data_3QQD
# 
_entry.id   3QQD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3QQD         
RCSB  RCSB063970   
WWPDB D_1000063970 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2011-03-09 
_pdbx_database_PDB_obs_spr.pdb_id           3QQD 
_pdbx_database_PDB_obs_spr.replace_pdb_id   3H2R 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3H2P 'HUMAN SOD1 D124V VARIANT'                  unspecified 
PDB 3H2Q 'HUMAN SOD1 H80R VARIANT, P21 CRYSTAL FORM' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3QQD 
_pdbx_database_status.recvd_initial_deposition_date   2011-02-15 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Seetharaman, S.V.' 1  
'Winkler, D.D.'     2  
'Taylor, A.B.'      3  
'Cao, X.'           4  
'Whitson, L.J.'     5  
'Doucette, P.A.'    6  
'Valentine, J.S.'   7  
'Schirf, V.'        8  
'Demeler, B.'       9  
'Carroll, M.C.'     10 
'Culotta, V.C.'     11 
'Hart, P.J.'        12 
# 
_citation.id                        primary 
_citation.title                     'Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R.' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            49 
_citation.page_first                5714 
_citation.page_last                 5725 
_citation.year                      2010 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20515040 
_citation.pdbx_database_id_DOI      10.1021/bi100314n 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Seetharaman, S.V.' 1  
primary 'Winkler, D.D.'     2  
primary 'Taylor, A.B.'      3  
primary 'Cao, X.'           4  
primary 'Whitson, L.J.'     5  
primary 'Doucette, P.A.'    6  
primary 'Valentine, J.S.'   7  
primary 'Schirf, V.'        8  
primary 'Demeler, B.'       9  
primary 'Carroll, M.C.'     10 
primary 'Culotta, V.C.'     11 
primary 'Hart, P.J.'        12 
# 
_cell.entry_id           3QQD 
_cell.length_a           40.245 
_cell.length_b           58.427 
_cell.length_c           104.825 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3QQD 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
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 'Superoxide dismutase [Cu-Zn]' 15920.646 1   1.15.1.1 YES ? ? 
2 polymer     man 'Superoxide dismutase [Cu-Zn]' 15888.647 1   1.15.1.1 YES ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    2   ?        ?   ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    2   ?        ?   ? ? 
5 water       nat water                          18.015    188 ?        ?   ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;(ACE)ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPK
DEERRVGDLGNVTADKDGVADVSIEDSVISLSGDH(OCS)IIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGI
AQ
;
;XATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
RVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
A ? 
2 'polypeptide(L)' no yes 
;(ACE)ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPK
DEERRVGDLGNVTADKDGVADVSIEDSVISLSGDH(CSX)IIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGI
AQ
;
;XATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
RVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ACE n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  ARG n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 OCS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
2 1   ACE n 
2 2   ALA n 
2 3   THR n 
2 4   LYS n 
2 5   ALA n 
2 6   VAL n 
2 7   CYS n 
2 8   VAL n 
2 9   LEU n 
2 10  LYS n 
2 11  GLY n 
2 12  ASP n 
2 13  GLY n 
2 14  PRO n 
2 15  VAL n 
2 16  GLN n 
2 17  GLY n 
2 18  ILE n 
2 19  ILE n 
2 20  ASN n 
2 21  PHE n 
2 22  GLU n 
2 23  GLN n 
2 24  LYS n 
2 25  GLU n 
2 26  SER n 
2 27  ASN n 
2 28  GLY n 
2 29  PRO n 
2 30  VAL n 
2 31  LYS n 
2 32  VAL n 
2 33  TRP n 
2 34  GLY n 
2 35  SER n 
2 36  ILE n 
2 37  LYS n 
2 38  GLY n 
2 39  LEU n 
2 40  THR n 
2 41  GLU n 
2 42  GLY n 
2 43  LEU n 
2 44  HIS n 
2 45  GLY n 
2 46  PHE n 
2 47  HIS n 
2 48  VAL n 
2 49  HIS n 
2 50  GLU n 
2 51  PHE n 
2 52  GLY n 
2 53  ASP n 
2 54  ASN n 
2 55  THR n 
2 56  ALA n 
2 57  GLY n 
2 58  CYS n 
2 59  THR n 
2 60  SER n 
2 61  ALA n 
2 62  GLY n 
2 63  PRO n 
2 64  HIS n 
2 65  PHE n 
2 66  ASN n 
2 67  PRO n 
2 68  LEU n 
2 69  SER n 
2 70  ARG n 
2 71  LYS n 
2 72  HIS n 
2 73  GLY n 
2 74  GLY n 
2 75  PRO n 
2 76  LYS n 
2 77  ASP n 
2 78  GLU n 
2 79  GLU n 
2 80  ARG n 
2 81  ARG n 
2 82  VAL n 
2 83  GLY n 
2 84  ASP n 
2 85  LEU n 
2 86  GLY n 
2 87  ASN n 
2 88  VAL n 
2 89  THR n 
2 90  ALA n 
2 91  ASP n 
2 92  LYS n 
2 93  ASP n 
2 94  GLY n 
2 95  VAL n 
2 96  ALA n 
2 97  ASP n 
2 98  VAL n 
2 99  SER n 
2 100 ILE n 
2 101 GLU n 
2 102 ASP n 
2 103 SER n 
2 104 VAL n 
2 105 ILE n 
2 106 SER n 
2 107 LEU n 
2 108 SER n 
2 109 GLY n 
2 110 ASP n 
2 111 HIS n 
2 112 CSX n 
2 113 ILE n 
2 114 ILE n 
2 115 GLY n 
2 116 ARG n 
2 117 THR n 
2 118 LEU n 
2 119 VAL n 
2 120 VAL n 
2 121 HIS n 
2 122 GLU n 
2 123 LYS n 
2 124 ALA n 
2 125 ASP n 
2 126 ASP n 
2 127 LEU n 
2 128 GLY n 
2 129 LYS n 
2 130 GLY n 
2 131 GLY n 
2 132 ASN n 
2 133 GLU n 
2 134 GLU n 
2 135 SER n 
2 136 THR n 
2 137 LYS n 
2 138 THR n 
2 139 GLY n 
2 140 ASN n 
2 141 ALA n 
2 142 GLY n 
2 143 SER n 
2 144 ARG n 
2 145 LEU n 
2 146 ALA n 
2 147 CYS n 
2 148 GLY n 
2 149 VAL n 
2 150 ILE n 
2 151 GLY n 
2 152 ILE n 
2 153 ALA n 
2 154 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample ? ? ? human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'SACCHAROMYCES CEREVISIAE' 4932 ? ? ? ? ? ? EGY118 ? 
? ? ? ? ? ? PLASMID ? ? ? YEP351-HSOD ? ? 
2 1 sample ? ? ? human ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'SACCHAROMYCES CEREVISIAE' 4932 ? ? ? ? ? ? EGY118 ? 
? ? ? ? ? ? PLASMID ? ? ? YEP351-HSOD ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP SODC_HUMAN 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 P00441 ? 
2 UNP SODC_HUMAN 2 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
2 P00441 ? 
# 
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 3QQD A 2 ? 154 ? P00441 2 ? 154 ? 1 153 
2 2 3QQD B 2 ? 154 ? P00441 2 ? 154 ? 1 153 
# 
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 3QQD ACE A 1  ? UNP P00441 ?   ?  ACETYLATION           0  1 
1 3QQD ARG A 81 ? UNP P00441 HIS 81 'ENGINEERED MUTATION' 80 2 
2 3QQD ACE B 1  ? UNP P00441 ?   ?  ACETYLATION           0  3 
2 3QQD ARG B 81 ? UNP P00441 HIS 81 'ENGINEERED MUTATION' 80 4 
# 
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 
ACE non-polymer         . 'ACETYL GROUP'          ? 'C2 H4 O'        44.053  
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 
CSX 'L-peptide linking' n 'S-OXY CYSTEINE'        ? 'C3 H7 N O3 S'   137.158 
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ? 'C3 H7 N O5 S'   169.156 
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 
SO4 non-polymer         . 'SULFATE ION'           ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'              ? 'Zn 2'           65.409  
# 
_exptl.entry_id          3QQD 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.94 
_exptl_crystal.density_percent_sol   36.61 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pdbx_details    '2.3 M AMMONIUM SULFATE, 0.1 M TRIS, TEMPERATURE 298K, pH 8.0, VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 210' 
_diffrn_detector.pdbx_collection_date   2004-11-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.282 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_wavelength             1.282 
_diffrn_source.pdbx_wavelength_list        1.282 
# 
_reflns.entry_id                     3QQD 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            1.650 
_reflns.number_obs                   30227 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.06400 
_reflns.pdbx_netI_over_sigmaI        23.2000 
_reflns.B_iso_Wilson_estimate        17.5 
_reflns.pdbx_redundancy              7.200 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.65 
_reflns_shell.d_res_low              1.71 
_reflns_shell.percent_possible_all   99.5 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.38500 
_reflns_shell.meanI_over_sigI_obs    5.500 
_reflns_shell.pdbx_redundancy        6.30 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3QQD 
_refine.ls_number_reflns_obs                     30227 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.32 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             39.015 
_refine.ls_d_res_high                            1.653 
_refine.ls_percent_reflns_obs                    99.56 
_refine.ls_R_factor_obs                          0.1466 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1445 
_refine.ls_R_factor_R_free                       0.1833 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_number_reflns_R_free                  1533 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            -3.8194 
_refine.aniso_B[2][2]                            0.9662 
_refine.aniso_B[3][3]                            -0.5823 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.406 
_refine.solvent_model_param_bsol                 40.000 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'pdb entry 1AZV' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.18 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 16.04 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1823 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.number_atoms_solvent             188 
_refine_hist.number_atoms_total               2023 
_refine_hist.d_res_high                       1.653 
_refine_hist.d_res_low                        39.015 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.005  ? ? 1862 'X-RAY DIFFRACTION' ? 
f_angle_d          0.913  ? ? 2518 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 10.365 ? ? 649  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.063  ? ? 287  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 332  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 1.6532 1.7065  2500 0.2264 97.00  0.2737 . . 113 . . . . 'X-RAY DIFFRACTION' 
. 1.7065 1.7675  2583 0.1546 99.00  0.2112 . . 128 . . . . 'X-RAY DIFFRACTION' 
. 1.7675 1.8383  2585 0.1232 100.00 0.1997 . . 129 . . . . 'X-RAY DIFFRACTION' 
. 1.8383 1.9220  2572 0.0967 100.00 0.1845 . . 137 . . . . 'X-RAY DIFFRACTION' 
. 1.9220 2.0233  2585 0.1004 100.00 0.1409 . . 144 . . . . 'X-RAY DIFFRACTION' 
. 2.0233 2.1501  2588 0.0996 100.00 0.1387 . . 140 . . . . 'X-RAY DIFFRACTION' 
. 2.1501 2.3160  2614 0.1219 100.00 0.1820 . . 125 . . . . 'X-RAY DIFFRACTION' 
. 2.3160 2.5491  2614 0.1469 100.00 0.1912 . . 145 . . . . 'X-RAY DIFFRACTION' 
. 2.5491 2.9178  2628 0.1644 100.00 0.1839 . . 144 . . . . 'X-RAY DIFFRACTION' 
. 2.9178 3.6757  2655 0.1530 100.00 0.1790 . . 157 . . . . 'X-RAY DIFFRACTION' 
. 3.6757 39.0257 2770 0.1635 100.00 0.1928 . . 171 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3QQD 
_struct.title                     'Human SOD1 H80R variant, P212121 crystal form' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3QQD 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, DISULFIDE BOND
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
1 ? 
2 ? 
# 
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 1 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 SER A 108 ? OCS A 112 ? SER A 107 OCS A 111 5 ? 5 
HELX_P HELX_P3 3 ALA B 56  ? ALA B 61  ? ALA B 55  ALA B 60  5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 58  SG  ? ? ? 1_555 A CYS 147 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.793 ? 
disulf2 disulf ? ? B CYS 58  SG  ? ? ? 1_555 B CYS 147 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.782 ? 
covale1 covale ? ? A HIS 111 C   ? ? ? 1_555 A OCS 112 N  ? ? A HIS 110 A OCS 111 1_555 ? ? ? ? ? ? ? 1.326 ? 
covale2 covale ? ? A OCS 112 C   ? ? ? 1_555 A ILE 113 N  ? ? A OCS 111 A ILE 112 1_555 ? ? ? ? ? ? ? 1.332 ? 
covale3 covale ? ? B HIS 111 C   ? ? ? 1_555 B CSX 112 N  ? ? B HIS 110 B CSX 111 1_555 ? ? ? ? ? ? ? 1.334 ? 
covale4 covale ? ? B CSX 112 C   ? ? ? 1_555 B ILE 113 N  ? ? B CSX 111 B ILE 112 1_555 ? ? ? ? ? ? ? 1.327 ? 
metalc1 metalc ? ? A HIS 47  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 46  A ZN  154 1_555 ? ? ? ? ? ? ? 2.271 ? 
metalc2 metalc ? ? A HIS 49  NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 48  A ZN  154 1_555 ? ? ? ? ? ? ? 2.254 ? 
metalc3 metalc ? ? A HIS 121 NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 120 A ZN  154 1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc4 metalc ? ? B HIS 47  ND1 ? ? ? 1_555 E ZN  .   ZN ? ? B HIS 46  B ZN  154 1_555 ? ? ? ? ? ? ? 2.144 ? 
metalc5 metalc ? ? B HIS 49  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? B HIS 48  B ZN  154 1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc6 metalc ? ? B HIS 121 NE2 ? ? ? 1_555 E ZN  .   ZN ? ? B HIS 120 B ZN  154 1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc7 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F SO4 .   O1 ? ? B ZN  154 B SO4 155 1_555 ? ? ? ? ? ? ? 2.174 ? 
covale5 covale ? ? B ALA 2   N   ? ? ? 1_555 B ACE 1   C  ? ? B ALA 1   B ACE 0   1_555 ? ? ? ? ? ? ? 1.332 ? 
metalc8 metalc ? ? A HIS 64  NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 63  A ZN  154 1_555 ? ? ? ? ? ? ? 2.436 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 9 ? 
B ? 5 ? 
C ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
A 5 6 ? anti-parallel 
A 6 7 ? anti-parallel 
A 7 8 ? anti-parallel 
A 8 9 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? 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 
A 1 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
A 2 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
A 3 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
A 4 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
A 5 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
A 6 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
A 7 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
A 8 LYS A 4   ? LEU A 9   ? LYS A 3   LEU A 8   
A 9 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
B 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
B 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
B 3 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
B 4 LYS B 4   ? LEU B 9   ? LYS B 3   LEU B 8   
B 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
C 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
C 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
C 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
C 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
# 
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 
A 1 2 O GLY A 148 ? O GLY A 147 N LEU A 118 ? N LEU A 117 
A 2 3 O THR A 117 ? O THR A 116 N HIS A 49  ? N HIS A 48  
A 3 4 N GLY A 42  ? N GLY A 41  O ALA A 90  ? O ALA A 89  
A 4 5 N THR A 89  ? N THR A 88  O ASP A 97  ? O ASP A 96  
A 5 6 O ASP A 102 ? O ASP A 101 N VAL A 30  ? N VAL A 29  
A 6 7 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
A 7 8 O ILE A 19  ? O ILE A 18  N CYS A 7   ? N CYS A 6   
A 8 9 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
B 1 2 O ALA B 96  ? O ALA B 95  N ILE B 36  ? N ILE B 35  
B 2 3 O TRP B 33  ? O TRP B 32  N ASN B 20  ? N ASN B 19  
B 3 4 O GLY B 17  ? O GLY B 16  N LEU B 9   ? N LEU B 8   
B 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
C 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
C 2 3 N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
C 3 4 N LEU B 118 ? N LEU B 117 O GLY B 148 ? O GLY B 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 154'  
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 155' 
AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE ACE B 0'   
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 154'  
AC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5 HIS A 47  ? HIS A 46  . ? 1_555 ? 
2  AC1 5 HIS A 49  ? HIS A 48  . ? 1_555 ? 
3  AC1 5 HIS A 64  ? HIS A 63  . ? 1_555 ? 
4  AC1 5 HIS A 121 ? HIS A 120 . ? 1_555 ? 
5  AC1 5 SO4 D .   ? SO4 A 155 . ? 1_555 ? 
6  AC2 5 HIS A 49  ? HIS A 48  . ? 1_555 ? 
7  AC2 5 HIS A 64  ? HIS A 63  . ? 1_555 ? 
8  AC2 5 HIS A 121 ? HIS A 120 . ? 1_555 ? 
9  AC2 5 ARG A 144 ? ARG A 143 . ? 1_555 ? 
10 AC2 5 ZN  C .   ? ZN  A 154 . ? 1_555 ? 
11 AC3 2 ALA B 2   ? ALA B 1   . ? 1_555 ? 
12 AC3 2 THR B 3   ? THR B 2   . ? 1_555 ? 
13 AC4 4 HIS B 47  ? HIS B 46  . ? 1_555 ? 
14 AC4 4 HIS B 49  ? HIS B 48  . ? 1_555 ? 
15 AC4 4 HIS B 121 ? HIS B 120 . ? 1_555 ? 
16 AC4 4 SO4 F .   ? SO4 B 155 . ? 1_555 ? 
17 AC5 7 HIS B 47  ? HIS B 46  . ? 1_555 ? 
18 AC5 7 HIS B 49  ? HIS B 48  . ? 1_555 ? 
19 AC5 7 HIS B 64  ? HIS B 63  . ? 1_555 ? 
20 AC5 7 HIS B 121 ? HIS B 120 . ? 1_555 ? 
21 AC5 7 ZN  E .   ? ZN  B 154 . ? 1_555 ? 
22 AC5 7 HOH H .   ? HOH B 227 . ? 1_555 ? 
23 AC5 7 HOH H .   ? HOH B 250 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3QQD 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3QQD 
_atom_sites.fract_transf_matrix[1][1]   0.024848 
_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]   0.017115 
_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]   0.009540 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 3   ? 10.038  -19.895 15.312 1.00 24.00 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 3   ? 8.687   -19.477 14.945 1.00 20.96 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 3   ? 7.682   -20.063 15.926 1.00 19.46 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 3   ? 7.771   -21.234 16.289 1.00 19.07 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 3   ? 8.330   -19.922 13.520 1.00 27.92 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 3   ? 9.324   -19.436 12.611 1.00 33.97 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 3   ? 6.983   -19.366 13.109 1.00 31.43 ? 2   THR A CG2 1 
ATOM   8    N  N   . LYS A 1 4   ? 6.735   -19.235 16.354 1.00 16.83 ? 3   LYS A N   1 
ATOM   9    C  CA  . LYS A 1 4   ? 5.773   -19.618 17.377 1.00 15.68 ? 3   LYS A CA  1 
ATOM   10   C  C   . LYS A 1 4   ? 4.367   -19.200 16.971 1.00 13.77 ? 3   LYS A C   1 
ATOM   11   O  O   . LYS A 1 4   ? 4.172   -18.161 16.325 1.00 15.20 ? 3   LYS A O   1 
ATOM   12   C  CB  . LYS A 1 4   ? 6.137   -18.984 18.727 1.00 18.84 ? 3   LYS A CB  1 
ATOM   13   C  CG  . LYS A 1 4   ? 7.445   -19.495 19.333 1.00 24.11 ? 3   LYS A CG  1 
ATOM   14   C  CD  . LYS A 1 4   ? 7.744   -18.833 20.669 1.00 30.53 ? 3   LYS A CD  1 
ATOM   15   C  CE  . LYS A 1 4   ? 9.111   -19.261 21.200 1.00 36.69 ? 3   LYS A CE  1 
ATOM   16   N  NZ  . LYS A 1 4   ? 9.426   -18.718 22.556 1.00 39.53 ? 3   LYS A NZ  1 
ATOM   17   N  N   . ALA A 1 5   ? 3.389   -20.018 17.349 1.00 12.66 ? 4   ALA A N   1 
ATOM   18   C  CA  . ALA A 1 5   ? 1.989   -19.704 17.109 1.00 11.26 ? 4   ALA A CA  1 
ATOM   19   C  C   . ALA A 1 5   ? 1.159   -20.158 18.296 1.00 11.46 ? 4   ALA A C   1 
ATOM   20   O  O   . ALA A 1 5   ? 1.640   -20.908 19.156 1.00 12.77 ? 4   ALA A O   1 
ATOM   21   C  CB  . ALA A 1 5   ? 1.489   -20.360 15.824 1.00 12.40 ? 4   ALA A CB  1 
ATOM   22   N  N   . VAL A 1 6   ? -0.083  -19.692 18.344 1.00 11.33 ? 5   VAL A N   1 
ATOM   23   C  CA  . VAL A 1 6   ? -0.983  -20.053 19.426 1.00 11.80 ? 5   VAL A CA  1 
ATOM   24   C  C   . VAL A 1 6   ? -2.415  -20.068 18.917 1.00 11.97 ? 5   VAL A C   1 
ATOM   25   O  O   . VAL A 1 6   ? -2.756  -19.396 17.938 1.00 13.51 ? 5   VAL A O   1 
ATOM   26   C  CB  . VAL A 1 6   ? -0.854  -19.084 20.621 1.00 12.57 ? 5   VAL A CB  1 
ATOM   27   C  CG1 . VAL A 1 6   ? -1.383  -17.705 20.260 1.00 16.54 ? 5   VAL A CG1 1 
ATOM   28   C  CG2 . VAL A 1 6   ? -1.573  -19.634 21.842 1.00 14.84 ? 5   VAL A CG2 1 
ATOM   29   N  N   . CYS A 1 7   ? -3.250  -20.854 19.573 1.00 10.20 ? 6   CYS A N   1 
ATOM   30   C  CA  . CYS A 1 7   ? -4.647  -20.951 19.193 1.00 10.69 ? 6   CYS A CA  1 
ATOM   31   C  C   . CYS A 1 7   ? -5.496  -21.081 20.444 1.00 12.30 ? 6   CYS A C   1 
ATOM   32   O  O   . CYS A 1 7   ? -5.214  -21.920 21.302 1.00 13.76 ? 6   CYS A O   1 
ATOM   33   C  CB  . CYS A 1 7   ? -4.862  -22.182 18.307 1.00 12.37 ? 6   CYS A CB  1 
ATOM   34   S  SG  . CYS A 1 7   ? -6.555  -22.320 17.688 1.00 15.56 ? 6   CYS A SG  1 
ATOM   35   N  N   . VAL A 1 8   ? -6.531  -20.251 20.549 1.00 9.62  ? 7   VAL A N   1 
ATOM   36   C  CA  . VAL A 1 8   ? -7.500  -20.386 21.626 1.00 10.69 ? 7   VAL A CA  1 
ATOM   37   C  C   . VAL A 1 8   ? -8.751  -21.067 21.088 1.00 10.53 ? 7   VAL A C   1 
ATOM   38   O  O   . VAL A 1 8   ? -9.418  -20.543 20.187 1.00 13.47 ? 7   VAL A O   1 
ATOM   39   C  CB  . VAL A 1 8   ? -7.886  -19.018 22.212 1.00 12.74 ? 7   VAL A CB  1 
ATOM   40   C  CG1 . VAL A 1 8   ? -8.908  -19.188 23.333 1.00 15.15 ? 7   VAL A CG1 1 
ATOM   41   C  CG2 . VAL A 1 8   ? -6.636  -18.279 22.698 1.00 14.07 ? 7   VAL A CG2 1 
ATOM   42   N  N   . LEU A 1 9   ? -9.064  -22.237 21.635 1.00 11.24 ? 8   LEU A N   1 
ATOM   43   C  CA  . LEU A 1 9   ? -10.229 -23.001 21.202 1.00 11.27 ? 8   LEU A CA  1 
ATOM   44   C  C   . LEU A 1 9   ? -11.456 -22.597 22.002 1.00 11.28 ? 8   LEU A C   1 
ATOM   45   O  O   . LEU A 1 9   ? -11.424 -22.590 23.233 1.00 14.68 ? 8   LEU A O   1 
ATOM   46   C  CB  . LEU A 1 9   ? -9.977  -24.498 21.398 1.00 12.65 ? 8   LEU A CB  1 
ATOM   47   C  CG  . LEU A 1 9   ? -8.803  -25.106 20.624 1.00 17.03 ? 8   LEU A CG  1 
ATOM   48   C  CD1 . LEU A 1 9   ? -8.459  -26.500 21.154 1.00 19.96 ? 8   LEU A CD1 1 
ATOM   49   C  CD2 . LEU A 1 9   ? -9.139  -25.154 19.151 1.00 17.26 ? 8   LEU A CD2 1 
ATOM   50   N  N   . LYS A 1 10  ? -12.533 -22.258 21.298 1.00 12.72 ? 9   LYS A N   1 
ATOM   51   C  CA  . LYS A 1 10  ? -13.804 -21.925 21.931 1.00 16.29 ? 9   LYS A CA  1 
ATOM   52   C  C   . LYS A 1 10  ? -14.949 -22.529 21.128 1.00 16.03 ? 9   LYS A C   1 
ATOM   53   O  O   . LYS A 1 10  ? -14.830 -22.738 19.919 1.00 16.50 ? 9   LYS A O   1 
ATOM   54   C  CB  . LYS A 1 10  ? -13.985 -20.409 22.021 1.00 21.95 ? 9   LYS A CB  1 
ATOM   55   C  CG  . LYS A 1 10  ? -12.978 -19.691 22.906 1.00 28.98 ? 9   LYS A CG  1 
ATOM   56   C  CD  . LYS A 1 10  ? -13.317 -18.211 23.018 1.00 35.38 ? 9   LYS A CD  1 
ATOM   57   C  CE  . LYS A 1 10  ? -12.247 -17.444 23.786 1.00 36.94 ? 9   LYS A CE  1 
ATOM   58   N  NZ  . LYS A 1 10  ? -12.103 -17.914 25.187 1.00 39.07 ? 9   LYS A NZ  1 
ATOM   59   N  N   . GLY A 1 11  ? -16.058 -22.813 21.801 1.00 17.42 ? 10  GLY A N   1 
ATOM   60   C  CA  . GLY A 1 11  ? -17.203 -23.403 21.133 1.00 19.62 ? 10  GLY A CA  1 
ATOM   61   C  C   . GLY A 1 11  ? -18.517 -22.968 21.735 1.00 24.01 ? 10  GLY A C   1 
ATOM   62   O  O   . GLY A 1 11  ? -18.572 -22.008 22.504 1.00 26.42 ? 10  GLY A O   1 
ATOM   63   N  N   . ASP A 1 12  ? -19.578 -23.682 21.384 1.00 26.84 ? 11  ASP A N   1 
ATOM   64   C  CA  . ASP A 1 12  ? -20.919 -23.381 21.884 1.00 31.58 ? 11  ASP A CA  1 
ATOM   65   C  C   . ASP A 1 12  ? -21.144 -23.907 23.298 1.00 29.70 ? 11  ASP A C   1 
ATOM   66   O  O   . ASP A 1 12  ? -22.043 -23.444 24.003 1.00 32.23 ? 11  ASP A O   1 
ATOM   67   C  CB  . ASP A 1 12  ? -21.977 -23.968 20.949 1.00 35.58 ? 11  ASP A CB  1 
ATOM   68   C  CG  . ASP A 1 12  ? -22.033 -23.257 19.615 1.00 43.16 ? 11  ASP A CG  1 
ATOM   69   O  OD1 . ASP A 1 12  ? -21.435 -22.165 19.501 1.00 44.05 ? 11  ASP A OD1 1 
ATOM   70   O  OD2 . ASP A 1 12  ? -22.682 -23.786 18.684 1.00 46.88 ? 11  ASP A OD2 1 
ATOM   71   N  N   . GLY A 1 13  ? -20.331 -24.878 23.706 1.00 26.39 ? 12  GLY A N   1 
ATOM   72   C  CA  . GLY A 1 13  ? -20.494 -25.508 25.003 1.00 25.27 ? 12  GLY A CA  1 
ATOM   73   C  C   . GLY A 1 13  ? -19.303 -25.294 25.923 1.00 22.16 ? 12  GLY A C   1 
ATOM   74   O  O   . GLY A 1 13  ? -18.712 -24.213 25.954 1.00 20.68 ? 12  GLY A O   1 
ATOM   75   N  N   . PRO A 1 14  ? -18.936 -26.333 26.682 1.00 19.72 ? 13  PRO A N   1 
ATOM   76   C  CA  . PRO A 1 14  ? -17.896 -26.199 27.705 1.00 18.83 ? 13  PRO A CA  1 
ATOM   77   C  C   . PRO A 1 14  ? -16.483 -26.395 27.172 1.00 17.46 ? 13  PRO A C   1 
ATOM   78   O  O   . PRO A 1 14  ? -15.532 -26.182 27.920 1.00 18.97 ? 13  PRO A O   1 
ATOM   79   C  CB  . PRO A 1 14  ? -18.232 -27.339 28.667 1.00 21.26 ? 13  PRO A CB  1 
ATOM   80   C  CG  . PRO A 1 14  ? -18.778 -28.400 27.771 1.00 22.17 ? 13  PRO A CG  1 
ATOM   81   C  CD  . PRO A 1 14  ? -19.556 -27.671 26.699 1.00 20.18 ? 13  PRO A CD  1 
ATOM   82   N  N   . VAL A 1 15  ? -16.338 -26.799 25.913 1.00 14.90 ? 14  VAL A N   1 
ATOM   83   C  CA  . VAL A 1 15  ? -15.016 -27.151 25.406 1.00 15.19 ? 14  VAL A CA  1 
ATOM   84   C  C   . VAL A 1 15  ? -14.177 -25.914 25.148 1.00 14.29 ? 14  VAL A C   1 
ATOM   85   O  O   . VAL A 1 15  ? -14.581 -25.024 24.403 1.00 17.48 ? 14  VAL A O   1 
ATOM   86   C  CB  . VAL A 1 15  ? -15.087 -28.014 24.125 1.00 14.46 ? 14  VAL A CB  1 
ATOM   87   C  CG1 . VAL A 1 15  ? -13.682 -28.376 23.655 1.00 16.84 ? 14  VAL A CG1 1 
ATOM   88   C  CG2 . VAL A 1 15  ? -15.904 -29.275 24.389 1.00 15.29 ? 14  VAL A CG2 1 
ATOM   89   N  N   . GLN A 1 16  ? -13.008 -25.855 25.773 1.00 13.68 ? 15  GLN A N   1 
ATOM   90   C  CA  . GLN A 1 16  ? -12.113 -24.729 25.566 1.00 16.26 ? 15  GLN A CA  1 
ATOM   91   C  C   . GLN A 1 16  ? -10.676 -25.134 25.828 1.00 15.78 ? 15  GLN A C   1 
ATOM   92   O  O   . GLN A 1 16  ? -10.405 -26.080 26.563 1.00 17.39 ? 15  GLN A O   1 
ATOM   93   C  CB  . GLN A 1 16  ? -12.501 -23.557 26.464 1.00 23.23 ? 15  GLN A CB  1 
ATOM   94   C  CG  . GLN A 1 16  ? -12.413 -23.844 27.942 1.00 29.14 ? 15  GLN A CG  1 
ATOM   95   C  CD  . GLN A 1 16  ? -13.139 -22.800 28.762 1.00 38.40 ? 15  GLN A CD  1 
ATOM   96   O  OE1 . GLN A 1 16  ? -13.711 -21.859 28.213 1.00 44.03 ? 15  GLN A OE1 1 
ATOM   97   N  NE2 . GLN A 1 16  ? -13.125 -22.961 30.077 1.00 41.02 ? 15  GLN A NE2 1 
ATOM   98   N  N   . GLY A 1 17  ? -9.745  -24.416 25.231 1.00 14.16 ? 16  GLY A N   1 
ATOM   99   C  CA  . GLY A 1 17  ? -8.353  -24.767 25.417 1.00 14.51 ? 16  GLY A CA  1 
ATOM   100  C  C   . GLY A 1 17  ? -7.416  -23.763 24.800 1.00 14.23 ? 16  GLY A C   1 
ATOM   101  O  O   . GLY A 1 17  ? -7.831  -22.867 24.067 1.00 15.29 ? 16  GLY A O   1 
ATOM   102  N  N   . ILE A 1 18  ? -6.142  -23.915 25.122 1.00 14.04 ? 17  ILE A N   1 
ATOM   103  C  CA  . ILE A 1 18  ? -5.087  -23.111 24.528 1.00 12.56 ? 17  ILE A CA  1 
ATOM   104  C  C   . ILE A 1 18  ? -4.036  -24.063 23.996 1.00 12.45 ? 17  ILE A C   1 
ATOM   105  O  O   . ILE A 1 18  ? -3.539  -24.930 24.727 1.00 13.11 ? 17  ILE A O   1 
ATOM   106  C  CB  . ILE A 1 18  ? -4.447  -22.166 25.558 1.00 14.22 ? 17  ILE A CB  1 
ATOM   107  C  CG1 . ILE A 1 18  ? -5.481  -21.151 26.053 1.00 17.25 ? 17  ILE A CG1 1 
ATOM   108  C  CG2 . ILE A 1 18  ? -3.237  -21.458 24.946 1.00 16.67 ? 17  ILE A CG2 1 
ATOM   109  C  CD1 . ILE A 1 18  ? -4.980  -20.278 27.186 1.00 19.28 ? 17  ILE A CD1 1 
