17.578 -11.855 1.00 20.58  ?  57  LEU C CD2 1 
ATOM   5262 N  N   . VAL D 1 63  ? 60.804 -19.798 -14.062 1.00 22.57  ?  58  VAL C N   1 
ATOM   5263 C  CA  . VAL D 1 63  ? 61.328 -20.812 -15.035 1.00 23.43  ?  58  VAL C CA  1 
ATOM   5264 C  C   . VAL D 1 63  ? 61.413 -22.170 -14.329 1.00 23.24  ?  58  VAL C C   1 
ATOM   5265 O  O   . VAL D 1 63  ? 61.980 -22.224 -13.247 1.00 21.90  ?  58  VAL C O   1 
ATOM   5266 C  CB  . VAL D 1 63  ? 62.684 -20.434 -15.671 1.00 23.79  ?  58  VAL C CB  1 
ATOM   5267 C  CG1 . VAL D 1 63  ? 63.210 -21.551 -16.566 1.00 25.32  ?  58  VAL C CG1 1 
ATOM   5268 C  CG2 . VAL D 1 63  ? 62.614 -19.134 -16.457 1.00 23.77  ?  58  VAL C CG2 1 
ATOM   5269 N  N   . GLY D 1 64  ? 60.816 -23.206 -14.911 1.00 23.58  ?  59  GLY C N   1 
ATOM   5270 C  CA  . GLY D 1 64  ? 60.857 -24.583 -14.392 1.00 26.58  ?  59  GLY C CA  1 
ATOM   5271 C  C   . GLY D 1 64  ? 59.567 -24.966 -13.693 1.00 28.65  ?  59  GLY C C   1 
ATOM   5272 O  O   . GLY D 1 64  ? 59.328 -26.173 -13.552 1.00 32.33  ?  59  GLY C O   1 
ATOM   5273 N  N   . ILE D 1 65  ? 58.730 -24.010 -13.289 1.00 25.67  ?  60  ILE C N   1 
ATOM   5274 C  CA  . ILE D 1 65  ? 57.469 -24.338 -12.565 1.00 23.76  ?  60  ILE C CA  1 
ATOM   5275 C  C   . ILE D 1 65  ? 56.319 -24.418 -13.567 1.00 22.65  ?  60  ILE C C   1 
ATOM   5276 O  O   . ILE D 1 65  ? 56.474 -23.968 -14.708 1.00 22.09  ?  60  ILE C O   1 
ATOM   5277 C  CB  . ILE D 1 65  ? 57.196 -23.378 -11.389 1.00 27.82  ?  60  ILE C CB  1 
ATOM   5278 C  CG1 . ILE D 1 65  ? 56.630 -22.023 -11.827 1.00 28.06  ?  60  ILE C CG1 1 
ATOM   5279 C  CG2 . ILE D 1 65  ? 58.461 -23.239 -10.542 1.00 30.02  ?  60  ILE C CG2 1 
ATOM   5280 C  CD1 . ILE D 1 65  ? 55.913 -21.279 -10.737 1.00 31.80  ?  60  ILE C CD1 1 
ATOM   5281 N  N   . THR D 1 66  ? 55.193 -24.981 -13.137 1.00 21.21  ?  61  THR C N   1 
ATOM   5282 C  CA  . THR D 1 66  ? 53.982 -25.129 -13.984 1.00 21.85  ?  61  THR C CA  1 
ATOM   5283 C  C   . THR D 1 66  ? 52.952 -24.130 -13.476 1.00 20.65  ?  61  THR C C   1 
ATOM   5284 O  O   . THR D 1 66  ? 52.759 -24.036 -12.253 1.00 20.65  ?  61  THR C O   1 
ATOM   5285 C  CB  . THR D 1 66  ? 53.463 -26.580 -14.000 1.00 23.38  ?  61  THR C CB  1 
ATOM   5286 O  OG1 . THR D 1 66  ? 54.535 -27.348 -14.544 1.00 25.72  ?  61  THR C OG1 1 
ATOM   5287 C  CG2 . THR D 1 66  ? 52.237 -26.785 -14.863 1.00 22.56  ?  61  THR C CG2 1 
ATOM   5288 N  N   . LEU D 1 67  ? 52.339 -23.389 -14.396 1.00 19.17  ?  62  LEU C N   1 
ATOM   5289 C  CA  . LEU D 1 67  ? 51.206 -22.524 -14.018 1.00 17.34  ?  62  LEU C CA  1 
ATOM   5290 C  C   . LEU D 1 67  ? 49.917 -23.274 -14.357 1.00 16.14  ?  62  LEU C C   1 
ATOM   5291 O  O   . LEU D 1 67  ? 49.945 -24.150 -15.210 1.00 18.48  ?  62  LEU C O   1 
ATOM   5292 C  CB  . LEU D 1 67  ? 51.339 -21.179 -14.730 1.00 17.27  ?  62  LEU C CB  1 
ATOM   5293 C  CG  . LEU D 1 67  ? 52.642 -20.408 -14.485 1.00 17.95  ?  62  LEU C CG  1 
ATOM   5294 C  CD1 . LEU D 1 67  ? 52.599 -19.088 -15.235 1.00 18.43  ?  62  LEU C CD1 1 
ATOM   5295 C  CD2 . LEU D 1 67  ? 52.908 -20.169 -13.013 1.00 20.91  ?  62  LEU C CD2 1 
ATOM   5296 N  N   . TRP D 1 68  ? 48.867 -22.987 -13.609 1.00 16.19  ?  63  TRP C N   1 
ATOM   5297 C  CA  . TRP D 1 68  ? 47.522 -23.559 -13.788 1.00 16.43  ?  63  TRP C CA  1 
ATOM   5298 C  C   . TRP D 1 68  ? 46.600 -22.435 -14.195 1.00 15.84  ?  63  TRP C C   1 
ATOM   5299 O  O   . TRP D 1 68  ? 46.654 -21.359 -13.527 1.00 15.86  ?  63  TRP C O   1 
ATOM   5300 C  CB  . TRP D 1 68  ? 47.017 -24.182 -12.505 1.00 17.11  ?  63  TRP C CB  1 
ATOM   5301 C  CG  . TRP D 1 68  ? 47.730 -25.392 -12.039 1.00 18.18  ?  63  TRP C CG  1 
ATOM   5302 C  CD1 . TRP D 1 68  ? 49.012 -25.809 -12.288 1.00 18.99  ?  63  TRP C CD1 1 
ATOM   5303 C  CD2 . TRP D 1 68  ? 47.168 -26.320 -11.112 1.00 18.97  ?  63  TRP C CD2 1 
ATOM   5304 N  NE1 . TRP D 1 68  ? 49.251 -26.980 -11.618 1.00 19.34  ?  63  TRP C NE1 1 
ATOM   5305 C  CE2 . TRP D 1 68  ? 48.135 -27.320 -10.890 1.00 18.59  ?  63  TRP C CE2 1 
ATOM   5306 C  CE3 . TRP D 1 68  ? 45.913 -26.413 -10.497 1.00 18.26  ?  63  TRP C CE3 1 
ATOM   5307 C  CZ2 . TRP D 1 68  ? 47.892 -28.397 -10.028 1.00 20.87  ?  63  TRP C CZ2 1 
ATOM   5308 C  CZ3 . TRP D 1 68  ? 45.679 -27.472 -9.651  1.00 19.23  ?  63  TRP C CZ3 1 
ATOM   5309 C  CH2 . TRP D 1 68  ? 46.641 -28.457 -9.441  1.00 20.87  ?  63  TRP C CH2 1 
ATOM   5310 N  N   . GLY D 1 69  ? 45.722 -22.710 -15.149 1.00 15.39  ?  64  GLY C N   1 
ATOM   5311 C  CA  . GLY D 1 69  ? 44.753 -21.724 -15.656 1.00 16.07  ?  64  GLY C CA  1 
ATOM   5312 C  C   . GLY D 1 69  ? 43.496 -22.385 -16.160 1.00 14.71  ?  64  GLY C C   1 
ATOM   5313 O  O   . GLY D 1 69  ? 43.453 -23.638 -16.256 1.00 17.28  ?  64  GLY C O   1 
ATOM   5314 N  N   . HIS D 1 70  ? 42.488 -21.603 -16.499 1.00 14.17  ?  65  HIS C N   1 
ATOM   5315 C  CA  . HIS D 1 70  ? 41.343 -22.123 -17.290 1.00 13.79  ?  65  HIS C CA  1 
ATOM   5316 C  C   . HIS D 1 70  ? 40.746 -21.034 -18.129 1.00 14.66  ?  65  HIS C C   1 
ATOM   5317 O  O   . HIS D 1 70  ? 40.967 -19.832 -17.873 1.00 14.10  ?  65  HIS C O   1 
ATOM   5318 C  CB  . HIS D 1 70  ? 40.255 -22.717 -16.408 1.00 15.41  ?  65  HIS C CB  1 
ATOM   5319 C  CG  . HIS D 1 70  ? 39.479 -21.738 -15.592 1.00 12.96  ?  65  HIS C CG  1 
ATOM   5320 N  ND1 . HIS D 1 70  ? 39.997 -21.218 -14.437 1.00 14.25  ?  65  HIS C ND1 1 
ATOM   5321 C  CD2 . HIS D 1 70  ? 38.175 -21.345 -15.621 1.00 17.01  ?  65  HIS C CD2 1 
ATOM   5322 C  CE1 . HIS D 1 70  ? 39.078 -20.476 -13.822 1.00 16.25  ?  65  HIS C CE1 1 
ATOM   5323 N  NE2 . HIS D 1 70  ? 37.948 -20.518 -14.523 1.00 14.98  ?  65  HIS C NE2 1 
ATOM   5324 N  N   . MET D 1 71  ? 39.966 -21.472 -19.087 1.00 15.90  ?  66  MET C N   1 
ATOM   5325 C  CA  . MET D 1 71  ? 39.243 -20.561 -19.981 1.00 16.70  ?  66  MET C CA  1 
ATOM   5326 C  C   . MET D 1 71  ? 37.951 -21.291 -20.297 1.00 15.94  ?  66  MET C C   1 
ATOM   5327 O  O   . MET D 1 71  ? 37.777 -22.414 -19.776 1.00 16.03  ?  66  MET C O   1 
ATOM   5328 C  CB  . MET D 1 71  ? 40.001 -20.237 -21.266 1.00 17.98  ?  66  MET C CB  1 
ATOM   5329 C  CG  . MET D 1 71  ? 39.857 -21.239 -22.396 1.00 20.43  ?  66  MET C CG  1 
ATOM   5330 S  SD  . MET D 1 71  ? 40.785 -20.727 -23.886 1.00 26.79  ?  66  MET C SD  1 
ATOM   5331 C  CE  . MET D 1 71  ? 42.326 -21.109 -23.086 1.00 21.34  ?  66  MET C CE  1 
ATOM   5332 N  N   . ASN D 1 72  ? 37.145 -20.668 -21.120 1.00 14.87  ?  67  ASN C N   1 
ATOM   5333 C  CA  . ASN D 1 72  ? 35.830 -21.193 -21.564 1.00 16.50  ?  67  ASN C CA  1 
ATOM   5334 C  C   . ASN D 1 72  ? 36.114 -22.128 -22.745 1.00 17.17  ?  67  ASN C C   1 
ATOM   5335 O  O   . ASN D 1 72  ? 36.755 -21.678 -23.734 1.00 16.42  ?  67  ASN C O   1 
ATOM   5336 C  CB  . ASN D 1 72  ? 34.873 -20.059 -21.894 1.00 15.56  ?  67  ASN C CB  1 
ATOM   5337 C  CG  . ASN D 1 72  ? 33.497 -20.593 -22.214 1.00 19.71  ?  67  ASN C CG  1 
ATOM   5338 O  OD1 . ASN D 1 72  ? 33.320 -21.794 -22.506 1.00 15.80  ?  67  ASN C OD1 1 
ATOM   5339 N  ND2 . ASN D 1 72  ? 32.511 -19.718 -22.134 1.00 19.27  ?  67  ASN C ND2 1 
ATOM   5340 N  N   . ARG D 1 73  ? 35.712 -23.392 -22.630 1.00 18.34  ?  68  ARG C N   1 
ATOM   5341 C  CA  . ARG D 1 73  ? 35.879 -24.408 -23.707 1.00 20.00  ?  68  ARG C CA  1 
ATOM   5342 C  C   . ARG D 1 73  ? 35.198 -23.956 -24.977 1.00 21.75  ?  68  ARG C C   1 
ATOM   5343 O  O   . ARG D 1 73  ? 35.580 -24.487 -25.989 1.00 22.92  ?  68  ARG C O   1 
ATOM   5344 C  CB  . ARG D 1 73  ? 35.298 -25.766 -23.319 1.00 22.07  ?  68  ARG C CB  1 
ATOM   5345 C  CG  . ARG D 1 73  ? 36.321 -26.629 -22.621 1.00 21.87  ?  68  ARG C CG  1 
ATOM   5346 C  CD  . ARG D 1 73  ? 35.934 -28.081 -22.666 1.00 21.49  ?  68  ARG C CD  1 
ATOM   5347 N  NE  . ARG D 1 73  ? 36.830 -28.660 -21.735 1.00 18.12  ?  68  ARG C NE  1 
ATOM   5348 C  CZ  . ARG D 1 73  ? 37.680 -29.629 -22.021 1.00 19.34  ?  68  ARG C CZ  1 
ATOM   5349 N  NH1 . ARG D 1 73  ? 37.665 -30.193 -23.213 1.00 17.97  ?  68  ARG C NH1 1 
ATOM   5350 N  NH2 . ARG D 1 73  ? 38.500 -30.070 -21.089 1.00 21.32  ?  68  ARG C NH2 1 
ATOM   5351 N  N   . ALA D 1 74  ? 34.186 -23.078 -24.878 1.00 20.20  ?  69  ALA C N   1 
ATOM   5352 C  CA  . ALA D 1 74  ? 33.391 -22.555 -26.010 1.00 22.50  ?  69  ALA C CA  1 
ATOM   5353 C  C   . ALA D 1 74  ? 34.130 -21.386 -26.647 1.00 19.58  ?  69  ALA C C   1 
ATOM   5354 O  O   . ALA D 1 74  ? 33.766 -20.956 -27.745 1.00 19.02  ?  69  ALA C O   1 
ATOM   5355 C  CB  . ALA D 1 74  ? 31.997 -22.124 -25.578 1.00 23.03  ?  69  ALA C CB  1 
ATOM   5356 N  N   . ASN D 1 75  ? 35.117 -20.842 -25.969 1.00 20.90  ?  70  ASN C N   1 
ATOM   5357 C  CA  . ASN D 1 75  ? 35.923 -19.754 -26.566 1.00 20.13  ?  70  ASN C CA  1 
ATOM   5358 C  C   . ASN D 1 75  ? 36.660 -20.366 -27.752 1.00 19.28  ?  70  ASN C C   1 
ATOM   5359 O  O   . ASN D 1 75  ? 37.426 -21.331 -27.574 1.00 18.09  ?  70  ASN C O   1 
ATOM   5360 C  CB  . ASN D 1 75  ? 36.841 -19.185 -25.492 1.00 18.39  ?  70  ASN C CB  1 
ATOM   5361 C  CG  . ASN D 1 75  ? 37.725 -18.039 -25.910 1.00 18.99  ?  70  ASN C CG  1 
ATOM   5362 O  OD1 . ASN D 1 75  ? 37.971 -17.822 -27.098 1.00 18.41  ?  70  ASN C OD1 1 
ATOM   5363 N  ND2 . ASN D 1 75  ? 38.248 -17.351 -24.902 1.00 18.23  ?  70  ASN C ND2 1 
ATOM   5364 N  N   . PRO D 1 76  ? 36.543 -19.812 -28.968 1.00 15.88  ?  71  PRO C N   1 
ATOM   5365 C  CA  . PRO D 1 76  ? 37.304 -20.358 -30.104 1.00 17.36  ?  71  PRO C CA  1 
ATOM   5366 C  C   . PRO D 1 76  ? 38.821 -20.447 -29.919 1.00 18.49  ?  71  PRO C C   1 
ATOM   5367 O  O   . PRO D 1 76  ? 39.466 -21.235 -30.607 1.00 17.61  ?  71  PRO C O   1 
ATOM   5368 C  CB  . PRO D 1 76  ? 36.958 -19.388 -31.253 1.00 18.06  ?  71  PRO C CB  1 
ATOM   5369 C  CG  . PRO D 1 76  ? 35.533 -18.965 -30.872 1.00 18.02  ?  71  PRO C CG  1 
ATOM   5370 C  CD  . PRO D 1 76  ? 35.659 -18.703 -29.387 1.00 17.57  ?  71  PRO C CD  1 
ATOM   5371 N  N   . HIS D 1 77  ? 39.378 -19.655 -29.002 1.00 17.74  ?  72  HIS C N   1 
ATOM   5372 C  CA  . HIS D 1 77  ? 40.814 -19.712 -28.626 1.00 16.10  ?  72  HIS C CA  1 
ATOM   5373 C  C   . HIS D 1 77  ? 41.166 -21.116 -28.121 1.00 16.98  ?  72  HIS C C   1 
ATOM   5374 O  O   . HIS D 1 77  ? 42.234 -21.615 -28.418 1.00 17.48  ?  72  HIS C O   1 
ATOM   5375 C  CB  . HIS D 1 77  ? 41.121 -18.640 -27.571 1.00 16.28  ?  72  HIS C CB  1 
ATOM   5376 C  CG  . HIS D 1 77  ? 42.588 -18.401 -27.367 1.00 14.84  ?  72  HIS C CG  1 
ATOM   5377 N  ND1 . HIS D 1 77  ? 43.039 -17.369 -26.567 1.00 14.99  ?  72  HIS C ND1 1 
ATOM   5378 C  CD2 . HIS D 1 77  ? 43.684 -18.978 -27.914 1.00 16.38  ?  72  HIS C CD2 1 
ATOM   5379 C  CE1 . HIS D 1 77  ? 44.380 -17.335 -26.613 1.00 15.67  ?  72  HIS C CE1 1 
ATOM   5380 N  NE2 . HIS D 1 77  ? 44.809 -18.376 -27.353 1.00 16.17  ?  72  HIS C NE2 1 
ATOM   5381 N  N   . TRP D 1 78  ? 40.280 -21.736 -27.367 1.00 17.73  ?  73  TRP C N   1 
ATOM   5382 C  CA  . TRP D 1 78  ? 40.481 -23.124 -26.879 1.00 19.36  ?  73  TRP C CA  1 
ATOM   5383 C  C   . TRP D 1 78  ? 40.738 -24.080 -28.055 1.00 19.49  ?  73  TRP C C   1 
ATOM   5384 O  O   . TRP D 1 78  ? 41.690 -24.873 -27.941 1.00 17.06  ?  73  TRP C O   1 
ATOM   5385 C  CB  . TRP D 1 78  ? 39.293 -23.597 -26.025 1.00 20.01  ?  73  TRP C CB  1 
ATOM   5386 C  CG  . TRP D 1 78  ? 39.468 -25.010 -25.541 1.00 18.07  ?  73  TRP C CG  1 
ATOM   5387 C  CD1 . TRP D 1 78  ? 38.954 -26.123 -26.150 1.00 18.91  ?  73  TRP C CD1 1 
ATOM   5388 C  CD2 . TRP D 1 78  ? 40.209 -25.479 -24.408 1.00 16.04  ?  73  TRP C CD2 1 
ATOM   5389 N  NE1 . TRP D 1 78  ? 39.242 -27.231 -25.422 1.00 20.84  ?  73  TRP C NE1 1 
ATOM   5390 C  CE2 . TRP D 1 78  ? 40.024 -26.875 -24.355 1.00 18.46  ?  73  TRP C CE2 1 
ATOM   5391 C  CE3 . TRP D 1 78  ? 41.000 -24.877 -23.432 1.00 16.28  ?  73  TRP C CE3 1 
ATOM   5392 C  CZ2 . TRP D 1 78  ? 40.619 -27.675 -23.386 1.00 19.86  ?  73  TRP C CZ2 1 
ATOM   5393 C  CZ3 . TRP D 1 78  ? 41.563 -25.665 -22.448 1.00 16.19  ?  73  TRP C CZ3 1 
ATOM   5394 C  CH2 . TRP D 1 78  ? 41.400 -27.047 -22.449 1.00 17.81  ?  73  TRP C CH2 1 
ATOM   5395 N  N   . ALA D 1 79  ? 39.960 -23.993 -29.143 1.00 18.57  ?  74  ALA C N   1 
ATOM   5396 C  CA  . ALA D 1 79  ? 40.049 -24.934 -30.294 1.00 23.57  ?  74  ALA C CA  1 
ATOM   5397 C  C   . ALA D 1 79  ? 41.343 -24.670 -31.081 1.00 23.98  ?  74  ALA C C   1 
ATOM   5398 O  O   . ALA D 1 79  ? 42.038 -25.646 -31.579 1.00 23.77  ?  74  ALA C O   1 
ATOM   5399 C  CB  . ALA D 1 79  ? 38.802 -24.783 -31.135 1.00 22.83  ?  74  ALA C CB  1 
ATOM   5400 N  N   . ALA D 1 80  ? 41.748 -23.404 -31.088 1.00 25.61  ?  75  ALA C N   1 
ATOM   5401 C  CA  . ALA D 1 80  ? 42.856 -22.862 -31.900 1.00 24.77  ?  75  ALA C CA  1 
ATOM   5402 C  C   . ALA D 1 80  ? 44.183 -23.241 -31.258 1.00 27.51  ?  75  ALA C C   1 
ATOM   5403 O  O   . ALA D 1 80  ? 45.186 -23.311 -31.992 1.00 30.23  ?  75  ALA C O   1 
ATOM   5404 C  CB  . ALA D 1 80  ? 42.717 -21.372 -32.079 1.00 24.69  ?  75  ALA C CB  1 
ATOM   5405 N  N   . LEU D 1 81  ? 44.198 -23.530 -29.962 1.00 28.93  ?  76  LEU C N   1 
ATOM   5406 C  CA  . LEU D 1 81  ? 45.456 -23.927 -29.281 1.00 29.37  ?  76  LEU C CA  1 
ATOM   5407 C  C   . LEU D 1 81  ? 45.944 -25.271 -29.851 1.00 40.28  ?  76  LEU C C   1 
ATOM   5408 O  O   . LEU D 1 81  ? 47.110 -25.345 -30.303 1.00 37.17  ?  76  LEU C O   1 
ATOM   5409 C  CB  . LEU D 1 81  ? 45.233 -23.932 -27.766 1.00 27.01  ?  76  LEU C CB  1 
ATOM   5410 C  CG  . LEU D 1 81  ? 45.146 -22.526 -27.153 1.00 26.17  ?  76  LEU C CG  1 
ATOM   5411 C  CD1 . LEU D 1 81  ? 44.538 -22.555 -25.753 1.00 26.00  ?  76  LEU C CD1 1 
ATOM   5412 C  CD2 . LEU D 1 81  ? 46.527 -21.874 -27.141 1.00 25.89  ?  76  LEU C CD2 1 
ATOM   5413 N  N   . GLY D 1 82  ? 45.072 -26.273 -29.932 1.00 44.57  ?  77  GLY C N   1 
ATOM   5414 C  CA  . GLY D 1 82  ? 45.505 -27.605 -30.388 1.00 47.49  ?  77  GLY C CA  1 
ATOM   5415 C  C   . GLY D 1 82  ? 46.417 -28.221 -29.350 1.00 53.33  ?  77  GLY C C   1 
ATOM   5416 O  O   . GLY D 1 82  ? 46.246 -27.898 -28.143 1.00 55.03  ?  77  GLY C O   1 
ATOM   5417 N  N   . GLY D 1 83  ? 47.375 -29.035 -29.788 1.00 56.01  ?  78  GLY C N   1 
ATOM   5418 C  CA  . GLY D 1 83  ? 48.034 -30.022 -28.918 1.00 54.15  ?  78  GLY C CA  1 
ATOM   5419 C  C   . GLY D 1 83  ? 49.098 -29.392 -28.050 1.00 53.74  ?  78  GLY C C   1 
ATOM   5420 O  O   . GLY D 1 83  ? 48.965 -29.451 -26.805 1.00 54.61  ?  78  GLY C O   1 
ATOM   5421 N  N   . ALA D 1 84  ? 50.147 -28.860 -28.677 1.00 52.36  ?  79  ALA C N   1 
ATOM   5422 C  CA  . ALA D 1 84  ? 51.356 -28.347 -27.996 1.00 43.80  ?  79  ALA C CA  1 
ATOM   5423 C  C   . ALA D 1 84  ? 51.608 -26.896 -28.419 1.00 41.75  ?  79  ALA C C   1 
ATOM   5424 O  O   . ALA D 1 84  ? 52.710 -26.617 -28.909 1.00 41.14  ?  79  ALA C O   1 
ATOM   5425 C  CB  . ALA D 1 84  ? 52.511 -29.232 -28.345 1.00 44.57  ?  79  ALA C CB  1 
ATOM   5426 N  N   . ALA D 1 85  ? 50.624 -26.006 -28.243 1.00 36.64  ?  80  ALA C N   1 
ATOM   5427 C  CA  . ALA D 1 85  ? 50.740 -24.579 -28.634 1.00 31.34  ?  80  ALA C CA  1 
ATOM   5428 C  C   . ALA D 1 85  ? 51.838 -23.903 -27.807 1.00 26.61  ?  80  ALA C C   1 
ATOM   5429 O  O   . ALA D 1 85  ? 51.862 -24.075 -26.573 1.00 23.09  ?  80  ALA C O   1 
ATOM   5430 C  CB  . ALA D 1 85  ? 49.436 -23.864 -28.464 1.00 32.38  ?  80  ALA C CB  1 
ATOM   5431 N  N   . ASN D 1 86  ? 52.723 -23.163 -28.479 1.00 25.02  ?  81  ASN C N   1 
ATOM   5432 C  CA  . ASN D 1 86  ? 53.710 -22.257 -27.831 1.00 24.54  ?  81  ASN C CA  1 
ATOM   5433 C  C   . ASN D 1 86  ? 53.010 -20.937 -27.492 1.00 20.75  ?  81  ASN C C   1 
ATOM   5434 O  O   . ASN D 1 86  ? 52.539 -20.270 -28.423 1.00 21.86  ?  81  ASN C O   1 
ATOM   5435 C  CB  . ASN D 1 86  ? 54.912 -22.058 -28.733 1.00 25.79  ?  81  ASN C CB  1 
ATOM   5436 C  CG  . ASN D 1 86  ? 55.697 -23.341 -28.896 1.00 29.57  ?  81  ASN C CG  1 
ATOM   5437 O  OD1 . ASN D 1 86  ? 55.873 -24.103 -27.943 1.00 30.79  ?  81  ASN C OD1 1 
ATOM   5438 N  ND2 . ASN D 1 86  ? 56.180 -23.571 -30.098 1.00 32.75  ?  81  ASN C ND2 1 
ATOM   5439 N  N   . VAL D 1 87  ? 52.892 -20.620 -26.206 1.00 18.63  ?  82  VAL C N   1 
ATOM   5440 C  CA  . VAL D 1 87  ? 52.030 -19.493 -25.759 1.00 17.61  ?  82  VAL C CA  1 
ATOM   5441 C  C   . VAL D 1 87  ? 52.865 -18.500 -24.958 1.00 16.49  ?  82  VAL C C   1 
ATOM   5442 O  O   . VAL D 1 87  ? 53.976 -18.825 -24.488 1.00 16.56  ?  82  VAL C O   1 
ATOM   5443 C  CB  . VAL D 1 87  ? 50.804 -19.988 -24.971 1.00 19.61  ?  82  VAL C CB  1 
ATOM   5444 C  CG1 . VAL D 1 87  ? 49.986 -20.985 -25.775 1.00 21.58  ?  82  VAL C CG1 1 
ATOM   5445 C  CG2 . VAL D 1 87  ? 51.174 -20.561 -23.619 1.00 18.82  ?  82  VAL C CG2 1 
ATOM   5446 N  N   . VAL D 1 88  ? 52.316 -17.306 -24.801 1.00 16.93  ?  83  VAL C N   1 
ATOM   5447 C  CA  . VAL D 1 88  ? 52.818 -16.298 -23.840 1.00 15.37  ?  83  VAL C CA  1 
ATOM   5448 C  C   . VAL D 1 88  ? 51.616 -15.909 -22.991 1.00 14.62  ?  83  VAL C C   1 
ATOM   5449 O  O   . VAL D 1 88  ? 50.499 -15.753 -23.539 1.00 16.14  ?  83  VAL C O   1 
ATOM   5450 C  CB  . VAL D 1 88  ? 53.495 -15.104 -24.534 1.00 15.45  ?  83  VAL C CB  1 
ATOM   5451 C  CG1 . VAL D 1 88  ? 52.575 -14.462 -25.561 1.00 15.36  ?  83  VAL C CG1 1 
ATOM   5452 C  CG2 . VAL D 1 88  ? 53.985 -14.074 -23.543 1.00 16.10  ?  83  VAL C CG2 1 
ATOM   5453 N  N   . ALA D 1 89  ? 51.834 -15.861 -21.686 1.00 14.92  ?  84  ALA C N   1 
ATOM   5454 C  CA  . ALA D 1 89  ? 50.885 -15.307 -20.699 1.00 14.93  ?  84  ALA C CA  1 
ATOM   5455 C  C   . ALA D 1 89  ? 51.531 -14.048 -20.107 1.00 15.89  ?  84  ALA C C   1 
ATOM   5456 O  O   . ALA D 1 89  ? 52.702 -14.129 -19.600 1.00 16.29  ?  84  ALA C O   1 
ATOM   5457 C  CB  . ALA D 1 89  ? 50.541 -16.344 -19.666 1.00 15.14  ?  84  ALA C CB  1 
ATOM   5458 N  N   . THR D 1 90  ? 50.862 -12.910 -20.238 1.00 16.06  ?  85  THR C N   1 
ATOM   5459 C  CA  . THR D 1 90  ? 51.386 -11.593 -19.779 1.00 14.31  ?  85  THR C CA  1 
ATOM   5460 C  C   . THR D 1 90  ? 50.587 -11.121 -18.571 1.00 14.19  ?  85  THR C C   1 
ATOM   5461 O  O   . THR D 1 90  ? 49.320 -11.067 -18.622 1.00 13.76  ?  85  THR C O   1 
ATOM   5462 C  CB  . THR D 1 90  ? 51.358 -10.512 -20.875 1.00 15.82  ?  85  THR C CB  1 
ATOM   5463 O  OG1 . THR D 1 90  ? 52.054 -11.012 -22.023 1.00 15.79  ?  85  THR C OG1 1 
ATOM   5464 C  CG2 . THR D 1 90  ? 51.933 -9.196  -20.376 1.00 15.24  ?  85  THR C CG2 1 
ATOM   5465 N  N   . PHE D 1 91  ? 51.284 -10.777 -17.527 1.00 13.61  ?  86  PHE C N   1 
ATOM   5466 C  CA  . PHE D 1 91  ? 50.704 -10.310 -16.251 1.00 14.89  ?  86  PHE C CA  1 
ATOM   5467 C  C   . PHE D 1 91  ? 51.074 -8.839  -16.128 1.00 16.03  ?  86  PHE C C   1 
ATOM   5468 O  O   . PHE D 1 91  ? 52.284 -8.474  -16.302 1.00 17.32  ?  86  PHE C O   1 
ATOM   5469 C  CB  . PHE D 1 91  ? 51.186 -11.151 -15.082 1.00 15.23  ?  86  PHE C CB  1 
ATOM   5470 C  CG  . PHE D 1 91  ? 50.906 -12.637 -15.213 1.00 14.97  ?  86  PHE C CG  1 
ATOM   5471 C  CD1 . PHE D 1 91  ? 51.701 -13.453 -15.998 1.00 14.88  ?  86  PHE C CD1 1 
ATOM   5472 C  CD2 . PHE D 1 91  ? 49.905 -13.229 -14.477 1.00 14.71  ?  86  PHE C CD2 1 
ATOM   5473 C  CE1 . PHE D 1 91  ? 51.480 -14.816 -16.053 1.00 15.60  ?  86  PHE C CE1 1 
ATOM   5474 C  CE2 . PHE D 1 91  ? 49.702 -14.598 -14.514 1.00 14.94  ?  86  PHE C CE2 1 
ATOM   5475 C  CZ  . PHE D 1 91  ? 50.463 -15.386 -15.341 1.00 15.07  ?  86  PHE C CZ  1 
ATOM   5476 N  N   . ALA D 1 92  ? 50.068 -7.999  -15.900 1.00 16.26  ?  87  ALA C N   1 
ATOM   5477 C  CA  . ALA D 1 92  ? 50.237 -6.523  -15.842 1.00 16.76  ?  87  ALA C CA  1 
ATOM   5478 C  C   . ALA D 1 92  ? 49.979 -6.034  -14.419 1.00 17.90  ?  87  ALA C C   1 
ATOM   5479 O  O   . ALA D 1 92  ? 48.904 -6.322  -13.852 1.00 17.42  ?  87  ALA C O   1 
ATOM   5480 C  CB  . ALA D 1 92  ? 49.356 -5.814  -16.843 1.00 17.46  ?  87  ALA C CB  1 
ATOM   5481 N  N   . GLY D 1 93  ? 50.990 -5.405  -13.834 1.00 17.01  ?  88  GLY C N   1 
ATOM   5482 C  CA  . GLY D 1 93  ? 50.941 -4.903  -12.456 1.00 16.81  ?  88  GLY C CA  1 
ATOM   5483 C  C   . GLY D 1 93  ? 50.750 -3.402  -12.391 1.00 16.20  ?  88  GLY C C   1 
ATOM   5484 O  O   . GLY D 1 93  ? 50.177 -2.795  -13.306 1.00 15.47  ?  88  GLY C O   1 
ATOM   5485 N  N   . PRO D 1 94  ? 51.149 -2.799  -11.253 1.00 16.85  ?  89  PRO C N   1 
ATOM   5486 C  CA  . PRO D 1 94  ? 50.970 -1.372  -11.041 1.00 16.83  ?  89  PRO C CA  1 
ATOM   5487 C  C   . PRO D 1 94  ? 51.594 -0.577  -12.204 1.00 15.24  ?  89  PRO C C   1 
ATOM   5488 O  O   . PRO D 1 94  ? 52.630 -0.945  -12.793 1.00 17.72  ?  89  PRO C O   1 
ATOM   5489 C  CB  . PRO D 1 94  ? 51.609 -1.101  -9.670  1.00 17.85  ?  89  PRO C CB  1 
ATOM   5490 C  CG  . PRO D 1 94  ? 51.471 -2.410  -8.967  1.00 17.56  ?  89  PRO C CG  1 
ATOM   5491 C  CD  . PRO D 1 94  ? 51.692 -3.452  -10.059 1.00 18.21  ?  89  PRO C CD  1 
ATOM   5492 N  N   . ASN D 1 95  ? 50.965 0.548   -12.523 1.00 15.78  ?  90  ASN C N   1 
ATOM   5493 C  CA  . ASN D 1 95  ? 51.446 1.428   -13.635 1.00 15.18  ?  90  ASN C CA  1 
ATOM   5494 C  C   . ASN D 1 95  ? 50.937 2.846   -13.399 1.00 14.26  ?  90  ASN C C   1 
ATOM   5495 O  O   . ASN D 1 95  ? 49.803 2.983   -12.864 1.00 14.49  ?  90  ASN C O   1 
ATOM   5496 C  CB  . ASN D 1 95  ? 51.055 0.861   -15.008 1.00 13.23  ?  90  ASN C CB  1 
ATOM   5497 C  CG  . ASN D 1 95  ? 49.567 0.903   -15.268 1.00 16.85  ?  90  ASN C CG  1 
ATOM   5498 O  OD1 . ASN D 1 95  ? 49.052 1.898   -15.753 1.00 18.65  ?  90  ASN C OD1 1 
ATOM   5499 N  ND2 . ASN D 1 95  ? 48.848 -0.150  -14.881 1.00 16.46  ?  90  ASN C ND2 1 
ATOM   5500 N  N   . ALA D 1 96  ? 51.640 3.858   -13.919 1.00 13.56  ?  91  ALA C N   1 
ATOM   5501 C  CA  . ALA D 1 96  ? 51.150 5.256   -13.912 1.00 14.96  ?  91  ALA C CA  1 
ATOM   5502 C  C   . ALA D 1 96  ? 51.853 6.083   -14.970 1.00 16.23  ?  91  ALA C C   1 
ATOM   5503 O  O   . ALA D 1 96  ? 53.074 5.911   -15.134 1.00 15.24  ?  91  ALA C O   1 
ATOM   5504 C  CB  . ALA D 1 96  ? 51.346 5.892   -12.581 1.00 15.03  ?  91  ALA C CB  1 
ATOM   5505 N  N   . TYR D 1 97  ? 51.112 7.014   -15.542 1.00 17.08  ?  92  TYR C N   1 
ATOM   5506 C  CA  . TYR D 1 97  ? 51.690 8.073   -16.405 1.00 18.17  ?  92  TYR C CA  1 
ATOM   5507 C  C   . TYR D 1 97  ? 52.660 8.940   -15.624 1.00 17.72  ?  92  TYR C C   1 
ATOM   5508 O  O   . TYR D 1 97  ? 52.336 9.289   -14.490 1.00 15.87  ?  92  TYR C O   1 
ATOM   5509 C  CB  . TYR D 1 97  ? 50.599 8.962   -16.955 1.00 17.89  ?  92  TYR C CB  1 
ATOM   5510 C  CG  . TYR D 1 97  ? 51.127 10.047  -17.853 1.00 17.72  ?  92  TYR C CG  1 
ATOM   5511 C  CD1 . TYR D 1 97  ? 51.581 9.750   -19.125 1.00 15.91  ?  92  TYR C CD1 1 
ATOM   5512 C  CD2 . TYR D 1 97  ? 51.149 11.367  -17.431 1.00 16.92  ?  92  TYR C CD2 1 
ATOM   5513 C  CE1 . TYR D 1 97  ? 51.998 10.747  -19.986 1.00 16.13  ?  92  TYR C CE1 1 
ATOM   5514 C  CE2 . TYR D 1 97  ? 51.602 12.372  -18.261 1.00 17.08  ?  92  TYR C CE2 1 
ATOM   5515 C  CZ  . TYR D 1 97  ? 52.037 12.054  -19.541 1.00 15.03  ?  92  TYR C CZ  1 
ATOM   5516 O  OH  . TYR D 1 97  ? 52.410 13.025  -20.393 1.00 15.06  ?  92  TYR C OH  1 
ATOM   5517 N  N   . VAL D 1 98  ? 53.837 9.220   -16.215 1.00 15.90  ?  93  VAL C N   1 
ATOM   5518 C  CA  . VAL D 1 98  ? 54.858 10.122  -15.625 1.00 15.65  ?  93  VAL C CA  1 
ATOM   5519 C  C   . VAL D 1 98  ? 54.854 11.433  -16.416 1.00 14.78  ?  93  VAL C C   1 
ATOM   5520 O  O   . VAL D 1 98  ? 55.368 11.470  -17.546 1.00 16.32  ?  93  VAL C O   1 
ATOM   5521 C  CB  . VAL D 1 98  ? 56.254 9.508   -15.643 1.00 15.88  ?  93  VAL C CB  1 
ATOM   5522 C  CG1 . VAL D 1 98  ? 57.207 10.490  -15.024 1.00 16.43  ?  93  VAL C CG1 1 
ATOM   5523 C  CG2 . VAL D 1 98  ? 56.272 8.186   -14.907 1.00 15.73  ?  93  VAL C CG2 1 
ATOM   5524 N  N   . SER D 1 99  ? 54.449 12.498  -15.753 1.00 15.16  ?  94  SER C N   1 
ATOM   5525 C  CA  . SER D 1 99  ? 54.531 13.882  -16.268 1.00 15.51  ?  94  SER C CA  1 
ATOM   5526 C  C   . SER D 1 99  ? 55.912 14.443  -16.007 1.00 14.99  ?  94  SER C C   1 
ATOM   5527 O  O   . SER D 1 99  ? 56.236 14.609  -14.848 1.00 17.46  ?  94  SER C O   1 
ATOM   5528 C  CB  . SER D 1 99  ? 53.554 14.741  -15.582 1.00 13.50  ?  94  SER C CB  1 
ATOM   5529 O  OG  . SER D 1 99  ? 53.651 16.099  -16.068 1.00 15.56  ?  94  SER C OG  1 
ATOM   5530 N  N   . PRO D 1 100 ? 56.639 14.999  -17.008 1.00 15.96  ?  95  PRO C N   1 
ATOM   5531 C  CA  . PRO D 1 100 ? 57.929 15.637  -16.716 1.00 16.49  ?  95  PRO C CA  1 
ATOM   5532 C  C   . PRO D 1 100 ? 57.744 16.871  -15.805 1.00 16.04  ?  95  PRO C C   1 
ATOM   5533 O  O   . PRO D 1 100 ? 58.680 17.365  -15.331 1.00 16.25  ?  95  PRO C O   1 
ATOM   5534 C  CB  . PRO D 1 100 ? 58.449 16.065  -18.112 1.00 17.18  ?  95  PRO C CB  1 
ATOM   5535 C  CG  . PRO D 1 100 ? 57.668 15.209  -19.097 1.00 16.62  ?  95  PRO C CG  1 
ATOM   5536 C  CD  . PRO D 1 100 ? 56.297 15.075  -18.440 1.00 14.85  ?  95  PRO C CD  1 
ATOM   5537 N  N   . ALA D 1 101 ? 56.513 17.365  -15.584 1.00 19.43  ?  96  ALA C N   1 
ATOM   5538 C  CA  . ALA D 1 101 ? 56.327 18.454  -14.597 1.00 21.47  ?  96  ALA C CA  1 
ATOM   5539 C  C   . ALA D 1 101 ? 56.971 17.996  -13.281 1.00 24.59  ?  96  ALA C C   1 
ATOM   5540 O  O   . ALA D 1 101 ? 57.407 18.856  -12.529 1.00 22.13  ?  96  ALA C O   1 
ATOM   5541 C  CB  . ALA D 1 101 ? 54.880 18.813  -14.411 1.00 21.38  ?  96  ALA C CB  1 
ATOM   5542 N  N   . VAL D 1 102 ? 56.939 16.690  -12.995 1.00 21.62  ?  97  VAL C N   1 
ATOM   5543 C  CA  . VAL D 1 102 ? 57.288 16.132  -11.659 1.00 22.69  ?  97  VAL C CA  1 
ATOM   5544 C  C   . VAL D 1 102 ? 58.810 16.160  -11.545 1.00 23.39  ?  97  VAL C C   1 
ATOM   5545 O  O   . VAL D 1 102 ? 59.309 16.291  -10.426 1.00 25.32  ?  97  VAL C O   1 
ATOM   5546 C  CB  . VAL D 1 102 ? 56.746 14.703  -11.514 1.00 23.83  ?  97  VAL C CB  1 
ATOM   5547 C  CG1 . VAL D 1 102 ? 57.363 13.944  -10.356 1.00 26.04  ?  97  VAL C CG1 1 
ATOM   5548 C  CG2 . VAL D 1 102 ? 55.233 14.727  -11.401 1.00 24.34  ?  97  VAL C CG2 1 
ATOM   5549 N  N   . TYR D 1 103 ? 59.498 16.002  -12.667 1.00 23.42  ?  98  TYR C N   1 
ATOM   5550 C  CA  . TYR D 1 103 ? 60.986 16.011  -12.717 1.00 19.59  ?  98  TYR C CA  1 
ATOM   5551 C  C   . TYR D 1 103 ? 61.542 17.378  -12.319 1.00 23.46  ?  98  TYR C C   1 
ATOM   5552 O  O   . TYR D 1 103 ? 62.629 17.382  -11.710 1.00 25.02  ?  98  TYR C O   1 
ATOM   5553 C  CB  . TYR D 1 103 ? 61.481 15.683  -14.109 1.00 18.26  ?  98  TYR C CB  1 
ATOM   5554 C  CG  . TYR D 1 103 ? 61.097 14.354  -14.709 1.00 18.61  ?  98  TYR C CG  1 