ATOM   110  N  N   . ILE A 1 19  ? -3.716  -23.912 22.717 1.00 12.09 ? 18  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 19  ? -2.747  -24.766 22.051 1.00 12.74 ? 18  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 19  ? -1.601  -23.917 21.515 1.00 12.42 ? 18  ILE A C   1 
ATOM   113  O  O   . ILE A 1 19  ? -1.825  -22.905 20.847 1.00 13.43 ? 18  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 19  ? -3.410  -25.537 20.889 1.00 12.70 ? 18  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 19  ? -4.590  -26.375 21.399 1.00 15.26 ? 18  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 19  ? -2.386  -26.391 20.148 1.00 14.11 ? 18  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 19  ? -4.210  -27.430 22.414 1.00 17.39 ? 18  ILE A CD1 1 
ATOM   118  N  N   . ASN A 1 20  ? -0.377  -24.330 21.831 1.00 11.54 ? 19  ASN A N   1 
ATOM   119  C  CA  . ASN A 1 20  ? 0.829   -23.643 21.399 1.00 12.24 ? 19  ASN A CA  1 
ATOM   120  C  C   . ASN A 1 20  ? 1.544   -24.430 20.309 1.00 14.42 ? 19  ASN A C   1 
ATOM   121  O  O   . ASN A 1 20  ? 1.485   -25.662 20.286 1.00 13.89 ? 19  ASN A O   1 
ATOM   122  C  CB  . ASN A 1 20  ? 1.784   -23.483 22.581 1.00 14.92 ? 19  ASN A CB  1 
ATOM   123  C  CG  . ASN A 1 20  ? 1.155   -22.746 23.740 1.00 18.25 ? 19  ASN A CG  1 
ATOM   124  O  OD1 . ASN A 1 20  ? 0.996   -21.532 23.695 1.00 20.66 ? 19  ASN A OD1 1 
ATOM   125  N  ND2 . ASN A 1 20  ? 0.793   -23.482 24.793 1.00 19.86 ? 19  ASN A ND2 1 
ATOM   126  N  N   . PHE A 1 21  ? 2.223   -23.709 19.421 1.00 13.63 ? 20  PHE A N   1 
ATOM   127  C  CA  . PHE A 1 21  ? 2.988   -24.309 18.332 1.00 13.05 ? 20  PHE A CA  1 
ATOM   128  C  C   . PHE A 1 21  ? 4.382   -23.709 18.331 1.00 13.32 ? 20  PHE A C   1 
ATOM   129  O  O   . PHE A 1 21  ? 4.540   -22.506 18.516 1.00 15.08 ? 20  PHE A O   1 
ATOM   130  C  CB  . PHE A 1 21  ? 2.349   -23.991 16.977 1.00 13.20 ? 20  PHE A CB  1 
ATOM   131  C  CG  . PHE A 1 21  ? 0.933   -24.474 16.828 1.00 13.85 ? 20  PHE A CG  1 
ATOM   132  C  CD1 . PHE A 1 21  ? 0.660   -25.679 16.196 1.00 15.61 ? 20  PHE A CD1 1 
ATOM   133  C  CD2 . PHE A 1 21  ? -0.126  -23.721 17.309 1.00 16.26 ? 20  PHE A CD2 1 
ATOM   134  C  CE1 . PHE A 1 21  ? -0.647  -26.125 16.047 1.00 16.03 ? 20  PHE A CE1 1 
ATOM   135  C  CE2 . PHE A 1 21  ? -1.437  -24.160 17.172 1.00 16.76 ? 20  PHE A CE2 1 
ATOM   136  C  CZ  . PHE A 1 21  ? -1.700  -25.366 16.547 1.00 16.42 ? 20  PHE A CZ  1 
ATOM   137  N  N   . GLU A 1 22  ? 5.393   -24.536 18.106 1.00 13.95 ? 21  GLU A N   1 
ATOM   138  C  CA  . GLU A 1 22  ? 6.753   -24.027 17.949 1.00 15.64 ? 21  GLU A CA  1 
ATOM   139  C  C   . GLU A 1 22  ? 7.507   -24.817 16.897 1.00 16.16 ? 21  GLU A C   1 
ATOM   140  O  O   . GLU A 1 22  ? 7.462   -26.046 16.873 1.00 17.87 ? 21  GLU A O   1 
ATOM   141  C  CB  . GLU A 1 22  ? 7.512   -24.049 19.276 1.00 19.74 ? 21  GLU A CB  1 
ATOM   142  C  CG  . GLU A 1 22  ? 8.897   -23.421 19.191 1.00 26.12 ? 21  GLU A CG  1 
ATOM   143  C  CD  . GLU A 1 22  ? 9.625   -23.406 20.522 1.00 35.59 ? 21  GLU A CD  1 
ATOM   144  O  OE1 . GLU A 1 22  ? 8.962   -23.502 21.574 1.00 39.63 ? 21  GLU A OE1 1 
ATOM   145  O  OE2 . GLU A 1 22  ? 10.868  -23.294 20.513 1.00 40.24 ? 21  GLU A OE2 1 
ATOM   146  N  N   . GLN A 1 23  ? 8.205   -24.100 16.027 1.00 16.37 ? 22  GLN A N   1 
ATOM   147  C  CA  . GLN A 1 23  ? 9.018   -24.726 14.995 1.00 16.48 ? 22  GLN A CA  1 
ATOM   148  C  C   . GLN A 1 23  ? 10.381  -24.064 14.979 1.00 20.66 ? 22  GLN A C   1 
ATOM   149  O  O   . GLN A 1 23  ? 10.496  -22.880 14.662 1.00 22.87 ? 22  GLN A O   1 
ATOM   150  C  CB  . GLN A 1 23  ? 8.347   -24.569 13.629 1.00 15.43 ? 22  GLN A CB  1 
ATOM   151  C  CG  . GLN A 1 23  ? 8.999   -25.389 12.528 1.00 15.80 ? 22  GLN A CG  1 
ATOM   152  C  CD  . GLN A 1 23  ? 8.289   -25.225 11.204 1.00 16.56 ? 22  GLN A CD  1 
ATOM   153  O  OE1 . GLN A 1 23  ? 7.686   -24.185 10.942 1.00 18.34 ? 22  GLN A OE1 1 
ATOM   154  N  NE2 . GLN A 1 23  ? 8.346   -26.252 10.366 1.00 17.04 ? 22  GLN A NE2 1 
ATOM   155  N  N   . LYS A 1 24  ? 11.416  -24.831 15.313 1.00 22.33 ? 23  LYS A N   1 
ATOM   156  C  CA  . LYS A 1 24  ? 12.766  -24.289 15.405 1.00 25.49 ? 23  LYS A CA  1 
ATOM   157  C  C   . LYS A 1 24  ? 13.432  -24.068 14.044 1.00 26.37 ? 23  LYS A C   1 
ATOM   158  O  O   . LYS A 1 24  ? 14.201  -23.121 13.878 1.00 28.37 ? 23  LYS A O   1 
ATOM   159  C  CB  . LYS A 1 24  ? 13.637  -25.180 16.290 1.00 29.21 ? 23  LYS A CB  1 
ATOM   160  C  CG  . LYS A 1 24  ? 13.146  -25.254 17.730 1.00 35.74 ? 23  LYS A CG  1 
ATOM   161  C  CD  . LYS A 1 24  ? 14.268  -25.554 18.708 1.00 41.96 ? 23  LYS A CD  1 
ATOM   162  C  CE  . LYS A 1 24  ? 13.795  -25.335 20.140 1.00 46.46 ? 23  LYS A CE  1 
ATOM   163  N  NZ  . LYS A 1 24  ? 14.888  -25.483 21.146 1.00 50.60 ? 23  LYS A NZ  1 
ATOM   164  N  N   . GLU A 1 25  ? 13.138  -24.941 13.083 1.00 25.61 ? 24  GLU A N   1 
ATOM   165  C  CA  . GLU A 1 25  ? 13.700  -24.831 11.736 1.00 27.47 ? 24  GLU A CA  1 
ATOM   166  C  C   . GLU A 1 25  ? 12.602  -24.990 10.695 1.00 25.70 ? 24  GLU A C   1 
ATOM   167  O  O   . GLU A 1 25  ? 11.677  -25.771 10.883 1.00 24.20 ? 24  GLU A O   1 
ATOM   168  C  CB  . GLU A 1 25  ? 14.766  -25.904 11.504 1.00 30.55 ? 24  GLU A CB  1 
ATOM   169  C  CG  . GLU A 1 25  ? 15.938  -25.860 12.456 1.00 38.69 ? 24  GLU A CG  1 
ATOM   170  C  CD  . GLU A 1 25  ? 16.959  -26.938 12.144 1.00 47.73 ? 24  GLU A CD  1 
ATOM   171  O  OE1 . GLU A 1 25  ? 16.780  -27.643 11.126 1.00 50.38 ? 24  GLU A OE1 1 
ATOM   172  O  OE2 . GLU A 1 25  ? 17.937  -27.080 12.910 1.00 52.43 ? 24  GLU A OE2 1 
ATOM   173  N  N   . SER A 1 26  ? 12.717  -24.275 9.581  1.00 25.13 ? 25  SER A N   1 
ATOM   174  C  CA  . SER A 1 26  ? 11.634  -24.257 8.600  1.00 26.78 ? 25  SER A CA  1 
ATOM   175  C  C   . SER A 1 26  ? 11.294  -25.641 8.048  1.00 29.27 ? 25  SER A C   1 
ATOM   176  O  O   . SER A 1 26  ? 10.151  -25.895 7.671  1.00 29.32 ? 25  SER A O   1 
ATOM   177  C  CB  . SER A 1 26  ? 11.955  -23.304 7.450  1.00 27.01 ? 25  SER A CB  1 
ATOM   178  O  OG  . SER A 1 26  ? 12.989  -23.835 6.649  1.00 27.92 ? 25  SER A OG  1 
ATOM   179  N  N   . ASN A 1 27  ? 12.276  -26.535 7.984  1.00 32.04 ? 26  ASN A N   1 
ATOM   180  C  CA  . ASN A 1 27  ? 12.008  -27.867 7.454  1.00 37.94 ? 26  ASN A CA  1 
ATOM   181  C  C   . ASN A 1 27  ? 11.878  -28.917 8.553  1.00 36.47 ? 26  ASN A C   1 
ATOM   182  O  O   . ASN A 1 27  ? 11.841  -30.116 8.274  1.00 40.84 ? 26  ASN A O   1 
ATOM   183  C  CB  . ASN A 1 27  ? 13.078  -28.286 6.442  1.00 43.29 ? 26  ASN A CB  1 
ATOM   184  C  CG  . ASN A 1 27  ? 14.331  -28.813 7.105  1.00 48.06 ? 26  ASN A CG  1 
ATOM   185  O  OD1 . ASN A 1 27  ? 14.738  -28.329 8.161  1.00 50.60 ? 26  ASN A OD1 1 
ATOM   186  N  ND2 . ASN A 1 27  ? 14.948  -29.818 6.491  1.00 49.77 ? 26  ASN A ND2 1 
ATOM   187  N  N   . GLY A 1 28  ? 11.803  -28.461 9.799  1.00 28.60 ? 27  GLY A N   1 
ATOM   188  C  CA  . GLY A 1 28  ? 11.745  -29.364 10.934 1.00 24.80 ? 27  GLY A CA  1 
ATOM   189  C  C   . GLY A 1 28  ? 10.340  -29.570 11.461 1.00 23.37 ? 27  GLY A C   1 
ATOM   190  O  O   . GLY A 1 28  ? 9.386   -28.980 10.959 1.00 23.02 ? 27  GLY A O   1 
ATOM   191  N  N   . PRO A 1 29  ? 10.204  -30.407 12.495 1.00 23.74 ? 28  PRO A N   1 
ATOM   192  C  CA  . PRO A 1 29  ? 8.897   -30.701 13.085 1.00 22.94 ? 28  PRO A CA  1 
ATOM   193  C  C   . PRO A 1 29  ? 8.323   -29.494 13.810 1.00 20.79 ? 28  PRO A C   1 
ATOM   194  O  O   . PRO A 1 29  ? 9.061   -28.627 14.289 1.00 22.04 ? 28  PRO A O   1 
ATOM   195  C  CB  . PRO A 1 29  ? 9.208   -31.795 14.113 1.00 27.68 ? 28  PRO A CB  1 
ATOM   196  C  CG  . PRO A 1 29  ? 10.580  -32.275 13.795 1.00 30.16 ? 28  PRO A CG  1 
ATOM   197  C  CD  . PRO A 1 29  ? 11.291  -31.125 13.176 1.00 28.28 ? 28  PRO A CD  1 
ATOM   198  N  N   . VAL A 1 30  ? 7.002   -29.445 13.882 1.00 18.85 ? 29  VAL A N   1 
ATOM   199  C  CA  . VAL A 1 30  ? 6.315   -28.461 14.694 1.00 17.76 ? 29  VAL A CA  1 
ATOM   200  C  C   . VAL A 1 30  ? 5.917   -29.131 15.998 1.00 18.08 ? 29  VAL A C   1 
ATOM   201  O  O   . VAL A 1 30  ? 5.259   -30.175 15.992 1.00 19.39 ? 29  VAL A O   1 
ATOM   202  C  CB  . VAL A 1 30  ? 5.045   -27.956 13.991 1.00 15.62 ? 29  VAL A CB  1 
ATOM   203  C  CG1 . VAL A 1 30  ? 4.307   -26.948 14.870 1.00 16.91 ? 29  VAL A CG1 1 
ATOM   204  C  CG2 . VAL A 1 30  ? 5.397   -27.339 12.634 1.00 17.46 ? 29  VAL A CG2 1 
ATOM   205  N  N   . LYS A 1 31  ? 6.329   -28.544 17.116 1.00 17.64 ? 30  LYS A N   1 
ATOM   206  C  CA  . LYS A 1 31  ? 5.878   -29.012 18.418 1.00 17.73 ? 30  LYS A CA  1 
ATOM   207  C  C   . LYS A 1 31  ? 4.528   -28.373 18.721 1.00 16.32 ? 30  LYS A C   1 
ATOM   208  O  O   . LYS A 1 31  ? 4.362   -27.163 18.578 1.00 17.20 ? 30  LYS A O   1 
ATOM   209  C  CB  . LYS A 1 31  ? 6.886   -28.636 19.501 1.00 23.03 ? 30  LYS A CB  1 
ATOM   210  C  CG  . LYS A 1 31  ? 6.539   -29.175 20.875 1.00 29.25 ? 30  LYS A CG  1 
ATOM   211  C  CD  . LYS A 1 31  ? 6.597   -30.696 20.897 1.00 37.69 ? 30  LYS A CD  1 
ATOM   212  C  CE  . LYS A 1 31  ? 6.268   -31.236 22.273 1.00 42.88 ? 30  LYS A CE  1 
ATOM   213  N  NZ  . LYS A 1 31  ? 4.933   -30.777 22.730 1.00 45.37 ? 30  LYS A NZ  1 
ATOM   214  N  N   . VAL A 1 32  ? 3.568   -29.195 19.132 1.00 16.40 ? 31  VAL A N   1 
ATOM   215  C  CA  . VAL A 1 32  ? 2.227   -28.731 19.451 1.00 15.80 ? 31  VAL A CA  1 
ATOM   216  C  C   . VAL A 1 32  ? 1.916   -29.165 20.867 1.00 17.38 ? 31  VAL A C   1 
ATOM   217  O  O   . VAL A 1 32  ? 2.003   -30.352 21.195 1.00 18.43 ? 31  VAL A O   1 
ATOM   218  C  CB  . VAL A 1 32  ? 1.172   -29.354 18.513 1.00 16.17 ? 31  VAL A CB  1 
ATOM   219  C  CG1 . VAL A 1 32  ? -0.193  -28.726 18.765 1.00 18.48 ? 31  VAL A CG1 1 
ATOM   220  C  CG2 . VAL A 1 32  ? 1.583   -29.188 17.049 1.00 17.87 ? 31  VAL A CG2 1 
ATOM   221  N  N   . TRP A 1 33  ? 1.559   -28.212 21.717 1.00 15.78 ? 32  TRP A N   1 
ATOM   222  C  CA  . TRP A 1 33  ? 1.286   -28.558 23.104 1.00 17.63 ? 32  TRP A CA  1 
ATOM   223  C  C   . TRP A 1 33  ? 0.318   -27.604 23.782 1.00 16.29 ? 32  TRP A C   1 
ATOM   224  O  O   . TRP A 1 33  ? 0.223   -26.428 23.437 1.00 16.14 ? 32  TRP A O   1 
ATOM   225  C  CB  . TRP A 1 33  ? 2.584   -28.667 23.899 1.00 19.05 ? 32  TRP A CB  1 
ATOM   226  C  CG  . TRP A 1 33  ? 3.162   -27.356 24.325 1.00 20.03 ? 32  TRP A CG  1 
ATOM   227  C  CD1 . TRP A 1 33  ? 3.074   -26.791 25.563 1.00 20.83 ? 32  TRP A CD1 1 
ATOM   228  C  CD2 . TRP A 1 33  ? 3.920   -26.442 23.519 1.00 21.09 ? 32  TRP A CD2 1 
ATOM   229  N  NE1 . TRP A 1 33  ? 3.734   -25.585 25.583 1.00 21.75 ? 32  TRP A NE1 1 
ATOM   230  C  CE2 . TRP A 1 33  ? 4.259   -25.346 24.340 1.00 21.68 ? 32  TRP A CE2 1 
ATOM   231  C  CE3 . TRP A 1 33  ? 4.346   -26.444 22.186 1.00 23.09 ? 32  TRP A CE3 1 
ATOM   232  C  CZ2 . TRP A 1 33  ? 5.005   -24.263 23.873 1.00 22.86 ? 32  TRP A CZ2 1 
ATOM   233  C  CZ3 . TRP A 1 33  ? 5.089   -25.364 21.722 1.00 22.89 ? 32  TRP A CZ3 1 
ATOM   234  C  CH2 . TRP A 1 33  ? 5.409   -24.290 22.566 1.00 23.82 ? 32  TRP A CH2 1 
ATOM   235  N  N   . GLY A 1 34  ? -0.396  -28.126 24.764 1.00 15.17 ? 33  GLY A N   1 
ATOM   236  C  CA  . GLY A 1 34  ? -1.373  -27.333 25.474 1.00 15.09 ? 33  GLY A CA  1 
ATOM   237  C  C   . GLY A 1 34  ? -2.378  -28.260 26.096 1.00 15.10 ? 33  GLY A C   1 
ATOM   238  O  O   . GLY A 1 34  ? -2.082  -29.429 26.356 1.00 16.12 ? 33  GLY A O   1 
ATOM   239  N  N   . SER A 1 35  ? -3.572  -27.747 26.344 1.00 14.59 ? 34  SER A N   1 
ATOM   240  C  CA  . SER A 1 35  ? -4.599  -28.570 26.946 1.00 17.36 ? 34  SER A CA  1 
ATOM   241  C  C   . SER A 1 35  ? -5.976  -28.113 26.512 1.00 15.28 ? 34  SER A C   1 
ATOM   242  O  O   . SER A 1 35  ? -6.180  -26.950 26.130 1.00 16.62 ? 34  SER A O   1 
ATOM   243  C  CB  . SER A 1 35  ? -4.491  -28.567 28.472 1.00 24.86 ? 34  SER A CB  1 
ATOM   244  O  OG  . SER A 1 35  ? -4.691  -27.270 28.995 1.00 30.80 ? 34  SER A OG  1 
ATOM   245  N  N   . ILE A 1 36  ? -6.913  -29.048 26.571 1.00 15.03 ? 35  ILE A N   1 
ATOM   246  C  CA  . ILE A 1 36  ? -8.298  -28.797 26.221 1.00 15.34 ? 35  ILE A CA  1 
ATOM   247  C  C   . ILE A 1 36  ? -9.165  -29.333 27.355 1.00 15.63 ? 35  ILE A C   1 
ATOM   248  O  O   . ILE A 1 36  ? -8.940  -30.443 27.849 1.00 17.33 ? 35  ILE A O   1 
ATOM   249  C  CB  . ILE A 1 36  ? -8.668  -29.498 24.894 1.00 15.16 ? 35  ILE A CB  1 
ATOM   250  C  CG1 . ILE A 1 36  ? -7.678  -29.113 23.791 1.00 16.73 ? 35  ILE A CG1 1 
ATOM   251  C  CG2 . ILE A 1 36  ? -10.084 -29.146 24.480 1.00 17.13 ? 35  ILE A CG2 1 
ATOM   252  C  CD1 . ILE A 1 36  ? -7.864  -29.889 22.510 1.00 17.91 ? 35  ILE A CD1 1 
ATOM   253  N  N   . LYS A 1 37  ? -10.125 -28.525 27.791 1.00 13.33 ? 36  LYS A N   1 
ATOM   254  C  CA  . LYS A 1 37  ? -11.028 -28.905 28.866 1.00 15.06 ? 36  LYS A CA  1 
ATOM   255  C  C   . LYS A 1 37  ? -12.450 -29.028 28.337 1.00 14.81 ? 36  LYS A C   1 
ATOM   256  O  O   . LYS A 1 37  ? -12.754 -28.560 27.236 1.00 13.93 ? 36  LYS A O   1 
ATOM   257  C  CB  . LYS A 1 37  ? -10.966 -27.868 29.986 1.00 20.25 ? 36  LYS A CB  1 
ATOM   258  C  CG  . LYS A 1 37  ? -9.568  -27.678 30.548 1.00 29.66 ? 36  LYS A CG  1 
ATOM   259  C  CD  . LYS A 1 37  ? -9.557  -26.683 31.693 1.00 36.79 ? 36  LYS A CD  1 
ATOM   260  C  CE  . LYS A 1 37  ? -8.184  -26.615 32.338 1.00 40.58 ? 36  LYS A CE  1 
ATOM   261  N  NZ  . LYS A 1 37  ? -7.803  -27.908 32.976 1.00 42.58 ? 36  LYS A NZ  1 
ATOM   262  N  N   . GLY A 1 38  ? -13.312 -29.676 29.116 1.00 13.66 ? 37  GLY A N   1 
ATOM   263  C  CA  . GLY A 1 38  ? -14.723 -29.774 28.792 1.00 13.30 ? 37  GLY A CA  1 
ATOM   264  C  C   . GLY A 1 38  ? -15.092 -30.901 27.846 1.00 15.18 ? 37  GLY A C   1 
ATOM   265  O  O   . GLY A 1 38  ? -16.205 -30.931 27.320 1.00 15.72 ? 37  GLY A O   1 
ATOM   266  N  N   . LEU A 1 39  ? -14.165 -31.830 27.636 1.00 15.11 ? 38  LEU A N   1 
ATOM   267  C  CA  . LEU A 1 39  ? -14.379 -32.955 26.727 1.00 15.06 ? 38  LEU A CA  1 
ATOM   268  C  C   . LEU A 1 39  ? -14.961 -34.185 27.420 1.00 16.51 ? 38  LEU A C   1 
ATOM   269  O  O   . LEU A 1 39  ? -14.785 -34.375 28.626 1.00 17.83 ? 38  LEU A O   1 
ATOM   270  C  CB  . LEU A 1 39  ? -13.051 -33.350 26.076 1.00 13.67 ? 38  LEU A CB  1 
ATOM   271  C  CG  . LEU A 1 39  ? -12.412 -32.335 25.135 1.00 13.16 ? 38  LEU A CG  1 
ATOM   272  C  CD1 . LEU A 1 39  ? -10.951 -32.707 24.880 1.00 15.47 ? 38  LEU A CD1 1 
ATOM   273  C  CD2 . LEU A 1 39  ? -13.206 -32.282 23.843 1.00 16.05 ? 38  LEU A CD2 1 
ATOM   274  N  N   . THR A 1 40  ? -15.658 -35.026 26.657 1.00 16.00 ? 39  THR A N   1 
ATOM   275  C  CA  . THR A 1 40  ? -16.013 -36.348 27.160 1.00 17.47 ? 39  THR A CA  1 
ATOM   276  C  C   . THR A 1 40  ? -14.747 -37.194 27.269 1.00 17.03 ? 39  THR A C   1 
ATOM   277  O  O   . THR A 1 40  ? -13.823 -37.042 26.472 1.00 16.51 ? 39  THR A O   1 
ATOM   278  C  CB  . THR A 1 40  ? -17.038 -37.061 26.256 1.00 18.75 ? 39  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 40  ? -16.532 -37.147 24.917 1.00 19.91 ? 39  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 40  ? -18.341 -36.293 26.239 1.00 17.17 ? 39  THR A CG2 1 
ATOM   281  N  N   . GLU A 1 41  ? -14.697 -38.068 28.269 1.00 18.22 ? 40  GLU A N   1 
ATOM   282  C  CA  . GLU A 1 41  ? -13.543 -38.941 28.452 1.00 20.49 ? 40  GLU A CA  1 
ATOM   283  C  C   . GLU A 1 41  ? -13.299 -39.751 27.181 1.00 20.56 ? 40  GLU A C   1 
ATOM   284  O  O   . GLU A 1 41  ? -14.239 -40.270 26.577 1.00 22.99 ? 40  GLU A O   1 
ATOM   285  C  CB  . GLU A 1 41  ? -13.762 -39.876 29.644 1.00 23.19 ? 40  GLU A CB  1 
ATOM   286  C  CG  . GLU A 1 41  ? -12.575 -40.772 29.968 1.00 27.37 ? 40  GLU A CG  1 
ATOM   287  C  CD  . GLU A 1 41  ? -12.820 -41.647 31.188 1.00 33.68 ? 40  GLU A CD  1 
ATOM   288  O  OE1 . GLU A 1 41  ? -13.922 -41.569 31.775 1.00 36.35 ? 40  GLU A OE1 1 
ATOM   289  O  OE2 . GLU A 1 41  ? -11.910 -42.415 31.563 1.00 35.90 ? 40  GLU A OE2 1 
ATOM   290  N  N   . GLY A 1 42  ? -12.042 -39.845 26.763 1.00 17.93 ? 41  GLY A N   1 
ATOM   291  C  CA  . GLY A 1 42  ? -11.705 -40.666 25.613 1.00 18.10 ? 41  GLY A CA  1 
ATOM   292  C  C   . GLY A 1 42  ? -11.142 -39.896 24.433 1.00 16.08 ? 41  GLY A C   1 
ATOM   293  O  O   . GLY A 1 42  ? -10.653 -38.779 24.588 1.00 16.86 ? 41  GLY A O   1 
ATOM   294  N  N   . LEU A 1 43  ? -11.230 -40.491 23.246 1.00 18.03 ? 42  LEU A N   1 
ATOM   295  C  CA  . LEU A 1 43  ? -10.539 -39.971 22.063 1.00 20.25 ? 42  LEU A CA  1 
ATOM   296  C  C   . LEU A 1 43  ? -11.324 -38.907 21.309 1.00 17.35 ? 42  LEU A C   1 
ATOM   297  O  O   . LEU A 1 43  ? -12.536 -39.040 21.117 1.00 20.26 ? 42  LEU A O   1 
ATOM   298  C  CB  . LEU A 1 43  ? -10.223 -41.114 21.098 1.00 22.50 ? 42  LEU A CB  1 
ATOM   299  C  CG  . LEU A 1 43  ? -9.198  -42.144 21.566 1.00 25.56 ? 42  LEU A CG  1 
ATOM   300  C  CD1 . LEU A 1 43  ? -9.153  -43.316 20.603 1.00 29.73 ? 42  LEU A CD1 1 
ATOM   301  C  CD2 . LEU A 1 43  ? -7.834  -41.489 21.690 1.00 25.81 ? 42  LEU A CD2 1 
ATOM   302  N  N   . HIS A 1 44  ? -10.619 -37.869 20.857 1.00 16.37 ? 43  HIS A N   1 
ATOM   303  C  CA  . HIS A 1 44  ? -11.227 -36.801 20.064 1.00 16.24 ? 43  HIS A CA  1 
ATOM   304  C  C   . HIS A 1 44  ? -10.358 -36.390 18.878 1.00 16.47 ? 43  HIS A C   1 
ATOM   305  O  O   . HIS A 1 44  ? -9.174  -36.106 19.038 1.00 15.79 ? 43  HIS A O   1 
ATOM   306  C  CB  . HIS A 1 44  ? -11.486 -35.582 20.947 1.00 17.34 ? 43  HIS A CB  1 
ATOM   307  C  CG  . HIS A 1 44  ? -12.499 -35.829 22.016 1.00 16.34 ? 43  HIS A CG  1 
ATOM   308  N  ND1 . HIS A 1 44  ? -13.849 -35.629 21.818 1.00 18.40 ? 43  HIS A ND1 1 
ATOM   309  C  CD2 . HIS A 1 44  ? -12.367 -36.296 23.279 1.00 16.12 ? 43  HIS A CD2 1 
ATOM   310  C  CE1 . HIS A 1 44  ? -14.503 -35.945 22.921 1.00 18.15 ? 43  HIS A CE1 1 
ATOM   311  N  NE2 . HIS A 1 44  ? -13.626 -36.361 23.820 1.00 17.42 ? 43  HIS A NE2 1 
ATOM   312  N  N   . GLY A 1 45  ? -10.953 -36.341 17.690 1.00 15.67 ? 44  GLY A N   1 
ATOM   313  C  CA  . GLY A 1 45  ? -10.229 -35.910 16.506 1.00 15.88 ? 44  GLY A CA  1 
ATOM   314  C  C   . GLY A 1 45  ? -9.706  -34.492 16.663 1.00 14.19 ? 44  GLY A C   1 
ATOM   315  O  O   . GLY A 1 45  ? -10.369 -33.640 17.248 1.00 17.07 ? 44  GLY A O   1 
ATOM   316  N  N   . PHE A 1 46  ? -8.513  -34.243 16.137 1.00 13.21 ? 45  PHE A N   1 
ATOM   317  C  CA  . PHE A 1 46  ? -7.822  -32.972 16.326 1.00 14.57 ? 45  PHE A CA  1 
ATOM   318  C  C   . PHE A 1 46  ? -7.257  -32.581 14.967 1.00 14.56 ? 45  PHE A C   1 
ATOM   319  O  O   . PHE A 1 46  ? -6.309  -33.209 14.484 1.00 16.72 ? 45  PHE A O   1 
ATOM   320  C  CB  . PHE A 1 46  ? -6.708  -33.190 17.356 1.00 16.06 ? 45  PHE A CB  1 
ATOM   321  C  CG  . PHE A 1 46  ? -6.108  -31.932 17.918 1.00 16.69 ? 45  PHE A CG  1 
ATOM   322  C  CD1 . PHE A 1 46  ? -6.908  -30.904 18.393 1.00 17.67 ? 45  PHE A CD1 1 
ATOM   323  C  CD2 . PHE A 1 46  ? -4.728  -31.809 18.026 1.00 16.61 ? 45  PHE A CD2 1 
ATOM   324  C  CE1 . PHE A 1 46  ? -6.338  -29.756 18.938 1.00 17.88 ? 45  PHE A CE1 1 
ATOM   325  C  CE2 . PHE A 1 46  ? -4.151  -30.675 18.566 1.00 17.79 ? 45  PHE A CE2 1 
ATOM   326  C  CZ  . PHE A 1 46  ? -4.952  -29.641 19.018 1.00 17.76 ? 45  PHE A CZ  1 
ATOM   327  N  N   . HIS A 1 47  ? -7.850  -31.566 14.342 1.00 12.97 ? 46  HIS A N   1 
ATOM   328  C  CA  . HIS A 1 47  ? -7.568  -31.265 12.938 1.00 14.79 ? 46  HIS A CA  1 
ATOM   329  C  C   . HIS A 1 47  ? -7.363  -29.788 12.660 1.00 15.73 ? 46  HIS A C   1 
ATOM   330  O  O   . HIS A 1 47  ? -8.030  -28.934 13.248 1.00 15.81 ? 46  HIS A O   1 
ATOM   331  C  CB  . HIS A 1 47  ? -8.739  -31.697 12.050 1.00 19.85 ? 46  HIS A CB  1 
ATOM   332  C  CG  . HIS A 1 47  ? -9.087  -33.146 12.150 1.00 24.28 ? 46  HIS A CG  1 
ATOM   333  N  ND1 . HIS A 1 47  ? -10.371 -33.609 11.970 1.00 29.66 ? 46  HIS A ND1 1 
ATOM   334  C  CD2 . HIS A 1 47  ? -8.325  -34.235 12.400 1.00 26.15 ? 46  HIS A CD2 1 
ATOM   335  C  CE1 . HIS A 1 47  ? -10.388 -34.922 12.109 1.00 29.05 ? 46  HIS A CE1 1 
ATOM   336  N  NE2 . HIS A 1 47  ? -9.160  -35.326 12.372 1.00 26.08 ? 46  HIS A NE2 1 
ATOM   337  N  N   . VAL A 1 48  ? -6.473  -29.495 11.718 1.00 13.41 ? 47  VAL A N   1 
ATOM   338  C  CA  . VAL A 1 48  ? -6.413  -28.167 11.132 1.00 12.74 ? 47  VAL A CA  1 
ATOM   339  C  C   . VAL A 1 48  ? -7.327  -28.149 9.921  1.00 12.60 ? 47  VAL A C   1 
ATOM   340  O  O   . VAL A 1 48  ? -7.224  -29.015 9.042  1.00 13.68 ? 47  VAL A O   1 
ATOM   341  C  CB  . VAL A 1 48  ? -4.982  -27.788 10.692 1.00 11.91 ? 47  VAL A CB  1 
ATOM   342  C  CG1 . VAL A 1 48  ? -4.963  -26.381 10.082 1.00 12.80 ? 47  VAL A CG1 1 
ATOM   343  C  CG2 . VAL A 1 48  ? -4.025  -27.880 11.871 1.00 14.97 ? 47  VAL A CG2 1 
ATOM   344  N  N   . HIS A 1 49  ? -8.216  -27.161 9.878  1.00 11.80 ? 48  HIS A N   1 
ATOM   345  C  CA  . HIS A 1 49  ? -9.103  -26.961 8.741  1.00 11.58 ? 48  HIS A CA  1 
ATOM   346  C  C   . HIS A 1 49  ? -8.632  -25.789 7.893  1.00 14.25 ? 48  HIS A C   1 
ATOM   347  O  O   . HIS A 1 49  ? -7.857  -24.946 8.349  1.00 15.33 ? 48  HIS A O   1 
ATOM   348  C  CB  . HIS A 1 49  ? -10.540 -26.760 9.212  1.00 14.45 ? 48  HIS A CB  1 
ATOM   349  C  CG  . HIS A 1 49  ? -11.167 -28.010 9.745  1.00 14.76 ? 48  HIS A CG  1 
ATOM   350  N  ND1 . HIS A 1 49  ? -12.304 -28.563 9.199  1.00 16.64 ? 48  HIS A ND1 1 
ATOM   351  C  CD2 . HIS A 1 49  ? -10.794 -28.833 10.753 1.00 16.11 ? 48  HIS A CD2 1 
ATOM   352  C  CE1 . HIS A 1 49  ? -12.617 -29.663 9.862  1.00 19.78 ? 48  HIS A CE1 1 
ATOM   353  N  NE2 . HIS A 1 49  ? -11.715 -29.849 10.807 1.00 17.55 ? 48  HIS A NE2 1 
ATOM   354  N  N   . GLU A 1 50  ? -9.124  -25.736 6.662  1.00 13.21 ? 49  GLU A N   1 
ATOM   355  C  CA  . GLU A 1 50  ? -8.541  -24.884 5.636  1.00 15.21 ? 49  GLU A CA  1 
ATOM   356  C  C   . GLU A 1 50  ? -8.622  -23.390 5.922  1.00 13.77 ? 49  GLU A C   1 
ATOM   357  O  O   . GLU A 1 50  ? -7.659  -22.654 5.684  1.00 16.66 ? 49  GLU A O   1 
ATOM   358  C  CB  . GLU A 1 50  ? -9.176  -25.179 4.276  1.00 18.73 ? 49  GLU A CB  1 
ATOM   359  C  CG  . GLU A 1 50  ? -8.503  -24.440 3.145  1.00 23.22 ? 49  GLU A CG  1 
ATOM   360  C  CD  . GLU A 1 50  ? -9.026  -24.851 1.792  1.00 29.06 ? 49  GLU A CD  1 
ATOM   361  O  OE1 . GLU A 1 50  ? -9.928  -25.713 1.746  1.00 29.01 ? 49  GLU A OE1 1 
ATOM   362  O  OE2 . GLU A 1 50  ? -8.534  -24.311 0.774  1.00 32.04 ? 49  GLU A OE2 1 
ATOM   363  N  N   . PHE A 1 51  ? -9.764  -22.931 6.419  1.00 11.87 ? 50  PHE A N   1 
ATOM   364  C  CA  . PHE A 1 51  ? -9.978  -21.492 6.527  1.00 11.32 ? 50  PHE A CA  1 
ATOM   365  C  C   . PHE A 1 51  ? -10.009 -21.011 7.971  1.00 12.65 ? 50  PHE A C   1 
ATOM   366  O  O   . PHE A 1 51  ? -10.571 -21.674 8.850  1.00 15.43 ? 50  PHE A O   1 
ATOM   367  C  CB  . PHE A 1 51  ? -11.277 -21.089 5.829  1.00 13.05 ? 50  PHE A CB  1 
ATOM   368  C  CG  . PHE A 1 51  ? -11.381 -21.575 4.416  1.00 18.44 ? 50  PHE A CG  1 
ATOM   369  C  CD1 . PHE A 1 51  ? -10.491 -21.127 3.449  1.00 20.84 ? 50  PHE A CD1 1 
ATOM   370  C  CD2 . PHE A 1 51  ? -12.372 -22.473 4.050  1.00 20.24 ? 50  PHE A CD2 1 
ATOM   371  C  CE1 . PHE A 1 51  ? -10.588 -21.571 2.132  1.00 23.32 ? 50  PHE A CE1 1 
ATOM   372  C  CE2 . PHE A 1 51  ? -12.473 -22.922 2.747  1.00 23.04 ? 50  PHE A CE2 1 
ATOM   373  C  CZ  . PHE A 1 51  ? -11.579 -22.469 1.782  1.00 22.90 ? 50  PHE A CZ  1 
ATOM   374  N  N   . GLY A 1 52  ? -9.395  -19.855 8.202  1.00 11.24 ? 51  GLY A N   1 
ATOM   375  C  CA  . GLY A 1 52  ? -9.445  -19.192 9.492  1.00 12.64 ? 51  GLY A CA  1 
ATOM   376  C  C   . GLY A 1 52  ? -10.655 -18.283 9.534  1.00 14.03 ? 51  GLY A C   1 
ATOM   377  O  O   . GLY A 1 52  ? -10.551 -17.102 9.860  1.00 15.17 ? 51  GLY A O   1 
ATOM   378  N  N   . ASP A 1 53  ? -11.810 -18.845 9.185  1.00 14.50 ? 52  ASP A N   1 
ATOM   379  C  CA  . ASP A 1 53  ? -13.056 -18.091 9.089  1.00 13.35 ? 52  ASP A CA  1 
ATOM   380  C  C   . ASP A 1 53  ? -13.990 -18.544 10.197 1.00 13.11 ? 52  ASP A C   1 
ATOM   381  O  O   . ASP A 1 53  ? -14.523 -19.657 10.154 1.00 14.88 ? 52  ASP A O   1 
ATOM   382  C  CB  . ASP A 1 53  ? -13.704 -18.334 7.724  1.00 13.89 ? 52  ASP A CB  1 
ATOM   383  C  CG  . ASP A 1 53  ? -14.977 -17.531 7.524  1.00 16.06 ? 52  ASP A CG  1 
ATOM   384  O  OD1 . ASP A 1 53  ? -15.704 -17.258 8.517  1.00 16.09 ? 52  ASP A OD1 1 
ATOM   385  O  OD2 . ASP A 1 53  ? -15.256 -17.182 6.361  1.00 19.14 ? 52  ASP A OD2 1 
ATOM   386  N  N   . ASN A 1 54  ? -14.172 -17.692 11.200 1.00 13.34 ? 53  ASN A N   1 
ATOM   387  C  CA  . ASN A 1 54  ? -14.996 -18.037 12.357 1.00 14.86 ? 53  ASN A CA  1 
ATOM   388  C  C   . ASN A 1 54  ? -16.342 -17.300 12.351 1.00 13.80 ? 53  ASN A C   1 
ATOM   389  O  O   . ASN A 1 54  ? -16.991 -17.158 13.390 1.00 17.38 ? 53  ASN A O   1 
ATOM   390  C  CB  . ASN A 1 54  ? -14.217 -17.750 13.650 1.00 23.13 ? 53  ASN A CB  1 
ATOM   391  C  CG  . ASN A 1 54  ? -14.949 -18.215 14.901 1.00 33.21 ? 53  ASN A CG  1 
ATOM   392  O  OD1 . ASN A 1 54  ? -15.182 -19.409 15.096 1.00 35.93 ? 53  ASN A OD1 1 
ATOM   393  N  ND2 . ASN A 1 54  ? -15.295 -17.269 15.768 1.00 37.50 ? 53  ASN A ND2 1 
ATOM   394  N  N   . THR A 1 55  ? -16.764 -16.841 11.175 1.00 12.54 ? 54  THR A N   1 
ATOM   395  C  CA  . THR A 1 55  ? -18.006 -16.073 11.063 1.00 13.95 ? 54  THR A CA  1 
ATOM   396  C  C   . THR A 1 55  ? -19.239 -16.895 11.424 1.00 16.79 ? 54  THR A C   1 
ATOM   397  O  O   . THR A 1 55  ? -20.250 -16.343 11.868 1.00 19.87 ? 54  THR A O   1 
ATOM   398  C  CB  . THR A 1 55  ? -18.183 -15.431 9.670  1.00 15.08 ? 54  THR A CB  1 
ATOM   399  O  OG1 . THR A 1 55  ? -18.167 -16.445 8.656  1.00 15.99 ? 54  THR A OG1 1 
ATOM   400  C  CG2 . THR A 1 55  ? -17.053 -14.442 9.404  1.00 16.10 ? 54  THR A CG2 1 
ATOM   401  N  N   . ALA A 1 56  ? -19.151 -18.209 11.239 1.00 16.70 ? 55  ALA A N   1 
ATOM   402  C  CA  . ALA A 1 56  ? -20.221 -19.116 11.642 1.00 16.73 ? 55  ALA A CA  1 
ATOM   403  C  C   . ALA A 1 56  ? -19.658 -20.138 12.620 1.00 17.90 ? 55  ALA A C   1 
ATOM   404  O  O   . ALA A 1 56  ? -19.949 -21.326 12.531 1.00 20.76 ? 55  ALA A O   1 
ATOM   405  C  CB  . ALA A 1 56  ? -20.821 -19.812 10.430 1.00 18.51 ? 55  ALA A CB  1 
ATOM   406  N  N   . GLY A 1 57  ? -18.834 -19.667 13.546 1.00 18.79 ? 56  GLY A N   1 
ATOM   407  C  CA  . GLY A 1 57  ? -18.186 -20.556 14.490 1.00 19.93 ? 56  GLY A CA  1 
ATOM   408  C  C   . GLY A 1 57  ? -17.337 -21.575 13.754 1.00 18.66 ? 56  GLY A C   1 
ATOM   409  O  O   . GLY A 1 57  ? -16.632 -21.228 12.810 1.00 19.07 ? 56  GLY A O   1 
ATOM   410  N  N   . CYS A 1 58  ? -17.417 -22.839 14.164 1.00 19.09 ? 57  CYS A N   1 
ATOM   411  C  CA  . CYS A 1 58  ? -16.588 -23.882 13.558 1.00 17.93 ? 57  CYS A CA  1 
ATOM   412  C  C   . CYS A 1 58  ? -17.065 -24.292 12.171 1.00 17.13 ? 57  CYS A C   1 
ATOM   413  O  O   . CYS A 1 58  ? -16.314 -24.889 11.396 1.00 17.92 ? 57  CYS A O   1 
ATOM   414  C  CB  . CYS A 1 58  ? -16.568 -25.123 14.443 1.00 22.11 ? 57  CYS A CB  1 
ATOM   415  S  SG  . CYS A 1 58  ? -16.027 -24.814 16.121 1.00 26.01 ? 57  CYS A SG  1 
ATOM   416  N  N   . THR A 1 59  ? -18.320 -23.982 11.872 1.00 18.37 ? 58  THR A N   1 
ATOM   417  C  CA  . THR A 1 59  ? -18.941 -24.402 10.624 1.00 20.24 ? 58  THR A CA  1 
ATOM   418  C  C   . THR A 1 59  ? -18.282 -23.776 9.402  1.00 21.11 ? 58  THR A C   1 
ATOM   419  O  O   . THR A 1 59  ? -18.237 -24.388 8.331  1.00 28.09 ? 58  THR A O   1 
ATOM   420  C  CB  . THR A 1 59  ? -20.441 -24.063 10.632 1.00 26.46 ? 58  THR A CB  1 
ATOM   421  O  OG1 . THR A 1 59  ? -21.020 -24.539 11.855 1.00 30.02 ? 58  THR A OG1 1 
ATOM   422  C  CG2 . THR A 1 59  ? -21.142 -24.697 9.444  1.00 29.34 ? 58  THR A CG2 1 
ATOM   423  N  N   . SER A 1 60  ? -17.756 -22.566 9.567  1.00 15.36 ? 59  SER A N   1 
ATOM   424  C  CA  . SER A 1 60  ? -17.173 -21.833 8.450  1.00 13.86 ? 59  SER A CA  1 
ATOM   425  C  C   . SER A 1 60  ? -15.690 -22.137 8.211  1.00 14.31 ? 59  SER A C   1 
ATOM   426  O  O   . SER A 1 60  ? -15.080 -21.572 7.306  1.00 15.44 ? 59  SER A O   1 
ATOM   427  C  CB  . SER A 1 60  ? -17.394 -20.331 8.637  1.00 12.75 ? 59  SER A CB  1 
ATOM   428  O  OG  . SER A 1 60  ? -17.170 -19.958 9.986  1.00 13.82 ? 59  SER A OG  1 
ATOM   429  N  N   . ALA A 1 61  ? -15.116 -23.030 9.013  1.00 14.36 ? 60  ALA A N   1 
ATOM   430  C  CA  . ALA A 1 61  ? -13.698 -23.361 8.893  1.00 14.60 ? 60  ALA A CA  1 
ATOM   431  C  C   . ALA A 1 61  ? -13.374 -24.150 7.622  1.00 13.89 ? 60  ALA A C   1 
ATOM   432  O  O   . ALA A 1 61  ? -12.205 -24.288 7.249  1.00 15.58 ? 60  ALA A O   1 
ATOM   433  C  CB  . ALA A 1 61  ? -13.214 -24.116 10.138 1.00 14.91 ? 60  ALA A CB  1 
ATOM   434  N  N   . GLY A 1 62  ? -14.403 -24.674 6.961  1.00 14.42 ? 61  GLY A N   1 
ATOM   435  C  CA  . GLY A 1 62  ? -14.195 -25.447 5.749  1.00 17.46 ? 61  GLY A CA  1 
ATOM   436  C  C   . GLY A 1 62  ? -13.700 -26.856 6.035  1.00 15.81 ? 61  GLY A C   1 
ATOM   437  O  O   . GLY A 1 62  ? -13.777 -27.323 7.164  1.00 17.03 ? 61  GLY A O   1 
ATOM   438  N  N   . PRO A 1 63  ? -13.168 -27.535 5.009  1.00 17.59 ? 62  PRO A N   1 
ATOM   439  C  CA  . PRO A 1 63  ? -12.711 -28.922 5.120  1.00 18.38 ? 62  PRO A CA  1 
ATOM   440  C  C   . PRO A 1 63  ? -11.362 -29.030 5.810  1.00 18.25 ? 62  PRO A C   1 
ATOM   441  O  O   . PRO A 1 63  ? -10.736 -28.017 6.128  1.00 16.78 ? 62  PRO A O   1 
ATOM   442  C  CB  . PRO A 1 63  ? -12.554 -29.360 3.659  1.00 23.20 ? 62  PRO A CB  1 
ATOM   443  C  CG  . PRO A 1 63  ? -12.550 -28.103 2.842  1.00 24.38 ? 62  PRO A CG  1 
ATOM   444  C  CD  . PRO A 1 63  ? -12.776 -26.924 3.730  1.00 21.14 ? 62  PRO A CD  1 
ATOM   445  N  N   . HIS A 1 64  ? -10.910 -30.260 6.022  1.00 17.59 ? 63  HIS A N   1 
ATOM   446  C  CA  . HIS A 1 64  ? -9.576  -30.483 6.557  1.00 19.62 ? 63  HIS A CA  1 
ATOM   447  C  C   . HIS A 1 64  ? -8.547  -29.875 5.624  1.00 18.39 ? 63  HIS A C   1 
ATOM   448  O  O   . HIS A 1 64  ? -8.684  -29.943 4.400  1.00 21.77 ? 63  HIS A O   1 
ATOM   449  C  CB  . HIS A 1 64  ? -9.302  -31.977 6.719  1.00 23.58 ? 63  HIS A CB  1 
ATOM   450  C  CG  . HIS A 1 64  ? -10.187 -32.642 7.723  1.00 30.90 ? 63  HIS A CG  1 
ATOM   451  N  ND1 . HIS A 1 64  ? -9.878  -33.856 8.296  1.00 35.66 ? 63  HIS A ND1 1 
ATOM   452  C  CD2 . HIS A 1 64  ? -11.371 -32.262 8.259  1.00 35.08 ? 63  HIS A CD2 1 
ATOM   453  C  CE1 . HIS A 1 64  ? -10.835 -34.197 9.142  1.00 37.26 ? 63  HIS A CE1 1 
ATOM   454  N  NE2 . HIS A 1 64  ? -11.752 -33.246 9.139  1.00 36.38 ? 63  HIS A NE2 1 
ATOM   455  N  N   . PHE A 1 65  ? -7.519  -29.277 6.213  1.00 17.27 ? 64  PHE A N   1 
ATOM   456  C  CA  . PHE A 1 65  ? -6.432  -28.679 5.457  1.00 16.49 ? 64  PHE A CA  1 
ATOM   457  C  C   . PHE A 1 65  ? -5.628  -29.788 4.797  1.00 20.02 ? 64  PHE A C   1 
ATOM   458  O  O   . PHE A 1 65  ? -5.152  -30.701 5.466  1.00 21.00 ? 64  PHE A O   1 
ATOM   459  C  CB  . PHE A 1 65  ? -5.555  -27.846 6.399  1.00 16.14 ? 64  PHE A CB  1 
ATOM   460  C  CG  . PHE A 1 65  ? -4.389  -27.184 5.729  1.00 17.66 ? 64  PHE A CG  1 
ATOM   461  C  CD1 . PHE A 1 65  ? -4.570  -26.378 4.614  1.00 20.39 ? 64  PHE A CD1 1 
ATOM   462  C  CD2 . PHE A 1 65  ? -3.110  -27.342 6.235  1.00 18.06 ? 64  PHE A CD2 1 
ATOM   463  C  CE1 . PHE A 1 65  ? -3.489  -25.759 4.006  1.00 20.32 ? 64  PHE A CE1 1 
ATOM   464  C  CE2 . PHE A 1 65  ? -2.029  -26.729 5.633  1.00 20.80 ? 64  PHE A CE2 1 
ATOM   465  C  CZ  . PHE A 1 65  ? -2.218  -25.932 4.520  1.00 21.53 ? 64  PHE A CZ  1 
ATOM   466  N  N   . ASN A 1 66  ? -5.485  -29.721 3.478  1.00 22.31 ? 65  ASN A N   1 
ATOM   467  C  CA  . ASN A 1 66  ? -4.713  -30.733 2.762  1.00 28.76 ? 65  ASN A CA  1 
ATOM   468  C  C   . ASN A 1 66  ? -4.258  -30.272 1.384  1.00 32.62 ? 65  ASN A C   1 
ATOM   469  O  O   . ASN A 1 66  ? -4.807  -30.705 0.370  1.00 36.17 ? 65  ASN A O   1 
ATOM   470  C  CB  . ASN A 1 66  ? -5.505  -32.032 2.644  1.00 33.11 ? 65  ASN A CB  1 
ATOM   471  C  CG  . ASN A 1 66  ? -4.633  -33.208 2.263  1.00 36.45 ? 65  ASN A CG  1 
ATOM   472  O  OD1 . ASN A 1 66  ? -3.441  -33.244 2.581  1.00 36.75 ? 65  ASN A OD1 1 
ATOM   473  N  ND2 . ASN A 1 66  ? -5.219  -34.177 1.575  1.00 38.39 ? 65  ASN A ND2 1 
ATOM   474  N  N   . PRO A 1 67  ? -3.236  -29.407 1.349  1.00 33.59 ? 66  PRO A N   1 
ATOM   475  C  CA  . PRO A 1 67  ? -2.678  -28.812 0.130  1.00 38.22 ? 66  PRO A CA  1 
ATOM   476  C  C   . PRO A 1 67  ? -2.564  -29.824 -1.004 1.00 43.86 ? 66  PRO A C   1 
ATOM   477  O  O   . PRO A 1 67  ? -2.590  -29.425 -2.173 1.00 47.66 ? 66  PRO A O   1 
ATOM   478  C  CB  . PRO A 1 67  ? -1.281  -28.373 0.570  1.00 38.09 ? 66  PRO A CB  1 
ATOM   479  C  CG  . PRO A 1 67  ? -1.412  -28.085 2.006  1.00 33.70 ? 66  PRO A CG  1 
ATOM   480  C  CD  . PRO A 1 67  ? -2.494  -28.991 2.553  1.00 33.50 ? 66  PRO A CD  1 
ATOM   481  N  N   . ARG A 1 81  ? -3.871  -36.797 5.640  1.00 36.52 ? 80  ARG A N   1 
ATOM   482  C  CA  . ARG A 1 81  ? -4.022  -35.383 5.320  1.00 34.93 ? 80  ARG A CA  1 
ATOM   483  C  C   . ARG A 1 81  ? -3.108  -34.516 6.178  1.00 31.77 ? 80  ARG A C   1 
ATOM   484  O  O   . ARG A 1 81  ? -2.906  -34.788 7.363  1.00 30.72 ? 80  ARG A O   1 
ATOM   485  C  CB  . ARG A 1 81  ? -5.475  -34.940 5.498  1.00 37.60 ? 80  ARG A CB  1 
ATOM   486  C  CG  . ARG A 1 81  ? -6.439  -35.548 4.499  1.00 41.72 ? 80  ARG A CG  1 
ATOM   487  C  CD  . ARG A 1 81  ? -7.852  -35.066 4.759  1.00 45.58 ? 80  ARG A CD  1 
ATOM   488  N  NE  . ARG A 1 81  ? -8.782  -35.537 3.739  1.00 49.91 ? 80  ARG A NE  1 
ATOM   489  C  CZ  . ARG A 1 81  ? -10.089 -35.301 3.756  1.00 54.03 ? 80  ARG A CZ  1 
ATOM   490  N  NH1 . ARG A 1 81  ? -10.622 -34.598 4.746  1.00 55.46 ? 80  ARG A NH1 1 
ATOM   491  N  NH2 . ARG A 1 81  ? -10.862 -35.767 2.784  1.00 55.34 ? 80  ARG A NH2 1 
ATOM   492  N  N   . VAL A 1 82  ? -2.565  -33.466 5.572  1.00 27.67 ? 81  VAL A N   1 
ATOM   493  C  CA  . VAL A 1 82  ? -1.662  -32.558 6.266  1.00 24.65 ? 81  VAL A CA  1 
ATOM   494  C  C   . VAL A 1 82  ? -2.269  -32.065 7.582  1.00 22.13 ? 81  VAL A C   1 
ATOM   495  O  O   . VAL A 1 82  ? -1.601  -32.034 8.618  1.00 22.30 ? 81  VAL A O   1 
ATOM   496  C  CB  . VAL A 1 82  ? -1.305  -31.354 5.373  1.00 26.37 ? 81  VAL A CB  1 
ATOM   497  C  CG1 . VAL A 1 82  ? -0.521  -30.317 6.158  1.00 26.14 ? 81  VAL A CG1 1 
ATOM   498  C  CG2 . VAL A 1 82  ? -0.521  -31.821 4.142  1.00 26.49 ? 81  VAL A CG2 1 
ATOM   499  N  N   . GLY A 1 83  ? -3.542  -31.692 7.540  1.00 20.32 ? 82  GLY A N   1 
ATOM   500  C  CA  . GLY A 1 83  ? -4.195  -31.114 8.700  1.00 19.35 ? 82  GLY A CA  1 
ATOM   501  C  C   . GLY A 1 83  ? -4.608  -32.090 9.784  1.00 20.94 ? 82  GLY A C   1 
ATOM   502  O  O   . GLY A 1 83  ? -5.051  -31.672 10.848 1.00 22.66 ? 82  GLY A O   1 
ATOM   503  N  N   . ASP A 1 84  ? -4.481  -33.387 9.525  1.00 21.86 ? 83  ASP A N   1 
ATOM   504  C  CA  A ASP A 1 84  ? -4.882  -34.386 10.507 0.50 23.52 ? 83  ASP A CA  1 
ATOM   505  C  CA  B ASP A 1 84  ? -4.874  -34.401 10.504 0.50 23.76 ? 83  ASP A CA  1 
ATOM   506  C  C   . ASP A 1 84  ? -3.787  -34.606 11.554 1.00 23.11 ? 83  ASP A C   1 
ATOM   507  O  O   . ASP A 1 84  ? -2.763  -35.237 11.283 1.00 26.28 ? 83  ASP A O   1 
ATOM   508  C  CB  A ASP A 1 84  ? -5.263  -35.695 9.812  0.50 27.50 ? 83  ASP A CB  1 
ATOM   509  C  CB  B ASP A 1 84  ? -5.172  -35.732 9.812  0.50 28.28 ? 83  ASP A CB  1 
ATOM   510  C  CG  A ASP A 1 84  ? -6.418  -35.523 8.835  0.50 30.43 ? 83  ASP A CG  1 
ATOM   511  C  CG  B ASP A 1 84  ? -5.755  -36.768 10.762 0.50 32.07 ? 83  ASP A CG  1 
ATOM   512  O  OD1 A ASP A 1 84  ? -7.172  -34.533 8.964  0.50 28.95 ? 83  ASP A OD1 1 
ATOM   513  O  OD1 B ASP A 1 84  ? -5.733  -36.546 11.993 0.50 32.91 ? 83  ASP A OD1 1 
ATOM   514  O  OD2 A ASP A 1 84  ? -6.574  -36.379 7.939  0.50 33.95 ? 83  ASP A OD2 1 
ATOM   515  O  OD2 B ASP A 1 84  ? -6.236  -37.813 10.274 0.50 35.26 ? 83  ASP A OD2 1 
ATOM   516  N  N   . LEU A 1 85  ? -4.013  -34.080 12.756 1.00 20.21 ? 84  LEU A N   1 
ATOM   517  C  CA  . LEU A 1 85  ? -3.025  -34.167 13.826 1.00 19.96 ? 84  LEU A CA  1 
ATOM   518  C  C   . LEU A 1 85  ? -3.221  -35.391 14.709 1.00 25.06 ? 84  LEU A C   1 
ATOM   519  O  O   . LEU A 1 85  ? -2.473  -35.597 15.665 1.00 30.00 ? 84  LEU A O   1 
ATOM   520  C  CB  . LEU A 1 85  ? -3.029  -32.897 14.679 1.00 20.64 ? 84  LEU A CB  1 
ATOM   521  C  CG  . LEU A 1 85  ? -2.670  -31.616 13.925 1.00 23.03 ? 84  LEU A CG  1 
ATOM   522  C  CD1 . LEU A 1 85  ? -2.605  -30.431 14.869 1.00 26.25 ? 84  LEU A CD1 1 
ATOM   523  C  CD2 . LEU A 1 85  ? -1.360  -31.783 13.179 1.00 28.38 ? 84  LEU A CD2 1 
ATOM   524  N  N   . GLY A 1 86  ? -4.220  -36.203 14.379 1.00 22.28 ? 85  GLY A N   1 
ATOM   525  C  CA  . GLY A 1 86  ? -4.497  -37.419 15.117 1.00 21.90 ? 85  GLY A CA  1 
ATOM   526  C  C   . GLY A 1 86  ? -5.599  -37.235 16.138 1.00 23.26 ? 85  GLY A C   1 
ATOM   527  O  O   . GLY A 1 86  ? -6.512  -36.433 15.945 1.00 26.37 ? 85  GLY A O   1 
ATOM   528  N  N   . ASN A 1 87  ? -5.517  -37.990 17.224 1.00 20.61 ? 86  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 87  ? -6.499  -37.894 18.294 1.00 19.40 ? 86  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 87  ? -5.868  -37.335 19.555 1.00 20.39 ? 86  ASN A C   1 
ATOM   531  O  O   . ASN A 1 87  ? -4.698  -37.591 19.837 1.00 22.70 ? 86  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 87  ? -7.074  -39.272 18.619 1.00 20.96 ? 86  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 87  ? -8.026  -39.776 17.564 1.00 24.52 ? 86  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 87  ? -8.899  -39.049 17.102 1.00 26.63 ? 86  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 87  ? -7.867  -41.033 17.179 1.00 27.58 ? 86  ASN A ND2 1 
ATOM   536  N  N   . VAL A 1 88  ? -6.645  -36.578 20.319 1.00 18.20 ? 87  VAL A N   1 
ATOM   537  C  CA  . VAL A 1 88  ? -6.243  -36.234 21.675 1.00 18.17 ? 87  VAL A CA  1 
ATOM   538  C  C   . VAL A 1 88  ? -7.098  -37.069 22.620 1.00 16.98 ? 87  VAL A C   1 
ATOM   539  O  O   . VAL A 1 88  ? -8.196  -37.498 22.256 1.00 19.72 ? 87  VAL A O   1 
ATOM   540  C  CB  . VAL A 1 88  ? -6.399  -34.725 21.972 1.00 18.33 ? 87  VAL A CB  1 
ATOM   541  C  CG1 . VAL A 1 88  ? -5.495  -33.904 21.050 1.00 21.24 ? 87  VAL A CG1 1 
ATOM   542  C  CG2 . VAL A 1 88  ? -7.851  -34.302 21.838 1.00 19.97 ? 87  VAL A CG2 1 
ATOM   543  N  N   . THR A 1 89  ? -6.592  -37.315 23.822 1.00 16.95 ? 88  THR A N   1 
ATOM   544  C  CA  . THR A 1 89  ? -7.293  -38.160 24.783 1.00 18.22 ? 88  THR A CA  1 
ATOM   545  C  C   . THR A 1 89  ? -7.647  -37.384 26.042 1.00 17.90 ? 88  THR A C   1 
ATOM   546  O  O   . THR A 1 89  ? -6.766  -36.839 26.712 1.00 18.79 ? 88  THR A O   1 
ATOM   547  C  CB  . THR A 1 89  ? -6.437  -39.382 25.187 1.00 22.91 ? 88  THR A CB  1 
ATOM   548  O  OG1 . THR A 1 89  ? -6.074  -40.130 24.018 1.00 27.38 ? 88  THR A OG1 1 
ATOM   549  C  CG2 . THR A 1 89  ? -7.212  -40.274 26.143 1.00 24.63 ? 88  THR A CG2 1 
ATOM   550  N  N   . ALA A 1 90  ? -8.935  -37.345 26.370 1.00 16.36 ? 89  ALA A N   1 
ATOM   551  C  CA  . ALA A 1 90  ? -9.398  -36.663 27.577 1.00 15.16 ? 89  ALA A CA  1 
ATOM   552  C  C   . ALA A 1 90  ? -9.513  -37.628 28.754 1.00 16.30 ? 89  ALA A C   1 
ATOM   553  O  O   . ALA A 1 90  ? -9.953  -38.769 28.587 1.00 17.34 ? 89  ALA A O   1 
ATOM   554  C  CB  . ALA A 1 90  ? -10.737 -35.971 27.319 1.00 15.06 ? 89  ALA A CB  1 
ATOM   555  N  N   . ASP A 1 91  ? -9.111  -37.164 29.938 1.00 15.26 ? 90  ASP A N   1 
ATOM   556  C  CA  . ASP A 1 91  ? -9.187  -37.969 31.158 1.00 16.54 ? 90  ASP A CA  1 
ATOM   557  C  C   . ASP A 1 91  ? -10.596 -37.944 31.750 1.00 18.04 ? 90  ASP A C   1 
ATOM   558  O  O   . ASP A 1 91  ? -11.525 -37.405 31.135 1.00 18.52 ? 90  ASP A O   1 
ATOM   559  C  CB  . ASP A 1 91  ? -8.130  -37.525 32.192 1.00 17.36 ? 90  ASP A CB  1 
ATOM   560  C  CG  . ASP A 1 91  ? -8.365  -36.112 32.724 1.00 17.28 ? 90  ASP A CG  1 
ATOM   561  O  OD1 . ASP A 1 91  ? -9.476  -35.584 32.556 1.00 17.67 ? 90  ASP A OD1 1 
ATOM   562  O  OD2 . ASP A 1 91  ? -7.435  -35.526 33.326 1.00 18.19 ? 90  ASP A OD2 1 
ATOM   563  N  N   . LYS A 1 92  ? -10.758 -38.527 32.936 1.00 18.56 ? 91  LYS A N   1 
ATOM   564  C  CA  . LYS A 1 92  ? -12.078 -38.624 33.565 1.00 20.71 ? 91  LYS A CA  1 
ATOM   565  C  C   . LYS A 1 92  ? -12.656 -37.270 33.975 1.00 18.85 ? 91  LYS A C   1 
ATOM   566  O  O   . LYS A 1 92  ? -13.843 -37.170 34.293 1.00 21.39 ? 91  LYS A O   1 
ATOM   567  C  CB  . LYS A 1 92  ? -12.009 -39.534 34.794 1.00 26.23 ? 91  LYS A CB  1 
ATOM   568  C  CG  . LYS A 1 92  ? -11.076 -39.000 35.862 1.00 31.67 ? 91  LYS A CG  1 
ATOM   569  C  CD  . LYS A 1 92  ? -11.062 -39.867 37.102 1.00 38.70 ? 91  LYS A CD  1 
ATOM   570  C  CE  . LYS A 1 92  ? -10.099 -39.302 38.133 1.00 42.40 ? 91  LYS A CE  1 
ATOM   571  N  NZ  . LYS A 1 92  ? -10.168 -40.049 39.418 1.00 45.98 ? 91  LYS A NZ  1 
ATOM   572  N  N   . ASP A 1 93  ? -11.815 -36.240 33.995 1.00 19.20 ? 92  ASP A N   1 
ATOM   573  C  CA  . ASP A 1 93  ? -12.253 -34.893 34.341 1.00 18.04 ? 92  ASP A CA  1 
ATOM   574  C  C   . ASP A 1 93  ? -12.503 -34.082 33.080 1.00 17.34 ? 92  ASP A C   1 
ATOM   575  O  O   . ASP A 1 93  ? -12.795 -32.885 33.148 1.00 17.78 ? 92  ASP A O   1 
ATOM   576  C  CB  . ASP A 1 93  ? -11.201 -34.184 35.201 1.00 20.25 ? 92  ASP A CB  1 
ATOM   577  C  CG  . ASP A 1 93  ? -11.180 -34.685 36.636 1.00 25.48 ? 92  ASP A CG  1 
ATOM   578  O  OD1 . ASP A 1 93  ? -12.158 -35.338 37.063 1.00 27.35 ? 92  ASP A OD1 1 
ATOM   579  O  OD2 . ASP A 1 93  ? -10.186 -34.409 37.343 1.00 27.92 ? 92  ASP A OD2 1 
ATOM   580  N  N   . GLY A 1 94  ? -12.369 -34.735 31.930 1.00 16.13 ? 93  GLY A N   1 
ATOM   581  C  CA  . GLY A 1 94  ? -12.610 -34.092 30.650 1.00 16.74 ? 93  GLY A CA  1 
ATOM   582  C  C   . GLY A 1 94  ? -11.453 -33.256 30.133 1.00 15.80 ? 93  GLY A C   1 
ATOM   583  O  O   . GLY A 1 94  ? -11.637 -32.426 29.243 1.00 15.54 ? 93  GLY A O   1 
ATOM   584  N  N   . VAL A 1 95  ? -10.260 -33.470 30.682 1.00 14.75 ? 94  VAL A N   1 
ATOM   585  C  CA  . VAL A 1 95  ? -9.095  -32.685 30.299 1.00 13.15 ? 94  VAL A CA  1 
ATOM   586  C  C   . VAL A 1 95  ? -8.186  -33.506 29.411 1.00 14.77 ? 94  VAL A C   1 
ATOM   587  O  O   . VAL A 1 95  ? -7.768  -34.605 29.788 1.00 15.12 ? 94  VAL A O   1 
ATOM   588  C  CB  . VAL A 1 95  ? -8.280  -32.238 31.533 1.00 14.71 ? 94  VAL A CB  1 
ATOM   589  C  CG1 . VAL A 1 95  ? -7.041  -31.435 31.098 1.00 15.15 ? 94  VAL A CG1 1 
ATOM   590  C  CG2 . VAL A 1 95  ? -9.159  -31.433 32.501 1.00 16.67 ? 94  VAL A CG2 1 
ATOM   591  N  N   . ALA A 1 96  ? -7.879  -32.970 28.232 1.00 14.97 ? 95  ALA A N   1 
ATOM   592  C  CA  . ALA A 1 96  ? -6.944  -33.608 27.319 1.00 16.90 ? 95  ALA A CA  1 
ATOM   593  C  C   . ALA A 1 96  ? -5.635  -32.840 27.300 1.00 17.21 ? 95  ALA A C   1 
ATOM   594  O  O   . ALA A 1 96  ? -5.612  -31.633 27.063 1.00 18.51 ? 95  ALA A O   1 
ATOM   595  C  CB  . ALA A 1 96  ? -7.529  -33.692 25.909 1.00 15.62 ? 95  ALA A CB  1 
ATOM   596  N  N   . ASP A 1 97  ? -4.545  -33.543 27.572 1.00 15.81 ? 96  ASP A N   1 
ATOM   597  C  CA  . ASP A 1 97  ? -3.226  -32.969 27.424 1.00 15.07 ? 96  ASP A CA  1 
ATOM   598  C  C   . ASP A 1 97  ? -2.852  -33.122 25.964 1.00 17.73 ? 96  ASP A C   1 
ATOM   599  O  O   . ASP A 1 97  ? -3.093  -34.166 25.363 1.00 24.05 ? 96  ASP A O   1 
ATOM   600  C  CB  . ASP A 1 97  ? -2.223  -33.733 28.283 1.00 18.32 ? 96  ASP A CB  1 
ATOM   601  C  CG  . ASP A 1 97  ? -0.817  -33.200 28.143 1.00 24.15 ? 96  ASP A CG  1 
ATOM   602  O  OD1 . ASP A 1 97  ? -0.628  -31.978 28.318 1.00 26.97 ? 96  ASP A OD1 1 
ATOM   603  O  OD2 . ASP A 1 97  ? 0.099   -34.000 27.853 1.00 26.82 ? 96  ASP A OD2 1 
ATOM   604  N  N   . VAL A 1 98  ? -2.271  -32.085 25.386 1.00 14.24 ? 97  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 98  ? -1.805  -32.170 24.013 1.00 14.95 ? 97  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 98  ? -0.291  -32.058 23.995 1.00 15.99 ? 97  VAL A C   1 
ATOM   607  O  O   . VAL A 1 98  ? 0.279   -31.081 24.480 1.00 17.02 ? 97  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 98  ? -2.423  -31.065 23.137 1.00 16.00 ? 97  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 98  ? -1.875  -31.148 21.719 1.00 20.71 ? 97  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 98  ? -3.954  -31.173 23.153 1.00 19.40 ? 97  VAL A CG2 1 
ATOM   611  N  N   . SER A 1 99  ? 0.358   -33.077 23.452 1.00 16.94 ? 98  SER A N   1 
ATOM   612  C  CA  . SER A 1 99  ? 1.796   -33.059 23.279 1.00 20.64 ? 98  SER A CA  1 
ATOM   613  C  C   . SER A 1 99  ? 2.117   -33.859 22.028 1.00 22.69 ? 98  SER A C   1 
ATOM   614  O  O   . SER A 1 99  ? 2.162   -35.092 22.049 1.00 26.13 ? 98  SER A O   1 
ATOM   615  C  CB  . SER A 1 99  ? 2.512   -33.633 24.502 1.00 24.14 ? 98  SER A CB  1 
ATOM   616  O  OG  . SER A 1 99  ? 3.916   -33.504 24.346 1.00 26.92 ? 98  SER A OG  1 
ATOM   617  N  N   . ILE A 1 100 ? 2.313   -33.132 20.936 1.00 23.44 ? 99  ILE A N   1 
ATOM   618  C  CA  . ILE A 1 100 ? 2.472   -33.712 19.614 1.00 24.13 ? 99  ILE A CA  1 
ATOM   619  C  C   . ILE A 1 100 ? 3.717   -33.133 18.962 1.00 24.56 ? 99  ILE A C   1 
ATOM   620  O  O   . ILE A 1 100 ? 4.046   -31.962 19.161 1.00 25.68 ? 99  ILE A O   1 
ATOM   621  C  CB  . ILE A 1 100 ? 1.247   -33.366 18.722 1.00 24.93 ? 99  ILE A CB  1 
ATOM   622  C  CG1 . ILE A 1 100 ? -0.034  -33.967 19.305 1.00 26.15 ? 99  ILE A CG1 1 
ATOM   623  C  CG2 . ILE A 1 100 ? 1.459   -33.837 17.290 1.00 28.39 ? 99  ILE A CG2 1 
ATOM   624  C  CD1 . ILE A 1 100 ? -1.287  -33.612 18.523 1.00 27.83 ? 99  ILE A CD1 1 
ATOM   625  N  N   . GLU A 1 101 ? 4.423   -33.961 18.204 1.00 23.13 ? 100 GLU A N   1 
ATOM   626  C  CA  . GLU A 1 101 ? 5.444   -33.467 17.297 1.00 23.87 ? 100 GLU A CA  1 
ATOM   627  C  C   . GLU A 1 101 ? 5.020   -33.908 15.905 1.00 24.88 ? 100 GLU A C   1 
ATOM   628  O  O   . GLU A 1 101 ? 4.799   -35.098 15.665 1.00 28.05 ? 100 GLU A O   1 
ATOM   629  C  CB  . GLU A 1 101 ? 6.819   -34.036 17.664 1.00 29.76 ? 100 GLU A CB  1 
ATOM   630  C  CG  . GLU A 1 101 ? 7.983   -33.294 17.036 1.00 37.48 ? 100 GLU A CG  1 
ATOM   631  C  CD  . GLU A 1 101 ? 9.287   -33.513 17.786 1.00 44.28 ? 100 GLU A CD  1 
ATOM   632  O  OE1 . GLU A 1 101 ? 10.337  -33.666 17.128 1.00 47.20 ? 100 GLU A OE1 1 
ATOM   633  O  OE2 . GLU A 1 101 ? 9.261   -33.527 19.037 1.00 46.87 ? 100 GLU A OE2 1 
ATOM   634  N  N   . ASP A 1 102 ? 4.880   -32.952 14.992 1.00 21.99 ? 101 ASP A N   1 
ATOM   635  C  CA  . ASP A 1 102 ? 4.360   -33.254 13.667 1.00 23.64 ? 101 ASP A CA  1 
ATOM   636  C  C   . ASP A 1 102 ? 5.272   -32.664 12.603 1.00 22.79 ? 101 ASP A C   1 
ATOM   637  O  O   . ASP A 1 102 ? 5.601   -31.480 12.644 1.00 23.34 ? 101 ASP A O   1 
ATOM   638  C  CB  . ASP A 1 102 ? 2.938   -32.709 13.519 1.00 25.19 ? 101 ASP A CB  1 
ATOM   639  C  CG  . ASP A 1 102 ? 2.240   -33.226 12.274 1.00 29.34 ? 101 ASP A CG  1 
ATOM   640  O  OD1 . ASP A 1 102 ? 1.340   -34.082 12.406 1.00 35.98 ? 101 ASP A OD1 1 
ATOM   641  O  OD2 . ASP A 1 102 ? 2.590   -32.780 11.165 1.00 26.51 ? 101 ASP A OD2 1 
ATOM   642  N  N   . SER A 1 103 ? 5.685   -33.491 11.651 1.00 25.39 ? 102 SER A N   1 
ATOM   643  C  CA  . SER A 1 103 ? 6.652   -33.053 10.654 1.00 25.50 ? 102 SER A CA  1 
ATOM   644  C  C   . SER A 1 103 ? 6.023   -32.746 9.294  1.00 26.31 ? 102 SER A C   1 
ATOM   645  O  O   . SER A 1 103 ? 6.731   -32.424 8.334  1.00 28.76 ? 102 SER A O   1 
ATOM   646  C  CB  . SER A 1 103 ? 7.773   -34.084 10.514 1.00 30.62 ? 102 SER A CB  1 
ATOM   647  O  OG  . SER A 1 103 ? 7.258   -35.347 10.126 1.00 35.82 ? 102 SER A OG  1 
ATOM   648  N  N   . VAL A 1 104 ? 4.699   -32.845 9.215  1.00 23.57 ? 103 VAL A N   1 
ATOM   649  C  CA  . VAL A 1 104 ? 3.981   -32.540 7.982  1.00 23.33 ? 103 VAL A CA  1 
ATOM   650  C  C   . VAL A 1 104 ? 3.447   -31.105 7.980  1.00 22.49 ? 103 VAL A C   1 
ATOM   651  O  O   . VAL A 1 104 ? 3.567   -30.396 6.981  1.00 23.97 ? 103 VAL A O   1 
ATOM   652  C  CB  . VAL A 1 104 ? 2.829   -33.531 7.724  1.00 27.94 ? 103 VAL A CB  1 
ATOM   653  C  CG1 . VAL A 1 104 ? 2.152   -33.210 6.407  1.00 30.76 ? 103 VAL A CG1 1 
ATOM   654  C  CG2 . VAL A 1 104 ? 3.354   -34.965 7.720  1.00 30.02 ? 103 VAL A CG2 1 
ATOM   655  N  N   . ILE A 1 105 ? 2.861   -30.671 9.091  1.00 20.02 ? 104 ILE A N   1 
ATOM   656  C  CA  . ILE A 1 105 ? 2.449   -29.277 9.190  1.00 17.44 ? 104 ILE A CA  1 
ATOM   657  C  C   . ILE A 1 105 ? 3.696   -28.408 9.297  1.00 17.65 ? 104 ILE A C   1 
ATOM   658  O  O   . ILE A 1 105 ? 4.800   -28.910 9.532  1.00 19.00 ? 104 ILE A O   1 
ATOM   659  C  CB  . ILE A 1 105 ? 1.519   -29.004 10.384 1.00 17.67 ? 104 ILE A CB  1 
ATOM   660  C  CG1 . ILE A 1 105 ? 2.210   -29.362 11.700 1.00 17.93 ? 104 ILE A CG1 1 
ATOM   661  C  CG2 . ILE A 1 105 ? 0.195   -29.760 10.226 1.00 19.21 ? 104 ILE A CG2 1 
ATOM   662  C  CD1 . ILE A 1 105 ? 1.472   -28.851 12.919 1.00 17.73 ? 104 ILE A CD1 1 
ATOM   663  N  N   . SER A 1 106 ? 3.518   -27.106 9.120  1.00 17.61 ? 105 SER A N   1 
ATOM   664  C  CA  . SER A 1 106 ? 4.629   -26.168 9.196  1.00 15.80 ? 105 SER A CA  1 
ATOM   665  C  C   . SER A 1 106 ? 4.105   -24.799 9.615  1.00 16.67 ? 105 SER A C   1 
ATOM   666  O  O   . SER A 1 106 ? 2.905   -24.527 9.515  1.00 16.66 ? 105 SER A O   1 
ATOM   667  C  CB  . SER A 1 106 ? 5.334   -26.069 7.840  1.00 18.57 ? 105 SER A CB  1 
ATOM   668  O  OG  . SER A 1 106 ? 6.569   -25.388 7.954  1.00 20.00 ? 105 SER A OG  1 
ATOM   669  N  N   . LEU A 1 107 ? 5.003   -23.954 10.107 1.00 15.90 ? 106 LEU A N   1 
ATOM   670  C  CA  . LEU A 1 107 ? 4.671   -22.568 10.393 1.00 16.63 ? 106 LEU A CA  1 
ATOM   671  C  C   . LEU A 1 107 ? 5.233   -21.645 9.303  1.00 20.13 ? 106 LEU A C   1 
ATOM   672  O  O   . LEU A 1 107 ? 5.280   -20.425 9.471  1.00 24.33 ? 106 LEU A O   1 
ATOM   673  C  CB  . LEU A 1 107 ? 5.156   -22.159 11.790 1.00 16.69 ? 106 LEU A CB  1 
ATOM   674  C  CG  . LEU A 1 107 ? 4.597   -23.001 12.951 1.00 14.70 ? 106 LEU A CG  1 
ATOM   675  C  CD1 . LEU A 1 107 ? 5.082   -22.460 14.276 1.00 16.92 ? 106 LEU A CD1 1 
ATOM   676  C  CD2 . LEU A 1 107 ? 3.059   -23.065 12.938 1.00 15.53 ? 106 LEU A CD2 1 
ATOM   677  N  N   . SER A 1 108 ? 5.662   -22.245 8.192  1.00 19.83 ? 107 SER A N   1 
ATOM   678  C  CA  . SER A 1 108 ? 6.004   -21.499 6.975  1.00 23.85 ? 107 SER A CA  1 
ATOM   679  C  C   . SER A 1 108 ? 5.920   -22.397 5.731  1.00 25.51 ? 107 SER A C   1 
ATOM   680  O  O   . SER A 1 108 ? 5.730   -23.605 5.849  1.00 27.81 ? 107 SER A O   1 
ATOM   681  C  CB  . SER A 1 108 ? 7.385   -20.858 7.098  1.00 28.69 ? 107 SER A CB  1 
ATOM   682  O  OG  . SER A 1 108 ? 8.395   -21.840 7.206  1.00 29.35 ? 107 SER A OG  1 
ATOM   683  N  N   . GLY A 1 109 ? 6.038   -21.813 4.540  1.00 26.11 ? 108 GLY A N   1 
ATOM   684  C  CA  . GLY A 1 109 ? 5.986   -22.602 3.316  1.00 26.20 ? 108 GLY A CA  1 
ATOM   685  C  C   . GLY A 1 109 ? 4.590   -23.086 2.958  1.00 25.31 ? 108 GLY A C   1 
ATOM   686  O  O   . GLY A 1 109 ? 3.602   -22.558 3.462  1.00 24.95 ? 108 GLY A O   1 
ATOM   687  N  N   . ASP A 1 110 ? 4.499   -24.102 2.098  1.00 24.42 ? 109 ASP A N   1 
ATOM   688  C  CA  . ASP A 1 110 ? 3.192   -24.543 1.583  1.00 25.93 ? 109 ASP A CA  1 
ATOM   689  C  C   . ASP A 1 110 ? 2.303   -25.294 2.582  1.00 24.18 ? 109 ASP A C   1 
ATOM   690  O  O   . ASP A 1 110 ? 1.080   -25.362 2.413  1.00 26.38 ? 109 ASP A O   1 
ATOM   691  C  CB  . ASP A 1 110 ? 3.347   -25.357 0.291  1.00 31.65 ? 109 ASP A CB  1 
ATOM   692  C  CG  . ASP A 1 110 ? 4.267   -26.549 0.450  1.00 35.06 ? 109 ASP A CG  1 
ATOM   693  O  OD1 . ASP A 1 110 ? 5.281   -26.435 1.170  1.00 36.60 ? 109 ASP A OD1 1 
ATOM   694  O  OD2 . ASP A 1 110 ? 3.982   -27.601 -0.160 1.00 38.41 ? 109 ASP A OD2 1 
ATOM   695  N  N   . HIS A 1 111 ? 2.901   -25.861 3.619  1.00 19.65 ? 110 HIS A N   1 
ATOM   696  C  CA  . HIS A 1 111 ? 2.101   -26.549 4.634  1.00 17.89 ? 110 HIS A CA  1 
ATOM   697  C  C   . HIS A 1 111 ? 1.844   -25.656 5.837  1.00 17.16 ? 110 HIS A C   1 
ATOM   698  O  O   . HIS A 1 111 ? 1.530   -26.136 6.926  1.00 16.77 ? 110 HIS A O   1 
ATOM   699  C  CB  . HIS A 1 111 ? 2.777   -27.849 5.067  1.00 21.68 ? 110 HIS A CB  1 
ATOM   700  C  CG  . HIS A 1 111 ? 2.776   -28.908 4.009  1.00 26.20 ? 110 HIS A CG  1 
ATOM   701  N  ND1 . HIS A 1 111 ? 3.210   -30.195 4.242  1.00 29.69 ? 110 HIS A ND1 1 
ATOM   702  C  CD2 . HIS A 1 111 ? 2.386   -28.872 2.713  1.00 28.25 ? 110 HIS A CD2 1 
ATOM   703  C  CE1 . HIS A 1 111 ? 3.095   -30.905 3.132  1.00 31.01 ? 110 HIS A CE1 1 
ATOM   704  N  NE2 . HIS A 1 111 ? 2.599   -30.125 2.189  1.00 28.37 ? 110 HIS A NE2 1 
HETATM 705  N  N   . OCS A 1 112 ? 1.981   -24.353 5.633  1.00 18.67 ? 111 OCS A N   1 
HETATM 706  C  CA  . OCS A 1 112 ? 1.851   -23.396 6.720  1.00 16.31 ? 111 OCS A CA  1 
HETATM 707  C  CB  . OCS A 1 112 ? 2.316   -22.027 6.250  1.00 19.33 ? 111 OCS A CB  1 
HETATM 708  S  SG  . OCS A 1 112 ? 2.230   -20.766 7.520  1.00 21.72 ? 111 OCS A SG  1 
HETATM 709  C  C   . OCS A 1 112 ? 0.416   -23.327 7.234  1.00 15.06 ? 111 OCS A C   1 
HETATM 710  O  O   . OCS A 1 112 ? -0.526  -23.191 6.449  1.00 16.58 ? 111 OCS A O   1 
HETATM 711  O  OD1 . OCS A 1 112 ? 0.903   -20.264 7.553  0.36 18.61 ? 111 OCS A OD1 1 
HETATM 712  O  OD2 . OCS A 1 112 ? 3.118   -19.705 7.188  0.43 23.36 ? 111 OCS A OD2 1 
HETATM 713  O  OD3 . OCS A 1 112 ? 2.565   -21.312 8.781  0.25 22.28 ? 111 OCS A OD3 1 
ATOM   714  N  N   . ILE A 1 113 ? 0.257   -23.416 8.553  1.00 12.86 ? 112 ILE A N   1 
ATOM   715  C  CA  . ILE A 1 113 ? -1.065  -23.448 9.169  1.00 13.07 ? 112 ILE A CA  1 