ATOM   5555 C  CD1 . TYR D 1 103 ? 60.659 13.267  -13.958 1.00 17.69  ?  98  TYR C CD1 1 
ATOM   5556 C  CD2 . TYR D 1 103 ? 61.265 14.175  -16.073 1.00 19.17  ?  98  TYR C CD2 1 
ATOM   5557 C  CE1 . TYR D 1 103 ? 60.411 12.047  -14.559 1.00 19.42  ?  98  TYR C CE1 1 
ATOM   5558 C  CE2 . TYR D 1 103 ? 60.999 12.969  -16.693 1.00 20.03  ?  98  TYR C CE2 1 
ATOM   5559 C  CZ  . TYR D 1 103 ? 60.576 11.897  -15.927 1.00 19.15  ?  98  TYR C CZ  1 
ATOM   5560 O  OH  . TYR D 1 103 ? 60.369 10.731  -16.588 1.00 18.92  ?  98  TYR C OH  1 
ATOM   5561 N  N   . ARG D 1 104 ? 60.849 18.474  -12.648 1.00 23.64  ?  99  ARG C N   1 
ATOM   5562 C  CA  . ARG D 1 104 ? 61.354 19.858  -12.449 1.00 31.71  ?  99  ARG C CA  1 
ATOM   5563 C  C   . ARG D 1 104 ? 62.710 19.992  -13.170 1.00 30.47  ?  99  ARG C C   1 
ATOM   5564 O  O   . ARG D 1 104 ? 63.622 20.604  -12.638 1.00 36.29  ?  99  ARG C O   1 
ATOM   5565 C  CB  . ARG D 1 104 ? 61.418 20.172  -10.950 1.00 32.91  ?  99  ARG C CB  1 
ATOM   5566 C  CG  . ARG D 1 104 ? 60.050 20.248  -10.282 1.00 38.47  ?  99  ARG C CG  1 
ATOM   5567 C  CD  . ARG D 1 104 ? 60.037 21.014  -8.973  1.00 41.80  ?  99  ARG C CD  1 
ATOM   5568 N  NE  . ARG D 1 104 ? 60.495 20.174  -7.870  1.00 46.76  ?  99  ARG C NE  1 
ATOM   5569 C  CZ  . ARG D 1 104 ? 61.673 20.257  -7.253  1.00 45.06  ?  99  ARG C CZ  1 
ATOM   5570 N  NH1 . ARG D 1 104 ? 62.577 21.158  -7.606  1.00 49.69  ?  99  ARG C NH1 1 
ATOM   5571 N  NH2 . ARG D 1 104 ? 61.941 19.422  -6.262  1.00 47.73  ?  99  ARG C NH2 1 
ATOM   5572 N  N   . THR D 1 105 ? 62.814 19.411  -14.356 1.00 30.20  ?  100 THR C N   1 
ATOM   5573 C  CA  . THR D 1 105 ? 64.058 19.297  -15.158 1.00 29.58  ?  100 THR C CA  1 
ATOM   5574 C  C   . THR D 1 105 ? 63.692 19.660  -16.595 1.00 29.57  ?  100 THR C C   1 
ATOM   5575 O  O   . THR D 1 105 ? 62.540 19.435  -16.975 1.00 23.20  ?  100 THR C O   1 
ATOM   5576 C  CB  . THR D 1 105 ? 64.598 17.866  -15.044 1.00 30.91  ?  100 THR C CB  1 
ATOM   5577 O  OG1 . THR D 1 105 ? 66.013 17.827  -15.251 1.00 42.40  ?  100 THR C OG1 1 
ATOM   5578 C  CG2 . THR D 1 105 ? 63.919 16.935  -16.017 1.00 28.71  ?  100 THR C CG2 1 
ATOM   5579 N  N   . ALA D 1 106 ? 64.638 20.149  -17.385 1.00 27.26  ?  101 ALA C N   1 
ATOM   5580 C  CA  . ALA D 1 106 ? 64.416 20.432  -18.816 1.00 27.31  ?  101 ALA C CA  1 
ATOM   5581 C  C   . ALA D 1 106 ? 65.716 20.228  -19.566 1.00 25.90  ?  101 ALA C C   1 
ATOM   5582 O  O   . ALA D 1 106 ? 66.800 20.434  -19.002 1.00 27.46  ?  101 ALA C O   1 
ATOM   5583 C  CB  . ALA D 1 106 ? 63.902 21.825  -19.011 1.00 28.31  ?  101 ALA C CB  1 
ATOM   5584 N  N   . PRO D 1 107 ? 65.662 19.705  -20.802 1.00 23.60  ?  102 PRO C N   1 
ATOM   5585 C  CA  . PRO D 1 107 ? 64.434 19.198  -21.414 1.00 21.01  ?  102 PRO C CA  1 
ATOM   5586 C  C   . PRO D 1 107 ? 64.130 17.760  -20.956 1.00 21.62  ?  102 PRO C C   1 
ATOM   5587 O  O   . PRO D 1 107 ? 64.911 17.131  -20.237 1.00 17.96  ?  102 PRO C O   1 
ATOM   5588 C  CB  . PRO D 1 107 ? 64.807 19.121  -22.897 1.00 23.75  ?  102 PRO C CB  1 
ATOM   5589 C  CG  . PRO D 1 107 ? 66.276 18.716  -22.846 1.00 22.97  ?  102 PRO C CG  1 
ATOM   5590 C  CD  . PRO D 1 107 ? 66.842 19.406  -21.627 1.00 22.12  ?  102 PRO C CD  1 
ATOM   5591 N  N   . ALA D 1 108 ? 62.985 17.246  -21.351 1.00 20.63  ?  103 ALA C N   1 
ATOM   5592 C  CA  . ALA D 1 108 ? 62.500 15.928  -20.873 1.00 18.65  ?  103 ALA C CA  1 
ATOM   5593 C  C   . ALA D 1 108 ? 61.413 15.410  -21.817 1.00 17.30  ?  103 ALA C C   1 
ATOM   5594 O  O   . ALA D 1 108 ? 61.024 16.105  -22.766 1.00 14.57  ?  103 ALA C O   1 
ATOM   5595 C  CB  . ALA D 1 108 ? 62.018 16.096  -19.464 1.00 20.69  ?  103 ALA C CB  1 
ATOM   5596 N  N   . ALA D 1 109 ? 61.004 14.163  -21.639 1.00 17.01  ?  104 ALA C N   1 
ATOM   5597 C  CA  . ALA D 1 109 ? 59.840 13.597  -22.339 1.00 17.95  ?  104 ALA C CA  1 
ATOM   5598 C  C   . ALA D 1 109 ? 59.045 12.789  -21.323 1.00 16.51  ?  104 ALA C C   1 
ATOM   5599 O  O   . ALA D 1 109 ? 59.622 12.251  -20.388 1.00 15.43  ?  104 ALA C O   1 
ATOM   5600 C  CB  . ALA D 1 109 ? 60.261 12.769  -23.528 1.00 19.04  ?  104 ALA C CB  1 
ATOM   5601 N  N   . PRO D 1 110 ? 57.705 12.745  -21.452 1.00 15.85  ?  105 PRO C N   1 
ATOM   5602 C  CA  . PRO D 1 110 ? 56.887 11.927  -20.565 1.00 15.80  ?  105 PRO C CA  1 
ATOM   5603 C  C   . PRO D 1 110 ? 57.167 10.444  -20.817 1.00 16.65  ?  105 PRO C C   1 
ATOM   5604 O  O   . PRO D 1 110 ? 57.758 10.048  -21.869 1.00 15.96  ?  105 PRO C O   1 
ATOM   5605 C  CB  . PRO D 1 110 ? 55.443 12.224  -20.949 1.00 16.55  ?  105 PRO C CB  1 
ATOM   5606 C  CG  . PRO D 1 110 ? 55.544 13.449  -21.806 1.00 17.22  ?  105 PRO C CG  1 
ATOM   5607 C  CD  . PRO D 1 110 ? 56.898 13.381  -22.497 1.00 16.70  ?  105 PRO C CD  1 
ATOM   5608 N  N   . THR D 1 111 ? 56.715 9.633   -19.882 1.00 15.15  ?  106 THR C N   1 
ATOM   5609 C  CA  . THR D 1 111 ? 56.787 8.162   -20.044 1.00 14.70  ?  106 THR C CA  1 
ATOM   5610 C  C   . THR D 1 111 ? 55.640 7.506   -19.278 1.00 15.59  ?  106 THR C C   1 
ATOM   5611 O  O   . THR D 1 111 ? 54.785 8.222   -18.719 1.00 17.59  ?  106 THR C O   1 
ATOM   5612 C  CB  . THR D 1 111 ? 58.184 7.616   -19.700 1.00 13.80  ?  106 THR C CB  1 
ATOM   5613 O  OG1 . THR D 1 111 ? 58.248 6.287   -20.214 1.00 14.45  ?  106 THR C OG1 1 
ATOM   5614 C  CG2 . THR D 1 111 ? 58.518 7.563   -18.226 1.00 13.50  ?  106 THR C CG2 1 
ATOM   5615 N  N   . TRP D 1 112 ? 55.590 6.173   -19.319 1.00 14.24  ?  107 TRP C N   1 
ATOM   5616 C  CA  . TRP D 1 112 ? 54.602 5.428   -18.508 1.00 14.68  ?  107 TRP C CA  1 
ATOM   5617 C  C   . TRP D 1 112 ? 55.378 4.435   -17.697 1.00 16.53  ?  107 TRP C C   1 
ATOM   5618 O  O   . TRP D 1 112 ? 56.108 3.624   -18.296 1.00 19.07  ?  107 TRP C O   1 
ATOM   5619 C  CB  . TRP D 1 112 ? 53.547 4.787   -19.386 1.00 14.41  ?  107 TRP C CB  1 
ATOM   5620 C  CG  . TRP D 1 112 ? 52.221 4.592   -18.703 1.00 13.99  ?  107 TRP C CG  1 
ATOM   5621 C  CD1 . TRP D 1 112 ? 51.968 3.749   -17.658 1.00 13.54  ?  107 TRP C CD1 1 
ATOM   5622 C  CD2 . TRP D 1 112 ? 51.005 5.306   -18.966 1.00 14.34  ?  107 TRP C CD2 1 
ATOM   5623 N  NE1 . TRP D 1 112 ? 50.635 3.806   -17.338 1.00 15.20  ?  107 TRP C NE1 1 
ATOM   5624 C  CE2 . TRP D 1 112 ? 50.025 4.769   -18.097 1.00 15.46  ?  107 TRP C CE2 1 
ATOM   5625 C  CE3 . TRP D 1 112 ? 50.617 6.313   -19.862 1.00 15.11  ?  107 TRP C CE3 1 
ATOM   5626 C  CZ2 . TRP D 1 112 ? 48.716 5.237   -18.063 1.00 16.13  ?  107 TRP C CZ2 1 
ATOM   5627 C  CZ3 . TRP D 1 112 ? 49.303 6.747   -19.854 1.00 15.91  ?  107 TRP C CZ3 1 
ATOM   5628 C  CH2 . TRP D 1 112 ? 48.375 6.237   -18.945 1.00 16.67  ?  107 TRP C CH2 1 
ATOM   5629 N  N   . ASN D 1 113 ? 55.301 4.568   -16.379 1.00 14.95  ?  108 ASN C N   1 
ATOM   5630 C  CA  . ASN D 1 113 ? 55.924 3.588   -15.486 1.00 13.97  ?  108 ASN C CA  1 
ATOM   5631 C  C   . ASN D 1 113 ? 54.994 2.379   -15.469 1.00 13.98  ?  108 ASN C C   1 
ATOM   5632 O  O   . ASN D 1 113 ? 53.785 2.536   -15.250 1.00 13.75  ?  108 ASN C O   1 
ATOM   5633 C  CB  . ASN D 1 113 ? 56.235 4.168   -14.108 1.00 15.13  ?  108 ASN C CB  1 
ATOM   5634 C  CG  . ASN D 1 113 ? 57.544 4.927   -14.091 1.00 16.09  ?  108 ASN C CG  1 
ATOM   5635 O  OD1 . ASN D 1 113 ? 58.152 5.112   -15.148 1.00 16.03  ?  108 ASN C OD1 1 
ATOM   5636 N  ND2 . ASN D 1 113 ? 57.946 5.432   -12.930 1.00 16.81  ?  108 ASN C ND2 1 
ATOM   5637 N  N   . PHE D 1 114 ? 55.529 1.192   -15.602 1.00 13.32  ?  109 PHE C N   1 
ATOM   5638 C  CA  . PHE D 1 114 ? 54.651 0.015   -15.608 1.00 14.85  ?  109 PHE C CA  1 
ATOM   5639 C  C   . PHE D 1 114 ? 55.434 -1.219  -15.280 1.00 16.05  ?  109 PHE C C   1 
ATOM   5640 O  O   . PHE D 1 114 ? 56.631 -1.184  -15.341 1.00 14.75  ?  109 PHE C O   1 
ATOM   5641 C  CB  . PHE D 1 114 ? 53.926 -0.093  -16.955 1.00 14.85  ?  109 PHE C CB  1 
ATOM   5642 C  CG  . PHE D 1 114 ? 54.744 -0.687  -18.053 1.00 15.59  ?  109 PHE C CG  1 
ATOM   5643 C  CD1 . PHE D 1 114 ? 55.528 0.119   -18.862 1.00 14.96  ?  109 PHE C CD1 1 
ATOM   5644 C  CD2 . PHE D 1 114 ? 54.709 -2.055  -18.295 1.00 16.32  ?  109 PHE C CD2 1 
ATOM   5645 C  CE1 . PHE D 1 114 ? 56.161 -0.428  -19.953 1.00 15.50  ?  109 PHE C CE1 1 
ATOM   5646 C  CE2 . PHE D 1 114 ? 55.426 -2.608  -19.342 1.00 14.12  ?  109 PHE C CE2 1 
ATOM   5647 C  CZ  . PHE D 1 114 ? 56.170 -1.779  -20.140 1.00 16.23  ?  109 PHE C CZ  1 
ATOM   5648 N  N   . THR D 1 115 ? 54.679 -2.248  -14.908 1.00 15.60  ?  110 THR C N   1 
ATOM   5649 C  CA  . THR D 1 115 ? 55.198 -3.566  -14.512 1.00 16.16  ?  110 THR C CA  1 
ATOM   5650 C  C   . THR D 1 115 ? 54.534 -4.629  -15.357 1.00 15.67  ?  110 THR C C   1 
ATOM   5651 O  O   . THR D 1 115 ? 53.269 -4.601  -15.507 1.00 14.08  ?  110 THR C O   1 
ATOM   5652 C  CB  . THR D 1 115 ? 55.028 -3.804  -13.012 1.00 17.62  ?  110 THR C CB  1 
ATOM   5653 O  OG1 . THR D 1 115 ? 53.660 -3.595  -12.670 1.00 19.61  ?  110 THR C OG1 1 
ATOM   5654 C  CG2 . THR D 1 115 ? 56.007 -2.939  -12.253 1.00 16.93  ?  110 THR C CG2 1 
ATOM   5655 N  N   . SER D 1 116 ? 55.330 -5.532  -15.912 1.00 16.50  ?  111 SER C N   1 
ATOM   5656 C  CA  . SER D 1 116 ? 54.765 -6.699  -16.622 1.00 17.05  ?  111 SER C CA  1 
ATOM   5657 C  C   . SER D 1 116 ? 55.674 -7.918  -16.499 1.00 16.97  ?  111 SER C C   1 
ATOM   5658 O  O   . SER D 1 116 ? 56.926 -7.811  -16.512 1.00 18.02  ?  111 SER C O   1 
ATOM   5659 C  CB  . SER D 1 116 ? 54.478 -6.394  -18.065 1.00 20.37  ?  111 SER C CB  1 
ATOM   5660 O  OG  . SER D 1 116 ? 55.692 -6.342  -18.765 1.00 25.73  ?  111 SER C OG  1 
ATOM   5661 N  N   . VAL D 1 117 ? 55.025 -9.057  -16.499 1.00 14.91  ?  112 VAL C N   1 
ATOM   5662 C  CA  . VAL D 1 117 ? 55.692 -10.380 -16.537 1.00 15.69  ?  112 VAL C CA  1 
ATOM   5663 C  C   . VAL D 1 117 ? 55.143 -11.087 -17.767 1.00 14.74  ?  112 VAL C C   1 
ATOM   5664 O  O   . VAL D 1 117 ? 53.881 -11.163 -17.928 1.00 14.50  ?  112 VAL C O   1 
ATOM   5665 C  CB  . VAL D 1 117 ? 55.541 -11.153 -15.211 1.00 14.88  ?  112 VAL C CB  1 
ATOM   5666 C  CG1 . VAL D 1 117 ? 56.047 -12.579 -15.289 1.00 16.31  ?  112 VAL C CG1 1 
ATOM   5667 C  CG2 . VAL D 1 117 ? 56.300 -10.442 -14.116 1.00 17.23  ?  112 VAL C CG2 1 
ATOM   5668 N  N   . GLN D 1 118 ? 56.071 -11.589 -18.576 1.00 13.01  ?  113 GLN C N   1 
ATOM   5669 C  CA  . GLN D 1 118 ? 55.788 -12.424 -19.732 1.00 13.18  ?  113 GLN C CA  1 
ATOM   5670 C  C   . GLN D 1 118 ? 56.378 -13.816 -19.521 1.00 14.96  ?  113 GLN C C   1 
ATOM   5671 O  O   . GLN D 1 118 ? 57.639 -13.962 -19.409 1.00 17.37  ?  113 GLN C O   1 
ATOM   5672 C  CB  . GLN D 1 118 ? 56.258 -11.828 -21.034 1.00 13.92  ?  113 GLN C CB  1 
ATOM   5673 C  CG  . GLN D 1 118 ? 55.457 -10.615 -21.450 1.00 14.17  ?  113 GLN C CG  1 
ATOM   5674 C  CD  . GLN D 1 118 ? 55.974 -10.020 -22.726 1.00 12.99  ?  113 GLN C CD  1 
ATOM   5675 O  OE1 . GLN D 1 118 ? 56.475 -10.747 -23.576 1.00 15.21  ?  113 GLN C OE1 1 
ATOM   5676 N  NE2 . GLN D 1 118 ? 55.744 -8.729  -22.895 1.00 11.61  ?  113 GLN C NE2 1 
ATOM   5677 N  N   . VAL D 1 119 ? 55.513 -14.802 -19.446 1.00 15.13  ?  114 VAL C N   1 
ATOM   5678 C  CA  . VAL D 1 119 ? 55.940 -16.231 -19.314 1.00 17.67  ?  114 VAL C CA  1 
ATOM   5679 C  C   . VAL D 1 119 ? 55.660 -16.945 -20.635 1.00 16.97  ?  114 VAL C C   1 
ATOM   5680 O  O   . VAL D 1 119 ? 54.594 -16.784 -21.224 1.00 16.22  ?  114 VAL C O   1 
ATOM   5681 C  CB  . VAL D 1 119 ? 55.290 -16.966 -18.135 1.00 19.54  ?  114 VAL C CB  1 
ATOM   5682 C  CG1 . VAL D 1 119 ? 55.798 -16.448 -16.802 1.00 20.12  ?  114 VAL C CG1 1 
ATOM   5683 C  CG2 . VAL D 1 119 ? 53.782 -16.968 -18.221 1.00 20.84  ?  114 VAL C CG2 1 
ATOM   5684 N  N   . ARG D 1 120 ? 56.613 -17.724 -21.107 1.00 18.82  ?  115 ARG C N   1 
ATOM   5685 C  CA  . ARG D 1 120 ? 56.406 -18.499 -22.348 1.00 17.35  ?  115 ARG C CA  1 
ATOM   5686 C  C   . ARG D 1 120 ? 56.628 -19.984 -22.057 1.00 18.12  ?  115 ARG C C   1 
ATOM   5687 O  O   . ARG D 1 120 ? 57.531 -20.327 -21.239 1.00 17.90  ?  115 ARG C O   1 
ATOM   5688 C  CB  . ARG D 1 120 ? 57.319 -17.986 -23.461 1.00 18.01  ?  115 ARG C CB  1 
ATOM   5689 C  CG  . ARG D 1 120 ? 56.899 -16.621 -23.976 1.00 17.42  ?  115 ARG C CG  1 
ATOM   5690 C  CD  . ARG D 1 120 ? 57.972 -15.983 -24.848 1.00 20.13  ?  115 ARG C CD  1 
ATOM   5691 N  NE  . ARG D 1 120 ? 57.348 -14.918 -25.598 1.00 20.61  ?  115 ARG C NE  1 
ATOM   5692 C  CZ  . ARG D 1 120 ? 57.137 -13.680 -25.150 1.00 19.58  ?  115 ARG C CZ  1 
ATOM   5693 N  NH1 . ARG D 1 120 ? 57.604 -13.280 -23.971 1.00 17.77  ?  115 ARG C NH1 1 
ATOM   5694 N  NH2 . ARG D 1 120 ? 56.529 -12.826 -25.939 1.00 20.27  ?  115 ARG C NH2 1 
ATOM   5695 N  N   . GLY D 1 121 ? 55.867 -20.805 -22.761 1.00 16.76  ?  116 GLY C N   1 
ATOM   5696 C  CA  . GLY D 1 121 ? 56.038 -22.259 -22.778 1.00 17.06  ?  116 GLY C CA  1 
ATOM   5697 C  C   . GLY D 1 121 ? 54.931 -22.947 -23.532 1.00 19.03  ?  116 GLY C C   1 
ATOM   5698 O  O   . GLY D 1 121 ? 54.165 -22.269 -24.275 1.00 17.36  ?  116 GLY C O   1 
ATOM   5699 N  N   . GLU D 1 122 ? 54.919 -24.282 -23.421 1.00 20.80  ?  117 GLU C N   1 
ATOM   5700 C  CA  . GLU D 1 122 ? 53.931 -25.168 -24.070 1.00 22.00  ?  117 GLU C CA  1 
ATOM   5701 C  C   . GLU D 1 122 ? 52.658 -25.221 -23.218 1.00 21.38  ?  117 GLU C C   1 
ATOM   5702 O  O   . GLU D 1 122 ? 52.745 -25.534 -22.011 1.00 22.68  ?  117 GLU C O   1 
ATOM   5703 C  CB  . GLU D 1 122 ? 54.462 -26.603 -24.165 1.00 26.90  ?  117 GLU C CB  1 
ATOM   5704 C  CG  . GLU D 1 122 ? 55.406 -26.871 -25.323 1.00 34.12  ?  117 GLU C CG  1 
ATOM   5705 C  CD  . GLU D 1 122 ? 55.362 -28.319 -25.819 1.00 41.51  ?  117 GLU C CD  1 
ATOM   5706 O  OE1 . GLU D 1 122 ? 55.762 -28.561 -26.984 1.00 42.95  ?  117 GLU C OE1 1 
ATOM   5707 O  OE2 . GLU D 1 122 ? 54.867 -29.203 -25.052 1.00 45.83  -1 117 GLU C OE2 1 
ATOM   5708 N  N   . LEU D 1 123 ? 51.507 -24.952 -23.809 1.00 18.69  ?  118 LEU C N   1 
ATOM   5709 C  CA  . LEU D 1 123 ? 50.215 -25.104 -23.095 1.00 20.37  ?  118 LEU C CA  1 
ATOM   5710 C  C   . LEU D 1 123 ? 49.695 -26.519 -23.361 1.00 20.54  ?  118 LEU C C   1 
ATOM   5711 O  O   . LEU D 1 123 ? 49.550 -26.880 -24.560 1.00 21.38  ?  118 LEU C O   1 
ATOM   5712 C  CB  . LEU D 1 123 ? 49.202 -24.083 -23.596 1.00 21.70  ?  118 LEU C CB  1 
ATOM   5713 C  CG  . LEU D 1 123 ? 47.875 -24.106 -22.831 1.00 21.56  ?  118 LEU C CG  1 
ATOM   5714 C  CD1 . LEU D 1 123 ? 47.322 -22.713 -22.665 1.00 22.17  ?  118 LEU C CD1 1 
ATOM   5715 C  CD2 . LEU D 1 123 ? 46.854 -25.028 -23.486 1.00 23.45  ?  118 LEU C CD2 1 
ATOM   5716 N  N   . ARG D 1 124 ? 49.402 -27.263 -22.300 1.00 21.71  ?  119 ARG C N   1 
ATOM   5717 C  CA  . ARG D 1 124 ? 48.791 -28.614 -22.378 1.00 20.17  ?  119 ARG C CA  1 
ATOM   5718 C  C   . ARG D 1 124 ? 47.357 -28.512 -21.881 1.00 22.17  ?  119 ARG C C   1 
ATOM   5719 O  O   . ARG D 1 124 ? 47.145 -27.922 -20.796 1.00 20.01  ?  119 ARG C O   1 
ATOM   5720 C  CB  . ARG D 1 124 ? 49.525 -29.653 -21.541 1.00 24.24  ?  119 ARG C CB  1 
ATOM   5721 C  CG  . ARG D 1 124 ? 48.928 -31.051 -21.732 1.00 28.10  ?  119 ARG C CG  1 
ATOM   5722 C  CD  . ARG D 1 124 ? 49.512 -32.184 -20.915 1.00 31.64  ?  119 ARG C CD  1 
ATOM   5723 N  NE  . ARG D 1 124 ? 49.451 -32.027 -19.463 1.00 35.56  ?  119 ARG C NE  1 
ATOM   5724 C  CZ  . ARG D 1 124 ? 48.357 -32.152 -18.704 1.00 35.02  ?  119 ARG C CZ  1 
ATOM   5725 N  NH1 . ARG D 1 124 ? 47.151 -32.348 -19.231 1.00 35.16  ?  119 ARG C NH1 1 
ATOM   5726 N  NH2 . ARG D 1 124 ? 48.492 -32.042 -17.398 1.00 33.87  ?  119 ARG C NH2 1 
ATOM   5727 N  N   . LYS D 1 125 ? 46.408 -28.982 -22.684 1.00 18.05  ?  120 LYS C N   1 
ATOM   5728 C  CA  . LYS D 1 125 ? 45.008 -28.989 -22.214 1.00 21.41  ?  120 LYS C CA  1 
ATOM   5729 C  C   . LYS D 1 125 ? 44.852 -30.097 -21.186 1.00 22.81  ?  120 LYS C C   1 
ATOM   5730 O  O   . LYS D 1 125 ? 45.352 -31.218 -21.408 1.00 20.37  ?  120 LYS C O   1 
ATOM   5731 C  CB  . LYS D 1 125 ? 44.035 -29.199 -23.358 1.00 22.05  ?  120 LYS C CB  1 
ATOM   5732 C  CG  . LYS D 1 125 ? 44.038 -28.062 -24.367 1.00 22.79  ?  120 LYS C CG  1 
ATOM   5733 C  CD  . LYS D 1 125 ? 43.262 -28.404 -25.579 1.00 24.38  ?  120 LYS C CD  1 
ATOM   5734 C  CE  . LYS D 1 125 ? 42.987 -27.181 -26.416 1.00 24.02  ?  120 LYS C CE  1 
ATOM   5735 N  NZ  . LYS D 1 125 ? 42.465 -27.488 -27.765 1.00 26.72  ?  120 LYS C NZ  1 
ATOM   5736 N  N   . VAL D 1 126 ? 44.126 -29.778 -20.122 1.00 20.88  ?  121 VAL C N   1 
ATOM   5737 C  CA  . VAL D 1 126 ? 43.616 -30.717 -19.109 1.00 20.16  ?  121 VAL C CA  1 
ATOM   5738 C  C   . VAL D 1 126 ? 42.329 -31.299 -19.667 1.00 20.43  ?  121 VAL C C   1 
ATOM   5739 O  O   . VAL D 1 126 ? 41.502 -30.522 -20.152 1.00 18.46  ?  121 VAL C O   1 
ATOM   5740 C  CB  . VAL D 1 126 ? 43.406 -29.990 -17.775 1.00 22.19  ?  121 VAL C CB  1 
ATOM   5741 C  CG1 . VAL D 1 126 ? 42.766 -30.896 -16.741 1.00 22.63  ?  121 VAL C CG1 1 
ATOM   5742 C  CG2 . VAL D 1 126 ? 44.729 -29.468 -17.212 1.00 21.74  ?  121 VAL C CG2 1 
ATOM   5743 N  N   . GLU D 1 127 ? 42.210 -32.631 -19.660 1.00 22.05  ?  122 GLU C N   1 
ATOM   5744 C  CA  . GLU D 1 127 ? 40.948 -33.307 -20.055 1.00 23.81  ?  122 GLU C CA  1 
ATOM   5745 C  C   . GLU D 1 127 ? 40.273 -33.991 -18.861 1.00 23.28  ?  122 GLU C C   1 
ATOM   5746 O  O   . GLU D 1 127 ? 39.040 -34.132 -18.925 1.00 23.47  ?  122 GLU C O   1 
ATOM   5747 C  CB  . GLU D 1 127 ? 41.198 -34.344 -21.154 1.00 23.50  ?  122 GLU C CB  1 
ATOM   5748 C  CG  . GLU D 1 127 ? 41.747 -33.730 -22.413 1.00 25.13  ?  122 GLU C CG  1 
ATOM   5749 C  CD  . GLU D 1 127 ? 40.848 -32.773 -23.174 1.00 24.08  ?  122 GLU C CD  1 
ATOM   5750 O  OE1 . GLU D 1 127 ? 39.656 -32.528 -22.764 1.00 21.68  ?  122 GLU C OE1 1 
ATOM   5751 O  OE2 . GLU D 1 127 ? 41.318 -32.304 -24.198 1.00 20.84  -1 122 GLU C OE2 1 
ATOM   5752 N  N   . SER D 1 128 ? 41.048 -34.472 -17.894 1.00 20.94  ?  123 SER C N   1 
ATOM   5753 C  CA  . SER D 1 128 ? 40.565 -35.176 -16.688 1.00 24.25  ?  123 SER C CA  1 
ATOM   5754 C  C   . SER D 1 128 ? 39.618 -34.281 -15.890 1.00 25.41  ?  123 SER C C   1 
ATOM   5755 O  O   . SER D 1 128 ? 39.870 -33.061 -15.851 1.00 20.60  ?  123 SER C O   1 
ATOM   5756 C  CB  . SER D 1 128 ? 41.690 -35.674 -15.856 1.00 26.17  ?  123 SER C CB  1 
ATOM   5757 O  OG  . SER D 1 128 ? 41.330 -35.674 -14.493 1.00 31.51  ?  123 SER C OG  1 
ATOM   5758 N  N   . ALA D 1 129 ? 38.535 -34.866 -15.348 1.00 26.47  ?  124 ALA C N   1 
ATOM   5759 C  CA  . ALA D 1 129 ? 37.516 -34.153 -14.541 1.00 27.97  ?  124 ALA C CA  1 
ATOM   5760 C  C   . ALA D 1 129 ? 38.131 -33.811 -13.192 1.00 29.25  ?  124 ALA C C   1 
ATOM   5761 O  O   . ALA D 1 129 ? 37.910 -32.696 -12.686 1.00 27.91  ?  124 ALA C O   1 
ATOM   5762 C  CB  . ALA D 1 129 ? 36.256 -34.984 -14.368 1.00 30.54  ?  124 ALA C CB  1 
ATOM   5763 N  N   . ASP D 1 130 ? 38.912 -34.735 -12.648 1.00 29.44  ?  125 ASP C N   1 
ATOM   5764 C  CA  . ASP D 1 130 ? 39.565 -34.563 -11.330 1.00 31.91  ?  125 ASP C CA  1 
ATOM   5765 C  C   . ASP D 1 130 ? 40.497 -33.350 -11.443 1.00 28.18  ?  125 ASP C C   1 
ATOM   5766 O  O   . ASP D 1 130 ? 40.404 -32.440 -10.580 1.00 24.47  ?  125 ASP C O   1 
ATOM   5767 C  CB  . ASP D 1 130 ? 40.180 -35.896 -10.892 1.00 37.49  ?  125 ASP C CB  1 
ATOM   5768 C  CG  . ASP D 1 130 ? 39.177 -37.045 -11.035 1.00 45.02  ?  125 ASP C CG  1 
ATOM   5769 O  OD1 . ASP D 1 130 ? 38.077 -36.935 -10.429 1.00 47.56  ?  125 ASP C OD1 1 
ATOM   5770 O  OD2 . ASP D 1 130 ? 39.453 -38.004 -11.808 1.00 45.64  -1 125 ASP C OD2 1 
ATOM   5771 N  N   . ASP D 1 131 ? 41.320 -33.304 -12.492 1.00 23.90  ?  126 ASP C N   1 
ATOM   5772 C  CA  . ASP D 1 131 ? 42.355 -32.246 -12.653 1.00 24.39  ?  126 ASP C CA  1 
ATOM   5773 C  C   . ASP D 1 131 ? 41.692 -30.904 -12.995 1.00 20.62  ?  126 ASP C C   1 
ATOM   5774 O  O   . ASP D 1 131 ? 42.210 -29.835 -12.547 1.00 20.04  ?  126 ASP C O   1 
ATOM   5775 C  CB  . ASP D 1 131 ? 43.429 -32.704 -13.634 1.00 27.82  ?  126 ASP C CB  1 
ATOM   5776 C  CG  . ASP D 1 131 ? 44.315 -33.805 -13.065 1.00 30.76  ?  126 ASP C CG  1 
ATOM   5777 O  OD1 . ASP D 1 131 ? 44.776 -33.652 -11.925 1.00 33.34  ?  126 ASP C OD1 1 
ATOM   5778 O  OD2 . ASP D 1 131 ? 44.504 -34.816 -13.748 1.00 39.46  -1 126 ASP C OD2 1 
ATOM   5779 N  N   . THR D 1 132 ? 40.557 -30.938 -13.680 1.00 19.60  ?  127 THR C N   1 
ATOM   5780 C  CA  . THR D 1 132 ? 39.779 -29.732 -14.033 1.00 20.74  ?  127 THR C CA  1 
ATOM   5781 C  C   . THR D 1 132 ? 39.221 -29.136 -12.732 1.00 21.72  ?  127 THR C C   1 
ATOM   5782 O  O   . THR D 1 132 ? 39.364 -27.905 -12.515 1.00 18.10  ?  127 THR C O   1 
ATOM   5783 C  CB  . THR D 1 132 ? 38.721 -30.027 -15.103 1.00 21.23  ?  127 THR C CB  1 
ATOM   5784 O  OG1 . THR D 1 132 ? 39.332 -30.450 -16.328 1.00 21.46  ?  127 THR C OG1 1 
ATOM   5785 C  CG2 . THR D 1 132 ? 37.907 -28.793 -15.418 1.00 22.38  ?  127 THR C CG2 1 
ATOM   5786 N  N   . LEU D 1 133 ? 38.572 -29.961 -11.905 1.00 21.74  ?  128 LEU C N   1 
ATOM   5787 C  CA  . LEU D 1 133 ? 37.974 -29.490 -10.634 1.00 22.04  ?  128 LEU C CA  1 
ATOM   5788 C  C   . LEU D 1 133 ? 39.098 -28.972 -9.736  1.00 19.81  ?  128 LEU C C   1 
ATOM   5789 O  O   . LEU D 1 133 ? 38.905 -27.930 -9.139  1.00 19.18  ?  128 LEU C O   1 
ATOM   5790 C  CB  . LEU D 1 133 ? 37.189 -30.623 -9.970  1.00 24.48  ?  128 LEU C CB  1 
ATOM   5791 C  CG  . LEU D 1 133 ? 36.596 -30.277 -8.605  1.00 26.07  ?  128 LEU C CG  1 
ATOM   5792 C  CD1 . LEU D 1 133 ? 35.563 -29.171 -8.736  1.00 26.26  ?  128 LEU C CD1 1 
ATOM   5793 C  CD2 . LEU D 1 133 ? 35.981 -31.506 -7.948  1.00 28.32  ?  128 LEU C CD2 1 
ATOM   5794 N  N   . ALA D 1 134 ? 40.218 -29.691 -9.638  1.00 18.78  ?  129 ALA C N   1 
ATOM   5795 C  CA  . ALA D 1 134 ? 41.395 -29.262 -8.844  1.00 18.88  ?  129 ALA C CA  1 
ATOM   5796 C  C   . ALA D 1 134 ? 41.817 -27.861 -9.308  1.00 17.66  ?  129 ALA C C   1 
ATOM   5797 O  O   . ALA D 1 134 ? 42.177 -27.039 -8.436  1.00 17.88  ?  129 ALA C O   1 
ATOM   5798 C  CB  . ALA D 1 134 ? 42.542 -30.238 -8.936  1.00 18.91  ?  129 ALA C CB  1 
ATOM   5799 N  N   . THR D 1 135 ? 41.753 -27.579 -10.607 1.00 17.57  ?  130 THR C N   1 
ATOM   5800 C  CA  . THR D 1 135 ? 42.249 -26.291 -11.158 1.00 17.78  ?  130 THR C CA  1 
ATOM   5801 C  C   . THR D 1 135 ? 41.379 -25.169 -10.579 1.00 18.18  ?  130 THR C C   1 
ATOM   5802 O  O   . THR D 1 135 ? 41.896 -24.161 -10.054 1.00 17.40  ?  130 THR C O   1 
ATOM   5803 C  CB  . THR D 1 135 ? 42.215 -26.295 -12.695 1.00 18.74  ?  130 THR C CB  1 
ATOM   5804 O  OG1 . THR D 1 135 ? 43.094 -27.296 -13.222 1.00 20.08  ?  130 THR C OG1 1 
ATOM   5805 C  CG2 . THR D 1 135 ? 42.635 -24.959 -13.265 1.00 17.77  ?  130 THR C CG2 1 
ATOM   5806 N  N   . VAL D 1 136 ? 40.072 -25.289 -10.746 1.00 18.73  ?  131 VAL C N   1 
ATOM   5807 C  CA  . VAL D 1 136 ? 39.167 -24.187 -10.342 1.00 18.37  ?  131 VAL C CA  1 
ATOM   5808 C  C   . VAL D 1 136 ? 39.170 -24.070 -8.811  1.00 18.53  ?  131 VAL C C   1 
ATOM   5809 O  O   . VAL D 1 136 ? 39.080 -22.937 -8.312  1.00 18.58  ?  131 VAL C O   1 
ATOM   5810 C  CB  . VAL D 1 136 ? 37.777 -24.353 -10.944 1.00 18.87  ?  131 VAL C CB  1 
ATOM   5811 C  CG1 . VAL D 1 136 ? 37.848 -24.244 -12.465 1.00 19.96  ?  131 VAL C CG1 1 
ATOM   5812 C  CG2 . VAL D 1 136 ? 37.093 -25.633 -10.509 1.00 19.21  ?  131 VAL C CG2 1 
ATOM   5813 N  N   . ARG D 1 137 ? 39.212 -25.180 -8.077  1.00 19.55  ?  132 ARG C N   1 
ATOM   5814 C  CA  . ARG D 1 137 ? 39.249 -25.127 -6.593  1.00 19.30  ?  132 ARG C CA  1 
ATOM   5815 C  C   . ARG D 1 137 ? 40.540 -24.440 -6.146  1.00 17.50  ?  132 ARG C C   1 
ATOM   5816 O  O   . ARG D 1 137 ? 40.508 -23.641 -5.209  1.00 18.64  ?  132 ARG C O   1 
ATOM   5817 C  CB  . ARG D 1 137 ? 39.112 -26.519 -5.959  1.00 21.78  ?  132 ARG C CB  1 
ATOM   5818 C  CG  . ARG D 1 137 ? 37.713 -27.100 -6.062  1.00 22.82  ?  132 ARG C CG  1 
ATOM   5819 C  CD  . ARG D 1 137 ? 37.614 -28.420 -5.312  1.00 26.49  ?  132 ARG C CD  1 
ATOM   5820 N  NE  . ARG D 1 137 ? 37.784 -28.158 -3.893  1.00 30.64  ?  132 ARG C NE  1 
ATOM   5821 C  CZ  . ARG D 1 137 ? 37.645 -29.055 -2.913  1.00 37.91  ?  132 ARG C CZ  1 
ATOM   5822 N  NH1 . ARG D 1 137 ? 37.313 -30.304 -3.183  1.00 38.92  ?  132 ARG C NH1 1 
ATOM   5823 N  NH2 . ARG D 1 137 ? 37.814 -28.683 -1.657  1.00 41.81  ?  132 ARG C NH2 1 
ATOM   5824 N  N   . ALA D 1 138 ? 41.669 -24.729 -6.769  1.00 17.13  ?  133 ALA C N   1 
ATOM   5825 C  CA  . ALA D 1 138 ? 42.942 -24.087 -6.382  1.00 16.18  ?  133 ALA C CA  1 
ATOM   5826 C  C   . ALA D 1 138 ? 42.866 -22.585 -6.701  1.00 15.93  ?  133 ALA C C   1 
ATOM   5827 O  O   . ALA D 1 138 ? 43.448 -21.755 -5.950  1.00 16.24  ?  133 ALA C O   1 
ATOM   5828 C  CB  . ALA D 1 138 ? 44.103 -24.755 -7.078  1.00 16.01  ?  133 ALA C CB  1 
ATOM   5829 N  N   . THR D 1 139 ? 42.215 -22.231 -7.803  1.00 15.10  ?  134 THR C N   1 
ATOM   5830 C  CA  . THR D 1 139 ? 42.079 -20.811 -8.220  1.00 16.54  ?  134 THR C CA  1 
ATOM   5831 C  C   . THR D 1 139 ? 41.205 -20.061 -7.202  1.00 17.26  ?  134 THR C C   1 
ATOM   5832 O  O   . THR D 1 139 ? 41.545 -18.906 -6.823  1.00 17.09  ?  134 THR C O   1 
ATOM   5833 C  CB  . THR D 1 139 ? 41.546 -20.694 -9.649  1.00 16.36  ?  134 THR C CB  1 
ATOM   5834 O  OG1 . THR D 1 139 ? 42.450 -21.477 -10.426 1.00 15.28  ?  134 THR C OG1 1 
ATOM   5835 C  CG2 . THR D 1 139 ? 41.460 -19.265 -10.129 1.00 15.16  ?  134 THR C CG2 1 
ATOM   5836 N  N   . VAL D 1 140 ? 40.078 -20.652 -6.791  1.00 17.27  ?  135 VAL C N   1 
ATOM   5837 C  CA  . VAL D 1 140 ? 39.281 -20.041 -5.696  1.00 17.58  ?  135 VAL C CA  1 
ATOM   5838 C  C   . VAL D 1 140 ? 40.185 -19.872 -4.457  1.00 17.47  ?  135 VAL C C   1 
ATOM   5839 O  O   . VAL D 1 140 ? 40.190 -18.778 -3.858  1.00 17.84  ?  135 VAL C O   1 
ATOM   5840 C  CB  . VAL D 1 140 ? 38.023 -20.857 -5.353  1.00 19.43  ?  135 VAL C CB  1 
ATOM   5841 C  CG1 . VAL D 1 140 ? 37.380 -20.327 -4.086  1.00 19.13  ?  135 VAL C CG1 1 
ATOM   5842 C  CG2 . VAL D 1 140 ? 37.048 -20.911 -6.503  1.00 19.50  ?  135 VAL C CG2 1 
ATOM   5843 N  N   . ALA D 1 141 ? 40.895 -20.909 -4.033  1.00 18.73  ?  136 ALA C N   1 
ATOM   5844 C  CA  . ALA D 1 141 ? 41.681 -20.871 -2.783  1.00 21.44  ?  136 ALA C CA  1 
ATOM   5845 C  C   . ALA D 1 141 ? 42.702 -19.723 -2.855  1.00 20.80  ?  136 ALA C C   1 
ATOM   5846 O  O   . ALA D 1 141 ? 42.836 -18.960 -1.878  1.00 20.85  ?  136 ALA C O   1 
ATOM   5847 C  CB  . ALA D 1 141 ? 42.340 -22.202 -2.516  1.00 22.16  ?  136 ALA C CB  1 
ATOM   5848 N  N   . ALA D 1 142 ? 43.400 -19.589 -3.981  1.00 19.23  ?  137 ALA C N   1 