ATOM   716  C  C   . ILE A 1 113 ? -1.455  -22.147 9.877  1.00 12.77 ? 112 ILE A C   1 
ATOM   717  O  O   . ILE A 1 113 ? -2.546  -22.049 10.445 1.00 12.26 ? 112 ILE A O   1 
ATOM   718  C  CB  . ILE A 1 113 ? -1.189  -24.619 10.164 1.00 14.33 ? 112 ILE A CB  1 
ATOM   719  C  CG1 . ILE A 1 113 ? -0.178  -24.462 11.308 1.00 14.60 ? 112 ILE A CG1 1 
ATOM   720  C  CG2 . ILE A 1 113 ? -1.014  -25.961 9.428  1.00 14.81 ? 112 ILE A CG2 1 
ATOM   721  C  CD1 . ILE A 1 113 ? -0.339  -25.496 12.417 1.00 18.59 ? 112 ILE A CD1 1 
ATOM   722  N  N   . ILE A 1 114 ? -0.574  -21.153 9.852  1.00 12.01 ? 113 ILE A N   1 
ATOM   723  C  CA  . ILE A 1 114 ? -0.916  -19.864 10.435 1.00 12.28 ? 113 ILE A CA  1 
ATOM   724  C  C   . ILE A 1 114 ? -2.086  -19.241 9.673  1.00 11.13 ? 113 ILE A C   1 
ATOM   725  O  O   . ILE A 1 114 ? -2.108  -19.226 8.435  1.00 13.61 ? 113 ILE A O   1 
ATOM   726  C  CB  . ILE A 1 114 ? 0.306   -18.919 10.503 1.00 14.49 ? 113 ILE A CB  1 
ATOM   727  C  CG1 . ILE A 1 114 ? 1.304   -19.474 11.533 1.00 19.14 ? 113 ILE A CG1 1 
ATOM   728  C  CG2 . ILE A 1 114 ? -0.128  -17.502 10.849 1.00 13.89 ? 113 ILE A CG2 1 
ATOM   729  C  CD1 . ILE A 1 114 ? 2.610   -18.725 11.636 1.00 24.78 ? 113 ILE A CD1 1 
ATOM   730  N  N   . GLY A 1 115 ? -3.076  -18.763 10.422 1.00 10.00 ? 114 GLY A N   1 
ATOM   731  C  CA  . GLY A 1 115 ? -4.255  -18.164 9.826  1.00 10.79 ? 114 GLY A CA  1 
ATOM   732  C  C   . GLY A 1 115 ? -5.314  -19.184 9.453  1.00 9.54  ? 114 GLY A C   1 
ATOM   733  O  O   . GLY A 1 115 ? -6.361  -18.830 8.916  1.00 11.14 ? 114 GLY A O   1 
ATOM   734  N  N   . ARG A 1 116 ? -5.059  -20.454 9.750  1.00 10.99 ? 115 ARG A N   1 
ATOM   735  C  CA  . ARG A 1 116 ? -6.073  -21.480 9.538  1.00 11.18 ? 115 ARG A CA  1 
ATOM   736  C  C   . ARG A 1 116 ? -6.756  -21.822 10.856 1.00 10.87 ? 115 ARG A C   1 
ATOM   737  O  O   . ARG A 1 116 ? -6.445  -21.222 11.879 1.00 13.06 ? 115 ARG A O   1 
ATOM   738  C  CB  . ARG A 1 116 ? -5.461  -22.702 8.856  1.00 12.20 ? 115 ARG A CB  1 
ATOM   739  C  CG  . ARG A 1 116 ? -4.767  -22.275 7.566  1.00 14.80 ? 115 ARG A CG  1 
ATOM   740  C  CD  . ARG A 1 116 ? -4.470  -23.400 6.618  1.00 17.42 ? 115 ARG A CD  1 
ATOM   741  N  NE  . ARG A 1 116 ? -3.635  -22.940 5.506  1.00 18.83 ? 115 ARG A NE  1 
ATOM   742  C  CZ  . ARG A 1 116 ? -4.105  -22.548 4.322  1.00 19.31 ? 115 ARG A CZ  1 
ATOM   743  N  NH1 . ARG A 1 116 ? -5.410  -22.561 4.087  1.00 19.84 ? 115 ARG A NH1 1 
ATOM   744  N  NH2 . ARG A 1 116 ? -3.271  -22.159 3.363  1.00 19.50 ? 115 ARG A NH2 1 
ATOM   745  N  N   . THR A 1 117 ? -7.695  -22.763 10.841 1.00 11.44 ? 116 THR A N   1 
ATOM   746  C  CA  . THR A 1 117 ? -8.473  -23.045 12.045 1.00 11.65 ? 116 THR A CA  1 
ATOM   747  C  C   . THR A 1 117 ? -8.132  -24.405 12.623 1.00 12.44 ? 116 THR A C   1 
ATOM   748  O  O   . THR A 1 117 ? -8.087  -25.401 11.904 1.00 16.23 ? 116 THR A O   1 
ATOM   749  C  CB  . THR A 1 117 ? -10.002 -22.977 11.765 1.00 11.93 ? 116 THR A CB  1 
ATOM   750  O  OG1 . THR A 1 117 ? -10.367 -21.632 11.441 1.00 15.16 ? 116 THR A OG1 1 
ATOM   751  C  CG2 . THR A 1 117 ? -10.817 -23.429 12.985 1.00 14.19 ? 116 THR A CG2 1 
ATOM   752  N  N   . LEU A 1 118 ? -7.889  -24.441 13.929 1.00 11.27 ? 117 LEU A N   1 
ATOM   753  C  CA  . LEU A 1 118 ? -7.716  -25.697 14.636 1.00 11.06 ? 117 LEU A CA  1 
ATOM   754  C  C   . LEU A 1 118 ? -9.073  -26.110 15.208 1.00 11.86 ? 117 LEU A C   1 
ATOM   755  O  O   . LEU A 1 118 ? -9.778  -25.286 15.787 1.00 12.97 ? 117 LEU A O   1 
ATOM   756  C  CB  . LEU A 1 118 ? -6.693  -25.521 15.756 1.00 13.49 ? 117 LEU A CB  1 
ATOM   757  C  CG  . LEU A 1 118 ? -6.288  -26.757 16.550 1.00 14.07 ? 117 LEU A CG  1 
ATOM   758  C  CD1 . LEU A 1 118 ? -5.581  -27.780 15.663 1.00 15.66 ? 117 LEU A CD1 1 
ATOM   759  C  CD2 . LEU A 1 118 ? -5.387  -26.329 17.714 1.00 16.11 ? 117 LEU A CD2 1 
ATOM   760  N  N   . VAL A 1 119 ? -9.440  -27.377 15.035 1.00 11.63 ? 118 VAL A N   1 
ATOM   761  C  CA  . VAL A 1 119 ? -10.745 -27.873 15.474 1.00 11.54 ? 118 VAL A CA  1 
ATOM   762  C  C   . VAL A 1 119 ? -10.580 -29.141 16.299 1.00 13.38 ? 118 VAL A C   1 
ATOM   763  O  O   . VAL A 1 119 ? -9.807  -30.026 15.936 1.00 14.19 ? 118 VAL A O   1 
ATOM   764  C  CB  . VAL A 1 119 ? -11.664 -28.195 14.267 1.00 11.93 ? 118 VAL A CB  1 
ATOM   765  C  CG1 . VAL A 1 119 ? -13.010 -28.781 14.737 1.00 16.46 ? 118 VAL A CG1 1 
ATOM   766  C  CG2 . VAL A 1 119 ? -11.887 -26.959 13.403 1.00 12.64 ? 118 VAL A CG2 1 
ATOM   767  N  N   . VAL A 1 120 ? -11.295 -29.230 17.415 1.00 12.52 ? 119 VAL A N   1 
ATOM   768  C  CA  . VAL A 1 120 ? -11.374 -30.487 18.150 1.00 13.63 ? 119 VAL A CA  1 
ATOM   769  C  C   . VAL A 1 120 ? -12.771 -31.066 17.970 1.00 13.58 ? 119 VAL A C   1 
ATOM   770  O  O   . VAL A 1 120 ? -13.777 -30.351 18.078 1.00 13.70 ? 119 VAL A O   1 
ATOM   771  C  CB  . VAL A 1 120 ? -11.019 -30.323 19.646 1.00 14.28 ? 119 VAL A CB  1 
ATOM   772  C  CG1 . VAL A 1 120 ? -11.936 -29.315 20.308 1.00 16.41 ? 119 VAL A CG1 1 
ATOM   773  C  CG2 . VAL A 1 120 ? -11.078 -31.664 20.358 1.00 15.98 ? 119 VAL A CG2 1 
ATOM   774  N  N   . HIS A 1 121 ? -12.821 -32.360 17.684 1.00 15.33 ? 120 HIS A N   1 
ATOM   775  C  CA  . HIS A 1 121 ? -14.054 -33.021 17.282 1.00 15.62 ? 120 HIS A CA  1 
ATOM   776  C  C   . HIS A 1 121 ? -14.673 -33.881 18.372 1.00 17.95 ? 120 HIS A C   1 
ATOM   777  O  O   . HIS A 1 121 ? -13.998 -34.323 19.303 1.00 19.43 ? 120 HIS A O   1 
ATOM   778  C  CB  . HIS A 1 121 ? -13.803 -33.889 16.053 1.00 18.69 ? 120 HIS A CB  1 
ATOM   779  C  CG  . HIS A 1 121 ? -13.645 -33.112 14.787 1.00 22.47 ? 120 HIS A CG  1 
ATOM   780  N  ND1 . HIS A 1 121 ? -14.702 -32.846 13.942 1.00 23.54 ? 120 HIS A ND1 1 
ATOM   781  C  CD2 . HIS A 1 121 ? -12.557 -32.545 14.216 1.00 23.77 ? 120 HIS A CD2 1 
ATOM   782  C  CE1 . HIS A 1 121 ? -14.271 -32.152 12.906 1.00 26.46 ? 120 HIS A CE1 1 
ATOM   783  N  NE2 . HIS A 1 121 ? -12.973 -31.951 13.049 1.00 23.65 ? 120 HIS A NE2 1 
ATOM   784  N  N   . GLU A 1 122 ? -15.963 -34.137 18.208 1.00 18.83 ? 121 GLU A N   1 
ATOM   785  C  CA  . GLU A 1 122 ? -16.757 -34.915 19.143 1.00 22.39 ? 121 GLU A CA  1 
ATOM   786  C  C   . GLU A 1 122 ? -16.310 -36.371 19.189 1.00 25.26 ? 121 GLU A C   1 
ATOM   787  O  O   . GLU A 1 122 ? -16.276 -36.987 20.257 1.00 26.43 ? 121 GLU A O   1 
ATOM   788  C  CB  . GLU A 1 122 ? -18.229 -34.829 18.733 1.00 26.98 ? 121 GLU A CB  1 
ATOM   789  C  CG  . GLU A 1 122 ? -19.178 -35.714 19.521 1.00 33.41 ? 121 GLU A CG  1 
ATOM   790  C  CD  . GLU A 1 122 ? -20.508 -35.901 18.808 1.00 40.60 ? 121 GLU A CD  1 
ATOM   791  O  OE1 . GLU A 1 122 ? -20.732 -35.224 17.782 1.00 42.46 ? 121 GLU A OE1 1 
ATOM   792  O  OE2 . GLU A 1 122 ? -21.325 -36.731 19.265 1.00 43.79 ? 121 GLU A OE2 1 
ATOM   793  N  N   . LYS A 1 123 ? -15.971 -36.921 18.027 1.00 24.97 ? 122 LYS A N   1 
ATOM   794  C  CA  . LYS A 1 123 ? -15.606 -38.328 17.941 1.00 27.98 ? 122 LYS A CA  1 
ATOM   795  C  C   . LYS A 1 123 ? -14.144 -38.522 17.570 1.00 25.54 ? 122 LYS A C   1 
ATOM   796  O  O   . LYS A 1 123 ? -13.483 -37.602 17.088 1.00 25.70 ? 122 LYS A O   1 
ATOM   797  C  CB  . LYS A 1 123 ? -16.493 -39.048 16.924 1.00 32.97 ? 122 LYS A CB  1 
ATOM   798  C  CG  . LYS A 1 123 ? -17.978 -38.941 17.210 1.00 37.89 ? 122 LYS A CG  1 
ATOM   799  C  CD  . LYS A 1 123 ? -18.774 -39.838 16.276 1.00 42.79 ? 122 LYS A CD  1 
ATOM   800  C  CE  . LYS A 1 123 ? -20.266 -39.651 16.484 1.00 47.08 ? 122 LYS A CE  1 
ATOM   801  N  NZ  . LYS A 1 123 ? -20.632 -39.745 17.926 1.00 49.57 ? 122 LYS A NZ  1 
ATOM   802  N  N   . ALA A 1 124 ? -13.651 -39.733 17.802 1.00 25.35 ? 123 ALA A N   1 
ATOM   803  C  CA  . ALA A 1 124 ? -12.289 -40.103 17.445 1.00 28.51 ? 123 ALA A CA  1 
ATOM   804  C  C   . ALA A 1 124 ? -12.115 -40.080 15.936 1.00 32.88 ? 123 ALA A C   1 
ATOM   805  O  O   . ALA A 1 124 ? -13.081 -40.256 15.194 1.00 34.67 ? 123 ALA A O   1 
ATOM   806  C  CB  . ALA A 1 124 ? -11.970 -41.492 17.982 1.00 28.98 ? 123 ALA A CB  1 
ATOM   807  N  N   . ASP A 1 125 ? -10.882 -39.869 15.487 1.00 36.38 ? 124 ASP A N   1 
ATOM   808  C  CA  . ASP A 1 125 ? -10.558 -39.950 14.066 1.00 42.46 ? 124 ASP A CA  1 
ATOM   809  C  C   . ASP A 1 125 ? -10.827 -41.349 13.530 1.00 43.02 ? 124 ASP A C   1 
ATOM   810  O  O   . ASP A 1 125 ? -10.150 -42.304 13.908 1.00 45.57 ? 124 ASP A O   1 
ATOM   811  C  CB  . ASP A 1 125 ? -9.093  -39.588 13.831 1.00 47.27 ? 124 ASP A CB  1 
ATOM   812  C  CG  . ASP A 1 125 ? -8.925  -38.213 13.229 1.00 52.77 ? 124 ASP A CG  1 
ATOM   813  O  OD1 . ASP A 1 125 ? -8.018  -37.476 13.670 1.00 54.78 ? 124 ASP A OD1 1 
ATOM   814  O  OD2 . ASP A 1 125 ? -9.698  -37.873 12.310 1.00 55.70 ? 124 ASP A OD2 1 
ATOM   815  N  N   . GLY A 1 142 ? -16.735 -36.441 13.855 1.00 44.15 ? 141 GLY A N   1 
ATOM   816  C  CA  . GLY A 1 142 ? -18.051 -35.999 14.280 1.00 43.07 ? 141 GLY A CA  1 
ATOM   817  C  C   . GLY A 1 142 ? -18.180 -34.487 14.340 1.00 40.11 ? 141 GLY A C   1 
ATOM   818  O  O   . GLY A 1 142 ? -17.449 -33.763 13.657 1.00 39.76 ? 141 GLY A O   1 
ATOM   819  N  N   . SER A 1 143 ? -19.112 -34.017 15.168 1.00 34.26 ? 142 SER A N   1 
ATOM   820  C  CA  . SER A 1 143 ? -19.379 -32.588 15.324 1.00 30.32 ? 142 SER A CA  1 
ATOM   821  C  C   . SER A 1 143 ? -18.157 -31.792 15.784 1.00 24.86 ? 142 SER A C   1 
ATOM   822  O  O   . SER A 1 143 ? -17.301 -32.296 16.513 1.00 25.12 ? 142 SER A O   1 
ATOM   823  C  CB  . SER A 1 143 ? -20.534 -32.371 16.301 1.00 35.76 ? 142 SER A CB  1 
ATOM   824  O  OG  . SER A 1 143 ? -20.829 -30.993 16.441 1.00 40.30 ? 142 SER A OG  1 
ATOM   825  N  N   . ARG A 1 144 ? -18.090 -30.538 15.358 1.00 19.90 ? 143 ARG A N   1 
ATOM   826  C  CA  . ARG A 1 144 ? -16.981 -29.666 15.722 1.00 17.27 ? 143 ARG A CA  1 
ATOM   827  C  C   . ARG A 1 144 ? -17.274 -28.984 17.051 1.00 17.84 ? 143 ARG A C   1 
ATOM   828  O  O   . ARG A 1 144 ? -18.129 -28.096 17.130 1.00 22.89 ? 143 ARG A O   1 
ATOM   829  C  CB  . ARG A 1 144 ? -16.738 -28.640 14.615 1.00 16.99 ? 143 ARG A CB  1 
ATOM   830  C  CG  . ARG A 1 144 ? -16.454 -29.299 13.274 1.00 17.86 ? 143 ARG A CG  1 
ATOM   831  C  CD  . ARG A 1 144 ? -16.293 -28.291 12.148 1.00 18.55 ? 143 ARG A CD  1 
ATOM   832  N  NE  . ARG A 1 144 ? -16.168 -28.978 10.870 1.00 18.95 ? 143 ARG A NE  1 
ATOM   833  C  CZ  . ARG A 1 144 ? -15.890 -28.383 9.717  1.00 19.72 ? 143 ARG A CZ  1 
ATOM   834  N  NH1 . ARG A 1 144 ? -15.702 -27.069 9.671  1.00 21.88 ? 143 ARG A NH1 1 
ATOM   835  N  NH2 . ARG A 1 144 ? -15.808 -29.107 8.607  1.00 21.82 ? 143 ARG A NH2 1 
ATOM   836  N  N   . LEU A 1 145 ? -16.571 -29.408 18.097 1.00 14.31 ? 144 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 145 ? -16.886 -28.953 19.454 1.00 14.14 ? 144 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 145 ? -16.324 -27.579 19.778 1.00 12.94 ? 144 LEU A C   1 
ATOM   839  O  O   . LEU A 1 145 ? -16.945 -26.806 20.498 1.00 14.75 ? 144 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 145 ? -16.363 -29.949 20.485 1.00 15.42 ? 144 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 145 ? -16.899 -31.372 20.413 1.00 19.29 ? 144 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 145 ? -16.239 -32.216 21.501 1.00 24.07 ? 144 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 145 ? -18.408 -31.354 20.573 1.00 23.62 ? 144 LEU A CD2 1 
ATOM   844  N  N   . ALA A 1 146 ? -15.127 -27.293 19.282 1.00 12.15 ? 145 ALA A N   1 
ATOM   845  C  CA  . ALA A 1 146 ? -14.491 -26.014 19.549 1.00 11.64 ? 145 ALA A CA  1 
ATOM   846  C  C   . ALA A 1 146 ? -13.433 -25.756 18.498 1.00 10.92 ? 145 ALA A C   1 
ATOM   847  O  O   . ALA A 1 146 ? -12.904 -26.687 17.887 1.00 13.10 ? 145 ALA A O   1 
ATOM   848  C  CB  . ALA A 1 146 ? -13.864 -25.998 20.943 1.00 13.35 ? 145 ALA A CB  1 
ATOM   849  N  N   . CYS A 1 147 ? -13.131 -24.485 18.281 1.00 10.98 ? 146 CYS A N   1 
ATOM   850  C  CA  . CYS A 1 147 ? -12.142 -24.120 17.288 1.00 11.36 ? 146 CYS A CA  1 
ATOM   851  C  C   . CYS A 1 147 ? -11.587 -22.735 17.562 1.00 12.65 ? 146 CYS A C   1 
ATOM   852  O  O   . CYS A 1 147 ? -12.108 -21.981 18.398 1.00 12.26 ? 146 CYS A O   1 
ATOM   853  C  CB  . CYS A 1 147 ? -12.768 -24.150 15.891 1.00 12.96 ? 146 CYS A CB  1 
ATOM   854  S  SG  . CYS A 1 147 ? -14.042 -22.899 15.679 1.00 19.11 ? 146 CYS A SG  1 
ATOM   855  N  N   . GLY A 1 148 ? -10.515 -22.403 16.855 1.00 10.80 ? 147 GLY A N   1 
ATOM   856  C  CA  . GLY A 1 148 ? -9.941  -21.075 16.944 1.00 11.66 ? 147 GLY A CA  1 
ATOM   857  C  C   . GLY A 1 148 ? -9.006  -20.873 15.777 1.00 10.80 ? 147 GLY A C   1 
ATOM   858  O  O   . GLY A 1 148 ? -8.563  -21.843 15.164 1.00 11.48 ? 147 GLY A O   1 
ATOM   859  N  N   . VAL A 1 149 ? -8.725  -19.618 15.457 1.00 10.91 ? 148 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 149 ? -7.802  -19.303 14.381 1.00 10.44 ? 148 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 149 ? -6.383  -19.356 14.932 1.00 9.93  ? 148 VAL A C   1 
ATOM   862  O  O   . VAL A 1 149 ? -6.112  -18.867 16.030 1.00 12.58 ? 148 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 149 ? -8.102  -17.926 13.763 1.00 10.57 ? 148 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 149 ? -7.099  -17.610 12.640 1.00 12.92 ? 148 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 149 ? -9.552  -17.885 13.225 1.00 13.77 ? 148 VAL A CG2 1 
ATOM   866  N  N   . ILE A 1 150 ? -5.476  -19.957 14.172 1.00 9.68  ? 149 ILE A N   1 
ATOM   867  C  CA  . ILE A 1 150 ? -4.089  -20.083 14.602 1.00 10.94 ? 149 ILE A CA  1 
ATOM   868  C  C   . ILE A 1 150 ? -3.345  -18.780 14.324 1.00 11.16 ? 149 ILE A C   1 
ATOM   869  O  O   . ILE A 1 150 ? -3.269  -18.324 13.183 1.00 13.80 ? 149 ILE A O   1 
ATOM   870  C  CB  . ILE A 1 150 ? -3.400  -21.268 13.896 1.00 11.16 ? 149 ILE A CB  1 
ATOM   871  C  CG1 . ILE A 1 150 ? -4.132  -22.570 14.231 1.00 11.28 ? 149 ILE A CG1 1 
ATOM   872  C  CG2 . ILE A 1 150 ? -1.933  -21.345 14.285 1.00 11.51 ? 149 ILE A CG2 1 
ATOM   873  C  CD1 . ILE A 1 150 ? -3.762  -23.725 13.332 1.00 13.72 ? 149 ILE A CD1 1 
ATOM   874  N  N   . GLY A 1 151 ? -2.806  -18.171 15.372 1.00 9.47  ? 150 GLY A N   1 
ATOM   875  C  CA  . GLY A 1 151 ? -2.177  -16.868 15.237 1.00 10.24 ? 150 GLY A CA  1 
ATOM   876  C  C   . GLY A 1 151 ? -0.705  -16.851 15.589 1.00 11.77 ? 150 GLY A C   1 
ATOM   877  O  O   . GLY A 1 151 ? -0.204  -17.742 16.277 1.00 13.08 ? 150 GLY A O   1 
ATOM   878  N  N   . ILE A 1 152 ? -0.008  -15.824 15.118 1.00 11.08 ? 151 ILE A N   1 
ATOM   879  C  CA  . ILE A 1 152 ? 1.401   -15.649 15.431 1.00 11.92 ? 151 ILE A CA  1 
ATOM   880  C  C   . ILE A 1 152 ? 1.564   -15.296 16.901 1.00 13.00 ? 151 ILE A C   1 
ATOM   881  O  O   . ILE A 1 152 ? 0.833   -14.455 17.435 1.00 14.76 ? 151 ILE A O   1 
ATOM   882  C  CB  . ILE A 1 152 ? 2.023   -14.554 14.552 1.00 13.45 ? 151 ILE A CB  1 
ATOM   883  C  CG1 . ILE A 1 152 ? 1.946   -14.981 13.087 1.00 16.13 ? 151 ILE A CG1 1 
ATOM   884  C  CG2 . ILE A 1 152 ? 3.456   -14.282 14.972 1.00 16.47 ? 151 ILE A CG2 1 
ATOM   885  C  CD1 . ILE A 1 152 ? 2.247   -13.873 12.100 1.00 20.60 ? 151 ILE A CD1 1 
ATOM   886  N  N   . ALA A 1 153 ? 2.520   -15.946 17.558 1.00 12.65 ? 152 ALA A N   1 
ATOM   887  C  CA  . ALA A 1 153 ? 2.713   -15.745 18.991 1.00 15.91 ? 152 ALA A CA  1 
ATOM   888  C  C   . ALA A 1 153 ? 4.112   -15.250 19.300 1.00 19.65 ? 152 ALA A C   1 
ATOM   889  O  O   . ALA A 1 153 ? 5.037   -15.412 18.499 1.00 19.84 ? 152 ALA A O   1 
ATOM   890  C  CB  . ALA A 1 153 ? 2.428   -17.036 19.755 1.00 17.46 ? 152 ALA A CB  1 
ATOM   891  N  N   . GLN A 1 154 ? 4.248   -14.645 20.475 1.00 22.68 ? 153 GLN A N   1 
ATOM   892  C  CA  . GLN A 1 154 ? 5.507   -14.086 20.932 1.00 33.42 ? 153 GLN A CA  1 
ATOM   893  C  C   . GLN A 1 154 ? 6.410   -15.197 21.439 1.00 40.56 ? 153 GLN A C   1 
ATOM   894  O  O   . GLN A 1 154 ? 5.935   -16.161 22.045 1.00 42.98 ? 153 GLN A O   1 
ATOM   895  C  CB  . GLN A 1 154 ? 5.238   -13.079 22.051 1.00 36.76 ? 153 GLN A CB  1 
ATOM   896  C  CG  . GLN A 1 154 ? 6.333   -12.062 22.270 1.00 41.35 ? 153 GLN A CG  1 
ATOM   897  C  CD  . GLN A 1 154 ? 5.868   -10.921 23.148 1.00 44.79 ? 153 GLN A CD  1 
ATOM   898  O  OE1 . GLN A 1 154 ? 4.860   -11.033 23.850 1.00 49.28 ? 153 GLN A OE1 1 
ATOM   899  N  NE2 . GLN A 1 154 ? 6.592   -9.815  23.110 1.00 43.81 ? 153 GLN A NE2 1 
ATOM   900  O  OXT . GLN A 1 154 ? 7.630   -15.152 21.261 1.00 43.87 ? 153 GLN A OXT 1 
HETATM 901  C  C   . ACE B 2 1   ? -2.094  -16.863 -1.210 1.00 47.03 ? 0   ACE B C   1 
HETATM 902  O  O   . ACE B 2 1   ? -0.908  -17.127 -1.429 1.00 51.65 ? 0   ACE B O   1 
HETATM 903  C  CH3 . ACE B 2 1   ? -3.187  -17.214 -2.177 1.00 45.77 ? 0   ACE B CH3 1 
ATOM   904  N  N   . ALA B 2 2   ? -2.415  -16.451 0.015  1.00 32.88 ? 1   ALA B N   1 
ATOM   905  C  CA  . ALA B 2 2   ? -3.772  -16.031 0.345  1.00 29.19 ? 1   ALA B CA  1 
ATOM   906  C  C   . ALA B 2 2   ? -4.134  -14.725 -0.356 1.00 26.37 ? 1   ALA B C   1 
ATOM   907  O  O   . ALA B 2 2   ? -3.329  -13.793 -0.409 1.00 26.77 ? 1   ALA B O   1 
ATOM   908  C  CB  . ALA B 2 2   ? -3.934  -15.884 1.849  1.00 30.97 ? 1   ALA B CB  1 
ATOM   909  N  N   . THR B 2 3   ? -5.349  -14.662 -0.888 1.00 23.08 ? 2   THR B N   1 
ATOM   910  C  CA  . THR B 2 3   ? -5.815  -13.450 -1.536 1.00 19.94 ? 2   THR B CA  1 
ATOM   911  C  C   . THR B 2 3   ? -6.987  -12.845 -0.782 1.00 15.18 ? 2   THR B C   1 
ATOM   912  O  O   . THR B 2 3   ? -7.397  -11.724 -1.067 1.00 15.05 ? 2   THR B O   1 
ATOM   913  C  CB  . THR B 2 3   ? -6.230  -13.714 -2.986 1.00 23.47 ? 2   THR B CB  1 
ATOM   914  O  OG1 . THR B 2 3   ? -7.287  -14.679 -3.004 1.00 26.67 ? 2   THR B OG1 1 
ATOM   915  C  CG2 . THR B 2 3   ? -5.045  -14.245 -3.784 1.00 26.68 ? 2   THR B CG2 1 
ATOM   916  N  N   . LYS B 2 4   ? -7.533  -13.592 0.176  1.00 13.90 ? 3   LYS B N   1 
ATOM   917  C  CA  . LYS B 2 4   ? -8.632  -13.084 0.995  1.00 13.35 ? 3   LYS B CA  1 
ATOM   918  C  C   . LYS B 2 4   ? -8.445  -13.479 2.452  1.00 11.81 ? 3   LYS B C   1 
ATOM   919  O  O   . LYS B 2 4   ? -7.965  -14.572 2.751  1.00 12.50 ? 3   LYS B O   1 
ATOM   920  C  CB  . LYS B 2 4   ? -9.992  -13.594 0.499  1.00 18.46 ? 3   LYS B CB  1 
ATOM   921  C  CG  . LYS B 2 4   ? -10.455 -13.011 -0.828 1.00 24.96 ? 3   LYS B CG  1 
ATOM   922  C  CD  . LYS B 2 4   ? -11.967 -13.120 -0.961 1.00 32.12 ? 3   LYS B CD  1 
ATOM   923  C  CE  . LYS B 2 4   ? -12.657 -12.362 0.170  1.00 39.20 ? 3   LYS B CE  1 
ATOM   924  N  NZ  . LYS B 2 4   ? -14.131 -12.257 -0.005 1.00 43.52 ? 3   LYS B NZ  1 
ATOM   925  N  N   . ALA B 2 5   ? -8.818  -12.578 3.354  1.00 11.39 ? 4   ALA B N   1 
ATOM   926  C  CA  . ALA B 2 5   ? -8.743  -12.849 4.782  1.00 10.41 ? 4   ALA B CA  1 
ATOM   927  C  C   . ALA B 2 5   ? -10.004 -12.328 5.452  1.00 10.87 ? 4   ALA B C   1 
ATOM   928  O  O   . ALA B 2 5   ? -10.751 -11.538 4.874  1.00 12.18 ? 4   ALA B O   1 
ATOM   929  C  CB  . ALA B 2 5   ? -7.498  -12.209 5.394  1.00 9.81  ? 4   ALA B CB  1 
ATOM   930  N  N   . VAL B 2 6   ? -10.246 -12.778 6.670  1.00 9.47  ? 5   VAL B N   1 
ATOM   931  C  CA  . VAL B 2 6   ? -11.440 -12.362 7.393  1.00 10.07 ? 5   VAL B CA  1 
ATOM   932  C  C   . VAL B 2 6   ? -11.122 -12.334 8.874  1.00 11.29 ? 5   VAL B C   1 
ATOM   933  O  O   . VAL B 2 6   ? -10.253 -13.065 9.343  1.00 11.53 ? 5   VAL B O   1 
ATOM   934  C  CB  . VAL B 2 6   ? -12.647 -13.303 7.093  1.00 11.12 ? 5   VAL B CB  1 
ATOM   935  C  CG1 . VAL B 2 6   ? -12.394 -14.705 7.654  1.00 14.50 ? 5   VAL B CG1 1 
ATOM   936  C  CG2 . VAL B 2 6   ? -13.947 -12.721 7.631  1.00 13.23 ? 5   VAL B CG2 1 
ATOM   937  N  N   . CYS B 2 7   ? -11.816 -11.471 9.602  1.00 11.28 ? 6   CYS B N   1 
ATOM   938  C  CA  . CYS B 2 7   ? -11.582 -11.317 11.023 1.00 11.29 ? 6   CYS B CA  1 
ATOM   939  C  C   . CYS B 2 7   ? -12.899 -11.063 11.735 1.00 12.33 ? 6   CYS B C   1 
ATOM   940  O  O   . CYS B 2 7   ? -13.665 -10.180 11.344 1.00 13.21 ? 6   CYS B O   1 
ATOM   941  C  CB  . CYS B 2 7   ? -10.632 -10.150 11.273 1.00 12.71 ? 6   CYS B CB  1 
ATOM   942  S  SG  . CYS B 2 7   ? -10.268 -9.890  13.005 1.00 16.40 ? 6   CYS B SG  1 
ATOM   943  N  N   . VAL B 2 8   ? -13.157 -11.846 12.777 1.00 10.23 ? 7   VAL B N   1 
ATOM   944  C  CA  . VAL B 2 8   ? -14.335 -11.649 13.608 1.00 11.22 ? 7   VAL B CA  1 
ATOM   945  C  C   . VAL B 2 8   ? -13.899 -10.913 14.868 1.00 12.35 ? 7   VAL B C   1 
ATOM   946  O  O   . VAL B 2 8   ? -13.097 -11.425 15.654 1.00 13.44 ? 7   VAL B O   1 
ATOM   947  C  CB  . VAL B 2 8   ? -15.000 -12.984 13.991 1.00 13.78 ? 7   VAL B CB  1 
ATOM   948  C  CG1 . VAL B 2 8   ? -16.194 -12.742 14.927 1.00 15.23 ? 7   VAL B CG1 1 
ATOM   949  C  CG2 . VAL B 2 8   ? -15.428 -13.756 12.731 1.00 14.74 ? 7   VAL B CG2 1 
ATOM   950  N  N   . LEU B 2 9   ? -14.405 -9.697  15.039 1.00 12.87 ? 8   LEU B N   1 
ATOM   951  C  CA  . LEU B 2 9   ? -14.077 -8.886  16.205 1.00 13.24 ? 8   LEU B CA  1 
ATOM   952  C  C   . LEU B 2 9   ? -15.026 -9.196  17.349 1.00 14.32 ? 8   LEU B C   1 
ATOM   953  O  O   . LEU B 2 9   ? -16.247 -9.162  17.177 1.00 15.49 ? 8   LEU B O   1 
ATOM   954  C  CB  . LEU B 2 9   ? -14.163 -7.398  15.867 1.00 14.57 ? 8   LEU B CB  1 
ATOM   955  C  CG  . LEU B 2 9   ? -13.232 -6.903  14.759 1.00 18.10 ? 8   LEU B CG  1 
ATOM   956  C  CD1 . LEU B 2 9   ? -13.616 -5.493  14.314 1.00 21.18 ? 8   LEU B CD1 1 
ATOM   957  C  CD2 . LEU B 2 9   ? -11.803 -6.939  15.250 1.00 19.24 ? 8   LEU B CD2 1 
ATOM   958  N  N   . LYS B 2 10  ? -14.454 -9.497  18.511 1.00 14.46 ? 9   LYS B N   1 
ATOM   959  C  CA  . LYS B 2 10  ? -15.226 -9.709  19.732 1.00 16.51 ? 9   LYS B CA  1 
ATOM   960  C  C   . LYS B 2 10  ? -14.463 -9.146  20.931 1.00 17.03 ? 9   LYS B C   1 
ATOM   961  O  O   . LYS B 2 10  ? -13.239 -9.063  20.909 1.00 16.77 ? 9   LYS B O   1 
ATOM   962  C  CB  . LYS B 2 10  ? -15.493 -11.201 19.939 1.00 21.81 ? 9   LYS B CB  1 
ATOM   963  C  CG  . LYS B 2 10  ? -16.545 -11.777 19.010 1.00 31.11 ? 9   LYS B CG  1 
ATOM   964  C  CD  . LYS B 2 10  ? -16.678 -13.284 19.165 1.00 36.88 ? 9   LYS B CD  1 
ATOM   965  C  CE  . LYS B 2 10  ? -17.500 -13.866 18.020 1.00 40.48 ? 9   LYS B CE  1 
ATOM   966  N  NZ  . LYS B 2 10  ? -17.442 -15.351 17.966 1.00 44.62 ? 9   LYS B NZ  1 
ATOM   967  N  N   . GLY B 2 11  ? -15.189 -8.770  21.978 1.00 19.37 ? 10  GLY B N   1 
ATOM   968  C  CA  . GLY B 2 11  ? -14.574 -8.231  23.177 1.00 23.18 ? 10  GLY B CA  1 
ATOM   969  C  C   . GLY B 2 11  ? -15.346 -8.595  24.429 1.00 24.75 ? 10  GLY B C   1 
ATOM   970  O  O   . GLY B 2 11  ? -16.218 -9.463  24.397 1.00 26.17 ? 10  GLY B O   1 
ATOM   971  N  N   . ASP B 2 12  ? -15.023 -7.932  25.535 1.00 27.07 ? 11  ASP B N   1 
ATOM   972  C  CA  . ASP B 2 12  ? -15.705 -8.166  26.807 1.00 28.84 ? 11  ASP B CA  1 
ATOM   973  C  C   . ASP B 2 12  ? -17.024 -7.406  26.874 1.00 28.39 ? 11  ASP B C   1 
ATOM   974  O  O   . ASP B 2 12  ? -17.874 -7.663  27.741 1.00 31.43 ? 11  ASP B O   1 
ATOM   975  C  CB  . ASP B 2 12  ? -14.812 -7.731  27.969 1.00 33.96 ? 11  ASP B CB  1 
ATOM   976  C  CG  . ASP B 2 12  ? -13.576 -8.595  28.112 1.00 39.68 ? 11  ASP B CG  1 
ATOM   977  O  OD1 . ASP B 2 12  ? -13.562 -9.717  27.559 1.00 42.23 ? 11  ASP B OD1 1 
ATOM   978  O  OD2 . ASP B 2 12  ? -12.624 -8.154  28.793 1.00 41.72 ? 11  ASP B OD2 1 
ATOM   979  N  N   . GLY B 2 13  ? -17.181 -6.450  25.969 1.00 26.25 ? 12  GLY B N   1 
ATOM   980  C  CA  . GLY B 2 13  ? -18.387 -5.654  25.899 1.00 24.00 ? 12  GLY B CA  1 
ATOM   981  C  C   . GLY B 2 13  ? -19.181 -5.984  24.653 1.00 20.52 ? 12  GLY B C   1 
ATOM   982  O  O   . GLY B 2 13  ? -19.082 -7.091  24.123 1.00 21.85 ? 12  GLY B O   1 
ATOM   983  N  N   . PRO B 2 14  ? -19.952 -5.008  24.161 1.00 19.78 ? 13  PRO B N   1 
ATOM   984  C  CA  . PRO B 2 14  ? -20.902 -5.181  23.059 1.00 20.10 ? 13  PRO B CA  1 
ATOM   985  C  C   . PRO B 2 14  ? -20.294 -4.976  21.674 1.00 19.25 ? 13  PRO B C   1 
ATOM   986  O  O   . PRO B 2 14  ? -21.006 -5.117  20.675 1.00 20.42 ? 13  PRO B O   1 
ATOM   987  C  CB  . PRO B 2 14  ? -21.919 -4.073  23.328 1.00 20.88 ? 13  PRO B CB  1 
ATOM   988  C  CG  . PRO B 2 14  ? -21.089 -2.978  23.920 1.00 21.52 ? 13  PRO B CG  1 
ATOM   989  C  CD  . PRO B 2 14  ? -20.032 -3.660  24.752 1.00 20.97 ? 13  PRO B CD  1 
ATOM   990  N  N   . VAL B 2 15  ? -19.010 -4.644  21.597 1.00 18.57 ? 14  VAL B N   1 
ATOM   991  C  CA  . VAL B 2 15  ? -18.429 -4.330  20.296 1.00 17.15 ? 14  VAL B CA  1 
ATOM   992  C  C   . VAL B 2 15  ? -18.164 -5.611  19.523 1.00 18.06 ? 14  VAL B C   1 
ATOM   993  O  O   . VAL B 2 15  ? -17.497 -6.518  20.012 1.00 20.20 ? 14  VAL B O   1 
ATOM   994  C  CB  . VAL B 2 15  ? -17.138 -3.490  20.407 1.00 17.85 ? 14  VAL B CB  1 
ATOM   995  C  CG1 . VAL B 2 15  ? -16.584 -3.198  19.015 1.00 18.08 ? 14  VAL B CG1 1 
ATOM   996  C  CG2 . VAL B 2 15  ? -17.422 -2.183  21.156 1.00 17.50 ? 14  VAL B CG2 1 
ATOM   997  N  N   . GLN B 2 16  ? -18.706 -5.688  18.316 1.00 18.47 ? 15  GLN B N   1 
ATOM   998  C  CA  . GLN B 2 16  ? -18.560 -6.887  17.507 1.00 20.28 ? 15  GLN B CA  1 
ATOM   999  C  C   . GLN B 2 16  ? -18.620 -6.519  16.039 1.00 20.10 ? 15  GLN B C   1 
ATOM   1000 O  O   . GLN B 2 16  ? -19.219 -5.513  15.659 1.00 20.83 ? 15  GLN B O   1 
ATOM   1001 C  CB  . GLN B 2 16  ? -19.654 -7.899  17.844 1.00 25.70 ? 15  GLN B CB  1 
ATOM   1002 C  CG  . GLN B 2 16  ? -21.058 -7.363  17.676 1.00 27.83 ? 15  GLN B CG  1 
ATOM   1003 C  CD  . GLN B 2 16  ? -22.122 -8.362  18.099 1.00 31.61 ? 15  GLN B CD  1 
ATOM   1004 O  OE1 . GLN B 2 16  ? -21.987 -9.567  17.872 1.00 35.65 ? 15  GLN B OE1 1 
ATOM   1005 N  NE2 . GLN B 2 16  ? -23.189 -7.865  18.715 1.00 31.49 ? 15  GLN B NE2 1 
ATOM   1006 N  N   . GLY B 2 17  ? -17.991 -7.331  15.209 1.00 17.50 ? 16  GLY B N   1 
ATOM   1007 C  CA  . GLY B 2 17  ? -17.997 -7.049  13.790 1.00 17.49 ? 16  GLY B CA  1 
ATOM   1008 C  C   . GLY B 2 17  ? -17.281 -8.097  12.976 1.00 14.41 ? 16  GLY B C   1 
ATOM   1009 O  O   . GLY B 2 17  ? -16.628 -8.989  13.510 1.00 17.09 ? 16  GLY B O   1 
ATOM   1010 N  N   . ILE B 2 18  ? -17.429 -7.988  11.666 1.00 14.08 ? 17  ILE B N   1 
ATOM   1011 C  CA  . ILE B 2 18  ? -16.742 -8.868  10.740 1.00 12.65 ? 17  ILE B CA  1 
ATOM   1012 C  C   . ILE B 2 18  ? -16.053 -7.967  9.729  1.00 13.65 ? 17  ILE B C   1 
ATOM   1013 O  O   . ILE B 2 18  ? -16.686 -7.097  9.122  1.00 14.25 ? 17  ILE B O   1 
ATOM   1014 C  CB  . ILE B 2 18  ? -17.721 -9.818  10.028 1.00 14.32 ? 17  ILE B CB  1 
ATOM   1015 C  CG1 . ILE B 2 18  ? -18.357 -10.782 11.033 1.00 18.78 ? 17  ILE B CG1 1 
ATOM   1016 C  CG2 . ILE B 2 18  ? -17.014 -10.597 8.924  1.00 16.20 ? 17  ILE B CG2 1 
ATOM   1017 C  CD1 . ILE B 2 18  ? -19.528 -11.563 10.462 1.00 21.89 ? 17  ILE B CD1 1 
ATOM   1018 N  N   . ILE B 2 19  ? -14.749 -8.152  9.582  1.00 11.99 ? 18  ILE B N   1 
ATOM   1019 C  CA  . ILE B 2 19  ? -13.960 -7.373  8.641  1.00 11.93 ? 18  ILE B CA  1 
ATOM   1020 C  C   . ILE B 2 19  ? -13.326 -8.300  7.605  1.00 13.10 ? 18  ILE B C   1 
ATOM   1021 O  O   . ILE B 2 19  ? -12.720 -9.334  7.946  1.00 12.11 ? 18  ILE B O   1 
ATOM   1022 C  CB  . ILE B 2 19  ? -12.858 -6.558  9.358  1.00 12.49 ? 18  ILE B CB  1 
ATOM   1023 C  CG1 . ILE B 2 19  ? -13.472 -5.580  10.371 1.00 14.98 ? 18  ILE B CG1 1 
ATOM   1024 C  CG2 . ILE B 2 19  ? -11.975 -5.829  8.337  1.00 11.61 ? 18  ILE B CG2 1 
ATOM   1025 C  CD1 . ILE B 2 19  ? -14.303 -4.473  9.734  1.00 15.29 ? 18  ILE B CD1 1 
ATOM   1026 N  N   . ASN B 2 20  ? -13.492 -7.933  6.337  1.00 11.41 ? 19  ASN B N   1 
ATOM   1027 C  CA  . ASN B 2 20  ? -12.913 -8.673  5.221  1.00 11.87 ? 19  ASN B CA  1 
ATOM   1028 C  C   . ASN B 2 20  ? -11.696 -7.963  4.651  1.00 11.36 ? 19  ASN B C   1 
ATOM   1029 O  O   . ASN B 2 20  ? -11.628 -6.735  4.660  1.00 12.77 ? 19  ASN B O   1 
ATOM   1030 C  CB  . ASN B 2 20  ? -13.955 -8.825  4.113  1.00 14.54 ? 19  ASN B CB  1 
ATOM   1031 C  CG  . ASN B 2 20  ? -15.227 -9.447  4.607  1.00 18.02 ? 19  ASN B CG  1 
ATOM   1032 O  OD1 . ASN B 2 20  ? -15.283 -10.649 4.859  1.00 19.91 ? 19  ASN B OD1 1 
ATOM   1033 N  ND2 . ASN B 2 20  ? -16.263 -8.628  4.769  1.00 21.34 ? 19  ASN B ND2 1 
ATOM   1034 N  N   . PHE B 2 21  ? -10.742 -8.746  4.154  1.00 11.76 ? 20  PHE B N   1 
ATOM   1035 C  CA  . PHE B 2 21  ? -9.559  -8.226  3.483  1.00 11.73 ? 20  PHE B CA  1 
ATOM   1036 C  C   . PHE B 2 21  ? -9.432  -8.926  2.140  1.00 13.45 ? 20  PHE B C   1 
ATOM   1037 O  O   . PHE B 2 21  ? -9.596  -10.144 2.057  1.00 15.11 ? 20  PHE B O   1 
ATOM   1038 C  CB  . PHE B 2 21  ? -8.293  -8.547  4.279  1.00 12.61 ? 20  PHE B CB  1 
ATOM   1039 C  CG  . PHE B 2 21  ? -8.267  -7.983  5.672  1.00 12.55 ? 20  PHE B CG  1 
ATOM   1040 C  CD1 . PHE B 2 21  ? -7.544  -6.832  5.952  1.00 13.92 ? 20  PHE B CD1 1 
ATOM   1041 C  CD2 . PHE B 2 21  ? -8.932  -8.622  6.712  1.00 13.29 ? 20  PHE B CD2 1 
ATOM   1042 C  CE1 . PHE B 2 21  ? -7.493  -6.314  7.239  1.00 15.63 ? 20  PHE B CE1 1 
ATOM   1043 C  CE2 . PHE B 2 21  ? -8.890  -8.108  8.009  1.00 15.91 ? 20  PHE B CE2 1 
ATOM   1044 C  CZ  . PHE B 2 21  ? -8.172  -6.954  8.273  1.00 15.41 ? 20  PHE B CZ  1 
ATOM   1045 N  N   . GLU B 2 22  ? -9.130  -8.177  1.087  1.00 12.85 ? 21  GLU B N   1 
ATOM   1046 C  CA  . GLU B 2 22  ? -8.842  -8.809  -0.197 1.00 12.13 ? 21  GLU B CA  1 
ATOM   1047 C  C   . GLU B 2 22  ? -7.636  -8.179  -0.868 1.00 12.41 ? 21  GLU B C   1 
ATOM   1048 O  O   . GLU B 2 22  ? -7.502  -6.949  -0.925 1.00 13.64 ? 21  GLU B O   1 
ATOM   1049 C  CB  . GLU B 2 22  ? -10.054 -8.772  -1.131 1.00 15.95 ? 21  GLU B CB  1 
ATOM   1050 C  CG  . GLU B 2 22  ? -9.810  -9.513  -2.442 1.00 20.43 ? 21  GLU B CG  1 
ATOM   1051 C  CD  . GLU B 2 22  ? -11.082 -9.818  -3.210 1.00 30.09 ? 21  GLU B CD  1 
ATOM   1052 O  OE1 . GLU B 2 22  ? -12.133 -9.250  -2.874 1.00 34.51 ? 21  GLU B OE1 1 
ATOM   1053 O  OE2 . GLU B 2 22  ? -11.027 -10.628 -4.159 1.00 37.82 ? 21  GLU B OE2 1 
ATOM   1054 N  N   . GLN B 2 23  ? -6.756  -9.036  -1.372 1.00 11.07 ? 22  GLN B N   1 
ATOM   1055 C  CA  . GLN B 2 23  ? -5.575  -8.606  -2.102 1.00 11.56 ? 22  GLN B CA  1 
ATOM   1056 C  C   . GLN B 2 23  ? -5.434  -9.510  -3.314 1.00 14.04 ? 22  GLN B C   1 
ATOM   1057 O  O   . GLN B 2 23  ? -4.764  -10.540 -3.261 1.00 17.40 ? 22  GLN B O   1 
ATOM   1058 C  CB  . GLN B 2 23  ? -4.330  -8.698  -1.206 1.00 12.01 ? 22  GLN B CB  1 
ATOM   1059 C  CG  . GLN B 2 23  ? -3.075  -8.071  -1.811 1.00 12.03 ? 22  GLN B CG  1 
ATOM   1060 C  CD  . GLN B 2 23  ? -1.846  -8.271  -0.943 1.00 14.73 ? 22  GLN B CD  1 
ATOM   1061 O  OE1 . GLN B 2 23  ? -1.697  -9.301  -0.289 1.00 16.13 ? 22  GLN B OE1 1 
ATOM   1062 N  NE2 . GLN B 2 23  ? -0.966  -7.283  -0.927 1.00 15.87 ? 22  GLN B NE2 1 
ATOM   1063 N  N   . LYS B 2 24  ? -6.088  -9.139  -4.406 1.00 14.65 ? 23  LYS B N   1 
ATOM   1064 C  CA  . LYS B 2 24  ? -6.088  -9.996  -5.593 1.00 17.59 ? 23  LYS B CA  1 
ATOM   1065 C  C   . LYS B 2 24  ? -4.730  -10.076 -6.292 1.00 16.65 ? 23  LYS B C   1 
ATOM   1066 O  O   . LYS B 2 24  ? -4.441  -11.054 -6.990 1.00 20.61 ? 23  LYS B O   1 
ATOM   1067 C  CB  . LYS B 2 24  ? -7.168  -9.560  -6.579 1.00 22.45 ? 23  LYS B CB  1 
ATOM   1068 C  CG  . LYS B 2 24  ? -8.575  -9.945  -6.149 1.00 31.16 ? 23  LYS B CG  1 
ATOM   1069 C  CD  . LYS B 2 24  ? -9.577  -9.634  -7.244 1.00 38.61 ? 23  LYS B CD  1 
ATOM   1070 C  CE  . LYS B 2 24  ? -9.156  -10.250 -8.566 1.00 42.64 ? 23  LYS B CE  1 
ATOM   1071 N  NZ  . LYS B 2 24  ? -10.136 -9.968  -9.654 1.00 46.97 ? 23  LYS B NZ  1 
ATOM   1072 N  N   . GLU B 2 25  ? -3.910  -9.044  -6.122 1.00 14.73 ? 24  GLU B N   1 
ATOM   1073 C  CA  . GLU B 2 25  ? -2.588  -9.009  -6.731 1.00 14.77 ? 24  GLU B CA  1 
ATOM   1074 C  C   . GLU B 2 25  ? -1.502  -9.029  -5.667 1.00 15.29 ? 24  GLU B C   1 
ATOM   1075 O  O   . GLU B 2 25  ? -1.537  -8.237  -4.719 1.00 16.61 ? 24  GLU B O   1 
ATOM   1076 C  CB  . GLU B 2 25  ? -2.430  -7.758  -7.598 1.00 16.33 ? 24  GLU B CB  1 
ATOM   1077 C  CG  . GLU B 2 25  ? -3.379  -7.712  -8.780 1.00 17.59 ? 24  GLU B CG  1 
ATOM   1078 C  CD  . GLU B 2 25  ? -4.627  -6.892  -8.517 1.00 24.13 ? 24  GLU B CD  1 
ATOM   1079 O  OE1 . GLU B 2 25  ? -4.646  -6.102  -7.546 1.00 26.16 ? 24  GLU B OE1 1 
ATOM   1080 O  OE2 . GLU B 2 25  ? -5.593  -7.029  -9.298 1.00 28.10 ? 24  GLU B OE2 1 
ATOM   1081 N  N   . SER B 2 26  ? -0.536  -9.928  -5.822 1.00 15.98 ? 25  SER B N   1 
ATOM   1082 C  CA  . SER B 2 26  ? 0.571   -9.987  -4.878 1.00 16.48 ? 25  SER B CA  1 
ATOM   1083 C  C   . SER B 2 26  ? 1.215   -8.612  -4.782 1.00 18.32 ? 25  SER B C   1 
ATOM   1084 O  O   . SER B 2 26  ? 1.447   -7.957  -5.800 1.00 16.64 ? 25  SER B O   1 
ATOM   1085 C  CB  . SER B 2 26  ? 1.604   -11.030 -5.314 1.00 21.09 ? 25  SER B CB  1 
ATOM   1086 O  OG  . SER B 2 26  ? 1.054   -12.337 -5.240 1.00 26.53 ? 25  SER B OG  1 
ATOM   1087 N  N   . ASN B 2 27  ? 1.482   -8.177  -3.553 1.00 17.23 ? 26  ASN B N   1 
ATOM   1088 C  CA  . ASN B 2 27  ? 2.101   -6.879  -3.292 1.00 17.81 ? 26  ASN B CA  1 
ATOM   1089 C  C   . ASN B 2 27  ? 1.260   -5.674  -3.700 1.00 18.52 ? 26  ASN B C   1 
ATOM   1090 O  O   . ASN B 2 27  ? 1.750   -4.546  -3.690 1.00 20.42 ? 26  ASN B O   1 
ATOM   1091 C  CB  . ASN B 2 27  ? 3.477   -6.805  -3.952 1.00 18.26 ? 26  ASN B CB  1 
ATOM   1092 C  CG  . ASN B 2 27  ? 4.354   -7.970  -3.565 1.00 19.10 ? 26  ASN B CG  1 
ATOM   1093 O  OD1 . ASN B 2 27  ? 4.467   -8.311  -2.384 1.00 22.68 ? 26  ASN B OD1 1 
ATOM   1094 N  ND2 . ASN B 2 27  ? 4.941   -8.620  -4.556 1.00 18.76 ? 26  ASN B ND2 1 
ATOM   1095 N  N   . GLY B 2 28  ? -0.000  -5.909  -4.054 1.00 16.62 ? 27  GLY B N   1 
ATOM   1096 C  CA  . GLY B 2 28  ? -0.898  -4.830  -4.427 1.00 17.00 ? 27  GLY B CA  1 
ATOM   1097 C  C   . GLY B 2 28  ? -1.682  -4.295  -3.240 1.00 17.20 ? 27  GLY B C   1 
ATOM   1098 O  O   . GLY B 2 28  ? -1.518  -4.762  -2.111 1.00 17.38 ? 27  GLY B O   1 
ATOM   1099 N  N   . PRO B 2 29  ? -2.538  -3.297  -3.483 1.00 18.12 ? 28  PRO B N   1 
ATOM   1100 C  CA  . PRO B 2 29  ? -3.352  -2.724  -2.409 1.00 18.25 ? 28  PRO B CA  1 
ATOM   1101 C  C   . PRO B 2 29  ? -4.271  -3.765  -1.792 1.00 16.69 ? 28  PRO B C   1 
ATOM   1102 O  O   . PRO B 2 29  ? -4.734  -4.679  -2.483 1.00 18.53 ? 28  PRO B O   1 
ATOM   1103 C  CB  . PRO B 2 29  ? -4.186  -1.665  -3.133 1.00 21.42 ? 28  PRO B CB  1 
ATOM   1104 C  CG  . PRO B 2 29  ? -3.383  -1.304  -4.321 1.00 23.95 ? 28  PRO B CG  1 
ATOM   1105 C  CD  . PRO B 2 29  ? -2.710  -2.572  -4.753 1.00 22.84 ? 28  PRO B CD  1 
ATOM   1106 N  N   . VAL B 2 30  ? -4.523  -3.626  -0.497 1.00 15.17 ? 29  VAL B N   1 
ATOM   1107 C  CA  . VAL B 2 30  ? -5.460  -4.490  0.196  1.00 14.79 ? 29  VAL B CA  1 
ATOM   1108 C  C   . VAL B 2 30  ? -6.747  -3.722  0.450  1.00 14.01 ? 29  VAL B C   1 
ATOM   1109 O  O   . VAL B 2 30  ? -6.721  -2.632  1.025  1.00 17.08 ? 29  VAL B O   1 
ATOM   1110 C  CB  . VAL B 2 30  ? -4.894  -4.959  1.551  1.00 12.83 ? 29  VAL B CB  1 
ATOM   1111 C  CG1 . VAL B 2 30  ? -5.906  -5.844  2.271  1.00 14.25 ? 29  VAL B CG1 1 
ATOM   1112 C  CG2 . VAL B 2 30  ? -3.570  -5.695  1.356  1.00 14.80 ? 29  VAL B CG2 1 
ATOM   1113 N  N   . LYS B 2 31  ? -7.870  -4.279  0.011  1.00 11.41 ? 30  LYS B N   1 
ATOM   1114 C  CA  . LYS B 2 31  ? -9.170  -3.698  0.321  1.00 13.08 ? 30  LYS B CA  1 
ATOM   1115 C  C   . LYS B 2 31  ? -9.631  -4.248  1.659  1.00 13.77 ? 30  LYS B C   1 
ATOM   1116 O  O   . LYS B 2 31  ? -9.538  -5.451  1.900  1.00 15.00 ? 30  LYS B O   1 
ATOM   1117 C  CB  . LYS B 2 31  ? -10.203 -4.063  -0.745 1.00 18.60 ? 30  LYS B CB  1 
ATOM   1118 C  CG  . LYS B 2 31  ? -9.922  -3.504  -2.127 1.00 23.63 ? 30  LYS B CG  1 
ATOM   1119 C  CD  . LYS B 2 31  ? -11.010 -3.930  -3.107 1.00 31.79 ? 30  LYS B CD  1 
ATOM   1120 C  CE  . LYS B 2 31  ? -10.639 -3.562  -4.533 1.00 35.17 ? 30  LYS B CE  1 
ATOM   1121 N  NZ  . LYS B 2 31  ? -11.654 -4.014  -5.547 1.00 35.26 ? 30  LYS B NZ  1 
ATOM   1122 N  N   . VAL B 2 32  ? -10.127 -3.366  2.520  1.00 13.08 ? 31  VAL B N   1 
ATOM   1123 C  CA  . VAL B 2 32  ? -10.610 -3.747  3.842  1.00 12.63 ? 31  VAL B CA  1 
ATOM   1124 C  C   . VAL B 2 32  ? -12.035 -3.238  3.996  1.00 14.72 ? 31  VAL B C   1 
ATOM   1125 O  O   . VAL B 2 32  ? -12.290 -2.041  3.834  1.00 16.90 ? 31  VAL B O   1 
ATOM   1126 C  CB  . VAL B 2 32  ? -9.730  -3.109  4.936  1.00 13.26 ? 31  VAL B CB  1 
ATOM   1127 C  CG1 . VAL B 2 32  ? -10.138 -3.591  6.323  1.00 14.51 ? 31  VAL B CG1 1 
ATOM   1128 C  CG2 . VAL B 2 32  ? -8.253  -3.396  4.662  1.00 14.14 ? 31  VAL B CG2 1 
ATOM   1129 N  N   . TRP B 2 33  ? -12.973 -4.131  4.302  1.00 11.91 ? 32  TRP B N   1 
ATOM   1130 C  CA  . TRP B 2 33  ? -14.363 -3.703  4.425  1.00 13.10 ? 32  TRP B CA  1 
ATOM   1131 C  C   . TRP B 2 33  ? -15.199 -4.568  5.348  1.00 13.78 ? 32  TRP B C   1 
ATOM   1132 O  O   . TRP B 2 33  ? -14.876 -5.726  5.604  1.00 15.28 ? 32  TRP B O   1 
ATOM   1133 C  CB  . TRP B 2 33  ? -15.036 -3.623  3.052  1.00 15.88 ? 32  TRP B CB  1 
ATOM   1134 C  CG  . TRP B 2 33  ? -15.431 -4.947  2.469  1.00 15.97 ? 32  TRP B CG  1 
ATOM   1135 C  CD1 . TRP B 2 33  ? -16.664 -5.537  2.532  1.00 18.78 ? 32  TRP B CD1 1 
ATOM   1136 C  CD2 . TRP B 2 33  ? -14.597 -5.843  1.720  1.00 16.55 ? 32  TRP B CD2 1 
ATOM   1137 N  NE1 . TRP B 2 33  ? -16.650 -6.735  1.861  1.00 19.10 ? 32  TRP B NE1 1 
ATOM   1138 C  CE2 . TRP B 2 33  ? -15.392 -6.951  1.360  1.00 18.90 ? 32  TRP B CE2 1 
ATOM   1139 C  CE3 . TRP B 2 33  ? -13.258 -5.816  1.321  1.00 16.98 ? 32  TRP B CE3 1 
ATOM   1140 C  CZ2 . TRP B 2 33  ? -14.891 -8.027  0.620  1.00 17.42 ? 32  TRP B CZ2 1 
ATOM   1141 C  CZ3 . TRP B 2 33  ? -12.757 -6.892  0.585  1.00 17.77 ? 32  TRP B CZ3 1 
ATOM   1142 C  CH2 . TRP B 2 33  ? -13.575 -7.977  0.239  1.00 16.49 ? 32  TRP B CH2 1 
ATOM   1143 N  N   . GLY B 2 34  ? -16.291 -3.995  5.835  1.00 13.23 ? 33  GLY B N   1 
ATOM   1144 C  CA  . GLY B 2 34  ? -17.172 -4.710  6.732  1.00 15.73 ? 33  GLY B CA  1 
ATOM   1145 C  C   . GLY B 2 34  ? -17.879 -3.747  7.654  1.00 16.24 ? 33  GLY B C   1 
ATOM   1146 O  O   . GLY B 2 34  ? -18.019 -2.562  7.344  1.00 18.32 ? 33  GLY B O   1 
ATOM   1147 N  N   . SER B 2 35  ? -18.329 -4.253  8.793  1.00 17.35 ? 34  SER B N   1 
ATOM   1148 C  CA  . SER B 2 35  ? -19.106 -3.438  9.712  1.00 19.13 ? 34  SER B CA  1 
ATOM   1149 C  C   . SER B 2 35  ? -18.749 -3.794  11.144 1.00 18.74 ? 34  SER B C   1 
ATOM   1150 O  O   . SER B 2 35  ? -18.422 -4.945  11.445 1.00 18.16 ? 34  SER B O   1 
ATOM   1151 C  CB  . SER B 2 35  ? -20.604 -3.647  9.461  1.00 23.93 ? 34  SER B CB  1 
ATOM   1152 O  OG  . SER B 2 35  ? -21.377 -2.702  10.171 1.00 32.48 ? 34  SER B OG  1 
ATOM   1153 N  N   . ILE B 2 36  ? -18.791 -2.795  12.016 1.00 17.39 ? 35  ILE B N   1 
ATOM   1154 C  CA  . ILE B 2 36  ? -18.590 -2.999  13.442 1.00 17.33 ? 35  ILE B CA  1 
ATOM   1155 C  C   . ILE B 2 36  ? -19.729 -2.307  14.167 1.00 18.80 ? 35  ILE B C   1 
ATOM   1156 O  O   . ILE B 2 36  ? -20.076 -1.170  13.843 1.00 22.52 ? 35  ILE B O   1 
ATOM   1157 C  CB  . ILE B 2 36  ? -17.260 -2.386  13.913 1.00 18.38 ? 35  ILE B CB  1 
ATOM   1158 C  CG1 . ILE B 2 36  ? -16.099 -2.896  13.052 1.00 20.53 ? 35  ILE B CG1 1 
ATOM   1159 C  CG2 . ILE B 2 36  ? -17.026 -2.686  15.393 1.00 20.72 ? 35  ILE B CG2 1 
ATOM   1160 C  CD1 . ILE B 2 36  ? -14.792 -2.167  13.295 1.00 21.21 ? 35  ILE B CD1 1 
ATOM   1161 N  N   . LYS B 2 37  ? -20.331 -2.990  15.134 1.00 16.79 ? 36  LYS B N   1 
ATOM   1162 C  CA  . LYS B 2 37  ? -21.404 -2.383  15.916 1.00 17.70 ? 36  LYS B CA  1 
ATOM   1163 C  C   . LYS B 2 37  ? -21.102 -2.419  17.416 1.00 17.52 ? 36  LYS B C   1 
ATOM   1164 O  O   . LYS B 2 37  ? -20.127 -3.031  17.842 1.00 18.97 ? 36  LYS B O   1 
ATOM   1165 C  CB  . LYS B 2 37  ? -22.762 -3.022  15.592 1.00 20.66 ? 36  LYS B CB  1 
ATOM   1166 C  CG  . LYS B 2 37  ? -22.903 -4.486  15.972 1.00 20.31 ? 36  LYS B CG  1 
ATOM   1167 C  CD  . LYS B 2 37  ? -24.210 -5.065  15.433 1.00 23.85 ? 36  LYS B CD  1 
ATOM   1168 C  CE  . LYS B 2 37  ? -24.370 -6.531  15.810 1.00 27.31 ? 36  LYS B CE  1 
ATOM   1169 N  NZ  . LYS B 2 37  ? -25.480 -7.190  15.056 1.00 30.61 ? 36  LYS B NZ  1 
ATOM   1170 N  N   . GLY B 2 38  ? -21.932 -1.744  18.207 1.00 16.75 ? 37  GLY B N   1 
ATOM   1171 C  CA  . GLY B 2 38  ? -21.735 -1.671  19.648 1.00 17.65 ? 37  GLY B CA  1 
ATOM   1172 C  C   . GLY B 2 38  ? -20.796 -0.564  20.100 1.00 18.88 ? 37  GLY B C   1 
ATOM   1173 O  O   . GLY B 2 38  ? -20.373 -0.534  21.260 1.00 20.70 ? 37  GLY B O   1 
ATOM   1174 N  N   . LEU B 2 39  ? -20.478 0.350   19.187 1.00 18.50 ? 38  LEU B N   1 
ATOM   1175 C  CA  . LEU B 2 39  ? -19.531 1.435   19.455 1.00 17.40 ? 38  LEU B CA  1 
ATOM   1176 C  C   . LEU B 2 39  ? -20.230 2.700   19.937 1.00 20.57 ? 38  LEU B C   1 
ATOM   1177 O  O   . LEU B 2 39  ? -21.413 2.909   19.666 1.00 23.08 ? 38  LEU B O   1 
ATOM   1178 C  CB  . LEU B 2 39  ? -18.747 1.768   18.180 1.00 16.64 ? 38  LEU B CB  1 
ATOM   1179 C  CG  . LEU B 2 39  ? -17.783 0.708   17.663 1.00 17.17 ? 38  LEU B CG  1 
ATOM   1180 C  CD1 . LEU B 2 39  ? -17.424 0.982   16.209 1.00 19.49 ? 38  LEU B CD1 1 
ATOM   1181 C  CD2 . LEU B 2 39  ? -16.525 0.646   18.527 1.00 17.81 ? 38  LEU B CD2 1 
ATOM   1182 N  N   . THR B 2 40  ? -19.498 3.542   20.663 1.00 20.17 ? 39  THR B N   1 
ATOM   1183 C  CA  . THR B 2 40  ? -19.965 4.891   20.936 1.00 22.97 ? 39  THR B CA  1 
ATOM   1184 C  C   . THR B 2 40  ? -19.838 5.705   19.648 1.00 21.96 ? 39  THR B C   1 
ATOM   1185 O  O   . THR B 2 40  ? -18.921 5.475   18.848 1.00 22.69 ? 39  THR B O   1 
ATOM   1186 C  CB  . THR B 2 40  ? -19.140 5.567   22.049 1.00 25.21 ? 39  THR B CB  1 
ATOM   1187 O  OG1 . THR B 2 40  ? -17.756 5.568   21.681 1.00 26.10 ? 39  THR B OG1 1 
ATOM   1188 C  CG2 . THR B 2 40  ? -19.302 4.823   23.367 1.00 23.88 ? 39  THR B CG2 1 
ATOM   1189 N  N   . GLU B 2 41  ? -20.762 6.638   19.438 1.00 24.16 ? 40  GLU B N   1 
ATOM   1190 C  CA  . GLU B 2 41  ? -20.730 7.488   18.252 1.00 24.95 ? 40  GLU B CA  1 
ATOM   1191 C  C   . GLU B 2 41  ? -19.396 8.231   18.152 1.00 26.40 ? 40  GLU B C   1 
ATOM   1192 O  O   . GLU B 2 41  ? -18.897 8.761   19.146 1.00 29.54 ? 40  GLU B O   1 
ATOM   1193 C  CB  . GLU B 2 41  ? -21.884 8.494   18.288 1.00 28.73 ? 40  GLU B CB  1 
ATOM   1194 C  CG  . GLU B 2 41  ? -21.885 9.480   17.135 1.00 32.59 ? 40  GLU B CG  1 
ATOM   1195 C  CD  . GLU B 2 41  ? -23.065 10.437  17.186 1.00 38.86 ? 40  GLU B CD  1 
ATOM   1196 O  OE1 . GLU B 2 41  ? -23.835 10.389  18.169 1.00 41.94 ? 40  GLU B OE1 1 
ATOM   1197 O  OE2 . GLU B 2 41  ? -23.222 11.240  16.241 1.00 40.31 ? 40  GLU B OE2 1 
ATOM   1198 N  N   . GLY B 2 42  ? -18.821 8.270   16.953 1.00 25.10 ? 41  GLY B N   1 
ATOM   1199 C  CA  . GLY B 2 42  ? -17.572 8.979   16.740 1.00 25.56 ? 41  GLY B CA  1 
ATOM   1200 C  C   . GLY B 2 42  ? -16.431 8.114   16.233 1.00 24.31 ? 41  GLY B C   1 
ATOM   1201 O  O   . GLY B 2 42  ? -16.649 6.996   15.764 1.00 22.47 ? 41  GLY B O   1 
ATOM   1202 N  N   . LEU B 2 43  ? -15.210 8.632   16.350 1.00 23.66 ? 42  LEU B N   1 
ATOM   1203 C  CA  . LEU B 2 43  ? -14.031 7.987   15.780 1.00 23.43 ? 42  LEU B CA  1 
ATOM   1204 C  C   . LEU B 2 43  ? -13.388 6.969   16.713 1.00 22.51 ? 42  LEU B C   1 
ATOM   1205 O  O   . LEU B 2 43  ? -13.295 7.194   17.924 1.00 23.28 ? 42  LEU B O   1 
ATOM   1206 C  CB  . LEU B 2 43  ? -12.990 9.040   15.405 1.00 27.26 ? 42  LEU B CB  1 
ATOM   1207 C  CG  . LEU B 2 43  ? -13.350 10.001  14.276 1.00 32.12 ? 42  LEU B CG  1 
ATOM   1208 C  CD1 . LEU B 2 43  ? -12.255 11.036  14.124 1.00 33.84 ? 42  LEU B CD1 1 
ATOM   1209 C  CD2 . LEU B 2 43  ? -13.549 9.234   12.985 1.00 34.12 ? 42  LEU B CD2 1 
ATOM   1210 N  N   . HIS B 2 44  ? -12.925 5.864   16.130 1.00 19.45 ? 43  HIS B N   1 
ATOM   1211 C  CA  . HIS B 2 44  ? -12.265 4.798   16.878 1.00 17.30 ? 43  HIS B CA  1 
ATOM   1212 C  C   . HIS B 2 44  ? -11.034 4.287   16.139 1.00 18.60 ? 43  HIS B C   1 
ATOM   1213 O  O   . HIS B 2 44  ? -11.115 3.930   14.961 1.00 18.58 ? 43  HIS B O   1 
ATOM   1214 C  CB  . HIS B 2 44  ? -13.231 3.637   17.110 1.00 17.99 ? 43  HIS B CB  1 
ATOM   1215 C  CG  . HIS B 2 44  ? -14.388 3.990   17.987 1.00 18.49 ? 43  HIS B CG  1 
ATOM   1216 N  ND1 . HIS B 2 44  ? -14.349 3.848   19.358 1.00 21.62 ? 43  HIS B ND1 1 
ATOM   1217 C  CD2 . HIS B 2 44  ? -15.606 4.506   17.696 1.00 19.25 ? 43  HIS B CD2 1 
ATOM   1218 C  CE1 . HIS B 2 44  ? -15.496 4.254   19.873 1.00 21.07 ? 43  HIS B CE1 1 
ATOM   1219 N  NE2 . HIS B 2 44  ? -16.276 4.657   18.885 1.00 20.53 ? 43  HIS B NE2 1 
ATOM   1220 N  N   . GLY B 2 45  ? -9.899  4.245   16.831 1.00 18.37 ? 44  GLY B N   1 
ATOM   1221 C  CA  . GLY B 2 45  ? -8.677  3.728   16.239 1.00 16.65 ? 44  GLY B CA  1 
ATOM   1222 C  C   . GLY B 2 45  ? -8.843  2.295   15.752 1.00 16.76 ? 44  GLY B C   1 
ATOM   1223 O  O   . GLY B 2 45  ? -9.494  1.478   16.397 1.00 18.21 ? 44  GLY B O   1 
ATOM   1224 N  N   . PHE B 2 46  ? -8.232  1.990   14.613 1.00 15.74 ? 45  PHE B N   1 
ATOM   1225 C  CA  . PHE B 2 46  ? -8.431  0.718   13.933 1.00 15.03 ? 45  PHE B CA  1 
ATOM   1226 C  C   . PHE B 2 46  ? -7.044  0.224   13.528 1.00 15.68 ? 45  PHE B C   1 
ATOM   1227 O  O   . PHE B 2 46  ? -6.433  0.771   12.611 1.00 16.70 ? 45  PHE B O   1 
ATOM   1228 C  CB  . PHE B 2 46  ? -9.335  0.973   12.718 1.00 15.50 ? 45  PHE B CB  1 
ATOM   1229 C  CG  . PHE B 2 46  ? -9.891  -0.260  12.070 1.00 16.10 ? 45  PHE B CG  1 
ATOM   1230 C  CD1 . PHE B 2 46  ? -10.487 -1.263  12.818 1.00 18.08 ? 45  PHE B CD1 1 
ATOM   1231 C  CD2 . PHE B 2 46  ? -9.878  -0.378  10.687 1.00 16.82 ? 45  PHE B CD2 1 
ATOM   1232 C  CE1 . PHE B 2 46  ? -11.021 -2.382  12.197 1.00 18.49 ? 45  PHE B CE1 1 
ATOM   1233 C  CE2 . PHE B 2 46  ? -10.410 -1.489  10.061 1.00 17.16 ? 45  PHE B CE2 1 
ATOM   1234 C  CZ  . PHE B 2 46  ? -10.983 -2.493  10.815 1.00 17.28 ? 45  PHE B CZ  1 
ATOM   1235 N  N   . HIS B 2 47  ? -6.538  -0.791  14.232 1.00 13.19 ? 46  HIS B N   1 
ATOM   1236 C  CA  . HIS B 2 47  ? -5.130  -1.171  14.128 1.00 14.20 ? 46  HIS B CA  1 
ATOM   1237 C  C   . HIS B 2 47  ? -4.927  -2.664  14.002 1.00 13.72 ? 46  HIS B C   1 
ATOM   1238 O  O   . HIS B 2 47  ? -5.643  -3.451  14.623 1.00 16.13 ? 46  HIS B O   1 
ATOM   1239 C  CB  . HIS B 2 47  ? -4.367  -0.778  15.395 1.00 17.58 ? 46  HIS B CB  1 
ATOM   1240 C  CG  . HIS B 2 47  ? -4.377  0.686   15.697 1.00 20.05 ? 46  HIS B CG  1 
ATOM   1241 N  ND1 . HIS B 2 47  ? -4.091  1.182   16.949 1.00 23.49 ? 46  HIS B ND1 1 
ATOM   1242 C  CD2 . HIS B 2 47  ? -4.620  1.761   14.913 1.00 21.47 ? 46  HIS B CD2 1 
ATOM   1243 C  CE1 . HIS B 2 47  ? -4.164  2.500   16.927 1.00 24.08 ? 46  HIS B CE1 1 
ATOM   1244 N  NE2 . HIS B 2 47  ? -4.482  2.877   15.702 1.00 22.91 ? 46  HIS B NE2 1 
ATOM   1245 N  N   . VAL B 2 48  ? -3.910  -3.050  13.236 1.00 11.73 ? 47  VAL B N   1 
ATOM   1246 C  CA  . VAL B 2 48  ? -3.383  -4.404  13.331 1.00 11.20 ? 47  VAL B CA  1 
ATOM   1247 C  C   . VAL B 2 48  ? -2.309  -4.433  14.412 1.00 12.16 ? 47  VAL B C   1 
ATOM   1248 O  O   . VAL B 2 48  ? -1.381  -3.607  14.403 1.00 12.26 ? 47  VAL B O   1 
ATOM   1249 C  CB  . VAL B 2 48  ? -2.789  -4.885  11.999 1.00 11.09 ? 47  VAL B CB  1 
ATOM   1250 C  CG1 . VAL B 2 48  ? -2.272  -6.307  12.143 1.00 12.20 ? 47  VAL B CG1 1 
ATOM   1251 C  CG2 . VAL B 2 48  ? -3.842  -4.803  10.900 1.00 14.36 ? 47  VAL B CG2 1 
ATOM   1252 N  N   . HIS B 2 49  ? -2.447  -5.370  15.346 1.00 11.30 ? 48  HIS B N   1 
ATOM   1253 C  CA  . HIS B 2 49  ? -1.447  -5.584  16.385 1.00 10.82 ? 48  HIS B CA  1 
ATOM   1254 C  C   . HIS B 2 49  ? -0.644  -6.842  16.094 1.00 11.37 ? 48  HIS B C   1 
ATOM   1255 O  O   . HIS B 2 49  ? -1.082  -7.715  15.335 1.00 14.36 ? 48  HIS B O   1 
ATOM   1256 C  CB  . HIS B 2 49  ? -2.096  -5.641  17.772 1.00 11.64 ? 48  HIS B CB  1 
ATOM   1257 C  CG  . HIS B 2 49  ? -2.508  -4.297  18.282 1.00 13.49 ? 48  HIS B CG  1 
ATOM   1258 N  ND1 . HIS B 2 49  ? -1.987  -3.740  19.431 1.00 15.70 ? 48  HIS B ND1 1 
ATOM   1259 C  CD2 . HIS B 2 49  ? -3.358  -3.377  17.771 1.00 15.62 ? 48  HIS B CD2 1 
ATOM   1260 C  CE1 . HIS B 2 49  ? -2.514  -2.543  19.616 1.00 18.89 ? 48  HIS B CE1 1 
ATOM   1261 N  NE2 . HIS B 2 49  ? -3.350  -2.301  18.621 1.00 18.43 ? 48  HIS B NE2 1 
ATOM   1262 N  N   . GLU B 2 50  ? 0.527   -6.925  16.708 1.00 11.51 ? 49  GLU B N   1 
ATOM   1263 C  CA  . GLU B 2 50  ? 1.562   -7.861  16.290 1.00 11.08 ? 49  GLU B CA  1 
ATOM   1264 C  C   . GLU B 2 50  ? 1.194   -9.330  16.411 1.00 11.40 ? 49  GLU B C   1 
ATOM   1265 O  O   . GLU B 2 50  ? 1.525   -10.126 15.532 1.00 12.60 ? 49  GLU B O   1 
ATOM   1266 C  CB  . GLU B 2 50  ? 2.859   -7.589  17.056 1.00 12.74 ? 49  GLU B CB  1 
ATOM   1267 C  CG  . GLU B 2 50  ? 4.039   -8.408  16.565 1.00 14.45 ? 49  GLU B CG  1 
ATOM   1268 C  CD  . GLU B 2 50  ? 5.334   -8.031  17.264 1.00 16.69 ? 49  GLU B CD  1 
ATOM   1269 O  OE1 . GLU B 2 50  ? 5.281   -7.241  18.234 1.00 18.00 ? 49  GLU B OE1 1 
ATOM   1270 O  OE2 . GLU B 2 50  ? 6.404   -8.534  16.856 1.00 17.83 ? 49  GLU B OE2 1 
ATOM   1271 N  N   . PHE B 2 51  ? 0.521   -9.703  17.493 1.00 10.77 ? 50  PHE B N   1 
ATOM   1272 C  CA  . PHE B 2 51  ? 0.304   -11.123 17.751 1.00 11.01 ? 50  PHE B CA  1 
ATOM   1273 C  C   . PHE B 2 51  ? -1.147  -11.547 17.633 1.00 11.06 ? 50  PHE B C   1 
ATOM   1274 O  O   . PHE B 2 51  ? -2.055  -10.849 18.096 1.00 14.67 ? 50  PHE B O   1 
ATOM   1275 C  CB  . PHE B 2 51  ? 0.869   -11.511 19.121 1.00 13.35 ? 50  PHE B CB  1 
ATOM   1276 C  CG  . PHE B 2 51  ? 2.331   -11.209 19.263 1.00 15.66 ? 50  PHE B CG  1 
ATOM   1277 C  CD1 . PHE B 2 51  ? 3.254   -11.821 18.432 1.00 16.61 ? 50  PHE B CD1 1 
ATOM   1278 C  CD2 . PHE B 2 51  ? 2.780   -10.296 20.204 1.00 19.73 ? 50  PHE B CD2 1 
ATOM   1279 C  CE1 . PHE B 2 51  ? 4.608   -11.537 18.545 1.00 18.92 ? 50  PHE B CE1 1 
ATOM   1280 C  CE2 . PHE B 2 51  ? 4.127   -10.006 20.323 1.00 20.85 ? 50  PHE B CE2 1 
ATOM   1281 C  CZ  . PHE B 2 51  ? 5.043   -10.625 19.490 1.00 20.18 ? 50  PHE B CZ  1 
ATOM   1282 N  N   . GLY B 2 52  ? -1.357  -12.707 17.020 1.00 10.93 ? 51  GLY B N   1 
ATOM   1283 C  CA  . GLY B 2 52  ? -2.683  -13.294 16.930 1.00 11.90 ? 51  GLY B CA  1 
ATOM   1284 C  C   . GLY B 2 52  ? -2.908  -14.155 18.157 1.00 14.71 ? 51  GLY B C   1 
ATOM   1285 O  O   . GLY B 2 52  ? -3.214  -15.343 18.055 1.00 16.19 ? 51  GLY B O   1 
ATOM   1286 N  N   . ASP B 2 53  ? -2.737  -13.538 19.323 1.00 16.08 ? 52  ASP B N   1 
ATOM   1287 C  CA  . ASP B 2 53  ? -2.774  -14.228 20.606 1.00 14.63 ? 52  ASP B CA  1 
ATOM   1288 C  C   . ASP B 2 53  ? -3.946  -13.679 21.404 1.00 15.58 ? 52  ASP B C   1 
ATOM   1289 O  O   . ASP B 2 53  ? -3.911  -12.534 21.872 1.00 17.83 ? 52  ASP B O   1 
ATOM   1290 C  CB  . ASP B 2 53  ? -1.453  -13.988 21.353 1.00 15.15 ? 52  ASP B CB  1 
ATOM   1291 C  CG  . ASP B 2 53  ? -1.375  -14.723 22.685 1.00 17.22 ? 52  ASP B CG  1 
ATOM   1292 O  OD1 . ASP B 2 53  ? -2.432  -15.049 23.259 1.00 17.89 ? 52  ASP B OD1 1 
ATOM   1293 O  OD2 . ASP B 2 53  ? -0.246  -14.954 23.173 1.00 21.30 ? 52  ASP B OD2 1 
ATOM   1294 N  N   . ASN B 2 54  ? -4.990  -14.490 21.537 1.00 15.77 ? 53  ASN B N   1 
ATOM   1295 C  CA  . ASN B 2 54  ? -6.201  -14.090 22.246 1.00 17.48 ? 53  ASN B CA  1 
ATOM   1296 C  C   . ASN B 2 54  ? -6.314  -14.789 23.598 1.00 16.91 ? 53  ASN B C   1 
ATOM   1297 O  O   . ASN B 2 54  ? -7.399  -14.855 24.183 1.00 18.78 ? 53  ASN B O   1 
ATOM   1298 C  CB  . ASN B 2 54  ? -7.440  -14.401 21.391 1.00 21.62 ? 53  ASN B CB  1 
ATOM   1299 C  CG  . ASN B 2 54  ? -8.706  -13.747 21.925 1.00 30.01 ? 53  ASN B CG  1 
ATOM   1300 O  OD1 . ASN B 2 54  ? -8.728  -12.549 22.215 1.00 32.81 ? 53  ASN B OD1 1 
ATOM   1301 N  ND2 . ASN B 2 54  ? -9.769  -14.534 22.054 1.00 31.75 ? 53  ASN B ND2 1 
ATOM   1302 N  N   . THR B 2 55  ? -5.198  -15.314 24.094 1.00 16.11 ? 54  THR B N   1 
ATOM   1303 C  CA  . THR B 2 55  ? -5.218  -16.069 25.349 1.00 17.48 ? 54  THR B CA  1 
ATOM   1304 C  C   . THR B 2 55  ? -5.693  -15.217 26.521 1.00 19.13 ? 54  THR B C   1 
ATOM   1305 O  O   . THR B 2 55  ? -6.274  -15.737 27.471 1.00 22.73 ? 54  THR B O   1 
ATOM   1306 C  CB  . THR B 2 55  ? -3.847  -16.703 25.683 1.00 18.90 ? 54  THR B CB  1 
ATOM   1307 O  OG1 . THR B 2 55  ? -2.846  -15.682 25.797 1.00 19.96 ? 54  THR B OG1 1 
ATOM   1308 C  CG2 . THR B 2 55  ? -3.444  -17.701 24.603 1.00 20.53 ? 54  THR B CG2 1 
ATOM   1309 N  N   . ALA B 2 56  ? -5.441  -13.912 26.450 1.00 19.17 ? 55  ALA B N   1 
ATOM   1310 C  CA  . ALA B 2 56  ? -5.928  -12.984 27.469 1.00 21.32 ? 55  ALA B CA  1 
ATOM   1311 C  C   . ALA B 2 56  ? -6.785  -11.906 26.816 1.00 21.98 ? 55  ALA B C   1 
ATOM   1312 O  O   . ALA B 2 56  ? -6.675  -10.719 27.132 1.00 26.08 ? 55  ALA B O   1 
ATOM   1313 C  CB  . ALA B 2 56  ? -4.771  -12.361 28.233 1.00 22.26 ? 55  ALA B CB  1 
ATOM   1314 N  N   . GLY B 2 57  ? -7.642  -12.325 25.898 1.00 21.71 ? 56  GLY B N   1 
ATOM   1315 C  CA  . GLY B 2 57  ? -8.468  -11.381 25.172 1.00 21.96 ? 56  GLY B CA  1 
ATOM   1316 C  C   . GLY B 2 57  ? -7.588  -10.412 24.411 1.00 21.72 ? 56  GLY B C   1 
ATOM   1317 O  O   . GLY B 2 57  ? -6.503  -10.779 23.951 1.00 22.51 ? 56  GLY B O   1 
ATOM   1318 N  N   . CYS B 2 58  ? -8.036  -9.166  24.290 1.00 20.09 ? 57  CYS B N   1 
ATOM   1319 C  CA  . CYS B 2 58  ? -7.300  -8.180  23.508 1.00 20.11 ? 57  CYS B CA  1 
ATOM   1320 C  C   . CYS B 2 58  ? -5.979  -7.805  24.165 1.00 20.08 ? 57  CYS B C   1 
ATOM   1321 O  O   . CYS B 2 58  ? -5.076  -7.279  23.511 1.00 20.07 ? 57  CYS B O   1 
ATOM   1322 C  CB  . CYS B 2 58  ? -8.144  -6.920  23.310 1.00 23.94 ? 57  CYS B CB  1 