ATOM   5849 C  CA  . ALA D 1 142 ? 44.480 -18.595 -4.164  1.00 19.87  ?  137 ALA C CA  1 
ATOM   5850 C  C   . ALA D 1 142 ? 43.880 -17.180 -4.248  1.00 17.43  ?  137 ALA C C   1 
ATOM   5851 O  O   . ALA D 1 142 ? 44.391 -16.268 -3.583  1.00 18.18  ?  137 ALA C O   1 
ATOM   5852 C  CB  . ALA D 1 142 ? 45.258 -18.942 -5.406  1.00 20.55  ?  137 ALA C CB  1 
ATOM   5853 N  N   . LEU D 1 143 ? 42.868 -16.975 -5.088  1.00 17.31  ?  138 LEU C N   1 
ATOM   5854 C  CA  . LEU D 1 143 ? 42.346 -15.616 -5.350  1.00 16.31  ?  138 LEU C CA  1 
ATOM   5855 C  C   . LEU D 1 143 ? 41.465 -15.137 -4.183  1.00 17.56  ?  138 LEU C C   1 
ATOM   5856 O  O   . LEU D 1 143 ? 41.545 -13.962 -3.855  1.00 14.73  ?  138 LEU C O   1 
ATOM   5857 C  CB  . LEU D 1 143 ? 41.554 -15.498 -6.653  1.00 17.11  ?  138 LEU C CB  1 
ATOM   5858 C  CG  . LEU D 1 143 ? 42.183 -15.978 -7.951  1.00 18.48  ?  138 LEU C CG  1 
ATOM   5859 C  CD1 . LEU D 1 143 ? 41.690 -15.205 -9.122  1.00 14.94  ?  138 LEU C CD1 1 
ATOM   5860 C  CD2 . LEU D 1 143 ? 43.681 -16.158 -7.920  1.00 16.92  ?  138 LEU C CD2 1 
ATOM   5861 N  N   . GLU D 1 144 ? 40.633 -15.989 -3.597  1.00 17.09  ?  139 GLU C N   1 
ATOM   5862 C  CA  . GLU D 1 144 ? 39.768 -15.568 -2.453  1.00 17.31  ?  139 GLU C CA  1 
ATOM   5863 C  C   . GLU D 1 144 ? 40.663 -15.173 -1.267  1.00 19.00  ?  139 GLU C C   1 
ATOM   5864 O  O   . GLU D 1 144 ? 40.388 -14.142 -0.597  1.00 17.45  ?  139 GLU C O   1 
ATOM   5865 C  CB  . GLU D 1 144 ? 38.794 -16.690 -2.111  1.00 18.88  ?  139 GLU C CB  1 
ATOM   5866 C  CG  . GLU D 1 144 ? 37.768 -16.299 -1.074  1.00 18.60  ?  139 GLU C CG  1 
ATOM   5867 C  CD  . GLU D 1 144 ? 36.804 -15.206 -1.477  1.00 19.21  ?  139 GLU C CD  1 
ATOM   5868 O  OE1 . GLU D 1 144 ? 36.542 -15.066 -2.703  1.00 18.13  ?  139 GLU C OE1 1 
ATOM   5869 O  OE2 . GLU D 1 144 ? 36.279 -14.491 -0.549  1.00 18.76  -1 139 GLU C OE2 1 
ATOM   5870 N  N   . SER D 1 145 ? 41.758 -15.898 -1.042  1.00 19.73  ?  140 SER C N   1 
ATOM   5871 C  CA  . SER D 1 145 ? 42.738 -15.546 0.018   1.00 22.04  ?  140 SER C CA  1 
ATOM   5872 C  C   . SER D 1 145 ? 43.315 -14.150 -0.222  1.00 20.31  ?  140 SER C C   1 
ATOM   5873 O  O   . SER D 1 145 ? 43.460 -13.364 0.708   1.00 21.60  ?  140 SER C O   1 
ATOM   5874 C  CB  . SER D 1 145 ? 43.854 -16.541 0.106   1.00 23.86  ?  140 SER C CB  1 
ATOM   5875 O  OG  . SER D 1 145 ? 44.789 -16.081 1.075   1.00 27.77  ?  140 SER C OG  1 
ATOM   5876 N  N   . ARG D 1 146 ? 43.703 -13.856 -1.445  1.00 20.16  ?  141 ARG C N   1 
ATOM   5877 C  CA  . ARG D 1 146 ? 44.455 -12.626 -1.742  1.00 21.44  ?  141 ARG C CA  1 
ATOM   5878 C  C   . ARG D 1 146 ? 43.511 -11.451 -2.005  1.00 19.32  ?  141 ARG C C   1 
ATOM   5879 O  O   . ARG D 1 146 ? 43.882 -10.337 -1.592  1.00 19.15  ?  141 ARG C O   1 
ATOM   5880 C  CB  . ARG D 1 146 ? 45.429 -12.955 -2.878  1.00 23.92  ?  141 ARG C CB  1 
ATOM   5881 C  CG  . ARG D 1 146 ? 46.628 -12.034 -2.957  1.00 29.62  ?  141 ARG C CG  1 
ATOM   5882 C  CD  . ARG D 1 146 ? 47.554 -12.559 -4.032  1.00 30.80  ?  141 ARG C CD  1 
ATOM   5883 N  NE  . ARG D 1 146 ? 48.315 -13.688 -3.512  1.00 37.30  ?  141 ARG C NE  1 
ATOM   5884 C  CZ  . ARG D 1 146 ? 49.479 -13.592 -2.889  1.00 37.89  ?  141 ARG C CZ  1 
ATOM   5885 N  NH1 . ARG D 1 146 ? 50.035 -12.408 -2.667  1.00 40.41  ?  141 ARG C NH1 1 
ATOM   5886 N  NH2 . ARG D 1 146 ? 50.067 -14.690 -2.464  1.00 42.40  ?  141 ARG C NH2 1 
ATOM   5887 N  N   . PHE D 1 147 ? 42.330 -11.634 -2.610  1.00 18.49  ?  142 PHE C N   1 
ATOM   5888 C  CA  . PHE D 1 147 ? 41.498 -10.511 -3.115  1.00 17.59  ?  142 PHE C CA  1 
ATOM   5889 C  C   . PHE D 1 147 ? 40.089 -10.514 -2.487  1.00 19.99  ?  142 PHE C C   1 
ATOM   5890 O  O   . PHE D 1 147 ? 39.300 -9.587  -2.728  1.00 20.14  ?  142 PHE C O   1 
ATOM   5891 C  CB  . PHE D 1 147 ? 41.391 -10.620 -4.630  1.00 17.72  ?  142 PHE C CB  1 
ATOM   5892 C  CG  . PHE D 1 147 ? 42.729 -10.684 -5.335  1.00 18.47  ?  142 PHE C CG  1 
ATOM   5893 C  CD1 . PHE D 1 147 ? 43.537 -9.566  -5.421  1.00 18.14  ?  142 PHE C CD1 1 
ATOM   5894 C  CD2 . PHE D 1 147 ? 43.186 -11.885 -5.853  1.00 17.53  ?  142 PHE C CD2 1 
ATOM   5895 C  CE1 . PHE D 1 147 ? 44.795 -9.653  -6.009  1.00 21.93  ?  142 PHE C CE1 1 
ATOM   5896 C  CE2 . PHE D 1 147 ? 44.451 -11.979 -6.445  1.00 18.17  ?  142 PHE C CE2 1 
ATOM   5897 C  CZ  . PHE D 1 147 ? 45.247 -10.857 -6.532  1.00 19.24  ?  142 PHE C CZ  1 
ATOM   5898 N  N   . GLY D 1 148 ? 39.780 -11.538 -1.698  1.00 20.79  ?  143 GLY C N   1 
ATOM   5899 C  CA  . GLY D 1 148 ? 38.393 -11.869 -1.356  1.00 18.81  ?  143 GLY C CA  1 
ATOM   5900 C  C   . GLY D 1 148 ? 38.033 -11.475 0.079   1.00 20.95  ?  143 GLY C C   1 
ATOM   5901 O  O   . GLY D 1 148 ? 38.570 -10.469 0.630   1.00 17.93  ?  143 GLY C O   1 
ATOM   5902 N  N   . ALA D 1 149 ? 37.095 -12.223 0.653   1.00 20.75  ?  144 ALA C N   1 
ATOM   5903 C  CA  . ALA D 1 149 ? 36.445 -11.870 1.926   1.00 21.15  ?  144 ALA C CA  1 
ATOM   5904 C  C   . ALA D 1 149 ? 36.065 -13.150 2.665   1.00 21.60  ?  144 ALA C C   1 
ATOM   5905 O  O   . ALA D 1 149 ? 34.974 -13.197 3.250   1.00 22.06  ?  144 ALA C O   1 
ATOM   5906 C  CB  . ALA D 1 149 ? 35.263 -10.971 1.647   1.00 22.89  ?  144 ALA C CB  1 
ATOM   5907 N  N   . GLY D 1 150 ? 36.964 -14.137 2.649   1.00 20.89  ?  145 GLY C N   1 
ATOM   5908 C  CA  . GLY D 1 150 ? 36.826 -15.375 3.424   1.00 20.58  ?  145 GLY C CA  1 
ATOM   5909 C  C   . GLY D 1 150 ? 35.639 -16.205 2.989   1.00 22.40  ?  145 GLY C C   1 
ATOM   5910 O  O   . GLY D 1 150 ? 35.167 -17.009 3.796   1.00 22.13  ?  145 GLY C O   1 
ATOM   5911 N  N   . TRP D 1 151 ? 35.237 -16.125 1.728   1.00 19.28  ?  146 TRP C N   1 
ATOM   5912 C  CA  . TRP D 1 151 ? 34.180 -17.018 1.207   1.00 20.22  ?  146 TRP C CA  1 
ATOM   5913 C  C   . TRP D 1 151 ? 34.654 -18.475 1.248   1.00 19.89  ?  146 TRP C C   1 
ATOM   5914 O  O   . TRP D 1 151 ? 35.810 -18.764 0.864   1.00 21.60  ?  146 TRP C O   1 
ATOM   5915 C  CB  . TRP D 1 151 ? 33.755 -16.606 -0.189  1.00 18.33  ?  146 TRP C CB  1 
ATOM   5916 C  CG  . TRP D 1 151 ? 32.653 -17.450 -0.730  1.00 18.83  ?  146 TRP C CG  1 
ATOM   5917 C  CD1 . TRP D 1 151 ? 31.333 -17.457 -0.356  1.00 18.73  ?  146 TRP C CD1 1 
ATOM   5918 C  CD2 . TRP D 1 151 ? 32.798 -18.429 -1.769  1.00 17.07  ?  146 TRP C CD2 1 
ATOM   5919 N  NE1 . TRP D 1 151 ? 30.644 -18.374 -1.105  1.00 17.22  ?  146 TRP C NE1 1 
ATOM   5920 C  CE2 . TRP D 1 151 ? 31.514 -18.981 -1.983  1.00 17.21  ?  146 TRP C CE2 1 
ATOM   5921 C  CE3 . TRP D 1 151 ? 33.880 -18.853 -2.548  1.00 17.93  ?  146 TRP C CE3 1 
ATOM   5922 C  CZ2 . TRP D 1 151 ? 31.293 -19.931 -2.976  1.00 17.68  ?  146 TRP C CZ2 1 
ATOM   5923 C  CZ3 . TRP D 1 151 ? 33.669 -19.839 -3.485  1.00 17.88  ?  146 TRP C CZ3 1 
ATOM   5924 C  CH2 . TRP D 1 151 ? 32.387 -20.353 -3.701  1.00 18.62  ?  146 TRP C CH2 1 
ATOM   5925 N  N   . ASP D 1 152 ? 33.787 -19.353 1.746   1.00 23.33  ?  147 ASP C N   1 
ATOM   5926 C  CA  . ASP D 1 152 ? 34.055 -20.804 1.890   1.00 23.86  ?  147 ASP C CA  1 
ATOM   5927 C  C   . ASP D 1 152 ? 33.375 -21.513 0.720   1.00 22.16  ?  147 ASP C C   1 
ATOM   5928 O  O   . ASP D 1 152 ? 32.150 -21.419 0.571   1.00 20.48  ?  147 ASP C O   1 
ATOM   5929 C  CB  . ASP D 1 152 ? 33.604 -21.290 3.268   1.00 27.16  ?  147 ASP C CB  1 
ATOM   5930 C  CG  . ASP D 1 152 ? 33.692 -22.790 3.497   1.00 31.20  ?  147 ASP C CG  1 
ATOM   5931 O  OD1 . ASP D 1 152 ? 34.221 -23.514 2.617   1.00 26.14  ?  147 ASP C OD1 1 
ATOM   5932 O  OD2 . ASP D 1 152 ? 33.196 -23.226 4.560   1.00 40.82  -1 147 ASP C OD2 1 
ATOM   5933 N  N   . MET D 1 153 ? 34.160 -22.155 -0.134  1.00 20.78  ?  148 MET C N   1 
ATOM   5934 C  CA  . MET D 1 153 ? 33.596 -22.784 -1.361  1.00 22.80  ?  148 MET C CA  1 
ATOM   5935 C  C   . MET D 1 153 ? 32.831 -24.086 -1.043  1.00 22.27  ?  148 MET C C   1 
ATOM   5936 O  O   . MET D 1 153 ? 32.180 -24.586 -1.966  1.00 20.95  ?  148 MET C O   1 
ATOM   5937 C  CB  . MET D 1 153 ? 34.693 -23.099 -2.375  1.00 22.13  ?  148 MET C CB  1 
ATOM   5938 C  CG  . MET D 1 153 ? 35.635 -24.178 -1.940  1.00 25.08  ?  148 MET C CG  1 
ATOM   5939 S  SD  . MET D 1 153 ? 36.928 -24.353 -3.187  1.00 23.78  ?  148 MET C SD  1 
ATOM   5940 C  CE  . MET D 1 153 ? 38.345 -23.653 -2.349  1.00 22.18  ?  148 MET C CE  1 
ATOM   5941 N  N   . THR D 1 154 ? 32.934 -24.640 0.172   1.00 25.04  ?  149 THR C N   1 
ATOM   5942 C  CA  . THR D 1 154 ? 32.489 -26.035 0.492   1.00 26.42  ?  149 THR C CA  1 
ATOM   5943 C  C   . THR D 1 154 ? 31.071 -26.273 -0.016  1.00 25.42  ?  149 THR C C   1 
ATOM   5944 O  O   . THR D 1 154 ? 30.880 -27.289 -0.704  1.00 27.71  ?  149 THR C O   1 
ATOM   5945 C  CB  . THR D 1 154 ? 32.519 -26.358 1.991   1.00 30.10  ?  149 THR C CB  1 
ATOM   5946 O  OG1 . THR D 1 154 ? 33.870 -26.224 2.426   1.00 29.95  ?  149 THR C OG1 1 
ATOM   5947 C  CG2 . THR D 1 154 ? 32.000 -27.753 2.295   1.00 32.26  ?  149 THR C CG2 1 
ATOM   5948 N  N   . GLY D 1 155 ? 30.140 -25.371 0.322   1.00 24.55  ?  150 GLY C N   1 
ATOM   5949 C  CA  . GLY D 1 155 ? 28.700 -25.419 -0.021  1.00 23.70  ?  150 GLY C CA  1 
ATOM   5950 C  C   . GLY D 1 155 ? 28.404 -25.217 -1.506  1.00 24.54  ?  150 GLY C C   1 
ATOM   5951 O  O   . GLY D 1 155 ? 27.253 -25.409 -1.924  1.00 25.79  ?  150 GLY C O   1 
ATOM   5952 N  N   . SER D 1 156 ? 29.409 -24.906 -2.330  1.00 24.55  ?  151 SER C N   1 
ATOM   5953 C  CA  . SER D 1 156 ? 29.223 -24.712 -3.787  1.00 23.27  ?  151 SER C CA  1 
ATOM   5954 C  C   . SER D 1 156 ? 29.943 -25.809 -4.603  1.00 23.10  ?  151 SER C C   1 
ATOM   5955 O  O   . SER D 1 156 ? 29.984 -25.683 -5.832  1.00 22.14  ?  151 SER C O   1 
ATOM   5956 C  CB  . SER D 1 156 ? 29.699 -23.316 -4.171  1.00 23.86  ?  151 SER C CB  1 
ATOM   5957 O  OG  . SER D 1 156 ? 28.922 -22.322 -3.525  1.00 24.57  ?  151 SER C OG  1 
ATOM   5958 N  N   . LEU D 1 157 ? 30.470 -26.854 -3.984  1.00 26.51  ?  152 LEU C N   1 
ATOM   5959 C  CA  . LEU D 1 157 ? 31.296 -27.844 -4.732  1.00 28.39  ?  152 LEU C CA  1 
ATOM   5960 C  C   . LEU D 1 157 ? 30.419 -28.628 -5.719  1.00 30.64  ?  152 LEU C C   1 
ATOM   5961 O  O   . LEU D 1 157 ? 30.901 -28.867 -6.833  1.00 29.27  ?  152 LEU C O   1 
ATOM   5962 C  CB  . LEU D 1 157 ? 32.083 -28.721 -3.768  1.00 29.84  ?  152 LEU C CB  1 
ATOM   5963 C  CG  . LEU D 1 157 ? 33.214 -28.023 -3.017  1.00 29.95  ?  152 LEU C CG  1 
ATOM   5964 C  CD1 . LEU D 1 157 ? 33.853 -28.978 -2.016  1.00 30.52  ?  152 LEU C CD1 1 
ATOM   5965 C  CD2 . LEU D 1 157 ? 34.276 -27.455 -3.961  1.00 31.52  ?  152 LEU C CD2 1 
ATOM   5966 N  N   . ASP D 1 158 ? 29.163 -28.949 -5.381  1.00 28.85  ?  153 ASP C N   1 
ATOM   5967 C  CA  . ASP D 1 158 ? 28.198 -29.593 -6.306  1.00 31.21  ?  153 ASP C CA  1 
ATOM   5968 C  C   . ASP D 1 158 ? 27.898 -28.666 -7.488  1.00 29.46  ?  153 ASP C C   1 
ATOM   5969 O  O   . ASP D 1 158 ? 27.763 -29.160 -8.637  1.00 23.93  ?  153 ASP C O   1 
ATOM   5970 C  CB  . ASP D 1 158 ? 26.890 -29.957 -5.592  1.00 36.45  ?  153 ASP C CB  1 
ATOM   5971 C  CG  . ASP D 1 158 ? 26.956 -31.272 -4.837  1.00 41.82  ?  153 ASP C CG  1 
ATOM   5972 O  OD1 . ASP D 1 158 ? 28.076 -31.832 -4.714  1.00 41.84  ?  153 ASP C OD1 1 
ATOM   5973 O  OD2 . ASP D 1 158 ? 25.872 -31.745 -4.398  1.00 51.30  -1 153 ASP C OD2 1 
ATOM   5974 N  N   . TYR D 1 159 ? 27.760 -27.363 -7.235  1.00 23.48  ?  154 TYR C N   1 
ATOM   5975 C  CA  . TYR D 1 159 ? 27.576 -26.363 -8.297  1.00 22.99  ?  154 TYR C CA  1 
ATOM   5976 C  C   . TYR D 1 159 ? 28.806 -26.403 -9.212  1.00 20.16  ?  154 TYR C C   1 
ATOM   5977 O  O   . TYR D 1 159 ? 28.600 -26.438 -10.427 1.00 20.64  ?  154 TYR C O   1 
ATOM   5978 C  CB  . TYR D 1 159 ? 27.359 -24.970 -7.714  1.00 23.80  ?  154 TYR C CB  1 
ATOM   5979 C  CG  . TYR D 1 159 ? 27.248 -23.877 -8.740  1.00 22.57  ?  154 TYR C CG  1 
ATOM   5980 C  CD1 . TYR D 1 159 ? 26.232 -23.883 -9.678  1.00 23.48  ?  154 TYR C CD1 1 
ATOM   5981 C  CD2 . TYR D 1 159 ? 28.122 -22.789 -8.729  1.00 23.36  ?  154 TYR C CD2 1 
ATOM   5982 C  CE1 . TYR D 1 159 ? 26.111 -22.873 -10.610 1.00 25.13  ?  154 TYR C CE1 1 
ATOM   5983 C  CE2 . TYR D 1 159 ? 27.999 -21.757 -9.642  1.00 23.00  ?  154 TYR C CE2 1 
ATOM   5984 C  CZ  . TYR D 1 159 ? 26.991 -21.808 -10.595 1.00 24.65  ?  154 TYR C CZ  1 
ATOM   5985 O  OH  . TYR D 1 159 ? 26.832 -20.842 -11.532 1.00 27.13  ?  154 TYR C OH  1 
ATOM   5986 N  N   . PHE D 1 160 ? 30.016 -26.358 -8.652  1.00 19.32  ?  155 PHE C N   1 
ATOM   5987 C  CA  . PHE D 1 160 ? 31.263 -26.426 -9.467  1.00 19.56  ?  155 PHE C CA  1 
ATOM   5988 C  C   . PHE D 1 160 ? 31.167 -27.640 -10.417 1.00 22.23  ?  155 PHE C C   1 
ATOM   5989 O  O   . PHE D 1 160 ? 31.363 -27.500 -11.630 1.00 19.88  ?  155 PHE C O   1 
ATOM   5990 C  CB  . PHE D 1 160 ? 32.507 -26.505 -8.591  1.00 18.20  ?  155 PHE C CB  1 
ATOM   5991 C  CG  . PHE D 1 160 ? 32.881 -25.276 -7.785  1.00 17.13  ?  155 PHE C CG  1 
ATOM   5992 C  CD1 . PHE D 1 160 ? 32.040 -24.181 -7.679  1.00 16.91  ?  155 PHE C CD1 1 
ATOM   5993 C  CD2 . PHE D 1 160 ? 34.090 -25.248 -7.089  1.00 17.13  ?  155 PHE C CD2 1 
ATOM   5994 C  CE1 . PHE D 1 160 ? 32.422 -23.080 -6.917  1.00 17.20  ?  155 PHE C CE1 1 
ATOM   5995 C  CE2 . PHE D 1 160 ? 34.462 -24.159 -6.316  1.00 17.48  ?  155 PHE C CE2 1 
ATOM   5996 C  CZ  . PHE D 1 160 ? 33.631 -23.073 -6.235  1.00 16.04  ?  155 PHE C CZ  1 
ATOM   5997 N  N   . ARG D 1 161 ? 30.794 -28.804 -9.885  1.00 25.05  ?  156 ARG C N   1 
ATOM   5998 C  CA  . ARG D 1 161 ? 30.742 -30.080 -10.663 1.00 25.45  ?  156 ARG C CA  1 
ATOM   5999 C  C   . ARG D 1 161 ? 29.712 -29.937 -11.778 1.00 24.97  ?  156 ARG C C   1 
ATOM   6000 O  O   . ARG D 1 161 ? 30.006 -30.351 -12.924 1.00 24.52  ?  156 ARG C O   1 
ATOM   6001 C  CB  . ARG D 1 161 ? 30.451 -31.269 -9.739  1.00 27.63  ?  156 ARG C CB  1 
ATOM   6002 C  CG  . ARG D 1 161 ? 31.564 -31.551 -8.746  1.00 31.82  ?  156 ARG C CG  1 
ATOM   6003 C  CD  . ARG D 1 161 ? 31.305 -32.815 -7.919  1.00 36.42  ?  156 ARG C CD  1 
ATOM   6004 N  NE  . ARG D 1 161 ? 32.417 -33.012 -7.010  1.00 38.30  ?  156 ARG C NE  1 
ATOM   6005 C  CZ  . ARG D 1 161 ? 32.420 -32.747 -5.703  1.00 41.81  ?  156 ARG C CZ  1 
ATOM   6006 N  NH1 . ARG D 1 161 ? 31.329 -32.309 -5.086  1.00 45.63  ?  156 ARG C NH1 1 
ATOM   6007 N  NH2 . ARG D 1 161 ? 33.528 -32.940 -5.006  1.00 43.55  ?  156 ARG C NH2 1 
ATOM   6008 N  N   . ARG D 1 162 ? 28.570 -29.342 -11.472 1.00 24.38  ?  157 ARG C N   1 
ATOM   6009 C  CA  . ARG D 1 162 ? 27.457 -29.181 -12.431 1.00 27.60  ?  157 ARG C CA  1 
ATOM   6010 C  C   . ARG D 1 162 ? 27.909 -28.322 -13.625 1.00 25.46  ?  157 ARG C C   1 
ATOM   6011 O  O   . ARG D 1 162 ? 27.478 -28.609 -14.765 1.00 23.82  ?  157 ARG C O   1 
ATOM   6012 C  CB  . ARG D 1 162 ? 26.238 -28.576 -11.737 1.00 33.45  ?  157 ARG C CB  1 
ATOM   6013 C  CG  . ARG D 1 162 ? 24.952 -28.692 -12.545 1.00 42.08  ?  157 ARG C CG  1 
ATOM   6014 C  CD  . ARG D 1 162 ? 23.791 -27.961 -11.889 1.00 48.07  ?  157 ARG C CD  1 
ATOM   6015 N  NE  . ARG D 1 162 ? 23.704 -26.596 -12.411 1.00 49.70  ?  157 ARG C NE  1 
ATOM   6016 C  CZ  . ARG D 1 162 ? 23.304 -25.526 -11.730 1.00 49.85  ?  157 ARG C CZ  1 
ATOM   6017 N  NH1 . ARG D 1 162 ? 22.936 -25.623 -10.460 1.00 54.68  ?  157 ARG C NH1 1 
ATOM   6018 N  NH2 . ARG D 1 162 ? 23.274 -24.351 -12.332 1.00 49.02  ?  157 ARG C NH2 1 
ATOM   6019 N  N   . ILE D 1 163 ? 28.760 -27.309 -13.415 1.00 24.77  ?  158 ILE C N   1 
ATOM   6020 C  CA  . ILE D 1 163 ? 29.141 -26.383 -14.527 1.00 20.38  ?  158 ILE C CA  1 
ATOM   6021 C  C   . ILE D 1 163 ? 30.525 -26.740 -15.083 1.00 19.70  ?  158 ILE C C   1 
ATOM   6022 O  O   . ILE D 1 163 ? 30.895 -26.087 -16.094 1.00 17.41  ?  158 ILE C O   1 
ATOM   6023 C  CB  . ILE D 1 163 ? 29.073 -24.909 -14.063 1.00 21.20  ?  158 ILE C CB  1 
ATOM   6024 C  CG1 . ILE D 1 163 ? 30.115 -24.581 -13.009 1.00 19.51  ?  158 ILE C CG1 1 
ATOM   6025 C  CG2 . ILE D 1 163 ? 27.667 -24.570 -13.579 1.00 23.20  ?  158 ILE C CG2 1 
ATOM   6026 C  CD1 . ILE D 1 163 ? 30.189 -23.087 -12.650 1.00 22.60  ?  158 ILE C CD1 1 
ATOM   6027 N  N   . LEU D 1 164 ? 31.197 -27.720 -14.471 1.00 21.82  ?  159 LEU C N   1 
ATOM   6028 C  CA  . LEU D 1 164 ? 32.596 -28.125 -14.775 1.00 22.02  ?  159 LEU C CA  1 
ATOM   6029 C  C   . LEU D 1 164 ? 32.779 -28.483 -16.259 1.00 23.17  ?  159 LEU C C   1 
ATOM   6030 O  O   . LEU D 1 164 ? 33.833 -28.208 -16.855 1.00 20.03  ?  159 LEU C O   1 
ATOM   6031 C  CB  . LEU D 1 164 ? 33.028 -29.272 -13.856 1.00 23.45  ?  159 LEU C CB  1 
ATOM   6032 C  CG  . LEU D 1 164 ? 34.541 -29.474 -13.806 1.00 22.22  ?  159 LEU C CG  1 
ATOM   6033 C  CD1 . LEU D 1 164 ? 35.184 -28.337 -13.056 1.00 21.75  ?  159 LEU C CD1 1 
ATOM   6034 C  CD2 . LEU D 1 164 ? 34.901 -30.825 -13.185 1.00 25.53  ?  159 LEU C CD2 1 
ATOM   6035 N  N   . PRO D 1 165 ? 31.782 -29.034 -16.977 1.00 21.12  ?  160 PRO C N   1 
ATOM   6036 C  CA  . PRO D 1 165 ? 32.015 -29.375 -18.399 1.00 21.91  ?  160 PRO C CA  1 
ATOM   6037 C  C   . PRO D 1 165 ? 32.455 -28.225 -19.326 1.00 18.32  ?  160 PRO C C   1 
ATOM   6038 O  O   . PRO D 1 165 ? 33.082 -28.445 -20.340 1.00 17.95  ?  160 PRO C O   1 
ATOM   6039 C  CB  . PRO D 1 165 ? 30.666 -29.919 -18.864 1.00 18.16  ?  160 PRO C CB  1 
ATOM   6040 C  CG  . PRO D 1 165 ? 30.062 -30.454 -17.584 1.00 21.32  ?  160 PRO C CG  1 
ATOM   6041 C  CD  . PRO D 1 165 ? 30.451 -29.441 -16.509 1.00 21.98  ?  160 PRO C CD  1 
ATOM   6042 N  N   . GLY D 1 166 ? 32.127 -26.979 -18.980 1.00 19.61  ?  161 GLY C N   1 
ATOM   6043 C  CA  . GLY D 1 166 ? 32.463 -25.823 -19.822 1.00 16.89  ?  161 GLY C CA  1 
ATOM   6044 C  C   . GLY D 1 166 ? 33.895 -25.357 -19.589 1.00 16.30  ?  161 GLY C C   1 
ATOM   6045 O  O   . GLY D 1 166 ? 34.409 -24.578 -20.408 1.00 16.60  ?  161 GLY C O   1 
ATOM   6046 N  N   . VAL D 1 167 ? 34.531 -25.837 -18.544 1.00 17.88  ?  162 VAL C N   1 
ATOM   6047 C  CA  . VAL D 1 167 ? 35.892 -25.369 -18.142 1.00 18.64  ?  162 VAL C CA  1 
ATOM   6048 C  C   . VAL D 1 167 ? 36.937 -26.008 -19.059 1.00 19.45  ?  162 VAL C C   1 
ATOM   6049 O  O   . VAL D 1 167 ? 36.953 -27.254 -19.196 1.00 19.00  ?  162 VAL C O   1 
ATOM   6050 C  CB  . VAL D 1 167 ? 36.203 -25.665 -16.671 1.00 16.72  ?  162 VAL C CB  1 
ATOM   6051 C  CG1 . VAL D 1 167 ? 37.629 -25.277 -16.275 1.00 14.02  ?  162 VAL C CG1 1 
ATOM   6052 C  CG2 . VAL D 1 167 ? 35.198 -25.004 -15.714 1.00 18.26  ?  162 VAL C CG2 1 
ATOM   6053 N  N   . GLY D 1 168 ? 37.782 -25.179 -19.649 1.00 17.72  ?  163 GLY C N   1 
ATOM   6054 C  CA  . GLY D 1 168 ? 38.985 -25.631 -20.368 1.00 17.95  ?  163 GLY C CA  1 
ATOM   6055 C  C   . GLY D 1 168 ? 40.205 -25.339 -19.519 1.00 16.93  ?  163 GLY C C   1 
ATOM   6056 O  O   . GLY D 1 168 ? 40.704 -24.219 -19.585 1.00 18.34  ?  163 GLY C O   1 
ATOM   6057 N  N   . ALA D 1 169 ? 40.579 -26.275 -18.662 1.00 16.22  ?  164 ALA C N   1 
ATOM   6058 C  CA  . ALA D 1 169 ? 41.678 -26.086 -17.713 1.00 15.54  ?  164 ALA C CA  1 
ATOM   6059 C  C   . ALA D 1 169 ? 42.960 -26.399 -18.470 1.00 15.93  ?  164 ALA C C   1 
ATOM   6060 O  O   . ALA D 1 169 ? 42.927 -27.214 -19.406 1.00 15.98  ?  164 ALA C O   1 
ATOM   6061 C  CB  . ALA D 1 169 ? 41.488 -26.899 -16.484 1.00 17.25  ?  164 ALA C CB  1 
ATOM   6062 N  N   . PHE D 1 170 ? 44.061 -25.745 -18.107 1.00 15.51  ?  165 PHE C N   1 
ATOM   6063 C  CA  . PHE D 1 170 ? 45.344 -26.001 -18.796 1.00 15.36  ?  165 PHE C CA  1 
ATOM   6064 C  C   . PHE D 1 170 ? 46.481 -25.908 -17.805 1.00 16.37  ?  165 PHE C C   1 
ATOM   6065 O  O   . PHE D 1 170 ? 46.296 -25.398 -16.658 1.00 17.26  ?  165 PHE C O   1 
ATOM   6066 C  CB  . PHE D 1 170 ? 45.527 -25.057 -19.971 1.00 16.27  ?  165 PHE C CB  1 
ATOM   6067 C  CG  . PHE D 1 170 ? 45.542 -23.588 -19.629 1.00 17.62  ?  165 PHE C CG  1 
ATOM   6068 C  CD1 . PHE D 1 170 ? 46.718 -22.980 -19.209 1.00 18.25  ?  165 PHE C CD1 1 
ATOM   6069 C  CD2 . PHE D 1 170 ? 44.386 -22.828 -19.743 1.00 18.33  ?  165 PHE C CD2 1 
ATOM   6070 C  CE1 . PHE D 1 170 ? 46.738 -21.614 -18.946 1.00 19.02  ?  165 PHE C CE1 1 
ATOM   6071 C  CE2 . PHE D 1 170 ? 44.401 -21.470 -19.440 1.00 19.99  ?  165 PHE C CE2 1 
ATOM   6072 C  CZ  . PHE D 1 170 ? 45.574 -20.868 -19.043 1.00 19.33  ?  165 PHE C CZ  1 
ATOM   6073 N  N   . ARG D 1 171 ? 47.645 -26.278 -18.317 1.00 17.08  ?  166 ARG C N   1 
ATOM   6074 C  CA  . ARG D 1 171 ? 48.935 -26.255 -17.602 1.00 17.68  ?  166 ARG C CA  1 
ATOM   6075 C  C   . ARG D 1 171 ? 49.959 -25.635 -18.547 1.00 18.47  ?  166 ARG C C   1 
ATOM   6076 O  O   . ARG D 1 171 ? 49.979 -25.995 -19.706 1.00 19.65  ?  166 ARG C O   1 
ATOM   6077 C  CB  . ARG D 1 171 ? 49.373 -27.668 -17.204 1.00 19.73  ?  166 ARG C CB  1 
ATOM   6078 C  CG  . ARG D 1 171 ? 48.363 -28.429 -16.356 1.00 19.88  ?  166 ARG C CG  1 
ATOM   6079 C  CD  . ARG D 1 171 ? 48.334 -27.840 -14.958 1.00 19.74  ?  166 ARG C CD  1 
ATOM   6080 N  NE  . ARG D 1 171 ? 47.501 -28.564 -14.025 1.00 20.13  ?  166 ARG C NE  1 
ATOM   6081 C  CZ  . ARG D 1 171 ? 46.238 -28.266 -13.739 1.00 19.78  ?  166 ARG C CZ  1 
ATOM   6082 N  NH1 . ARG D 1 171 ? 45.643 -27.230 -14.302 1.00 18.41  ?  166 ARG C NH1 1 
ATOM   6083 N  NH2 . ARG D 1 171 ? 45.574 -29.007 -12.872 1.00 22.09  ?  166 ARG C NH2 1 
ATOM   6084 N  N   . LEU D 1 172 ? 50.820 -24.778 -18.026 1.00 19.60  ?  167 LEU C N   1 
ATOM   6085 C  CA  . LEU D 1 172 ? 51.823 -24.018 -18.808 1.00 20.70  ?  167 LEU C CA  1 
ATOM   6086 C  C   . LEU D 1 172 ? 53.132 -24.212 -18.043 1.00 22.05  ?  167 LEU C C   1 
ATOM   6087 O  O   . LEU D 1 172 ? 53.296 -23.626 -16.966 1.00 20.26  ?  167 LEU C O   1 
ATOM   6088 C  CB  . LEU D 1 172 ? 51.401 -22.548 -18.913 1.00 22.96  ?  167 LEU C CB  1 
ATOM   6089 C  CG  . LEU D 1 172 ? 52.389 -21.615 -19.620 1.00 23.40  ?  167 LEU C CG  1 
ATOM   6090 C  CD1 . LEU D 1 172 ? 52.777 -22.153 -20.975 1.00 28.30  ?  167 LEU C CD1 1 
ATOM   6091 C  CD2 . LEU D 1 172 ? 51.818 -20.218 -19.743 1.00 23.10  ?  167 LEU C CD2 1 
ATOM   6092 N  N   . ARG D 1 173 ? 53.971 -25.125 -18.513 1.00 24.16  ?  168 ARG C N   1 
ATOM   6093 C  CA  . ARG D 1 173 ? 55.334 -25.280 -17.961 1.00 26.47  ?  168 ARG C CA  1 
ATOM   6094 C  C   . ARG D 1 173 ? 56.097 -24.064 -18.479 1.00 20.21  ?  168 ARG C C   1 
ATOM   6095 O  O   . ARG D 1 173 ? 56.156 -23.870 -19.678 1.00 21.55  ?  168 ARG C O   1 
ATOM   6096 C  CB  . ARG D 1 173 ? 55.964 -26.635 -18.323 1.00 33.54  ?  168 ARG C CB  1 
ATOM   6097 C  CG  . ARG D 1 173 ? 55.500 -27.216 -19.653 1.00 43.80  ?  168 ARG C CG  1 
ATOM   6098 C  CD  . ARG D 1 173 ? 55.840 -28.686 -19.885 1.00 50.48  ?  168 ARG C CD  1 
ATOM   6099 N  NE  . ARG D 1 173 ? 55.939 -29.046 -21.303 1.00 56.17  ?  168 ARG C NE  1 
ATOM   6100 C  CZ  . ARG D 1 173 ? 56.961 -28.735 -22.114 1.00 59.47  ?  168 ARG C CZ  1 
ATOM   6101 N  NH1 . ARG D 1 173 ? 56.955 -29.134 -23.378 1.00 60.44  ?  168 ARG C NH1 1 
ATOM   6102 N  NH2 . ARG D 1 173 ? 57.981 -28.018 -21.672 1.00 58.10  ?  168 ARG C NH2 1 
ATOM   6103 N  N   . VAL D 1 174 ? 56.619 -23.249 -17.574 1.00 22.03  ?  169 VAL C N   1 
ATOM   6104 C  CA  . VAL D 1 174 ? 57.346 -21.998 -17.922 1.00 20.09  ?  169 VAL C CA  1 
ATOM   6105 C  C   . VAL D 1 174 ? 58.754 -22.373 -18.403 1.00 19.18  ?  169 VAL C C   1 
ATOM   6106 O  O   . VAL D 1 174 ? 59.551 -22.850 -17.583 1.00 20.40  ?  169 VAL C O   1 
ATOM   6107 C  CB  . VAL D 1 174 ? 57.386 -21.003 -16.750 1.00 18.82  ?  169 VAL C CB  1 
ATOM   6108 C  CG1 . VAL D 1 174 ? 58.076 -19.717 -17.146 1.00 19.89  ?  169 VAL C CG1 1 
ATOM   6109 C  CG2 . VAL D 1 174 ? 55.987 -20.719 -16.222 1.00 18.26  ?  169 VAL C CG2 1 
ATOM   6110 N  N   . ALA D 1 175 ? 59.008 -22.132 -19.683 1.00 20.18  ?  170 ALA C N   1 
ATOM   6111 C  CA  . ALA D 1 175 ? 60.319 -22.322 -20.340 1.00 21.25  ?  170 ALA C CA  1 
ATOM   6112 C  C   . ALA D 1 175 ? 61.116 -21.020 -20.260 1.00 21.06  ?  170 ALA C C   1 
ATOM   6113 O  O   . ALA D 1 175 ? 62.339 -21.103 -20.097 1.00 21.28  ?  170 ALA C O   1 
ATOM   6114 C  CB  . ALA D 1 175 ? 60.114 -22.792 -21.754 1.00 21.06  ?  170 ALA C CB  1 
ATOM   6115 N  N   . GLU D 1 176 ? 60.457 -19.862 -20.368 1.00 20.42  ?  171 GLU C N   1 
ATOM   6116 C  CA  . GLU D 1 176 ? 61.116 -18.529 -20.344 1.00 23.86  ?  171 GLU C CA  1 
ATOM   6117 C  C   . GLU D 1 176 ? 60.263 -17.596 -19.495 1.00 20.77  ?  171 GLU C C   1 
ATOM   6118 O  O   . GLU D 1 176 ? 59.017 -17.638 -19.650 1.00 19.68  ?  171 GLU C O   1 
ATOM   6119 C  CB  . GLU D 1 176 ? 61.279 -17.887 -21.730 1.00 27.26  ?  171 GLU C CB  1 
ATOM   6120 C  CG  . GLU D 1 176 ? 61.694 -18.835 -22.853 1.00 34.39  ?  171 GLU C CG  1 
ATOM   6121 C  CD  . GLU D 1 176 ? 61.721 -18.216 -24.251 1.00 42.48  ?  171 GLU C CD  1 
ATOM   6122 O  OE1 . GLU D 1 176 ? 62.592 -17.340 -24.511 1.00 44.45  ?  171 GLU C OE1 1 
ATOM   6123 O  OE2 . GLU D 1 176 ? 60.850 -18.588 -25.084 1.00 52.33  -1 171 GLU C OE2 1 
ATOM   6124 N  N   . ALA D 1 177 ? 60.890 -16.767 -18.663 1.00 19.80  ?  172 ALA C N   1 
ATOM   6125 C  CA  . ALA D 1 177 ? 60.177 -15.751 -17.841 1.00 19.62  ?  172 ALA C CA  1 
ATOM   6126 C  C   . ALA D 1 177 ? 60.928 -14.438 -17.950 1.00 20.69  ?  172 ALA C C   1 
ATOM   6127 O  O   . ALA D 1 177 ? 62.149 -14.434 -17.726 1.00 23.78  ?  172 ALA C O   1 
ATOM   6128 C  CB  . ALA D 1 177 ? 60.043 -16.182 -16.412 1.00 17.71  ?  172 ALA C CB  1 
ATOM   6129 N  N   . ASP D 1 178 ? 60.261 -13.378 -18.364 1.00 22.23  ?  173 ASP C N   1 
ATOM   6130 C  CA  . ASP D 1 178 ? 60.880 -12.027 -18.445 1.00 21.28  ?  173 ASP C CA  1 
ATOM   6131 C  C   . ASP D 1 178 ? 59.977 -11.035 -17.692 1.00 19.45  ?  173 ASP C C   1 
ATOM   6132 O  O   . ASP D 1 178 ? 58.821 -11.223 -17.743 1.00 16.66  ?  173 ASP C O   1 
ATOM   6133 C  CB  . ASP D 1 178 ? 61.124 -11.688 -19.915 1.00 24.54  ?  173 ASP C CB  1 
ATOM   6134 C  CG  . ASP D 1 178 ? 62.100 -12.625 -20.650 1.00 30.82  ?  173 ASP C CG  1 
ATOM   6135 O  OD1 . ASP D 1 178 ? 61.635 -13.504 -21.459 1.00 32.84  ?  173 ASP C OD1 1 
ATOM   6136 O  OD2 . ASP D 1 178 ? 63.327 -12.437 -20.482 1.00 34.47  -1 173 ASP C OD2 1 
ATOM   6137 N  N   . GLY D 1 179 ? 60.565 -10.019 -17.075 1.00 18.73  ?  174 GLY C N   1 
ATOM   6138 C  CA  . GLY D 1 179 ? 59.902 -9.007  -16.231 1.00 20.96  ?  174 GLY C CA  1 
ATOM   6139 C  C   . GLY D 1 179 ? 60.359 -7.610  -16.614 1.00 20.29  ?  174 GLY C C   1 
ATOM   6140 O  O   . GLY D 1 179 ? 61.612 -7.340  -16.530 1.00 19.40  ?  174 GLY C O   1 
ATOM   6141 N  N   . MET D 1 180 ? 59.412 -6.759  -17.004 1.00 18.70  ?  175 MET C N   1 
ATOM   6142 C  CA  . MET D 1 180 ? 59.605 -5.299  -17.186 1.00 19.35  ?  175 MET C CA  1 