ATOM   1323 S  SG  . CYS B 2 58  ? -9.732  -7.220  22.529 1.00 29.62 ? 57  CYS B SG  1 
ATOM   1324 N  N   . THR B 2 59  ? -5.860  -8.072  25.460 1.00 19.73 ? 58  THR B N   1 
ATOM   1325 C  CA  . THR B 2 59  ? -4.663  -7.668  26.185 1.00 19.66 ? 58  THR B CA  1 
ATOM   1326 C  C   . THR B 2 59  ? -3.398  -8.390  25.719 1.00 19.13 ? 58  THR B C   1 
ATOM   1327 O  O   . THR B 2 59  ? -2.294  -7.888  25.924 1.00 23.09 ? 58  THR B O   1 
ATOM   1328 C  CB  . THR B 2 59  ? -4.833  -7.850  27.705 1.00 21.98 ? 58  THR B CB  1 
ATOM   1329 O  OG1 . THR B 2 59  ? -4.688  -9.232  28.034 1.00 27.96 ? 58  THR B OG1 1 
ATOM   1330 C  CG2 . THR B 2 59  ? -6.204  -7.365  28.144 1.00 23.18 ? 58  THR B CG2 1 
ATOM   1331 N  N   . SER B 2 60  ? -3.553  -9.553  25.086 1.00 16.00 ? 59  SER B N   1 
ATOM   1332 C  CA  . SER B 2 60  ? -2.402  -10.333 24.635 1.00 17.01 ? 59  SER B CA  1 
ATOM   1333 C  C   . SER B 2 60  ? -2.018  -10.106 23.174 1.00 15.81 ? 59  SER B C   1 
ATOM   1334 O  O   . SER B 2 60  ? -1.124  -10.777 22.652 1.00 17.00 ? 59  SER B O   1 
ATOM   1335 C  CB  . SER B 2 60  ? -2.619  -11.828 24.903 1.00 18.75 ? 59  SER B CB  1 
ATOM   1336 O  OG  . SER B 2 60  ? -3.933  -12.222 24.567 1.00 19.96 ? 59  SER B OG  1 
ATOM   1337 N  N   . ALA B 2 61  ? -2.676  -9.149  22.523 1.00 15.62 ? 60  ALA B N   1 
ATOM   1338 C  CA  . ALA B 2 61  ? -2.448  -8.893  21.101 1.00 16.90 ? 60  ALA B CA  1 
ATOM   1339 C  C   . ALA B 2 61  ? -1.087  -8.262  20.803 1.00 14.25 ? 60  ALA B C   1 
ATOM   1340 O  O   . ALA B 2 61  ? -0.665  -8.211  19.642 1.00 16.54 ? 60  ALA B O   1 
ATOM   1341 C  CB  . ALA B 2 61  ? -3.559  -8.019  20.543 1.00 18.58 ? 60  ALA B CB  1 
ATOM   1342 N  N   . GLY B 2 62  ? -0.419  -7.761  21.838 1.00 14.35 ? 61  GLY B N   1 
ATOM   1343 C  CA  . GLY B 2 62  ? 0.903   -7.183  21.681 1.00 13.93 ? 61  GLY B CA  1 
ATOM   1344 C  C   . GLY B 2 62  ? 0.853   -5.760  21.158 1.00 14.61 ? 61  GLY B C   1 
ATOM   1345 O  O   . GLY B 2 62  ? -0.210  -5.149  21.119 1.00 15.34 ? 61  GLY B O   1 
ATOM   1346 N  N   . PRO B 2 63  ? 2.011   -5.222  20.754 1.00 15.97 ? 62  PRO B N   1 
ATOM   1347 C  CA  . PRO B 2 63  ? 2.121   -3.842  20.263 1.00 16.57 ? 62  PRO B CA  1 
ATOM   1348 C  C   . PRO B 2 63  ? 1.432   -3.641  18.916 1.00 15.18 ? 62  PRO B C   1 
ATOM   1349 O  O   . PRO B 2 63  ? 1.112   -4.611  18.227 1.00 14.64 ? 62  PRO B O   1 
ATOM   1350 C  CB  . PRO B 2 63  ? 3.632   -3.651  20.067 1.00 18.50 ? 62  PRO B CB  1 
ATOM   1351 C  CG  . PRO B 2 63  ? 4.290   -4.847  20.647 1.00 20.25 ? 62  PRO B CG  1 
ATOM   1352 C  CD  . PRO B 2 63  ? 3.297   -5.936  20.730 1.00 16.93 ? 62  PRO B CD  1 
ATOM   1353 N  N   . HIS B 2 64  ? 1.202   -2.382  18.559 1.00 15.91 ? 63  HIS B N   1 
ATOM   1354 C  CA  . HIS B 2 64  ? 0.829   -2.005  17.202 1.00 19.50 ? 63  HIS B CA  1 
ATOM   1355 C  C   . HIS B 2 64  ? 1.824   -2.678  16.255 1.00 17.60 ? 63  HIS B C   1 
ATOM   1356 O  O   . HIS B 2 64  ? 3.031   -2.623  16.487 1.00 19.94 ? 63  HIS B O   1 
ATOM   1357 C  CB  . HIS B 2 64  ? 0.955   -0.483  17.097 1.00 25.68 ? 63  HIS B CB  1 
ATOM   1358 C  CG  . HIS B 2 64  ? 0.125   0.136   16.021 1.00 32.81 ? 63  HIS B CG  1 
ATOM   1359 N  ND1 . HIS B 2 64  ? -0.778  1.147   16.276 1.00 35.07 ? 63  HIS B ND1 1 
ATOM   1360 C  CD2 . HIS B 2 64  ? 0.090   -0.072  14.684 1.00 36.65 ? 63  HIS B CD2 1 
ATOM   1361 C  CE1 . HIS B 2 64  ? -1.351  1.518   15.145 1.00 36.59 ? 63  HIS B CE1 1 
ATOM   1362 N  NE2 . HIS B 2 64  ? -0.842  0.794   14.164 1.00 37.77 ? 63  HIS B NE2 1 
ATOM   1363 N  N   . PHE B 2 65  ? 1.332   -3.324  15.201 1.00 16.10 ? 64  PHE B N   1 
ATOM   1364 C  CA  . PHE B 2 65  ? 2.210   -4.010  14.253 1.00 15.09 ? 64  PHE B CA  1 
ATOM   1365 C  C   . PHE B 2 65  ? 3.045   -2.983  13.498 1.00 16.97 ? 64  PHE B C   1 
ATOM   1366 O  O   . PHE B 2 65  ? 2.509   -2.112  12.810 1.00 19.91 ? 64  PHE B O   1 
ATOM   1367 C  CB  . PHE B 2 65  ? 1.382   -4.853  13.275 1.00 14.53 ? 64  PHE B CB  1 
ATOM   1368 C  CG  . PHE B 2 65  ? 2.200   -5.621  12.265 1.00 15.94 ? 64  PHE B CG  1 
ATOM   1369 C  CD1 . PHE B 2 65  ? 3.262   -6.419  12.660 1.00 16.49 ? 64  PHE B CD1 1 
ATOM   1370 C  CD2 . PHE B 2 65  ? 1.871   -5.571  10.917 1.00 17.25 ? 64  PHE B CD2 1 
ATOM   1371 C  CE1 . PHE B 2 65  ? 3.997   -7.140  11.719 1.00 16.07 ? 64  PHE B CE1 1 
ATOM   1372 C  CE2 . PHE B 2 65  ? 2.601   -6.280  9.973  1.00 17.41 ? 64  PHE B CE2 1 
ATOM   1373 C  CZ  . PHE B 2 65  ? 3.665   -7.066  10.373 1.00 17.92 ? 64  PHE B CZ  1 
ATOM   1374 N  N   . ASN B 2 66  ? 4.359   -3.082  13.632 1.00 18.59 ? 65  ASN B N   1 
ATOM   1375 C  CA  . ASN B 2 66  ? 5.246   -2.143  12.966 1.00 21.03 ? 65  ASN B CA  1 
ATOM   1376 C  C   . ASN B 2 66  ? 6.665   -2.680  12.944 1.00 22.38 ? 65  ASN B C   1 
ATOM   1377 O  O   . ASN B 2 66  ? 7.521   -2.230  13.706 1.00 24.88 ? 65  ASN B O   1 
ATOM   1378 C  CB  . ASN B 2 66  ? 5.196   -0.782  13.657 1.00 26.13 ? 65  ASN B CB  1 
ATOM   1379 C  CG  . ASN B 2 66  ? 5.759   0.331   12.791 1.00 31.46 ? 65  ASN B CG  1 
ATOM   1380 O  OD1 . ASN B 2 66  ? 5.526   0.377   11.577 1.00 31.27 ? 65  ASN B OD1 1 
ATOM   1381 N  ND2 . ASN B 2 66  ? 6.504   1.236   13.411 1.00 35.70 ? 65  ASN B ND2 1 
ATOM   1382 N  N   . PRO B 2 67  ? 6.919   -3.650  12.059 1.00 24.57 ? 66  PRO B N   1 
ATOM   1383 C  CA  . PRO B 2 67  ? 8.201   -4.358  12.002 1.00 28.48 ? 66  PRO B CA  1 
ATOM   1384 C  C   . PRO B 2 67  ? 9.354   -3.400  11.744 1.00 31.59 ? 66  PRO B C   1 
ATOM   1385 O  O   . PRO B 2 67  ? 9.274   -2.596  10.815 1.00 33.28 ? 66  PRO B O   1 
ATOM   1386 C  CB  . PRO B 2 67  ? 8.042   -5.285  10.790 1.00 30.24 ? 66  PRO B CB  1 
ATOM   1387 C  CG  . PRO B 2 67  ? 6.594   -5.335  10.498 1.00 28.64 ? 66  PRO B CG  1 
ATOM   1388 C  CD  . PRO B 2 67  ? 6.011   -4.047  10.969 1.00 25.89 ? 66  PRO B CD  1 
ATOM   1389 N  N   . LEU B 2 68  ? 10.407  -3.485  12.551 1.00 32.66 ? 67  LEU B N   1 
ATOM   1390 C  CA  . LEU B 2 68  ? 11.590  -2.662  12.328 1.00 38.01 ? 67  LEU B CA  1 
ATOM   1391 C  C   . LEU B 2 68  ? 12.389  -3.183  11.140 1.00 44.70 ? 67  LEU B C   1 
ATOM   1392 O  O   . LEU B 2 68  ? 13.147  -2.438  10.517 1.00 46.98 ? 67  LEU B O   1 
ATOM   1393 C  CB  . LEU B 2 68  ? 12.471  -2.616  13.578 1.00 37.35 ? 67  LEU B CB  1 
ATOM   1394 C  CG  . LEU B 2 68  ? 11.868  -1.907  14.791 1.00 39.94 ? 67  LEU B CG  1 
ATOM   1395 C  CD1 . LEU B 2 68  ? 12.899  -1.768  15.906 1.00 38.53 ? 67  LEU B CD1 1 
ATOM   1396 C  CD2 . LEU B 2 68  ? 11.320  -0.545  14.390 1.00 42.47 ? 67  LEU B CD2 1 
ATOM   1397 N  N   . SER B 2 69  ? 12.215  -4.464  10.830 1.00 49.51 ? 68  SER B N   1 
ATOM   1398 C  CA  . SER B 2 69  ? 12.916  -5.087  9.711  1.00 53.70 ? 68  SER B CA  1 
ATOM   1399 C  C   . SER B 2 69  ? 12.811  -4.241  8.444  1.00 55.14 ? 68  SER B C   1 
ATOM   1400 O  O   . SER B 2 69  ? 11.723  -3.807  8.064  1.00 55.65 ? 68  SER B O   1 
ATOM   1401 C  CB  . SER B 2 69  ? 12.370  -6.493  9.447  1.00 55.08 ? 68  SER B CB  1 
ATOM   1402 O  OG  . SER B 2 69  ? 11.043  -6.446  8.950  1.00 55.81 ? 68  SER B OG  1 
ATOM   1403 N  N   . ARG B 2 81  ? 2.588   3.935   11.059 1.00 29.93 ? 80  ARG B N   1 
ATOM   1404 C  CA  . ARG B 2 81  ? 2.957   2.553   11.353 1.00 29.50 ? 80  ARG B CA  1 
ATOM   1405 C  C   . ARG B 2 81  ? 2.232   1.584   10.429 1.00 24.52 ? 80  ARG B C   1 
ATOM   1406 O  O   . ARG B 2 81  ? 1.108   1.840   10.012 1.00 22.76 ? 80  ARG B O   1 
ATOM   1407 C  CB  . ARG B 2 81  ? 2.666   2.214   12.816 1.00 35.98 ? 80  ARG B CB  1 
ATOM   1408 C  CG  . ARG B 2 81  ? 3.589   2.915   13.802 1.00 42.80 ? 80  ARG B CG  1 
ATOM   1409 C  CD  . ARG B 2 81  ? 3.249   2.573   15.248 1.00 48.16 ? 80  ARG B CD  1 
ATOM   1410 N  NE  . ARG B 2 81  ? 2.151   3.387   15.765 1.00 51.68 ? 80  ARG B NE  1 
ATOM   1411 C  CZ  . ARG B 2 81  ? 1.795   3.438   17.046 1.00 54.99 ? 80  ARG B CZ  1 
ATOM   1412 N  NH1 . ARG B 2 81  ? 2.450   2.723   17.952 1.00 56.82 ? 80  ARG B NH1 1 
ATOM   1413 N  NH2 . ARG B 2 81  ? 0.783   4.209   17.422 1.00 56.24 ? 80  ARG B NH2 1 
ATOM   1414 N  N   . VAL B 2 82  ? 2.881   0.468   10.116 1.00 21.20 ? 81  VAL B N   1 
ATOM   1415 C  CA  . VAL B 2 82  ? 2.315   -0.510  9.192  1.00 19.69 ? 81  VAL B CA  1 
ATOM   1416 C  C   . VAL B 2 82  ? 0.892   -0.911  9.585  1.00 18.32 ? 81  VAL B C   1 
ATOM   1417 O  O   . VAL B 2 82  ? -0.005  -0.948  8.744  1.00 18.37 ? 81  VAL B O   1 
ATOM   1418 C  CB  . VAL B 2 82  ? 3.208   -1.766  9.100  1.00 21.74 ? 81  VAL B CB  1 
ATOM   1419 C  CG1 . VAL B 2 82  ? 2.507   -2.870  8.337  1.00 20.94 ? 81  VAL B CG1 1 
ATOM   1420 C  CG2 . VAL B 2 82  ? 4.547   -1.419  8.456  1.00 23.95 ? 81  VAL B CG2 1 
ATOM   1421 N  N   . GLY B 2 83  ? 0.685   -1.198  10.866 1.00 16.32 ? 82  GLY B N   1 
ATOM   1422 C  CA  . GLY B 2 83  ? -0.603  -1.691  11.329 1.00 15.50 ? 82  GLY B CA  1 
ATOM   1423 C  C   . GLY B 2 83  ? -1.691  -0.645  11.490 1.00 17.60 ? 82  GLY B C   1 
ATOM   1424 O  O   . GLY B 2 83  ? -2.822  -0.979  11.827 1.00 18.69 ? 82  GLY B O   1 
ATOM   1425 N  N   . ASP B 2 84  ? -1.364  0.622   11.260 1.00 19.19 ? 83  ASP B N   1 
ATOM   1426 C  CA  . ASP B 2 84  ? -2.323  1.700   11.506 1.00 20.71 ? 83  ASP B CA  1 
ATOM   1427 C  C   . ASP B 2 84  ? -3.240  1.888   10.306 1.00 20.28 ? 83  ASP B C   1 
ATOM   1428 O  O   . ASP B 2 84  ? -2.827  2.424   9.278  1.00 24.35 ? 83  ASP B O   1 
ATOM   1429 C  CB  . ASP B 2 84  ? -1.584  3.003   11.836 1.00 23.68 ? 83  ASP B CB  1 
ATOM   1430 C  CG  . ASP B 2 84  ? -2.516  4.121   12.285 1.00 30.16 ? 83  ASP B CG  1 
ATOM   1431 O  OD1 . ASP B 2 84  ? -3.744  3.897   12.385 1.00 31.36 ? 83  ASP B OD1 1 
ATOM   1432 O  OD2 . ASP B 2 84  ? -2.007  5.233   12.555 1.00 33.31 ? 83  ASP B OD2 1 
ATOM   1433 N  N   . LEU B 2 85  ? -4.485  1.440   10.438 1.00 18.17 ? 84  LEU B N   1 
ATOM   1434 C  CA  . LEU B 2 85  ? -5.456  1.549   9.355  1.00 19.28 ? 84  LEU B CA  1 
ATOM   1435 C  C   . LEU B 2 85  ? -6.302  2.808   9.477  1.00 22.37 ? 84  LEU B C   1 
ATOM   1436 O  O   . LEU B 2 85  ? -7.236  3.009   8.704  1.00 27.42 ? 84  LEU B O   1 
ATOM   1437 C  CB  . LEU B 2 85  ? -6.352  0.309   9.312  1.00 19.73 ? 84  LEU B CB  1 
ATOM   1438 C  CG  . LEU B 2 85  ? -5.579  -0.997  9.125  1.00 21.76 ? 84  LEU B CG  1 
ATOM   1439 C  CD1 . LEU B 2 85  ? -6.513  -2.200  9.157  1.00 21.48 ? 84  LEU B CD1 1 
ATOM   1440 C  CD2 . LEU B 2 85  ? -4.789  -0.947  7.824  1.00 25.32 ? 84  LEU B CD2 1 
ATOM   1441 N  N   . GLY B 2 86  ? -5.965  3.654   10.445 1.00 21.21 ? 85  GLY B N   1 
ATOM   1442 C  CA  . GLY B 2 86  ? -6.665  4.909   10.642 1.00 22.27 ? 85  GLY B CA  1 
ATOM   1443 C  C   . GLY B 2 86  ? -7.783  4.802   11.657 1.00 21.58 ? 85  GLY B C   1 
ATOM   1444 O  O   . GLY B 2 86  ? -7.685  4.047   12.622 1.00 24.58 ? 85  GLY B O   1 
ATOM   1445 N  N   . ASN B 2 87  ? -8.840  5.577   11.439 1.00 23.57 ? 86  ASN B N   1 
ATOM   1446 C  CA  . ASN B 2 87  ? -10.021 5.548   12.288 1.00 22.24 ? 86  ASN B CA  1 
ATOM   1447 C  C   . ASN B 2 87  ? -11.223 4.997   11.536 1.00 22.59 ? 86  ASN B C   1 
ATOM   1448 O  O   . ASN B 2 87  ? -11.349 5.196   10.324 1.00 25.64 ? 86  ASN B O   1 
ATOM   1449 C  CB  . ASN B 2 87  ? -10.372 6.961   12.768 1.00 25.07 ? 86  ASN B CB  1 
ATOM   1450 C  CG  . ASN B 2 87  ? -9.401  7.491   13.800 1.00 25.88 ? 86  ASN B CG  1 
ATOM   1451 O  OD1 . ASN B 2 87  ? -9.084  6.814   14.773 1.00 27.49 ? 86  ASN B OD1 1 
ATOM   1452 N  ND2 . ASN B 2 87  ? -8.926  8.711   13.593 1.00 29.75 ? 86  ASN B ND2 1 
ATOM   1453 N  N   . VAL B 2 88  ? -12.104 4.309   12.255 1.00 20.07 ? 87  VAL B N   1 
ATOM   1454 C  CA  . VAL B 2 88  ? -13.439 4.023   11.742 1.00 20.22 ? 87  VAL B CA  1 
ATOM   1455 C  C   . VAL B 2 88  ? -14.423 4.961   12.430 1.00 21.34 ? 87  VAL B C   1 
ATOM   1456 O  O   . VAL B 2 88  ? -14.173 5.416   13.549 1.00 22.34 ? 87  VAL B O   1 
ATOM   1457 C  CB  . VAL B 2 88  ? -13.857 2.552   11.965 1.00 20.59 ? 87  VAL B CB  1 
ATOM   1458 C  CG1 . VAL B 2 88  ? -12.915 1.619   11.213 1.00 22.07 ? 87  VAL B CG1 1 
ATOM   1459 C  CG2 . VAL B 2 88  ? -13.891 2.216   13.457 1.00 22.41 ? 87  VAL B CG2 1 
ATOM   1460 N  N   . THR B 2 89  ? -15.533 5.257   11.761 1.00 20.63 ? 88  THR B N   1 
ATOM   1461 C  CA  . THR B 2 89  ? -16.501 6.213   12.286 1.00 23.39 ? 88  THR B CA  1 
ATOM   1462 C  C   . THR B 2 89  ? -17.827 5.535   12.593 1.00 22.17 ? 88  THR B C   1 
ATOM   1463 O  O   . THR B 2 89  ? -18.489 5.028   11.694 1.00 23.41 ? 88  THR B O   1 
ATOM   1464 C  CB  . THR B 2 89  ? -16.770 7.347   11.282 1.00 27.41 ? 88  THR B CB  1 
ATOM   1465 O  OG1 . THR B 2 89  ? -15.539 8.000   10.949 1.00 30.48 ? 88  THR B OG1 1 
ATOM   1466 C  CG2 . THR B 2 89  ? -17.743 8.364   11.874 1.00 27.31 ? 88  THR B CG2 1 
ATOM   1467 N  N   . ALA B 2 90  ? -18.213 5.532   13.864 1.00 23.31 ? 89  ALA B N   1 
ATOM   1468 C  CA  . ALA B 2 90  ? -19.504 4.989   14.267 1.00 22.17 ? 89  ALA B CA  1 
ATOM   1469 C  C   . ALA B 2 90  ? -20.596 6.059   14.195 1.00 24.06 ? 89  ALA B C   1 
ATOM   1470 O  O   . ALA B 2 90  ? -20.379 7.211   14.589 1.00 25.30 ? 89  ALA B O   1 
ATOM   1471 C  CB  . ALA B 2 90  ? -19.422 4.410   15.673 1.00 23.17 ? 89  ALA B CB  1 
ATOM   1472 N  N   . ASP B 2 91  ? -21.766 5.678   13.689 1.00 25.98 ? 90  ASP B N   1 
ATOM   1473 C  CA  . ASP B 2 91  ? -22.905 6.591   13.635 1.00 26.90 ? 90  ASP B CA  1 
ATOM   1474 C  C   . ASP B 2 91  ? -23.670 6.622   14.959 1.00 29.07 ? 90  ASP B C   1 
ATOM   1475 O  O   . ASP B 2 91  ? -23.217 6.059   15.956 1.00 28.40 ? 90  ASP B O   1 
ATOM   1476 C  CB  . ASP B 2 91  ? -23.830 6.261   12.456 1.00 30.41 ? 90  ASP B CB  1 
ATOM   1477 C  CG  . ASP B 2 91  ? -24.463 4.876   12.556 1.00 33.04 ? 90  ASP B CG  1 
ATOM   1478 O  OD1 . ASP B 2 91  ? -24.502 4.292   13.661 1.00 30.52 ? 90  ASP B OD1 1 
ATOM   1479 O  OD2 . ASP B 2 91  ? -24.943 4.376   11.513 1.00 36.93 ? 90  ASP B OD2 1 
ATOM   1480 N  N   . LYS B 2 92  ? -24.821 7.287   14.971 1.00 31.18 ? 91  LYS B N   1 
ATOM   1481 C  CA  . LYS B 2 92  ? -25.584 7.457   16.204 1.00 33.30 ? 91  LYS B CA  1 
ATOM   1482 C  C   . LYS B 2 92  ? -26.148 6.136   16.723 1.00 34.17 ? 91  LYS B C   1 
ATOM   1483 O  O   . LYS B 2 92  ? -26.510 6.024   17.896 1.00 37.75 ? 91  LYS B O   1 
ATOM   1484 C  CB  . LYS B 2 92  ? -26.712 8.481   16.014 1.00 37.52 ? 91  LYS B CB  1 
ATOM   1485 C  CG  . LYS B 2 92  ? -27.789 8.058   15.022 1.00 42.62 ? 91  LYS B CG  1 
ATOM   1486 C  CD  . LYS B 2 92  ? -28.978 9.016   15.053 1.00 46.96 ? 91  LYS B CD  1 
ATOM   1487 C  CE  . LYS B 2 92  ? -30.142 8.500   14.215 1.00 51.42 ? 91  LYS B CE  1 
ATOM   1488 N  NZ  . LYS B 2 92  ? -29.846 8.493   12.750 1.00 53.50 ? 91  LYS B NZ  1 
ATOM   1489 N  N   . ASP B 2 93  ? -26.223 5.138   15.847 1.00 31.58 ? 92  ASP B N   1 
ATOM   1490 C  CA  . ASP B 2 93  ? -26.711 3.819   16.237 1.00 31.74 ? 92  ASP B CA  1 
ATOM   1491 C  C   . ASP B 2 93  ? -25.575 2.922   16.706 1.00 27.52 ? 92  ASP B C   1 
ATOM   1492 O  O   . ASP B 2 93  ? -25.797 1.763   17.069 1.00 26.86 ? 92  ASP B O   1 
ATOM   1493 C  CB  . ASP B 2 93  ? -27.473 3.153   15.087 1.00 34.53 ? 92  ASP B CB  1 
ATOM   1494 C  CG  . ASP B 2 93  ? -28.871 3.717   14.913 1.00 40.58 ? 92  ASP B CG  1 
ATOM   1495 O  OD1 . ASP B 2 93  ? -29.585 3.867   15.927 1.00 43.63 ? 92  ASP B OD1 1 
ATOM   1496 O  OD2 . ASP B 2 93  ? -29.254 4.012   13.764 1.00 42.90 ? 92  ASP B OD2 1 
ATOM   1497 N  N   . GLY B 2 94  ? -24.360 3.463   16.687 1.00 23.93 ? 93  GLY B N   1 
ATOM   1498 C  CA  . GLY B 2 94  ? -23.188 2.743   17.155 1.00 22.53 ? 93  GLY B CA  1 
ATOM   1499 C  C   . GLY B 2 94  ? -22.561 1.838   16.110 1.00 21.17 ? 93  GLY B C   1 
ATOM   1500 O  O   . GLY B 2 94  ? -21.752 0.976   16.441 1.00 20.12 ? 93  GLY B O   1 
ATOM   1501 N  N   . VAL B 2 95  ? -22.931 2.035   14.847 1.00 20.24 ? 94  VAL B N   1 
ATOM   1502 C  CA  . VAL B 2 95  ? -22.439 1.193   13.762 1.00 19.87 ? 94  VAL B CA  1 
ATOM   1503 C  C   . VAL B 2 95  ? -21.398 1.923   12.925 1.00 20.47 ? 94  VAL B C   1 
ATOM   1504 O  O   . VAL B 2 95  ? -21.633 3.046   12.475 1.00 22.49 ? 94  VAL B O   1 
ATOM   1505 C  CB  . VAL B 2 95  ? -23.593 0.744   12.833 1.00 21.34 ? 94  VAL B CB  1 
ATOM   1506 C  CG1 . VAL B 2 95  ? -23.064 -0.102  11.680 1.00 22.31 ? 94  VAL B CG1 1 
ATOM   1507 C  CG2 . VAL B 2 95  ? -24.643 -0.020  13.624 1.00 23.61 ? 94  VAL B CG2 1 
ATOM   1508 N  N   . ALA B 2 96  ? -20.246 1.283   12.724 1.00 18.80 ? 95  ALA B N   1 
ATOM   1509 C  CA  . ALA B 2 96  ? -19.219 1.810   11.834 1.00 20.60 ? 95  ALA B CA  1 
ATOM   1510 C  C   . ALA B 2 96  ? -19.117 0.955   10.582 1.00 22.09 ? 95  ALA B C   1 
ATOM   1511 O  O   . ALA B 2 96  ? -18.763 -0.222  10.649 1.00 23.76 ? 95  ALA B O   1 
ATOM   1512 C  CB  . ALA B 2 96  ? -17.875 1.868   12.535 1.00 21.09 ? 95  ALA B CB  1 
ATOM   1513 N  N   . ASP B 2 97  ? -19.438 1.546   9.438  1.00 22.10 ? 96  ASP B N   1 
ATOM   1514 C  CA  . ASP B 2 97  ? -19.238 0.868   8.169  1.00 22.48 ? 96  ASP B CA  1 
ATOM   1515 C  C   . ASP B 2 97  ? -17.833 1.163   7.688  1.00 22.71 ? 96  ASP B C   1 
ATOM   1516 O  O   . ASP B 2 97  ? -17.397 2.316   7.679  1.00 24.63 ? 96  ASP B O   1 
ATOM   1517 C  CB  . ASP B 2 97  ? -20.278 1.311   7.141  1.00 29.04 ? 96  ASP B CB  1 
ATOM   1518 C  CG  . ASP B 2 97  ? -21.658 0.770   7.449  1.00 37.11 ? 96  ASP B CG  1 
ATOM   1519 O  OD1 . ASP B 2 97  ? -21.754 -0.409  7.859  1.00 39.12 ? 96  ASP B OD1 1 
ATOM   1520 O  OD2 . ASP B 2 97  ? -22.643 1.523   7.298  1.00 42.22 ? 96  ASP B OD2 1 
ATOM   1521 N  N   . VAL B 2 98  ? -17.121 0.110   7.311  1.00 19.48 ? 97  VAL B N   1 
ATOM   1522 C  CA  . VAL B 2 98  ? -15.712 0.215   6.969  1.00 19.44 ? 97  VAL B CA  1 
ATOM   1523 C  C   . VAL B 2 98  ? -15.484 -0.056  5.487  1.00 18.27 ? 97  VAL B C   1 
ATOM   1524 O  O   . VAL B 2 98  ? -15.942 -1.060  4.950  1.00 17.66 ? 97  VAL B O   1 
ATOM   1525 C  CB  . VAL B 2 98  ? -14.875 -0.788  7.791  1.00 19.28 ? 97  VAL B CB  1 
ATOM   1526 C  CG1 . VAL B 2 98  ? -13.396 -0.681  7.437  1.00 20.11 ? 97  VAL B CG1 1 
ATOM   1527 C  CG2 . VAL B 2 98  ? -15.100 -0.568  9.286  1.00 20.97 ? 97  VAL B CG2 1 
ATOM   1528 N  N   . SER B 2 99  ? -14.776 0.850   4.831  1.00 19.17 ? 98  SER B N   1 
ATOM   1529 C  CA  . SER B 2 99  ? -14.329 0.626   3.464  1.00 20.80 ? 98  SER B CA  1 
ATOM   1530 C  C   . SER B 2 99  ? -13.044 1.409   3.249  1.00 21.81 ? 98  SER B C   1 
ATOM   1531 O  O   . SER B 2 99  ? -13.059 2.638   3.135  1.00 26.58 ? 98  SER B O   1 
ATOM   1532 C  CB  . SER B 2 99  ? -15.396 1.042   2.451  1.00 26.06 ? 98  SER B CB  1 
ATOM   1533 O  OG  . SER B 2 99  ? -14.941 0.812   1.124  1.00 30.24 ? 98  SER B OG  1 
ATOM   1534 N  N   . ILE B 2 100 ? -11.934 0.681   3.211  1.00 19.39 ? 99  ILE B N   1 
ATOM   1535 C  CA  . ILE B 2 100 ? -10.605 1.261   3.171  1.00 20.90 ? 99  ILE B CA  1 
ATOM   1536 C  C   . ILE B 2 100 ? -9.789  0.542   2.111  1.00 19.19 ? 99  ILE B C   1 
ATOM   1537 O  O   . ILE B 2 100 ? -10.029 -0.632  1.818  1.00 21.20 ? 99  ILE B O   1 
ATOM   1538 C  CB  . ILE B 2 100 ? -9.890  1.072   4.535  1.00 26.35 ? 99  ILE B CB  1 
ATOM   1539 C  CG1 . ILE B 2 100 ? -10.753 1.612   5.679  1.00 31.40 ? 99  ILE B CG1 1 
ATOM   1540 C  CG2 . ILE B 2 100 ? -8.517  1.730   4.533  1.00 32.45 ? 99  ILE B CG2 1 
ATOM   1541 C  CD1 . ILE B 2 100 ? -10.106 1.476   7.042  1.00 30.65 ? 99  ILE B CD1 1 
ATOM   1542 N  N   . GLU B 2 101 ? -8.833  1.255   1.531  1.00 18.80 ? 100 GLU B N   1 
ATOM   1543 C  CA  . GLU B 2 101 ? -7.804  0.643   0.713  1.00 21.32 ? 100 GLU B CA  1 
ATOM   1544 C  C   . GLU B 2 101 ? -6.461  1.002   1.333  1.00 21.63 ? 100 GLU B C   1 
ATOM   1545 O  O   . GLU B 2 101 ? -6.190  2.172   1.602  1.00 23.28 ? 100 GLU B O   1 
ATOM   1546 C  CB  . GLU B 2 101 ? -7.887  1.173   -0.717 1.00 27.81 ? 100 GLU B CB  1 
ATOM   1547 C  CG  . GLU B 2 101 ? -6.790  0.676   -1.634 1.00 32.35 ? 100 GLU B CG  1 
ATOM   1548 C  CD  . GLU B 2 101 ? -6.949  1.195   -3.049 1.00 38.62 ? 100 GLU B CD  1 
ATOM   1549 O  OE1 . GLU B 2 101 ? -8.100  1.452   -3.462 1.00 41.21 ? 100 GLU B OE1 1 
ATOM   1550 O  OE2 . GLU B 2 101 ? -5.924  1.356   -3.745 1.00 41.22 ? 100 GLU B OE2 1 
ATOM   1551 N  N   . ASP B 2 102 ? -5.624  -0.001  1.571  1.00 19.90 ? 101 ASP B N   1 
ATOM   1552 C  CA  . ASP B 2 102 ? -4.320  0.230   2.193  1.00 19.81 ? 101 ASP B CA  1 
ATOM   1553 C  C   . ASP B 2 102 ? -3.239  -0.484  1.397  1.00 19.72 ? 101 ASP B C   1 
ATOM   1554 O  O   . ASP B 2 102 ? -3.356  -1.675  1.122  1.00 21.21 ? 101 ASP B O   1 
ATOM   1555 C  CB  . ASP B 2 102 ? -4.322  -0.266  3.642  1.00 22.12 ? 101 ASP B CB  1 
ATOM   1556 C  CG  . ASP B 2 102 ? -3.118  0.221   4.432  1.00 26.50 ? 101 ASP B CG  1 
ATOM   1557 O  OD1 . ASP B 2 102 ? -3.279  1.148   5.252  1.00 32.10 ? 101 ASP B OD1 1 
ATOM   1558 O  OD2 . ASP B 2 102 ? -2.010  -0.313  4.235  1.00 24.58 ? 101 ASP B OD2 1 
ATOM   1559 N  N   . SER B 2 103 ? -2.187  0.240   1.022  1.00 21.85 ? 102 SER B N   1 
ATOM   1560 C  CA  . SER B 2 103 ? -1.118  -0.351  0.225  1.00 23.22 ? 102 SER B CA  1 
ATOM   1561 C  C   . SER B 2 103 ? 0.141   -0.653  1.043  1.00 23.13 ? 102 SER B C   1 
ATOM   1562 O  O   . SER B 2 103 ? 1.184   -0.988  0.481  1.00 26.12 ? 102 SER B O   1 
ATOM   1563 C  CB  . SER B 2 103 ? -0.767  0.553   -0.957 1.00 30.24 ? 102 SER B CB  1 
ATOM   1564 O  OG  . SER B 2 103 ? -0.345  1.828   -0.503 1.00 36.42 ? 102 SER B OG  1 
ATOM   1565 N  N   . VAL B 2 104 ? 0.043   -0.528  2.363  1.00 21.77 ? 103 VAL B N   1 
ATOM   1566 C  CA  . VAL B 2 104 ? 1.173   -0.821  3.239  1.00 20.99 ? 103 VAL B CA  1 
ATOM   1567 C  C   . VAL B 2 104 ? 1.039   -2.207  3.881  1.00 18.83 ? 103 VAL B C   1 
ATOM   1568 O  O   . VAL B 2 104 ? 2.003   -2.971  3.938  1.00 22.50 ? 103 VAL B O   1 
ATOM   1569 C  CB  . VAL B 2 104 ? 1.350   0.265   4.316  1.00 24.75 ? 103 VAL B CB  1 
ATOM   1570 C  CG1 . VAL B 2 104 ? 2.471   -0.110  5.266  1.00 28.19 ? 103 VAL B CG1 1 
ATOM   1571 C  CG2 . VAL B 2 104 ? 1.632   1.613   3.655  1.00 27.22 ? 103 VAL B CG2 1 
ATOM   1572 N  N   . ILE B 2 105 ? -0.153  -2.547  4.359  1.00 16.63 ? 104 ILE B N   1 
ATOM   1573 C  CA  . ILE B 2 105 ? -0.375  -3.909  4.827  1.00 15.64 ? 104 ILE B CA  1 
ATOM   1574 C  C   . ILE B 2 105 ? -0.400  -4.857  3.631  1.00 15.70 ? 104 ILE B C   1 
ATOM   1575 O  O   . ILE B 2 105 ? -0.500  -4.420  2.482  1.00 17.02 ? 104 ILE B O   1 
ATOM   1576 C  CB  . ILE B 2 105 ? -1.680  -4.052  5.628  1.00 15.73 ? 104 ILE B CB  1 
ATOM   1577 C  CG1 . ILE B 2 105 ? -2.874  -3.597  4.785  1.00 16.07 ? 104 ILE B CG1 1 
ATOM   1578 C  CG2 . ILE B 2 105 ? -1.590  -3.255  6.927  1.00 19.65 ? 104 ILE B CG2 1 
ATOM   1579 C  CD1 . ILE B 2 105 ? -4.217  -4.032  5.341  1.00 16.84 ? 104 ILE B CD1 1 
ATOM   1580 N  N   . SER B 2 106 ? -0.302  -6.153  3.904  1.00 14.61 ? 105 SER B N   1 
ATOM   1581 C  CA  . SER B 2 106 ? -0.304  -7.155  2.848  1.00 14.15 ? 105 SER B CA  1 
ATOM   1582 C  C   . SER B 2 106 ? -0.828  -8.475  3.391  1.00 13.73 ? 105 SER B C   1 
ATOM   1583 O  O   . SER B 2 106 ? -0.851  -8.683  4.601  1.00 13.98 ? 105 SER B O   1 
ATOM   1584 C  CB  . SER B 2 106 ? 1.112   -7.341  2.295  1.00 16.33 ? 105 SER B CB  1 
ATOM   1585 O  OG  . SER B 2 106 ? 1.105   -8.181  1.156  1.00 18.26 ? 105 SER B OG  1 
ATOM   1586 N  N   . LEU B 2 107 ? -1.269  -9.356  2.498  1.00 15.10 ? 106 LEU B N   1 
ATOM   1587 C  CA  . LEU B 2 107 ? -1.665  -10.704 2.893  1.00 14.40 ? 106 LEU B CA  1 
ATOM   1588 C  C   . LEU B 2 107 ? -0.544  -11.702 2.599  1.00 18.68 ? 106 LEU B C   1 
ATOM   1589 O  O   . LEU B 2 107 ? -0.743  -12.920 2.677  1.00 21.65 ? 106 LEU B O   1 
ATOM   1590 C  CB  . LEU B 2 107 ? -2.985  -11.122 2.228  1.00 15.23 ? 106 LEU B CB  1 
ATOM   1591 C  CG  . LEU B 2 107 ? -4.201  -10.231 2.513  1.00 14.75 ? 106 LEU B CG  1 
ATOM   1592 C  CD1 . LEU B 2 107 ? -5.480  -10.798 1.872  1.00 16.52 ? 106 LEU B CD1 1 
ATOM   1593 C  CD2 . LEU B 2 107 ? -4.408  -10.013 4.017  1.00 16.31 ? 106 LEU B CD2 1 
ATOM   1594 N  N   . SER B 2 108 ? 0.631   -11.171 2.259  1.00 20.68 ? 107 SER B N   1 
ATOM   1595 C  CA  . SER B 2 108 ? 1.862   -11.960 2.152  1.00 26.95 ? 107 SER B CA  1 
ATOM   1596 C  C   . SER B 2 108 ? 3.095   -11.078 2.402  1.00 26.96 ? 107 SER B C   1 
ATOM   1597 O  O   . SER B 2 108 ? 2.975   -9.861  2.539  1.00 27.79 ? 107 SER B O   1 
ATOM   1598 C  CB  . SER B 2 108 ? 1.973   -12.594 0.771  1.00 32.16 ? 107 SER B CB  1 
ATOM   1599 O  OG  . SER B 2 108 ? 2.355   -11.623 -0.186 1.00 35.44 ? 107 SER B OG  1 
ATOM   1600 N  N   . GLY B 2 109 ? 4.277   -11.687 2.460  1.00 29.13 ? 108 GLY B N   1 
ATOM   1601 C  CA  . GLY B 2 109 ? 5.515   -10.924 2.555  1.00 29.42 ? 108 GLY B CA  1 
ATOM   1602 C  C   . GLY B 2 109 ? 5.807   -10.306 3.918  1.00 30.77 ? 108 GLY B C   1 
ATOM   1603 O  O   . GLY B 2 109 ? 5.196   -10.680 4.916  1.00 30.84 ? 108 GLY B O   1 
ATOM   1604 N  N   . ASP B 2 110 ? 6.739   -9.352  3.951  1.00 29.95 ? 109 ASP B N   1 
ATOM   1605 C  CA  . ASP B 2 110 ? 7.196   -8.737  5.206  1.00 31.90 ? 109 ASP B CA  1 
ATOM   1606 C  C   . ASP B 2 110 ? 6.096   -8.032  6.003  1.00 30.31 ? 109 ASP B C   1 
ATOM   1607 O  O   . ASP B 2 110 ? 6.151   -7.976  7.239  1.00 30.20 ? 109 ASP B O   1 
ATOM   1608 C  CB  . ASP B 2 110 ? 8.333   -7.742  4.939  1.00 37.87 ? 109 ASP B CB  1 
ATOM   1609 C  CG  . ASP B 2 110 ? 9.681   -8.419  4.777  1.00 43.84 ? 109 ASP B CG  1 
ATOM   1610 O  OD1 . ASP B 2 110 ? 9.832   -9.569  5.240  1.00 47.22 ? 109 ASP B OD1 1 
ATOM   1611 O  OD2 . ASP B 2 110 ? 10.593  -7.793  4.193  1.00 44.83 ? 109 ASP B OD2 1 
ATOM   1612 N  N   . HIS B 2 111 ? 5.113   -7.474  5.303  1.00 24.80 ? 110 HIS B N   1 
ATOM   1613 C  CA  . HIS B 2 111 ? 4.032   -6.756  5.975  1.00 22.71 ? 110 HIS B CA  1 
ATOM   1614 C  C   . HIS B 2 111 ? 2.761   -7.595  6.087  1.00 19.70 ? 110 HIS B C   1 
ATOM   1615 O  O   . HIS B 2 111 ? 1.660   -7.050  6.194  1.00 18.05 ? 110 HIS B O   1 
ATOM   1616 C  CB  . HIS B 2 111 ? 3.733   -5.435  5.261  1.00 24.97 ? 110 HIS B CB  1 
ATOM   1617 C  CG  . HIS B 2 111 ? 4.840   -4.432  5.360  1.00 29.61 ? 110 HIS B CG  1 
ATOM   1618 N  ND1 . HIS B 2 111 ? 4.847   -3.257  4.639  1.00 33.54 ? 110 HIS B ND1 1 
ATOM   1619 C  CD2 . HIS B 2 111 ? 5.975   -4.427  6.099  1.00 31.01 ? 110 HIS B CD2 1 
ATOM   1620 C  CE1 . HIS B 2 111 ? 5.941   -2.572  4.927  1.00 32.92 ? 110 HIS B CE1 1 
ATOM   1621 N  NE2 . HIS B 2 111 ? 6.642   -3.260  5.809  1.00 31.34 ? 110 HIS B NE2 1 
HETATM 1622 N  N   . CSX B 2 112 ? 2.921   -8.919  6.073  1.00 19.58 ? 111 CSX B N   1 
HETATM 1623 C  CA  . CSX B 2 112 ? 1.796   -9.816  6.115  1.00 16.55 ? 111 CSX B CA  1 
HETATM 1624 C  CB  . CSX B 2 112 ? 2.218   -11.225 5.870  1.00 20.02 ? 111 CSX B CB  1 
HETATM 1625 S  SG  . CSX B 2 112 ? 0.927   -12.426 5.766  1.00 24.48 ? 111 CSX B SG  1 
HETATM 1626 C  C   . CSX B 2 112 ? 1.093   -9.731  7.428  1.00 13.21 ? 111 CSX B C   1 
HETATM 1627 O  O   . CSX B 2 112 ? 1.723   -9.713  8.483  1.00 16.90 ? 111 CSX B O   1 
HETATM 1628 O  OD  . CSX B 2 112 ? 1.474   -13.670 5.200  1.00 32.17 ? 111 CSX B OD  1 
ATOM   1629 N  N   . ILE B 2 113 ? -0.232  -9.676  7.376  1.00 10.27 ? 112 ILE B N   1 
ATOM   1630 C  CA  . ILE B 2 113 ? -1.040  -9.532  8.587  1.00 11.56 ? 112 ILE B CA  1 
ATOM   1631 C  C   . ILE B 2 113 ? -1.863  -10.769 8.921  1.00 9.95  ? 112 ILE B C   1 
ATOM   1632 O  O   . ILE B 2 113 ? -2.587  -10.776 9.918  1.00 11.33 ? 112 ILE B O   1 
ATOM   1633 C  CB  . ILE B 2 113 ? -1.979  -8.312  8.510  1.00 11.50 ? 112 ILE B CB  1 
ATOM   1634 C  CG1 . ILE B 2 113 ? -2.981  -8.470  7.356  1.00 14.65 ? 112 ILE B CG1 1 
ATOM   1635 C  CG2 . ILE B 2 113 ? -1.162  -7.021  8.392  1.00 14.50 ? 112 ILE B CG2 1 
ATOM   1636 C  CD1 . ILE B 2 113 ? -4.023  -7.375  7.307  1.00 17.07 ? 112 ILE B CD1 1 
ATOM   1637 N  N   . ILE B 2 114 ? -1.769  -11.809 8.093  1.00 11.40 ? 113 ILE B N   1 
ATOM   1638 C  CA  . ILE B 2 114 ? -2.431  -13.074 8.403  1.00 11.25 ? 113 ILE B CA  1 
ATOM   1639 C  C   . ILE B 2 114 ? -1.881  -13.632 9.709  1.00 9.81  ? 113 ILE B C   1 
ATOM   1640 O  O   . ILE B 2 114 ? -0.660  -13.689 9.905  1.00 12.83 ? 113 ILE B O   1 
ATOM   1641 C  CB  . ILE B 2 114 ? -2.209  -14.127 7.291  1.00 13.38 ? 113 ILE B CB  1 
ATOM   1642 C  CG1 . ILE B 2 114 ? -2.772  -13.629 5.961  1.00 18.63 ? 113 ILE B CG1 1 
ATOM   1643 C  CG2 . ILE B 2 114 ? -2.804  -15.471 7.694  1.00 12.90 ? 113 ILE B CG2 1 
ATOM   1644 C  CD1 . ILE B 2 114 ? -4.256  -13.460 5.963  1.00 19.38 ? 113 ILE B CD1 1 
ATOM   1645 N  N   . GLY B 2 115 ? -2.776  -14.048 10.601 1.00 9.90  ? 114 GLY B N   1 
ATOM   1646 C  CA  . GLY B 2 115 ? -2.368  -14.585 11.890 1.00 10.80 ? 114 GLY B CA  1 
ATOM   1647 C  C   . GLY B 2 115 ? -2.043  -13.513 12.920 1.00 10.97 ? 114 GLY B C   1 
ATOM   1648 O  O   . GLY B 2 115 ? -1.625  -13.819 14.035 1.00 10.87 ? 114 GLY B O   1 
ATOM   1649 N  N   . ARG B 2 116 ? -2.221  -12.249 12.558 1.00 10.82 ? 115 ARG B N   1 
ATOM   1650 C  CA  . ARG B 2 116 ? -2.059  -11.179 13.540 1.00 10.47 ? 115 ARG B CA  1 
ATOM   1651 C  C   . ARG B 2 116 ? -3.438  -10.759 14.035 1.00 11.91 ? 115 ARG B C   1 
ATOM   1652 O  O   . ARG B 2 116 ? -4.425  -11.388 13.681 1.00 12.85 ? 115 ARG B O   1 
ATOM   1653 C  CB  . ARG B 2 116 ? -1.237  -10.028 12.962 1.00 11.17 ? 115 ARG B CB  1 
ATOM   1654 C  CG  . ARG B 2 116 ? 0.129   -10.547 12.456 1.00 10.65 ? 115 ARG B CG  1 
ATOM   1655 C  CD  . ARG B 2 116 ? 1.135   -9.460  12.170 1.00 11.82 ? 115 ARG B CD  1 
ATOM   1656 N  NE  . ARG B 2 116 ? 2.340   -9.993  11.526 1.00 14.14 ? 115 ARG B NE  1 
ATOM   1657 C  CZ  . ARG B 2 116 ? 3.418   -10.425 12.182 1.00 15.16 ? 115 ARG B CZ  1 
ATOM   1658 N  NH1 . ARG B 2 116 ? 3.443   -10.399 13.509 1.00 15.18 ? 115 ARG B NH1 1 
ATOM   1659 N  NH2 . ARG B 2 116 ? 4.474   -10.884 11.512 1.00 16.15 ? 115 ARG B NH2 1 
ATOM   1660 N  N   . THR B 2 117 ? -3.520  -9.726  14.867 1.00 9.95  ? 116 THR B N   1 
ATOM   1661 C  CA  . THR B 2 117 ? -4.800  -9.369  15.475 1.00 12.00 ? 116 THR B CA  1 
ATOM   1662 C  C   . THR B 2 117 ? -5.283  -8.003  15.017 1.00 12.38 ? 116 THR B C   1 
ATOM   1663 O  O   . THR B 2 117 ? -4.521  -7.041  15.028 1.00 15.62 ? 116 THR B O   1 
ATOM   1664 C  CB  . THR B 2 117 ? -4.697  -9.384  17.020 1.00 13.97 ? 116 THR B CB  1 
ATOM   1665 O  OG1 . THR B 2 117 ? -4.529  -10.736 17.465 1.00 16.91 ? 116 THR B OG1 1 
ATOM   1666 C  CG2 . THR B 2 117 ? -5.950  -8.810  17.669 1.00 14.96 ? 116 THR B CG2 1 
ATOM   1667 N  N   . LEU B 2 118 ? -6.547  -7.923  14.609 1.00 10.77 ? 117 LEU B N   1 
ATOM   1668 C  CA  . LEU B 2 118 ? -7.173  -6.643  14.306 1.00 9.55  ? 117 LEU B CA  1 
ATOM   1669 C  C   . LEU B 2 118 ? -7.868  -6.139  15.566 1.00 11.89 ? 117 LEU B C   1 
ATOM   1670 O  O   . LEU B 2 118 ? -8.562  -6.901  16.232 1.00 13.73 ? 117 LEU B O   1 
ATOM   1671 C  CB  . LEU B 2 118 ? -8.194  -6.824  13.185 1.00 11.68 ? 117 LEU B CB  1 
ATOM   1672 C  CG  . LEU B 2 118 ? -8.896  -5.584  12.648 1.00 13.33 ? 117 LEU B CG  1 
ATOM   1673 C  CD1 . LEU B 2 118 ? -7.909  -4.628  11.998 1.00 15.81 ? 117 LEU B CD1 1 
ATOM   1674 C  CD2 . LEU B 2 118 ? -9.972  -6.011  11.651 1.00 13.75 ? 117 LEU B CD2 1 
ATOM   1675 N  N   . VAL B 2 119 ? -7.673  -4.860  15.889 1.00 11.64 ? 118 VAL B N   1 
ATOM   1676 C  CA  . VAL B 2 119 ? -8.213  -4.273  17.110 1.00 13.24 ? 118 VAL B CA  1 
ATOM   1677 C  C   . VAL B 2 119 ? -8.966  -2.980  16.823 1.00 14.26 ? 118 VAL B C   1 
ATOM   1678 O  O   . VAL B 2 119 ? -8.496  -2.143  16.060 1.00 15.53 ? 118 VAL B O   1 
ATOM   1679 C  CB  . VAL B 2 119 ? -7.084  -3.941  18.112 1.00 13.17 ? 118 VAL B CB  1 
ATOM   1680 C  CG1 . VAL B 2 119 ? -7.650  -3.210  19.344 1.00 15.73 ? 118 VAL B CG1 1 
ATOM   1681 C  CG2 . VAL B 2 119 ? -6.325  -5.207  18.504 1.00 15.16 ? 118 VAL B CG2 1 
ATOM   1682 N  N   . VAL B 2 120 ? -10.141 -2.827  17.425 1.00 12.89 ? 119 VAL B N   1 
ATOM   1683 C  CA  . VAL B 2 120 ? -10.825 -1.536  17.418 1.00 15.57 ? 119 VAL B CA  1 
ATOM   1684 C  C   . VAL B 2 120 ? -10.734 -0.909  18.808 1.00 14.45 ? 119 VAL B C   1 
ATOM   1685 O  O   . VAL B 2 120 ? -10.984 -1.572  19.821 1.00 15.72 ? 119 VAL B O   1 
ATOM   1686 C  CB  . VAL B 2 120 ? -12.288 -1.627  16.912 1.00 16.97 ? 119 VAL B CB  1 
ATOM   1687 C  CG1 . VAL B 2 120 ? -13.104 -2.589  17.750 1.00 18.54 ? 119 VAL B CG1 1 
ATOM   1688 C  CG2 . VAL B 2 120 ? -12.935 -0.241  16.888 1.00 17.59 ? 119 VAL B CG2 1 
ATOM   1689 N  N   . HIS B 2 121 ? -10.352 0.364   18.843 1.00 15.16 ? 120 HIS B N   1 
ATOM   1690 C  CA  . HIS B 2 121 ? -10.033 1.051   20.091 1.00 17.33 ? 120 HIS B CA  1 
ATOM   1691 C  C   . HIS B 2 121 ? -11.145 1.946   20.608 1.00 18.26 ? 120 HIS B C   1 
ATOM   1692 O  O   . HIS B 2 121 ? -12.040 2.347   19.868 1.00 20.48 ? 120 HIS B O   1 
ATOM   1693 C  CB  . HIS B 2 121 ? -8.773  1.899   19.913 1.00 17.91 ? 120 HIS B CB  1 
ATOM   1694 C  CG  . HIS B 2 121 ? -7.503  1.111   19.935 1.00 18.98 ? 120 HIS B CG  1 
ATOM   1695 N  ND1 . HIS B 2 121 ? -6.826  0.830   21.102 1.00 20.10 ? 120 HIS B ND1 1 
ATOM   1696 C  CD2 . HIS B 2 121 ? -6.777  0.564   18.933 1.00 19.55 ? 120 HIS B CD2 1 
ATOM   1697 C  CE1 . HIS B 2 121 ? -5.736  0.137   20.818 1.00 22.37 ? 120 HIS B CE1 1 
ATOM   1698 N  NE2 . HIS B 2 121 ? -5.686  -0.041  19.511 1.00 21.59 ? 120 HIS B NE2 1 
ATOM   1699 N  N   . GLU B 2 122 ? -11.041 2.280   21.889 1.00 18.50 ? 121 GLU B N   1 
ATOM   1700 C  CA  . GLU B 2 122 ? -12.002 3.126   22.590 1.00 23.28 ? 121 GLU B CA  1 
ATOM   1701 C  C   . GLU B 2 122 ? -12.022 4.556   22.048 1.00 25.05 ? 121 GLU B C   1 
ATOM   1702 O  O   . GLU B 2 122 ? -13.089 5.156   21.885 1.00 25.60 ? 121 GLU B O   1 
ATOM   1703 C  CB  . GLU B 2 122 ? -11.655 3.135   24.082 1.00 26.98 ? 121 GLU B CB  1 
ATOM   1704 C  CG  . GLU B 2 122 ? -12.369 4.178   24.921 1.00 32.27 ? 121 GLU B CG  1 
ATOM   1705 C  CD  . GLU B 2 122 ? -11.708 4.366   26.283 1.00 37.77 ? 121 GLU B CD  1 
ATOM   1706 O  OE1 . GLU B 2 122 ? -10.597 3.825   26.495 1.00 39.63 ? 121 GLU B OE1 1 
ATOM   1707 O  OE2 . GLU B 2 122 ? -12.294 5.057   27.142 1.00 40.93 ? 121 GLU B OE2 1 
ATOM   1708 N  N   . LYS B 2 123 ? -10.840 5.098   21.770 1.00 26.02 ? 122 LYS B N   1 
ATOM   1709 C  CA  . LYS B 2 123 ? -10.725 6.480   21.313 1.00 29.11 ? 122 LYS B CA  1 
ATOM   1710 C  C   . LYS B 2 123 ? -10.131 6.562   19.911 1.00 27.19 ? 122 LYS B C   1 
ATOM   1711 O  O   . LYS B 2 123 ? -9.658  5.564   19.366 1.00 24.63 ? 122 LYS B O   1 
ATOM   1712 C  CB  . LYS B 2 123 ? -9.872  7.299   22.286 1.00 33.49 ? 122 LYS B CB  1 
ATOM   1713 C  CG  . LYS B 2 123 ? -10.404 7.334   23.713 1.00 38.09 ? 122 LYS B CG  1 
ATOM   1714 C  CD  . LYS B 2 123 ? -9.548  8.236   24.593 1.00 41.59 ? 122 LYS B CD  1 
ATOM   1715 C  CE  . LYS B 2 123 ? -9.937  8.130   26.061 1.00 44.56 ? 122 LYS B CE  1 
ATOM   1716 N  NZ  . LYS B 2 123 ? -11.334 8.591   26.324 1.00 46.92 ? 122 LYS B NZ  1 
ATOM   1717 N  N   . ALA B 2 124 ? -10.156 7.761   19.337 1.00 28.38 ? 123 ALA B N   1 
ATOM   1718 C  CA  . ALA B 2 124 ? -9.622  7.988   17.998 1.00 29.57 ? 123 ALA B CA  1 
ATOM   1719 C  C   . ALA B 2 124 ? -8.103  7.900   18.008 1.00 30.39 ? 123 ALA B C   1 
ATOM   1720 O  O   . ALA B 2 124 ? -7.466  8.221   19.009 1.00 31.92 ? 123 ALA B O   1 
ATOM   1721 C  CB  . ALA B 2 124 ? -10.063 9.344   17.479 1.00 32.32 ? 123 ALA B CB  1 
ATOM   1722 N  N   . ASP B 2 125 ? -7.522  7.472   16.893 1.00 31.86 ? 124 ASP B N   1 
ATOM   1723 C  CA  . ASP B 2 125 ? -6.068  7.380   16.797 1.00 47.74 ? 124 ASP B CA  1 
ATOM   1724 C  C   . ASP B 2 125 ? -5.519  8.389   15.797 1.00 67.57 ? 124 ASP B C   1 
ATOM   1725 O  O   . ASP B 2 125 ? -5.552  9.595   16.046 1.00 76.34 ? 124 ASP B O   1 
ATOM   1726 C  CB  . ASP B 2 125 ? -5.634  5.954   16.437 1.00 42.92 ? 124 ASP B CB  1 
ATOM   1727 C  CG  . ASP B 2 125 ? -4.892  5.883   15.115 1.00 49.11 ? 124 ASP B CG  1 
ATOM   1728 O  OD1 . ASP B 2 125 ? -5.535  5.590   14.086 1.00 70.67 ? 124 ASP B OD1 1 
ATOM   1729 O  OD2 . ASP B 2 125 ? -3.665  6.116   15.106 1.00 78.80 ? 124 ASP B OD2 1 
ATOM   1730 N  N   . ASN B 2 140 ? -2.774  8.284   21.730 1.00 50.80 ? 139 ASN B N   1 
ATOM   1731 C  CA  . ASN B 2 140 ? -3.311  7.181   22.520 1.00 48.97 ? 139 ASN B CA  1 
ATOM   1732 C  C   . ASN B 2 140 ? -4.770  6.876   22.203 1.00 44.55 ? 139 ASN B C   1 
ATOM   1733 O  O   . ASN B 2 140 ? -5.659  7.674   22.508 1.00 45.84 ? 139 ASN B O   1 
ATOM   1734 C  CB  . ASN B 2 140 ? -3.176  7.477   24.011 1.00 52.10 ? 139 ASN B CB  1 
ATOM   1735 C  CG  . ASN B 2 140 ? -3.892  6.455   24.865 1.00 53.42 ? 139 ASN B CG  1 
ATOM   1736 O  OD1 . ASN B 2 140 ? -3.793  5.255   24.621 1.00 50.70 ? 139 ASN B OD1 1 
ATOM   1737 N  ND2 . ASN B 2 140 ? -4.635  6.926   25.862 1.00 55.93 ? 139 ASN B ND2 1 
ATOM   1738 N  N   . ALA B 2 141 ? -5.015  5.709   21.611 1.00 38.11 ? 140 ALA B N   1 
ATOM   1739 C  CA  . ALA B 2 141 ? -6.371  5.308   21.249 1.00 31.48 ? 140 ALA B CA  1 
ATOM   1740 C  C   . ALA B 2 141 ? -7.105  4.611   22.397 1.00 28.61 ? 140 ALA B C   1 
ATOM   1741 O  O   . ALA B 2 141 ? -8.226  4.142   22.231 1.00 27.74 ? 140 ALA B O   1 
ATOM   1742 C  CB  . ALA B 2 141 ? -6.355  4.429   19.999 1.00 31.41 ? 140 ALA B CB  1 
ATOM   1743 N  N   . GLY B 2 142 ? -6.476  4.554   23.566 1.00 30.07 ? 141 GLY B N   1 
ATOM   1744 C  CA  . GLY B 2 142 ? -7.122  3.983   24.737 1.00 29.41 ? 141 GLY B CA  1 
ATOM   1745 C  C   . GLY B 2 142 ? -7.356  2.482   24.670 1.00 29.32 ? 141 GLY B C   1 
ATOM   1746 O  O   . GLY B 2 142 ? -6.649  1.756   23.960 1.00 28.77 ? 141 GLY B O   1 
ATOM   1747 N  N   . SER B 2 143 ? -8.367  2.021   25.401 1.00 27.35 ? 142 SER B N   1 
ATOM   1748 C  CA  . SER B 2 143 ? -8.597  0.592   25.592 1.00 26.95 ? 142 SER B CA  1 
ATOM   1749 C  C   . SER B 2 143 ? -8.957  -0.137  24.306 1.00 23.74 ? 142 SER B C   1 
ATOM   1750 O  O   . SER B 2 143 ? -9.404  0.465   23.328 1.00 22.92 ? 142 SER B O   1 
ATOM   1751 C  CB  . SER B 2 143 ? -9.691  0.353   26.632 1.00 32.15 ? 142 SER B CB  1 
ATOM   1752 O  OG  . SER B 2 143 ? -10.973 0.438   26.039 1.00 34.87 ? 142 SER B OG  1 
ATOM   1753 N  N   . ARG B 2 144 ? -8.764  -1.449  24.325 1.00 20.54 ? 143 ARG B N   1 
ATOM   1754 C  CA  . ARG B 2 144 ? -9.090  -2.287  23.181 1.00 20.04 ? 143 ARG B CA  1 
ATOM   1755 C  C   . ARG B 2 144 ? -10.471 -2.883  23.371 1.00 19.60 ? 143 ARG B C   1 
ATOM   1756 O  O   . ARG B 2 144 ? -10.669 -3.767  24.209 1.00 24.10 ? 143 ARG B O   1 
ATOM   1757 C  CB  . ARG B 2 144 ? -8.042  -3.375  23.026 1.00 20.06 ? 143 ARG B CB  1 
ATOM   1758 C  CG  . ARG B 2 144 ? -6.651  -2.799  22.898 1.00 18.69 ? 143 ARG B CG  1 
ATOM   1759 C  CD  . ARG B 2 144 ? -5.569  -3.860  22.963 1.00 20.23 ? 143 ARG B CD  1 
ATOM   1760 N  NE  . ARG B 2 144 ? -4.253  -3.234  22.939 1.00 21.33 ? 143 ARG B NE  1 
ATOM   1761 C  CZ  . ARG B 2 144 ? -3.104  -3.892  23.004 1.00 21.55 ? 143 ARG B CZ  1 
ATOM   1762 N  NH1 . ARG B 2 144 ? -3.094  -5.215  23.088 1.00 22.46 ? 143 ARG B NH1 1 
ATOM   1763 N  NH2 . ARG B 2 144 ? -1.962  -3.223  22.977 1.00 22.17 ? 143 ARG B NH2 1 
ATOM   1764 N  N   . LEU B 2 145 ? -11.430 -2.382  22.603 1.00 16.10 ? 144 LEU B N   1 
ATOM   1765 C  CA  . LEU B 2 145 ? -12.831 -2.754  22.791 1.00 15.96 ? 144 LEU B CA  1 
ATOM   1766 C  C   . LEU B 2 145 ? -13.144 -4.139  22.230 1.00 16.85 ? 144 LEU B C   1 
ATOM   1767 O  O   . LEU B 2 145 ? -13.941 -4.882  22.795 1.00 17.79 ? 144 LEU B O   1 
ATOM   1768 C  CB  . LEU B 2 145 ? -13.749 -1.715  22.141 1.00 18.25 ? 144 LEU B CB  1 
ATOM   1769 C  CG  . LEU B 2 145 ? -13.646 -0.275  22.641 1.00 24.26 ? 144 LEU B CG  1 
ATOM   1770 C  CD1 . LEU B 2 145 ? -14.592 0.617   21.847 1.00 27.27 ? 144 LEU B CD1 1 
ATOM   1771 C  CD2 . LEU B 2 145 ? -13.960 -0.205  24.124 1.00 26.55 ? 144 LEU B CD2 1 
ATOM   1772 N  N   . ALA B 2 146 ? -12.527 -4.476  21.107 1.00 16.06 ? 145 ALA B N   1 
ATOM   1773 C  CA  . ALA B 2 146 ? -12.766 -5.770  20.482 1.00 13.83 ? 145 ALA B CA  1 
ATOM   1774 C  C   . ALA B 2 146 ? -11.598 -6.130  19.592 1.00 13.57 ? 145 ALA B C   1 
ATOM   1775 O  O   . ALA B 2 146 ? -10.874 -5.257  19.119 1.00 14.36 ? 145 ALA B O   1 
ATOM   1776 C  CB  . ALA B 2 146 ? -14.069 -5.755  19.676 1.00 15.03 ? 145 ALA B CB  1 
ATOM   1777 N  N   . CYS B 2 147 ? -11.413 -7.422  19.368 1.00 13.46 ? 146 CYS B N   1 
ATOM   1778 C  CA  . CYS B 2 147 ? -10.325 -7.880  18.520 1.00 14.36 ? 146 CYS B CA  1 
ATOM   1779 C  C   . CYS B 2 147 ? -10.597 -9.270  17.973 1.00 13.10 ? 146 CYS B C   1 
ATOM   1780 O  O   . CYS B 2 147 ? -11.512 -9.973  18.420 1.00 13.88 ? 146 CYS B O   1 
ATOM   1781 C  CB  . CYS B 2 147 ? -9.018  -7.897  19.310 1.00 17.00 ? 146 CYS B CB  1 
ATOM   1782 S  SG  . CYS B 2 147 ? -9.007  -9.119  20.629 1.00 21.79 ? 146 CYS B SG  1 
ATOM   1783 N  N   . GLY B 2 148 ? -9.779  -9.675  17.017 1.00 11.40 ? 147 GLY B N   1 
ATOM   1784 C  CA  . GLY B 2 148 ? -9.889  -11.008 16.462 1.00 11.75 ? 147 GLY B CA  1 
ATOM   1785 C  C   . GLY B 2 148 ? -8.640  -11.325 15.681 1.00 12.21 ? 147 GLY B C   1 
ATOM   1786 O  O   . GLY B 2 148 ? -7.917  -10.422 15.244 1.00 11.79 ? 147 GLY B O   1 
ATOM   1787 N  N   . VAL B 2 149 ? -8.374  -12.614 15.519 1.00 10.62 ? 148 VAL B N   1 
ATOM   1788 C  CA  . VAL B 2 149 ? -7.234  -13.044 14.734 1.00 11.52 ? 148 VAL B CA  1 
ATOM   1789 C  C   . VAL B 2 149 ? -7.613  -13.006 13.258 1.00 10.05 ? 148 VAL B C   1 
ATOM   1790 O  O   . VAL B 2 149 ? -8.716  -13.413 12.872 1.00 12.83 ? 148 VAL B O   1 
ATOM   1791 C  CB  . VAL B 2 149 ? -6.775  -14.453 15.149 1.00 11.91 ? 148 VAL B CB  1 
ATOM   1792 C  CG1 . VAL B 2 149 ? -5.545  -14.867 14.357 1.00 12.53 ? 148 VAL B CG1 1 
ATOM   1793 C  CG2 . VAL B 2 149 ? -6.476  -14.476 16.644 1.00 14.25 ? 148 VAL B CG2 1 
ATOM   1794 N  N   . ILE B 2 150 ? -6.705  -12.502 12.431 1.00 9.90  ? 149 ILE B N   1 
ATOM   1795 C  CA  . ILE B 2 150 ? -6.955  -12.390 10.997 1.00 9.55  ? 149 ILE B CA  1 
ATOM   1796 C  C   . ILE B 2 150 ? -6.681  -13.744 10.330 1.00 9.74  ? 149 ILE B C   1 
ATOM   1797 O  O   . ILE B 2 150 ? -5.550  -14.233 10.329 1.00 12.29 ? 149 ILE B O   1 
ATOM   1798 C  CB  . ILE B 2 150 ? -6.074  -11.283 10.379 1.00 10.99 ? 149 ILE B CB  1 
ATOM   1799 C  CG1 . ILE B 2 150 ? -6.405  -9.937  11.044 1.00 12.41 ? 149 ILE B CG1 1 
ATOM   1800 C  CG2 . ILE B 2 150 ? -6.268  -11.226 8.868  1.00 12.24 ? 149 ILE B CG2 1 
ATOM   1801 C  CD1 . ILE B 2 150 ? -5.376  -8.849  10.796 1.00 13.56 ? 149 ILE B CD1 1 
ATOM   1802 N  N   . GLY B 2 151 ? -7.718  -14.351 9.770  1.00 9.00  ? 150 GLY B N   1 
ATOM   1803 C  CA  . GLY B 2 151 ? -7.609  -15.693 9.227  1.00 10.33 ? 150 GLY B CA  1 
ATOM   1804 C  C   . GLY B 2 151 ? -7.713  -15.748 7.713  1.00 11.18 ? 150 GLY B C   1 
ATOM   1805 O  O   . GLY B 2 151 ? -8.236  -14.833 7.084  1.00 12.72 ? 150 GLY B O   1 
ATOM   1806 N  N   . ILE B 2 152 ? -7.204  -16.827 7.126  1.00 10.37 ? 151 ILE B N   1 
ATOM   1807 C  CA  . ILE B 2 152 ? -7.309  -17.038 5.685  1.00 9.89  ? 151 ILE B CA  1 
ATOM   1808 C  C   . ILE B 2 152 ? -8.754  -17.348 5.286  1.00 10.86 ? 151 ILE B C   1 
ATOM   1809 O  O   . ILE B 2 152 ? -9.392  -18.225 5.882  1.00 13.04 ? 151 ILE B O   1 
ATOM   1810 C  CB  . ILE B 2 152 ? -6.394  -18.197 5.243  1.00 12.48 ? 151 ILE B CB  1 
ATOM   1811 C  CG1 . ILE B 2 152 ? -4.931  -17.818 5.487  1.00 15.46 ? 151 ILE B CG1 1 
ATOM   1812 C  CG2 . ILE B 2 152 ? -6.653  -18.562 3.785  1.00 15.97 ? 151 ILE B CG2 1 
ATOM   1813 C  CD1 . ILE B 2 152 ? -3.946  -18.957 5.328  1.00 18.59 ? 151 ILE B CD1 1 
ATOM   1814 N  N   . ALA B 2 153 ? -9.268  -16.634 4.280  1.00 12.24 ? 152 ALA B N   1 
ATOM   1815 C  CA  . ALA B 2 153 ? -10.663 -16.798 3.855  1.00 13.68 ? 152 ALA B CA  1 
ATOM   1816 C  C   . ALA B 2 153 ? -10.789 -17.424 2.476  1.00 18.39 ? 152 ALA B C   1 
ATOM   1817 O  O   . ALA B 2 153 ? -11.865 -17.910 2.114  1.00 19.49 ? 152 ALA B O   1 
ATOM   1818 C  CB  . ALA B 2 153 ? -11.395 -15.463 3.875  1.00 15.40 ? 152 ALA B CB  1 
ATOM   1819 N  N   . GLN B 2 154 ? -9.693  -17.368 1.718  1.00 22.36 ? 153 GLN B N   1 
ATOM   1820 C  CA  . GLN B 2 154 ? -9.582  -17.914 0.367  1.00 31.77 ? 153 GLN B CA  1 
ATOM   1821 C  C   . GLN B 2 154 ? -8.129  -17.768 -0.083 1.00 34.31 ? 153 GLN B C   1 
ATOM   1822 O  O   . GLN B 2 154 ? -7.617  -18.587 -0.842 1.00 38.19 ? 153 GLN B O   1 
ATOM   1823 C  CB  . GLN B 2 154 ? -10.498 -17.180 -0.615 1.00 37.59 ? 153 GLN B CB  1 
ATOM   1824 C  CG  . GLN B 2 154 ? -10.379 -17.676 -2.053 1.00 42.45 ? 153 GLN B CG  1 
ATOM   1825 C  CD  . GLN B 2 154 ? -11.074 -16.767 -3.051 1.00 45.81 ? 153 GLN B CD  1 
ATOM   1826 O  OE1 . GLN B 2 154 ? -11.730 -15.795 -2.674 1.00 47.05 ? 153 GLN B OE1 1 
ATOM   1827 N  NE2 . GLN B 2 154 ? -10.927 -17.077 -4.334 1.00 47.10 ? 153 GLN B NE2 1 
ATOM   1828 O  OXT . GLN B 2 154 ? -7.427  -16.821 0.305  1.00 29.33 ? 153 GLN B OXT 1 
HETATM 1829 ZN ZN  . ZN  C 3 .   ? -11.863 -32.052 11.259 0.36 28.43 ? 154 ZN  A ZN  1 
HETATM 1830 S  S   . SO4 D 4 .   ? -15.534 -32.583 9.681  0.71 45.27 ? 155 SO4 A S   1 
HETATM 1831 O  O1  . SO4 D 4 .   ? -14.255 -32.979 10.261 0.71 47.16 ? 155 SO4 A O1  1 
HETATM 1832 O  O2  . SO4 D 4 .   ? -15.293 -31.857 8.439  0.71 45.36 ? 155 SO4 A O2  1 
HETATM 1833 O  O3  . SO4 D 4 .   ? -16.316 -33.783 9.399  0.71 44.69 ? 155 SO4 A O3  1 
HETATM 1834 O  O4  . SO4 D 4 .   ? -16.271 -31.734 10.613 0.71 43.76 ? 155 SO4 A O4  1 
HETATM 1835 ZN ZN  . ZN  E 3 .   ? -3.834  -0.228  18.543 0.53 21.76 ? 154 ZN  B ZN  1 
HETATM 1836 S  S   . SO4 F 4 .   ? -2.159  1.356   20.659 0.72 44.10 ? 155 SO4 B S   1 
HETATM 1837 O  O1  . SO4 F 4 .   ? -2.113  0.873   19.285 0.72 38.87 ? 155 SO4 B O1  1 
HETATM 1838 O  O2  . SO4 F 4 .   ? -3.089  2.479   20.740 0.72 42.14 ? 155 SO4 B O2  1 
HETATM 1839 O  O3  . SO4 F 4 .   ? -2.598  0.276   21.544 0.72 45.72 ? 155 SO4 B O3  1 
HETATM 1840 O  O4  . SO4 F 4 .   ? -0.828  1.790   21.065 0.72 43.26 ? 155 SO4 B O4  1 
HETATM 1841 O  O   . HOH G 5 .   ? -8.199  -33.732 0.777  1.00 53.94 ? 156 HOH A O   1 
HETATM 1842 O  O   . HOH G 5 .   ? -6.984  -18.175 18.496 1.00 12.90 ? 157 HOH A O   1 
HETATM 1843 O  O   . HOH G 5 .   ? -12.316 -15.482 11.301 1.00 14.58 ? 158 HOH A O   1 
HETATM 1844 O  O   . HOH G 5 .   ? -12.881 -30.377 31.923 1.00 17.47 ? 159 HOH A O   1 
HETATM 1845 O  O   . HOH G 5 .   ? -16.738 -34.039 24.068 1.00 20.57 ? 160 HOH A O   1 
HETATM 1846 O  O   . HOH G 5 .   ? -14.425 -15.421 17.310 1.00 49.78 ? 161 HOH A O   1 
HETATM 1847 O  O   . HOH G 5 .   ? 4.754   -21.291 21.205 1.00 42.73 ? 162 HOH A O   1 
HETATM 1848 O  O   . HOH G 5 .   ? -18.105 -35.911 22.504 1.00 40.44 ? 163 HOH A O   1 
HETATM 1849 O  O   . HOH G 5 .   ? -2.155  -36.779 20.276 1.00 48.33 ? 164 HOH A O   1 
HETATM 1850 O  O   . HOH G 5 .   ? -14.030 -18.047 4.075  1.00 25.40 ? 165 HOH A O   1 
HETATM 1851 O  O   . HOH G 5 .   ? -6.893  -33.183 34.885 1.00 25.22 ? 166 HOH A O   1 
HETATM 1852 O  O   . HOH G 5 .   ? -17.728 -31.845 25.317 1.00 19.63 ? 167 HOH A O   1 
HETATM 1853 O  O   . HOH G 5 .   ? 4.910   -36.615 12.048 1.00 55.71 ? 168 HOH A O   1 
HETATM 1854 O  O   . HOH G 5 .   ? 11.825  -21.275 17.603 1.00 43.55 ? 169 HOH A O   1 
HETATM 1855 O  O   . HOH G 5 .   ? -16.790 -38.001 30.323 1.00 27.75 ? 170 HOH A O   1 
HETATM 1856 O  O   . HOH G 5 .   ? -16.855 -15.174 5.599  1.00 28.03 ? 171 HOH A O   1 
HETATM 1857 O  O   . HOH G 5 .   ? -9.882  -17.422 17.020 1.00 23.54 ? 172 HOH A O   1 
HETATM 1858 O  O   . HOH G 5 .   ? -12.132 -25.900 -0.116 1.00 51.48 ? 173 HOH A O   1 
HETATM 1859 O  O   . HOH G 5 .   ? 2.384   -36.989 15.574 1.00 57.14 ? 174 HOH A O   1 
HETATM 1860 O  O   . HOH G 5 .   ? -15.510 -39.594 24.259 1.00 39.00 ? 175 HOH A O   1 
HETATM 1861 O  O   . HOH G 5 .   ? -16.791 -40.734 27.490 1.00 46.57 ? 176 HOH A O   1 
HETATM 1862 O  O   . HOH G 5 .   ? -18.107 -26.785 23.298 1.00 24.65 ? 177 HOH A O   1 
HETATM 1863 O  O   . HOH G 5 .   ? -16.378 -23.128 24.654 1.00 27.00 ? 178 HOH A O   1 
HETATM 1864 O  O   . HOH G 5 .   ? 12.310  -22.496 4.131  1.00 23.78 ? 179 HOH A O   1 
HETATM 1865 O  O   . HOH G 5 .   ? -4.423  -39.516 21.967 1.00 53.29 ? 180 HOH A O   1 
HETATM 1866 O  O   . HOH G 5 .   ? -11.117 -18.587 19.566 1.00 33.57 ? 181 HOH A O   1 
HETATM 1867 O  O   . HOH G 5 .   ? -9.791  -43.460 26.906 1.00 56.39 ? 182 HOH A O   1 
HETATM 1868 O  O   . HOH G 5 .   ? 5.718   -26.089 4.356  1.00 33.56 ? 183 HOH A O   1 
HETATM 1869 O  O   . HOH G 5 .   ? 13.846  -28.971 14.825 1.00 49.61 ? 184 HOH A O   1 
HETATM 1870 O  O   . HOH G 5 .   ? -3.873  -36.367 24.202 1.00 27.33 ? 185 HOH A O   1 
HETATM 1871 O  O   . HOH G 5 .   ? 0.437   -35.741 14.212 1.00 48.30 ? 186 HOH A O   1 
HETATM 1872 O  O   . HOH G 5 .   ? -0.324  -34.266 9.889  1.00 31.39 ? 187 HOH A O   1 
HETATM 1873 O  O   . HOH G 5 .   ? 1.134   -30.408 27.007 1.00 30.21 ? 188 HOH A O   1 
HETATM 1874 O  O   . HOH G 5 .   ? 11.736  -27.543 13.872 1.00 29.10 ? 189 HOH A O   1 
HETATM 1875 O  O   . HOH G 5 .   ? -8.622  -40.458 33.734 1.00 29.56 ? 190 HOH A O   1 
HETATM 1876 O  O   . HOH G 5 .   ? -15.464 -41.695 19.198 1.00 39.24 ? 191 HOH A O   1 
HETATM 1877 O  O   . HOH G 5 .   ? -13.739 -21.262 12.310 1.00 42.03 ? 192 HOH A O   1 
HETATM 1878 O  O   . HOH G 5 .   ? -1.708  -30.097 29.489 1.00 39.69 ? 193 HOH A O   1 
HETATM 1879 O  O   . HOH G 5 .   ? -15.778 -35.668 30.733 1.00 35.83 ? 194 HOH A O   1 
HETATM 1880 O  O   . HOH G 5 .   ? -15.095 -32.260 34.169 1.00 30.74 ? 195 HOH A O   1 
HETATM 1881 O  O   . HOH G 5 .   ? 2.577   -20.159 21.875 1.00 29.16 ? 196 HOH A O   1 
HETATM 1882 O  O   . HOH G 5 .   ? 11.301  -22.032 11.864 1.00 36.47 ? 197 HOH A O   1 
HETATM 1883 O  O   . HOH G 5 .   ? -19.459 -25.978 19.796 1.00 38.48 ? 198 HOH A O   1 
HETATM 1884 O  O   . HOH G 5 .   ? -1.474  -35.452 22.679 1.00 39.23 ? 199 HOH A O   1 
HETATM 1885 O  O   . HOH G 5 .   ? -6.626  -27.510 1.893  1.00 37.63 ? 200 HOH A O   1 
HETATM 1886 O  O   . HOH G 5 .   ? -11.372 -20.511 25.300 1.00 35.80 ? 201 HOH A O   1 
HETATM 1887 O  O   . HOH G 5 .   ? -6.014  -22.393 1.253  1.00 41.28 ? 202 HOH A O   1 
HETATM 1888 O  O   . HOH G 5 .   ? -4.393  -36.403 27.785 1.00 32.05 ? 203 HOH A O   1 
HETATM 1889 O  O   . HOH G 5 .   ? -20.183 -29.151 13.810 1.00 36.40 ? 204 HOH A O   1 
HETATM 1890 O  O   . HOH G 5 .   ? 13.065  -18.905 16.757 1.00 45.23 ? 205 HOH A O   1 
HETATM 1891 O  O   . HOH G 5 .   ? -12.565 -32.490 5.021  1.00 44.46 ? 206 HOH A O   1 
HETATM 1892 O  O   . HOH G 5 .   ? -12.684 -43.098 23.092 1.00 36.77 ? 207 HOH A O   1 
HETATM 1893 O  O   . HOH G 5 .   ? -16.429 -28.445 5.593  1.00 40.05 ? 209 HOH A O   1 
HETATM 1894 O  O   . HOH G 5 .   ? -5.612  -42.634 18.534 1.00 47.16 ? 210 HOH A O   1 
HETATM 1895 O  O   . HOH G 5 .   ? -5.686  -36.574 29.833 1.00 29.35 ? 211 HOH A O   1 
HETATM 1896 O  O   . HOH G 5 .   ? -9.675  -31.587 2.381  1.00 42.24 ? 212 HOH A O   1 
HETATM 1897 O  O   . HOH G 5 .   ? -20.354 -28.544 23.024 1.00 40.24 ? 213 HOH A O   1 
HETATM 1898 O  O   . HOH G 5 .   ? 7.448   -29.440 9.083  1.00 37.09 ? 214 HOH A O   1 
HETATM 1899 O  O   . HOH G 5 .   ? -9.294  -42.112 31.689 1.00 45.68 ? 215 HOH A O   1 
HETATM 1900 O  O   . HOH G 5 .   ? -13.604 -19.596 18.229 1.00 44.73 ? 216 HOH A O   1 
HETATM 1901 O  O   . HOH G 5 .   ? -9.112  -41.460 28.913 1.00 46.27 ? 217 HOH A O   1 
HETATM 1902 O  O   . HOH G 5 .   ? 10.265  -27.573 16.871 1.00 39.60 ? 218 HOH A O   1 
HETATM 1903 O  O   . HOH G 5 .   ? -5.820  -24.744 28.160 1.00 33.92 ? 219 HOH A O   1 
HETATM 1904 O  O   . HOH G 5 .   ? -0.368  -22.673 3.685  1.00 38.27 ? 220 HOH A O   1 
HETATM 1905 O  O   . HOH G 5 .   ? -1.443  -37.196 17.572 1.00 43.42 ? 221 HOH A O   1 
HETATM 1906 O  O   . HOH G 5 .   ? -15.445 -29.289 32.030 1.00 42.20 ? 222 HOH A O   1 
HETATM 1907 O  O   . HOH G 5 .   ? -15.120 -26.369 30.633 1.00 46.15 ? 223 HOH A O   1 
HETATM 1908 O  O   . HOH G 5 .   ? -19.610 -28.327 10.808 1.00 57.51 ? 224 HOH A O   1 
HETATM 1909 O  O   . HOH G 5 .   ? -12.317 -15.747 15.539 1.00 44.57 ? 225 HOH A O   1 
HETATM 1910 O  O   . HOH G 5 .   ? -4.009  -24.315 0.386  1.00 51.22 ? 226 HOH A O   1 
HETATM 1911 O  O   . HOH G 5 .   ? -19.123 -23.179 16.611 1.00 45.12 ? 227 HOH A O   1 
HETATM 1912 O  O   . HOH G 5 .   ? -18.542 -15.663 15.158 1.00 48.72 ? 228 HOH A O   1 
HETATM 1913 O  O   . HOH G 5 .   ? -2.090  -24.510 27.218 1.00 39.41 ? 229 HOH A O   1 
HETATM 1914 O  O   . HOH G 5 .   ? -13.401 -43.819 20.519 1.00 45.98 ? 230 HOH A O   1 
HETATM 1915 O  O   . HOH G 5 .   ? 3.714   -36.940 18.225 1.00 45.95 ? 231 HOH A O   1 
HETATM 1916 O  O   . HOH G 5 .   ? -7.406  -41.702 36.110 1.00 44.30 ? 232 HOH A O   1 
HETATM 1917 O  O   . HOH G 5 .   ? -3.178  -39.838 17.549 1.00 43.24 ? 233 HOH A O   1 
HETATM 1918 O  O   . HOH G 5 .   ? -0.635  -24.373 0.804  1.00 44.36 ? 234 HOH A O   1 
HETATM 1919 O  O   . HOH G 5 .   ? -19.788 -26.420 15.234 1.00 57.27 ? 235 HOH A O   1 
HETATM 1920 O  O   . HOH G 5 .   ? -0.063  -19.424 25.489 1.00 37.80 ? 236 HOH A O   1 
HETATM 1921 O  O   . HOH G 5 .   ? -14.799 -40.393 21.818 1.00 54.26 ? 237 HOH A O   1 
HETATM 1922 O  O   . HOH G 5 .   ? -9.231  -20.803 26.765 1.00 40.40 ? 238 HOH A O   1 
HETATM 1923 O  O   . HOH H 5 .   ? -11.283 -13.997 13.468 1.00 12.34 ? 156 HOH B O   1 
HETATM 1924 O  O   . HOH H 5 .   ? -14.528 7.439   22.958 1.00 50.32 ? 157 HOH B O   1 
HETATM 1925 O  O   . HOH H 5 .   ? -10.252 -14.722 16.510 1.00 24.63 ? 158 HOH B O   1 
HETATM 1926 O  O   . HOH H 5 .   ? 0.378   -4.411  -0.094 1.00 29.31 ? 159 HOH B O   1 
HETATM 1927 O  O   . HOH H 5 .   ? -9.443  -13.709 19.104 1.00 39.37 ? 160 HOH B O   1 
HETATM 1928 O  O   . HOH H 5 .   ? -4.932  -16.746 19.708 1.00 15.09 ? 161 HOH B O   1 
HETATM 1929 O  O   . HOH H 5 .   ? -0.590  -11.962 -7.845 1.00 19.02 ? 162 HOH B O   1 
HETATM 1930 O  O   . HOH H 5 .   ? -4.241  -6.364  -4.727 1.00 18.70 ? 163 HOH B O   1 