ATOM   6143 C  C   . MET D 1 180 ? 59.227 -4.576  -15.903 1.00 16.98  ?  175 MET C C   1 
ATOM   6144 O  O   . MET D 1 180 ? 58.025 -4.611  -15.495 1.00 17.33  ?  175 MET C O   1 
ATOM   6145 C  CB  . MET D 1 180 ? 58.767 -4.778  -18.360 1.00 21.41  ?  175 MET C CB  1 
ATOM   6146 C  CG  . MET D 1 180 ? 58.886 -3.279  -18.555 1.00 23.14  ?  175 MET C CG  1 
ATOM   6147 S  SD  . MET D 1 180 ? 60.332 -2.769  -19.507 1.00 25.13  ?  175 MET C SD  1 
ATOM   6148 C  CE  . MET D 1 180 ? 59.835 -3.447  -21.084 1.00 23.95  ?  175 MET C CE  1 
ATOM   6149 N  N   . PHE D 1 181 ? 60.199 -3.992  -15.223 1.00 16.60  ?  176 PHE C N   1 
ATOM   6150 C  CA  . PHE D 1 181 ? 59.935 -3.126  -14.040 1.00 16.40  ?  176 PHE C CA  1 
ATOM   6151 C  C   . PHE D 1 181 ? 60.364 -1.708  -14.408 1.00 17.86  ?  176 PHE C C   1 
ATOM   6152 O  O   . PHE D 1 181 ? 61.450 -1.307  -14.011 1.00 17.83  ?  176 PHE C O   1 
ATOM   6153 C  CB  . PHE D 1 181 ? 60.552 -3.712  -12.764 1.00 17.04  ?  176 PHE C CB  1 
ATOM   6154 C  CG  . PHE D 1 181 ? 59.856 -4.986  -12.365 1.00 18.17  ?  176 PHE C CG  1 
ATOM   6155 C  CD1 . PHE D 1 181 ? 60.138 -6.173  -13.023 1.00 19.04  ?  176 PHE C CD1 1 
ATOM   6156 C  CD2 . PHE D 1 181 ? 58.844 -4.977  -11.421 1.00 17.33  ?  176 PHE C CD2 1 
ATOM   6157 C  CE1 . PHE D 1 181 ? 59.468 -7.345  -12.704 1.00 18.43  ?  176 PHE C CE1 1 
ATOM   6158 C  CE2 . PHE D 1 181 ? 58.184 -6.153  -11.099 1.00 18.72  ?  176 PHE C CE2 1 
ATOM   6159 C  CZ  . PHE D 1 181 ? 58.513 -7.331  -11.726 1.00 17.58  ?  176 PHE C CZ  1 
ATOM   6160 N  N   . LYS D 1 182 ? 59.529 -1.040  -15.205 1.00 17.05  ?  177 LYS C N   1 
ATOM   6161 C  CA  . LYS D 1 182 ? 59.810 0.301   -15.765 1.00 17.73  ?  177 LYS C CA  1 
ATOM   6162 C  C   . LYS D 1 182 ? 59.418 1.331   -14.712 1.00 16.49  ?  177 LYS C C   1 
ATOM   6163 O  O   . LYS D 1 182 ? 58.229 1.656   -14.641 1.00 15.66  ?  177 LYS C O   1 
ATOM   6164 C  CB  . LYS D 1 182 ? 59.092 0.496   -17.092 1.00 16.95  ?  177 LYS C CB  1 
ATOM   6165 C  CG  . LYS D 1 182 ? 59.420 1.808   -17.767 1.00 19.92  ?  177 LYS C CG  1 
ATOM   6166 C  CD  . LYS D 1 182 ? 59.101 1.799   -19.245 1.00 24.61  ?  177 LYS C CD  1 
ATOM   6167 C  CE  . LYS D 1 182 ? 58.982 3.186   -19.828 1.00 27.99  ?  177 LYS C CE  1 
ATOM   6168 N  NZ  . LYS D 1 182 ? 59.817 4.165   -19.087 1.00 30.07  ?  177 LYS C NZ  1 
ATOM   6169 N  N   . LEU D 1 183 ? 60.387 1.735   -13.877 1.00 16.55  ?  178 LEU C N   1 
ATOM   6170 C  CA  . LEU D 1 183 ? 60.105 2.469   -12.624 1.00 16.80  ?  178 LEU C CA  1 
ATOM   6171 C  C   . LEU D 1 183 ? 61.143 3.587   -12.423 1.00 15.78  ?  178 LEU C C   1 
ATOM   6172 O  O   . LEU D 1 183 ? 61.576 3.786   -11.265 1.00 17.72  ?  178 LEU C O   1 
ATOM   6173 C  CB  . LEU D 1 183 ? 60.113 1.475   -11.452 1.00 16.52  ?  178 LEU C CB  1 
ATOM   6174 C  CG  . LEU D 1 183 ? 59.066 0.345   -11.419 1.00 15.95  ?  178 LEU C CG  1 
ATOM   6175 C  CD1 . LEU D 1 183 ? 59.393 -0.586  -10.266 1.00 16.75  ?  178 LEU C CD1 1 
ATOM   6176 C  CD2 . LEU D 1 183 ? 57.671 0.880   -11.259 1.00 16.33  ?  178 LEU C CD2 1 
ATOM   6177 N  N   . SER D 1 184 ? 61.481 4.314   -13.485 1.00 16.00  ?  179 SER C N   1 
ATOM   6178 C  CA  . SER D 1 184 ? 62.304 5.567   -13.484 1.00 18.17  ?  179 SER C CA  1 
ATOM   6179 C  C   . SER D 1 184 ? 63.776 5.271   -13.079 1.00 16.90  ?  179 SER C C   1 
ATOM   6180 O  O   . SER D 1 184 ? 64.548 6.220   -12.838 1.00 17.96  ?  179 SER C O   1 
ATOM   6181 C  CB  . SER D 1 184 ? 61.689 6.631   -12.618 1.00 18.18  ?  179 SER C CB  1 
ATOM   6182 O  OG  . SER D 1 184 ? 60.321 6.906   -12.967 1.00 18.65  ?  179 SER C OG  1 
ATOM   6183 N  N   . GLN D 1 185 ? 64.224 4.036   -13.224 1.00 18.60  ?  180 GLN C N   1 
ATOM   6184 C  CA  . GLN D 1 185 ? 65.635 3.654   -12.899 1.00 19.00  ?  180 GLN C CA  1 
ATOM   6185 C  C   . GLN D 1 185 ? 66.637 4.393   -13.808 1.00 20.34  ?  180 GLN C C   1 
ATOM   6186 O  O   . GLN D 1 185 ? 67.787 4.560   -13.333 1.00 21.37  ?  180 GLN C O   1 
ATOM   6187 C  CB  . GLN D 1 185 ? 65.855 2.142   -12.964 1.00 20.14  ?  180 GLN C CB  1 
ATOM   6188 C  CG  . GLN D 1 185 ? 65.087 1.320   -11.916 1.00 19.89  ?  180 GLN C CG  1 
ATOM   6189 C  CD  . GLN D 1 185 ? 63.823 0.742   -12.525 1.00 18.77  ?  180 GLN C CD  1 
ATOM   6190 O  OE1 . GLN D 1 185 ? 63.160 1.420   -13.318 1.00 18.17  ?  180 GLN C OE1 1 
ATOM   6191 N  NE2 . GLN D 1 185 ? 63.539 -0.535  -12.270 1.00 17.43  ?  180 GLN C NE2 1 
ATOM   6192 N  N   . GLU D 1 186 ? 66.214 4.856   -14.992 1.00 21.24  ?  181 GLU C N   1 
ATOM   6193 C  CA  . GLU D 1 186 ? 66.992 5.621   -16.021 1.00 24.93  ?  181 GLU C CA  1 
ATOM   6194 C  C   . GLU D 1 186 ? 67.219 7.067   -15.541 1.00 25.72  ?  181 GLU C C   1 
ATOM   6195 O  O   . GLU D 1 186 ? 68.141 7.766   -16.081 1.00 23.75  ?  181 GLU C O   1 
ATOM   6196 C  CB  . GLU D 1 186 ? 66.301 5.588   -17.400 1.00 25.36  ?  181 GLU C CB  1 
ATOM   6197 C  CG  . GLU D 1 186 ? 65.177 6.639   -17.657 1.00 26.39  ?  181 GLU C CG  1 
ATOM   6198 C  CD  . GLU D 1 186 ? 63.800 6.403   -17.039 1.00 33.00  ?  181 GLU C CD  1 
ATOM   6199 O  OE1 . GLU D 1 186 ? 63.639 5.334   -16.437 1.00 28.01  ?  181 GLU C OE1 1 
ATOM   6200 O  OE2 . GLU D 1 186 ? 62.892 7.313   -17.097 1.00 30.78  -1 181 GLU C OE2 1 
ATOM   6201 N  N   . GLN D 1 187 ? 66.391 7.572   -14.616 1.00 23.79  ?  182 GLN C N   1 
ATOM   6202 C  CA  . GLN D 1 187 ? 66.548 8.967   -14.137 1.00 23.79  ?  182 GLN C CA  1 
ATOM   6203 C  C   . GLN D 1 187 ? 67.647 9.031   -13.055 1.00 21.47  ?  182 GLN C C   1 
ATOM   6204 O  O   . GLN D 1 187 ? 67.982 7.984   -12.420 1.00 19.04  ?  182 GLN C O   1 
ATOM   6205 C  CB  . GLN D 1 187 ? 65.209 9.544   -13.692 1.00 24.23  ?  182 GLN C CB  1 
ATOM   6206 C  CG  . GLN D 1 187 ? 64.154 9.484   -14.781 1.00 23.97  ?  182 GLN C CG  1 
ATOM   6207 C  CD  . GLN D 1 187 ? 64.397 10.444  -15.920 1.00 28.53  ?  182 GLN C CD  1 
ATOM   6208 O  OE1 . GLN D 1 187 ? 64.859 11.578  -15.747 1.00 29.30  ?  182 GLN C OE1 1 
ATOM   6209 N  NE2 . GLN D 1 187 ? 63.968 10.030  -17.088 1.00 27.19  ?  182 GLN C NE2 1 
ATOM   6210 N  N   . GLN D 1 188 ? 68.170 10.232  -12.843 1.00 23.14  ?  183 GLN C N   1 
ATOM   6211 C  CA  . GLN D 1 188 ? 69.098 10.536  -11.720 1.00 27.06  ?  183 GLN C CA  1 
ATOM   6212 C  C   . GLN D 1 188 ? 68.341 10.322  -10.405 1.00 27.41  ?  183 GLN C C   1 
ATOM   6213 O  O   . GLN D 1 188 ? 67.121 10.519  -10.337 1.00 23.70  ?  183 GLN C O   1 
ATOM   6214 C  CB  . GLN D 1 188 ? 69.640 11.967  -11.842 1.00 27.16  ?  183 GLN C CB  1 
ATOM   6215 C  CG  . GLN D 1 188 ? 70.404 12.252  -13.131 1.00 29.60  ?  183 GLN C CG  1 
ATOM   6216 C  CD  . GLN D 1 188 ? 71.594 11.333  -13.256 1.00 31.76  ?  183 GLN C CD  1 
ATOM   6217 O  OE1 . GLN D 1 188 ? 72.341 11.134  -12.306 1.00 32.60  ?  183 GLN C OE1 1 
ATOM   6218 N  NE2 . GLN D 1 188 ? 71.769 10.738  -14.422 1.00 34.30  ?  183 GLN C NE2 1 
ATOM   6219 N  N   . PRO D 1 189 ? 69.049 9.938   -9.322  1.00 30.78  ?  184 PRO C N   1 
ATOM   6220 C  CA  . PRO D 1 189 ? 68.437 9.748   -7.997  1.00 30.93  ?  184 PRO C CA  1 
ATOM   6221 C  C   . PRO D 1 189 ? 67.435 10.811  -7.518  1.00 29.73  ?  184 PRO C C   1 
ATOM   6222 O  O   . PRO D 1 189 ? 66.412 10.417  -6.944  1.00 29.48  ?  184 PRO C O   1 
ATOM   6223 C  CB  . PRO D 1 189 ? 69.663 9.750   -7.070  1.00 33.39  ?  184 PRO C CB  1 
ATOM   6224 C  CG  . PRO D 1 189 ? 70.773 9.130   -7.922  1.00 32.24  ?  184 PRO C CG  1 
ATOM   6225 C  CD  . PRO D 1 189 ? 70.496 9.632   -9.325  1.00 34.45  ?  184 PRO C CD  1 
ATOM   6226 N  N   . ALA D 1 190 ? 67.741 12.095  -7.737  1.00 28.44  ?  185 ALA C N   1 
ATOM   6227 C  CA  . ALA D 1 190 ? 66.931 13.258  -7.306  1.00 29.72  ?  185 ALA C CA  1 
ATOM   6228 C  C   . ALA D 1 190 ? 65.583 13.205  -8.030  1.00 29.67  ?  185 ALA C C   1 
ATOM   6229 O  O   . ALA D 1 190 ? 64.533 13.468  -7.400  1.00 25.28  ?  185 ALA C O   1 
ATOM   6230 C  CB  . ALA D 1 190 ? 67.654 14.542  -7.611  1.00 32.87  ?  185 ALA C CB  1 
ATOM   6231 N  N   . ILE D 1 191 ? 65.618 12.849  -9.316  1.00 27.30  ?  186 ILE C N   1 
ATOM   6232 C  CA  . ILE D 1 191 ? 64.402 12.813  -10.162 1.00 26.09  ?  186 ILE C CA  1 
ATOM   6233 C  C   . ILE D 1 191 ? 63.577 11.601  -9.735  1.00 24.19  ?  186 ILE C C   1 
ATOM   6234 O  O   . ILE D 1 191 ? 62.367 11.771  -9.600  1.00 23.01  ?  186 ILE C O   1 
ATOM   6235 C  CB  . ILE D 1 191 ? 64.733 12.864  -11.667 1.00 26.55  ?  186 ILE C CB  1 
ATOM   6236 C  CG1 . ILE D 1 191 ? 65.364 14.219  -12.012 1.00 31.36  ?  186 ILE C CG1 1 
ATOM   6237 C  CG2 . ILE D 1 191 ? 63.495 12.593  -12.496 1.00 23.20  ?  186 ILE C CG2 1 
ATOM   6238 C  CD1 . ILE D 1 191 ? 65.973 14.282  -13.371 1.00 31.81  ?  186 ILE C CD1 1 
ATOM   6239 N  N   . ARG D 1 192 ? 64.203 10.440  -9.542  1.00 22.24  ?  187 ARG C N   1 
ATOM   6240 C  CA  . ARG D 1 192 ? 63.511 9.214   -9.047  1.00 25.67  ?  187 ARG C CA  1 
ATOM   6241 C  C   . ARG D 1 192 ? 62.783 9.545   -7.736  1.00 23.84  ?  187 ARG C C   1 
ATOM   6242 O  O   . ARG D 1 192 ? 61.594 9.134   -7.576  1.00 20.64  ?  187 ARG C O   1 
ATOM   6243 C  CB  . ARG D 1 192 ? 64.479 8.044   -8.853  1.00 26.58  ?  187 ARG C CB  1 
ATOM   6244 C  CG  . ARG D 1 192 ? 65.136 7.564   -10.137 1.00 28.00  ?  187 ARG C CG  1 
ATOM   6245 C  CD  . ARG D 1 192 ? 66.262 6.611   -9.844  1.00 32.26  ?  187 ARG C CD  1 
ATOM   6246 N  NE  . ARG D 1 192 ? 65.773 5.268   -9.582  1.00 41.37  ?  187 ARG C NE  1 
ATOM   6247 C  CZ  . ARG D 1 192 ? 66.360 4.416   -8.738  1.00 47.76  ?  187 ARG C CZ  1 
ATOM   6248 N  NH1 . ARG D 1 192 ? 65.892 3.183   -8.584  1.00 38.29  ?  187 ARG C NH1 1 
ATOM   6249 N  NH2 . ARG D 1 192 ? 67.412 4.814   -8.040  1.00 55.82  ?  187 ARG C NH2 1 
ATOM   6250 N  N   . ARG D 1 193 ? 63.412 10.312  -6.848  1.00 23.89  ?  188 ARG C N   1 
ATOM   6251 C  CA  . ARG D 1 193 ? 62.764 10.633  -5.546  1.00 24.57  ?  188 ARG C CA  1 
ATOM   6252 C  C   . ARG D 1 193 ? 61.587 11.572  -5.782  1.00 20.76  ?  188 ARG C C   1 
ATOM   6253 O  O   . ARG D 1 193 ? 60.524 11.327  -5.170  1.00 19.99  ?  188 ARG C O   1 
ATOM   6254 C  CB  . ARG D 1 193 ? 63.775 11.165  -4.545  1.00 28.72  ?  188 ARG C CB  1 
ATOM   6255 C  CG  . ARG D 1 193 ? 64.825 10.120  -4.194  1.00 36.28  ?  188 ARG C CG  1 
ATOM   6256 C  CD  . ARG D 1 193 ? 65.619 10.565  -2.986  1.00 43.18  ?  188 ARG C CD  1 
ATOM   6257 N  NE  . ARG D 1 193 ? 66.234 11.844  -3.279  1.00 43.69  ?  188 ARG C NE  1 
ATOM   6258 C  CZ  . ARG D 1 193 ? 67.497 12.009  -3.656  1.00 46.34  ?  188 ARG C CZ  1 
ATOM   6259 N  NH1 . ARG D 1 193 ? 68.300 10.969  -3.798  1.00 46.43  ?  188 ARG C NH1 1 
ATOM   6260 N  NH2 . ARG D 1 193 ? 67.946 13.227  -3.896  1.00 44.69  ?  188 ARG C NH2 1 
ATOM   6261 N  N   . ARG D 1 194 ? 61.713 12.538  -6.702  1.00 20.54  ?  189 ARG C N   1 
ATOM   6262 C  CA  . ARG D 1 194 ? 60.603 13.463  -7.051  1.00 18.96  ?  189 ARG C CA  1 
ATOM   6263 C  C   . ARG D 1 194 ? 59.395 12.665  -7.556  1.00 19.51  ?  189 ARG C C   1 
ATOM   6264 O  O   . ARG D 1 194 ? 58.305 12.894  -7.043  1.00 17.48  ?  189 ARG C O   1 
ATOM   6265 C  CB  . ARG D 1 194 ? 61.058 14.505  -8.078  1.00 20.54  ?  189 ARG C CB  1 
ATOM   6266 C  CG  . ARG D 1 194 ? 61.854 15.631  -7.449  1.00 23.78  ?  189 ARG C CG  1 
ATOM   6267 C  CD  . ARG D 1 194 ? 62.416 16.596  -8.477  1.00 27.65  ?  189 ARG C CD  1 
ATOM   6268 N  NE  . ARG D 1 194 ? 63.541 17.281  -7.860  1.00 31.72  ?  189 ARG C NE  1 
ATOM   6269 C  CZ  . ARG D 1 194 ? 64.569 17.836  -8.508  1.00 36.06  ?  189 ARG C CZ  1 
ATOM   6270 N  NH1 . ARG D 1 194 ? 64.640 17.825  -9.832  1.00 34.07  ?  189 ARG C NH1 1 
ATOM   6271 N  NH2 . ARG D 1 194 ? 65.551 18.379  -7.815  1.00 38.05  ?  189 ARG C NH2 1 
ATOM   6272 N  N   . VAL D 1 195 ? 59.619 11.731  -8.487  1.00 18.65  ?  190 VAL C N   1 
ATOM   6273 C  CA  . VAL D 1 195 ? 58.571 10.826  -9.027  1.00 19.76  ?  190 VAL C CA  1 
ATOM   6274 C  C   . VAL D 1 195 ? 57.956 9.998   -7.884  1.00 18.74  ?  190 VAL C C   1 
ATOM   6275 O  O   . VAL D 1 195 ? 56.707 9.963   -7.749  1.00 17.77  ?  190 VAL C O   1 
ATOM   6276 C  CB  . VAL D 1 195 ? 59.129 9.940   -10.156 1.00 19.39  ?  190 VAL C CB  1 
ATOM   6277 C  CG1 . VAL D 1 195 ? 58.109 8.909   -10.604 1.00 18.65  ?  190 VAL C CG1 1 
ATOM   6278 C  CG2 . VAL D 1 195 ? 59.602 10.769  -11.335 1.00 20.17  ?  190 VAL C CG2 1 
ATOM   6279 N  N   . ARG D 1 196 ? 58.777 9.274   -7.144  1.00 19.75  ?  191 ARG C N   1 
ATOM   6280 C  CA  . ARG D 1 196 ? 58.280 8.423   -6.026  1.00 26.73  ?  191 ARG C CA  1 
ATOM   6281 C  C   . ARG D 1 196 ? 57.389 9.295   -5.127  1.00 24.12  ?  191 ARG C C   1 
ATOM   6282 O  O   . ARG D 1 196 ? 56.293 8.841   -4.724  1.00 25.92  ?  191 ARG C O   1 
ATOM   6283 C  CB  . ARG D 1 196 ? 59.448 7.796   -5.251  1.00 31.25  ?  191 ARG C CB  1 
ATOM   6284 C  CG  . ARG D 1 196 ? 59.060 6.579   -4.424  1.00 39.80  ?  191 ARG C CG  1 
ATOM   6285 C  CD  . ARG D 1 196 ? 58.586 6.952   -3.030  1.00 47.57  ?  191 ARG C CD  1 
ATOM   6286 N  NE  . ARG D 1 196 ? 59.750 7.288   -2.212  1.00 54.55  ?  191 ARG C NE  1 
ATOM   6287 C  CZ  . ARG D 1 196 ? 59.981 8.458   -1.614  1.00 65.01  ?  191 ARG C CZ  1 
ATOM   6288 N  NH1 . ARG D 1 196 ? 59.103 9.449   -1.673  1.00 65.69  ?  191 ARG C NH1 1 
ATOM   6289 N  NH2 . ARG D 1 196 ? 61.103 8.625   -0.932  1.00 73.02  ?  191 ARG C NH2 1 
ATOM   6290 N  N   . HIS D 1 197 ? 57.802 10.532  -4.862  1.00 22.89  ?  192 HIS C N   1 
ATOM   6291 C  CA  . HIS D 1 197 ? 57.111 11.416  -3.893  1.00 24.13  ?  192 HIS C CA  1 
ATOM   6292 C  C   . HIS D 1 197 ? 55.784 11.856  -4.499  1.00 24.58  ?  192 HIS C C   1 
ATOM   6293 O  O   . HIS D 1 197 ? 54.773 11.861  -3.765  1.00 27.78  ?  192 HIS C O   1 
ATOM   6294 C  CB  . HIS D 1 197 ? 57.962 12.601  -3.500  1.00 26.59  ?  192 HIS C CB  1 
ATOM   6295 C  CG  . HIS D 1 197 ? 57.171 13.612  -2.751  1.00 31.53  ?  192 HIS C CG  1 
ATOM   6296 N  ND1 . HIS D 1 197 ? 56.892 14.870  -3.270  1.00 36.74  ?  192 HIS C ND1 1 
ATOM   6297 C  CD2 . HIS D 1 197 ? 56.542 13.534  -1.559  1.00 31.66  ?  192 HIS C CD2 1 
ATOM   6298 C  CE1 . HIS D 1 197 ? 56.172 15.543  -2.387  1.00 33.22  ?  192 HIS C CE1 1 
ATOM   6299 N  NE2 . HIS D 1 197 ? 55.946 14.742  -1.335  1.00 32.48  ?  192 HIS C NE2 1 
ATOM   6300 N  N   . SER D 1 198 ? 55.755 12.154  -5.793  1.00 25.04  ?  193 SER C N   1 
ATOM   6301 C  CA  . SER D 1 198 ? 54.498 12.547  -6.494  1.00 24.90  ?  193 SER C CA  1 
ATOM   6302 C  C   . SER D 1 198 ? 53.494 11.405  -6.488  1.00 22.10  ?  193 SER C C   1 
ATOM   6303 O  O   . SER D 1 198 ? 52.332 11.713  -6.431  1.00 28.06  ?  193 SER C O   1 
ATOM   6304 C  CB  . SER D 1 198 ? 54.717 13.024  -7.908  1.00 27.82  ?  193 SER C CB  1 
ATOM   6305 O  OG  . SER D 1 198 ? 54.996 11.918  -8.766  1.00 32.06  ?  193 SER C OG  1 
ATOM   6306 N  N   . PHE D 1 199 ? 53.920 10.156  -6.645  1.00 22.63  ?  194 PHE C N   1 
ATOM   6307 C  CA  . PHE D 1 199 ? 53.030 8.964   -6.775  1.00 22.20  ?  194 PHE C CA  1 
ATOM   6308 C  C   . PHE D 1 199 ? 52.512 8.544   -5.392  1.00 23.62  ?  194 PHE C C   1 
ATOM   6309 O  O   . PHE D 1 199 ? 51.472 7.868   -5.322  1.00 19.57  ?  194 PHE C O   1 
ATOM   6310 C  CB  . PHE D 1 199 ? 53.748 7.813   -7.479  1.00 20.00  ?  194 PHE C CB  1 
ATOM   6311 C  CG  . PHE D 1 199 ? 53.886 7.933   -8.992  1.00 18.43  ?  194 PHE C CG  1 
ATOM   6312 C  CD1 . PHE D 1 199 ? 53.101 8.799   -9.744  1.00 21.31  ?  194 PHE C CD1 1 
ATOM   6313 C  CD2 . PHE D 1 199 ? 54.759 7.110   -9.683  1.00 19.15  ?  194 PHE C CD2 1 
ATOM   6314 C  CE1 . PHE D 1 199 ? 53.234 8.887   -11.131 1.00 19.65  ?  194 PHE C CE1 1 
ATOM   6315 C  CE2 . PHE D 1 199 ? 54.888 7.195   -11.066 1.00 18.43  ?  194 PHE C CE2 1 
ATOM   6316 C  CZ  . PHE D 1 199 ? 54.118 8.077   -11.798 1.00 19.38  ?  194 PHE C CZ  1 
ATOM   6317 N  N   . GLY D 1 200 ? 53.211 8.955   -4.334  1.00 24.54  ?  195 GLY C N   1 
ATOM   6318 C  CA  . GLY D 1 200 ? 52.854 8.639   -2.928  1.00 29.41  ?  195 GLY C CA  1 
ATOM   6319 C  C   . GLY D 1 200 ? 51.578 9.318   -2.430  1.00 31.68  ?  195 GLY C C   1 
ATOM   6320 O  O   . GLY D 1 200 ? 51.034 8.859   -1.403  1.00 41.25  ?  195 GLY C O   1 
ATOM   6321 N  N   . GLY D 1 201 ? 51.075 10.339  -3.114  1.00 34.05  ?  196 GLY C N   1 
ATOM   6322 C  CA  . GLY D 1 201 ? 49.938 11.159  -2.636  1.00 38.94  ?  196 GLY C CA  1 
ATOM   6323 C  C   . GLY D 1 201 ? 48.621 10.898  -3.356  1.00 42.00  ?  196 GLY C C   1 
ATOM   6324 O  O   . GLY D 1 201 ? 47.800 11.843  -3.369  1.00 44.50  ?  196 GLY C O   1 
ATOM   6325 N  N   . ALA D 1 202 ? 48.387 9.696   -3.908  1.00 37.16  ?  197 ALA C N   1 
ATOM   6326 C  CA  . ALA D 1 202 ? 47.072 9.312   -4.490  1.00 38.50  ?  197 ALA C CA  1 
ATOM   6327 C  C   . ALA D 1 202 ? 46.934 7.791   -4.610  1.00 38.73  ?  197 ALA C C   1 
ATOM   6328 O  O   . ALA D 1 202 ? 47.927 7.102   -4.937  1.00 35.83  ?  197 ALA C O   1 
ATOM   6329 C  CB  . ALA D 1 202 ? 46.845 9.998   -5.817  1.00 40.40  ?  197 ALA C CB  1 
ATOM   6330 N  N   . GLU D 1 203 ? 45.731 7.280   -4.340  1.00 35.00  ?  198 GLU C N   1 
ATOM   6331 C  CA  . GLU D 1 203 ? 45.433 5.829   -4.356  1.00 36.04  ?  198 GLU C CA  1 
ATOM   6332 C  C   . GLU D 1 203 ? 45.873 5.228   -5.693  1.00 31.93  ?  198 GLU C C   1 
ATOM   6333 O  O   . GLU D 1 203 ? 46.500 4.172   -5.652  1.00 32.71  ?  198 GLU C O   1 
ATOM   6334 C  CB  . GLU D 1 203 ? 43.950 5.547   -4.104  1.00 39.09  ?  198 GLU C CB  1 
ATOM   6335 C  CG  . GLU D 1 203 ? 43.630 4.057   -4.064  1.00 42.72  ?  198 GLU C CG  1 
ATOM   6336 C  CD  . GLU D 1 203 ? 43.476 3.356   -5.412  1.00 46.40  ?  198 GLU C CD  1 
ATOM   6337 O  OE1 . GLU D 1 203 ? 43.368 4.070   -6.449  1.00 56.43  ?  198 GLU C OE1 1 
ATOM   6338 O  OE2 . GLU D 1 203 ? 43.475 2.092   -5.438  1.00 42.79  -1 198 GLU C OE2 1 
ATOM   6339 N  N   . ALA D 1 204 ? 45.562 5.887   -6.820  1.00 30.09  ?  199 ALA C N   1 
ATOM   6340 C  CA  . ALA D 1 204 ? 45.820 5.403   -8.198  1.00 28.93  ?  199 ALA C CA  1 
ATOM   6341 C  C   . ALA D 1 204 ? 47.302 5.066   -8.386  1.00 27.65  ?  199 ALA C C   1 
ATOM   6342 O  O   . ALA D 1 204 ? 47.585 4.164   -9.207  1.00 27.44  ?  199 ALA C O   1 
ATOM   6343 C  CB  . ALA D 1 204 ? 45.374 6.428   -9.218  1.00 30.67  ?  199 ALA C CB  1 
ATOM   6344 N  N   . THR D 1 205 ? 48.216 5.734   -7.669  1.00 24.27  ?  200 THR C N   1 
ATOM   6345 C  CA  . THR D 1 205 ? 49.686 5.658   -7.952  1.00 23.21  ?  200 THR C CA  1 
ATOM   6346 C  C   . THR D 1 205 ? 50.514 5.115   -6.776  1.00 21.83  ?  200 THR C C   1 
ATOM   6347 O  O   . THR D 1 205 ? 51.703 4.893   -6.972  1.00 18.31  ?  200 THR C O   1 
ATOM   6348 C  CB  . THR D 1 205 ? 50.211 7.030   -8.382  1.00 25.06  ?  200 THR C CB  1 
ATOM   6349 O  OG1 . THR D 1 205 ? 49.937 8.030   -7.393  1.00 24.33  ?  200 THR C OG1 1 
ATOM   6350 C  CG2 . THR D 1 205 ? 49.596 7.474   -9.692  1.00 27.79  ?  200 THR C CG2 1 
ATOM   6351 N  N   . ARG D 1 206 ? 49.943 4.885   -5.598  1.00 21.18  ?  201 ARG C N   1 
ATOM   6352 C  CA  . ARG D 1 206 ? 50.699 4.431   -4.401  1.00 23.24  ?  201 ARG C CA  1 
ATOM   6353 C  C   . ARG D 1 206 ? 51.359 3.072   -4.624  1.00 22.01  ?  201 ARG C C   1 
ATOM   6354 O  O   . ARG D 1 206 ? 52.458 2.887   -4.099  1.00 21.80  ?  201 ARG C O   1 
ATOM   6355 C  CB  . ARG D 1 206 ? 49.805 4.404   -3.156  1.00 25.61  ?  201 ARG C CB  1 
ATOM   6356 C  CG  . ARG D 1 206 ? 49.711 5.768   -2.495  1.00 29.00  ?  201 ARG C CG  1 
ATOM   6357 C  CD  . ARG D 1 206 ? 48.800 5.861   -1.277  1.00 33.40  ?  201 ARG C CD  1 
ATOM   6358 N  NE  . ARG D 1 206 ? 48.645 7.268   -0.933  1.00 34.13  ?  201 ARG C NE  1 
ATOM   6359 C  CZ  . ARG D 1 206 ? 47.491 7.927   -0.858  1.00 37.80  ?  201 ARG C CZ  1 
ATOM   6360 N  NH1 . ARG D 1 206 ? 46.338 7.313   -1.080  1.00 38.84  ?  201 ARG C NH1 1 
ATOM   6361 N  NH2 . ARG D 1 206 ? 47.500 9.207   -0.522  1.00 41.51  ?  201 ARG C NH2 1 
ATOM   6362 N  N   . ALA D 1 207 ? 50.741 2.160   -5.374  1.00 20.81  ?  202 ALA C N   1 
ATOM   6363 C  CA  . ALA D 1 207 ? 51.304 0.821   -5.676  1.00 19.94  ?  202 ALA C CA  1 
ATOM   6364 C  C   . ALA D 1 207 ? 52.598 0.953   -6.505  1.00 17.53  ?  202 ALA C C   1 
ATOM   6365 O  O   . ALA D 1 207 ? 53.600 0.295   -6.209  1.00 20.51  ?  202 ALA C O   1 
ATOM   6366 C  CB  . ALA D 1 207 ? 50.255 -0.014  -6.368  1.00 21.67  ?  202 ALA C CB  1 
ATOM   6367 N  N   . VAL D 1 208 ? 52.632 1.862   -7.458  1.00 18.28  ?  203 VAL C N   1 
ATOM   6368 C  CA  . VAL D 1 208 ? 53.900 2.166   -8.186  1.00 18.50  ?  203 VAL C CA  1 
ATOM   6369 C  C   . VAL D 1 208 ? 54.901 2.785   -7.202  1.00 17.76  ?  203 VAL C C   1 
ATOM   6370 O  O   . VAL D 1 208 ? 56.070 2.316   -7.163  1.00 19.05  ?  203 VAL C O   1 
ATOM   6371 C  CB  . VAL D 1 208 ? 53.622 3.093   -9.374  1.00 21.50  ?  203 VAL C CB  1 
ATOM   6372 C  CG1 . VAL D 1 208 ? 54.918 3.505   -10.054 1.00 20.65  ?  203 VAL C CG1 1 
ATOM   6373 C  CG2 . VAL D 1 208 ? 52.695 2.436   -10.355 1.00 23.67  ?  203 VAL C CG2 1 
ATOM   6374 N  N   . ALA D 1 209 ? 54.499 3.772   -6.400  1.00 17.07  ?  204 ALA C N   1 
ATOM   6375 C  CA  . ALA D 1 209 ? 55.384 4.360   -5.361  1.00 18.63  ?  204 ALA C CA  1 
ATOM   6376 C  C   . ALA D 1 209 ? 55.954 3.244   -4.472  1.00 21.51  ?  204 ALA C C   1 
ATOM   6377 O  O   . ALA D 1 209 ? 57.177 3.271   -4.222  1.00 22.40  ?  204 ALA C O   1 
ATOM   6378 C  CB  . ALA D 1 209 ? 54.684 5.433   -4.558  1.00 18.30  ?  204 ALA C CB  1 
ATOM   6379 N  N   . GLY D 1 210 ? 55.121 2.279   -4.048  1.00 22.37  ?  205 GLY C N   1 
ATOM   6380 C  CA  . GLY D 1 210 ? 55.532 1.136   -3.196  1.00 23.99  ?  205 GLY C CA  1 
ATOM   6381 C  C   . GLY D 1 210 ? 56.663 0.318   -3.822  1.00 23.05  ?  205 GLY C C   1 
ATOM   6382 O  O   . GLY D 1 210 ? 57.653 0.017   -3.121  1.00 24.25  ?  205 GLY C O   1 
ATOM   6383 N  N   . LEU D 1 211 ? 56.548 -0.021  -5.106  1.00 21.06  ?  206 LEU C N   1 
ATOM   6384 C  CA  . LEU D 1 211 ? 57.611 -0.743  -5.863  1.00 21.33  ?  206 LEU C CA  1 
ATOM   6385 C  C   . LEU D 1 211 ? 58.880 0.113   -6.020  1.00 19.86  ?  206 LEU C C   1 
ATOM   6386 O  O   . LEU D 1 211 ? 60.005 -0.412  -5.828  1.00 22.56  ?  206 LEU C O   1 
ATOM   6387 C  CB  . LEU D 1 211 ? 56.996 -1.141  -7.207  1.00 23.37  ?  206 LEU C CB  1 
ATOM   6388 C  CG  . LEU D 1 211 ? 55.943 -2.236  -7.108  1.00 25.78  ?  206 LEU C CG  1 
ATOM   6389 C  CD1 . LEU D 1 211 ? 55.096 -2.306  -8.375  1.00 25.09  ?  206 LEU C CD1 1 
ATOM   6390 C  CD2 . LEU D 1 211 ? 56.568 -3.580  -6.800  1.00 26.83  ?  206 LEU C CD2 1 
ATOM   6391 N  N   . MET D 1 212 ? 58.739 1.396   -6.358  1.00 20.46  ?  207 MET C N   1 
ATOM   6392 C  CA  . MET D 1 212 ? 59.890 2.318   -6.483  1.00 22.86  ?  207 MET C CA  1 
ATOM   6393 C  C   . MET D 1 212 ? 60.610 2.457   -5.129  1.00 26.89  ?  207 MET C C   1 
ATOM   6394 O  O   . MET D 1 212 ? 61.824 2.631   -5.169  1.00 24.39  ?  207 MET C O   1 
ATOM   6395 C  CB  . MET D 1 212 ? 59.450 3.701   -6.954  1.00 23.39  ?  207 MET C CB  1 
ATOM   6396 C  CG  . MET D 1 212 ? 58.961 3.722   -8.377  1.00 23.54  ?  207 MET C CG  1 
ATOM   6397 S  SD  . MET D 1 212 ? 58.462 5.365   -8.903  1.00 23.05  ?  207 MET C SD  1 
ATOM   6398 C  CE  . MET D 1 212 ? 60.108 6.082   -9.066  1.00 21.15  ?  207 MET C CE  1 
ATOM   6399 N  N   . ASP D 1 213 ? 59.888 2.435   -3.990  1.00 26.40  ?  208 ASP C N   1 
ATOM   6400 C  CA  . ASP D 1 213 ? 60.477 2.463   -2.618  1.00 28.90  ?  208 ASP C CA  1 
ATOM   6401 C  C   . ASP D 1 213 ? 61.363 1.228   -2.364  1.00 30.52  ?  208 ASP C C   1 
ATOM   6402 O  O   . ASP D 1 213 ? 62.248 1.312   -1.505  1.00 30.82  ?  208 ASP C O   1 
ATOM   6403 C  CB  . ASP D 1 213 ? 59.396 2.560   -1.535  1.00 30.86  ?  208 ASP C CB  1 
ATOM   6404 C  CG  . ASP D 1 213 ? 58.786 3.946   -1.372  1.00 38.66  ?  208 ASP C CG  1 
ATOM   6405 O  OD1 . ASP D 1 213 ? 59.481 4.916   -1.754  1.00 43.63  ?  208 ASP C OD1 1 
ATOM   6406 O  OD2 . ASP D 1 213 ? 57.590 4.055   -0.886  1.00 43.23  -1 208 ASP C OD2 1 
ATOM   6407 N  N   . ARG D 1 214 ? 61.188 0.132   -3.099  1.00 30.67  ?  209 ARG C N   1 
ATOM   6408 C  CA  . ARG D 1 214 ? 61.869 -1.159  -2.811  1.00 31.89  ?  209 ARG C CA  1 
ATOM   6409 C  C   . ARG D 1 214 ? 63.049 -1.412  -3.743  1.00 34.76  ?  209 ARG C C   1 
ATOM   6410 O  O   . ARG D 1 214 ? 63.708 -2.448  -3.547  1.00 33.11  ?  209 ARG C O   1 
ATOM   6411 C  CB  . ARG D 1 214 ? 60.893 -2.316  -2.945  1.00 31.93  ?  209 ARG C CB  1 
ATOM   6412 C  CG  . ARG D 1 214 ? 59.843 -2.328  -1.848  1.00 35.11  ?  209 ARG C CG  1 
ATOM   6413 C  CD  . ARG D 1 214 ? 58.852 -3.447  -2.089  1.00 36.38  ?  209 ARG C CD  1 
ATOM   6414 N  NE  . ARG D 1 214 ? 59.535 -4.735  -2.192  1.00 38.44  ?  209 ARG C NE  1 
ATOM   6415 C  CZ  . ARG D 1 214 ? 59.193 -5.726  -3.030  1.00 41.90  ?  209 ARG C CZ  1 
ATOM   6416 N  NH1 . ARG D 1 214 ? 58.186 -5.588  -3.880  1.00 40.53  ?  209 ARG C NH1 1 
ATOM   6417 N  NH2 . ARG D 1 214 ? 59.886 -6.853  -3.021  1.00 42.28  ?  209 ARG C NH2 1 
ATOM   6418 N  N   . LEU D 1 215 ? 63.319 -0.527  -4.702  1.00 32.66  ?  210 LEU C N   1 
ATOM   6419 C  CA  . LEU D 1 215 ? 64.499 -0.683  -5.580  1.00 36.53  ?  210 LEU C CA  1 
ATOM   6420 C  C   . LEU D 1 215 ? 65.731 -0.423  -4.722  1.00 43.74  ?  210 LEU C C   1 
ATOM   6421 O  O   . LEU D 1 215 ? 65.697 0.467   -3.880  1.00 53.67  ?  210 LEU C O   1 
ATOM   6422 C  CB  . LEU D 1 215 ? 64.400 0.292   -6.753  1.00 31.97  ?  210 LEU C CB  1 
ATOM   6423 C  CG  . LEU D 1 215 ? 63.297 -0.045  -7.753  1.00 29.85  ?  210 LEU C CG  1 
ATOM   6424 C  CD1 . LEU D 1 215 ? 63.127 1.091   -8.731  1.00 24.72  ?  210 LEU C CD1 1 
ATOM   6425 C  CD2 . LEU D 1 215 ? 63.583 -1.337  -8.496  1.00 30.37  ?  210 LEU C CD2 1 
ATOM   6426 N  N   . PRO D 1 216 ? 66.815 -1.224  -4.849  1.00 52.69  ?  211 PRO C N   1 
ATOM   6427 C  CA  . PRO D 1 216 ? 68.081 -0.929  -4.170  1.00 53.91  ?  211 PRO C CA  1 
ATOM   6428 C  C   . PRO D 1 216 ? 68.541 0.526   -4.340  1.00 51.55  ?  211 PRO C C   1 
ATOM   6429 O  O   . PRO D 1 216 ? 68.099 1.161   -5.301  1.00 49.71  ?  211 PRO C O   1 
ATOM   6430 C  CB  . PRO D 1 216 ? 69.049 -1.906  -4.858  1.00 55.31  ?  211 PRO C CB  1 
ATOM   6431 C  CG  . PRO D 1 216 ? 68.180 -3.106  -5.166  1.00 56.36  ?  211 PRO C CG  1 
ATOM   6432 C  CD  . PRO D 1 216 ? 66.856 -2.501  -5.583  1.00 52.76  ?  211 PRO C CD  1 
HETATM 6433 C  CHA . HEM E 2 .   ? 60.043 -9.993  26.215  1.00 16.43  ?  301 HEM B CHA 1 
HETATM 6434 C  CHB . HEM E 2 .   ? 56.067 -11.297 23.740  1.00 15.94  ?  301 HEM B CHB 1 
HETATM 6435 C  CHC . HEM E 2 .   ? 56.618 -15.968 25.101  1.00 16.09  ?  301 HEM B CHC 1 
HETATM 6436 C  CHD . HEM E 2 .   ? 60.901 -14.748 27.072  1.00 15.15  ?  301 HEM B CHD 1 
HETATM 6437 C  C1A . HEM E 2 .   ? 58.862 -9.968  25.505  1.00 14.27  ?  301 HEM B C1A 1 
HETATM 6438 C  C2A . HEM E 2 .   ? 58.380 -8.789  24.818  1.00 16.39  ?  301 HEM B C2A 1 
HETATM 6439 C  C3A . HEM E 2 .   ? 57.280 -9.135  24.106  1.00 15.75  ?  301 HEM B C3A 1 
HETATM 6440 C  C4A . HEM E 2 .   ? 57.084 -10.549 24.300  1.00 15.30  ?  301 HEM B C4A 1 
HETATM 6441 C  CMA . HEM E 2 .   ? 56.498 -8.142  23.256  1.00 15.42  ?  301 HEM B CMA 1 
HETATM 6442 C  CAA . HEM E 2 .   ? 58.950 -7.363  24.879  1.00 16.37  ?  301 HEM B CAA 1 
HETATM 6443 C  CBA . HEM E 2 .   ? 58.332 -6.574  26.025  1.00 15.75  ?  301 HEM B CBA 1 
HETATM 6444 C  CGA . HEM E 2 .   ? 59.089 -5.264  26.213  1.00 15.92  ?  301 HEM B CGA 1 
HETATM 6445 O  O1A . HEM E 2 .   ? 59.322 -4.491  25.197  1.00 15.92  ?  301 HEM B O1A 1 
HETATM 6446 O  O2A . HEM E 2 .   ? 59.453 -4.903  27.370  1.00 14.41  ?  301 HEM B O2A 1 
HETATM 6447 C  C1B . HEM E 2 .   ? 55.871 -12.680 23.916  1.00 16.43  ?  301 HEM B C1B 1 
HETATM 6448 C  C2B . HEM E 2 .   ? 54.817 -13.391 23.291  1.00 16.13  ?  301 HEM B C2B 1 
HETATM 6449 C  C3B . HEM E 2 .   ? 54.943 -14.711 23.668  1.00 15.87  ?  301 HEM B C3B 1 
HETATM 6450 C  C4B . HEM E 2 .   ? 56.145 -14.792 24.499  1.00 14.56  ?  301 HEM B C4B 1 
HETATM 6451 C  CMB . HEM E 2 .   ? 53.712 -12.841 22.398  1.00 16.26  ?  301 HEM B CMB 1 
HETATM 6452 C  CAB . HEM E 2 .   ? 53.949 -15.725 23.267  1.00 18.78  ?  301 HEM B CAB 1 
HETATM 6453 C  CBB . HEM E 2 .   ? 53.774 -16.899 23.812  1.00 18.47  ?  301 HEM B CBB 1 
HETATM 6454 C  C1C . HEM E 2 .   ? 57.798 -16.048 25.737  1.00 15.41  ?  301 HEM B C1C 1 
HETATM 6455 C  C2C . HEM E 2 .   ? 58.300 -17.218 26.323  1.00 15.51  ?  301 HEM B C2C 1 
HETATM 6456 C  C3C . HEM E 2 .   ? 59.578 -16.886 26.838  1.00 15.82  ?  301 HEM B C3C 1 
HETATM 6457 C  C4C . HEM E 2 .   ? 59.762 -15.455 26.684  1.00 15.21  ?  301 HEM B C4C 1 
HETATM 6458 C  CMC . HEM E 2 .   ? 57.642 -18.560 26.264  1.00 16.29  ?  301 HEM B CMC 1 
HETATM 6459 C  CAC . HEM E 2 .   ? 60.371 -17.833 27.604  1.00 16.82  ?  301 HEM B CAC 1 
HETATM 6460 C  CBC . HEM E 2 .   ? 61.253 -17.528 28.554  1.00 16.94  ?  301 HEM B CBC 1 
HETATM 6461 C  C1D . HEM E 2 .   ? 61.005 -13.365 26.946  1.00 15.58  ?  301 HEM B C1D 1 
HETATM 6462 C  C2D . HEM E 2 .   ? 62.213 -12.654 27.337  1.00 13.18  ?  301 HEM B C2D 1 
HETATM 6463 C  C3D . HEM E 2 .   ? 61.976 -11.374 27.130  1.00 15.42  ?  301 HEM B C3D 1 
HETATM 6464 C  C4D . HEM E 2 .   ? 60.594 -11.239 26.586  1.00 15.49  ?  301 HEM B C4D 1 
HETATM 6465 C  CMD . HEM E 2 .   ? 63.495 -13.203 27.980  1.00 16.60  ?  301 HEM B CMD 1 
HETATM 6466 C  CAD . HEM E 2 .   ? 62.940 -10.225 27.435  1.00 18.02  ?  301 HEM B CAD 1 
HETATM 6467 C  CBD . HEM E 2 .   ? 63.509 -9.614  26.113  1.00 21.87  ?  301 HEM B CBD 1 
HETATM 6468 C  CGD . HEM E 2 .   ? 63.947 -10.635 25.076  1.00 27.44  ?  301 HEM B CGD 1 
HETATM 6469 O  O1D . HEM E 2 .   ? 64.890 -11.411 25.396  1.00 23.97  ?  301 HEM B O1D 1 
HETATM 6470 O  O2D . HEM E 2 .   ? 63.362 -10.763 23.947  1.00 27.55  ?  301 HEM B O2D 1 
HETATM 6471 N  NA  . HEM E 2 .   ? 58.073 -11.044 25.130  1.00 16.00  ?  301 HEM B NA  1 
HETATM 6472 N  NB  . HEM E 2 .   ? 56.589 -13.552 24.681  1.00 14.17  ?  301 HEM B NB  1 
HETATM 6473 N  NC  . HEM E 2 .   ? 58.655 -14.981 25.988  1.00 14.43  ?  301 HEM B NC  1 
HETATM 6474 N  ND  . HEM E 2 .   ? 60.026 -12.494 26.468  1.00 14.53  ?  301 HEM B ND  1 
HETATM 6475 FE FE  . HEM E 2 .   ? 58.293 -12.955 25.720  1.00 16.27  ?  301 HEM B FE  1 
HETATM 6476 C  CHA . HEM F 2 .   ? 35.259 13.157  17.831  1.00 15.27  ?  301 HEM D CHA 1 
HETATM 6477 C  CHB . HEM F 2 .   ? 37.422 10.515  14.586  1.00 14.94  ?  301 HEM D CHB 1 
HETATM 6478 C  CHC . HEM F 2 .   ? 36.417 13.772  11.003  1.00 15.39  ?  301 HEM D CHC 1 
HETATM 6479 C  CHD . HEM F 2 .   ? 33.723 16.152  14.330  1.00 16.98  ?  301 HEM D CHD 1 
HETATM 6480 C  C1A . HEM F 2 .   ? 35.997 12.183  17.237  1.00 15.05  ?  301 HEM D C1A 1 
HETATM 6481 C  C2A . HEM F 2 .   ? 36.550 11.062  17.922  1.00 15.67  ?  301 HEM D C2A 1 
HETATM 6482 C  C3A . HEM F 2 .   ? 37.110 10.302  17.011  1.00 16.79  ?  301 HEM D C3A 1 
HETATM 6483 C  C4A . HEM F 2 .   ? 36.948 10.981  15.760  1.00 14.97  ?  301 HEM D C4A 1 
HETATM 6484 C  CMA . HEM F 2 .   ? 37.793 8.943   17.292  1.00 16.85  ?  301 HEM D CMA 1 
HETATM 6485 C  CAA . HEM F 2 .   ? 36.452 10.687  19.389  1.00 16.11  ?  301 HEM D CAA 1 
HETATM 6486 C  CBA . HEM F 2 .   ? 37.660 11.100  20.257  1.00 15.03  ?  301 HEM D CBA 1 
HETATM 6487 C  CGA . HEM F 2 .   ? 37.374 10.999  21.698  1.00 14.26  ?  301 HEM D CGA 1 
HETATM 6488 O  O1A . HEM F 2 .   ? 37.452 11.997  22.489  1.00 13.87  ?  301 HEM D O1A 1 
HETATM 6489 O  O2A . HEM F 2 .   ? 37.004 9.896   22.125  1.00 13.95  ?  301 HEM D O2A 1 
HETATM 6490 C  C1B . HEM F 2 .   ? 37.297 11.165  13.320  1.00 15.78  ?  301 HEM D C1B 1 
HETATM 6491 C  C2B . HEM F 2 .   ? 37.863 10.616  12.132  1.00 15.57  ?  301 HEM D C2B 1 
HETATM 6492 C  C3B . HEM F 2 .   ? 37.648 11.520  11.118  1.00 15.00  ?  301 HEM D C3B 1 
HETATM 6493 C  C4B . HEM F 2 .   ? 36.902 12.652  11.726  1.00 15.56  ?  301 HEM D C4B 1 
HETATM 6494 C  CMB . HEM F 2 .   ? 38.613 9.295   12.032  1.00 17.52  ?  301 HEM D CMB 1 
HETATM 6495 C  CAB . HEM F 2 .   ? 37.994 11.277  9.718   1.00 15.30  ?  301 HEM D CAB 1 
HETATM 6496 C  CBB . HEM F 2 .   ? 38.062 12.133  8.782   1.00 17.01  ?  301 HEM D CBB 1 
HETATM 6497 C  C1C . HEM F 2 .   ? 35.557 14.698  11.677  1.00 14.83  ?  301 HEM D C1C 1 
HETATM 6498 C  C2C . HEM F 2 .   ? 34.938 15.742  11.041  1.00 16.60  ?  301 HEM D C2C 1 
HETATM 6499 C  C3C . HEM F 2 .   ? 34.205 16.487  11.904  1.00 15.43  ?  301 HEM D C3C 1 
HETATM 6500 C  C4C . HEM F 2 .   ? 34.366 15.798  13.168  1.00 18.79  ?  301 HEM D C4C 1 
HETATM 6501 C  CMC . HEM F 2 .   ? 35.147 16.081  9.580   1.00 16.86  ?  301 HEM D CMC 1 
HETATM 6502 C  CAC . HEM F 2 .   ? 33.530 17.739  11.498  1.00 15.43  ?  301 HEM D CAC 1 
HETATM 6503 C  CBC . HEM F 2 .   ? 33.259 18.718  12.372  1.00 17.34  ?  301 HEM D CBC 1 
HETATM 6504 C  C1D . HEM F 2 .   ? 33.932 15.498  15.524  1.00 17.41  ?  301 HEM D C1D 1 
HETATM 6505 C  C2D . HEM F 2 .   ? 33.153 15.869  16.722  1.00 17.54  ?  301 HEM D C2D 1 
HETATM 6506 C  C3D . HEM F 2 .   ? 33.562 15.049  17.689  1.00 19.99  ?  301 HEM D C3D 1 
HETATM 6507 C  C4D . HEM F 2 .   ? 34.627 14.185  17.087  1.00 16.93  ?  301 HEM D C4D 1 
HETATM 6508 C  CMD . HEM F 2 .   ? 32.097 16.874  16.875  1.00 16.20  ?  301 HEM D CMD 1 
HETATM 6509 C  CAD . HEM F 2 .   ? 33.040 15.043  19.088  1.00 24.34  ?  301 HEM D CAD 1 
HETATM 6510 C  CBD . HEM F 2 .   ? 32.206 13.752  19.187  1.00 32.78  ?  301 HEM D CBD 1 
HETATM 6511 C  CGD . HEM F 2 .   ? 30.912 13.799  18.417  1.00 43.08  ?  301 HEM D CGD 1 
HETATM 6512 O  O1D . HEM F 2 .   ? 30.719 12.968  17.474  1.00 49.07  ?  301 HEM D O1D 1 
HETATM 6513 O  O2D . HEM F 2 .   ? 30.040 14.672  18.690  1.00 46.90  ?  301 HEM D O2D 1 
HETATM 6514 N  NA  . HEM F 2 .   ? 36.293 12.174  15.883  1.00 14.48  ?  301 HEM D NA  1 
HETATM 6515 N  NB  . HEM F 2 .   ? 36.792 12.372  13.054  1.00 14.02  ?  301 HEM D NB  1 
HETATM 6516 N  NC  . HEM F 2 .   ? 35.216 14.724  12.967  1.00 15.38  ?  301 HEM D NC  1 
HETATM 6517 N  ND  . HEM F 2 .   ? 34.824 14.510  15.781  1.00 17.08  ?  301 HEM D ND  1 
HETATM 6518 FE FE  . HEM F 2 .   ? 35.945 13.575  14.521  1.00 14.58  ?  301 HEM D FE  1 
HETATM 6519 C  CHA . HEM G 2 .   ? 60.020 4.018   -26.269 1.00 19.94  ?  301 HEM A CHA 1 
HETATM 6520 C  CHB . HEM G 2 .   ? 56.020 5.323   -23.857 1.00 17.15  ?  301 HEM A CHB 1 
HETATM 6521 C  CHC . HEM G 2 .   ? 56.529 9.885   -25.465 1.00 19.13  ?  301 HEM A CHC 1 
HETATM 6522 C  CHD . HEM G 2 .   ? 60.724 8.694   -27.473 1.00 20.07  ?  301 HEM A CHD 1 
HETATM 6523 C  C1A . HEM G 2 .   ? 58.844 4.014   -25.559 1.00 15.90  ?  301 HEM A C1A 1 
HETATM 6524 C  C2A . HEM G 2 .   ? 58.374 2.844   -24.857 1.00 17.22  ?  301 HEM A C2A 1 
HETATM 6525 C  C3A . HEM G 2 .   ? 57.264 3.173   -24.139 1.00 16.65  ?  301 HEM A C3A 1 
HETATM 6526 C  C4A . HEM G 2 .   ? 57.064 4.583   -24.387 1.00 16.86  ?  301 HEM A C4A 1 
HETATM 6527 C  CMA . HEM G 2 .   ? 56.423 2.150   -23.300 1.00 15.59  ?  301 HEM A CMA 1 
HETATM 6528 C  CAA . HEM G 2 .   ? 58.988 1.447   -24.911 1.00 17.35  ?  301 HEM A CAA 1 
HETATM 6529 C  CBA . HEM G 2 .   ? 58.405 0.673   -26.062 1.00 16.88  ?  301 HEM A CBA 1 
HETATM 6530 C  CGA . HEM G 2 .   ? 59.137 -0.652  -26.312 1.00 15.38  ?  301 HEM A CGA 1 
HETATM 6531 O  O1A . HEM G 2 .   ? 59.434 -1.037  -27.476 1.00 17.26  ?  301 HEM A O1A 1 
HETATM 6532 O  O2A . HEM G 2 .   ? 59.345 -1.449  -25.338 1.00 15.73  ?  301 HEM A O2A 1 
HETATM 6533 C  C1B . HEM G 2 .   ? 55.825 6.708   -24.074 1.00 18.68  ?  301 HEM A C1B 1 
HETATM 6534 C  C2B . HEM G 2 .   ? 54.726 7.405   -23.512 1.00 17.88  ?  301 HEM A C2B 1 
HETATM 6535 C  C3B . HEM G 2 .   ? 54.815 8.694   -23.948 1.00 18.59  ?  301 HEM A C3B 1 
HETATM 6536 C  C4B . HEM G 2 .   ? 56.044 8.778   -24.798 1.00 17.74  ?  301 HEM A C4B 1 
HETATM 6537 C  CMB . HEM G 2 .   ? 53.686 6.898   -22.519 1.00 18.77  ?  301 HEM A CMB 1 
HETATM 6538 C  CAB . HEM G 2 .   ? 53.828 9.711   -23.537 1.00 18.09  ?  301 HEM A CAB 1 
HETATM 6539 C  CBB . HEM G 2 .   ? 53.755 10.859  -24.135 1.00 17.65  ?  301 HEM A CBB 1 
HETATM 6540 C  C1C . HEM G 2 .   ? 57.707 10.007  -26.137 1.00 18.43  ?  301 HEM A C1C 1 
HETATM 6541 C  C2C . HEM G 2 .   ? 58.288 11.190  -26.707 1.00 19.18  ?  301 HEM A C2C 1 
HETATM 6542 C  C3C . HEM G 2 .   ? 59.489 10.854  -27.305 1.00 16.89  ?  301 HEM A C3C 1 
HETATM 6543 C  C4C . HEM G 2 .   ? 59.662 9.449   -27.080 1.00 18.95  ?  301 HEM A C4C 1 
HETATM 6544 C  CMC . HEM G 2 .   ? 57.723 12.565  -26.698 1.00 17.54  ?  301 HEM A CMC 1 
HETATM 6545 C  CAC . HEM G 2 .   ? 60.255 11.828  -28.088 1.00 21.96  ?  301 HEM A CAC 1 
HETATM 6546 C  CBC . HEM G 2 .   ? 61.065 11.479  -29.089 1.00 22.12  ?  301 HEM A CBC 1 
HETATM 6547 C  C1D . HEM G 2 .   ? 60.833 7.338   -27.263 1.00 19.87  ?  301 HEM A C1D 1 
HETATM 6548 C  C2D . HEM G 2 .   ? 62.085 6.642   -27.644 1.00 19.82  ?  301 HEM A C2D 1 
HETATM 6549 C  C3D . HEM G 2 .   ? 61.893 5.360   -27.309 1.00 22.70  ?  301 HEM A C3D 1 
HETATM 6550 C  C4D . HEM G 2 .   ? 60.528 5.251   -26.728 1.00 20.08  ?  301 HEM A C4D 1 
HETATM 6551 C  CMD . HEM G 2 .   ? 63.380 7.194   -28.276 1.00 20.49  ?  301 HEM A CMD 1 
HETATM 6552 C  CAD . HEM G 2 .   ? 62.919 4.258   -27.521 1.00 23.98  ?  301 HEM A CAD 1 
HETATM 6553 C  CBD . HEM G 2 .   ? 63.470 3.790   -26.160 1.00 27.59  ?  301 HEM A CBD 1 
HETATM 6554 C  CGD . HEM G 2 .   ? 63.965 4.894   -25.263 1.00 33.69  ?  301 HEM A CGD 1 
HETATM 6555 O  O1D . HEM G 2 .   ? 64.951 5.596   -25.674 1.00 31.18  ?  301 HEM A O1D 1 
HETATM 6556 O  O2D . HEM G 2 .   ? 63.395 5.062   -24.132 1.00 35.34  ?  301 HEM A O2D 1 
HETATM 6557 N  NA  . HEM G 2 .   ? 58.062 5.095   -25.231 1.00 16.63  ?  301 HEM A NA  1 
HETATM 6558 N  NB  . HEM G 2 .   ? 56.528 7.545   -24.878 1.00 18.73  ?  301 HEM A NB  1 
HETATM 6559 N  NC  . HEM G 2 .   ? 58.580 8.977   -26.371 1.00 19.00  ?  301 HEM A NC  1 
HETATM 6560 N  ND  . HEM G 2 .   ? 59.936 6.488   -26.716 1.00 18.73  ?  301 HEM A ND  1 
HETATM 6561 FE FE  . HEM G 2 .   ? 58.195 6.955   -26.019 1.00 17.61  ?  301 HEM A FE  1 
HETATM 6562 C  CHA . HEM H 2 .   ? 35.225 -19.162 -17.644 1.00 18.16  ?  301 HEM C CHA 1 
HETATM 6563 C  CHB . HEM H 2 .   ? 37.527 -16.477 -14.405 1.00 17.50  ?  301 HEM C CHB 1 
HETATM 6564 C  CHC . HEM H 2 .   ? 36.528 -19.639 -10.828 1.00 15.80  ?  301 HEM C CHC 1 
HETATM 6565 C  CHD . HEM H 2 .   ? 33.934 -22.160 -14.097 1.00 18.59  ?  301 HEM C CHD 1 
HETATM 6566 C  C1A . HEM H 2 .   ? 35.971 -18.153 -17.057 1.00 18.13  ?  301 HEM C C1A 1 
HETATM 6567 C  C2A . HEM H 2 .   ? 36.494 -16.988 -17.740 1.00 18.69  ?  301 HEM C C2A 1 
HETATM 6568 C  C3A . HEM H 2 .   ? 37.174 -16.269 -16.809 1.00 19.19  ?  301 HEM C C3A 1 
HETATM 6569 C  C4A . HEM H 2 .   ? 37.012 -16.925 -15.587 1.00 16.56  ?  301 HEM C C4A 1 
HETATM 6570 C  CMA . HEM H 2 .   ? 37.902 -14.936 -17.024 1.00 20.05  ?  301 HEM C CMA 1 
HETATM 6571 C  CAA . HEM H 2 .   ? 36.412 -16.602 -19.212 1.00 18.14  ?  301 HEM C CAA 1 
HETATM 6572 C  CBA . HEM H 2 .   ? 37.572 -17.162 -20.080 1.00 16.29  ?  301 HEM C CBA 1 
HETATM 6573 C  CGA . HEM H 2 .   ? 37.316 -17.058 -21.570 1.00 14.90  ?  301 HEM C CGA 1 
HETATM 6574 O  O1A . HEM H 2 .   ? 37.516 -17.991 -22.346 1.00 13.72  ?  301 HEM C O1A 1 
HETATM 6575 O  O2A . HEM H 2 .   ? 36.921 -15.985 -22.028 1.00 14.33  ?  301 HEM C O2A 1 
HETATM 6576 C  C1B . HEM H 2 .   ? 37.443 -17.133 -13.159 1.00 17.97  ?  301 HEM C C1B 1 
HETATM 6577 C  C2B . HEM H 2 .   ? 38.005 -16.572 -11.994 1.00 17.89  ?  301 HEM C C2B 1 
HETATM 6578 C  C3B . HEM H 2 .   ? 37.750 -17.377 -10.940 1.00 15.70  ?  301 HEM C C3B 1 
HETATM 6579 C  C4B . HEM H 2 .   ? 37.019 -18.535 -11.513 1.00 16.89  ?  301 HEM C C4B 1 
HETATM 6580 C  CMB . HEM H 2 .   ? 38.740 -15.236 -11.905 1.00 17.50  ?  301 HEM C CMB 1 
HETATM 6581 C  CAB . HEM H 2 .   ? 38.242 -17.023 -9.579  1.00 16.83  ?  301 HEM C CAB 1 
HETATM 6582 C  CBB . HEM H 2 .   ? 38.203 -17.859 -8.558  1.00 18.71  ?  301 HEM C CBB 1 
HETATM 6583 C  C1C . HEM H 2 .   ? 35.694 -20.611 -11.422 1.00 16.48  ?  301 HEM C C1C 1 
HETATM 6584 C  C2C . HEM H 2 .   ? 35.135 -21.723 -10.812 1.00 18.99  ?  301 HEM C C2C 1 
HETATM 6585 C  C3C . HEM H 2 .   ? 34.383 -22.466 -11.694 1.00 17.32  ?  301 HEM C C3C 1 
HETATM 6586 C  C4C . HEM H 2 .   ? 34.528 -21.785 -12.929 1.00 18.44  ?  301 HEM C C4C 1 
HETATM 6587 C  CMC . HEM H 2 .   ? 35.320 -22.064 -9.361  1.00 20.39  ?  301 HEM C CMC 1 
HETATM 6588 C  CAC . HEM H 2 .   ? 33.735 -23.749 -11.317 1.00 19.27  ?  301 HEM C CAC 1 
HETATM 6589 C  CBC . HEM H 2 .   ? 33.464 -24.762 -12.158 1.00 19.68  ?  301 HEM C CBC 1 
HETATM 6590 C  C1D . HEM H 2 .   ? 34.094 -21.501 -15.300 1.00 18.77  ?  301 HEM C C1D 1 
HETATM 6591 C  C2D . HEM H 2 .   ? 33.306 -21.946 -16.451 1.00 22.36  ?  301 HEM C C2D 1 
HETATM 6592 C  C3D . HEM H 2 .   ? 33.696 -21.129 -17.450 1.00 21.66  ?  301 HEM C C3D 1 
HETATM 6593 C  C4D . HEM H 2 .   ? 34.679 -20.184 -16.881 1.00 19.72  ?  301 HEM C C4D 1 
HETATM 6594 C  CMD . HEM H 2 .   ? 32.284 -23.087 -16.547 1.00 21.01  ?  301 HEM C CMD 1 
HETATM 6595 C  CAD . HEM H 2 .   ? 33.156 -21.173 -18.819 1.00 24.20  ?  301 HEM C CAD 1 
HETATM 6596 C  CBD . HEM H 2 .   ? 32.151 -20.034 -19.064 1.00 31.31  ?  301 HEM C CBD 1 
HETATM 6597 C  CGD . HEM H 2 .   ? 31.036 -19.788 -18.057 1.00 38.43  ?  301 HEM C CGD 1 
HETATM 6598 O  O1D . HEM H 2 .   ? 30.190 -20.677 -17.841 1.00 42.15  ?  301 HEM C O1D 1 
HETATM 6599 O  O2D . HEM H 2 .   ? 30.883 -18.666 -17.476 1.00 44.42  ?  301 HEM C O2D 1 
HETATM 6600 N  NA  . HEM H 2 .   ? 36.298 -18.107 -15.723 1.00 16.77  ?  301 HEM C NA  1 
HETATM 6601 N  NB  . HEM H 2 .   ? 36.905 -18.300 -12.843 1.00 16.95  ?  301 HEM C NB  1 
HETATM 6602 N  NC  . HEM H 2 .   ? 35.326 -20.669 -12.727 1.00 18.12  ?  301 HEM C NC  1 
HETATM 6603 N  ND  . HEM H 2 .   ? 34.927 -20.470 -15.577 1.00 18.52  ?  301 HEM C ND  1 
HETATM 6604 FE FE  . HEM H 2 .   ? 36.029 -19.528 -14.310 1.00 16.62  ?  301 HEM C FE  1 
HETATM 6605 O  O   . HOH I 3 .   ? 65.957 -11.322 27.107  1.00 35.78  ?  401 HOH B O   1 
HETATM 6606 O  O   . HOH I 3 .   ? 58.123 -1.019  26.093  1.00 15.73  ?  402 HOH B O   1 
HETATM 6607 O  O   . HOH I 3 .   ? 24.236 11.274  5.956   1.00 30.44  ?  403 HOH B O   1 
HETATM 6608 O  O   . HOH I 3 .   ? 36.528 3.793   34.782  1.00 33.31  ?  404 HOH B O   1 
HETATM 6609 O  O   . HOH I 3 .   ? 43.455 -21.939 31.774  1.00 33.00  ?  405 HOH B O   1 
HETATM 6610 O  O   . HOH I 3 .   ? 60.316 4.428   29.239  1.00 42.70  ?  406 HOH B O   1 
HETATM 6611 O  O   . HOH I 3 .   ? 37.491 -20.365 38.585  1.00 33.55  ?  407 HOH B O   1 
HETATM 6612 O  O   . HOH I 3 .   ? 55.490 3.003   40.524  1.00 45.29  ?  408 HOH B O   1 
HETATM 6613 O  O   . HOH I 3 .   ? 36.793 10.900  34.178  1.00 35.21  ?  409 HOH B O   1 
HETATM 6614 O  O   . HOH I 3 .   ? 47.216 -5.983  41.102  1.00 29.78  ?  410 HOH B O   1 
HETATM 6615 O  O   . HOH I 3 .   ? 55.178 -33.617 23.586  1.00 20.71  ?  411 HOH B O   1 
HETATM 6616 O  O   . HOH I 3 .   ? 41.794 -12.396 7.801   1.00 40.66  ?  412 HOH B O   1 
HETATM 6617 O  O   . HOH I 3 .   ? 30.465 -12.615 23.357  1.00 36.44  ?  413 HOH B O   1 
HETATM 6618 O  O   . HOH I 3 .   ? 64.529 -17.553 21.829  1.00 26.84  ?  414 HOH B O   1 
HETATM 6619 O  O   . HOH I 3 .   ? 55.699 4.527   35.451  1.00 28.95  ?  415 HOH B O   1 
HETATM 6620 O  O   . HOH I 3 .   ? 32.999 -2.271  31.948  1.00 30.91  ?  416 HOH B O   1 
HETATM 6621 O  O   . HOH I 3 .   ? 29.048 -12.626 13.424  1.00 35.50  ?  417 HOH B O   1 
HETATM 6622 O  O   . HOH I 3 .   ? 28.979 5.721   -2.800  1.00 31.42  ?  418 HOH B O   1 
HETATM 6623 O  O   . HOH I 3 .   ? 34.534 -10.131 14.394  1.00 21.52  ?  419 HOH B O   1 
HETATM 6624 O  O   . HOH I 3 .   ? 44.613 -14.583 24.164  1.00 21.97  ?  420 HOH B O   1 
HETATM 6625 O  O   . HOH I 3 .   ? 25.576 -12.542 8.706   1.00 50.38  ?  421 HOH B O   1 
HETATM 6626 O  O   . HOH I 3 .   ? 35.194 -22.204 32.360  1.00 55.61  ?  422 HOH B O   1 
HETATM 6627 O  O   . HOH I 3 .   ? 41.153 -18.842 32.762  1.00 27.14  ?  423 HOH B O   1 
HETATM 6628 O  O   . HOH I 3 .   ? 53.104 -19.140 39.597  1.00 18.99  ?  424 HOH B O   1 
HETATM 6629 O  O   . HOH I 3 .   ? 57.844 9.292   28.307  1.00 29.20  ?  425 HOH B O   1 
HETATM 6630 O  O   . HOH I 3 .   ? 58.513 1.328   25.692  1.00 27.71  ?  426 HOH B O   1 
HETATM 6631 O  O   . HOH I 3 .   ? 34.768 5.205   32.129  1.00 36.94  ?  427 HOH B O   1 
HETATM 6632 O  O   . HOH I 3 .   ? 30.725 4.637   14.555  1.00 16.53  ?  428 HOH B O   1 
HETATM 6633 O  O   . HOH I 3 .   ? 58.120 8.152   31.338  1.00 39.11  ?  429 HOH B O   1 
HETATM 6634 O  O   . HOH I 3 .   ? 50.275 -26.700 20.019  1.00 26.83  ?  430 HOH B O   1 
HETATM 6635 O  O   . HOH I 3 .   ? 64.135 -1.775  33.743  1.00 25.74  ?  431 HOH B O   1 
HETATM 6636 O  O   . HOH I 3 .   ? 65.662 -20.465 34.891  1.00 25.38  ?  432 HOH B O   1 
HETATM 6637 O  O   . HOH I 3 .   ? 64.559 -25.804 39.829  1.00 34.05  ?  433 HOH B O   1 
HETATM 6638 O  O   . HOH I 3 .   ? 29.498 4.931   11.349  1.00 20.14  ?  434 HOH B O   1 
HETATM 6639 O  O   . HOH I 3 .   ? 61.588 -4.859  24.004  1.00 41.58  ?  435 HOH B O   1 
HETATM 6640 O  O   . HOH I 3 .   ? 59.563 -11.716 36.780  1.00 18.57  ?  436 HOH B O   1 
HETATM 6641 O  O   . HOH I 3 .   ? 40.175 -2.938  8.733   1.00 31.57  ?  437 HOH B O   1 
HETATM 6642 O  O   . HOH I 3 .   ? 68.777 -18.509 22.942  1.00 38.19  ?  438 HOH B O   1 
HETATM 6643 O  O   . HOH I 3 .   ? 62.481 -6.148  39.695  1.00 34.49  ?  439 HOH B O   1 
HETATM 6644 O  O   . HOH I 3 .   ? 22.509 7.879   9.864   1.00 26.70  ?  440 HOH B O   1 
HETATM 6645 O  O   . HOH I 3 .   ? 44.519 -3.591  41.092  1.00 26.26  ?  441 HOH B O   1 
HETATM 6646 O  O   . HOH I 3 .   ? 66.623 -8.738  28.508  1.00 29.23  ?  442 HOH B O   1 
HETATM 6647 O  O   . HOH I 3 .   ? 31.376 -11.476 4.567   1.00 25.07  ?  443 HOH B O   1 
HETATM 6648 O  O   . HOH I 3 .   ? 59.953 -2.425  41.769  1.00 42.33  ?  444 HOH B O   1 
HETATM 6649 O  O   . HOH I 3 .   ? 24.321 1.108   21.171  1.00 35.19  ?  445 HOH B O   1 
HETATM 6650 O  O   . HOH I 3 .   ? 63.452 3.423   34.356  1.00 23.67  ?  446 HOH B O   1 
HETATM 6651 O  O   . HOH I 3 .   ? 43.818 -19.735 24.623  1.00 35.83  ?  447 HOH B O   1 
HETATM 6652 O  O   . HOH I 3 .   ? 26.607 -0.923  21.326  1.00 38.78  ?  448 HOH B O   1 
HETATM 6653 O  O   . HOH I 3 .   ? 33.564 -4.421  0.334   1.00 29.15  ?  449 HOH B O   1 
HETATM 6654 O  O   . HOH I 3 .   ? 42.353 -17.724 40.262  1.00 33.00  ?  450 HOH B O   1 
HETATM 6655 O  O   . HOH I 3 .   ? 37.521 8.046   24.729  1.00 22.01  ?  451 HOH B O   1 
HETATM 6656 O  O   . HOH I 3 .   ? 36.946 -2.580  41.458  1.00 37.26  ?  452 HOH B O   1 
HETATM 6657 O  O   . HOH I 3 .   ? 57.452 -4.445  23.329  1.00 17.78  ?  453 HOH B O   1 
HETATM 6658 O  O   . HOH I 3 .   ? 71.385 -20.435 29.129  1.00 25.42  ?  454 HOH B O   1 
HETATM 6659 O  O   . HOH I 3 .   ? 26.852 1.614   0.266   1.00 27.19  ?  455 HOH B O   1 
HETATM 6660 O  O   . HOH I 3 .   ? 41.674 -12.298 17.341  1.00 22.93  ?  456 HOH B O   1 
HETATM 6661 O  O   . HOH I 3 .   ? 45.847 -5.137  18.864  1.00 34.06  ?  457 HOH B O   1 
HETATM 6662 O  O   . HOH I 3 .   ? 34.834 -12.744 35.924  1.00 33.64  ?  458 HOH B O   1 
HETATM 6663 O  O   . HOH I 3 .   ? 38.886 -8.761  9.267   1.00 19.76  ?  459 HOH B O   1 
HETATM 6664 O  O   . HOH I 3 .   ? 35.316 -17.371 36.319  1.00 40.87  ?  460 HOH B O   1 
HETATM 6665 O  O   . HOH I 3 .   ? 47.410 2.028   27.141  1.00 21.52  ?  461 HOH B O   1 
HETATM 6666 O  O   . HOH I 3 .   ? 47.963 -15.851 14.114  1.00 25.33  ?  462 HOH B O   1 
HETATM 6667 O  O   . HOH I 3 .   ? 34.157 -6.735  -2.574  1.00 27.10  ?  463 HOH B O   1 
HETATM 6668 O  O   . HOH I 3 .   ? 29.923 9.352   10.489  1.00 14.03  ?  464 HOH B O   1 
HETATM 6669 O  O   . HOH I 3 .   ? 36.017 -14.668 26.229  1.00 29.90  ?  465 HOH B O   1 
HETATM 6670 O  O   . HOH I 3 .   ? 37.973 -13.720 21.479  1.00 30.63  ?  466 HOH B O   1 
HETATM 6671 O  O   . HOH I 3 .   ? 34.339 1.444   34.348  1.00 51.31  ?  467 HOH B O   1 
HETATM 6672 O  O   . HOH I 3 .   ? 52.697 -12.903 29.194  1.00 15.02  ?  468 HOH B O   1 
HETATM 6673 O  O   . HOH I 3 .   ? 63.200 -13.371 35.228  1.00 25.25  ?  469 HOH B O   1 
HETATM 6674 O  O   . HOH I 3 .   ? 26.813 -9.160  8.224   1.00 39.30  ?  470 HOH B O   1 
HETATM 6675 O  O   . HOH I 3 .   ? 44.732 -12.317 26.128  1.00 16.65  ?  471 HOH B O   1 
HETATM 6676 O  O   . HOH I 3 .   ? 31.633 -1.361  26.791  1.00 24.49  ?  472 HOH B O   1 
HETATM 6677 O  O   . HOH I 3 .   ? 32.222 9.429   34.422  1.00 50.02  ?  473 HOH B O   1 
HETATM 6678 O  O   . HOH I 3 .   ? 47.355 -20.816 29.838  1.00 24.21  ?  474 HOH B O   1 
HETATM 6679 O  O   . HOH I 3 .   ? 27.024 9.277   25.698  1.00 33.74  ?  475 HOH B O   1 
HETATM 6680 O  O   . HOH I 3 .   ? 52.733 -25.512 22.873  1.00 34.66  ?  476 HOH B O   1 
HETATM 6681 O  O   . HOH I 3 .   ? 60.309 2.172   27.940  1.00 30.25  ?  477 HOH B O   1 
HETATM 6682 O  O   . HOH I 3 .   ? 50.683 5.707   36.565  1.00 21.34  ?  478 HOH B O   1 
HETATM 6683 O  O   . HOH I 3 .   ? 66.787 -13.589 29.080  1.00 24.09  ?  479 HOH B O   1 
HETATM 6684 O  O   . HOH I 3 .   ? 28.698 -8.123  1.988   1.00 32.80  ?  480 HOH B O   1 
HETATM 6685 O  O   . HOH I 3 .   ? 39.451 1.432   32.492  1.00 19.50  ?  481 HOH B O   1 
HETATM 6686 O  O   . HOH I 3 .   ? 51.077 -16.961 39.578  1.00 32.67  ?  482 HOH B O   1 
HETATM 6687 O  O   . HOH I 3 .   ? 25.756 -0.857  13.901  1.00 33.79  ?  483 HOH B O   1 
HETATM 6688 O  O   . HOH I 3 .   ? 29.894 9.135   12.952  1.00 39.83  ?  484 HOH B O   1 
HETATM 6689 O  O   . HOH I 3 .   ? 27.473 9.748   0.786   1.00 24.68  ?  485 HOH B O   1 
HETATM 6690 O  O   . HOH I 3 .   ? 35.251 -15.811 28.800  1.00 30.34  ?  486 HOH B O   1 
HETATM 6691 O  O   . HOH I 3 .   ? 26.782 -1.189  1.354   1.00 21.46  ?  487 HOH B O   1 
HETATM 6692 O  O   . HOH I 3 .   ? 45.375 -10.466 17.932  1.00 21.42  ?  488 HOH B O   1 
HETATM 6693 O  O   . HOH I 3 .   ? 46.273 -1.508  22.237  1.00 19.23  ?  489 HOH B O   1 
HETATM 6694 O  O   . HOH I 3 .   ? 60.016 9.962   33.413  1.00 40.74  ?  490 HOH B O   1 
HETATM 6695 O  O   . HOH I 3 .   ? 41.271 7.007   29.318  1.00 24.16  ?  491 HOH B O   1 
HETATM 6696 O  O   . HOH I 3 .   ? 48.117 -24.144 17.498  1.00 24.36  ?  492 HOH B O   1 
HETATM 6697 O  O   . HOH I 3 .   ? 20.139 -0.753  4.154   1.00 28.97  ?  493 HOH B O   1 
HETATM 6698 O  O   . HOH I 3 .   ? 62.946 -6.727  24.237  1.00 38.34  ?  494 HOH B O   1 
HETATM 6699 O  O   . HOH I 3 .   ? 23.687 14.099  8.501   1.00 36.89  ?  495 HOH B O   1 
HETATM 6700 O  O   . HOH I 3 .   ? 41.734 -13.930 38.506  1.00 22.80  ?  496 HOH B O   1 
HETATM 6701 O  O   . HOH I 3 .   ? 59.616 -27.455 21.665  1.00 25.07  ?  497 HOH B O   1 
HETATM 6702 O  O   . HOH I 3 .   ? 41.731 8.227   33.145  1.00 27.95  ?  498 HOH B O   1 
HETATM 6703 O  O   . HOH I 3 .   ? 61.805 -0.607  40.285  1.00 45.43  ?  499 HOH B O   1 
HETATM 6704 O  O   . HOH I 3 .   ? 48.253 -1.616  19.978  1.00 28.93  ?  500 HOH B O   1 
HETATM 6705 O  O   . HOH I 3 .   ? 44.185 -17.497 29.729  1.00 24.27  ?  501 HOH B O   1 
HETATM 6706 O  O   . HOH I 3 .   ? 40.738 -1.036  17.408  1.00 12.86  ?  502 HOH B O   1 
HETATM 6707 O  O   . HOH I 3 .   ? 45.700 -20.460 14.566  1.00 36.02  ?  503 HOH B O   1 
HETATM 6708 O  O   . HOH I 3 .   ? 45.701 -5.389  21.799  1.00 14.50  ?  504 HOH B O   1 
HETATM 6709 O  O   . HOH I 3 .   ? 34.512 -8.327  21.469  1.00 22.59  ?  505 HOH B O   1 
HETATM 6710 O  O   . HOH I 3 .   ? 39.421 -22.682 40.585  1.00 46.88  ?  506 HOH B O   1 
HETATM 6711 O  O   . HOH I 3 .   ? 42.298 -5.964  8.965   1.00 32.86  ?  507 HOH B O   1 
HETATM 6712 O  O   . HOH I 3 .   ? 60.984 -9.969  22.715  1.00 21.45  ?  508 HOH B O   1 
HETATM 6713 O  O   . HOH I 3 .   ? 36.355 -9.247  -2.002  1.00 28.79  ?  509 HOH B O   1 
HETATM 6714 O  O   . HOH I 3 .   ? 58.299 -30.487 21.631  1.00 30.24  ?  510 HOH B O   1 
HETATM 6715 O  O   . HOH I 3 .   ? 57.765 -11.184 43.863  1.00 44.48  ?  511 HOH B O   1 
HETATM 6716 O  O   . HOH I 3 .   ? 35.020 -4.387  2.214   1.00 44.63  ?  512 HOH B O   1 
HETATM 6717 O  O   . HOH I 3 .   ? 35.001 -18.183 29.918  1.00 39.75  ?  513 HOH B O   1 
HETATM 6718 O  O   . HOH I 3 .   ? 57.888 13.613  27.860  1.00 29.01  ?  514 HOH B O   1 
HETATM 6719 O  O   . HOH I 3 .   ? 40.816 -7.066  2.407   1.00 24.33  ?  515 HOH B O   1 
HETATM 6720 O  O   . HOH I 3 .   ? 34.908 2.807   4.455   1.00 16.31  ?  516 HOH B O   1 
HETATM 6721 O  O   . HOH I 3 .   ? 46.219 -17.664 39.488  1.00 25.17  ?  517 HOH B O   1 
HETATM 6722 O  O   . HOH I 3 .   ? 39.288 -5.650  41.513  1.00 39.03  ?  518 HOH B O   1 
HETATM 6723 O  O   . HOH I 3 .   ? 56.920 -22.898 37.250  1.00 21.29  ?  519 HOH B O   1 
HETATM 6724 O  O   . HOH I 3 .   ? 55.191 -4.773  42.354  1.00 32.88  ?  520 HOH B O   1 
HETATM 6725 O  O   . HOH I 3 .   ? 32.152 1.098   31.477  1.00 43.87  ?  521 HOH B O   1 
HETATM 6726 O  O   . HOH I 3 .   ? 40.956 -20.830 40.550  1.00 41.95  ?  522 HOH B O   1 
HETATM 6727 O  O   . HOH I 3 .   ? 43.882 1.479   13.483  1.00 36.45  ?  523 HOH B O   1 
HETATM 6728 O  O   . HOH I 3 .   ? 28.742 -8.258  6.450   1.00 28.23  ?  524 HOH B O   1 
HETATM 6729 O  O   . HOH I 3 .   ? 64.108 -11.236 21.241  1.00 31.22  ?  525 HOH B O   1 