HETATM 1931 O  O   . HOH H 5 .   ? -24.534 -0.462  17.859 1.00 23.37 ? 164 HOH B O   1 
HETATM 1932 O  O   . HOH H 5 .   ? -14.784 -14.469 3.197  1.00 42.61 ? 165 HOH B O   1 
HETATM 1933 O  O   . HOH H 5 .   ? -23.529 4.452   20.332 1.00 48.87 ? 166 HOH B O   1 
HETATM 1934 O  O   . HOH H 5 .   ? -19.764 -10.251 21.582 1.00 51.99 ? 167 HOH B O   1 
HETATM 1935 O  O   . HOH H 5 .   ? -1.121  1.113   7.180  1.00 27.72 ? 168 HOH B O   1 
HETATM 1936 O  O   . HOH H 5 .   ? -18.486 0.468   22.991 1.00 23.52 ? 169 HOH B O   1 
HETATM 1937 O  O   . HOH H 5 .   ? -8.239  -18.018 26.968 1.00 43.45 ? 170 HOH B O   1 
HETATM 1938 O  O   . HOH H 5 .   ? -10.260 -0.338  -3.956 1.00 49.36 ? 171 HOH B O   1 
HETATM 1939 O  O   . HOH H 5 .   ? -20.045 -4.568  4.758  1.00 59.70 ? 172 HOH B O   1 
HETATM 1940 O  O   . HOH H 5 .   ? -13.419 -12.208 3.717  1.00 23.11 ? 173 HOH B O   1 
HETATM 1941 O  O   . HOH H 5 .   ? 5.505   -5.123  15.249 1.00 21.90 ? 174 HOH B O   1 
HETATM 1942 O  O   . HOH H 5 .   ? 4.573   -7.361  2.690  1.00 30.42 ? 175 HOH B O   1 
HETATM 1943 O  O   . HOH H 5 .   ? 0.902   -10.019 -1.398 1.00 26.27 ? 176 HOH B O   1 
HETATM 1944 O  O   . HOH H 5 .   ? 9.348   -0.321  17.009 1.00 46.58 ? 177 HOH B O   1 
HETATM 1945 O  O   . HOH H 5 .   ? -19.575 -12.647 6.857  1.00 54.13 ? 178 HOH B O   1 
HETATM 1946 O  O   . HOH H 5 .   ? -27.057 2.337   11.673 1.00 55.66 ? 179 HOH B O   1 
HETATM 1947 O  O   . HOH H 5 .   ? 6.074   -10.549 14.812 1.00 26.61 ? 180 HOH B O   1 
HETATM 1948 O  O   . HOH H 5 .   ? 5.111   -13.575 5.669  1.00 60.47 ? 181 HOH B O   1 
HETATM 1949 O  O   . HOH H 5 .   ? -18.073 -8.241  21.860 1.00 22.19 ? 182 HOH B O   1 
HETATM 1950 O  O   . HOH H 5 .   ? -21.531 -5.981  12.777 1.00 54.55 ? 183 HOH B O   1 
HETATM 1951 O  O   . HOH H 5 .   ? -12.898 -13.372 17.514 1.00 29.05 ? 184 HOH B O   1 
HETATM 1952 O  O   . HOH H 5 .   ? 0.837   -2.242  -2.367 1.00 42.12 ? 185 HOH B O   1 
HETATM 1953 O  O   . HOH H 5 .   ? 5.258   -1.667  17.896 1.00 25.68 ? 186 HOH B O   1 
HETATM 1954 O  O   . HOH H 5 .   ? -22.258 -8.070  9.122  1.00 52.00 ? 187 HOH B O   1 
HETATM 1955 O  O   . HOH H 5 .   ? 4.629   -12.223 -1.715 1.00 54.72 ? 188 HOH B O   1 
HETATM 1956 O  O   . HOH H 5 .   ? -17.934 -0.770  25.495 1.00 31.79 ? 189 HOH B O   1 
HETATM 1957 O  O   . HOH H 5 .   ? -17.096 2.565   22.142 1.00 26.89 ? 190 HOH B O   1 
HETATM 1958 O  O   . HOH H 5 .   ? -16.636 -4.656  23.669 1.00 27.60 ? 191 HOH B O   1 
HETATM 1959 O  O   . HOH H 5 .   ? 2.066   -13.844 22.136 1.00 26.92 ? 192 HOH B O   1 
HETATM 1960 O  O   . HOH H 5 .   ? -13.652 -19.630 0.765  1.00 28.62 ? 193 HOH B O   1 
HETATM 1961 O  O   . HOH H 5 .   ? -20.000 -1.472  27.609 1.00 28.67 ? 194 HOH B O   1 
HETATM 1962 O  O   . HOH H 5 .   ? -23.538 -4.930  19.667 1.00 25.40 ? 195 HOH B O   1 
HETATM 1963 O  O   . HOH H 5 .   ? -0.201  -7.361  24.661 1.00 33.16 ? 196 HOH B O   1 
HETATM 1964 O  O   . HOH H 5 .   ? -17.331 -12.451 5.638  1.00 29.64 ? 197 HOH B O   1 
HETATM 1965 O  O   . HOH H 5 .   ? 8.757   -2.928  15.941 1.00 31.46 ? 198 HOH B O   1 
HETATM 1966 O  O   . HOH H 5 .   ? 4.476   -10.413 8.650  1.00 29.53 ? 199 HOH B O   1 
HETATM 1967 O  O   . HOH H 5 .   ? -16.392 -2.821  25.741 1.00 41.76 ? 200 HOH B O   1 
HETATM 1968 O  O   . HOH H 5 .   ? -18.406 -10.918 16.829 1.00 38.19 ? 201 HOH B O   1 
HETATM 1969 O  O   . HOH H 5 .   ? 1.424   -11.408 23.452 1.00 33.20 ? 202 HOH B O   1 
HETATM 1970 O  O   . HOH H 5 .   ? 3.541   -7.719  0.112  1.00 30.08 ? 203 HOH B O   1 
HETATM 1971 O  O   . HOH H 5 .   ? -15.618 3.980   9.240  1.00 34.09 ? 204 HOH B O   1 
HETATM 1972 O  O   . HOH H 5 .   ? -13.995 3.159   6.492  1.00 41.14 ? 205 HOH B O   1 
HETATM 1973 O  O   . HOH H 5 .   ? -23.081 6.805   21.321 1.00 44.33 ? 206 HOH B O   1 
HETATM 1974 O  O   . HOH H 5 .   ? -5.825  -10.715 21.041 1.00 30.90 ? 207 HOH B O   1 
HETATM 1975 O  O   . HOH H 5 .   ? -9.191  -16.448 19.195 1.00 31.39 ? 208 HOH B O   1 
HETATM 1976 O  O   . HOH H 5 .   ? -28.348 0.717   18.604 1.00 43.22 ? 209 HOH B O   1 
HETATM 1977 O  O   . HOH H 5 .   ? -18.911 -3.430  29.287 1.00 41.06 ? 210 HOH B O   1 
HETATM 1978 O  O   . HOH H 5 .   ? -9.023  4.228   1.832  1.00 31.86 ? 211 HOH B O   1 
HETATM 1979 O  O   . HOH H 5 .   ? -16.687 8.074   20.734 1.00 40.28 ? 212 HOH B O   1 
HETATM 1980 O  O   . HOH H 5 .   ? -11.053 -7.153  -9.990 1.00 39.52 ? 213 HOH B O   1 
HETATM 1981 O  O   . HOH H 5 .   ? 2.959   -4.797  -0.287 1.00 43.90 ? 214 HOH B O   1 
HETATM 1982 O  O   . HOH H 5 .   ? -13.378 -5.629  25.464 1.00 38.89 ? 215 HOH B O   1 
HETATM 1983 O  O   . HOH H 5 .   ? -25.151 9.408   12.747 1.00 50.02 ? 216 HOH B O   1 
HETATM 1984 O  O   . HOH H 5 .   ? -19.107 -7.446  7.683  1.00 34.60 ? 217 HOH B O   1 
HETATM 1985 O  O   . HOH H 5 .   ? -1.808  2.934   1.869  1.00 43.88 ? 218 HOH B O   1 
HETATM 1986 O  O   . HOH H 5 .   ? -10.580 -6.957  -4.682 1.00 36.38 ? 219 HOH B O   1 
HETATM 1987 O  O   . HOH H 5 .   ? -19.141 -9.958  25.115 1.00 43.54 ? 220 HOH B O   1 
HETATM 1988 O  O   . HOH H 5 .   ? -16.500 1.494   26.647 1.00 47.00 ? 221 HOH B O   1 
HETATM 1989 O  O   . HOH H 5 .   ? -8.799  7.525   9.205  1.00 39.49 ? 222 HOH B O   1 
HETATM 1990 O  O   . HOH H 5 .   ? -24.439 -10.333 19.737 1.00 40.55 ? 223 HOH B O   1 
HETATM 1991 O  O   . HOH H 5 .   ? 7.222   -8.783  12.917 1.00 42.99 ? 224 HOH B O   1 
HETATM 1992 O  O   . HOH H 5 .   ? -6.949  -11.897 19.024 1.00 32.58 ? 225 HOH B O   1 
HETATM 1993 O  O   . HOH H 5 .   ? -1.614  -11.938 -1.465 1.00 38.71 ? 226 HOH B O   1 
HETATM 1994 O  O   . HOH H 5 .   ? 1.542   -0.274  20.436 1.00 39.15 ? 227 HOH B O   1 
HETATM 1995 O  O   . HOH H 5 .   ? -1.814  -13.607 -5.766 1.00 40.39 ? 228 HOH B O   1 
HETATM 1996 O  O   . HOH H 5 .   ? 1.573   -14.340 8.451  1.00 46.09 ? 229 HOH B O   1 
HETATM 1997 O  O   . HOH H 5 .   ? -14.139 -11.071 -4.966 1.00 53.83 ? 230 HOH B O   1 
HETATM 1998 O  O   . HOH H 5 .   ? -0.343  -15.667 2.612  1.00 40.82 ? 231 HOH B O   1 
HETATM 1999 O  O   . HOH H 5 .   ? 6.837   -12.574 12.916 1.00 51.63 ? 232 HOH B O   1 
HETATM 2000 O  O   . HOH H 5 .   ? -14.904 11.295  17.727 1.00 39.27 ? 233 HOH B O   1 
HETATM 2001 O  O   . HOH H 5 .   ? -0.594  1.350   24.197 1.00 37.16 ? 234 HOH B O   1 
HETATM 2002 O  O   . HOH H 5 .   ? -5.381  2.812   5.427  1.00 44.62 ? 235 HOH B O   1 
HETATM 2003 O  O   . HOH H 5 .   ? -3.581  -15.269 -7.097 1.00 50.75 ? 236 HOH B O   1 
HETATM 2004 O  O   . HOH H 5 .   ? 2.143   -8.602  25.074 1.00 42.01 ? 237 HOH B O   1 
HETATM 2005 O  O   . HOH H 5 .   ? -9.747  -15.995 25.374 1.00 49.84 ? 238 HOH B O   1 
HETATM 2006 O  O   . HOH H 5 .   ? 11.554  -6.720  12.724 1.00 42.92 ? 239 HOH B O   1 
HETATM 2007 O  O   . HOH H 5 .   ? -18.979 -9.398  5.787  1.00 44.81 ? 240 HOH B O   1 
HETATM 2008 O  O   . HOH H 5 .   ? -3.916  -0.774  24.719 1.00 41.71 ? 241 HOH B O   1 
HETATM 2009 O  O   . HOH H 5 .   ? 3.854   -3.233  1.684  1.00 53.61 ? 242 HOH B O   1 
HETATM 2010 O  O   . HOH H 5 .   ? -9.055  4.656   7.559  1.00 52.82 ? 243 HOH B O   1 
HETATM 2011 O  O   . HOH H 5 .   ? 8.913   -2.652  7.121  1.00 50.92 ? 244 HOH B O   1 
HETATM 2012 O  O   . HOH H 5 .   ? -11.070 -16.571 21.243 1.00 46.36 ? 245 HOH B O   1 
HETATM 2013 O  O   . HOH H 5 .   ? -20.129 -11.329 19.001 1.00 45.77 ? 246 HOH B O   1 
HETATM 2014 O  O   . HOH H 5 .   ? -10.511 -8.523  25.719 1.00 43.07 ? 247 HOH B O   1 
HETATM 2015 O  O   . HOH H 5 .   ? -19.950 9.583   21.486 1.00 44.59 ? 248 HOH B O   1 
HETATM 2016 O  O   . HOH H 5 .   ? -19.529 -10.887 14.520 1.00 45.24 ? 249 HOH B O   1 
HETATM 2017 O  O   . HOH H 5 .   ? -3.893  1.803   23.398 1.00 43.18 ? 250 HOH B O   1 
HETATM 2018 O  O   . HOH H 5 .   ? -2.761  -12.171 -9.602 1.00 44.61 ? 251 HOH B O   1 
HETATM 2019 O  O   . HOH H 5 .   ? -20.339 -7.267  10.690 1.00 40.95 ? 252 HOH B O   1 
HETATM 2020 O  O   . HOH H 5 .   ? -9.739  9.931   10.959 1.00 53.97 ? 253 HOH B O   1 
HETATM 2021 O  O   . HOH H 5 .   ? -18.674 -1.598  3.903  1.00 44.52 ? 254 HOH B O   1 
HETATM 2022 O  O   . HOH H 5 .   ? 7.298   -9.014  9.647  1.00 54.79 ? 255 HOH B O   1 
HETATM 2023 O  O   . HOH H 5 .   ? -2.533  -11.738 -3.919 1.00 47.46 ? 256 HOH B O   1 
HETATM 2024 O  O   . HOH H 5 .   ? -18.965 -8.835  1.576  1.00 46.75 ? 257 HOH B O   1 
HETATM 2025 O  O   . HOH H 5 .   ? -15.511 4.320   23.295 1.00 35.20 ? 258 HOH B O   1 
HETATM 2026 O  O   . HOH H 5 .   ? -5.676  -13.399 -7.560 1.00 46.50 ? 259 HOH B O   1 
HETATM 2027 O  O   . HOH H 5 .   ? 7.590   -6.775  14.617 1.00 46.93 ? 260 HOH B O   1 
HETATM 2028 O  O   . HOH H 5 .   ? 7.750   -8.295  1.334  1.00 38.39 ? 261 HOH B O   1 
# 
# 
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   ACE 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   ?   ?   ?   A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  ?   ?   ?   A . n 
A 1 69  SER 69  68  ?   ?   ?   A . n 
A 1 70  ARG 70  69  ?   ?   ?   A . n 
A 1 71  LYS 71  70  ?   ?   ?   A . n 
A 1 72  HIS 72  71  ?   ?   ?   A . n 
A 1 73  GLY 73  72  ?   ?   ?   A . n 
A 1 74  GLY 74  73  ?   ?   ?   A . n 
A 1 75  PRO 75  74  ?   ?   ?   A . n 
A 1 76  LYS 76  75  ?   ?   ?   A . n 
A 1 77  ASP 77  76  ?   ?   ?   A . n 
A 1 78  GLU 78  77  ?   ?   ?   A . n 
A 1 79  GLU 79  78  ?   ?   ?   A . n 
A 1 80  ARG 80  79  ?   ?   ?   A . n 
A 1 81  ARG 81  80  80  ARG ARG A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 OCS 112 111 111 OCS OCS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 ?   ?   ?   A . n 
A 1 127 LEU 127 126 ?   ?   ?   A . n 
A 1 128 GLY 128 127 ?   ?   ?   A . n 
A 1 129 LYS 129 128 ?   ?   ?   A . n 
A 1 130 GLY 130 129 ?   ?   ?   A . n 
A 1 131 GLY 131 130 ?   ?   ?   A . n 
A 1 132 ASN 132 131 ?   ?   ?   A . n 
A 1 133 GLU 133 132 ?   ?   ?   A . n 
A 1 134 GLU 134 133 ?   ?   ?   A . n 
A 1 135 SER 135 134 ?   ?   ?   A . n 
A 1 136 THR 136 135 ?   ?   ?   A . n 
A 1 137 LYS 137 136 ?   ?   ?   A . n 
A 1 138 THR 138 137 ?   ?   ?   A . n 
A 1 139 GLY 139 138 ?   ?   ?   A . n 
A 1 140 ASN 140 139 ?   ?   ?   A . n 
A 1 141 ALA 141 140 ?   ?   ?   A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 2 1   ACE 1   0   0   ACE ACE B . n 
B 2 2   ALA 2   1   1   ALA ALA B . n 
B 2 3   THR 3   2   2   THR THR B . n 
B 2 4   LYS 4   3   3   LYS LYS B . n 
B 2 5   ALA 5   4   4   ALA ALA B . n 
B 2 6   VAL 6   5   5   VAL VAL B . n 
B 2 7   CYS 7   6   6   CYS CYS B . n 
B 2 8   VAL 8   7   7   VAL VAL B . n 
B 2 9   LEU 9   8   8   LEU LEU B . n 
B 2 10  LYS 10  9   9   LYS LYS B . n 
B 2 11  GLY 11  10  10  GLY GLY B . n 
B 2 12  ASP 12  11  11  ASP ASP B . n 
B 2 13  GLY 13  12  12  GLY GLY B . n 
B 2 14  PRO 14  13  13  PRO PRO B . n 
B 2 15  VAL 15  14  14  VAL VAL B . n 
B 2 16  GLN 16  15  15  GLN GLN B . n 
B 2 17  GLY 17  16  16  GLY GLY B . n 
B 2 18  ILE 18  17  17  ILE ILE B . n 
B 2 19  ILE 19  18  18  ILE ILE B . n 
B 2 20  ASN 20  19  19  ASN ASN B . n 
B 2 21  PHE 21  20  20  PHE PHE B . n 
B 2 22  GLU 22  21  21  GLU GLU B . n 
B 2 23  GLN 23  22  22  GLN GLN B . n 
B 2 24  LYS 24  23  23  LYS LYS B . n 
B 2 25  GLU 25  24  24  GLU GLU B . n 
B 2 26  SER 26  25  25  SER SER B . n 
B 2 27  ASN 27  26  26  ASN ASN B . n 
B 2 28  GLY 28  27  27  GLY GLY B . n 
B 2 29  PRO 29  28  28  PRO PRO B . n 
B 2 30  VAL 30  29  29  VAL VAL B . n 
B 2 31  LYS 31  30  30  LYS LYS B . n 
B 2 32  VAL 32  31  31  VAL VAL B . n 
B 2 33  TRP 33  32  32  TRP TRP B . n 
B 2 34  GLY 34  33  33  GLY GLY B . n 
B 2 35  SER 35  34  34  SER SER B . n 
B 2 36  ILE 36  35  35  ILE ILE B . n 
B 2 37  LYS 37  36  36  LYS LYS B . n 
B 2 38  GLY 38  37  37  GLY GLY B . n 
B 2 39  LEU 39  38  38  LEU LEU B . n 
B 2 40  THR 40  39  39  THR THR B . n 
B 2 41  GLU 41  40  40  GLU GLU B . n 
B 2 42  GLY 42  41  41  GLY GLY B . n 
B 2 43  LEU 43  42  42  LEU LEU B . n 
B 2 44  HIS 44  43  43  HIS HIS B . n 
B 2 45  GLY 45  44  44  GLY GLY B . n 
B 2 46  PHE 46  45  45  PHE PHE B . n 
B 2 47  HIS 47  46  46  HIS HIS B . n 
B 2 48  VAL 48  47  47  VAL VAL B . n 
B 2 49  HIS 49  48  48  HIS HIS B . n 
B 2 50  GLU 50  49  49  GLU GLU B . n 
B 2 51  PHE 51  50  50  PHE PHE B . n 
B 2 52  GLY 52  51  51  GLY GLY B . n 
B 2 53  ASP 53  52  52  ASP ASP B . n 
B 2 54  ASN 54  53  53  ASN ASN B . n 
B 2 55  THR 55  54  54  THR THR B . n 
B 2 56  ALA 56  55  55  ALA ALA B . n 
B 2 57  GLY 57  56  56  GLY GLY B . n 
B 2 58  CYS 58  57  57  CYS CYS B . n 
B 2 59  THR 59  58  58  THR THR B . n 
B 2 60  SER 60  59  59  SER SER B . n 
B 2 61  ALA 61  60  60  ALA ALA B . n 
B 2 62  GLY 62  61  61  GLY GLY B . n 
B 2 63  PRO 63  62  62  PRO PRO B . n 
B 2 64  HIS 64  63  63  HIS HIS B . n 
B 2 65  PHE 65  64  64  PHE PHE B . n 
B 2 66  ASN 66  65  65  ASN ASN B . n 
B 2 67  PRO 67  66  66  PRO PRO B . n 
B 2 68  LEU 68  67  67  LEU LEU B . n 
B 2 69  SER 69  68  68  SER SER B . n 
B 2 70  ARG 70  69  ?   ?   ?   B . n 
B 2 71  LYS 71  70  ?   ?   ?   B . n 
B 2 72  HIS 72  71  ?   ?   ?   B . n 
B 2 73  GLY 73  72  ?   ?   ?   B . n 
B 2 74  GLY 74  73  ?   ?   ?   B . n 
B 2 75  PRO 75  74  ?   ?   ?   B . n 
B 2 76  LYS 76  75  ?   ?   ?   B . n 
B 2 77  ASP 77  76  ?   ?   ?   B . n 
B 2 78  GLU 78  77  ?   ?   ?   B . n 
B 2 79  GLU 79  78  ?   ?   ?   B . n 
B 2 80  ARG 80  79  ?   ?   ?   B . n 
B 2 81  ARG 81  80  80  ARG ARG B . n 
B 2 82  VAL 82  81  81  VAL VAL B . n 
B 2 83  GLY 83  82  82  GLY GLY B . n 
B 2 84  ASP 84  83  83  ASP ASP B . n 
B 2 85  LEU 85  84  84  LEU LEU B . n 
B 2 86  GLY 86  85  85  GLY GLY B . n 
B 2 87  ASN 87  86  86  ASN ASN B . n 
B 2 88  VAL 88  87  87  VAL VAL B . n 
B 2 89  THR 89  88  88  THR THR B . n 
B 2 90  ALA 90  89  89  ALA ALA B . n 
B 2 91  ASP 91  90  90  ASP ASP B . n 
B 2 92  LYS 92  91  91  LYS LYS B . n 
B 2 93  ASP 93  92  92  ASP ASP B . n 
B 2 94  GLY 94  93  93  GLY GLY B . n 
B 2 95  VAL 95  94  94  VAL VAL B . n 
B 2 96  ALA 96  95  95  ALA ALA B . n 
B 2 97  ASP 97  96  96  ASP ASP B . n 
B 2 98  VAL 98  97  97  VAL VAL B . n 
B 2 99  SER 99  98  98  SER SER B . n 
B 2 100 ILE 100 99  99  ILE ILE B . n 
B 2 101 GLU 101 100 100 GLU GLU B . n 
B 2 102 ASP 102 101 101 ASP ASP B . n 
B 2 103 SER 103 102 102 SER SER B . n 
B 2 104 VAL 104 103 103 VAL VAL B . n 
B 2 105 ILE 105 104 104 ILE ILE B . n 
B 2 106 SER 106 105 105 SER SER B . n 
B 2 107 LEU 107 106 106 LEU LEU B . n 
B 2 108 SER 108 107 107 SER SER B . n 
B 2 109 GLY 109 108 108 GLY GLY B . n 
B 2 110 ASP 110 109 109 ASP ASP B . n 
B 2 111 HIS 111 110 110 HIS HIS B . n 
B 2 112 CSX 112 111 111 CSX CSX B . n 
B 2 113 ILE 113 112 112 ILE ILE B . n 
B 2 114 ILE 114 113 113 ILE ILE B . n 
B 2 115 GLY 115 114 114 GLY GLY B . n 
B 2 116 ARG 116 115 115 ARG ARG B . n 
B 2 117 THR 117 116 116 THR THR B . n 
B 2 118 LEU 118 117 117 LEU LEU B . n 
B 2 119 VAL 119 118 118 VAL VAL B . n 
B 2 120 VAL 120 119 119 VAL VAL B . n 
B 2 121 HIS 121 120 120 HIS HIS B . n 
B 2 122 GLU 122 121 121 GLU GLU B . n 
B 2 123 LYS 123 122 122 LYS LYS B . n 
B 2 124 ALA 124 123 123 ALA ALA B . n 
B 2 125 ASP 125 124 124 ASP ASP B . n 
B 2 126 ASP 126 125 ?   ?   ?   B . n 
B 2 127 LEU 127 126 ?   ?   ?   B . n 
B 2 128 GLY 128 127 ?   ?   ?   B . n 
B 2 129 LYS 129 128 ?   ?   ?   B . n 
B 2 130 GLY 130 129 ?   ?   ?   B . n 
B 2 131 GLY 131 130 ?   ?   ?   B . n 
B 2 132 ASN 132 131 ?   ?   ?   B . n 
B 2 133 GLU 133 132 ?   ?   ?   B . n 
B 2 134 GLU 134 133 ?   ?   ?   B . n 
B 2 135 SER 135 134 ?   ?   ?   B . n 
B 2 136 THR 136 135 ?   ?   ?   B . n 
B 2 137 LYS 137 136 ?   ?   ?   B . n 
B 2 138 THR 138 137 ?   ?   ?   B . n 
B 2 139 GLY 139 138 ?   ?   ?   B . n 
B 2 140 ASN 140 139 139 ASN ASN B . n 
B 2 141 ALA 141 140 140 ALA ALA B . n 
B 2 142 GLY 142 141 141 GLY GLY B . n 
B 2 143 SER 143 142 142 SER SER B . n 
B 2 144 ARG 144 143 143 ARG ARG B . n 
B 2 145 LEU 145 144 144 LEU LEU B . n 
B 2 146 ALA 146 145 145 ALA ALA B . n 
B 2 147 CYS 147 146 146 CYS CYS B . n 
B 2 148 GLY 148 147 147 GLY GLY B . n 
B 2 149 VAL 149 148 148 VAL VAL B . n 
B 2 150 ILE 150 149 149 ILE ILE B . n 
B 2 151 GLY 151 150 150 GLY GLY B . n 
B 2 152 ILE 152 151 151 ILE ILE B . n 
B 2 153 ALA 153 152 152 ALA ALA B . n 
B 2 154 GLN 154 153 153 GLN GLN B . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A OCS 112 A OCS 111 ? CYS 'CYSTEINESULFONIC ACID' 
2 B CSX 112 B CSX 111 ? CYS 'S-OXY CYSTEINE'        
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
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)' 2100  ? 
1 MORE         -96   ? 
1 'SSA (A^2)'  11640 ? 
# 
_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_
_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  ND1 ? A HIS 47  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 49  ? A HIS 48  ? 1_555 133.6 ? 
2  ND1 ? A HIS 47  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 96.5  ? 
3  NE2 ? A HIS 49  ? A HIS 48  ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 99.1  ? 
4  ND1 ? A HIS 47  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 64  ? A HIS 63  ? 1_555 84.6  ? 
5  NE2 ? A HIS 49  ? A HIS 48  ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 64  ? A HIS 63  ? 1_555 107.6 ? 
6  NE2 ? A HIS 121 ? A HIS 120 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 NE2 ? A HIS 64  ? A HIS 63  ? 1_555 141.8 ? 
7  ND1 ? B HIS 47  ? B HIS 46  ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 NE2 ? B HIS 49  ? B HIS 48  ? 1_555 134.0 ? 
8  ND1 ? B HIS 47  ? B HIS 46  ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 100.3 ? 
9  NE2 ? B HIS 49  ? B HIS 48  ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 105.7 ? 
10 ND1 ? B HIS 47  ? B HIS 46  ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 O1  ? F SO4 .   ? B SO4 155 ? 1_555 90.9  ? 
11 NE2 ? B HIS 49  ? B HIS 48  ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 O1  ? F SO4 .   ? B SO4 155 ? 1_555 107.5 ? 
12 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 ZN ? E ZN . ? B ZN 154 ? 1_555 O1  ? F SO4 .   ? B SO4 155 ? 1_555 119.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2011-03-09 
2 'Structure model' 1 1 2011-07-13 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MOLREP   phasing          .                          ? 1 
PHENIX   refinement       '(phenix.refine: 1.7_650)' ? 2 
HKL-2000 'data reduction' .                          ? 3 
HKL-2000 'data scaling'   .                          ? 4 
# 
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 ASN A 65 ? ? -160.51 75.46 
2 1 ASN B 65 ? ? -164.02 75.92 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ACE 0   ? A ACE 1   
2  1 Y 1 A ALA 1   ? A ALA 2   
3  1 Y 1 A LEU 67  ? A LEU 68  
4  1 Y 1 A SER 68  ? A SER 69  
5  1 Y 1 A ARG 69  ? A ARG 70  
6  1 Y 1 A LYS 70  ? A LYS 71  
7  1 Y 1 A HIS 71  ? A HIS 72  
8  1 Y 1 A GLY 72  ? A GLY 73  
9  1 Y 1 A GLY 73  ? A GLY 74  
10 1 Y 1 A PRO 74  ? A PRO 75  
11 1 Y 1 A LYS 75  ? A LYS 76  
12 1 Y 1 A ASP 76  ? A ASP 77  
13 1 Y 1 A GLU 77  ? A GLU 78  
14 1 Y 1 A GLU 78  ? A GLU 79  
15 1 Y 1 A ARG 79  ? A ARG 80  
16 1 Y 1 A ASP 125 ? A ASP 126 
17 1 Y 1 A LEU 126 ? A LEU 127 
18 1 Y 1 A GLY 127 ? A GLY 128 
19 1 Y 1 A LYS 128 ? A LYS 129 
20 1 Y 1 A GLY 129 ? A GLY 130 
21 1 Y 1 A GLY 130 ? A GLY 131 
22 1 Y 1 A ASN 131 ? A ASN 132 
23 1 Y 1 A GLU 132 ? A GLU 133 
24 1 Y 1 A GLU 133 ? A GLU 134 
25 1 Y 1 A SER 134 ? A SER 135 
26 1 Y 1 A THR 135 ? A THR 136 
27 1 Y 1 A LYS 136 ? A LYS 137 
28 1 Y 1 A THR 137 ? A THR 138 
29 1 Y 1 A GLY 138 ? A GLY 139 
30 1 Y 1 A ASN 139 ? A ASN 140 
31 1 Y 1 A ALA 140 ? A ALA 141 
32 1 Y 1 B ARG 69  ? B ARG 70  
33 1 Y 1 B LYS 70  ? B LYS 71  
34 1 Y 1 B HIS 71  ? B HIS 72  
35 1 Y 1 B GLY 72  ? B GLY 73  
36 1 Y 1 B GLY 73  ? B GLY 74  
37 1 Y 1 B PRO 74  ? B PRO 75  
38 1 Y 1 B LYS 75  ? B LYS 76  
39 1 Y 1 B ASP 76  ? B ASP 77  
40 1 Y 1 B GLU 77  ? B GLU 78  
41 1 Y 1 B GLU 78  ? B GLU 79  
42 1 Y 1 B ARG 79  ? B ARG 80  
43 1 Y 1 B ASP 125 ? B ASP 126 
44 1 Y 1 B LEU 126 ? B LEU 127 
45 1 Y 1 B GLY 127 ? B GLY 128 
46 1 Y 1 B LYS 128 ? B LYS 129 
47 1 Y 1 B GLY 129 ? B GLY 130 
48 1 Y 1 B GLY 130 ? B GLY 131 
49 1 Y 1 B ASN 131 ? B ASN 132 
50 1 Y 1 B GLU 132 ? B GLU 133 
51 1 Y 1 B GLU 133 ? B GLU 134 
52 1 Y 1 B SER 134 ? B SER 135 
53 1 Y 1 B THR 135 ? B THR 136 
54 1 Y 1 B LYS 136 ? B LYS 137 
55 1 Y 1 B THR 137 ? B THR 138 
56 1 Y 1 B GLY 138 ? B GLY 139 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'ZINC ION'    ZN  
4 'SULFATE ION' SO4 
5 water         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 ZN  1   154 154 ZN  ZN  A . 
D 4 SO4 1   155 155 SO4 SO4 A . 
E 3 ZN  1   154 154 ZN  ZN  B . 
F 4 SO4 1   155 155 SO4 SO4 B . 
G 5 HOH 1   156 156 HOH HOH A . 
G 5 HOH 2   157 157 HOH HOH A . 
G 5 HOH 3   158 158 HOH HOH A . 
G 5 HOH 4   159 159 HOH HOH A . 
G 5 HOH 5   160 160 HOH HOH A . 
G 5 HOH 6   161 161 HOH HOH A . 
G 5 HOH 7   162 162 HOH HOH A . 
G 5 HOH 8   163 163 HOH HOH A . 
G 5 HOH 9   164 164 HOH HOH A . 
G 5 HOH 10  165 165 HOH HOH A . 
G 5 HOH 11  166 166 HOH HOH A . 
G 5 HOH 12  167 167 HOH HOH A . 
G 5 HOH 13  168 168 HOH HOH A . 
G 5 HOH 14  169 169 HOH HOH A . 
G 5 HOH 15  170 170 HOH HOH A . 
G 5 HOH 16  171 171 HOH HOH A . 
G 5 HOH 17  172 172 HOH HOH A . 
G 5 HOH 18  173 173 HOH HOH A . 
G 5 HOH 19  174 174 HOH HOH A . 
G 5 HOH 20  175 175 HOH HOH A . 
G 5 HOH 21  176 176 HOH HOH A . 
G 5 HOH 22  177 177 HOH HOH A . 
G 5 HOH 23  178 178 HOH HOH A . 
G 5 HOH 24  179 179 HOH HOH A . 
G 5 HOH 25  180 180 HOH HOH A . 
G 5 HOH 26  181 181 HOH HOH A . 
G 5 HOH 27  182 182 HOH HOH A . 
G 5 HOH 28  183 183 HOH HOH A . 
G 5 HOH 29  184 184 HOH HOH A . 
G 5 HOH 30  185 185 HOH HOH A . 
G 5 HOH 31  186 186 HOH HOH A . 
G 5 HOH 32  187 187 HOH HOH A . 
G 5 HOH 33  188 188 HOH HOH A . 
G 5 HOH 34  189 189 HOH HOH A . 
G 5 HOH 35  190 190 HOH HOH A . 
G 5 HOH 36  191 191 HOH HOH A . 
G 5 HOH 37  192 192 HOH HOH A . 
G 5 HOH 38  193 193 HOH HOH A . 
G 5 HOH 39  194 194 HOH HOH A . 
G 5 HOH 40  195 195 HOH HOH A . 
G 5 HOH 41  196 196 HOH HOH A . 
G 5 HOH 42  197 197 HOH HOH A . 
G 5 HOH 43  198 198 HOH HOH A . 
G 5 HOH 44  199 199 HOH HOH A . 
G 5 HOH 45  200 200 HOH HOH A . 
G 5 HOH 46  201 201 HOH HOH A . 
G 5 HOH 47  202 202 HOH HOH A . 
G 5 HOH 48  203 203 HOH HOH A . 
G 5 HOH 49  204 204 HOH HOH A . 
G 5 HOH 50  205 205 HOH HOH A . 
G 5 HOH 51  206 206 HOH HOH A . 
G 5 HOH 52  207 207 HOH HOH A . 
G 5 HOH 53  209 209 HOH HOH A . 
G 5 HOH 54  210 210 HOH HOH A . 
G 5 HOH 55  211 211 HOH HOH A . 
G 5 HOH 56  212 212 HOH HOH A . 
G 5 HOH 57  213 213 HOH HOH A . 
G 5 HOH 58  214 214 HOH HOH A . 
G 5 HOH 59  215 215 HOH HOH A . 
G 5 HOH 60  216 216 HOH HOH A . 
G 5 HOH 61  217 217 HOH HOH A . 
G 5 HOH 62  218 218 HOH HOH A . 
G 5 HOH 63  219 219 HOH HOH A . 
G 5 HOH 64  220 220 HOH HOH A . 
G 5 HOH 65  221 221 HOH HOH A . 
G 5 HOH 66  222 222 HOH HOH A . 
G 5 HOH 67  223 223 HOH HOH A . 
G 5 HOH 68  224 224 HOH HOH A . 
G 5 HOH 69  225 225 HOH HOH A . 
G 5 HOH 70  226 226 HOH HOH A . 
G 5 HOH 71  227 227 HOH HOH A . 
G 5 HOH 72  228 228 HOH HOH A . 
G 5 HOH 73  229 229 HOH HOH A . 
G 5 HOH 74  230 230 HOH HOH A . 
G 5 HOH 75  231 231 HOH HOH A . 
G 5 HOH 76  232 232 HOH HOH A . 
G 5 HOH 77  233 233 HOH HOH A . 
G 5 HOH 78  234 234 HOH HOH A . 
G 5 HOH 79  235 235 HOH HOH A . 
G 5 HOH 80  236 236 HOH HOH A . 
G 5 HOH 81  237 237 HOH HOH A . 
G 5 HOH 82  238 238 HOH HOH A . 
H 5 HOH 1   156 156 HOH HOH B . 
H 5 HOH 2   157 157 HOH HOH B . 
H 5 HOH 3   158 158 HOH HOH B . 
H 5 HOH 4   159 159 HOH HOH B . 
H 5 HOH 5   160 160 HOH HOH B . 
H 5 HOH 6   161 161 HOH HOH B . 
H 5 HOH 7   162 162 HOH HOH B . 
H 5 HOH 8   163 163 HOH HOH B . 
H 5 HOH 9   164 164 HOH HOH B . 
H 5 HOH 10  165 165 HOH HOH B . 
H 5 HOH 11  166 166 HOH HOH B . 
H 5 HOH 12  167 167 HOH HOH B . 
H 5 HOH 13  168 168 HOH HOH B . 
H 5 HOH 14  169 169 HOH HOH B . 
H 5 HOH 15  170 170 HOH HOH B . 
H 5 HOH 16  171 171 HOH HOH B . 
H 5 HOH 17  172 172 HOH HOH B . 
H 5 HOH 18  173 173 HOH HOH B . 
H 5 HOH 19  174 174 HOH HOH B . 
H 5 HOH 20  175 175 HOH HOH B . 
H 5 HOH 21  176 176 HOH HOH B . 
H 5 HOH 22  177 177 HOH HOH B . 
H 5 HOH 23  178 178 HOH HOH B . 
H 5 HOH 24  179 179 HOH HOH B . 
H 5 HOH 25  180 180 HOH HOH B . 
H 5 HOH 26  181 181 HOH HOH B . 
H 5 HOH 27  182 182 HOH HOH B . 
H 5 HOH 28  183 183 HOH HOH B . 
H 5 HOH 29  184 184 HOH HOH B . 
H 5 HOH 30  185 185 HOH HOH B . 
H 5 HOH 31  186 186 HOH HOH B . 
H 5 HOH 32  187 187 HOH HOH B . 
H 5 HOH 33  188 188 HOH HOH B . 
H 5 HOH 34  189 189 HOH HOH B . 
H 5 HOH 35  190 190 HOH HOH B . 
H 5 HOH 36  191 191 HOH HOH B . 
H 5 HOH 37  192 192 HOH HOH B . 
H 5 HOH 38  193 193 HOH HOH B . 
H 5 HOH 39  194 194 HOH HOH B . 
H 5 HOH 40  195 195 HOH HOH B . 
H 5 HOH 41  196 196 HOH HOH B . 
H 5 HOH 42  197 197 HOH HOH B . 
H 5 HOH 43  198 198 HOH HOH B . 
H 5 HOH 44  199 199 HOH HOH B . 
H 5 HOH 45  200 200 HOH HOH B . 
H 5 HOH 46  201 201 HOH HOH B . 
H 5 HOH 47  202 202 HOH HOH B . 
H 5 HOH 48  203 203 HOH HOH B . 
H 5 HOH 49  204 204 HOH HOH B . 
H 5 HOH 50  205 205 HOH HOH B . 
H 5 HOH 51  206 206 HOH HOH B . 
H 5 HOH 52  207 207 HOH HOH B . 
H 5 HOH 53  208 208 HOH HOH B . 
H 5 HOH 54  209 209 HOH HOH B . 
H 5 HOH 55  210 210 HOH HOH B . 
H 5 HOH 56  211 211 HOH HOH B . 
H 5 HOH 57  212 212 HOH HOH B . 
H 5 HOH 58  213 213 HOH HOH B . 
H 5 HOH 59  214 214 HOH HOH B . 
H 5 HOH 60  215 215 HOH HOH B . 
H 5 HOH 61  216 216 HOH HOH B . 
H 5 HOH 62  217 217 HOH HOH B . 
H 5 HOH 63  218 218 HOH HOH B . 
H 5 HOH 64  219 219 HOH HOH B . 
H 5 HOH 65  220 220 HOH HOH B . 
H 5 HOH 66  221 221 HOH HOH B . 
H 5 HOH 67  222 222 HOH HOH B . 
H 5 HOH 68  223 223 HOH HOH B . 
H 5 HOH 69  224 224 HOH HOH B . 
H 5 HOH 70  225 225 HOH HOH B . 
H 5 HOH 71  226 226 HOH HOH B . 
H 5 HOH 72  227 227 HOH HOH B . 
H 5 HOH 73  228 228 HOH HOH B . 
H 5 HOH 74  229 229 HOH HOH B . 
H 5 HOH 75  230 230 HOH HOH B . 
H 5 HOH 76  231 231 HOH HOH B . 
H 5 HOH 77  232 232 HOH HOH B . 
H 5 HOH 78  233 233 HOH HOH B . 
H 5 HOH 79  234 234 HOH HOH B . 
H 5 HOH 80  235 235 HOH HOH B . 
H 5 HOH 81  236 236 HOH HOH B . 
H 5 HOH 82  237 237 HOH HOH B . 
H 5 HOH 83  238 238 HOH HOH B . 
H 5 HOH 84  239 239 HOH HOH B . 
H 5 HOH 85  240 240 HOH HOH B . 
H 5 HOH 86  241 241 HOH HOH B . 
H 5 HOH 87  242 242 HOH HOH B . 
H 5 HOH 88  243 243 HOH HOH B . 
H 5 HOH 89  244 244 HOH HOH B . 
H 5 HOH 90  245 245 HOH HOH B . 
H 5 HOH 91  246 246 HOH HOH B . 
H 5 HOH 92  247 247 HOH HOH B . 
H 5 HOH 93  248 248 HOH HOH B . 
H 5 HOH 94  249 249 HOH HOH B . 
H 5 HOH 95  250 250 HOH HOH B . 
H 5 HOH 96  251 251 HOH HOH B . 
H 5 HOH 97  252 252 HOH HOH B . 
H 5 HOH 98  253 253 HOH HOH B . 
H 5 HOH 99  254 254 HOH HOH B . 
H 5 HOH 100 255 255 HOH HOH B . 
H 5 HOH 101 256 256 HOH HOH B . 
H 5 HOH 102 257 257 HOH HOH B . 
H 5 HOH 103 258 258 HOH HOH B . 
H 5 HOH 104 259 259 HOH HOH B . 
H 5 HOH 105 260 260 HOH HOH B . 
H 5 HOH 106 261 208 HOH HOH B . 
# 