HETATM 6730 O  O   . HOH I 3 .   ? 64.706 -27.372 26.146  1.00 29.96  ?  526 HOH B O   1 
HETATM 6731 O  O   . HOH I 3 .   ? 27.701 13.101  1.567   1.00 26.59  ?  527 HOH B O   1 
HETATM 6732 O  O   . HOH I 3 .   ? 36.507 -3.065  2.957   1.00 22.81  ?  528 HOH B O   1 
HETATM 6733 O  O   . HOH I 3 .   ? 37.796 0.592   5.623   1.00 15.78  ?  529 HOH B O   1 
HETATM 6734 O  O   . HOH I 3 .   ? 67.047 -30.885 28.369  1.00 46.43  ?  530 HOH B O   1 
HETATM 6735 O  O   . HOH I 3 .   ? 42.484 -0.909  10.037  1.00 31.91  ?  531 HOH B O   1 
HETATM 6736 O  O   . HOH I 3 .   ? 66.725 -3.867  34.769  1.00 48.07  ?  532 HOH B O   1 
HETATM 6737 O  O   . HOH I 3 .   ? 26.236 -10.664 22.966  1.00 35.88  ?  533 HOH B O   1 
HETATM 6738 O  O   . HOH I 3 .   ? 40.363 -4.808  11.920  1.00 21.18  ?  534 HOH B O   1 
HETATM 6739 O  O   . HOH I 3 .   ? 61.349 -19.870 42.033  1.00 28.67  ?  535 HOH B O   1 
HETATM 6740 O  O   . HOH I 3 .   ? 43.893 -16.995 24.524  1.00 31.51  ?  536 HOH B O   1 
HETATM 6741 O  O   . HOH I 3 .   ? 70.155 -26.678 23.557  1.00 41.79  ?  537 HOH B O   1 
HETATM 6742 O  O   . HOH I 3 .   ? 46.465 -15.037 39.362  1.00 27.44  ?  538 HOH B O   1 
HETATM 6743 O  O   . HOH I 3 .   ? 32.650 -10.188 21.263  1.00 29.18  ?  539 HOH B O   1 
HETATM 6744 O  O   . HOH I 3 .   ? 36.841 9.593   30.956  1.00 26.24  ?  540 HOH B O   1 
HETATM 6745 O  O   . HOH I 3 .   ? 64.292 -14.281 39.568  1.00 35.27  ?  541 HOH B O   1 
HETATM 6746 O  O   . HOH I 3 .   ? 34.015 -7.215  31.143  1.00 26.03  ?  542 HOH B O   1 
HETATM 6747 O  O   . HOH I 3 .   ? 67.293 -28.851 26.464  1.00 43.95  ?  543 HOH B O   1 
HETATM 6748 O  O   . HOH I 3 .   ? 32.833 -5.072  31.933  1.00 29.78  ?  544 HOH B O   1 
HETATM 6749 O  O   . HOH I 3 .   ? 50.579 -19.099 13.430  1.00 23.13  ?  545 HOH B O   1 
HETATM 6750 O  O   . HOH I 3 .   ? 51.240 4.707   40.454  1.00 34.30  ?  546 HOH B O   1 
HETATM 6751 O  O   . HOH I 3 .   ? 20.961 11.999  1.857   1.00 39.69  ?  547 HOH B O   1 
HETATM 6752 O  O   . HOH I 3 .   ? 16.960 3.545   8.543   1.00 30.43  ?  548 HOH B O   1 
HETATM 6753 O  O   . HOH I 3 .   ? 55.950 -28.900 17.601  1.00 21.34  ?  549 HOH B O   1 
HETATM 6754 O  O   . HOH I 3 .   ? 58.757 7.146   35.575  1.00 38.37  ?  550 HOH B O   1 
HETATM 6755 O  O   . HOH I 3 .   ? 28.441 -10.972 29.749  1.00 28.02  ?  551 HOH B O   1 
HETATM 6756 O  O   . HOH I 3 .   ? 21.112 6.378   -0.748  1.00 51.49  ?  552 HOH B O   1 
HETATM 6757 O  O   . HOH I 3 .   ? 63.544 -21.812 35.788  1.00 37.53  ?  553 HOH B O   1 
HETATM 6758 O  O   . HOH I 3 .   ? 42.791 -16.617 26.982  1.00 28.50  ?  554 HOH B O   1 
HETATM 6759 O  O   . HOH I 3 .   ? 34.774 -0.819  35.612  1.00 20.30  ?  555 HOH B O   1 
HETATM 6760 O  O   . HOH I 3 .   ? 59.959 -25.682 32.013  1.00 24.51  ?  556 HOH B O   1 
HETATM 6761 O  O   . HOH I 3 .   ? 47.231 -8.736  19.909  1.00 18.98  ?  557 HOH B O   1 
HETATM 6762 O  O   . HOH I 3 .   ? 43.324 -14.163 27.672  1.00 20.60  ?  558 HOH B O   1 
HETATM 6763 O  O   . HOH I 3 .   ? 67.677 -6.360  32.136  1.00 38.68  ?  559 HOH B O   1 
HETATM 6764 O  O   . HOH I 3 .   ? 28.660 -12.352 10.873  1.00 44.99  ?  560 HOH B O   1 
HETATM 6765 O  O   . HOH I 3 .   ? 40.653 1.197   7.388   1.00 18.89  ?  561 HOH B O   1 
HETATM 6766 O  O   . HOH I 3 .   ? 57.708 -22.611 43.745  1.00 45.46  ?  562 HOH B O   1 
HETATM 6767 O  O   . HOH I 3 .   ? 28.040 11.216  9.313   1.00 23.31  ?  563 HOH B O   1 
HETATM 6768 O  O   . HOH I 3 .   ? 54.088 -34.710 21.519  1.00 42.69  ?  564 HOH B O   1 
HETATM 6769 O  O   . HOH I 3 .   ? 23.363 -3.747  10.720  1.00 29.64  ?  565 HOH B O   1 
HETATM 6770 O  O   . HOH I 3 .   ? 71.107 -27.523 27.541  1.00 37.93  ?  566 HOH B O   1 
HETATM 6771 O  O   . HOH I 3 .   ? 25.557 10.433  8.713   1.00 22.70  ?  567 HOH B O   1 
HETATM 6772 O  O   . HOH I 3 .   ? 38.047 -5.943  10.444  1.00 22.42  ?  568 HOH B O   1 
HETATM 6773 O  O   . HOH I 3 .   ? 67.949 -10.125 34.836  1.00 38.52  ?  569 HOH B O   1 
HETATM 6774 O  O   . HOH I 3 .   ? 56.955 -1.748  23.007  1.00 17.18  ?  570 HOH B O   1 
HETATM 6775 O  O   . HOH I 3 .   ? 25.130 -3.290  12.715  1.00 36.04  ?  571 HOH B O   1 
HETATM 6776 O  O   . HOH I 3 .   ? 57.470 -19.375 43.582  1.00 37.43  ?  572 HOH B O   1 
HETATM 6777 O  O   . HOH I 3 .   ? 32.529 0.818   28.939  1.00 41.57  ?  573 HOH B O   1 
HETATM 6778 O  O   . HOH I 3 .   ? 32.334 7.689   29.688  1.00 31.62  ?  574 HOH B O   1 
HETATM 6779 O  O   . HOH I 3 .   ? 46.082 -10.631 42.290  1.00 29.11  ?  575 HOH B O   1 
HETATM 6780 O  O   . HOH I 3 .   ? 21.785 -9.138  6.530   1.00 41.81  ?  576 HOH B O   1 
HETATM 6781 O  O   . HOH I 3 .   ? 38.349 -11.547 9.236   1.00 34.46  ?  577 HOH B O   1 
HETATM 6782 O  O   . HOH I 3 .   ? 66.469 -11.215 28.067  1.00 27.90  ?  578 HOH B O   1 
HETATM 6783 O  O   . HOH I 3 .   ? 21.671 -0.687  0.475   1.00 49.64  ?  579 HOH B O   1 
HETATM 6784 O  O   . HOH I 3 .   ? 62.724 -29.559 27.592  1.00 32.45  ?  580 HOH B O   1 
HETATM 6785 O  O   . HOH I 3 .   ? 48.557 -14.677 42.936  1.00 35.66  ?  581 HOH B O   1 
HETATM 6786 O  O   . HOH I 3 .   ? 44.871 2.143   37.607  1.00 35.49  ?  582 HOH B O   1 
HETATM 6787 O  O   . HOH I 3 .   ? 39.845 -19.775 26.118  1.00 41.37  ?  583 HOH B O   1 
HETATM 6788 O  O   . HOH I 3 .   ? 22.383 -7.880  12.340  1.00 39.34  ?  584 HOH B O   1 
HETATM 6789 O  O   . HOH I 3 .   ? 33.713 -6.047  34.225  1.00 22.00  ?  585 HOH B O   1 
HETATM 6790 O  O   . HOH I 3 .   ? 44.424 1.108   40.049  1.00 43.57  ?  586 HOH B O   1 
HETATM 6791 O  O   . HOH I 3 .   ? 27.526 -8.987  4.205   1.00 28.55  ?  587 HOH B O   1 
HETATM 6792 O  O   . HOH I 3 .   ? 61.643 13.565  33.412  1.00 30.83  ?  588 HOH B O   1 
HETATM 6793 O  O   . HOH I 3 .   ? 60.616 7.757   34.767  1.00 46.03  ?  589 HOH B O   1 
HETATM 6794 O  O   . HOH I 3 .   ? 68.877 -27.049 30.967  1.00 38.04  ?  590 HOH B O   1 
HETATM 6795 O  O   . HOH I 3 .   ? 33.260 -24.389 34.241  1.00 33.52  ?  591 HOH B O   1 
HETATM 6796 O  O   . HOH I 3 .   ? 62.156 5.689   30.727  1.00 43.04  ?  592 HOH B O   1 
HETATM 6797 O  O   . HOH I 3 .   ? 37.858 -18.965 26.261  1.00 46.43  ?  593 HOH B O   1 
HETATM 6798 O  O   . HOH I 3 .   ? 25.809 11.013  12.612  1.00 40.63  ?  594 HOH B O   1 
HETATM 6799 O  O   . HOH I 3 .   ? 39.024 10.877  34.067  1.00 27.84  ?  595 HOH B O   1 
HETATM 6800 O  O   . HOH I 3 .   ? 23.706 -1.048  16.050  1.00 33.69  ?  596 HOH B O   1 
HETATM 6801 O  O   . HOH I 3 .   ? 46.066 -7.066  17.980  1.00 49.31  ?  597 HOH B O   1 
HETATM 6802 O  O   . HOH I 3 .   ? 34.075 9.292   31.117  1.00 29.52  ?  598 HOH B O   1 
HETATM 6803 O  O   . HOH I 3 .   ? 37.858 -24.290 41.420  1.00 43.18  ?  599 HOH B O   1 
HETATM 6804 O  O   . HOH I 3 .   ? 39.661 -13.977 40.065  1.00 32.22  ?  600 HOH B O   1 
HETATM 6805 O  O   . HOH I 3 .   ? 63.482 3.907   36.926  1.00 39.26  ?  601 HOH B O   1 
HETATM 6806 O  O   . HOH I 3 .   ? 28.170 -12.033 24.854  1.00 36.81  ?  602 HOH B O   1 
HETATM 6807 O  O   . HOH I 3 .   ? 42.630 0.640   16.728  1.00 23.30  ?  603 HOH B O   1 
HETATM 6808 O  O   . HOH I 3 .   ? 32.653 -2.465  34.795  1.00 36.41  ?  604 HOH B O   1 
HETATM 6809 O  O   . HOH I 3 .   ? 61.389 12.914  38.245  1.00 50.55  ?  605 HOH B O   1 
HETATM 6810 O  O   . HOH I 3 .   ? 50.048 -3.843  17.748  1.00 28.44  ?  606 HOH B O   1 
HETATM 6811 O  O   . HOH I 3 .   ? 24.039 -2.049  0.723   1.00 35.31  ?  607 HOH B O   1 
HETATM 6812 O  O   . HOH I 3 .   ? 58.903 -33.049 22.116  1.00 35.23  ?  608 HOH B O   1 
HETATM 6813 O  O   . HOH I 3 .   ? 51.544 15.655  32.022  1.00 40.80  ?  609 HOH B O   1 
HETATM 6814 O  O   . HOH I 3 .   ? 65.366 -7.532  23.025  1.00 40.11  ?  610 HOH B O   1 
HETATM 6815 O  O   . HOH I 3 .   ? 63.544 -15.058 36.891  1.00 34.82  ?  611 HOH B O   1 
HETATM 6816 O  O   . HOH I 3 .   ? 59.644 -17.021 45.479  1.00 49.52  ?  612 HOH B O   1 
HETATM 6817 O  O   . HOH I 3 .   ? 64.279 -3.135  38.756  1.00 36.19  ?  613 HOH B O   1 
HETATM 6818 O  O   . HOH I 3 .   ? 41.011 -7.148  13.123  1.00 36.07  ?  614 HOH B O   1 
HETATM 6819 O  O   . HOH I 3 .   ? 68.950 -23.408 33.258  1.00 38.26  ?  615 HOH B O   1 
HETATM 6820 O  O   . HOH I 3 .   ? 59.404 -5.790  21.328  1.00 23.99  ?  616 HOH B O   1 
HETATM 6821 O  O   . HOH I 3 .   ? 40.731 -8.329  10.782  1.00 38.67  ?  617 HOH B O   1 
HETATM 6822 O  O   . HOH I 3 .   ? 36.306 -5.633  -3.471  1.00 32.90  ?  618 HOH B O   1 
HETATM 6823 O  O   . HOH I 3 .   ? 38.886 -20.640 28.774  1.00 30.60  ?  619 HOH B O   1 
HETATM 6824 O  O   . HOH I 3 .   ? 43.863 5.421   40.731  1.00 36.65  ?  620 HOH B O   1 
HETATM 6825 O  O   . HOH I 3 .   ? 36.627 -8.910  19.276  1.00 45.57  ?  621 HOH B O   1 
HETATM 6826 O  O   . HOH I 3 .   ? 26.741 -12.240 20.579  1.00 49.37  ?  622 HOH B O   1 
HETATM 6827 O  O   . HOH I 3 .   ? 46.809 -2.990  17.821  1.00 38.85  ?  623 HOH B O   1 
HETATM 6828 O  O   . HOH I 3 .   ? 54.761 18.910  34.857  1.00 33.69  ?  624 HOH B O   1 
HETATM 6829 O  O   . HOH I 3 .   ? 30.549 -10.409 6.863   1.00 34.85  ?  625 HOH B O   1 
HETATM 6830 O  O   . HOH I 3 .   ? 55.721 -27.738 15.275  1.00 30.98  ?  626 HOH B O   1 
HETATM 6831 O  O   . HOH I 3 .   ? 42.129 5.739   37.295  1.00 25.47  ?  627 HOH B O   1 
HETATM 6832 O  O   . HOH I 3 .   ? 42.818 -10.706 14.776  1.00 40.77  ?  628 HOH B O   1 
HETATM 6833 O  O   . HOH I 3 .   ? 30.347 7.735   33.847  1.00 43.52  ?  629 HOH B O   1 
HETATM 6834 O  O   . HOH I 3 .   ? 60.919 6.577   37.001  1.00 39.10  ?  630 HOH B O   1 
HETATM 6835 O  O   . HOH I 3 .   ? 62.718 -30.608 20.001  1.00 32.48  ?  631 HOH B O   1 
HETATM 6836 O  O   . HOH I 3 .   ? 24.170 6.222   -5.169  1.00 35.78  ?  632 HOH B O   1 
HETATM 6837 O  O   . HOH I 3 .   ? 29.425 6.064   31.871  1.00 45.65  ?  633 HOH B O   1 
HETATM 6838 O  O   . HOH I 3 .   ? 39.795 -1.104  6.418   1.00 28.81  ?  634 HOH B O   1 
HETATM 6839 O  O   . HOH I 3 .   ? 64.305 -32.993 33.561  1.00 45.90  ?  635 HOH B O   1 
HETATM 6840 O  O   . HOH I 3 .   ? 63.437 5.801   32.714  1.00 37.41  ?  636 HOH B O   1 
HETATM 6841 O  O   . HOH I 3 .   ? 45.420 -5.284  43.513  1.00 42.53  ?  637 HOH B O   1 
HETATM 6842 O  O   . HOH I 3 .   ? 33.030 -2.168  39.435  1.00 46.89  ?  638 HOH B O   1 
HETATM 6843 O  O   . HOH I 3 .   ? 39.284 -3.117  2.403   1.00 31.02  ?  639 HOH B O   1 
HETATM 6844 O  O   . HOH I 3 .   ? 64.398 -34.332 31.389  1.00 41.52  ?  640 HOH B O   1 
HETATM 6845 O  O   . HOH I 3 .   ? 44.812 -20.143 29.567  1.00 24.12  ?  641 HOH B O   1 
HETATM 6846 O  O   . HOH I 3 .   ? 72.215 -28.141 24.420  1.00 43.29  ?  642 HOH B O   1 
HETATM 6847 O  O   . HOH I 3 .   ? 40.684 -4.672  1.262   1.00 31.12  ?  643 HOH B O   1 
HETATM 6848 O  O   . HOH I 3 .   ? 46.173 -11.900 15.554  1.00 23.26  ?  644 HOH B O   1 
HETATM 6849 O  O   . HOH I 3 .   ? 38.535 10.447  37.638  1.00 47.94  ?  645 HOH B O   1 
HETATM 6850 O  O   . HOH I 3 .   ? 35.574 -14.775 37.250  1.00 41.81  ?  646 HOH B O   1 
HETATM 6851 O  O   . HOH I 3 .   ? 62.051 -18.129 45.101  1.00 33.65  ?  647 HOH B O   1 
HETATM 6852 O  O   . HOH I 3 .   ? 62.472 10.397  31.977  1.00 31.17  ?  648 HOH B O   1 
HETATM 6853 O  O   . HOH I 3 .   ? 52.309 18.516  34.699  1.00 34.77  ?  649 HOH B O   1 
HETATM 6854 O  O   . HOH I 3 .   ? 40.900 -1.948  4.324   1.00 26.96  ?  650 HOH B O   1 
HETATM 6855 O  O   . HOH I 3 .   ? 71.100 -30.938 26.428  1.00 36.28  ?  651 HOH B O   1 
HETATM 6856 O  O   . HOH I 3 .   ? 24.726 8.541   -5.748  1.00 34.27  ?  652 HOH B O   1 
HETATM 6857 O  O   . HOH I 3 .   ? 62.377 -15.473 48.724  1.00 51.40  ?  653 HOH B O   1 
HETATM 6858 O  O   . HOH J 3 .   ? 60.691 19.191  18.004  1.00 31.98  ?  401 HOH D O   1 
HETATM 6859 O  O   . HOH J 3 .   ? 35.286 21.829  -1.526  1.00 35.47  ?  402 HOH D O   1 
HETATM 6860 O  O   . HOH J 3 .   ? 36.074 25.409  14.161  1.00 13.30  ?  403 HOH D O   1 
HETATM 6861 O  O   . HOH J 3 .   ? 65.785 3.112   12.961  1.00 41.01  ?  404 HOH D O   1 
HETATM 6862 O  O   . HOH J 3 .   ? 64.869 -22.015 16.996  1.00 37.35  ?  405 HOH D O   1 
HETATM 6863 O  O   . HOH J 3 .   ? 47.825 -9.959  11.976  1.00 27.54  ?  406 HOH D O   1 
HETATM 6864 O  O   . HOH J 3 .   ? 40.464 3.381   23.443  1.00 25.84  ?  407 HOH D O   1 
HETATM 6865 O  O   . HOH J 3 .   ? 63.782 8.240   15.872  1.00 34.34  ?  408 HOH D O   1 
HETATM 6866 O  O   . HOH J 3 .   ? 64.400 17.761  9.065   1.00 46.15  ?  409 HOH D O   1 
HETATM 6867 O  O   . HOH J 3 .   ? 67.995 -4.725  12.707  1.00 36.97  ?  410 HOH D O   1 
HETATM 6868 O  O   . HOH J 3 .   ? 51.117 6.679   39.664  1.00 51.50  ?  411 HOH D O   1 
HETATM 6869 O  O   . HOH J 3 .   ? 31.962 14.675  29.651  1.00 34.86  ?  412 HOH D O   1 
HETATM 6870 O  O   . HOH J 3 .   ? 57.003 -8.030  -0.693  1.00 32.70  ?  413 HOH D O   1 
HETATM 6871 O  O   . HOH J 3 .   ? 59.332 7.003   28.373  1.00 34.26  ?  414 HOH D O   1 
HETATM 6872 O  O   . HOH J 3 .   ? 56.957 16.873  26.164  1.00 36.03  ?  415 HOH D O   1 
HETATM 6873 O  O   . HOH J 3 .   ? 30.043 26.399  5.852   1.00 34.79  ?  416 HOH D O   1 
HETATM 6874 O  O   . HOH J 3 .   ? 32.594 8.143   -3.937  1.00 21.14  ?  417 HOH D O   1 
HETATM 6875 O  O   . HOH J 3 .   ? 53.108 21.256  20.189  1.00 38.18  ?  418 HOH D O   1 
HETATM 6876 O  O   . HOH J 3 .   ? 51.395 13.993  30.626  1.00 26.55  ?  419 HOH D O   1 
HETATM 6877 O  O   . HOH J 3 .   ? 28.642 13.091  11.506  1.00 45.42  ?  420 HOH D O   1 
HETATM 6878 O  O   . HOH J 3 .   ? 33.596 12.054  -5.499  1.00 34.06  ?  421 HOH D O   1 
HETATM 6879 O  O   . HOH J 3 .   ? 29.451 18.768  18.040  1.00 24.46  ?  422 HOH D O   1 
HETATM 6880 O  O   . HOH J 3 .   ? 47.951 -8.031  6.370   1.00 26.84  ?  423 HOH D O   1 
HETATM 6881 O  O   . HOH J 3 .   ? 30.179 16.810  20.004  1.00 34.88  ?  424 HOH D O   1 
HETATM 6882 O  O   . HOH J 3 .   ? 61.131 -16.409 18.862  1.00 20.14  ?  425 HOH D O   1 
HETATM 6883 O  O   . HOH J 3 .   ? 30.314 11.892  15.227  1.00 40.81  ?  426 HOH D O   1 
HETATM 6884 O  O   . HOH J 3 .   ? 57.790 11.193  -0.334  1.00 42.09  ?  427 HOH D O   1 
HETATM 6885 O  O   . HOH J 3 .   ? 48.223 20.385  26.716  1.00 27.77  ?  428 HOH D O   1 
HETATM 6886 O  O   . HOH J 3 .   ? 45.602 26.769  23.630  1.00 28.00  ?  429 HOH D O   1 
HETATM 6887 O  O   . HOH J 3 .   ? 41.267 13.291  -0.180  1.00 27.73  ?  430 HOH D O   1 
HETATM 6888 O  O   . HOH J 3 .   ? 56.784 19.544  21.608  1.00 27.19  ?  431 HOH D O   1 
HETATM 6889 O  O   . HOH J 3 .   ? 48.707 15.286  6.129   1.00 31.75  ?  432 HOH D O   1 
HETATM 6890 O  O   . HOH J 3 .   ? 57.957 -11.487 -1.889  1.00 42.74  ?  433 HOH D O   1 
HETATM 6891 O  O   . HOH J 3 .   ? 58.340 -23.256 8.005   1.00 25.80  ?  434 HOH D O   1 
HETATM 6892 O  O   . HOH J 3 .   ? 42.202 22.065  31.974  1.00 43.60  ?  435 HOH D O   1 
HETATM 6893 O  O   . HOH J 3 .   ? 46.505 27.751  13.958  1.00 38.59  ?  436 HOH D O   1 
HETATM 6894 O  O   . HOH J 3 .   ? 55.299 0.205   21.320  1.00 24.99  ?  437 HOH D O   1 
HETATM 6895 O  O   . HOH J 3 .   ? 65.518 -3.425  11.466  1.00 31.10  ?  438 HOH D O   1 
HETATM 6896 O  O   . HOH J 3 .   ? 37.496 27.288  21.218  1.00 20.88  ?  439 HOH D O   1 
HETATM 6897 O  O   . HOH J 3 .   ? 60.138 -25.506 15.159  1.00 28.68  ?  440 HOH D O   1 
HETATM 6898 O  O   . HOH J 3 .   ? 59.786 3.644   3.179   1.00 34.09  ?  441 HOH D O   1 
HETATM 6899 O  O   . HOH J 3 .   ? 26.562 25.506  9.419   1.00 31.52  ?  442 HOH D O   1 
HETATM 6900 O  O   . HOH J 3 .   ? 42.245 15.035  13.398  1.00 11.27  ?  443 HOH D O   1 
HETATM 6901 O  O   . HOH J 3 .   ? 46.738 14.621  31.371  1.00 23.67  ?  444 HOH D O   1 
HETATM 6902 O  O   . HOH J 3 .   ? 64.433 16.196  12.907  1.00 37.38  ?  445 HOH D O   1 
HETATM 6903 O  O   . HOH J 3 .   ? 46.956 9.243   7.308   1.00 22.85  ?  446 HOH D O   1 
HETATM 6904 O  O   . HOH J 3 .   ? 47.512 1.490   6.059   1.00 30.13  ?  447 HOH D O   1 
HETATM 6905 O  O   . HOH J 3 .   ? 37.680 12.375  -2.080  1.00 34.16  ?  448 HOH D O   1 
HETATM 6906 O  O   . HOH J 3 .   ? 35.574 23.479  18.524  1.00 18.64  ?  449 HOH D O   1 
HETATM 6907 O  O   . HOH J 3 .   ? 48.351 3.331   24.865  1.00 16.00  ?  450 HOH D O   1 
HETATM 6908 O  O   . HOH J 3 .   ? 57.559 -5.364  0.419   1.00 33.95  ?  451 HOH D O   1 
HETATM 6909 O  O   . HOH J 3 .   ? 43.482 26.937  25.295  1.00 22.90  ?  452 HOH D O   1 
HETATM 6910 O  O   . HOH J 3 .   ? 57.211 22.901  23.616  1.00 39.56  ?  453 HOH D O   1 
HETATM 6911 O  O   . HOH J 3 .   ? 49.557 11.892  8.361   1.00 20.53  ?  454 HOH D O   1 
HETATM 6912 O  O   . HOH J 3 .   ? 40.686 3.110   -0.150  1.00 21.52  ?  455 HOH D O   1 
HETATM 6913 O  O   . HOH J 3 .   ? 50.169 11.929  39.195  1.00 27.93  ?  456 HOH D O   1 
HETATM 6914 O  O   . HOH J 3 .   ? 66.972 7.505   8.077   1.00 30.49  ?  457 HOH D O   1 
HETATM 6915 O  O   . HOH J 3 .   ? 46.258 0.887   14.335  1.00 28.27  ?  458 HOH D O   1 
HETATM 6916 O  O   . HOH J 3 .   ? 60.747 -13.934 15.345  1.00 20.67  ?  459 HOH D O   1 
HETATM 6917 O  O   . HOH J 3 .   ? 51.937 4.466   4.692   1.00 28.69  ?  460 HOH D O   1 
HETATM 6918 O  O   . HOH J 3 .   ? 47.085 24.137  25.353  1.00 20.70  ?  461 HOH D O   1 
HETATM 6919 O  O   . HOH J 3 .   ? 63.071 2.723   14.466  1.00 30.27  ?  462 HOH D O   1 
HETATM 6920 O  O   . HOH J 3 .   ? 47.467 3.649   15.000  1.00 18.86  ?  463 HOH D O   1 
HETATM 6921 O  O   . HOH J 3 .   ? 53.284 -3.828  4.554   1.00 23.55  ?  464 HOH D O   1 
HETATM 6922 O  O   . HOH J 3 .   ? 45.309 16.775  4.515   1.00 28.27  ?  465 HOH D O   1 
HETATM 6923 O  O   . HOH J 3 .   ? 61.917 15.192  6.473   1.00 33.36  ?  466 HOH D O   1 
HETATM 6924 O  O   . HOH J 3 .   ? 49.683 -8.363  8.780   1.00 37.98  ?  467 HOH D O   1 
HETATM 6925 O  O   . HOH J 3 .   ? 50.191 -15.178 12.798  1.00 18.53  ?  468 HOH D O   1 
HETATM 6926 O  O   . HOH J 3 .   ? 39.705 7.974   -1.908  1.00 24.26  ?  469 HOH D O   1 
HETATM 6927 O  O   . HOH J 3 .   ? 39.325 15.573  33.446  1.00 21.80  ?  470 HOH D O   1 
HETATM 6928 O  O   . HOH J 3 .   ? 47.131 -9.271  14.343  1.00 29.41  ?  471 HOH D O   1 
HETATM 6929 O  O   . HOH J 3 .   ? 29.682 16.201  1.175   1.00 26.74  ?  472 HOH D O   1 
HETATM 6930 O  O   . HOH J 3 .   ? 43.186 6.945   34.474  1.00 23.63  ?  473 HOH D O   1 
HETATM 6931 O  O   . HOH J 3 .   ? 63.366 -10.196 9.223   1.00 29.62  ?  474 HOH D O   1 
HETATM 6932 O  O   . HOH J 3 .   ? 32.737 12.847  15.218  1.00 35.41  ?  475 HOH D O   1 
HETATM 6933 O  O   . HOH J 3 .   ? 49.844 5.895   23.866  1.00 19.99  ?  476 HOH D O   1 
HETATM 6934 O  O   . HOH J 3 .   ? 60.692 -10.669 16.278  1.00 19.61  ?  477 HOH D O   1 
HETATM 6935 O  O   . HOH J 3 .   ? 39.498 23.064  18.877  1.00 15.61  ?  478 HOH D O   1 
HETATM 6936 O  O   . HOH J 3 .   ? 57.681 -21.225 6.099   1.00 24.28  ?  479 HOH D O   1 
HETATM 6937 O  O   . HOH J 3 .   ? 55.268 20.976  10.752  1.00 23.87  ?  480 HOH D O   1 
HETATM 6938 O  O   . HOH J 3 .   ? 39.442 27.475  8.387   1.00 33.55  ?  481 HOH D O   1 
HETATM 6939 O  O   . HOH J 3 .   ? 46.609 10.754  2.466   1.00 35.78  ?  482 HOH D O   1 
HETATM 6940 O  O   . HOH J 3 .   ? 29.797 13.978  22.991  1.00 34.26  ?  483 HOH D O   1 
HETATM 6941 O  O   . HOH J 3 .   ? 33.819 12.361  12.842  1.00 36.75  ?  484 HOH D O   1 
HETATM 6942 O  O   . HOH J 3 .   ? 38.924 9.918   29.000  1.00 24.30  ?  485 HOH D O   1 
HETATM 6943 O  O   . HOH J 3 .   ? 38.058 7.722   20.774  1.00 19.17  ?  486 HOH D O   1 
HETATM 6944 O  O   . HOH J 3 .   ? 48.230 9.993   9.784   1.00 17.47  ?  487 HOH D O   1 
HETATM 6945 O  O   . HOH J 3 .   ? 51.551 -3.328  15.687  1.00 17.20  ?  488 HOH D O   1 
HETATM 6946 O  O   . HOH J 3 .   ? 31.357 12.418  -3.011  1.00 26.74  ?  489 HOH D O   1 
HETATM 6947 O  O   . HOH J 3 .   ? 64.813 -19.370 17.585  1.00 24.69  ?  490 HOH D O   1 
HETATM 6948 O  O   . HOH J 3 .   ? 48.108 2.670   18.722  1.00 18.74  ?  491 HOH D O   1 
HETATM 6949 O  O   . HOH J 3 .   ? 41.580 33.433  10.554  1.00 39.16  ?  492 HOH D O   1 
HETATM 6950 O  O   . HOH J 3 .   ? 36.337 27.145  18.531  1.00 28.09  ?  493 HOH D O   1 
HETATM 6951 O  O   . HOH J 3 .   ? 39.750 24.535  26.202  1.00 29.70  ?  494 HOH D O   1 
HETATM 6952 O  O   . HOH J 3 .   ? 44.308 11.276  -3.407  1.00 44.69  ?  495 HOH D O   1 
HETATM 6953 O  O   . HOH J 3 .   ? 35.939 20.884  27.628  1.00 22.77  ?  496 HOH D O   1 
HETATM 6954 O  O   . HOH J 3 .   ? 36.518 15.345  0.612   1.00 32.38  ?  497 HOH D O   1 
HETATM 6955 O  O   . HOH J 3 .   ? 39.959 1.439   4.195   1.00 20.49  ?  498 HOH D O   1 
HETATM 6956 O  O   . HOH J 3 .   ? 39.986 10.946  31.073  1.00 36.71  ?  499 HOH D O   1 
HETATM 6957 O  O   . HOH J 3 .   ? 67.438 -18.108 14.471  1.00 32.69  ?  500 HOH D O   1 
HETATM 6958 O  O   . HOH J 3 .   ? 36.597 17.852  -1.439  1.00 33.83  ?  501 HOH D O   1 
HETATM 6959 O  O   . HOH J 3 .   ? 63.648 11.124  18.824  1.00 20.94  ?  502 HOH D O   1 
HETATM 6960 O  O   . HOH J 3 .   ? 39.248 2.734   5.472   1.00 48.56  ?  503 HOH D O   1 
HETATM 6961 O  O   . HOH J 3 .   ? 59.019 8.621   21.773  1.00 20.23  ?  504 HOH D O   1 
HETATM 6962 O  O   . HOH J 3 .   ? 52.720 -17.746 13.150  1.00 14.83  ?  505 HOH D O   1 
HETATM 6963 O  O   . HOH J 3 .   ? 36.991 17.500  29.227  1.00 22.87  ?  506 HOH D O   1 
HETATM 6964 O  O   . HOH J 3 .   ? 44.937 2.025   9.206   1.00 24.62  ?  507 HOH D O   1 
HETATM 6965 O  O   . HOH J 3 .   ? 32.856 11.284  21.108  1.00 20.35  ?  508 HOH D O   1 
HETATM 6966 O  O   . HOH J 3 .   ? 30.998 17.389  22.457  1.00 25.59  ?  509 HOH D O   1 
HETATM 6967 O  O   . HOH J 3 .   ? 45.487 0.305   11.401  1.00 30.32  ?  510 HOH D O   1 
HETATM 6968 O  O   . HOH J 3 .   ? 24.711 20.922  1.363   1.00 39.98  ?  511 HOH D O   1 
HETATM 6969 O  O   . HOH J 3 .   ? 45.476 16.554  34.783  1.00 30.54  ?  512 HOH D O   1 
HETATM 6970 O  O   . HOH J 3 .   ? 60.623 16.366  8.319   1.00 27.74  ?  513 HOH D O   1 
HETATM 6971 O  O   . HOH J 3 .   ? 39.153 8.087   26.846  1.00 17.76  ?  514 HOH D O   1 
HETATM 6972 O  O   . HOH J 3 .   ? 55.020 22.244  29.807  1.00 43.32  ?  515 HOH D O   1 
HETATM 6973 O  O   . HOH J 3 .   ? 49.419 -16.424 8.277   1.00 28.93  ?  516 HOH D O   1 
HETATM 6974 O  O   . HOH J 3 .   ? 44.379 4.758   38.395  1.00 27.11  ?  517 HOH D O   1 
HETATM 6975 O  O   . HOH J 3 .   ? 56.044 14.260  25.837  1.00 24.75  ?  518 HOH D O   1 
HETATM 6976 O  O   . HOH J 3 .   ? 34.268 9.039   22.102  1.00 30.54  ?  519 HOH D O   1 
HETATM 6977 O  O   . HOH J 3 .   ? 64.599 13.524  19.505  1.00 33.34  ?  520 HOH D O   1 
HETATM 6978 O  O   . HOH J 3 .   ? 74.909 -15.790 14.508  1.00 54.20  ?  521 HOH D O   1 
HETATM 6979 O  O   . HOH J 3 .   ? 57.846 4.273   26.386  1.00 26.10  ?  522 HOH D O   1 
HETATM 6980 O  O   . HOH J 3 .   ? 45.892 -6.199  14.802  1.00 29.45  ?  523 HOH D O   1 
HETATM 6981 O  O   . HOH J 3 .   ? 63.403 4.251   17.102  1.00 24.15  ?  524 HOH D O   1 
HETATM 6982 O  O   . HOH J 3 .   ? 60.909 -26.344 18.664  1.00 27.98  ?  525 HOH D O   1 
HETATM 6983 O  O   . HOH J 3 .   ? 56.557 1.621   7.927   1.00 17.24  ?  526 HOH D O   1 
HETATM 6984 O  O   . HOH J 3 .   ? 64.351 8.342   5.774   1.00 29.95  ?  527 HOH D O   1 
HETATM 6985 O  O   . HOH J 3 .   ? 61.690 -11.681 20.730  1.00 42.32  ?  528 HOH D O   1 
HETATM 6986 O  O   . HOH J 3 .   ? 43.488 -6.957  2.685   1.00 46.33  ?  529 HOH D O   1 
HETATM 6987 O  O   . HOH J 3 .   ? 39.120 6.247   22.861  1.00 16.94  ?  530 HOH D O   1 
HETATM 6988 O  O   . HOH J 3 .   ? 66.855 -27.200 15.310  1.00 33.73  ?  531 HOH D O   1 
HETATM 6989 O  O   . HOH J 3 .   ? 48.307 -13.136 14.740  1.00 17.12  ?  532 HOH D O   1 
HETATM 6990 O  O   . HOH J 3 .   ? 51.901 16.535  4.820   1.00 32.48  ?  533 HOH D O   1 
HETATM 6991 O  O   . HOH J 3 .   ? 59.336 -12.918 22.891  1.00 29.98  ?  534 HOH D O   1 
HETATM 6992 O  O   . HOH J 3 .   ? 52.774 -18.031 10.421  1.00 23.62  ?  535 HOH D O   1 
HETATM 6993 O  O   . HOH J 3 .   ? 39.841 20.968  2.588   1.00 31.82  ?  536 HOH D O   1 
HETATM 6994 O  O   . HOH J 3 .   ? 62.240 -14.102 19.747  1.00 27.94  ?  537 HOH D O   1 
HETATM 6995 O  O   . HOH J 3 .   ? 60.850 9.540   11.689  1.00 18.77  ?  538 HOH D O   1 
HETATM 6996 O  O   . HOH J 3 .   ? 59.359 -1.584  24.480  1.00 28.93  ?  539 HOH D O   1 
HETATM 6997 O  O   . HOH J 3 .   ? 43.566 24.238  28.576  1.00 36.72  ?  540 HOH D O   1 
HETATM 6998 O  O   . HOH J 3 .   ? 51.326 22.990  11.912  1.00 29.61  ?  541 HOH D O   1 
HETATM 6999 O  O   . HOH J 3 .   ? 42.501 22.182  5.886   1.00 21.23  ?  542 HOH D O   1 
HETATM 7000 O  O   . HOH J 3 .   ? 26.402 20.668  4.789   1.00 23.25  ?  543 HOH D O   1 
HETATM 7001 O  O   . HOH J 3 .   ? 48.296 -6.912  11.078  1.00 22.90  ?  544 HOH D O   1 
HETATM 7002 O  O   . HOH J 3 .   ? 66.071 1.852   23.241  1.00 33.07  ?  545 HOH D O   1 
HETATM 7003 O  O   . HOH J 3 .   ? 40.788 23.876  28.090  1.00 32.75  ?  546 HOH D O   1 
HETATM 7004 O  O   . HOH J 3 .   ? 62.999 8.913   13.169  1.00 29.53  ?  547 HOH D O   1 
HETATM 7005 O  O   . HOH J 3 .   ? 39.068 33.961  9.263   1.00 35.79  ?  548 HOH D O   1 
HETATM 7006 O  O   . HOH J 3 .   ? 62.917 -18.700 19.596  1.00 17.82  ?  549 HOH D O   1 
HETATM 7007 O  O   . HOH J 3 .   ? 49.997 14.417  39.792  1.00 37.51  ?  550 HOH D O   1 
HETATM 7008 O  O   . HOH J 3 .   ? 42.343 32.269  12.066  1.00 45.45  ?  551 HOH D O   1 
HETATM 7009 O  O   . HOH J 3 .   ? 28.352 22.745  2.595   1.00 28.15  ?  552 HOH D O   1 
HETATM 7010 O  O   . HOH J 3 .   ? 63.959 1.543   3.140   1.00 38.07  ?  553 HOH D O   1 
HETATM 7011 O  O   . HOH J 3 .   ? 43.718 -14.064 6.940   1.00 36.99  ?  554 HOH D O   1 
HETATM 7012 O  O   . HOH J 3 .   ? 37.260 23.640  26.306  1.00 27.14  ?  555 HOH D O   1 
HETATM 7013 O  O   . HOH J 3 .   ? 64.845 -20.388 4.318   1.00 39.09  ?  556 HOH D O   1 
HETATM 7014 O  O   . HOH J 3 .   ? 44.569 3.654   12.080  1.00 18.37  ?  557 HOH D O   1 
HETATM 7015 O  O   . HOH J 3 .   ? 52.910 17.461  31.517  1.00 30.01  ?  558 HOH D O   1 
HETATM 7016 O  O   . HOH J 3 .   ? 62.900 -10.522 6.767   1.00 32.57  ?  559 HOH D O   1 
HETATM 7017 O  O   . HOH J 3 .   ? 43.625 11.415  36.457  1.00 43.51  ?  560 HOH D O   1 
HETATM 7018 O  O   . HOH J 3 .   ? 41.887 4.996   -1.269  1.00 38.52  ?  561 HOH D O   1 
HETATM 7019 O  O   . HOH J 3 .   ? 30.028 17.067  -2.133  1.00 32.51  ?  562 HOH D O   1 
HETATM 7020 O  O   . HOH J 3 .   ? 45.586 1.323   18.557  1.00 18.76  ?  563 HOH D O   1 
HETATM 7021 O  O   . HOH J 3 .   ? 47.163 25.224  11.925  1.00 34.55  ?  564 HOH D O   1 
HETATM 7022 O  O   . HOH J 3 .   ? 57.916 19.041  23.765  1.00 34.55  ?  565 HOH D O   1 
HETATM 7023 O  O   . HOH J 3 .   ? 62.645 11.623  13.375  1.00 25.92  ?  566 HOH D O   1 
HETATM 7024 O  O   . HOH J 3 .   ? 38.200 1.357   1.014   1.00 37.63  ?  567 HOH D O   1 
HETATM 7025 O  O   . HOH J 3 .   ? 30.849 22.202  22.869  1.00 33.93  ?  568 HOH D O   1 
HETATM 7026 O  O   . HOH J 3 .   ? 48.587 14.416  36.085  1.00 43.04  ?  569 HOH D O   1 
HETATM 7027 O  O   . HOH J 3 .   ? 67.007 -21.949 9.717   1.00 111.58 ?  570 HOH D O   1 
HETATM 7028 O  O   . HOH J 3 .   ? 29.169 28.398  3.522   1.00 42.51  ?  571 HOH D O   1 
HETATM 7029 O  O   . HOH J 3 .   ? 42.354 1.639   1.618   1.00 29.81  ?  572 HOH D O   1 
HETATM 7030 O  O   . HOH J 3 .   ? 25.590 23.205  2.247   1.00 39.07  ?  573 HOH D O   1 
HETATM 7031 O  O   . HOH J 3 .   ? 24.082 21.258  5.075   1.00 35.00  ?  574 HOH D O   1 
HETATM 7032 O  O   . HOH J 3 .   ? 23.373 19.094  12.258  1.00 42.09  ?  575 HOH D O   1 
HETATM 7033 O  O   . HOH J 3 .   ? 52.305 15.277  34.940  1.00 40.84  ?  576 HOH D O   1 
HETATM 7034 O  O   . HOH J 3 .   ? 59.488 -22.170 4.312   1.00 43.17  ?  577 HOH D O   1 
HETATM 7035 O  O   . HOH J 3 .   ? 62.166 4.026   27.789  1.00 41.20  ?  578 HOH D O   1 
HETATM 7036 O  O   . HOH J 3 .   ? 26.611 14.606  14.949  1.00 38.33  ?  579 HOH D O   1 
HETATM 7037 O  O   . HOH J 3 .   ? 68.052 -2.516  12.645  1.00 34.84  ?  580 HOH D O   1 
HETATM 7038 O  O   . HOH J 3 .   ? 59.030 19.030  28.390  1.00 46.53  ?  581 HOH D O   1 
HETATM 7039 O  O   . HOH J 3 .   ? 56.469 -23.774 3.383   1.00 45.92  ?  582 HOH D O   1 
HETATM 7040 O  O   . HOH J 3 .   ? 65.900 -8.749  8.799   1.00 35.54  ?  583 HOH D O   1 
HETATM 7041 O  O   . HOH J 3 .   ? 45.684 19.573  34.560  1.00 32.31  ?  584 HOH D O   1 
HETATM 7042 O  O   . HOH J 3 .   ? 54.964 0.834   4.538   1.00 32.03  ?  585 HOH D O   1 
HETATM 7043 O  O   . HOH J 3 .   ? 41.931 20.324  3.932   1.00 23.02  ?  586 HOH D O   1 
HETATM 7044 O  O   . HOH J 3 .   ? 35.066 27.986  11.403  1.00 36.92  ?  587 HOH D O   1 
HETATM 7045 O  O   . HOH J 3 .   ? 40.253 24.848  3.873   1.00 34.46  ?  588 HOH D O   1 
HETATM 7046 O  O   . HOH J 3 .   ? 47.221 30.065  12.874  1.00 48.69  ?  589 HOH D O   1 
HETATM 7047 O  O   . HOH J 3 .   ? 49.279 26.306  11.019  1.00 35.79  ?  590 HOH D O   1 
HETATM 7048 O  O   . HOH J 3 .   ? 64.597 10.006  21.202  1.00 46.93  ?  591 HOH D O   1 
HETATM 7049 O  O   . HOH J 3 .   ? 47.600 -12.105 12.235  1.00 36.92  ?  592 HOH D O   1 
HETATM 7050 O  O   . HOH J 3 .   ? 35.683 25.320  16.929  1.00 32.36  ?  593 HOH D O   1 
HETATM 7051 O  O   . HOH J 3 .   ? 37.129 13.955  -3.982  1.00 35.07  ?  594 HOH D O   1 
HETATM 7052 O  O   . HOH J 3 .   ? 67.429 -6.184  7.970   1.00 42.41  ?  595 HOH D O   1 
HETATM 7053 O  O   . HOH J 3 .   ? 54.369 1.756   6.745   1.00 29.40  ?  596 HOH D O   1 
HETATM 7054 O  O   . HOH J 3 .   ? 61.079 -8.113  21.703  1.00 38.40  ?  597 HOH D O   1 
HETATM 7055 O  O   . HOH J 3 .   ? 32.475 10.015  -5.902  1.00 40.44  ?  598 HOH D O   1 
HETATM 7056 O  O   . HOH J 3 .   ? 40.244 11.632  -1.742  1.00 37.04  ?  599 HOH D O   1 
HETATM 7057 O  O   . HOH J 3 .   ? 29.154 13.783  14.325  1.00 35.25  ?  600 HOH D O   1 
HETATM 7058 O  O   . HOH J 3 .   ? 38.478 22.014  29.102  1.00 30.35  ?  601 HOH D O   1 
HETATM 7059 O  O   . HOH J 3 .   ? 24.224 12.734  10.196  1.00 53.30  ?  602 HOH D O   1 
HETATM 7060 O  O   . HOH J 3 .   ? 37.229 20.696  -2.574  1.00 42.86  ?  603 HOH D O   1 
HETATM 7061 O  O   . HOH J 3 .   ? 47.649 24.457  33.066  1.00 32.56  ?  604 HOH D O   1 
HETATM 7062 O  O   . HOH J 3 .   ? 29.105 13.890  -2.236  1.00 43.59  ?  605 HOH D O   1 
HETATM 7063 O  O   . HOH J 3 .   ? 39.125 25.411  6.290   1.00 26.60  ?  606 HOH D O   1 
HETATM 7064 O  O   . HOH J 3 .   ? 59.549 11.898  27.750  1.00 39.63  ?  607 HOH D O   1 
HETATM 7065 O  O   . HOH J 3 .   ? 51.487 25.772  30.650  1.00 47.95  ?  608 HOH D O   1 
HETATM 7066 O  O   . HOH J 3 .   ? 55.073 -21.636 6.006   1.00 39.68  ?  609 HOH D O   1 
HETATM 7067 O  O   . HOH J 3 .   ? 64.163 5.459   26.710  1.00 43.25  ?  610 HOH D O   1 
HETATM 7068 O  O   . HOH J 3 .   ? 50.216 1.178   5.458   1.00 34.23  ?  611 HOH D O   1 
HETATM 7069 O  O   . HOH J 3 .   ? 46.079 32.302  13.992  1.00 39.54  ?  612 HOH D O   1 
HETATM 7070 O  O   . HOH J 3 .   ? 35.279 7.111   20.013  1.00 33.65  ?  613 HOH D O   1 
HETATM 7071 O  O   . HOH J 3 .   ? 59.618 15.818  29.338  1.00 36.94  ?  614 HOH D O   1 
HETATM 7072 O  O   . HOH J 3 .   ? 66.196 8.852   18.735  1.00 44.55  ?  615 HOH D O   1 
HETATM 7073 O  O   . HOH J 3 .   ? 33.393 15.929  31.927  1.00 36.59  ?  616 HOH D O   1 
HETATM 7074 O  O   . HOH J 3 .   ? 26.984 27.060  11.758  1.00 35.64  ?  617 HOH D O   1 
HETATM 7075 O  O   . HOH J 3 .   ? 51.963 12.864  40.404  1.00 50.26  ?  618 HOH D O   1 
HETATM 7076 O  O   . HOH J 3 .   ? 42.101 28.124  7.731   1.00 28.04  ?  619 HOH D O   1 
HETATM 7077 O  O   . HOH J 3 .   ? 68.747 5.538   18.167  1.00 47.06  ?  620 HOH D O   1 
HETATM 7078 O  O   . HOH J 3 .   ? 65.166 10.856  16.099  1.00 33.32  ?  621 HOH D O   1 
HETATM 7079 O  O   . HOH J 3 .   ? 52.289 22.529  32.766  1.00 34.44  ?  622 HOH D O   1 
HETATM 7080 O  O   . HOH J 3 .   ? 58.561 -27.641 14.602  1.00 45.59  ?  623 HOH D O   1 
HETATM 7081 O  O   . HOH J 3 .   ? 40.365 9.392   35.362  1.00 36.16  ?  624 HOH D O   1 
HETATM 7082 O  O   . HOH J 3 .   ? 31.053 19.486  23.936  1.00 36.39  ?  625 HOH D O   1 
HETATM 7083 O  O   . HOH J 3 .   ? 53.018 26.607  26.576  1.00 33.71  ?  626 HOH D O   1 
HETATM 7084 O  O   . HOH J 3 .   ? 25.590 16.874  -0.928  1.00 36.01  ?  627 HOH D O   1 
HETATM 7085 O  O   . HOH J 3 .   ? 31.379 12.958  12.800  1.00 44.95  ?  628 HOH D O   1 
HETATM 7086 O  O   . HOH J 3 .   ? 31.494 12.893  -5.299  1.00 36.35  ?  629 HOH D O   1 
HETATM 7087 O  O   . HOH J 3 .   ? 40.533 19.942  0.741   1.00 35.79  ?  630 HOH D O   1 
HETATM 7088 O  O   . HOH J 3 .   ? 51.348 -4.132  2.952   1.00 40.86  ?  631 HOH D O   1 
HETATM 7089 O  O   . HOH J 3 .   ? 64.864 12.523  13.457  1.00 42.09  ?  632 HOH D O   1 
HETATM 7090 O  O   . HOH J 3 .   ? 30.931 9.610   -2.600  1.00 26.42  ?  633 HOH D O   1 
HETATM 7091 O  O   . HOH J 3 .   ? 67.359 -4.184  10.005  1.00 48.33  ?  634 HOH D O   1 
HETATM 7092 O  O   . HOH J 3 .   ? 41.242 24.374  5.657   1.00 34.72  ?  635 HOH D O   1 
HETATM 7093 O  O   . HOH J 3 .   ? 66.043 7.548   15.820  1.00 39.66  ?  636 HOH D O   1 
HETATM 7094 O  O   . HOH J 3 .   ? 44.875 25.516  27.053  1.00 27.06  ?  637 HOH D O   1 
HETATM 7095 O  O   . HOH J 3 .   ? 34.970 24.500  -1.303  1.00 40.36  ?  638 HOH D O   1 
HETATM 7096 O  O   . HOH J 3 .   ? 51.651 -1.958  5.710   1.00 33.78  ?  639 HOH D O   1 
HETATM 7097 O  O   . HOH J 3 .   ? 50.531 -16.999 10.451  1.00 26.59  ?  640 HOH D O   1 
HETATM 7098 O  O   . HOH J 3 .   ? 32.429 11.787  31.019  1.00 33.53  ?  641 HOH D O   1 
HETATM 7099 O  O   . HOH J 3 .   ? 43.699 0.606   4.308   1.00 38.37  ?  642 HOH D O   1 
HETATM 7100 O  O   . HOH J 3 .   ? 41.805 9.984   36.964  1.00 37.46  ?  643 HOH D O   1 
HETATM 7101 O  O   . HOH J 3 .   ? 47.958 22.605  34.409  1.00 34.77  ?  644 HOH D O   1 
HETATM 7102 O  O   . HOH J 3 .   ? 51.706 -20.534 10.408  1.00 44.05  ?  645 HOH D O   1 
HETATM 7103 O  O   . HOH J 3 .   ? 28.682 11.422  23.960  1.00 45.08  ?  646 HOH D O   1 
HETATM 7104 O  O   . HOH J 3 .   ? 63.642 8.516   30.171  1.00 40.18  ?  647 HOH D O   1 
HETATM 7105 O  O   . HOH J 3 .   ? 44.535 19.140  2.846   1.00 36.09  ?  648 HOH D O   1 
HETATM 7106 O  O   . HOH J 3 .   ? 43.177 0.862   7.743   1.00 22.77  ?  649 HOH D O   1 
HETATM 7107 O  O   . HOH J 3 .   ? 28.871 16.750  24.205  1.00 34.80  ?  650 HOH D O   1 
HETATM 7108 O  O   . HOH J 3 .   ? 59.528 18.151  7.132   1.00 25.85  ?  651 HOH D O   1 
HETATM 7109 O  O   . HOH J 3 .   ? 22.256 27.328  7.576   1.00 42.67  ?  652 HOH D O   1 
HETATM 7110 O  O   . HOH J 3 .   ? 36.972 30.228  3.099   1.00 32.39  ?  653 HOH D O   1 
HETATM 7111 O  O   . HOH J 3 .   ? 35.648 19.423  -7.550  1.00 46.03  ?  654 HOH D O   1 
HETATM 7112 O  O   . HOH J 3 .   ? 21.475 15.688  9.885   1.00 42.57  ?  655 HOH D O   1 
HETATM 7113 O  O   . HOH J 3 .   ? 66.653 13.332  17.875  1.00 42.42  ?  656 HOH D O   1 
HETATM 7114 O  O   . HOH J 3 .   ? 48.550 -3.540  3.498   1.00 44.52  ?  657 HOH D O   1 
HETATM 7115 O  O   . HOH J 3 .   ? 43.672 -2.527  4.282   1.00 39.02  ?  658 HOH D O   1 
HETATM 7116 O  O   . HOH J 3 .   ? 28.427 15.232  26.595  1.00 45.31  ?  659 HOH D O   1 
HETATM 7117 O  O   . HOH J 3 .   ? 30.170 32.157  4.416   1.00 36.87  ?  660 HOH D O   1 
HETATM 7118 O  O   . HOH J 3 .   ? 63.412 11.595  30.469  1.00 37.13  ?  661 HOH D O   1 
HETATM 7119 O  O   . HOH J 3 .   ? 43.192 27.562  6.164   1.00 35.13  ?  662 HOH D O   1 
HETATM 7120 O  O   . HOH J 3 .   ? 47.624 19.975  36.689  1.00 44.19  ?  663 HOH D O   1 
HETATM 7121 O  O   . HOH J 3 .   ? 49.941 0.877   2.841   1.00 45.70  ?  664 HOH D O   1 
HETATM 7122 O  O   . HOH J 3 .   ? 39.065 14.721  -6.162  1.00 37.84  ?  665 HOH D O   1 
HETATM 7123 O  O   . HOH J 3 .   ? 43.422 19.671  0.645   1.00 42.27  ?  666 HOH D O   1 
HETATM 7124 O  O   . HOH J 3 .   ? 43.231 21.754  -0.035  1.00 44.28  ?  667 HOH D O   1 
HETATM 7125 O  O   . HOH J 3 .   ? 34.125 14.941  -9.688  1.00 39.56  ?  668 HOH D O   1 
HETATM 7126 O  O   . HOH J 3 .   ? 40.630 29.531  5.304   1.00 39.41  ?  669 HOH D O   1 
HETATM 7127 O  O   . HOH J 3 .   ? 65.615 9.603   30.761  1.00 44.20  ?  670 HOH D O   1 
HETATM 7128 O  O   . HOH J 3 .   ? 19.039 21.514  15.079  1.00 41.30  ?  671 HOH D O   1 
HETATM 7129 O  O   . HOH J 3 .   ? 40.206 16.633  -4.719  1.00 51.80  ?  672 HOH D O   1 
HETATM 7130 O  O   . HOH J 3 .   ? 27.931 33.127  7.386   1.00 46.08  ?  673 HOH D O   1 
HETATM 7131 O  O   . HOH J 3 .   ? 19.605 14.769  10.986  1.00 43.93  ?  674 HOH D O   1 
HETATM 7132 O  O   . HOH J 3 .   ? 17.594 19.093  13.067  1.00 39.57  ?  675 HOH D O   1 
HETATM 7133 O  O   . HOH J 3 .   ? 21.334 17.954  18.502  1.00 44.58  ?  676 HOH D O   1 
HETATM 7134 O  O   . HOH K 3 .   ? 58.278 18.969  -25.633 1.00 14.18  ?  401 HOH A O   1 
HETATM 7135 O  O   . HOH K 3 .   ? 61.925 6.011   -22.985 1.00 52.10  ?  402 HOH A O   1 
HETATM 7136 O  O   . HOH K 3 .   ? 23.813 0.045   -13.592 1.00 41.44  ?  403 HOH A O   1 
HETATM 7137 O  O   . HOH K 3 .   ? 30.614 -14.669 -16.047 1.00 39.33  ?  404 HOH A O   1 
HETATM 7138 O  O   . HOH K 3 .   ? 33.154 9.423   -23.871 1.00 38.43  ?  405 HOH A O   1 
HETATM 7139 O  O   . HOH K 3 .   ? 26.592 -5.122  -21.474 1.00 40.13  ?  406 HOH A O   1 
HETATM 7140 O  O   . HOH K 3 .   ? 43.378 15.992  -31.907 1.00 28.35  ?  407 HOH A O   1 
HETATM 7141 O  O   . HOH K 3 .   ? 51.299 24.333  -17.515 1.00 38.88  ?  408 HOH A O   1 
HETATM 7142 O  O   . HOH K 3 .   ? 63.622 11.035  -22.332 1.00 40.63  ?  409 HOH A O   1 
HETATM 7143 O  O   . HOH K 3 .   ? 42.879 17.508  -19.428 1.00 42.76  ?  410 HOH A O   1 
HETATM 7144 O  O   . HOH K 3 .   ? 44.044 17.658  -40.070 1.00 32.31  ?  411 HOH A O   1 
HETATM 7145 O  O   . HOH K 3 .   ? 52.890 13.048  -39.861 1.00 25.68  ?  412 HOH A O   1 
HETATM 7146 O  O   . HOH K 3 .   ? 41.748 6.763   -7.727  1.00 38.06  ?  413 HOH A O   1 
HETATM 7147 O  O   . HOH K 3 .   ? 54.872 -1.285  -42.708 1.00 30.87  ?  414 HOH A O   1 
HETATM 7148 O  O   . HOH K 3 .   ? 62.614 6.796   -35.975 1.00 26.85  ?  415 HOH A O   1 
HETATM 7149 O  O   . HOH K 3 .   ? 30.414 6.888   -23.190 1.00 28.78  ?  416 HOH A O   1 
HETATM 7150 O  O   . HOH K 3 .   ? 23.347 4.699   -8.781  1.00 50.53  ?  417 HOH A O   1 
HETATM 7151 O  O   . HOH K 3 .   ? 30.640 4.992   -19.397 1.00 37.80  ?  418 HOH A O   1 
HETATM 7152 O  O   . HOH K 3 .   ? 50.499 -11.567 -36.628 1.00 24.49  ?  419 HOH A O   1 
HETATM 7153 O  O   . HOH K 3 .   ? 55.324 -10.622 -35.518 1.00 33.24  ?  420 HOH A O   1 
HETATM 7154 O  O   . HOH K 3 .   ? 36.779 -3.807  -41.306 1.00 34.76  ?  421 HOH A O   1 
HETATM 7155 O  O   . HOH K 3 .   ? 36.431 -16.878 -34.444 1.00 37.56  ?  422 HOH A O   1 
HETATM 7156 O  O   . HOH K 3 .   ? 34.628 4.012   -14.288 1.00 21.87  ?  423 HOH A O   1 
HETATM 7157 O  O   . HOH K 3 .   ? 59.104 5.641   -36.999 1.00 23.31  ?  424 HOH A O   1 
HETATM 7158 O  O   . HOH K 3 .   ? 60.396 -7.952  -28.058 1.00 26.08  ?  425 HOH A O   1 
HETATM 7159 O  O   . HOH K 3 .   ? 29.816 0.561   -0.362  1.00 36.61  ?  426 HOH A O   1 
HETATM 7160 O  O   . HOH K 3 .   ? 31.145 5.463   -4.279  1.00 23.73  ?  427 HOH A O   1 
HETATM 7161 O  O   . HOH K 3 .   ? 45.685 -0.762  -18.964 1.00 26.02  ?  428 HOH A O   1 
HETATM 7162 O  O   . HOH K 3 .   ? 44.446 8.680   -24.297 1.00 23.29  ?  429 HOH A O   1 
HETATM 7163 O  O   . HOH K 3 .   ? 31.619 -4.626  -26.557 1.00 32.99  ?  430 HOH A O   1 
HETATM 7164 O  O   . HOH K 3 .   ? 41.032 12.890  -32.723 1.00 31.77  ?  431 HOH A O   1 
HETATM 7165 O  O   . HOH K 3 .   ? 55.351 27.577  -24.295 1.00 31.49  ?  432 HOH A O   1 
HETATM 7166 O  O   . HOH K 3 .   ? 37.863 7.601   -21.482 1.00 23.52  ?  433 HOH A O   1 
HETATM 7167 O  O   . HOH K 3 .   ? 28.998 -11.835 2.994   1.00 34.73  ?  434 HOH A O   1 
HETATM 7168 O  O   . HOH K 3 .   ? 24.179 -7.456  -20.626 1.00 32.86  ?  435 HOH A O   1 
HETATM 7169 O  O   . HOH K 3 .   ? 30.255 -15.388 -10.177 1.00 23.35  ?  436 HOH A O   1 
HETATM 7170 O  O   . HOH K 3 .   ? 34.228 0.703   2.612   1.00 33.44  ?  437 HOH A O   1 
HETATM 7171 O  O   . HOH K 3 .   ? 45.774 -0.526  -21.822 1.00 13.25  ?  438 HOH A O   1 
HETATM 7172 O  O   . HOH K 3 .   ? 34.694 6.663   -35.823 1.00 27.64  ?  439 HOH A O   1 
HETATM 7173 O  O   . HOH K 3 .   ? 66.717 7.567   -29.473 1.00 27.24  ?  440 HOH A O   1 
HETATM 7174 O  O   . HOH K 3 .   ? 27.021 -7.642  -0.085  1.00 23.67  ?  441 HOH A O   1 
HETATM 7175 O  O   . HOH K 3 .   ? 57.842 -15.358 -28.385 1.00 26.68  ?  442 HOH A O   1 
HETATM 7176 O  O   . HOH K 3 .   ? 57.509 -1.430  -23.447 1.00 13.19  ?  443 HOH A O   1 
HETATM 7177 O  O   . HOH K 3 .   ? 52.436 6.953   -29.499 1.00 18.48  ?  444 HOH A O   1 
HETATM 7178 O  O   . HOH K 3 .   ? 41.438 -14.205 -32.992 1.00 28.79  ?  445 HOH A O   1 
HETATM 7179 O  O   . HOH K 3 .   ? 36.243 3.467   2.017   1.00 31.04  ?  446 HOH A O   1 
HETATM 7180 O  O   . HOH K 3 .   ? 22.589 -13.744 -9.514  1.00 32.20  ?  447 HOH A O   1 
HETATM 7181 O  O   . HOH K 3 .   ? 44.194 -2.438  -41.084 1.00 30.79  ?  448 HOH A O   1 
HETATM 7182 O  O   . HOH K 3 .   ? 39.242 16.030  -39.755 1.00 46.28  ?  449 HOH A O   1 
HETATM 7183 O  O   . HOH K 3 .   ? 45.604 4.793   -42.130 1.00 33.17  ?  450 HOH A O   1 
HETATM 7184 O  O   . HOH K 3 .   ? 32.494 8.095   -34.916 1.00 46.05  ?  451 HOH A O   1 
HETATM 7185 O  O   . HOH K 3 .   ? 61.472 -0.872  -23.860 1.00 34.72  ?  452 HOH A O   1 
HETATM 7186 O  O   . HOH K 3 .   ? 20.230 -5.438  -3.988  1.00 30.20  ?  453 HOH A O   1 
HETATM 7187 O  O   . HOH K 3 .   ? 47.261 14.866  -29.968 1.00 20.56  ?  454 HOH A O   1 
HETATM 7188 O  O   . HOH K 3 .   ? 40.258 -2.777  -8.685  1.00 34.51  ?  455 HOH A O   1 
HETATM 7189 O  O   . HOH K 3 .   ? 28.827 6.403   -13.392 1.00 37.63  ?  456 HOH A O   1 
HETATM 7190 O  O   . HOH K 3 .   ? 56.605 16.595  -37.747 1.00 26.80  ?  457 HOH A O   1 
HETATM 7191 O  O   . HOH K 3 .   ? 45.359 4.595   -18.105 1.00 17.77  ?  458 HOH A O   1 
HETATM 7192 O  O   . HOH K 3 .   ? 38.725 2.901   -9.129  1.00 18.78  ?  459 HOH A O   1 
HETATM 7193 O  O   . HOH K 3 .   ? 64.123 -4.353  -34.117 1.00 31.34  ?  460 HOH A O   1 
HETATM 7194 O  O   . HOH K 3 .   ? 48.085 18.311  -17.987 1.00 21.35  ?  461 HOH A O   1 
HETATM 7195 O  O   . HOH K 3 .   ? 25.709 -5.224  -13.585 1.00 28.23  ?  462 HOH A O   1 
HETATM 7196 O  O   . HOH K 3 .   ? 39.379 -7.524  -32.411 1.00 21.39  ?  463 HOH A O   1 
HETATM 7197 O  O   . HOH K 3 .   ? 27.550 -15.743 -0.531  1.00 29.52  ?  464 HOH A O   1 
HETATM 7198 O  O   . HOH K 3 .   ? 26.927 -4.738  -1.178  1.00 24.10  ?  465 HOH A O   1 
HETATM 7199 O  O   . HOH K 3 .   ? 63.331 -9.567  -34.472 1.00 23.83  ?  466 HOH A O   1 
HETATM 7200 O  O   . HOH K 3 .   ? 33.877 -1.458  -0.374  1.00 37.58  ?  467 HOH A O   1 
HETATM 7201 O  O   . HOH K 3 .   ? 29.516 -11.114 -11.226 1.00 23.87  ?  468 HOH A O   1 
HETATM 7202 O  O   . HOH K 3 .   ? 63.845 5.423   -21.499 1.00 40.46  ?  469 HOH A O   1 
HETATM 7203 O  O   . HOH K 3 .   ? 75.987 15.452  -32.508 1.00 32.51  ?  470 HOH A O   1 
HETATM 7204 O  O   . HOH K 3 .   ? 25.647 -16.085 -8.318  1.00 32.53  ?  471 HOH A O   1 
HETATM 7205 O  O   . HOH K 3 .   ? 35.127 -11.098 -32.146 1.00 39.79  ?  472 HOH A O   1 
HETATM 7206 O  O   . HOH K 3 .   ? 35.109 9.837   -28.633 1.00 28.97  ?  473 HOH A O   1 
HETATM 7207 O  O   . HOH K 3 .   ? 45.778 11.934  -39.438 1.00 35.76  ?  474 HOH A O   1 
HETATM 7208 O  O   . HOH K 3 .   ? 25.481 6.884   -8.659  1.00 41.84  ?  475 HOH A O   1 
HETATM 7209 O  O   . HOH K 3 .   ? 47.321 -8.018  -27.098 1.00 17.50  ?  476 HOH A O   1 
HETATM 7210 O  O   . HOH K 3 .   ? 43.586 13.855  -24.584 1.00 34.36  ?  477 HOH A O   1 
HETATM 7211 O  O   . HOH K 3 .   ? 27.856 -19.092 -1.540  1.00 29.70  ?  478 HOH A O   1 
HETATM 7212 O  O   . HOH K 3 .   ? 47.873 10.098  -14.214 1.00 28.15  ?  479 HOH A O   1 
HETATM 7213 O  O   . HOH K 3 .   ? 42.530 -4.993  -10.061 1.00 27.59  ?  480 HOH A O   1 
HETATM 7214 O  O   . HOH K 3 .   ? 38.814 -0.447  -41.284 1.00 41.89  ?  481 HOH A O   1 
HETATM 7215 O  O   . HOH K 3 .   ? 43.997 11.551  -29.819 1.00 25.09  ?  482 HOH A O   1 
HETATM 7216 O  O   . HOH K 3 .   ? 50.269 21.139  -20.708 1.00 32.66  ?  483 HOH A O   1 
HETATM 7217 O  O   . HOH K 3 .   ? 59.103 -13.639 -35.258 1.00 37.45  ?  484 HOH A O   1 
HETATM 7218 O  O   . HOH K 3 .   ? 34.413 2.151   -21.461 1.00 18.94  ?  485 HOH A O   1 
HETATM 7219 O  O   . HOH K 3 .   ? 36.036 8.892   -26.115 1.00 32.18  ?  486 HOH A O   1 
HETATM 7220 O  O   . HOH K 3 .   ? 40.597 -4.905  -17.314 1.00 11.13  ?  487 HOH A O   1 
HETATM 7221 O  O   . HOH K 3 .   ? 66.612 3.003   -33.667 1.00 27.58  ?  488 HOH A O   1 
HETATM 7222 O  O   . HOH K 3 .   ? 46.140 -4.495  -22.268 1.00 16.40  ?  489 HOH A O   1 
HETATM 7223 O  O   . HOH K 3 .   ? 44.622 6.358   -26.145 1.00 13.95  ?  490 HOH A O   1 
HETATM 7224 O  O   . HOH K 3 .   ? 66.296 5.318   -28.061 1.00 28.06  ?  491 HOH A O   1 
HETATM 7225 O  O   . HOH K 3 .   ? 51.176 11.254  -39.757 1.00 30.77  ?  492 HOH A O   1 
HETATM 7226 O  O   . HOH K 3 .   ? 37.496 -14.084 -24.340 1.00 20.69  ?  493 HOH A O   1 
HETATM 7227 O  O   . HOH K 3 .   ? 52.864 -23.250 -31.418 1.00 29.29  ?  494 HOH A O   1 
HETATM 7228 O  O   . HOH K 3 .   ? 26.017 6.912   -13.404 1.00 38.95  ?  495 HOH A O   1 
HETATM 7229 O  O   . HOH K 3 .   ? 58.597 -7.005  -25.859 1.00 30.80  ?  496 HOH A O   1 
HETATM 7230 O  O   . HOH K 3 .   ? 42.175 0.118   -9.025  1.00 31.03  ?  497 HOH A O   1 
HETATM 7231 O  O   . HOH K 3 .   ? 32.549 -1.001  -31.736 1.00 29.72  ?  498 HOH A O   1 
HETATM 7232 O  O   . HOH K 3 .   ? 37.774 -6.524  -5.453  1.00 14.96  ?  499 HOH A O   1 
HETATM 7233 O  O   . HOH K 3 .   ? 28.706 2.205   -1.777  1.00 32.83  ?  500 HOH A O   1 
HETATM 7234 O  O   . HOH K 3 .   ? 30.717 -10.690 -14.331 1.00 20.30  ?  501 HOH A O   1 
HETATM 7235 O  O   . HOH K 3 .   ? 64.773 23.508  -22.523 1.00 33.96  ?  502 HOH A O   1 
HETATM 7236 O  O   . HOH K 3 .   ? 59.900 21.324  -22.199 1.00 24.00  ?  503 HOH A O   1 
HETATM 7237 O  O   . HOH K 3 .   ? 38.270 3.815   -17.264 1.00 33.18  ?  504 HOH A O   1 
HETATM 7238 O  O   . HOH K 3 .   ? 41.880 11.818  -40.310 1.00 31.50  ?  505 HOH A O   1 
HETATM 7239 O  O   . HOH K 3 .   ? 58.307 24.323  -22.019 1.00 30.25  ?  506 HOH A O   1 
HETATM 7240 O  O   . HOH K 3 .   ? 45.193 -0.742  -43.283 1.00 38.57  ?  507 HOH A O   1 
HETATM 7241 O  O   . HOH K 3 .   ? 62.913 0.955   -24.513 1.00 32.81  ?  508 HOH A O   1 
HETATM 7242 O  O   . HOH K 3 .   ? 34.982 -8.745  -4.274  1.00 17.70  ?  509 HOH A O   1 
HETATM 7243 O  O   . HOH K 3 .   ? 40.874 1.297   -2.302  1.00 21.99  ?  510 HOH A O   1 
HETATM 7244 O  O   . HOH K 3 .   ? 40.857 9.837   -18.895 1.00 40.72  ?  511 HOH A O   1 
HETATM 7245 O  O   . HOH K 3 .   ? 43.651 11.076  -24.605 1.00 30.09  ?  512 HOH A O   1 
HETATM 7246 O  O   . HOH K 3 .   ? 57.894 -19.547 -27.941 1.00 29.91  ?  513 HOH A O   1 
HETATM 7247 O  O   . HOH K 3 .   ? 69.607 12.468  -34.055 1.00 37.62  ?  514 HOH A O   1 
HETATM 7248 O  O   . HOH K 3 .   ? 33.777 1.180   -31.041 1.00 24.78  ?  515 HOH A O   1 
HETATM 7249 O  O   . HOH K 3 .   ? 45.284 1.707   -16.931 1.00 30.04  ?  516 HOH A O   1 
HETATM 7250 O  O   . HOH K 3 .   ? 41.493 7.972   -38.515 1.00 24.13  ?  517 HOH A O   1 
HETATM 7251 O  O   . HOH K 3 .   ? 36.275 -9.757  -34.651 1.00 35.31  ?  518 HOH A O   1 
HETATM 7252 O  O   . HOH K 3 .   ? 28.716 2.262   -6.380  1.00 29.57  ?  519 HOH A O   1 
HETATM 7253 O  O   . HOH K 3 .   ? 66.139 20.293  -33.760 1.00 28.69  ?  520 HOH A O   1 
HETATM 7254 O  O   . HOH K 3 .   ? 69.349 9.520   -31.520 1.00 31.81  ?  521 HOH A O   1 
HETATM 7255 O  O   . HOH K 3 .   ? 32.339 -13.597 -29.398 1.00 41.04  ?  522 HOH A O   1 
HETATM 7256 O  O   . HOH K 3 .   ? 36.716 -15.530 -30.837 1.00 29.18  ?  523 HOH A O   1 
HETATM 7257 O  O   . HOH K 3 .   ? 34.583 -5.177  -35.399 1.00 24.47  ?  524 HOH A O   1 
HETATM 7258 O  O   . HOH K 3 .   ? 20.865 -3.581  -10.437 1.00 46.94  ?  525 HOH A O   1 
HETATM 7259 O  O   . HOH K 3 .   ? 32.575 4.365   -21.164 1.00 30.37  ?  526 HOH A O   1 
HETATM 7260 O  O   . HOH K 3 .   ? 33.641 -7.388  -34.050 1.00 44.67  ?  527 HOH A O   1 
HETATM 7261 O  O   . HOH K 3 .   ? 25.070 -2.740  -12.697 1.00 37.46  ?  528 HOH A O   1 
HETATM 7262 O  O   . HOH K 3 .   ? 41.378 6.569   -17.307 1.00 21.92  ?  529 HOH A O   1 
HETATM 7263 O  O   . HOH K 3 .   ? 32.417 -6.653  -28.760 1.00 39.87  ?  530 HOH A O   1 
HETATM 7264 O  O   . HOH K 3 .   ? 28.264 4.814   -29.538 1.00 31.32  ?  531 HOH A O   1 
HETATM 7265 O  O   . HOH K 3 .   ? 43.181 8.219   -27.756 1.00 21.23  ?  532 HOH A O   1 
HETATM 7266 O  O   . HOH K 3 .   ? 57.863 16.900  -43.837 1.00 42.26  ?  533 HOH A O   1 
HETATM 7267 O  O   . HOH K 3 .   ? 47.151 2.762   -19.994 1.00 22.74  ?  534 HOH A O   1 
HETATM 7268 O  O   . HOH K 3 .   ? 63.223 22.827  -27.949 1.00 31.98  ?  535 HOH A O   1 
HETATM 7269 O  O   . HOH K 3 .   ? 37.653 13.972  -39.134 1.00 34.71  ?  536 HOH A O   1 
HETATM 7270 O  O   . HOH K 3 .   ? 56.823 -4.180  -23.181 1.00 14.81  ?  537 HOH A O   1 
HETATM 7271 O  O   . HOH K 3 .   ? 43.893 -7.193  -13.823 1.00 28.80  ?  538 HOH A O   1 
HETATM 7272 O  O   . HOH K 3 .   ? 48.065 -4.116  -20.118 1.00 26.37  ?  539 HOH A O   1 
HETATM 7273 O  O   . HOH K 3 .   ? 38.017 0.062   -10.288 1.00 18.81  ?  540 HOH A O   1 
HETATM 7274 O  O   . HOH K 3 .   ? 66.691 3.023   -29.059 1.00 31.28  ?  541 HOH A O   1 
HETATM 7275 O  O   . HOH K 3 .   ? 21.717 3.260   -6.864  1.00 36.03  ?  542 HOH A O   1 
HETATM 7276 O  O   . HOH K 3 .   ? 42.929 16.271  -21.474 1.00 31.86  ?  543 HOH A O   1 
HETATM 7277 O  O   . HOH K 3 .   ? 64.610 0.113   -37.752 1.00 41.05  ?  544 HOH A O   1 
HETATM 7278 O  O   . HOH K 3 .   ? 26.335 1.590   -30.408 1.00 43.07  ?  545 HOH A O   1 
HETATM 7279 O  O   . HOH K 3 .   ? 47.901 16.398  -12.057 1.00 40.58  ?  546 HOH A O   1 
HETATM 7280 O  O   . HOH K 3 .   ? 46.176 8.772   -39.555 1.00 29.40  ?  547 HOH A O   1 
HETATM 7281 O  O   . HOH K 3 .   ? 29.277 13.330  -28.953 1.00 45.05  ?  548 HOH A O   1 
HETATM 7282 O  O   . HOH K 3 .   ? 16.969 -9.629  -8.256  1.00 36.98  ?  549 HOH A O   1 
HETATM 7283 O  O   . HOH K 3 .   ? 28.432 6.428   -10.490 1.00 37.06  ?  550 HOH A O   1 
HETATM 7284 O  O   . HOH K 3 .   ? 40.379 -1.072  -11.717 1.00 23.94  ?  551 HOH A O   1 
HETATM 7285 O  O   . HOH K 3 .   ? 56.013 22.956  -17.963 1.00 22.04  ?  552 HOH A O   1 
HETATM 7286 O  O   . HOH K 3 .   ? 35.211 12.342  -27.544 1.00 49.33  ?  553 HOH A O   1 
HETATM 7287 O  O   . HOH K 3 .   ? 33.513 0.021   -34.073 1.00 25.47  ?  554 HOH A O   1 
HETATM 7288 O  O   . HOH K 3 .   ? 46.121 17.977  -15.463 1.00 44.64  ?  555 HOH A O   1 
HETATM 7289 O  O   . HOH K 3 .   ? 30.209 -15.377 -12.614 1.00 36.43  ?  556 HOH A O   1 
HETATM 7290 O  O   . HOH K 3 .   ? 50.762 13.431  -13.655 1.00 27.41  ?  557 HOH A O   1 
HETATM 7291 O  O   . HOH K 3 .   ? 26.527 -16.829 -12.361 1.00 38.49  ?  558 HOH A O   1 
HETATM 7292 O  O   . HOH K 3 .   ? 62.443 0.019   -39.958 1.00 41.98  ?  559 HOH A O   1 
HETATM 7293 O  O   . HOH K 3 .   ? 36.396 -2.960  -2.671  1.00 20.19  ?  560 HOH A O   1 
HETATM 7294 O  O   . HOH K 3 .   ? 28.023 -17.352 -9.005  1.00 18.81  ?  561 HOH A O   1 
HETATM 7295 O  O   . HOH K 3 .   ? 48.108 8.501   -40.478 1.00 32.39  ?  562 HOH A O   1 
HETATM 7296 O  O   . HOH K 3 .   ? 22.957 -2.333  -10.288 1.00 28.46  ?  563 HOH A O   1 
HETATM 7297 O  O   . HOH K 3 .   ? 21.499 -5.341  -0.320  1.00 45.56  ?  564 HOH A O   1 
HETATM 7298 O  O   . HOH K 3 .   ? 40.858 -7.155  -7.249  1.00 13.69  ?  565 HOH A O   1 
HETATM 7299 O  O   . HOH K 3 .   ? 44.799 -8.314  -37.602 1.00 31.14  ?  566 HOH A O   1 
HETATM 7300 O  O   . HOH K 3 .   ? 59.928 19.424  -32.370 1.00 30.45  ?  567 HOH A O   1 
HETATM 7301 O  O   . HOH K 3 .   ? 59.153 -22.598 -31.968 1.00 44.32  ?  568 HOH A O   1 
HETATM 7302 O  O   . HOH K 3 .   ? 27.346 3.224   -4.206  1.00 30.44  ?  569 HOH A O   1 
HETATM 7303 O  O   . HOH K 3 .   ? 43.033 10.807  -27.141 1.00 23.02  ?  570 HOH A O   1 
HETATM 7304 O  O   . HOH K 3 .   ? 62.956 15.732  -36.669 1.00 35.51  ?  571 HOH A O   1 
HETATM 7305 O  O   . HOH K 3 .   ? 34.635 10.347  -10.852 1.00 47.05  ?  572 HOH A O   1 
HETATM 7306 O  O   . HOH K 3 .   ? 26.317 -15.848 -24.470 1.00 40.60  ?  573 HOH A O   1 
HETATM 7307 O  O   . HOH K 3 .   ? 49.937 4.412   -42.717 1.00 39.59  ?  574 HOH A O   1 
HETATM 7308 O  O   . HOH K 3 .   ? 32.195 13.963  -28.593 1.00 37.21  ?  575 HOH A O   1 
HETATM 7309 O  O   . HOH K 3 .   ? 28.157 -3.007  0.091   1.00 32.26  ?  576 HOH A O   1 
HETATM 7310 O  O   . HOH K 3 .   ? 52.283 24.612  -20.025 1.00 35.92  ?  577 HOH A O   1 
HETATM 7311 O  O   . HOH K 3 .   ? 39.652 8.675   -40.418 1.00 41.06  ?  578 HOH A O   1 
HETATM 7312 O  O   . HOH K 3 .   ? 66.658 3.813   -23.423 1.00 38.90  ?  579 HOH A O   1 
HETATM 7313 O  O   . HOH K 3 .   ? 38.278 5.602   -9.302  1.00 29.21  ?  580 HOH A O   1 
HETATM 7314 O  O   . HOH K 3 .   ? 22.221 1.741   -12.483 1.00 31.32  ?  581 HOH A O   1 
HETATM 7315 O  O   . HOH K 3 .   ? 71.133 13.965  -34.842 1.00 38.89  ?  582 HOH A O   1 
HETATM 7316 O  O   . HOH K 3 .   ? 21.079 2.755   -10.193 1.00 44.50  ?  583 HOH A O   1 
HETATM 7317 O  O   . HOH K 3 .   ? 23.609 -5.012  -15.951 1.00 41.29  ?  584 HOH A O   1 
HETATM 7318 O  O   . HOH K 3 .   ? 32.507 -3.611  -34.612 1.00 38.77  ?  585 HOH A O   1 
HETATM 7319 O  O   . HOH K 3 .   ? 38.702 -17.103 -33.798 1.00 35.11  ?  586 HOH A O   1 
HETATM 7320 O  O   . HOH K 3 .   ? 49.904 -1.950  -17.821 1.00 24.44  ?  587 HOH A O   1 
HETATM 7321 O  O   . HOH K 3 .   ? 54.702 23.769  -16.080 1.00 41.40  ?  588 HOH A O   1 
HETATM 7322 O  O   . HOH K 3 .   ? 42.646 -6.576  -16.626 1.00 26.90  ?  589 HOH A O   1 
HETATM 7323 O  O   . HOH K 3 .   ? 36.090 3.984   -15.945 1.00 40.47  ?  590 HOH A O   1 
HETATM 7324 O  O   . HOH K 3 .   ? 33.888 -15.597 -30.848 1.00 28.97  ?  591 HOH A O   1 
HETATM 7325 O  O   . HOH K 3 .   ? 67.839 16.403  -34.935 1.00 28.23  ?  592 HOH A O   1 
HETATM 7326 O  O   . HOH K 3 .   ? 28.328 6.262   -24.410 1.00 45.36  ?  593 HOH A O   1 
HETATM 7327 O  O   . HOH K 3 .   ? 35.785 5.272   -18.037 1.00 41.00  ?  594 HOH A O   1 
HETATM 7328 O  O   . HOH K 3 .   ? 55.136 18.990  -38.994 1.00 42.64  ?  595 HOH A O   1 
HETATM 7329 O  O   . HOH K 3 .   ? 53.216 20.456  -11.141 1.00 37.57  ?  596 HOH A O   1 
HETATM 7330 O  O   . HOH K 3 .   ? 59.287 -0.165  -21.724 1.00 32.60  ?  597 HOH A O   1 
HETATM 7331 O  O   . HOH K 3 .   ? 42.983 0.745   -14.585 1.00 36.33  ?  598 HOH A O   1 
HETATM 7332 O  O   . HOH K 3 .   ? 61.365 16.194  -38.569 1.00 38.76  ?  599 HOH A O   1 
HETATM 7333 O  O   . HOH K 3 .   ? 62.924 9.003   -23.726 1.00 44.11  ?  600 HOH A O   1 
HETATM 7334 O  O   . HOH K 3 .   ? 41.462 15.313  -22.642 1.00 38.57  ?  601 HOH A O   1 
HETATM 7335 O  O   . HOH K 3 .   ? 43.606 -11.588 -40.754 1.00 38.58  ?  602 HOH A O   1 
HETATM 7336 O  O   . HOH K 3 .   ? 42.121 -11.711 -37.067 1.00 28.12  ?  603 HOH A O   1 
HETATM 7337 O  O   . HOH K 3 .   ? 45.467 -2.420  -13.730 1.00 35.86  ?  604 HOH A O   1 
HETATM 7338 O  O   . HOH K 3 .   ? 19.680 0.814   -10.802 1.00 50.83  ?  605 HOH A O   1 
HETATM 7339 O  O   . HOH K 3 .   ? 41.082 1.311   -13.048 1.00 32.86  ?  606 HOH A O   1 
HETATM 7340 O  O   . HOH K 3 .   ? 27.695 -16.728 -14.192 1.00 33.98  ?  607 HOH A O   1 
HETATM 7341 O  O   . HOH K 3 .   ? 36.116 -0.390  3.594   1.00 39.23  ?  608 HOH A O   1 
HETATM 7342 O  O   . HOH K 3 .   ? 60.760 22.753  -19.912 1.00 39.40  ?  609 HOH A O   1 
HETATM 7343 O  O   . HOH K 3 .   ? 40.860 14.873  -19.509 1.00 41.86  ?  610 HOH A O   1 
HETATM 7344 O  O   . HOH K 3 .   ? 24.115 -3.644  -1.062  1.00 40.30  ?  611 HOH A O   1 
HETATM 7345 O  O   . HOH K 3 .   ? 66.080 6.160   -21.063 1.00 38.02  ?  612 HOH A O   1 
HETATM 7346 O  O   . HOH K 3 .   ? 52.752 23.566  -12.933 1.00 35.24  ?  613 HOH A O   1 
HETATM 7347 O  O   . HOH K 3 .   ? 48.388 12.821  -11.205 1.00 34.33  ?  614 HOH A O   1 
HETATM 7348 O  O   . HOH K 3 .   ? 30.445 4.489   -6.782  1.00 35.55  ?  615 HOH A O   1 
HETATM 7349 O  O   . HOH K 3 .   ? 40.837 2.573   -10.825 1.00 28.84  ?  616 HOH A O   1 
HETATM 7350 O  O   . HOH K 3 .   ? 64.792 26.289  -24.054 1.00 29.35  ?  617 HOH A O   1 
HETATM 7351 O  O   . HOH K 3 .   ? 36.263 3.185   -19.389 1.00 36.83  ?  618 HOH A O   1 
HETATM 7352 O  O   . HOH K 3 .   ? 55.778 21.763  -15.708 1.00 31.40  ?  619 HOH A O   1 
HETATM 7353 O  O   . HOH K 3 .   ? 34.489 13.913  -24.947 1.00 35.80  ?  620 HOH A O   1 
HETATM 7354 O  O   . HOH K 3 .   ? 31.881 14.247  -24.936 1.00 43.25  ?  621 HOH A O   1 
HETATM 7355 O  O   . HOH K 3 .   ? 29.909 8.423   -11.274 1.00 29.48  ?  622 HOH A O   1 
HETATM 7356 O  O   . HOH K 3 .   ? 63.024 -11.846 -33.144 1.00 35.34  ?  623 HOH A O   1 
HETATM 7357 O  O   . HOH K 3 .   ? 66.021 -8.591  -34.224 1.00 43.75  ?  624 HOH A O   1 
HETATM 7358 O  O   . HOH K 3 .   ? 21.340 4.847   -5.943  1.00 37.94  ?  625 HOH A O   1 
HETATM 7359 O  O   . HOH K 3 .   ? 38.409 6.222   -11.582 1.00 34.33  ?  626 HOH A O   1 
HETATM 7360 O  O   . HOH K 3 .   ? 39.998 -4.620  -6.399  1.00 28.20  ?  627 HOH A O   1 
HETATM 7361 O  O   . HOH K 3 .   ? 39.332 -2.806  -2.469  1.00 29.76  ?  628 HOH A O   1 
HETATM 7362 O  O   . HOH K 3 .   ? 44.727 14.123  -29.685 1.00 26.59  ?  629 HOH A O   1 
HETATM 7363 O  O   . HOH K 3 .   ? 48.572 23.976  -15.416 1.00 35.27  ?  630 HOH A O   1 
HETATM 7364 O  O   . HOH K 3 .   ? 38.170 12.125  -10.380 1.00 38.91  ?  631 HOH A O   1 
HETATM 7365 O  O   . HOH K 3 .   ? 62.769 24.509  -20.517 1.00 38.27  ?  632 HOH A O   1 
HETATM 7366 O  O   . HOH K 3 .   ? 47.256 22.797  -17.834 1.00 44.33  ?  633 HOH A O   1 
HETATM 7367 O  O   . HOH K 3 .   ? 45.611 20.755  -20.442 1.00 35.56  ?  634 HOH A O   1 
HETATM 7368 O  O   . HOH K 3 .   ? 40.091 10.616  -16.411 1.00 43.39  ?  635 HOH A O   1 
HETATM 7369 O  O   . HOH K 3 .   ? 37.534 15.782  -23.665 1.00 31.77  ?  636 HOH A O   1 
HETATM 7370 O  O   . HOH K 3 .   ? 57.954 29.754  -21.854 1.00 43.24  ?  637 HOH A O   1 
HETATM 7371 O  O   . HOH K 3 .   ? 46.053 6.106   -15.498 1.00 25.83  ?  638 HOH A O   1 
HETATM 7372 O  O   . HOH K 3 .   ? 28.168 5.958   -6.843  1.00 46.84  ?  639 HOH A O   1 
HETATM 7373 O  O   . HOH K 3 .   ? 61.545 26.973  -21.594 1.00 39.42  ?  640 HOH A O   1 
HETATM 7374 O  O   . HOH K 3 .   ? 55.823 30.539  -20.937 1.00 41.64  ?  641 HOH A O   1 
HETATM 7375 O  O   . HOH K 3 .   ? 40.637 -1.409  -0.981  1.00 27.06  ?  642 HOH A O   1 
HETATM 7376 O  O   . HOH K 3 .   ? 19.728 4.975   -7.990  1.00 55.65  ?  643 HOH A O   1 
HETATM 7377 O  O   . HOH K 3 .   ? 19.351 4.444   -10.504 1.00 50.13  ?  644 HOH A O   1 
HETATM 7378 O  O   . HOH K 3 .   ? 40.866 -3.961  -4.130  1.00 20.36  ?  645 HOH A O   1 
HETATM 7379 O  O   . HOH K 3 .   ? 35.268 12.593  -11.525 1.00 40.21  ?  646 HOH A O   1 
HETATM 7380 O  O   . HOH K 3 .   ? 56.326 26.919  -17.188 1.00 43.75  ?  647 HOH A O   1 
HETATM 7381 O  O   . HOH K 3 .   ? 35.883 15.189  -27.389 1.00 43.43  ?  648 HOH A O   1 
HETATM 7382 O  O   . HOH K 3 .   ? 29.758 -17.065 -31.025 1.00 38.26  ?  649 HOH A O   1 
HETATM 7383 O  O   . HOH K 3 .   ? 38.707 -16.882 -38.259 1.00 40.85  ?  650 HOH A O   1 
HETATM 7384 O  O   . HOH K 3 .   ? 52.072 28.589  -18.133 1.00 36.63  ?  651 HOH A O   1 
HETATM 7385 O  O   . HOH K 3 .   ? 30.308 13.828  -22.672 1.00 45.23  ?  652 HOH A O   1 
HETATM 7386 O  O   . HOH K 3 .   ? 38.823 14.380  -8.824  1.00 39.42  ?  653 HOH A O   1 
HETATM 7387 O  O   . HOH K 3 .   ? 38.128 8.909   -15.657 1.00 31.44  ?  654 HOH A O   1 
HETATM 7388 O  O   . HOH K 3 .   ? 47.696 16.552  -8.440  1.00 46.19  ?  655 HOH A O   1 
HETATM 7389 O  O   . HOH K 3 .   ? 56.288 26.146  -14.705 1.00 39.27  ?  656 HOH A O   1 
HETATM 7390 O  O   . HOH K 3 .   ? 39.082 9.257   -13.889 1.00 38.11  ?  657 HOH A O   1 
HETATM 7391 O  O   . HOH K 3 .   ? 31.495 14.206  -14.239 1.00 43.10  ?  658 HOH A O   1 
HETATM 7392 O  O   . HOH K 3 .   ? 27.369 13.472  -13.238 1.00 41.02  ?  659 HOH A O   1 
HETATM 7393 O  O   . HOH K 3 .   ? 26.050 14.993  -14.793 1.00 49.13  ?  660 HOH A O   1 
HETATM 7394 O  O   . HOH L 3 .   ? 36.490 -12.909 -3.088  1.00 41.06  ?  401 HOH C O   1 
HETATM 7395 O  O   . HOH L 3 .   ? 47.902 3.561   -11.689 1.00 39.99  ?  402 HOH C O   1 
HETATM 7396 O  O   . HOH L 3 .   ? 40.487 -9.303  -23.591 1.00 32.44  ?  403 HOH C O   1 
HETATM 7397 O  O   . HOH L 3 .   ? 29.630 -25.001 -17.809 1.00 29.76  ?  404 HOH C O   1 
HETATM 7398 O  O   . HOH L 3 .   ? 64.302 21.677  -9.205  1.00 49.52  ?  405 HOH C O   1 
HETATM 7399 O  O   . HOH L 3 .   ? 56.855 -22.822 -26.148 1.00 41.03  ?  406 HOH C O   1 
HETATM 7400 O  O   . HOH L 3 .   ? 58.398 17.292  -8.424  1.00 15.54  ?  407 HOH C O   1 
HETATM 7401 O  O   . HOH L 3 .   ? 40.023 -16.888 -31.361 1.00 41.08  ?  408 HOH C O   1 
HETATM 7402 O  O   . HOH L 3 .   ? 26.124 -30.533 -15.466 1.00 34.74  ?  409 HOH C O   1 
HETATM 7403 O  O   . HOH L 3 .   ? 43.435 -32.780 -25.359 1.00 22.69  ?  410 HOH C O   1 
HETATM 7404 O  O   . HOH L 3 .   ? 44.331 0.009   -6.571  1.00 41.57  ?  411 HOH C O   1 
HETATM 7405 O  O   . HOH L 3 .   ? 68.029 -1.037  -12.759 1.00 39.06  ?  412 HOH C O   1 
HETATM 7406 O  O   . HOH L 3 .   ? 47.124 -15.023 -7.145  1.00 22.37  ?  413 HOH C O   1 
HETATM 7407 O  O   . HOH L 3 .   ? 51.532 -19.756 -30.709 1.00 26.49  ?  414 HOH C O   1 
HETATM 7408 O  O   . HOH L 3 .   ? 59.209 -13.018 -28.589 1.00 33.39  ?  415 HOH C O   1 
HETATM 7409 O  O   . HOH L 3 .   ? 63.707 -13.692 -15.837 1.00 38.67  ?  416 HOH C O   1 
HETATM 7410 O  O   . HOH L 3 .   ? 63.399 4.329   -9.325  1.00 28.91  ?  417 HOH C O   1 
HETATM 7411 O  O   . HOH L 3 .   ? 63.041 -8.575  -14.793 1.00 30.76  ?  418 HOH C O   1 
HETATM 7412 O  O   . HOH L 3 .   ? 60.406 19.639  -15.539 1.00 26.30  ?  419 HOH C O   1 
HETATM 7413 O  O   . HOH L 3 .   ? 64.508 -21.821 -12.853 1.00 36.55  ?  420 HOH C O   1 
HETATM 7414 O  O   . HOH L 3 .   ? 32.658 -13.966 4.127   1.00 23.31  ?  421 HOH C O   1 
HETATM 7415 O  O   . HOH L 3 .   ? 36.736 -23.515 -28.817 1.00 19.40  ?  422 HOH C O   1 
HETATM 7416 O  O   . HOH L 3 .   ? 47.942 2.159   -6.483  1.00 32.91  ?  423 HOH C O   1 
HETATM 7417 O  O   . HOH L 3 .   ? 39.819 -33.152 -8.136  1.00 35.52  ?  424 HOH C O   1 
HETATM 7418 O  O   . HOH L 3 .   ? 31.187 -23.272 -22.196 1.00 23.17  ?  425 HOH C O   1 
HETATM 7419 O  O   . HOH L 3 .   ? 48.102 -26.226 -26.636 1.00 34.77  ?  426 HOH C O   1 
HETATM 7420 O  O   . HOH L 3 .   ? 42.343 -20.870 -13.310 1.00 13.87  ?  427 HOH C O   1 
HETATM 7421 O  O   . HOH L 3 .   ? 45.548 -22.553 -4.577  1.00 24.79  ?  428 HOH C O   1 
HETATM 7422 O  O   . HOH L 3 .   ? 50.152 9.277   -13.016 1.00 13.75  ?  429 HOH C O   1 
HETATM 7423 O  O   . HOH L 3 .   ? 55.341 -26.828 -10.821 1.00 23.42  ?  430 HOH C O   1 
HETATM 7424 O  O   . HOH L 3 .   ? 60.996 10.365  -19.127 1.00 20.66  ?  431 HOH C O   1 
HETATM 7425 O  O   . HOH L 3 .   ? 38.716 -16.055 -28.915 1.00 22.88  ?  432 HOH C O   1 
HETATM 7426 O  O   . HOH L 3 .   ? 46.312 -6.785  -14.098 1.00 25.54  ?  433 HOH C O   1 
HETATM 7427 O  O   . HOH L 3 .   ? 55.371 -5.802  -21.334 1.00 32.06  ?  434 HOH C O   1 
HETATM 7428 O  O   . HOH L 3 .   ? 48.288 -15.858 -9.788  1.00 17.06  ?  435 HOH C O   1 
HETATM 7429 O  O   . HOH L 3 .   ? 40.666 -8.872  0.384   1.00 26.19  ?  436 HOH C O   1 
HETATM 7430 O  O   . HOH L 3 .   ? 38.049 -13.669 -20.489 1.00 17.76  ?  437 HOH C O   1 
HETATM 7431 O  O   . HOH L 3 .   ? 46.738 -20.352 -31.442 1.00 25.82  ?  438 HOH C O   1 
HETATM 7432 O  O   . HOH L 3 .   ? 35.872 -26.830 -27.192 1.00 31.43  ?  439 HOH C O   1 
HETATM 7433 O  O   . HOH L 3 .   ? 39.554 -29.131 -18.619 1.00 16.64  ?  440 HOH C O   1 
HETATM 7434 O  O   . HOH L 3 .   ? 43.964 -15.974 3.595   1.00 34.19  ?  441 HOH C O   1 
HETATM 7435 O  O   . HOH L 3 .   ? 45.851 -31.313 -11.275 1.00 43.96  ?  442 HOH C O   1 
HETATM 7436 O  O   . HOH L 3 .   ? 39.349 -21.731 -33.217 1.00 25.45  ?  443 HOH C O   1 
HETATM 7437 O  O   . HOH L 3 .   ? 60.976 -21.957 -8.595  1.00 31.76  ?  444 HOH C O   1 
HETATM 7438 O  O   . HOH L 3 .   ? 41.484 -19.186 0.406   1.00 27.56  ?  445 HOH C O   1 
HETATM 7439 O  O   . HOH L 3 .   ? 45.503 -32.566 -23.701 1.00 29.84  ?  446 HOH C O   1 
HETATM 7440 O  O   . HOH L 3 .   ? 35.692 -29.518 -18.245 1.00 17.27  ?  447 HOH C O   1 
HETATM 7441 O  O   . HOH L 3 .   ? 56.977 1.984   0.679   1.00 29.75  ?  448 HOH C O   1 
HETATM 7442 O  O   . HOH L 3 .   ? 57.689 -10.160 -26.443 1.00 25.15  ?  449 HOH C O   1 
HETATM 7443 O  O   . HOH L 3 .   ? 52.202 -22.435 -5.052  1.00 46.04  ?  450 HOH C O   1 
HETATM 7444 O  O   . HOH L 3 .   ? 39.884 -13.729 1.997   1.00 25.01  ?  451 HOH C O   1 
HETATM 7445 O  O   . HOH L 3 .   ? 57.335 -0.437  -0.502  1.00 33.81  ?  452 HOH C O   1 
HETATM 7446 O  O   . HOH L 3 .   ? 59.809 -9.686  -3.007  1.00 33.33  ?  453 HOH C O   1 
HETATM 7447 O  O   . HOH L 3 .   ? 47.707 -7.078  -6.313  1.00 23.21  ?  454 HOH C O   1 
HETATM 7448 O  O   . HOH L 3 .   ? 37.643 -33.292 -21.161 1.00 22.53  ?  455 HOH C O   1 
HETATM 7449 O  O   . HOH L 3 .   ? 47.613 -9.604  -14.959 1.00 18.53  ?  456 HOH C O   1 
HETATM 7450 O  O   . HOH L 3 .   ? 61.962 -5.346  -1.194  1.00 37.67  ?  457 HOH C O   1 
HETATM 7451 O  O   . HOH L 3 .   ? 38.020 -18.358 2.351   1.00 38.17  ?  458 HOH C O   1 
HETATM 7452 O  O   . HOH L 3 .   ? 60.995 20.388  -18.970 1.00 33.10  ?  459 HOH C O   1 
HETATM 7453 O  O   . HOH L 3 .   ? 45.941 -8.730  -2.272  1.00 40.76  ?  460 HOH C O   1 
HETATM 7454 O  O   . HOH L 3 .   ? 48.376 -9.406  -24.718 1.00 17.82  ?  461 HOH C O   1 
HETATM 7455 O  O   . HOH L 3 .   ? 41.261 -12.915 -29.059 1.00 24.61  ?  462 HOH C O   1 
HETATM 7456 O  O   . HOH L 3 .   ? 69.836 -2.812  -21.839 1.00 30.52  ?  463 HOH C O   1 
HETATM 7457 O  O   . HOH L 3 .   ? 65.381 -2.483  -11.292 1.00 24.27  ?  464 HOH C O   1 
HETATM 7458 O  O   . HOH L 3 .   ? 26.731 -31.598 -9.267  1.00 37.18  ?  465 HOH C O   1 
HETATM 7459 O  O   . HOH L 3 .   ? 57.662 15.458  -6.396  1.00 24.89  ?  466 HOH C O   1 
HETATM 7460 O  O   . HOH L 3 .   ? 45.351 -22.557 -34.605 1.00 40.17  ?  467 HOH C O   1 
HETATM 7461 O  O   . HOH L 3 .   ? 57.052 -25.462 -21.849 1.00 32.13  ?  468 HOH C O   1 
HETATM 7462 O  O   . HOH L 3 .   ? 57.713 -7.731  -5.657  1.00 44.89  ?  469 HOH C O   1 
HETATM 7463 O  O   . HOH L 3 .   ? 47.146 3.330   -14.424 1.00 30.17  ?  470 HOH C O   1 
HETATM 7464 O  O   . HOH L 3 .   ? 48.210 -8.567  -18.650 1.00 19.64  ?  471 HOH C O   1 
HETATM 7465 O  O   . HOH L 3 .   ? 43.040 -12.804 -34.406 1.00 22.25  ?  472 HOH C O   1 
HETATM 7466 O  O   . HOH L 3 .   ? 47.048 -30.287 -25.035 1.00 24.68  ?  473 HOH C O   1 
HETATM 7467 O  O   . HOH L 3 .   ? 48.977 -20.943 -5.981  1.00 30.76  ?  474 HOH C O   1 
HETATM 7468 O  O   . HOH L 3 .   ? 49.332 2.165   -8.514  1.00 39.37  ?  475 HOH C O   1 
HETATM 7469 O  O   . HOH L 3 .   ? 36.583 -33.118 -18.217 1.00 38.25  ?  476 HOH C O   1 
HETATM 7470 O  O   . HOH L 3 .   ? 43.745 9.087   -3.732  1.00 35.38  ?  477 HOH C O   1 
HETATM 7471 O  O   . HOH L 3 .   ? 50.185 -17.802 -39.142 1.00 30.16  ?  478 HOH C O   1 
HETATM 7472 O  O   . HOH L 3 .   ? 53.223 3.618   -1.556  1.00 34.51  ?  479 HOH C O   1 
HETATM 7473 O  O   . HOH L 3 .   ? 60.662 8.181   -15.387 1.00 18.18  ?  480 HOH C O   1 
HETATM 7474 O  O   . HOH L 3 .   ? 29.939 -20.014 -23.081 1.00 33.66  ?  481 HOH C O   1 
HETATM 7475 O  O   . HOH L 3 .   ? 51.488 -2.519  -15.823 1.00 11.23  ?  482 HOH C O   1 
HETATM 7476 O  O   . HOH L 3 .   ? 70.024 7.428   -18.072 1.00 41.86  ?  483 HOH C O   1 
HETATM 7477 O  O   . HOH L 3 .   ? 53.356 -1.913  -4.560  1.00 24.89  ?  484 HOH C O   1 
HETATM 7478 O  O   . HOH L 3 .   ? 64.568 13.608  -17.610 1.00 34.21  ?  485 HOH C O   1 
HETATM 7479 O  O   . HOH L 3 .   ? 34.301 -15.117 -21.786 1.00 26.57  ?  486 HOH C O   1 
HETATM 7480 O  O   . HOH L 3 .   ? 49.948 -11.886 -23.834 1.00 18.24  ?  487 HOH C O   1 
HETATM 7481 O  O   . HOH L 3 .   ? 67.131 -13.423 -8.165  1.00 30.53  ?  488 HOH C O   1 
HETATM 7482 O  O   . HOH L 3 .   ? 54.068 -29.373 -16.392 1.00 37.87  ?  489 HOH C O   1 
HETATM 7483 O  O   . HOH L 3 .   ? 56.676 -7.476  -8.029  1.00 19.79  ?  490 HOH C O   1 
HETATM 7484 O  O   . HOH L 3 .   ? 62.702 4.678   -6.842  1.00 43.50  ?  491 HOH C O   1 
HETATM 7485 O  O   . HOH L 3 .   ? 45.554 -6.229  -11.240 1.00 36.26  ?  492 HOH C O   1 
HETATM 7486 O  O   . HOH L 3 .   ? 45.166 -7.791  -9.249  1.00 23.60  ?  493 HOH C O   1 
HETATM 7487 O  O   . HOH L 3 .   ? 64.523 -19.384 -19.716 1.00 36.32  ?  494 HOH C O   1 
HETATM 7488 O  O   . HOH L 3 .   ? 50.816 -11.008 -40.372 1.00 35.97  ?  495 HOH C O   1 
HETATM 7489 O  O   . HOH L 3 .   ? 39.998 -7.361  -4.292  1.00 15.56  ?  496 HOH C O   1 
HETATM 7490 O  O   . HOH L 3 .   ? 29.809 -22.016 -0.871  1.00 32.25  ?  497 HOH C O   1 
HETATM 7491 O  O   . HOH L 3 .   ? 62.045 -21.276 -6.289  1.00 33.85  ?  498 HOH C O   1 
HETATM 7492 O  O   . HOH L 3 .   ? 60.939 -15.348 -11.743 1.00 19.27  ?  499 HOH C O   1 
HETATM 7493 O  O   . HOH L 3 .   ? 49.224 10.547  -8.443  1.00 23.12  ?  500 HOH C O   1 
HETATM 7494 O  O   . HOH L 3 .   ? 52.764 11.859  -13.409 1.00 16.01  ?  501 HOH C O   1 
HETATM 7495 O  O   . HOH L 3 .   ? 39.169 -14.023 -26.696 1.00 20.89  ?  502 HOH C O   1 
HETATM 7496 O  O   . HOH L 3 .   ? 36.812 -21.066 -0.425  1.00 34.59  ?  503 HOH C O   1 
HETATM 7497 O  O   . HOH L 3 .   ? 59.008 -14.542 -21.811 1.00 17.84  ?  504 HOH C O   1 
HETATM 7498 O  O   . HOH L 3 .   ? 44.047 -10.867 -38.139 1.00 26.81  ?  505 HOH C O   1 
HETATM 7499 O  O   . HOH L 3 .   ? 30.352 -23.274 2.225   1.00 30.65  ?  506 HOH C O   1 
HETATM 7500 O  O   . HOH L 3 .   ? 61.929 23.719  -6.562  1.00 42.08  ?  507 HOH C O   1 
HETATM 7501 O  O   . HOH L 3 .   ? 65.865 -7.401  -23.678 1.00 29.31  ?  508 HOH C O   1 
HETATM 7502 O  O   . HOH L 3 .   ? 49.795 -17.655 -8.202  1.00 20.27  ?  509 HOH C O   1 
HETATM 7503 O  O   . HOH L 3 .   ? 63.366 -9.993  -17.601 1.00 32.29  ?  510 HOH C O   1 
HETATM 7504 O  O   . HOH L 3 .   ? 34.127 -18.021 -13.442 1.00 43.44  ?  511 HOH C O   1 
HETATM 7505 O  O   . HOH L 3 .   ? 31.443 -32.625 -13.894 1.00 30.63  ?  512 HOH C O   1 
HETATM 7506 O  O   . HOH L 3 .   ? 45.496 4.585   -1.243  1.00 38.56  ?  513 HOH C O   1 
HETATM 7507 O  O   . HOH L 3 .   ? 52.693 13.822  -3.543  1.00 42.66  ?  514 HOH C O   1 
HETATM 7508 O  O   . HOH L 3 .   ? 42.917 -28.081 -5.863  1.00 23.13  ?  515 HOH C O   1 
HETATM 7509 O  O   . HOH L 3 .   ? 63.744 -16.909 -18.966 1.00 24.89  ?  516 HOH C O   1 
HETATM 7510 O  O   . HOH L 3 .   ? 52.795 12.292  -10.577 1.00 24.30  ?  517 HOH C O   1 
HETATM 7511 O  O   . HOH L 3 .   ? 41.879 -11.008 1.195   1.00 36.74  ?  518 HOH C O   1 
HETATM 7512 O  O   . HOH L 3 .   ? 62.181 7.830   -19.839 1.00 27.61  ?  519 HOH C O   1 
HETATM 7513 O  O   . HOH L 3 .   ? 68.608 22.469  -19.943 1.00 30.11  ?  520 HOH C O   1 
HETATM 7514 O  O   . HOH L 3 .   ? 60.776 -25.441 -17.909 1.00 40.37  ?  521 HOH C O   1 
HETATM 7515 O  O   . HOH L 3 .   ? 59.397 6.558   -22.856 1.00 34.29  ?  522 HOH C O   1 
HETATM 7516 O  O   . HOH L 3 .   ? 31.520 -18.387 3.264   1.00 23.76  ?  523 HOH C O   1 
HETATM 7517 O  O   . HOH L 3 .   ? 43.691 -30.015 -28.475 1.00 29.25  ?  524 HOH C O   1 
HETATM 7518 O  O   . HOH L 3 .   ? 67.623 12.198  -15.132 1.00 28.94  ?  525 HOH C O   1 
HETATM 7519 O  O   . HOH L 3 .   ? 45.568 -7.194  -18.634 1.00 18.52  ?  526 HOH C O   1 
HETATM 7520 O  O   . HOH L 3 .   ? 60.761 4.780   -16.385 1.00 19.85  ?  527 HOH C O   1 
HETATM 7521 O  O   . HOH L 3 .   ? 51.973 -10.606 -4.559  1.00 27.96  ?  528 HOH C O   1 
HETATM 7522 O  O   . HOH L 3 .   ? 36.904 -34.894 -8.717  1.00 46.28  ?  529 HOH C O   1 
HETATM 7523 O  O   . HOH L 3 .   ? 48.271 7.247   -14.862 1.00 18.15  ?  530 HOH C O   1 
HETATM 7524 O  O   . HOH L 3 .   ? 59.138 -4.448  -24.661 1.00 27.03  ?  531 HOH C O   1 
HETATM 7525 O  O   . HOH L 3 .   ? 39.093 -12.259 -22.762 1.00 14.76  ?  532 HOH C O   1 
HETATM 7526 O  O   . HOH L 3 .   ? 63.986 -7.408  -3.387  1.00 41.79  ?  533 HOH C O   1 
HETATM 7527 O  O   . HOH L 3 .   ? 26.724 -26.751 -4.521  1.00 27.93  ?  534 HOH C O   1 
HETATM 7528 O  O   . HOH L 3 .   ? 39.700 -30.424 -25.870 1.00 32.09  ?  535 HOH C O   1 
HETATM 7529 O  O   . HOH L 3 .   ? 63.048 -14.764 -13.282 1.00 29.43  ?  536 HOH C O   1 
HETATM 7530 O  O   . HOH L 3 .   ? 66.868 21.354  -15.783 1.00 37.20  ?  537 HOH C O   1 
HETATM 7531 O  O   . HOH L 3 .   ? 36.834 -29.440 -25.999 1.00 27.28  ?  538 HOH C O   1 
HETATM 7532 O  O   . HOH L 3 .   ? 41.208 -28.223 -32.889 1.00 44.86  ?  539 HOH C O   1 
HETATM 7533 O  O   . HOH L 3 .   ? 51.409 -29.042 -12.013 1.00 28.41  ?  540 HOH C O   1 
HETATM 7534 O  O   . HOH L 3 .   ? 28.642 -28.643 -2.235  1.00 31.31  ?  541 HOH C O   1 
HETATM 7535 O  O   . HOH L 3 .   ? 56.076 -20.472 -25.927 1.00 31.40  ?  542 HOH C O   1 
HETATM 7536 O  O   . HOH L 3 .   ? 44.683 -9.580  -11.973 1.00 15.68  ?  543 HOH C O   1 
HETATM 7537 O  O   . HOH L 3 .   ? 64.517 -14.153 -5.707  1.00 30.13  ?  544 HOH C O   1 
HETATM 7538 O  O   . HOH L 3 .   ? 62.549 7.387   -3.468  1.00 44.98  ?  545 HOH C O   1 
HETATM 7539 O  O   . HOH L 3 .   ? 68.164 -5.077  -11.602 1.00 43.73  ?  546 HOH C O   1 
HETATM 7540 O  O   . HOH L 3 .   ? 32.052 -16.140 -18.866 1.00 54.04  ?  547 HOH C O   1 
HETATM 7541 O  O   . HOH L 3 .   ? 62.720 -17.380 -13.602 1.00 25.48  ?  548 HOH C O   1 
HETATM 7542 O  O   . HOH L 3 .   ? 43.609 8.333   -6.814  1.00 40.83  ?  549 HOH C O   1 
HETATM 7543 O  O   . HOH L 3 .   ? 37.951 -7.046  -1.485  1.00 39.90  ?  550 HOH C O   1 
HETATM 7544 O  O   . HOH L 3 .   ? 48.437 1.200   -10.673 1.00 20.47  ?  551 HOH C O   1 
HETATM 7545 O  O   . HOH L 3 .   ? 32.925 -16.911 -20.794 1.00 19.69  ?  552 HOH C O   1 
HETATM 7546 O  O   . HOH L 3 .   ? 62.904 12.764  -19.546 1.00 21.55  ?  553 HOH C O   1 
HETATM 7547 O  O   . HOH L 3 .   ? 59.611 16.087  -4.350  1.00 40.91  ?  554 HOH C O   1 
HETATM 7548 O  O   . HOH L 3 .   ? 50.280 -20.034 -39.957 1.00 44.89  ?  555 HOH C O   1 
HETATM 7549 O  O   . HOH L 3 .   ? 51.793 -21.166 -35.131 1.00 40.23  ?  556 HOH C O   1 
HETATM 7550 O  O   . HOH L 3 .   ? 40.206 -26.606 -2.377  1.00 43.22  ?  557 HOH C O   1 
HETATM 7551 O  O   . HOH L 3 .   ? 47.521 0.807   -12.037 1.00 33.27  ?  558 HOH C O   1 
HETATM 7552 O  O   . HOH L 3 .   ? 67.905 10.923  -16.887 1.00 35.84  ?  559 HOH C O   1 
HETATM 7553 O  O   . HOH L 3 .   ? 64.337 22.891  -15.624 1.00 40.65  ?  560 HOH C O   1 
HETATM 7554 O  O   . HOH L 3 .   ? 42.657 -26.057 -34.777 1.00 37.24  ?  561 HOH C O   1 
HETATM 7555 O  O   . HOH L 3 .   ? 59.498 -17.719 -27.947 1.00 36.76  ?  562 HOH C O   1 
HETATM 7556 O  O   . HOH L 3 .   ? 26.004 -29.713 -1.822  1.00 47.78  ?  563 HOH C O   1 
HETATM 7557 O  O   . HOH L 3 .   ? 42.422 -7.338  -1.807  1.00 30.37  ?  564 HOH C O   1 
HETATM 7558 O  O   . HOH L 3 .   ? 55.065 -6.812  -4.411  1.00 40.80  ?  565 HOH C O   1 
HETATM 7559 O  O   . HOH L 3 .   ? 28.839 -25.377 3.478   1.00 42.03  ?  566 HOH C O   1 
HETATM 7560 O  O   . HOH L 3 .   ? 38.466 -28.206 -28.620 1.00 34.73  ?  567 HOH C O   1 
HETATM 7561 O  O   . HOH L 3 .   ? 45.429 0.242   -15.492 1.00 31.81  ?  568 HOH C O   1 
HETATM 7562 O  O   . HOH L 3 .   ? 42.367 -26.300 -3.711  1.00 32.13  ?  569 HOH C O   1 
HETATM 7563 O  O   . HOH L 3 .   ? 46.524 -37.685 -14.013 1.00 43.64  ?  570 HOH C O   1 
HETATM 7564 O  O   . HOH L 3 .   ? 43.467 1.009   -2.082  1.00 37.72  ?  571 HOH C O   1 
HETATM 7565 O  O   . HOH L 3 .   ? 51.826 -12.071 -38.711 1.00 43.31  ?  572 HOH C O   1 
HETATM 7566 O  O   . HOH L 3 .   ? 58.358 -24.838 -24.062 1.00 36.54  ?  573 HOH C O   1 
HETATM 7567 O  O   . HOH L 3 .   ? 33.008 -21.968 -31.086 1.00 35.18  ?  574 HOH C O   1 
HETATM 7568 O  O   . HOH L 3 .   ? 40.293 -17.374 1.886   1.00 29.50  ?  575 HOH C O   1 
HETATM 7569 O  O   . HOH L 3 .   ? 54.879 15.637  -6.172  1.00 28.32  ?  576 HOH C O   1 
HETATM 7570 O  O   . HOH L 3 .   ? 40.817 -23.737 -34.562 1.00 30.31  ?  577 HOH C O   1 
HETATM 7571 O  O   . HOH L 3 .   ? 32.989 -32.371 -16.110 1.00 45.14  ?  578 HOH C O   1 
HETATM 7572 O  O   . HOH L 3 .   ? 46.045 -32.482 -29.370 1.00 32.11  ?  579 HOH C O   1 
HETATM 7573 O  O   . HOH L 3 .   ? 53.964 -32.322 -26.887 1.00 46.81  ?  580 HOH C O   1 
HETATM 7574 O  O   . HOH L 3 .   ? 39.290 -31.196 -6.349  1.00 31.33  ?  581 HOH C O   1 
HETATM 7575 O  O   . HOH L 3 .   ? 54.344 -7.255  -6.977  1.00 30.67  ?  582 HOH C O   1 
HETATM 7576 O  O   . HOH L 3 .   ? 50.631 -7.236  -5.539  1.00 43.85  ?  583 HOH C O   1 
HETATM 7577 O  O   . HOH L 3 .   ? 57.028 21.819  -7.856  1.00 36.84  ?  584 HOH C O   1 
HETATM 7578 O  O   . HOH L 3 .   ? 30.428 -19.686 -12.630 1.00 49.08  ?  585 HOH C O   1 
HETATM 7579 O  O   . HOH L 3 .   ? 47.362 -2.290  -17.961 1.00 29.34  ?  586 HOH C O   1 
HETATM 7580 O  O   . HOH L 3 .   ? 44.793 -31.487 -26.910 1.00 25.42  ?  587 HOH C O   1 
HETATM 7581 O  O   . HOH L 3 .   ? 46.427 -1.272  -11.807 1.00 45.70  ?  588 HOH C O   1 
HETATM 7582 O  O   . HOH L 3 .   ? 59.617 -21.504 -29.218 1.00 36.77  ?  589 HOH C O   1 
HETATM 7583 O  O   . HOH L 3 .   ? 44.982 -0.380  -13.395 1.00 35.73  ?  590 HOH C O   1 
HETATM 7584 O  O   . HOH L 3 .   ? 70.253 0.084   -21.549 1.00 39.40  ?  591 HOH C O   1 
HETATM 7585 O  O   . HOH L 3 .   ? 24.169 -27.160 -5.034  1.00 33.96  ?  592 HOH C O   1 
HETATM 7586 O  O   . HOH L 3 .   ? 41.095 -15.455 3.551   1.00 30.75  ?  593 HOH C O   1 
HETATM 7587 O  O   . HOH L 3 .   ? 34.494 -13.227 -19.882 1.00 39.94  ?  594 HOH C O   1 
HETATM 7588 O  O   . HOH L 3 .   ? 41.272 -30.259 -5.324  1.00 35.01  ?  595 HOH C O   1 
HETATM 7589 O  O   . HOH L 3 .   ? 28.793 -19.665 2.649   1.00 44.30  ?  596 HOH C O   1 
HETATM 7590 O  O   . HOH L 3 .   ? 31.029 -15.687 2.660   1.00 24.42  ?  597 HOH C O   1 
HETATM 7591 O  O   . HOH L 3 .   ? 68.430 19.760  -12.186 1.00 40.61  ?  598 HOH C O   1 
HETATM 7592 O  O   . HOH L 3 .   ? 64.802 8.257   -20.989 1.00 36.44  ?  599 HOH C O   1 
HETATM 7593 O  O   . HOH L 3 .   ? 48.099 -28.198 -34.113 1.00 41.02  ?  600 HOH C O   1 
HETATM 7594 O  O   . HOH L 3 .   ? 68.008 21.591  -12.865 1.00 42.74  ?  601 HOH C O   1 
HETATM 7595 O  O   . HOH L 3 .   ? 50.578 11.036  -10.689 1.00 29.18  ?  602 HOH C O   1 
HETATM 7596 O  O   . HOH L 3 .   ? 51.817 -3.933  -5.835  1.00 33.60  ?  603 HOH C O   1 
HETATM 7597 O  O   . HOH L 3 .   ? 60.797 23.539  -15.688 1.00 47.48  ?  604 HOH C O   1 
HETATM 7598 O  O   . HOH L 3 .   ? 44.597 -25.002 -2.829  1.00 44.54  ?  605 HOH C O   1 
HETATM 7599 O  O   . HOH L 3 .   ? 32.272 -17.550 -30.771 1.00 26.55  ?  606 HOH C O   1 
HETATM 7600 O  O   . HOH L 3 .   ? 42.488 -23.125 -35.960 1.00 35.26  ?  607 HOH C O   1 
HETATM 7601 O  O   . HOH L 3 .   ? 43.221 -6.754  -7.675  1.00 22.28  ?  608 HOH C O   1 
HETATM 7602 O  O   . HOH L 3 .   ? 59.741 -24.124 -7.158  1.00 27.74  ?  609 HOH C O   1 
HETATM 7603 O  O   . HOH L 3 .   ? 64.469 25.219  -17.506 1.00 43.02  ?  610 HOH C O   1 
HETATM 7604 O  O   . HOH L 3 .   ? 28.961 -19.659 -28.761 1.00 37.01  ?  611 HOH C O   1 
HETATM 7605 O  O   . HOH L 3 .   ? 56.309 -31.579 -31.123 1.00 41.37  ?  612 HOH C O   1 
HETATM 7606 O  O   . HOH L 3 .   ? 28.907 -19.471 -25.935 1.00 43.28  ?  613 HOH C O   1 
HETATM 7607 O  O   . HOH L 3 .   ? 43.524 -5.871  -4.598  1.00 38.07  ?  614 HOH C O   1 
HETATM 7608 O  O   . HOH L 3 .   ? 48.551 -2.725  -3.877  1.00 42.61  ?  615 HOH C O   1 
HETATM 7609 O  O   . HOH L 3 .   ? 43.345 -1.907  -0.612  1.00 39.63  ?  616 HOH C O   1 
HETATM 7610 O  O   . HOH L 3 .   ? 61.261 26.209  -14.320 1.00 45.66  ?  617 HOH C O   1 
# 
